data_7HAY
# 
_entry.id   7HAY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7HAY         pdb_00007hay 10.2210/pdb7hay/pdb 
WWPDB D_1001407245 ?            ?                   
# 
_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       2025-03-26 
_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.entry_id                        7HAY 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
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 'Heat shock protein HSP 90-alpha'                                  26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn 'N-(2-{[(4-chlorophenyl)methyl]sulfanyl}ethyl)furan-2-carboxamide' 295.784   1   ?        ? ? ? 
3 water       nat water                                                              18.015    150 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_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       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_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 'N-(2-{[(4-chlorophenyl)methyl]sulfanyl}ethyl)furan-2-carboxamide' A1AYH 
3 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   ASP n 
1 3   GLN n 
1 4   PRO n 
1 5   MET n 
1 6   GLU n 
1 7   GLU n 
1 8   GLU n 
1 9   GLU n 
1 10  VAL n 
1 11  GLU n 
1 12  THR n 
1 13  PHE n 
1 14  ALA n 
1 15  PHE n 
1 16  GLN n 
1 17  ALA n 
1 18  GLU n 
1 19  ILE n 
1 20  ALA n 
1 21  GLN n 
1 22  LEU n 
1 23  MET n 
1 24  SER n 
1 25  LEU n 
1 26  ILE n 
1 27  ILE n 
1 28  ASN n 
1 29  THR n 
1 30  PHE n 
1 31  TYR n 
1 32  SER n 
1 33  ASN n 
1 34  LYS n 
1 35  GLU n 
1 36  ILE n 
1 37  PHE n 
1 38  LEU n 
1 39  ARG n 
1 40  GLU n 
1 41  LEU n 
1 42  ILE n 
1 43  SER n 
1 44  ASN n 
1 45  SER n 
1 46  SER n 
1 47  ASP n 
1 48  ALA n 
1 49  LEU n 
1 50  ASP n 
1 51  LYS n 
1 52  ILE n 
1 53  ARG n 
1 54  TYR n 
1 55  GLU n 
1 56  SER n 
1 57  LEU n 
1 58  THR n 
1 59  ASP n 
1 60  PRO n 
1 61  SER n 
1 62  LYS n 
1 63  LEU n 
1 64  ASP n 
1 65  SER n 
1 66  GLY n 
1 67  LYS n 
1 68  GLU n 
1 69  LEU n 
1 70  HIS n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ILE n 
1 75  PRO n 
1 76  ASN n 
1 77  LYS n 
1 78  GLN n 
1 79  ASP n 
1 80  ARG n 
1 81  THR n 
1 82  LEU n 
1 83  THR n 
1 84  ILE n 
1 85  VAL n 
1 86  ASP n 
1 87  THR n 
1 88  GLY n 
1 89  ILE n 
1 90  GLY n 
1 91  MET n 
1 92  THR n 
1 93  LYS n 
1 94  ALA n 
1 95  ASP n 
1 96  LEU n 
1 97  ILE n 
1 98  ASN n 
1 99  ASN n 
1 100 LEU n 
1 101 GLY n 
1 102 THR n 
1 103 ILE n 
1 104 ALA n 
1 105 LYS n 
1 106 SER n 
1 107 GLY n 
1 108 THR n 
1 109 LYS n 
1 110 ALA n 
1 111 PHE n 
1 112 MET n 
1 113 GLU n 
1 114 ALA n 
1 115 LEU n 
1 116 GLN n 
1 117 ALA n 
1 118 GLY n 
1 119 ALA n 
1 120 ASP n 
1 121 ILE n 
1 122 SER n 
1 123 MET n 
1 124 ILE n 
1 125 GLY n 
1 126 GLN n 
1 127 PHE n 
1 128 GLY n 
1 129 VAL n 
1 130 GLY n 
1 131 PHE n 
1 132 TYR n 
1 133 SER n 
1 134 ALA n 
1 135 TYR n 
1 136 LEU n 
1 137 VAL n 
1 138 ALA n 
1 139 GLU n 
1 140 LYS n 
1 141 VAL n 
1 142 THR n 
1 143 VAL n 
1 144 ILE n 
1 145 THR n 
1 146 LYS n 
1 147 HIS n 
1 148 ASN n 
1 149 ASP n 
1 150 ASP n 
1 151 GLU n 
1 152 GLN n 
1 153 TYR n 
1 154 ALA n 
1 155 TRP n 
1 156 GLU n 
1 157 SER n 
1 158 SER n 
1 159 ALA n 
1 160 GLY n 
1 161 GLY n 
1 162 SER n 
1 163 PHE n 
1 164 THR n 
1 165 VAL n 
1 166 ARG n 
1 167 THR n 
1 168 ASP n 
1 169 THR n 
1 170 GLY n 
1 171 GLU n 
1 172 PRO n 
1 173 MET n 
1 174 GLY n 
1 175 ARG n 
1 176 GLY n 
1 177 THR n 
1 178 LYS n 
1 179 VAL n 
1 180 ILE n 
1 181 LEU n 
1 182 HIS n 
1 183 LEU n 
1 184 LYS n 
1 185 GLU n 
1 186 ASP n 
1 187 GLN n 
1 188 THR n 
1 189 GLU n 
1 190 TYR n 
1 191 LEU n 
1 192 GLU n 
1 193 GLU n 
1 194 ARG n 
1 195 ARG n 
1 196 ILE n 
1 197 LYS n 
1 198 GLU n 
1 199 ILE n 
1 200 VAL n 
1 201 LYS n 
1 202 LYS n 
1 203 HIS n 
1 204 SER n 
1 205 GLN n 
1 206 PHE n 
1 207 ILE n 
1 208 GLY n 
1 209 TYR n 
1 210 PRO n 
1 211 ILE n 
1 212 THR n 
1 213 LEU n 
1 214 PHE n 
1 215 VAL n 
1 216 GLU n 
1 217 LYS n 
1 218 GLU n 
1 219 ARG n 
1 220 ASP n 
1 221 LYS n 
1 222 GLU n 
1 223 VAL n 
1 224 SER n 
1 225 ASP n 
1 226 ASP n 
1 227 GLU n 
1 228 ALA n 
1 229 GLU n 
1 230 LEU n 
1 231 GLU n 
1 232 HIS n 
1 233 HIS n 
1 234 HIS n 
1 235 HIS n 
1 236 HIS n 
1 237 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                   237 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HSP90AA1, HSP90A, HSPC1, HSPCA' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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                       pET28 
_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 
A1AYH non-polymer         . 'N-(2-{[(4-chlorophenyl)methyl]sulfanyl}ethyl)furan-2-carboxamide' ? 'C14 H14 Cl N O2 S' 295.784 
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 
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 
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   8   ?   ?   ?   A . n 
A 1 2   ASP 2   9   ?   ?   ?   A . n 
A 1 3   GLN 3   10  ?   ?   ?   A . n 
A 1 4   PRO 4   11  ?   ?   ?   A . n 
A 1 5   MET 5   12  ?   ?   ?   A . n 
A 1 6   GLU 6   13  ?   ?   ?   A . n 
A 1 7   GLU 7   14  ?   ?   ?   A . n 
A 1 8   GLU 8   15  ?   ?   ?   A . n 
A 1 9   GLU 9   16  16  GLU GLU A . n 
A 1 10  VAL 10  17  17  VAL VAL A . n 
A 1 11  GLU 11  18  18  GLU GLU A . n 
A 1 12  THR 12  19  19  THR THR A . n 
A 1 13  PHE 13  20  20  PHE PHE A . n 
A 1 14  ALA 14  21  21  ALA ALA A . n 
A 1 15  PHE 15  22  22  PHE PHE A . n 
A 1 16  GLN 16  23  23  GLN GLN A . n 
A 1 17  ALA 17  24  24  ALA ALA A . n 
A 1 18  GLU 18  25  25  GLU GLU A . n 
A 1 19  ILE 19  26  26  ILE ILE A . n 
A 1 20  ALA 20  27  27  ALA ALA A . n 
A 1 21  GLN 21  28  28  GLN GLN A . n 
A 1 22  LEU 22  29  29  LEU LEU A . n 
A 1 23  MET 23  30  30  MET MET A . n 
A 1 24  SER 24  31  31  SER SER A . n 
A 1 25  LEU 25  32  32  LEU LEU A . n 
A 1 26  ILE 26  33  33  ILE ILE A . n 
A 1 27  ILE 27  34  34  ILE ILE A . n 
A 1 28  ASN 28  35  35  ASN ASN A . n 
A 1 29  THR 29  36  36  THR THR A . n 
A 1 30  PHE 30  37  37  PHE PHE A . n 
A 1 31  TYR 31  38  38  TYR TYR A . n 
A 1 32  SER 32  39  39  SER SER A . n 
A 1 33  ASN 33  40  40  ASN ASN A . n 
A 1 34  LYS 34  41  41  LYS LYS A . n 
A 1 35  GLU 35  42  42  GLU GLU A . n 
A 1 36  ILE 36  43  43  ILE ILE A . n 
A 1 37  PHE 37  44  44  PHE PHE A . n 
A 1 38  LEU 38  45  45  LEU LEU A . n 
A 1 39  ARG 39  46  46  ARG ARG A . n 
A 1 40  GLU 40  47  47  GLU GLU A . n 
A 1 41  LEU 41  48  48  LEU LEU A . n 
A 1 42  ILE 42  49  49  ILE ILE A . n 
A 1 43  SER 43  50  50  SER SER A . n 
A 1 44  ASN 44  51  51  ASN ASN A . n 
A 1 45  SER 45  52  52  SER SER A . n 
A 1 46  SER 46  53  53  SER SER A . n 
A 1 47  ASP 47  54  54  ASP ASP A . n 
A 1 48  ALA 48  55  55  ALA ALA A . n 
A 1 49  LEU 49  56  56  LEU LEU A . n 
A 1 50  ASP 50  57  57  ASP ASP A . n 
A 1 51  LYS 51  58  58  LYS LYS A . n 
A 1 52  ILE 52  59  59  ILE ILE A . n 
A 1 53  ARG 53  60  60  ARG ARG A . n 
A 1 54  TYR 54  61  61  TYR TYR A . n 
A 1 55  GLU 55  62  62  GLU GLU A . n 
A 1 56  SER 56  63  63  SER SER A . n 
A 1 57  LEU 57  64  64  LEU LEU A . n 
A 1 58  THR 58  65  65  THR THR A . n 
A 1 59  ASP 59  66  66  ASP ASP A . n 
A 1 60  PRO 60  67  67  PRO PRO A . n 
A 1 61  SER 61  68  68  SER SER A . n 
A 1 62  LYS 62  69  69  LYS LYS A . n 
A 1 63  LEU 63  70  70  LEU LEU A . n 
A 1 64  ASP 64  71  71  ASP ASP A . n 
A 1 65  SER 65  72  72  SER SER A . n 
A 1 66  GLY 66  73  73  GLY GLY A . n 
A 1 67  LYS 67  74  74  LYS LYS A . n 
A 1 68  GLU 68  75  75  GLU GLU A . n 
A 1 69  LEU 69  76  76  LEU LEU A . n 
A 1 70  HIS 70  77  77  HIS HIS A . n 
A 1 71  ILE 71  78  78  ILE ILE A . n 
A 1 72  ASN 72  79  79  ASN ASN A . n 
A 1 73  LEU 73  80  80  LEU LEU A . n 
A 1 74  ILE 74  81  81  ILE ILE A . n 
A 1 75  PRO 75  82  82  PRO PRO A . n 
A 1 76  ASN 76  83  83  ASN ASN A . n 
A 1 77  LYS 77  84  84  LYS LYS A . n 
A 1 78  GLN 78  85  85  GLN GLN A . n 
A 1 79  ASP 79  86  86  ASP ASP A . n 
A 1 80  ARG 80  87  87  ARG ARG A . n 
A 1 81  THR 81  88  88  THR THR A . n 
A 1 82  LEU 82  89  89  LEU LEU A . n 
A 1 83  THR 83  90  90  THR THR A . n 
A 1 84  ILE 84  91  91  ILE ILE A . n 
A 1 85  VAL 85  92  92  VAL VAL A . n 
A 1 86  ASP 86  93  93  ASP ASP A . n 
A 1 87  THR 87  94  94  THR THR A . n 
A 1 88  GLY 88  95  95  GLY GLY A . n 
A 1 89  ILE 89  96  96  ILE ILE A . n 
A 1 90  GLY 90  97  97  GLY GLY A . n 
A 1 91  MET 91  98  98  MET MET A . n 
A 1 92  THR 92  99  99  THR THR A . n 
A 1 93  LYS 93  100 100 LYS LYS A . n 
A 1 94  ALA 94  101 101 ALA ALA A . n 
A 1 95  ASP 95  102 102 ASP ASP A . n 
A 1 96  LEU 96  103 103 LEU LEU A . n 
A 1 97  ILE 97  104 104 ILE ILE A . n 
A 1 98  ASN 98  105 105 ASN ASN A . n 
A 1 99  ASN 99  106 106 ASN ASN A . n 
A 1 100 LEU 100 107 107 LEU LEU A . n 
A 1 101 GLY 101 108 108 GLY GLY A . n 
A 1 102 THR 102 109 109 THR THR A . n 
A 1 103 ILE 103 110 110 ILE ILE A . n 
A 1 104 ALA 104 111 111 ALA ALA A . n 
A 1 105 LYS 105 112 112 LYS LYS A . n 
A 1 106 SER 106 113 113 SER SER A . n 
A 1 107 GLY 107 114 114 GLY GLY A . n 
A 1 108 THR 108 115 115 THR THR A . n 
A 1 109 LYS 109 116 116 LYS LYS A . n 
A 1 110 ALA 110 117 117 ALA ALA A . n 
A 1 111 PHE 111 118 118 PHE PHE A . n 
A 1 112 MET 112 119 119 MET MET A . n 
A 1 113 GLU 113 120 120 GLU GLU A . n 
A 1 114 ALA 114 121 121 ALA ALA A . n 
A 1 115 LEU 115 122 122 LEU LEU A . n 
A 1 116 GLN 116 123 123 GLN GLN A . n 
A 1 117 ALA 117 124 124 ALA ALA A . n 
A 1 118 GLY 118 125 125 GLY GLY A . n 
A 1 119 ALA 119 126 126 ALA ALA A . n 
A 1 120 ASP 120 127 127 ASP ASP A . n 
A 1 121 ILE 121 128 128 ILE ILE A . n 
A 1 122 SER 122 129 129 SER SER A . n 
A 1 123 MET 123 130 130 MET MET A . n 
A 1 124 ILE 124 131 131 ILE ILE A . n 
A 1 125 GLY 125 132 132 GLY GLY A . n 
A 1 126 GLN 126 133 133 GLN GLN A . n 
A 1 127 PHE 127 134 134 PHE PHE A . n 
A 1 128 GLY 128 135 135 GLY GLY A . n 
A 1 129 VAL 129 136 136 VAL VAL A . n 
A 1 130 GLY 130 137 137 GLY GLY A . n 
A 1 131 PHE 131 138 138 PHE PHE A . n 
A 1 132 TYR 132 139 139 TYR TYR A . n 
A 1 133 SER 133 140 140 SER SER A . n 
A 1 134 ALA 134 141 141 ALA ALA A . n 
A 1 135 TYR 135 142 142 TYR TYR A . n 
A 1 136 LEU 136 143 143 LEU LEU A . n 
A 1 137 VAL 137 144 144 VAL VAL A . n 
A 1 138 ALA 138 145 145 ALA ALA A . n 
A 1 139 GLU 139 146 146 GLU GLU A . n 
A 1 140 LYS 140 147 147 LYS LYS A . n 
A 1 141 VAL 141 148 148 VAL VAL A . n 
A 1 142 THR 142 149 149 THR THR A . n 
A 1 143 VAL 143 150 150 VAL VAL A . n 
A 1 144 ILE 144 151 151 ILE ILE A . n 
A 1 145 THR 145 152 152 THR THR A . n 
A 1 146 LYS 146 153 153 LYS LYS A . n 
A 1 147 HIS 147 154 154 HIS HIS A . n 
A 1 148 ASN 148 155 155 ASN ASN A . n 
A 1 149 ASP 149 156 156 ASP ASP A . n 
A 1 150 ASP 150 157 157 ASP ASP A . n 
A 1 151 GLU 151 158 158 GLU GLU A . n 
A 1 152 GLN 152 159 159 GLN GLN A . n 
A 1 153 TYR 153 160 160 TYR TYR A . n 
A 1 154 ALA 154 161 161 ALA ALA A . n 
A 1 155 TRP 155 162 162 TRP TRP A . n 
A 1 156 GLU 156 163 163 GLU GLU A . n 
A 1 157 SER 157 164 164 SER SER A . n 
A 1 158 SER 158 165 165 SER SER A . n 
A 1 159 ALA 159 166 166 ALA ALA A . n 
A 1 160 GLY 160 167 167 GLY GLY A . n 
A 1 161 GLY 161 168 168 GLY GLY A . n 
A 1 162 SER 162 169 169 SER SER A . n 
A 1 163 PHE 163 170 170 PHE PHE A . n 
A 1 164 THR 164 171 171 THR THR A . n 
A 1 165 VAL 165 172 172 VAL VAL A . n 
A 1 166 ARG 166 173 173 ARG ARG A . n 
A 1 167 THR 167 174 174 THR THR A . n 
A 1 168 ASP 168 175 175 ASP ASP A . n 
A 1 169 THR 169 176 176 THR THR A . n 
A 1 170 GLY 170 177 177 GLY GLY A . n 
A 1 171 GLU 171 178 178 GLU GLU A . n 
A 1 172 PRO 172 179 179 PRO PRO A . n 
A 1 173 MET 173 180 180 MET MET A . n 
A 1 174 GLY 174 181 181 GLY GLY A . n 
A 1 175 ARG 175 182 182 ARG ARG A . n 
A 1 176 GLY 176 183 183 GLY GLY A . n 
A 1 177 THR 177 184 184 THR THR A . n 
A 1 178 LYS 178 185 185 LYS LYS A . n 
A 1 179 VAL 179 186 186 VAL VAL A . n 
A 1 180 ILE 180 187 187 ILE ILE A . n 
A 1 181 LEU 181 188 188 LEU LEU A . n 
A 1 182 HIS 182 189 189 HIS HIS A . n 
A 1 183 LEU 183 190 190 LEU LEU A . n 
A 1 184 LYS 184 191 191 LYS LYS A . n 
A 1 185 GLU 185 192 192 GLU GLU A . n 
A 1 186 ASP 186 193 193 ASP ASP A . n 
A 1 187 GLN 187 194 194 GLN GLN A . n 
A 1 188 THR 188 195 195 THR THR A . n 
A 1 189 GLU 189 196 196 GLU GLU A . n 
A 1 190 TYR 190 197 197 TYR TYR A . n 
A 1 191 LEU 191 198 198 LEU LEU A . n 
A 1 192 GLU 192 199 199 GLU GLU A . n 
A 1 193 GLU 193 200 200 GLU GLU A . n 
A 1 194 ARG 194 201 201 ARG ARG A . n 
A 1 195 ARG 195 202 202 ARG ARG A . n 
A 1 196 ILE 196 203 203 ILE ILE A . n 
A 1 197 LYS 197 204 204 LYS LYS A . n 
A 1 198 GLU 198 205 205 GLU GLU A . n 
A 1 199 ILE 199 206 206 ILE ILE A . n 
A 1 200 VAL 200 207 207 VAL VAL A . n 
A 1 201 LYS 201 208 208 LYS LYS A . n 
A 1 202 LYS 202 209 209 LYS LYS A . n 
A 1 203 HIS 203 210 210 HIS HIS A . n 
A 1 204 SER 204 211 211 SER SER A . n 
A 1 205 GLN 205 212 212 GLN GLN A . n 
A 1 206 PHE 206 213 213 PHE PHE A . n 
A 1 207 ILE 207 214 214 ILE ILE A . n 
A 1 208 GLY 208 215 215 GLY GLY A . n 
A 1 209 TYR 209 216 216 TYR TYR A . n 
A 1 210 PRO 210 217 217 PRO PRO A . n 
A 1 211 ILE 211 218 218 ILE ILE A . n 
A 1 212 THR 212 219 219 THR THR A . n 
A 1 213 LEU 213 220 220 LEU LEU A . n 
A 1 214 PHE 214 221 221 PHE PHE A . n 
A 1 215 VAL 215 222 222 VAL VAL A . n 
A 1 216 GLU 216 223 223 GLU GLU A . n 
A 1 217 LYS 217 224 224 LYS LYS A . n 
A 1 218 GLU 218 225 ?   ?   ?   A . n 
A 1 219 ARG 219 226 ?   ?   ?   A . n 
A 1 220 ASP 220 227 ?   ?   ?   A . n 
A 1 221 LYS 221 228 ?   ?   ?   A . n 
A 1 222 GLU 222 229 ?   ?   ?   A . n 
A 1 223 VAL 223 230 ?   ?   ?   A . n 
A 1 224 SER 224 231 ?   ?   ?   A . n 
A 1 225 ASP 225 232 ?   ?   ?   A . n 
A 1 226 ASP 226 233 ?   ?   ?   A . n 
A 1 227 GLU 227 234 ?   ?   ?   A . n 
A 1 228 ALA 228 235 ?   ?   ?   A . n 
A 1 229 GLU 229 236 ?   ?   ?   A . n 
A 1 230 LEU 230 237 ?   ?   ?   A . n 
A 1 231 GLU 231 238 ?   ?   ?   A . n 
A 1 232 HIS 232 239 ?   ?   ?   A . n 
A 1 233 HIS 233 240 ?   ?   ?   A . n 
A 1 234 HIS 234 241 ?   ?   ?   A . n 
A 1 235 HIS 235 242 ?   ?   ?   A . n 
A 1 236 HIS 236 243 ?   ?   ?   A . n 
A 1 237 HIS 237 244 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AYH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYH 
_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 A1AYH 1   301 301 A1AYH A8A A . 
C 3 HOH   1   401 134 HOH   HOH A . 
C 3 HOH   2   402 25  HOH   HOH A . 
C 3 HOH   3   403 41  HOH   HOH A . 
C 3 HOH   4   404 103 HOH   HOH A . 
C 3 HOH   5   405 55  HOH   HOH A . 
C 3 HOH   6   406 46  HOH   HOH A . 
C 3 HOH   7   407 20  HOH   HOH A . 
C 3 HOH   8   408 42  HOH   HOH A . 
C 3 HOH   9   409 136 HOH   HOH A . 
C 3 HOH   10  410 27  HOH   HOH A . 
C 3 HOH   11  411 33  HOH   HOH A . 
C 3 HOH   12  412 99  HOH   HOH A . 
C 3 HOH   13  413 6   HOH   HOH A . 
C 3 HOH   14  414 73  HOH   HOH A . 
C 3 HOH   15  415 1   HOH   HOH A . 
C 3 HOH   16  416 30  HOH   HOH A . 
C 3 HOH   17  417 18  HOH   HOH A . 
C 3 HOH   18  418 146 HOH   HOH A . 
C 3 HOH   19  419 13  HOH   HOH A . 
C 3 HOH   20  420 2   HOH   HOH A . 
C 3 HOH   21  421 24  HOH   HOH A . 
C 3 HOH   22  422 48  HOH   HOH A . 
C 3 HOH   23  423 7   HOH   HOH A . 
C 3 HOH   24  424 122 HOH   HOH A . 
C 3 HOH   25  425 4   HOH   HOH A . 
C 3 HOH   26  426 23  HOH   HOH A . 
C 3 HOH   27  427 117 HOH   HOH A . 
C 3 HOH   28  428 29  HOH   HOH A . 
C 3 HOH   29  429 9   HOH   HOH A . 
C 3 HOH   30  430 35  HOH   HOH A . 
C 3 HOH   31  431 90  HOH   HOH A . 
C 3 HOH   32  432 5   HOH   HOH A . 
C 3 HOH   33  433 53  HOH   HOH A . 
C 3 HOH   34  434 12  HOH   HOH A . 
C 3 HOH   35  435 87  HOH   HOH A . 
C 3 HOH   36  436 19  HOH   HOH A . 
C 3 HOH   37  437 40  HOH   HOH A . 
C 3 HOH   38  438 147 HOH   HOH A . 
C 3 HOH   39  439 84  HOH   HOH A . 
C 3 HOH   40  440 47  HOH   HOH A . 
C 3 HOH   41  441 10  HOH   HOH A . 
C 3 HOH   42  442 16  HOH   HOH A . 
C 3 HOH   43  443 8   HOH   HOH A . 
C 3 HOH   44  444 43  HOH   HOH A . 
C 3 HOH   45  445 75  HOH   HOH A . 
C 3 HOH   46  446 26  HOH   HOH A . 
C 3 HOH   47  447 39  HOH   HOH A . 
C 3 HOH   48  448 67  HOH   HOH A . 
C 3 HOH   49  449 56  HOH   HOH A . 
C 3 HOH   50  450 15  HOH   HOH A . 
C 3 HOH   51  451 63  HOH   HOH A . 
C 3 HOH   52  452 3   HOH   HOH A . 
C 3 HOH   53  453 118 HOH   HOH A . 
C 3 HOH   54  454 144 HOH   HOH A . 
C 3 HOH   55  455 61  HOH   HOH A . 
C 3 HOH   56  456 22  HOH   HOH A . 
C 3 HOH   57  457 58  HOH   HOH A . 
C 3 HOH   58  458 119 HOH   HOH A . 
C 3 HOH   59  459 71  HOH   HOH A . 
C 3 HOH   60  460 135 HOH   HOH A . 
C 3 HOH   61  461 17  HOH   HOH A . 
C 3 HOH   62  462 123 HOH   HOH A . 
C 3 HOH   63  463 65  HOH   HOH A . 
C 3 HOH   64  464 45  HOH   HOH A . 
C 3 HOH   65  465 76  HOH   HOH A . 
C 3 HOH   66  466 79  HOH   HOH A . 
C 3 HOH   67  467 28  HOH   HOH A . 
C 3 HOH   68  468 101 HOH   HOH A . 
C 3 HOH   69  469 80  HOH   HOH A . 
C 3 HOH   70  470 57  HOH   HOH A . 
C 3 HOH   71  471 94  HOH   HOH A . 
C 3 HOH   72  472 51  HOH   HOH A . 
C 3 HOH   73  473 21  HOH   HOH A . 
C 3 HOH   74  474 142 HOH   HOH A . 
C 3 HOH   75  475 54  HOH   HOH A . 
C 3 HOH   76  476 52  HOH   HOH A . 
C 3 HOH   77  477 72  HOH   HOH A . 
C 3 HOH   78  478 124 HOH   HOH A . 
C 3 HOH   79  479 97  HOH   HOH A . 
C 3 HOH   80  480 145 HOH   HOH A . 
C 3 HOH   81  481 109 HOH   HOH A . 
C 3 HOH   82  482 32  HOH   HOH A . 
C 3 HOH   83  483 14  HOH   HOH A . 
C 3 HOH   84  484 34  HOH   HOH A . 
C 3 HOH   85  485 113 HOH   HOH A . 
C 3 HOH   86  486 66  HOH   HOH A . 
C 3 HOH   87  487 11  HOH   HOH A . 
C 3 HOH   88  488 77  HOH   HOH A . 
C 3 HOH   89  489 38  HOH   HOH A . 
C 3 HOH   90  490 112 HOH   HOH A . 
C 3 HOH   91  491 49  HOH   HOH A . 
C 3 HOH   92  492 44  HOH   HOH A . 
C 3 HOH   93  493 50  HOH   HOH A . 
C 3 HOH   94  494 150 HOH   HOH A . 
C 3 HOH   95  495 137 HOH   HOH A . 
C 3 HOH   96  496 96  HOH   HOH A . 
C 3 HOH   97  497 149 HOH   HOH A . 
C 3 HOH   98  498 141 HOH   HOH A . 
C 3 HOH   99  499 120 HOH   HOH A . 
C 3 HOH   100 500 62  HOH   HOH A . 
C 3 HOH   101 501 93  HOH   HOH A . 
C 3 HOH   102 502 68  HOH   HOH A . 
C 3 HOH   103 503 82  HOH   HOH A . 
C 3 HOH   104 504 105 HOH   HOH A . 
C 3 HOH   105 505 86  HOH   HOH A . 
C 3 HOH   106 506 108 HOH   HOH A . 
C 3 HOH   107 507 131 HOH   HOH A . 
C 3 HOH   108 508 140 HOH   HOH A . 
C 3 HOH   109 509 106 HOH   HOH A . 
C 3 HOH   110 510 116 HOH   HOH A . 
C 3 HOH   111 511 85  HOH   HOH A . 
C 3 HOH   112 512 129 HOH   HOH A . 
C 3 HOH   113 513 111 HOH   HOH A . 
C 3 HOH   114 514 70  HOH   HOH A . 
C 3 HOH   115 515 81  HOH   HOH A . 
C 3 HOH   116 516 126 HOH   HOH A . 
C 3 HOH   117 517 83  HOH   HOH A . 
C 3 HOH   118 518 107 HOH   HOH A . 
C 3 HOH   119 519 88  HOH   HOH A . 
C 3 HOH   120 520 64  HOH   HOH A . 
C 3 HOH   121 521 133 HOH   HOH A . 
C 3 HOH   122 522 114 HOH   HOH A . 
C 3 HOH   123 523 110 HOH   HOH A . 
C 3 HOH   124 524 130 HOH   HOH A . 
C 3 HOH   125 525 31  HOH   HOH A . 
C 3 HOH   126 526 59  HOH   HOH A . 
C 3 HOH   127 527 89  HOH   HOH A . 
C 3 HOH   128 528 92  HOH   HOH A . 
C 3 HOH   129 529 139 HOH   HOH A . 
C 3 HOH   130 530 138 HOH   HOH A . 
C 3 HOH   131 531 69  HOH   HOH A . 
C 3 HOH   132 532 125 HOH   HOH A . 
C 3 HOH   133 533 78  HOH   HOH A . 
C 3 HOH   134 534 36  HOH   HOH A . 
C 3 HOH   135 535 128 HOH   HOH A . 
C 3 HOH   136 536 143 HOH   HOH A . 
C 3 HOH   137 537 91  HOH   HOH A . 
C 3 HOH   138 538 132 HOH   HOH A . 
C 3 HOH   139 539 100 HOH   HOH A . 
C 3 HOH   140 540 74  HOH   HOH A . 
C 3 HOH   141 541 102 HOH   HOH A . 
C 3 HOH   142 542 104 HOH   HOH A . 
C 3 HOH   143 543 60  HOH   HOH A . 
C 3 HOH   144 544 121 HOH   HOH A . 
C 3 HOH   145 545 148 HOH   HOH A . 
C 3 HOH   146 546 37  HOH   HOH A . 
C 3 HOH   147 547 95  HOH   HOH A . 
C 3 HOH   148 548 98  HOH   HOH A . 
C 3 HOH   149 549 115 HOH   HOH A . 
C 3 HOH   150 550 127 HOH   HOH A . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 XDS         .           ?               package 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/     ?   ? 
2 Aimless     0.7.7       23/04/21        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 DIMPLE      .           ?               program 'Marcin Wojdyr'   wojdyr@gmail.com                        phasing           
http://ccp4.github.io/dimple/                       ?   ? 
4 PHENIX      1.20.1_4487 ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                       C++ ? 
5 PDB_EXTRACT 3.28        'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.volume             617337.151 
_cell.length_a           68.817 
_cell.length_b           90.264 
_cell.length_c           99.383 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAY 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.entry_id                         7HAY 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAY 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-22 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAY 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             56.580 
_reflns.d_resolution_high            2.270 
_reflns.number_obs                   14339 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         97.300 
_reflns.pdbx_Rmerge_I_obs            0.103 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.600 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              7.500 
_reflns.pdbx_Rrim_I_all              0.111 
_reflns.pdbx_Rpim_I_all              0.041 
_reflns.pdbx_CC_half                 0.992 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     108037 
_reflns.pdbx_scaling_rejects         316 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 2.270 2.390  ? 16011 2079 ? 0.471 ? ? ? 7.700 ? 5.100  ? ? ? ? ? ? 97.900 0.505 0.178 0.952 
1 2 7.160 56.580 ? 3564  502  ? 0.056 ? ? ? 7.100 ? 25.500 ? ? ? ? ? ? 97.300 0.060 0.022 0.996 
# 
_refine.entry_id                                 7HAY 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.ls_percent_reflns_R_free                 5.10 
_refine.pdbx_overall_phase_error                 24.2780 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_R_factor_obs                          0.1975 
_refine.B_iso_mean                               38.02 
_refine.ls_number_reflns_R_free                  720 
_refine.ls_percent_reflns_obs                    96.34 
_refine.ls_R_factor_R_work                       0.1952 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.27 
_refine.ls_number_reflns_obs                     14116 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  13396 
_refine.ls_d_res_low                             28.80 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2379 
_refine.overall_SU_ML                            0.2637 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         19 
_refine_hist.number_atoms_solvent             150 
_refine_hist.number_atoms_total               1813 
_refine_hist.d_res_high                       2.27 
_refine_hist.d_res_low                        28.80 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1690 0.0017 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2276 0.4176 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0380 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      290  0.0034 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 229  5.5931 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 2.27 2.45  2629 0.2391 96.89 0.3336 145 . . . . . 
'X-RAY DIFFRACTION' 2.45 2.69  2503 0.2323 90.01 0.2957 119 . . . . . 
'X-RAY DIFFRACTION' 2.69 3.08  2733 0.2195 99.55 0.2794 144 . . . . . 
'X-RAY DIFFRACTION' 3.08 3.88  2704 0.2120 97.33 0.2722 144 . . . . . 
'X-RAY DIFFRACTION' 3.88 28.80 2827 0.1561 97.84 0.1721 168 . . . . . 
# 
_struct.entry_id                  7HAY 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr14271' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAY 
_struct_keywords.pdbx_keywords   CHAPERONE 
_struct_keywords.text            
'Crystallographic Fragment Screening; Fragment-Based Drug Discovery (FBDD); Heat shock protein 90 (HSP90), CHAPERONE' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HS90A_HUMAN 
_struct_ref.pdbx_db_accession          P07900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRT
LTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGG
SFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAE
;
_struct_ref.pdbx_align_begin           9 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HAY 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 229 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P07900 
_struct_ref_seq.db_align_beg                  9 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  236 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       9 
_struct_ref_seq.pdbx_auth_seq_align_end       236 
# 
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 7HAY MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAY LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAY GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAY HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAY HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAY HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAY HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAY HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAY HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            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 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ASN A 98  ? ALA A 117 ? ASN A 105 ALA A 124 1 ? 20 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? 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 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N ILE A 144 ? N ILE A 151 O LYS A 178 ? O LYS A 185 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HAY 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 521 ? ? O A HOH 529 ? ? 1.98 
2 1 OE1 A GLU 158 ? ? O A HOH 401 ? ? 2.10 
3 1 O   A HOH 503 ? ? O A HOH 512 ? ? 2.15 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     497 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     497 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_556 
_pdbx_validate_symm_contact.dist              2.04 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 66  ? ? -153.75 87.42   
2 1 THR A 94  ? ? -101.28 40.47   
3 1 ASN A 105 ? ? -102.70 -61.29  
4 1 ALA A 166 ? ? 60.70   -151.90 
5 1 ARG A 182 ? ? -172.42 140.54  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1  ? 'X-RAY DIFFRACTION' refined 13.6061479674  27.2433190567 31.7135143089 0.282092445571 0.284278907193 0.355436322104 
0.0518320116717   -0.0649703735102   0.00912716073176  4.58446986983 2.41540343796 8.12324310862 -1.33637283442  -3.70726545985 
0.956176629571  -0.0966756642208 -0.386316994734  -0.0652527812094 0.211912035815   -0.145888877818   -0.111222891491   
0.0540681976887 0.663003867908   0.142769861738   
2  ? 'X-RAY DIFFRACTION' refined -6.60269508428 38.503408356  23.9661730154 0.23169052591  0.256032977276 0.301126261197 
0.0129160227238   -0.0161458298535   -0.01829149562    1.78541901004 4.10038629632 8.17953656147 -2.01225373817  2.2125901852   
-4.77732612315  -0.121049943991  0.115275930928   0.269048736923   0.16378421093    -0.105578164047   -0.0482421378374  
-0.492954554557 -0.0991292498283 0.0967480334837  
3  ? 'X-RAY DIFFRACTION' refined -3.3911073201  26.6486964071 25.9271339554 0.310140409089 0.230904034138 0.258118630987 
-0.058811876792   -0.0647608883062   -0.0607571316084  2.63440735081 2.58983620801 5.45713708399 -0.690959472839 -1.94090151656 
-2.48172860973  -0.058086912     -0.0594764920387 -0.0528924425402 -0.271944677445  0.254741562328    0.216105989525    
0.472958958414  -0.151821154462  -0.173610591259  
4  ? 'X-RAY DIFFRACTION' refined 15.2582102744  38.6916077576 31.2902762969 0.255079927717 0.351231561696 0.518353940492 
-0.0165004759878  -0.0586560791441   0.0597441462588   2.12246575367 3.8706220952  5.85963784573 -0.106966503177 -2.16968896884 
1.51131491734   -0.437403377396  -0.181177749539  0.200039684911   0.190028376046   -0.134662708716   -0.263649988138   
-0.353676560284 1.10703746507    0.335378111786   
5  ? 'X-RAY DIFFRACTION' refined 9.29636167801  39.6072787219 39.1789325157 0.353344882379 0.377017400683 0.418932342387 
-0.0593653936391  -0.0298710569543   -0.110633111021   5.32058871367 6.45383777045 5.4560984239  0.435667217219  -1.48345540779 
1.09357672779   0.00954780879973 -0.811933790451  0.944109260078   0.807417567093   -0.269177970182   0.236659107394    
-0.293631622472 -0.33999742062   0.482745009664   
6  ? 'X-RAY DIFFRACTION' refined 4.06657508761  25.9841939858 29.4808132091 0.22312892335  0.249606288115 0.279578406383 
0.0064879139013   0.0233495061094    0.000944156627477 3.62517278651 2.42311320092 6.46186959687 -0.386081964857 2.6398712798   
0.289996617414  0.0855808935591  -0.159365699543  -0.419997268889  -0.0314763725667 -0.00288439944394 -0.00869470984991 
0.48332777537   0.0355068478677  -0.0836531302588 
7  ? 'X-RAY DIFFRACTION' refined 1.5349410328   27.7693465339 15.7138205162 0.308698108712 0.344333763792 0.280664158351 
-0.00820690380663 -0.000889168029424 -0.00941926300586 4.18114066318 5.86944242029 3.7782196647  -3.00830174249  3.8484903905   
-2.0542708307   0.253093705545   0.544260013955   -0.654912201291  -0.379196159788  0.0326366652868   0.0588203691341   
0.231894523279  0.391281096383   -0.328838860815  
8  ? 'X-RAY DIFFRACTION' refined 1.13488174744  23.1127557951 21.9724450918 0.309688025211 0.258819660812 0.348431026712 
-0.0233348869741  -0.0134648131433   -0.0443251529075  3.12078218942 3.65962896839 4.01312731214 -2.75203118415  0.302111113018 
-2.27894651154  0.0340437863903  0.16367659446    -0.513001418059  -0.367769432807  0.00729458351333  0.346405387583    
0.501602092223  -0.253438666469  -0.132507490736  
9  ? 'X-RAY DIFFRACTION' refined -5.87808496267 25.5372732937 42.7271694249 0.271518702037 0.378888717079 0.232667864039 
-0.0461034632426  -0.00327928811019  0.04534786849     7.51532085411 8.04702572084 6.61192225948 -2.86051282349  -0.24779825276 
-0.353802289818 -0.0818774571272 -0.719002645203  -0.495995357027  0.259703059941   0.0610895472398   0.649331794542    
0.338790191133  -0.270257393171  0.0224976689101  
10 ? 'X-RAY DIFFRACTION' refined -13.1974426182 31.6070531916 33.7995563346 0.199768134559 0.323775597145 0.228367667699 
-0.00290839953867 0.0230259155546    0.0228212386674   4.31626264672 8.13132427993 3.56529816435 0.213420505769  0.772756031133 
-1.12633110221  0.144643819012   -0.507647529192  -0.113172844857  0.761725572688   -0.0729415810829  0.239604058608    
0.0486867278517 -0.319992715705  -0.161176259438  
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  1  'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2  2  'X-RAY DIFFRACTION' A 41  A 26  A 76  A 61  . 
;chain 'A' and (resid 41 through 76 )
;
3  3  'X-RAY DIFFRACTION' A 77  A 62  A 105 A 90  . 
;chain 'A' and (resid 77 through 105 )
;
4  4  'X-RAY DIFFRACTION' A 106 A 91  A 123 A 108 . 
;chain 'A' and (resid 106 through 123 )
;
5  5  'X-RAY DIFFRACTION' A 124 A 109 A 136 A 121 . 
;chain 'A' and (resid 124 through 136 )
;
6  6  'X-RAY DIFFRACTION' A 137 A 122 A 153 A 138 . 
;chain 'A' and (resid 137 through 153 )
;
7  7  'X-RAY DIFFRACTION' A 154 A 139 A 164 A 149 . 
;chain 'A' and (resid 154 through 164 )
;
8  8  'X-RAY DIFFRACTION' A 165 A 150 A 190 A 175 . 
;chain 'A' and (resid 165 through 190 )
;
9  9  'X-RAY DIFFRACTION' A 191 A 176 A 210 A 195 . 
;chain 'A' and (resid 191 through 210 )
;
10 10 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
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 MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
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 
A1AYH C10  C  Y N 1   
A1AYH C13  C  Y N 2   
A1AYH C11  C  Y N 3   
A1AYH C12  C  Y N 4   
A1AYH C14  C  Y N 5   
A1AYH C1   C  Y N 6   
A1AYH C2   C  Y N 7   
A1AYH C3   C  Y N 8   
A1AYH C4   C  Y N 9   
A1AYH C5   C  N N 10  
A1AYH C6   C  N N 11  
A1AYH C7   C  N N 12  
A1AYH C8   C  N N 13  
A1AYH C9   C  Y N 14  
A1AYH N1   N  N N 15  
A1AYH O1   O  N N 16  
A1AYH O2   O  Y N 17  
A1AYH S1   S  N N 18  
A1AYH CL1  CL N N 19  
A1AYH H10  H  N N 20  
A1AYH H13  H  N N 21  
A1AYH H11  H  N N 22  
A1AYH H12  H  N N 23  
A1AYH H14  H  N N 24  
A1AYH H2   H  N N 25  
A1AYH H3   H  N N 26  
A1AYH H53  H  N N 27  
A1AYH H52  H  N N 28  
A1AYH H63  H  N N 29  
A1AYH H62  H  N N 30  
A1AYH H72  H  N N 31  
A1AYH H73  H  N N 32  
A1AYH H1   H  N N 33  
ALA   N    N  N N 34  
ALA   CA   C  N S 35  
ALA   C    C  N N 36  
ALA   O    O  N N 37  
ALA   CB   C  N N 38  
ALA   OXT  O  N N 39  
ALA   H    H  N N 40  
ALA   H2   H  N N 41  
ALA   HA   H  N N 42  
ALA   HB1  H  N N 43  
ALA   HB2  H  N N 44  
ALA   HB3  H  N N 45  
ALA   HXT  H  N N 46  
ARG   N    N  N N 47  
ARG   CA   C  N S 48  
ARG   C    C  N N 49  
ARG   O    O  N N 50  
ARG   CB   C  N N 51  
ARG   CG   C  N N 52  
ARG   CD   C  N N 53  
ARG   NE   N  N N 54  
ARG   CZ   C  N N 55  
ARG   NH1  N  N N 56  
ARG   NH2  N  N N 57  
ARG   OXT  O  N N 58  
ARG   H    H  N N 59  
ARG   H2   H  N N 60  
ARG   HA   H  N N 61  
ARG   HB2  H  N N 62  
ARG   HB3  H  N N 63  
ARG   HG2  H  N N 64  
ARG   HG3  H  N N 65  
ARG   HD2  H  N N 66  
ARG   HD3  H  N N 67  
ARG   HE   H  N N 68  
ARG   HH11 H  N N 69  
ARG   HH12 H  N N 70  
ARG   HH21 H  N N 71  
ARG   HH22 H  N N 72  
ARG   HXT  H  N N 73  
ASN   N    N  N N 74  
ASN   CA   C  N S 75  
ASN   C    C  N N 76  
ASN   O    O  N N 77  
ASN   CB   C  N N 78  
ASN   CG   C  N N 79  
ASN   OD1  O  N N 80  
ASN   ND2  N  N N 81  
ASN   OXT  O  N N 82  
ASN   H    H  N N 83  
ASN   H2   H  N N 84  
ASN   HA   H  N N 85  
ASN   HB2  H  N N 86  
ASN   HB3  H  N N 87  
ASN   HD21 H  N N 88  
ASN   HD22 H  N N 89  
ASN   HXT  H  N N 90  
ASP   N    N  N N 91  
ASP   CA   C  N S 92  
ASP   C    C  N N 93  
ASP   O    O  N N 94  
ASP   CB   C  N N 95  
ASP   CG   C  N N 96  
ASP   OD1  O  N N 97  
ASP   OD2  O  N N 98  
ASP   OXT  O  N N 99  
ASP   H    H  N N 100 
ASP   H2   H  N N 101 
ASP   HA   H  N N 102 
ASP   HB2  H  N N 103 
ASP   HB3  H  N N 104 
ASP   HD2  H  N N 105 
ASP   HXT  H  N N 106 
GLN   N    N  N N 107 
GLN   CA   C  N S 108 
GLN   C    C  N N 109 
GLN   O    O  N N 110 
GLN   CB   C  N N 111 
GLN   CG   C  N N 112 
GLN   CD   C  N N 113 
GLN   OE1  O  N N 114 
GLN   NE2  N  N N 115 
GLN   OXT  O  N N 116 
GLN   H    H  N N 117 
GLN   H2   H  N N 118 
GLN   HA   H  N N 119 
GLN   HB2  H  N N 120 
GLN   HB3  H  N N 121 
GLN   HG2  H  N N 122 
GLN   HG3  H  N N 123 
GLN   HE21 H  N N 124 
GLN   HE22 H  N N 125 
GLN   HXT  H  N N 126 
GLU   N    N  N N 127 
GLU   CA   C  N S 128 
GLU   C    C  N N 129 
GLU   O    O  N N 130 
GLU   CB   C  N N 131 
GLU   CG   C  N N 132 
GLU   CD   C  N N 133 
GLU   OE1  O  N N 134 
GLU   OE2  O  N N 135 
GLU   OXT  O  N N 136 
GLU   H    H  N N 137 
GLU   H2   H  N N 138 
GLU   HA   H  N N 139 
GLU   HB2  H  N N 140 
GLU   HB3  H  N N 141 
GLU   HG2  H  N N 142 
GLU   HG3  H  N N 143 
GLU   HE2  H  N N 144 
GLU   HXT  H  N N 145 
GLY   N    N  N N 146 
GLY   CA   C  N N 147 
GLY   C    C  N N 148 
GLY   O    O  N N 149 
GLY   OXT  O  N N 150 
GLY   H    H  N N 151 
GLY   H2   H  N N 152 
GLY   HA2  H  N N 153 
GLY   HA3  H  N N 154 
GLY   HXT  H  N N 155 
HIS   N    N  N N 156 
HIS   CA   C  N S 157 
HIS   C    C  N N 158 
HIS   O    O  N N 159 
HIS   CB   C  N N 160 
HIS   CG   C  Y N 161 
HIS   ND1  N  Y N 162 
HIS   CD2  C  Y N 163 
HIS   CE1  C  Y N 164 
HIS   NE2  N  Y N 165 
HIS   OXT  O  N N 166 
HIS   H    H  N N 167 
HIS   H2   H  N N 168 
HIS   HA   H  N N 169 
HIS   HB2  H  N N 170 
HIS   HB3  H  N N 171 
HIS   HD1  H  N N 172 
HIS   HD2  H  N N 173 
HIS   HE1  H  N N 174 
HIS   HE2  H  N N 175 
HIS   HXT  H  N N 176 
HOH   O    O  N N 177 
HOH   H1   H  N N 178 
HOH   H2   H  N N 179 
ILE   N    N  N N 180 
ILE   CA   C  N S 181 
ILE   C    C  N N 182 
ILE   O    O  N N 183 
ILE   CB   C  N S 184 
ILE   CG1  C  N N 185 
ILE   CG2  C  N N 186 
ILE   CD1  C  N N 187 
ILE   OXT  O  N N 188 
ILE   H    H  N N 189 
ILE   H2   H  N N 190 
ILE   HA   H  N N 191 
ILE   HB   H  N N 192 
ILE   HG12 H  N N 193 
ILE   HG13 H  N N 194 
ILE   HG21 H  N N 195 
ILE   HG22 H  N N 196 
ILE   HG23 H  N N 197 
ILE   HD11 H  N N 198 
ILE   HD12 H  N N 199 
ILE   HD13 H  N N 200 
ILE   HXT  H  N N 201 
LEU   N    N  N N 202 
LEU   CA   C  N S 203 
LEU   C    C  N N 204 
LEU   O    O  N N 205 
LEU   CB   C  N N 206 
LEU   CG   C  N N 207 
LEU   CD1  C  N N 208 
LEU   CD2  C  N N 209 
LEU   OXT  O  N N 210 
LEU   H    H  N N 211 
LEU   H2   H  N N 212 
LEU   HA   H  N N 213 
LEU   HB2  H  N N 214 
LEU   HB3  H  N N 215 
LEU   HG   H  N N 216 
LEU   HD11 H  N N 217 
LEU   HD12 H  N N 218 
LEU   HD13 H  N N 219 
LEU   HD21 H  N N 220 
LEU   HD22 H  N N 221 
LEU   HD23 H  N N 222 
LEU   HXT  H  N N 223 
LYS   N    N  N N 224 
LYS   CA   C  N S 225 
LYS   C    C  N N 226 
LYS   O    O  N N 227 
LYS   CB   C  N N 228 
LYS   CG   C  N N 229 
LYS   CD   C  N N 230 
LYS   CE   C  N N 231 
LYS   NZ   N  N N 232 
LYS   OXT  O  N N 233 
LYS   H    H  N N 234 
LYS   H2   H  N N 235 
LYS   HA   H  N N 236 
LYS   HB2  H  N N 237 
LYS   HB3  H  N N 238 
LYS   HG2  H  N N 239 
LYS   HG3  H  N N 240 
LYS   HD2  H  N N 241 
LYS   HD3  H  N N 242 
LYS   HE2  H  N N 243 
LYS   HE3  H  N N 244 
LYS   HZ1  H  N N 245 
LYS   HZ2  H  N N 246 
LYS   HZ3  H  N N 247 
LYS   HXT  H  N N 248 
MET   N    N  N N 249 
MET   CA   C  N S 250 
MET   C    C  N N 251 
MET   O    O  N N 252 
MET   CB   C  N N 253 
MET   CG   C  N N 254 
MET   SD   S  N N 255 
MET   CE   C  N N 256 
MET   OXT  O  N N 257 
MET   H    H  N N 258 
MET   H2   H  N N 259 
MET   HA   H  N N 260 
MET   HB2  H  N N 261 
MET   HB3  H  N N 262 
MET   HG2  H  N N 263 
MET   HG3  H  N N 264 
MET   HE1  H  N N 265 
MET   HE2  H  N N 266 
MET   HE3  H  N N 267 
MET   HXT  H  N N 268 
PHE   N    N  N N 269 
PHE   CA   C  N S 270 
PHE   C    C  N N 271 
PHE   O    O  N N 272 
PHE   CB   C  N N 273 
PHE   CG   C  Y N 274 
PHE   CD1  C  Y N 275 
PHE   CD2  C  Y N 276 
PHE   CE1  C  Y N 277 
PHE   CE2  C  Y N 278 
PHE   CZ   C  Y N 279 
PHE   OXT  O  N N 280 
PHE   H    H  N N 281 
PHE   H2   H  N N 282 
PHE   HA   H  N N 283 
PHE   HB2  H  N N 284 
PHE   HB3  H  N N 285 
PHE   HD1  H  N N 286 
PHE   HD2  H  N N 287 
PHE   HE1  H  N N 288 
PHE   HE2  H  N N 289 
PHE   HZ   H  N N 290 
PHE   HXT  H  N N 291 
PRO   N    N  N N 292 
PRO   CA   C  N S 293 
PRO   C    C  N N 294 
PRO   O    O  N N 295 
PRO   CB   C  N N 296 
PRO   CG   C  N N 297 
PRO   CD   C  N N 298 
PRO   OXT  O  N N 299 
PRO   H    H  N N 300 
PRO   HA   H  N N 301 
PRO   HB2  H  N N 302 
PRO   HB3  H  N N 303 
PRO   HG2  H  N N 304 
PRO   HG3  H  N N 305 
PRO   HD2  H  N N 306 
PRO   HD3  H  N N 307 
PRO   HXT  H  N N 308 
SER   N    N  N N 309 
SER   CA   C  N S 310 
SER   C    C  N N 311 
SER   O    O  N N 312 
SER   CB   C  N N 313 
SER   OG   O  N N 314 
SER   OXT  O  N N 315 
SER   H    H  N N 316 
SER   H2   H  N N 317 
SER   HA   H  N N 318 
SER   HB2  H  N N 319 
SER   HB3  H  N N 320 
SER   HG   H  N N 321 
SER   HXT  H  N N 322 
THR   N    N  N N 323 
THR   CA   C  N S 324 
THR   C    C  N N 325 
THR   O    O  N N 326 
THR   CB   C  N R 327 
THR   OG1  O  N N 328 
THR   CG2  C  N N 329 
THR   OXT  O  N N 330 
THR   H    H  N N 331 
THR   H2   H  N N 332 
THR   HA   H  N N 333 
THR   HB   H  N N 334 
THR   HG1  H  N N 335 
THR   HG21 H  N N 336 
THR   HG22 H  N N 337 
THR   HG23 H  N N 338 
THR   HXT  H  N N 339 
TRP   N    N  N N 340 
TRP   CA   C  N S 341 
TRP   C    C  N N 342 
TRP   O    O  N N 343 
TRP   CB   C  N N 344 
TRP   CG   C  Y N 345 
TRP   CD1  C  Y N 346 
TRP   CD2  C  Y N 347 
TRP   NE1  N  Y N 348 
TRP   CE2  C  Y N 349 
TRP   CE3  C  Y N 350 
TRP   CZ2  C  Y N 351 
TRP   CZ3  C  Y N 352 
TRP   CH2  C  Y N 353 
TRP   OXT  O  N N 354 
TRP   H    H  N N 355 
TRP   H2   H  N N 356 
TRP   HA   H  N N 357 
TRP   HB2  H  N N 358 
TRP   HB3  H  N N 359 
TRP   HD1  H  N N 360 
TRP   HE1  H  N N 361 
TRP   HE3  H  N N 362 
TRP   HZ2  H  N N 363 
TRP   HZ3  H  N N 364 
TRP   HH2  H  N N 365 
TRP   HXT  H  N N 366 
TYR   N    N  N N 367 
TYR   CA   C  N S 368 
TYR   C    C  N N 369 
TYR   O    O  N N 370 
TYR   CB   C  N N 371 
TYR   CG   C  Y N 372 
TYR   CD1  C  Y N 373 
TYR   CD2  C  Y N 374 
TYR   CE1  C  Y N 375 
TYR   CE2  C  Y N 376 
TYR   CZ   C  Y N 377 
TYR   OH   O  N N 378 
TYR   OXT  O  N N 379 
TYR   H    H  N N 380 
TYR   H2   H  N N 381 
TYR   HA   H  N N 382 
TYR   HB2  H  N N 383 
TYR   HB3  H  N N 384 
TYR   HD1  H  N N 385 
TYR   HD2  H  N N 386 
TYR   HE1  H  N N 387 
TYR   HE2  H  N N 388 
TYR   HH   H  N N 389 
TYR   HXT  H  N N 390 
VAL   N    N  N N 391 
VAL   CA   C  N S 392 
VAL   C    C  N N 393 
VAL   O    O  N N 394 
VAL   CB   C  N N 395 
VAL   CG1  C  N N 396 
VAL   CG2  C  N N 397 
VAL   OXT  O  N N 398 
VAL   H    H  N N 399 
VAL   H2   H  N N 400 
VAL   HA   H  N N 401 
VAL   HB   H  N N 402 
VAL   HG11 H  N N 403 
VAL   HG12 H  N N 404 
VAL   HG13 H  N N 405 
VAL   HG21 H  N N 406 
VAL   HG22 H  N N 407 
VAL   HG23 H  N N 408 
VAL   HXT  H  N N 409 
# 
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 
A1AYH CL1 C1   sing N N 1   
A1AYH C1  C2   doub Y N 2   
A1AYH C1  C14  sing Y N 3   
A1AYH C2  C3   sing Y N 4   
A1AYH C3  C4   doub Y N 5   
A1AYH C4  C5   sing N N 6   
A1AYH C4  C13  sing Y N 7   
A1AYH C5  S1   sing N N 8   
A1AYH S1  C6   sing N N 9   
A1AYH C6  C7   sing N N 10  
A1AYH C7  N1   sing N N 11  
A1AYH N1  C8   sing N N 12  
A1AYH C8  O1   doub N N 13  
A1AYH C8  C9   sing N N 14  
A1AYH C9  C10  doub Y N 15  
A1AYH C9  O2   sing Y N 16  
A1AYH C10 C11  sing Y N 17  
A1AYH C11 C12  doub Y N 18  
A1AYH C12 O2   sing Y N 19  
A1AYH C13 C14  doub Y N 20  
A1AYH C10 H10  sing N N 21  
A1AYH C13 H13  sing N N 22  
A1AYH C11 H11  sing N N 23  
A1AYH C12 H12  sing N N 24  
A1AYH C14 H14  sing N N 25  
A1AYH C2  H2   sing N N 26  
A1AYH C3  H3   sing N N 27  
A1AYH C5  H53  sing N N 28  
A1AYH C5  H52  sing N N 29  
A1AYH C6  H63  sing N N 30  
A1AYH C6  H62  sing N N 31  
A1AYH C7  H72  sing N N 32  
A1AYH C7  H73  sing N N 33  
A1AYH N1  H1   sing N N 34  
ALA   N   CA   sing N N 35  
ALA   N   H    sing N N 36  
ALA   N   H2   sing N N 37  
ALA   CA  C    sing N N 38  
ALA   CA  CB   sing N N 39  
ALA   CA  HA   sing N N 40  
ALA   C   O    doub N N 41  
ALA   C   OXT  sing N N 42  
ALA   CB  HB1  sing N N 43  
ALA   CB  HB2  sing N N 44  
ALA   CB  HB3  sing N N 45  
ALA   OXT HXT  sing N N 46  
ARG   N   CA   sing N N 47  
ARG   N   H    sing N N 48  
ARG   N   H2   sing N N 49  
ARG   CA  C    sing N N 50  
ARG   CA  CB   sing N N 51  
ARG   CA  HA   sing N N 52  
ARG   C   O    doub N N 53  
ARG   C   OXT  sing N N 54  
ARG   CB  CG   sing N N 55  
ARG   CB  HB2  sing N N 56  
ARG   CB  HB3  sing N N 57  
ARG   CG  CD   sing N N 58  
ARG   CG  HG2  sing N N 59  
ARG   CG  HG3  sing N N 60  
ARG   CD  NE   sing N N 61  
ARG   CD  HD2  sing N N 62  
ARG   CD  HD3  sing N N 63  
ARG   NE  CZ   sing N N 64  
ARG   NE  HE   sing N N 65  
ARG   CZ  NH1  sing N N 66  
ARG   CZ  NH2  doub N N 67  
ARG   NH1 HH11 sing N N 68  
ARG   NH1 HH12 sing N N 69  
ARG   NH2 HH21 sing N N 70  
ARG   NH2 HH22 sing N N 71  
ARG   OXT HXT  sing N N 72  
ASN   N   CA   sing N N 73  
ASN   N   H    sing N N 74  
ASN   N   H2   sing N N 75  
ASN   CA  C    sing N N 76  
ASN   CA  CB   sing N N 77  
ASN   CA  HA   sing N N 78  
ASN   C   O    doub N N 79  
ASN   C   OXT  sing N N 80  
ASN   CB  CG   sing N N 81  
ASN   CB  HB2  sing N N 82  
ASN   CB  HB3  sing N N 83  
ASN   CG  OD1  doub N N 84  
ASN   CG  ND2  sing N N 85  
ASN   ND2 HD21 sing N N 86  
ASN   ND2 HD22 sing N N 87  
ASN   OXT HXT  sing N N 88  
ASP   N   CA   sing N N 89  
ASP   N   H    sing N N 90  
ASP   N   H2   sing N N 91  
ASP   CA  C    sing N N 92  
ASP   CA  CB   sing N N 93  
ASP   CA  HA   sing N N 94  
ASP   C   O    doub N N 95  
ASP   C   OXT  sing N N 96  
ASP   CB  CG   sing N N 97  
ASP   CB  HB2  sing N N 98  
ASP   CB  HB3  sing N N 99  
ASP   CG  OD1  doub N N 100 
ASP   CG  OD2  sing N N 101 
ASP   OD2 HD2  sing N N 102 
ASP   OXT HXT  sing N N 103 
GLN   N   CA   sing N N 104 
GLN   N   H    sing N N 105 
GLN   N   H2   sing N N 106 
GLN   CA  C    sing N N 107 
GLN   CA  CB   sing N N 108 
GLN   CA  HA   sing N N 109 
GLN   C   O    doub N N 110 
GLN   C   OXT  sing N N 111 
GLN   CB  CG   sing N N 112 
GLN   CB  HB2  sing N N 113 
GLN   CB  HB3  sing N N 114 
GLN   CG  CD   sing N N 115 
GLN   CG  HG2  sing N N 116 
GLN   CG  HG3  sing N N 117 
GLN   CD  OE1  doub N N 118 
GLN   CD  NE2  sing N N 119 
GLN   NE2 HE21 sing N N 120 
GLN   NE2 HE22 sing N N 121 
GLN   OXT HXT  sing N N 122 
GLU   N   CA   sing N N 123 
GLU   N   H    sing N N 124 
GLU   N   H2   sing N N 125 
GLU   CA  C    sing N N 126 
GLU   CA  CB   sing N N 127 
GLU   CA  HA   sing N N 128 
GLU   C   O    doub N N 129 
GLU   C   OXT  sing N N 130 
GLU   CB  CG   sing N N 131 
GLU   CB  HB2  sing N N 132 
GLU   CB  HB3  sing N N 133 
GLU   CG  CD   sing N N 134 
GLU   CG  HG2  sing N N 135 
GLU   CG  HG3  sing N N 136 
GLU   CD  OE1  doub N N 137 
GLU   CD  OE2  sing N N 138 
GLU   OE2 HE2  sing N N 139 
GLU   OXT HXT  sing N N 140 
GLY   N   CA   sing N N 141 
GLY   N   H    sing N N 142 
GLY   N   H2   sing N N 143 
GLY   CA  C    sing N N 144 
GLY   CA  HA2  sing N N 145 
GLY   CA  HA3  sing N N 146 
GLY   C   O    doub N N 147 
GLY   C   OXT  sing N N 148 
GLY   OXT HXT  sing N N 149 
HIS   N   CA   sing N N 150 
HIS   N   H    sing N N 151 
HIS   N   H2   sing N N 152 
HIS   CA  C    sing N N 153 
HIS   CA  CB   sing N N 154 
HIS   CA  HA   sing N N 155 
HIS   C   O    doub N N 156 
HIS   C   OXT  sing N N 157 
HIS   CB  CG   sing N N 158 
HIS   CB  HB2  sing N N 159 
HIS   CB  HB3  sing N N 160 
HIS   CG  ND1  sing Y N 161 
HIS   CG  CD2  doub Y N 162 
HIS   ND1 CE1  doub Y N 163 
HIS   ND1 HD1  sing N N 164 
HIS   CD2 NE2  sing Y N 165 
HIS   CD2 HD2  sing N N 166 
HIS   CE1 NE2  sing Y N 167 
HIS   CE1 HE1  sing N N 168 
HIS   NE2 HE2  sing N N 169 
HIS   OXT HXT  sing N N 170 
HOH   O   H1   sing N N 171 
HOH   O   H2   sing N N 172 
ILE   N   CA   sing N N 173 
ILE   N   H    sing N N 174 
ILE   N   H2   sing N N 175 
ILE   CA  C    sing N N 176 
ILE   CA  CB   sing N N 177 
ILE   CA  HA   sing N N 178 
ILE   C   O    doub N N 179 
ILE   C   OXT  sing N N 180 
ILE   CB  CG1  sing N N 181 
ILE   CB  CG2  sing N N 182 
ILE   CB  HB   sing N N 183 
ILE   CG1 CD1  sing N N 184 
ILE   CG1 HG12 sing N N 185 
ILE   CG1 HG13 sing N N 186 
ILE   CG2 HG21 sing N N 187 
ILE   CG2 HG22 sing N N 188 
ILE   CG2 HG23 sing N N 189 
ILE   CD1 HD11 sing N N 190 
ILE   CD1 HD12 sing N N 191 
ILE   CD1 HD13 sing N N 192 
ILE   OXT HXT  sing N N 193 
LEU   N   CA   sing N N 194 
LEU   N   H    sing N N 195 
LEU   N   H2   sing N N 196 
LEU   CA  C    sing N N 197 
LEU   CA  CB   sing N N 198 
LEU   CA  HA   sing N N 199 
LEU   C   O    doub N N 200 
LEU   C   OXT  sing N N 201 
LEU   CB  CG   sing N N 202 
LEU   CB  HB2  sing N N 203 
LEU   CB  HB3  sing N N 204 
LEU   CG  CD1  sing N N 205 
LEU   CG  CD2  sing N N 206 
LEU   CG  HG   sing N N 207 
LEU   CD1 HD11 sing N N 208 
LEU   CD1 HD12 sing N N 209 
LEU   CD1 HD13 sing N N 210 
LEU   CD2 HD21 sing N N 211 
LEU   CD2 HD22 sing N N 212 
LEU   CD2 HD23 sing N N 213 
LEU   OXT HXT  sing N N 214 
LYS   N   CA   sing N N 215 
LYS   N   H    sing N N 216 
LYS   N   H2   sing N N 217 
LYS   CA  C    sing N N 218 
LYS   CA  CB   sing N N 219 
LYS   CA  HA   sing N N 220 
LYS   C   O    doub N N 221 
LYS   C   OXT  sing N N 222 
LYS   CB  CG   sing N N 223 
LYS   CB  HB2  sing N N 224 
LYS   CB  HB3  sing N N 225 
LYS   CG  CD   sing N N 226 
LYS   CG  HG2  sing N N 227 
LYS   CG  HG3  sing N N 228 
LYS   CD  CE   sing N N 229 
LYS   CD  HD2  sing N N 230 
LYS   CD  HD3  sing N N 231 
LYS   CE  NZ   sing N N 232 
LYS   CE  HE2  sing N N 233 
LYS   CE  HE3  sing N N 234 
LYS   NZ  HZ1  sing N N 235 
LYS   NZ  HZ2  sing N N 236 
LYS   NZ  HZ3  sing N N 237 
LYS   OXT HXT  sing N N 238 
MET   N   CA   sing N N 239 
MET   N   H    sing N N 240 
MET   N   H2   sing N N 241 
MET   CA  C    sing N N 242 
MET   CA  CB   sing N N 243 
MET   CA  HA   sing N N 244 
MET   C   O    doub N N 245 
MET   C   OXT  sing N N 246 
MET   CB  CG   sing N N 247 
MET   CB  HB2  sing N N 248 
MET   CB  HB3  sing N N 249 
MET   CG  SD   sing N N 250 
MET   CG  HG2  sing N N 251 
MET   CG  HG3  sing N N 252 
MET   SD  CE   sing N N 253 
MET   CE  HE1  sing N N 254 
MET   CE  HE2  sing N N 255 
MET   CE  HE3  sing N N 256 
MET   OXT HXT  sing N N 257 
PHE   N   CA   sing N N 258 
PHE   N   H    sing N N 259 
PHE   N   H2   sing N N 260 
PHE   CA  C    sing N N 261 
PHE   CA  CB   sing N N 262 
PHE   CA  HA   sing N N 263 
PHE   C   O    doub N N 264 
PHE   C   OXT  sing N N 265 
PHE   CB  CG   sing N N 266 
PHE   CB  HB2  sing N N 267 
PHE   CB  HB3  sing N N 268 
PHE   CG  CD1  doub Y N 269 
PHE   CG  CD2  sing Y N 270 
PHE   CD1 CE1  sing Y N 271 
PHE   CD1 HD1  sing N N 272 
PHE   CD2 CE2  doub Y N 273 
PHE   CD2 HD2  sing N N 274 
PHE   CE1 CZ   doub Y N 275 
PHE   CE1 HE1  sing N N 276 
PHE   CE2 CZ   sing Y N 277 
PHE   CE2 HE2  sing N N 278 
PHE   CZ  HZ   sing N N 279 
PHE   OXT HXT  sing N N 280 
PRO   N   CA   sing N N 281 
PRO   N   CD   sing N N 282 
PRO   N   H    sing N N 283 
PRO   CA  C    sing N N 284 
PRO   CA  CB   sing N N 285 
PRO   CA  HA   sing N N 286 
PRO   C   O    doub N N 287 
PRO   C   OXT  sing N N 288 
PRO   CB  CG   sing N N 289 
PRO   CB  HB2  sing N N 290 
PRO   CB  HB3  sing N N 291 
PRO   CG  CD   sing N N 292 
PRO   CG  HG2  sing N N 293 
PRO   CG  HG3  sing N N 294 
PRO   CD  HD2  sing N N 295 
PRO   CD  HD3  sing N N 296 
PRO   OXT HXT  sing N N 297 
SER   N   CA   sing N N 298 
SER   N   H    sing N N 299 
SER   N   H2   sing N N 300 
SER   CA  C    sing N N 301 
SER   CA  CB   sing N N 302 
SER   CA  HA   sing N N 303 
SER   C   O    doub N N 304 
SER   C   OXT  sing N N 305 
SER   CB  OG   sing N N 306 
SER   CB  HB2  sing N N 307 
SER   CB  HB3  sing N N 308 
SER   OG  HG   sing N N 309 
SER   OXT HXT  sing N N 310 
THR   N   CA   sing N N 311 
THR   N   H    sing N N 312 
THR   N   H2   sing N N 313 
THR   CA  C    sing N N 314 
THR   CA  CB   sing N N 315 
THR   CA  HA   sing N N 316 
THR   C   O    doub N N 317 
THR   C   OXT  sing N N 318 
THR   CB  OG1  sing N N 319 
THR   CB  CG2  sing N N 320 
THR   CB  HB   sing N N 321 
THR   OG1 HG1  sing N N 322 
THR   CG2 HG21 sing N N 323 
THR   CG2 HG22 sing N N 324 
THR   CG2 HG23 sing N N 325 
THR   OXT HXT  sing N N 326 
TRP   N   CA   sing N N 327 
TRP   N   H    sing N N 328 
TRP   N   H2   sing N N 329 
TRP   CA  C    sing N N 330 
TRP   CA  CB   sing N N 331 
TRP   CA  HA   sing N N 332 
TRP   C   O    doub N N 333 
TRP   C   OXT  sing N N 334 
TRP   CB  CG   sing N N 335 
TRP   CB  HB2  sing N N 336 
TRP   CB  HB3  sing N N 337 
TRP   CG  CD1  doub Y N 338 
TRP   CG  CD2  sing Y N 339 
TRP   CD1 NE1  sing Y N 340 
TRP   CD1 HD1  sing N N 341 
TRP   CD2 CE2  doub Y N 342 
TRP   CD2 CE3  sing Y N 343 
TRP   NE1 CE2  sing Y N 344 
TRP   NE1 HE1  sing N N 345 
TRP   CE2 CZ2  sing Y N 346 
TRP   CE3 CZ3  doub Y N 347 
TRP   CE3 HE3  sing N N 348 
TRP   CZ2 CH2  doub Y N 349 
TRP   CZ2 HZ2  sing N N 350 
TRP   CZ3 CH2  sing Y N 351 
TRP   CZ3 HZ3  sing N N 352 
TRP   CH2 HH2  sing N N 353 
TRP   OXT HXT  sing N N 354 
TYR   N   CA   sing N N 355 
TYR   N   H    sing N N 356 
TYR   N   H2   sing N N 357 
TYR   CA  C    sing N N 358 
TYR   CA  CB   sing N N 359 
TYR   CA  HA   sing N N 360 
TYR   C   O    doub N N 361 
TYR   C   OXT  sing N N 362 
TYR   CB  CG   sing N N 363 
TYR   CB  HB2  sing N N 364 
TYR   CB  HB3  sing N N 365 
TYR   CG  CD1  doub Y N 366 
TYR   CG  CD2  sing Y N 367 
TYR   CD1 CE1  sing Y N 368 
TYR   CD1 HD1  sing N N 369 
TYR   CD2 CE2  doub Y N 370 
TYR   CD2 HD2  sing N N 371 
TYR   CE1 CZ   doub Y N 372 
TYR   CE1 HE1  sing N N 373 
TYR   CE2 CZ   sing Y N 374 
TYR   CE2 HE2  sing N N 375 
TYR   CZ  OH   sing N N 376 
TYR   OH  HH   sing N N 377 
TYR   OXT HXT  sing N N 378 
VAL   N   CA   sing N N 379 
VAL   N   H    sing N N 380 
VAL   N   H2   sing N N 381 
VAL   CA  C    sing N N 382 
VAL   CA  CB   sing N N 383 
VAL   CA  HA   sing N N 384 
VAL   C   O    doub N N 385 
VAL   C   OXT  sing N N 386 
VAL   CB  CG1  sing N N 387 
VAL   CB  CG2  sing N N 388 
VAL   CB  HB   sing N N 389 
VAL   CG1 HG11 sing N N 390 
VAL   CG1 HG12 sing N N 391 
VAL   CG1 HG13 sing N N 392 
VAL   CG2 HG21 sing N N 393 
VAL   CG2 HG22 sing N N 394 
VAL   CG2 HG23 sing N N 395 
VAL   OXT HXT  sing N N 396 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFC2301405 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         'Crystallographic fragment screening of Human heat shock protein 90' 
_pdbx_deposit_group.group_description   
;Heat shock protein 90 (HSP90) is one of the most active molecular chaperones in cells. It plays a vital role in the cell maturation process and serves as a molecular chaperone involved in many oncogenic proteins folding, assembly and stabilization. Many HSP90 client proteins are kinases or transcription factors involved in signal transduction pathways and are key regulatory factors in tumor growth and maintenance. Therefore, HSP90 inhibitors can be used as drugs for cancer treatment.
;
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002298 
# 
_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                    7HAY 
_atom_sites.fract_transf_matrix[1][1]   0.014531 
_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]   0.011079 
_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]   0.010062 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
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.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 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   . GLU   A 1 9   ? 7.00267   15.89300 11.19632 1.000 61.97286  ? 16  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 9   ? 8.31523   16.52160 11.28118 1.000 60.22773  ? 16  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 9   ? 8.41322   17.40580 12.51885 1.000 57.16538  ? 16  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 9   ? 7.56116   18.26466 12.74988 1.000 60.48628  ? 16  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 9   ? 8.60113   17.34115 10.02224 1.000 62.55834  ? 16  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 9   ? 10.07278  17.40518 9.63149  1.000 71.34342  ? 16  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 9   ? 10.82516  16.12193 9.94221  1.000 85.89312  ? 16  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 9   ? 10.79227  15.19176 9.10738  1.000 78.32695  ? 16  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 9   ? 11.46276  16.04911 11.01464 1.000 88.39892  ? 16  GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 10  ? 9.45947   17.19203 13.31228 1.000 45.64140  ? 17  VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 10  ? 9.65557   17.89166 14.57578 1.000 42.12733  ? 17  VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 10  ? 11.00706  18.58943 14.53725 1.000 39.53495  ? 17  VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 10  ? 12.02909  17.95734 14.24607 1.000 40.13964  ? 17  VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 10  ? 9.57358   16.92748 15.77358 1.000 42.42904  ? 17  VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 10  ? 9.63885   17.69651 17.08303 1.000 39.19314  ? 17  VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 10  ? 8.30388   16.08887 15.69715 1.000 45.93379  ? 17  VAL   A CG2 1 
ATOM   17   N  N   . GLU   A 1 11  ? 11.01092  19.88628 14.83118 1.000 37.13070  ? 18  GLU   A N   1 
ATOM   18   C  CA  . GLU   A 1 11  ? 12.23566  20.67135 14.90388 1.000 36.82543  ? 18  GLU   A CA  1 
ATOM   19   C  C   . GLU   A 1 11  ? 12.57907  20.93957 16.36217 1.000 32.73974  ? 18  GLU   A C   1 
ATOM   20   O  O   . GLU   A 1 11  ? 11.70762  21.32394 17.14870 1.000 31.89669  ? 18  GLU   A O   1 
ATOM   21   C  CB  . GLU   A 1 11  ? 12.08972  21.99114 14.14643 1.000 34.76635  ? 18  GLU   A CB  1 
ATOM   22   C  CG  . GLU   A 1 11  ? 11.88350  21.83460 12.65256 1.000 40.64576  ? 18  GLU   A CG  1 
ATOM   23   C  CD  . GLU   A 1 11  ? 11.78629  23.16898 11.93868 1.000 51.63693  ? 18  GLU   A CD  1 
ATOM   24   O  OE1 . GLU   A 1 11  ? 10.80784  23.90766 12.18086 1.000 37.83146  ? 18  GLU   A OE1 1 
ATOM   25   O  OE2 . GLU   A 1 11  ? 12.69291  23.48245 11.13973 1.000 48.53748  ? 18  GLU   A OE2 1 
ATOM   26   N  N   . THR   A 1 12  ? 13.84534  20.74035 16.71551 1.000 32.09606  ? 19  THR   A N   1 
ATOM   27   C  CA  . THR   A 1 12  ? 14.32537  20.91645 18.07911 1.000 30.52415  ? 19  THR   A CA  1 
ATOM   28   C  C   . THR   A 1 12  ? 15.23659  22.13386 18.14593 1.000 30.67124  ? 19  THR   A C   1 
ATOM   29   O  O   . THR   A 1 12  ? 16.20132  22.23632 17.38029 1.000 30.86007  ? 19  THR   A O   1 
ATOM   30   C  CB  . THR   A 1 12  ? 15.07115  19.67082 18.56056 1.000 31.72632  ? 19  THR   A CB  1 
ATOM   31   O  OG1 . THR   A 1 12  ? 14.17006  18.55707 18.58768 1.000 33.49001  ? 19  THR   A OG1 1 
ATOM   32   C  CG2 . THR   A 1 12  ? 15.63591  19.89154 19.95542 1.000 30.59803  ? 19  THR   A CG2 1 
ATOM   33   N  N   . PHE   A 1 13  ? 14.92860  23.04983 19.06003 1.000 27.70473  ? 20  PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 13  ? 15.68736  24.27803 19.23121 1.000 29.03416  ? 20  PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 13  ? 16.22669  24.36209 20.65046 1.000 32.02924  ? 20  PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 13  ? 15.68728  23.74991 21.57583 1.000 33.05277  ? 20  PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 13  ? 14.83301  25.51903 18.95180 1.000 28.68821  ? 20  PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 13  ? 14.13854  25.49772 17.62385 1.000 28.96708  ? 20  PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 13  ? 12.91905  24.85792 17.47769 1.000 31.64786  ? 20  PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 13  ? 14.69457  26.13004 16.52539 1.000 28.71405  ? 20  PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 13  ? 12.27148  24.84002 16.25947 1.000 31.93398  ? 20  PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 13  ? 14.05176  26.11662 15.30269 1.000 32.24171  ? 20  PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 13  ? 12.83821  25.47029 15.16944 1.000 30.88170  ? 20  PHE   A CZ  1 
ATOM   44   N  N   . ALA   A 1 14  ? 17.28731  25.14340 20.81329 1.000 29.69520  ? 21  ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 14  ? 17.89660  25.37872 22.11198 1.000 35.13651  ? 21  ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 14  ? 17.43918  26.72105 22.66380 1.000 39.00294  ? 21  ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 14  ? 17.29716  27.69595 21.91968 1.000 33.02775  ? 21  ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 14  ? 19.42285  25.34983 22.01357 1.000 27.90756  ? 21  ALA   A CB  1 
ATOM   49   N  N   . PHE   A 1 15  ? 17.19953  26.76295 23.96949 1.000 32.41844  ? 22  PHE   A N   1 
ATOM   50   C  CA  . PHE   A 1 15  ? 16.91226  28.02800 24.62554 1.000 31.49234  ? 22  PHE   A CA  1 
ATOM   51   C  C   . PHE   A 1 15  ? 18.17213  28.87696 24.68775 1.000 28.91417  ? 22  PHE   A C   1 
ATOM   52   O  O   . PHE   A 1 15  ? 19.28635  28.35540 24.78634 1.000 32.92937  ? 22  PHE   A O   1 
ATOM   53   C  CB  . PHE   A 1 15  ? 16.38050  27.78856 26.03716 1.000 31.05354  ? 22  PHE   A CB  1 
ATOM   54   C  CG  . PHE   A 1 15  ? 14.92181  27.45163 26.08729 1.000 35.43994  ? 22  PHE   A CG  1 
ATOM   55   C  CD1 . PHE   A 1 15  ? 13.96459  28.39388 25.74991 1.000 23.98004  ? 22  PHE   A CD1 1 
ATOM   56   C  CD2 . PHE   A 1 15  ? 14.50709  26.18498 26.45749 1.000 28.29105  ? 22  PHE   A CD2 1 
ATOM   57   C  CE1 . PHE   A 1 15  ? 12.61814  28.08174 25.79396 1.000 33.80615  ? 22  PHE   A CE1 1 
ATOM   58   C  CE2 . PHE   A 1 15  ? 13.16319  25.86583 26.50081 1.000 32.17535  ? 22  PHE   A CE2 1 
ATOM   59   C  CZ  . PHE   A 1 15  ? 12.21708  26.81578 26.16911 1.000 24.38114  ? 22  PHE   A CZ  1 
ATOM   60   N  N   . GLN   A 1 16  ? 17.99643  30.19258 24.61471 1.000 34.50881  ? 23  GLN   A N   1 
ATOM   61   C  CA  . GLN   A 1 16  ? 19.09438  31.08043 24.95914 1.000 33.72399  ? 23  GLN   A CA  1 
ATOM   62   C  C   . GLN   A 1 16  ? 19.51005  30.82161 26.40228 1.000 37.31343  ? 23  GLN   A C   1 
ATOM   63   O  O   . GLN   A 1 16  ? 18.68701  30.46973 27.25254 1.000 33.44127  ? 23  GLN   A O   1 
ATOM   64   C  CB  . GLN   A 1 16  ? 18.69104  32.54313 24.76839 1.000 39.95263  ? 23  GLN   A CB  1 
ATOM   65   C  CG  . GLN   A 1 16  ? 18.55645  32.97007 23.31709 1.000 36.05754  ? 23  GLN   A CG  1 
ATOM   66   C  CD  . GLN   A 1 16  ? 17.12101  32.94560 22.83617 1.000 38.57715  ? 23  GLN   A CD  1 
ATOM   67   O  OE1 . GLN   A 1 16  ? 16.35862  32.04184 23.17534 1.000 33.16737  ? 23  GLN   A OE1 1 
ATOM   68   N  NE2 . GLN   A 1 16  ? 16.74112  33.94688 22.04907 1.000 34.61153  ? 23  GLN   A NE2 1 
ATOM   69   N  N   . ALA   A 1 17  ? 20.80961  30.97586 26.67018 1.000 38.03265  ? 24  ALA   A N   1 
ATOM   70   C  CA  . ALA   A 1 17  ? 21.34399  30.62271 27.98332 1.000 40.29874  ? 24  ALA   A CA  1 
ATOM   71   C  C   . ALA   A 1 17  ? 20.62015  31.36013 29.10253 1.000 43.38801  ? 24  ALA   A C   1 
ATOM   72   O  O   . ALA   A 1 17  ? 20.40644  30.80677 30.18786 1.000 38.50289  ? 24  ALA   A O   1 
ATOM   73   C  CB  . ALA   A 1 17  ? 22.84362  30.91507 28.03534 1.000 38.88973  ? 24  ALA   A CB  1 
ATOM   74   N  N   . GLU   A 1 18  ? 20.22561  32.60877 28.85217 1.000 35.85866  ? 25  GLU   A N   1 
ATOM   75   C  CA  . GLU   A 1 18  ? 19.53641  33.38489 29.87585 1.000 39.23315  ? 25  GLU   A CA  1 
ATOM   76   C  C   . GLU   A 1 18  ? 18.17671  32.77902 30.20721 1.000 42.38351  ? 25  GLU   A C   1 
ATOM   77   O  O   . GLU   A 1 18  ? 17.84387  32.59905 31.38478 1.000 36.43448  ? 25  GLU   A O   1 
ATOM   78   C  CB  . GLU   A 1 18  ? 19.39425  34.83969 29.42037 1.000 41.47809  ? 25  GLU   A CB  1 
ATOM   79   C  CG  . GLU   A 1 18  ? 20.71954  35.53466 29.08393 1.000 55.11809  ? 25  GLU   A CG  1 
ATOM   80   C  CD  . GLU   A 1 18  ? 21.28123  35.15468 27.71775 1.000 57.63367  ? 25  GLU   A CD  1 
ATOM   81   O  OE1 . GLU   A 1 18  ? 20.64550  34.34715 27.00740 1.000 58.17025  ? 25  GLU   A OE1 1 
ATOM   82   O  OE2 . GLU   A 1 18  ? 22.37067  35.65330 27.36122 1.000 67.62926  ? 25  GLU   A OE2 1 
ATOM   83   N  N   . ILE   A 1 19  ? 17.38410  32.44572 29.18440 1.000 32.06466  ? 26  ILE   A N   1 
ATOM   84   C  CA  . ILE   A 1 19  ? 16.07131  31.85156 29.42388 1.000 29.89227  ? 26  ILE   A CA  1 
ATOM   85   C  C   . ILE   A 1 19  ? 16.21488  30.48038 30.07177 1.000 35.13434  ? 26  ILE   A C   1 
ATOM   86   O  O   . ILE   A 1 19  ? 15.45848  30.12917 30.98597 1.000 34.71856  ? 26  ILE   A O   1 
ATOM   87   C  CB  . ILE   A 1 19  ? 15.26438  31.77370 28.11321 1.000 32.57226  ? 26  ILE   A CB  1 
ATOM   88   C  CG1 . ILE   A 1 19  ? 14.88046  33.17150 27.62603 1.000 31.22561  ? 26  ILE   A CG1 1 
ATOM   89   C  CG2 . ILE   A 1 19  ? 14.01311  30.92294 28.29712 1.000 34.59397  ? 26  ILE   A CG2 1 
ATOM   90   C  CD1 . ILE   A 1 19  ? 15.77298  33.69956 26.52867 1.000 48.90792  ? 26  ILE   A CD1 1 
ATOM   91   N  N   . ALA   A 1 20  ? 17.19513  29.69236 29.62225 1.000 34.65694  ? 27  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 20  ? 17.36440  28.33791 30.14048 1.000 34.92688  ? 27  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 20  ? 17.63905  28.34759 31.63910 1.000 35.07387  ? 27  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 20  ? 17.04667  27.56936 32.39567 1.000 32.61016  ? 27  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 20  ? 18.49218  27.62765 29.39146 1.000 31.00749  ? 27  ALA   A CB  1 
ATOM   96   N  N   . GLN   A 1 21  ? 18.53348  29.22821 32.08950 1.000 31.08039  ? 28  GLN   A N   1 
ATOM   97   C  CA  . GLN   A 1 21  ? 18.89176  29.25942 33.50099 1.000 40.94409  ? 28  GLN   A CA  1 
ATOM   98   C  C   . GLN   A 1 21  ? 17.84481  29.96029 34.35898 1.000 37.26279  ? 28  GLN   A C   1 
ATOM   99   O  O   . GLN   A 1 21  ? 17.83328  29.76279 35.57868 1.000 35.19707  ? 28  GLN   A O   1 
ATOM   100  C  CB  . GLN   A 1 21  ? 20.26488  29.91562 33.68078 1.000 44.88992  ? 28  GLN   A CB  1 
ATOM   101  C  CG  . GLN   A 1 21  ? 20.23372  31.38470 34.05353 1.000 48.57718  ? 28  GLN   A CG  1 
ATOM   102  C  CD  . GLN   A 1 21  ? 21.47137  32.13588 33.58509 1.000 63.65472  ? 28  GLN   A CD  1 
ATOM   103  O  OE1 . GLN   A 1 21  ? 22.08818  31.77586 32.58165 1.000 58.42595  ? 28  GLN   A OE1 1 
ATOM   104  N  NE2 . GLN   A 1 21  ? 21.84340  33.18058 34.31692 1.000 59.13914  ? 28  GLN   A NE2 1 
ATOM   105  N  N   . LEU   A 1 22  ? 16.96495  30.76788 33.76111 1.000 34.73405  ? 29  LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 22  ? 15.80696  31.24494 34.51020 1.000 36.93349  ? 29  LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 22  ? 14.79899  30.12368 34.71299 1.000 38.26149  ? 29  LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 22  ? 14.20027  30.00469 35.78911 1.000 32.32674  ? 29  LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 22  ? 15.14522  32.42340 33.79729 1.000 33.03401  ? 29  LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 22  ? 13.71128  32.72945 34.25039 1.000 41.67179  ? 29  LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 22  ? 13.70232  33.31205 35.66082 1.000 34.17725  ? 29  LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 22  ? 12.99103  33.65382 33.27681 1.000 49.25139  ? 29  LEU   A CD2 1 
ATOM   113  N  N   . MET   A 1 23  ? 14.60250  29.28842 33.68906 1.000 32.82247  ? 30  MET   A N   1 
ATOM   114  C  CA  . MET   A 1 23  ? 13.66208  28.18185 33.81595 1.000 36.87212  ? 30  MET   A CA  1 
ATOM   115  C  C   . MET   A 1 23  ? 14.10148  27.21996 34.90866 1.000 38.64141  ? 30  MET   A C   1 
ATOM   116  O  O   . MET   A 1 23  ? 13.28132  26.76609 35.71463 1.000 34.10429  ? 30  MET   A O   1 
ATOM   117  C  CB  . MET   A 1 23  ? 13.52556  27.43990 32.48859 1.000 30.85088  ? 30  MET   A CB  1 
ATOM   118  C  CG  . MET   A 1 23  ? 12.36418  27.90035 31.63872 1.000 28.87550  ? 30  MET   A CG  1 
ATOM   119  S  SD  . MET   A 1 23  ? 12.66736  27.58748 29.89418 1.000 34.60970  ? 30  MET   A SD  1 
ATOM   120  C  CE  . MET   A 1 23  ? 11.86893  25.98884 29.75885 1.000 33.28389  ? 30  MET   A CE  1 
ATOM   121  N  N   . SER   A 1 24  ? 15.39667  26.89942 34.95179 1.000 30.26552  ? 31  SER   A N   1 
ATOM   122  C  CA  . SER   A 1 24  ? 15.90781  26.03728 36.00952 1.000 35.53804  ? 31  SER   A CA  1 
ATOM   123  C  C   . SER   A 1 24  ? 15.77979  26.69665 37.37477 1.000 34.97952  ? 31  SER   A C   1 
ATOM   124  O  O   . SER   A 1 24  ? 15.60200  26.00359 38.38228 1.000 39.24958  ? 31  SER   A O   1 
ATOM   125  C  CB  . SER   A 1 24  ? 17.36540  25.67492 35.73506 1.000 32.53842  ? 31  SER   A CB  1 
ATOM   126  O  OG  . SER   A 1 24  ? 18.23478  26.51755 36.47018 1.000 58.43427  ? 31  SER   A OG  1 
ATOM   127  N  N   . LEU   A 1 25  ? 15.87513  28.02655 37.42969 1.000 38.21027  ? 32  LEU   A N   1 
ATOM   128  C  CA  . LEU   A 1 25  ? 15.68235  28.72731 38.69392 1.000 33.50333  ? 32  LEU   A CA  1 
ATOM   129  C  C   . LEU   A 1 25  ? 14.24178  28.60659 39.17419 1.000 37.39015  ? 32  LEU   A C   1 
ATOM   130  O  O   . LEU   A 1 25  ? 13.99403  28.43119 40.37160 1.000 39.80068  ? 32  LEU   A O   1 
ATOM   131  C  CB  . LEU   A 1 25  ? 16.08092  30.19478 38.54484 1.000 35.17470  ? 32  LEU   A CB  1 
ATOM   132  C  CG  . LEU   A 1 25  ? 16.29945  30.98513 39.83534 1.000 47.08867  ? 32  LEU   A CG  1 
ATOM   133  C  CD1 . LEU   A 1 25  ? 17.73959  30.84848 40.30244 1.000 57.24296  ? 32  LEU   A CD1 1 
ATOM   134  C  CD2 . LEU   A 1 25  ? 15.93672  32.44908 39.63645 1.000 48.93552  ? 32  LEU   A CD2 1 
ATOM   135  N  N   . ILE   A 1 26  ? 13.27853  28.69155 38.25423 1.000 32.22048  ? 33  ILE   A N   1 
ATOM   136  C  CA  . ILE   A 1 26  ? 11.87744  28.53161 38.63014 1.000 36.26048  ? 33  ILE   A CA  1 
ATOM   137  C  C   . ILE   A 1 26  ? 11.58480  27.08684 39.02470 1.000 34.14212  ? 33  ILE   A C   1 
ATOM   138  O  O   . ILE   A 1 26  ? 10.74818  26.83010 39.89983 1.000 31.68066  ? 33  ILE   A O   1 
ATOM   139  C  CB  . ILE   A 1 26  ? 10.97102  29.01401 37.47966 1.000 36.29542  ? 33  ILE   A CB  1 
ATOM   140  C  CG1 . ILE   A 1 26  ? 10.97739  30.54263 37.40320 1.000 33.89804  ? 33  ILE   A CG1 1 
ATOM   141  C  CG2 . ILE   A 1 26  ? 9.54739   28.49637 37.63621 1.000 33.08291  ? 33  ILE   A CG2 1 
ATOM   142  C  CD1 . ILE   A 1 26  ? 10.39433  31.08981 36.12126 1.000 34.86590  ? 33  ILE   A CD1 1 
ATOM   143  N  N   . ILE   A 1 27  ? 12.28290  26.12579 38.41886 1.000 35.86788  ? 34  ILE   A N   1 
ATOM   144  C  CA  . ILE   A 1 27  ? 12.02747  24.71736 38.70704 1.000 39.04117  ? 34  ILE   A CA  1 
ATOM   145  C  C   . ILE   A 1 27  ? 12.65386  24.29920 40.03484 1.000 40.83512  ? 34  ILE   A C   1 
ATOM   146  O  O   . ILE   A 1 27  ? 12.06913  23.50936 40.78539 1.000 52.10205  ? 34  ILE   A O   1 
ATOM   147  C  CB  . ILE   A 1 27  ? 12.53056  23.84470 37.54064 1.000 45.76675  ? 34  ILE   A CB  1 
ATOM   148  C  CG1 . ILE   A 1 27  ? 11.70415  24.10449 36.27756 1.000 34.16109  ? 34  ILE   A CG1 1 
ATOM   149  C  CG2 . ILE   A 1 27  ? 12.51469  22.36913 37.91368 1.000 50.32527  ? 34  ILE   A CG2 1 
ATOM   150  C  CD1 . ILE   A 1 27  ? 10.58744  23.10445 36.04523 1.000 43.55178  ? 34  ILE   A CD1 1 
ATOM   151  N  N   . ASN   A 1 28  ? 13.83709  24.82561 40.35856 1.000 45.14275  ? 35  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 28  ? 14.61878  24.31189 41.47785 1.000 52.46775  ? 35  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 28  ? 14.50407  25.13363 42.75713 1.000 57.08721  ? 35  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 28  ? 14.85670  24.62443 43.82686 1.000 58.86488  ? 35  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 28  ? 16.09887  24.21268 41.08525 1.000 50.54669  ? 35  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 28  ? 16.31591  23.38038 39.83576 1.000 56.87519  ? 35  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 28  ? 15.63429  22.37866 39.61712 1.000 62.08795  ? 35  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 28  ? 17.27030  23.79160 39.00864 1.000 53.66761  ? 35  ASN   A ND2 1 
ATOM   159  N  N   . THR   A 1 29  ? 14.02886  26.37521 42.68621 1.000 47.50357  ? 36  THR   A N   1 
ATOM   160  C  CA  . THR   A 1 29  ? 13.98000  27.23102 43.86603 1.000 54.39542  ? 36  THR   A CA  1 
ATOM   161  C  C   . THR   A 1 29  ? 12.77957  26.88278 44.73852 1.000 47.45677  ? 36  THR   A C   1 
ATOM   162  O  O   . THR   A 1 29  ? 11.67848  26.63591 44.23823 1.000 38.62823  ? 36  THR   A O   1 
ATOM   163  C  CB  . THR   A 1 29  ? 13.91789  28.70646 43.46071 1.000 61.79771  ? 36  THR   A CB  1 
ATOM   164  O  OG1 . THR   A 1 29  ? 15.08650  29.04665 42.70407 1.000 50.91401  ? 36  THR   A OG1 1 
ATOM   165  C  CG2 . THR   A 1 29  ? 13.84380  29.60987 44.68782 1.000 54.20853  ? 36  THR   A CG2 1 
ATOM   166  N  N   . PHE   A 1 30  ? 13.00261  26.86148 46.05219 1.000 45.05710  ? 37  PHE   A N   1 
ATOM   167  C  CA  . PHE   A 1 30  ? 11.93981  26.61137 47.02110 1.000 47.10425  ? 37  PHE   A CA  1 
ATOM   168  C  C   . PHE   A 1 30  ? 11.08527  27.86690 47.15106 1.000 50.13116  ? 37  PHE   A C   1 
ATOM   169  O  O   . PHE   A 1 30  ? 11.50409  28.85174 47.76840 1.000 54.26484  ? 37  PHE   A O   1 
ATOM   170  C  CB  . PHE   A 1 30  ? 12.53384  26.20523 48.36700 1.000 47.76325  ? 37  PHE   A CB  1 
ATOM   171  C  CG  . PHE   A 1 30  ? 11.50601  25.90408 49.42318 1.000 55.58750  ? 37  PHE   A CG  1 
ATOM   172  C  CD1 . PHE   A 1 30  ? 10.83315  24.69366 49.42643 1.000 55.94964  ? 37  PHE   A CD1 1 
ATOM   173  C  CD2 . PHE   A 1 30  ? 11.22275  26.82488 50.42039 1.000 54.50901  ? 37  PHE   A CD2 1 
ATOM   174  C  CE1 . PHE   A 1 30  ? 9.89143   24.40870 50.39866 1.000 53.43632  ? 37  PHE   A CE1 1 
ATOM   175  C  CE2 . PHE   A 1 30  ? 10.28139  26.54536 51.39602 1.000 51.88484  ? 37  PHE   A CE2 1 
ATOM   176  C  CZ  . PHE   A 1 30  ? 9.61560   25.33532 51.38429 1.000 51.94640  ? 37  PHE   A CZ  1 
ATOM   177  N  N   . TYR   A 1 31  ? 9.88752   27.83476 46.57018 1.000 40.92660  ? 38  TYR   A N   1 
ATOM   178  C  CA  . TYR   A 1 31  ? 8.98607   28.98454 46.59728 1.000 45.67719  ? 38  TYR   A CA  1 
ATOM   179  C  C   . TYR   A 1 31  ? 7.56302   28.45440 46.70674 1.000 43.47711  ? 38  TYR   A C   1 
ATOM   180  O  O   . TYR   A 1 31  ? 7.07387   27.79103 45.78705 1.000 36.38092  ? 38  TYR   A O   1 
ATOM   181  C  CB  . TYR   A 1 31  ? 9.16832   29.84953 45.35332 1.000 42.60789  ? 38  TYR   A CB  1 
ATOM   182  C  CG  . TYR   A 1 31  ? 8.34088   31.11248 45.34541 1.000 40.81019  ? 38  TYR   A CG  1 
ATOM   183  C  CD1 . TYR   A 1 31  ? 8.75457   32.24438 46.03744 1.000 44.05595  ? 38  TYR   A CD1 1 
ATOM   184  C  CD2 . TYR   A 1 31  ? 7.15470   31.17924 44.63059 1.000 37.92062  ? 38  TYR   A CD2 1 
ATOM   185  C  CE1 . TYR   A 1 31  ? 7.99954   33.40272 46.02769 1.000 52.44728  ? 38  TYR   A CE1 1 
ATOM   186  C  CE2 . TYR   A 1 31  ? 6.39651   32.33095 44.61360 1.000 42.73266  ? 38  TYR   A CE2 1 
ATOM   187  C  CZ  . TYR   A 1 31  ? 6.82153   33.43848 45.31282 1.000 47.39539  ? 38  TYR   A CZ  1 
ATOM   188  O  OH  . TYR   A 1 31  ? 6.06270   34.58457 45.29480 1.000 54.87633  ? 38  TYR   A OH  1 
ATOM   189  N  N   . SER   A 1 32  ? 6.90214   28.75066 47.82842 1.000 39.77561  ? 39  SER   A N   1 
ATOM   190  C  CA  . SER   A 1 32  ? 5.62508   28.11624 48.13999 1.000 44.56368  ? 39  SER   A CA  1 
ATOM   191  C  C   . SER   A 1 32  ? 4.44808   28.75939 47.41670 1.000 48.49563  ? 39  SER   A C   1 
ATOM   192  O  O   . SER   A 1 32  ? 3.45298   28.07830 47.14355 1.000 41.82721  ? 39  SER   A O   1 
ATOM   193  C  CB  . SER   A 1 32  ? 5.37978   28.14992 49.64871 1.000 43.07416  ? 39  SER   A CB  1 
ATOM   194  O  OG  . SER   A 1 32  ? 6.20892   27.21799 50.32051 1.000 47.16865  ? 39  SER   A OG  1 
ATOM   195  N  N   . ASN   A 1 33  ? 4.53305   30.05295 47.10277 1.000 42.66990  ? 40  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 33  ? 3.41648   30.78374 46.50186 1.000 45.43425  ? 40  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 33  ? 3.34313   30.51243 44.99587 1.000 41.32656  ? 40  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 33  ? 3.52109   31.39398 44.15597 1.000 46.57242  ? 40  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 33  ? 3.54774   32.27284 46.79747 1.000 39.09139  ? 40  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 33  ? 2.34074   33.06883 46.33991 1.000 44.77442  ? 40  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 33  ? 1.20090   32.62290 46.47458 1.000 42.88821  ? 40  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 33  ? 2.58649   34.25614 45.79645 1.000 37.39947  ? 40  ASN   A ND2 1 
ATOM   203  N  N   . LYS   A 1 34  ? 3.05120   29.25290 44.66445 1.000 30.60863  ? 41  LYS   A N   1 
ATOM   204  C  CA  . LYS   A 1 34  ? 3.04276   28.81733 43.27296 1.000 36.29119  ? 41  LYS   A CA  1 
ATOM   205  C  C   . LYS   A 1 34  ? 1.78661   29.23274 42.51975 1.000 36.87760  ? 41  LYS   A C   1 
ATOM   206  O  O   . LYS   A 1 34  ? 1.79663   29.22515 41.28407 1.000 31.74528  ? 41  LYS   A O   1 
ATOM   207  C  CB  . LYS   A 1 34  ? 3.19086   27.29671 43.19667 1.000 33.91272  ? 41  LYS   A CB  1 
ATOM   208  C  CG  . LYS   A 1 34  ? 4.53746   26.78444 43.67080 1.000 37.91498  ? 41  LYS   A CG  1 
ATOM   209  C  CD  . LYS   A 1 34  ? 4.58644   25.26593 43.65650 1.000 36.59937  ? 41  LYS   A CD  1 
ATOM   210  C  CE  . LYS   A 1 34  ? 5.93685   24.75341 44.13198 1.000 33.04082  ? 41  LYS   A CE  1 
ATOM   211  N  NZ  . LYS   A 1 34  ? 6.98780   24.91635 43.09362 1.000 32.98588  ? 41  LYS   A NZ  1 
ATOM   212  N  N   . GLU   A 1 35  ? 0.71568   29.59837 43.22916 1.000 26.62247  ? 42  GLU   A N   1 
ATOM   213  C  CA  . GLU   A 1 35  ? -0.56550  29.86741 42.58458 1.000 25.13645  ? 42  GLU   A CA  1 
ATOM   214  C  C   . GLU   A 1 35  ? -0.50058  31.01853 41.58975 1.000 31.47677  ? 42  GLU   A C   1 
ATOM   215  O  O   . GLU   A 1 35  ? -1.37758  31.12064 40.72486 1.000 26.21070  ? 42  GLU   A O   1 
ATOM   216  C  CB  . GLU   A 1 35  ? -1.62734  30.16971 43.64099 1.000 30.98136  ? 42  GLU   A CB  1 
ATOM   217  C  CG  . GLU   A 1 35  ? -1.38248  31.46555 44.39330 1.000 33.31663  ? 42  GLU   A CG  1 
ATOM   218  C  CD  . GLU   A 1 35  ? -2.35433  31.67123 45.53440 1.000 34.57053  ? 42  GLU   A CD  1 
ATOM   219  O  OE1 . GLU   A 1 35  ? -2.71709  30.67502 46.19251 1.000 41.48502  ? 42  GLU   A OE1 1 
ATOM   220  O  OE2 . GLU   A 1 35  ? -2.75346  32.82984 45.77488 1.000 45.44651  ? 42  GLU   A OE2 1 
ATOM   221  N  N   . ILE   A 1 36  ? 0.51201   31.88474 41.68767 1.000 24.91079  ? 43  ILE   A N   1 
ATOM   222  C  CA  . ILE   A 1 36  ? 0.59305   33.04764 40.81066 1.000 26.05496  ? 43  ILE   A CA  1 
ATOM   223  C  C   . ILE   A 1 36  ? 0.80694   32.66109 39.35586 1.000 34.21452  ? 43  ILE   A C   1 
ATOM   224  O  O   . ILE   A 1 36  ? 0.68139   33.51464 38.47034 1.000 30.65133  ? 43  ILE   A O   1 
ATOM   225  C  CB  . ILE   A 1 36  ? 1.70505   34.00520 41.28640 1.000 28.28483  ? 43  ILE   A CB  1 
ATOM   226  C  CG1 . ILE   A 1 36  ? 3.06673   33.30489 41.28848 1.000 32.11162  ? 43  ILE   A CG1 1 
ATOM   227  C  CG2 . ILE   A 1 36  ? 1.37579   34.55297 42.66630 1.000 30.62112  ? 43  ILE   A CG2 1 
ATOM   228  C  CD1 . ILE   A 1 36  ? 3.96454   33.70455 40.12937 1.000 39.09882  ? 43  ILE   A CD1 1 
ATOM   229  N  N   . PHE   A 1 37  ? 1.13826   31.39435 39.08561 1.000 23.28492  ? 44  PHE   A N   1 
ATOM   230  C  CA  . PHE   A 1 37  ? 1.25840   30.93113 37.70738 1.000 28.78483  ? 44  PHE   A CA  1 
ATOM   231  C  C   . PHE   A 1 37  ? -0.03252  31.17365 36.93583 1.000 26.52519  ? 44  PHE   A C   1 
ATOM   232  O  O   . PHE   A 1 37  ? -0.00228  31.54825 35.75768 1.000 25.47047  ? 44  PHE   A O   1 
ATOM   233  C  CB  . PHE   A 1 37  ? 1.63382   29.44357 37.68740 1.000 20.82667  ? 44  PHE   A CB  1 
ATOM   234  C  CG  . PHE   A 1 37  ? 0.44997   28.51352 37.79528 1.000 25.07878  ? 44  PHE   A CG  1 
ATOM   235  C  CD1 . PHE   A 1 37  ? -0.03922  28.12749 39.03424 1.000 26.02493  ? 44  PHE   A CD1 1 
ATOM   236  C  CD2 . PHE   A 1 37  ? -0.17993  28.03415 36.65694 1.000 28.25061  ? 44  PHE   A CD2 1 
ATOM   237  C  CE1 . PHE   A 1 37  ? -1.13128  27.28201 39.13404 1.000 22.61891  ? 44  PHE   A CE1 1 
ATOM   238  C  CE2 . PHE   A 1 37  ? -1.27517  27.19437 36.75273 1.000 20.37398  ? 44  PHE   A CE2 1 
ATOM   239  C  CZ  . PHE   A 1 37  ? -1.74815  26.81540 37.99140 1.000 25.15389  ? 44  PHE   A CZ  1 
ATOM   240  N  N   . LEU   A 1 38  ? -1.17932  30.96868 37.59059 1.000 24.04538  ? 45  LEU   A N   1 
ATOM   241  C  CA  . LEU   A 1 38  ? -2.46171  31.13366 36.91648 1.000 29.42640  ? 45  LEU   A CA  1 
ATOM   242  C  C   . LEU   A 1 38  ? -2.71772  32.59442 36.57805 1.000 28.30335  ? 45  LEU   A C   1 
ATOM   243  O  O   . LEU   A 1 38  ? -3.26617  32.90503 35.51431 1.000 25.61883  ? 45  LEU   A O   1 
ATOM   244  C  CB  . LEU   A 1 38  ? -3.58655  30.58088 37.79029 1.000 25.40829  ? 45  LEU   A CB  1 
ATOM   245  C  CG  . LEU   A 1 38  ? -4.95782  30.48387 37.12207 1.000 31.30510  ? 45  LEU   A CG  1 
ATOM   246  C  CD1 . LEU   A 1 38  ? -4.85417  29.72704 35.80466 1.000 19.07033  ? 45  LEU   A CD1 1 
ATOM   247  C  CD2 . LEU   A 1 38  ? -5.95844  29.81605 38.05243 1.000 27.16568  ? 45  LEU   A CD2 1 
ATOM   248  N  N   . ARG   A 1 39  ? -2.32594  33.50366 37.47306 1.000 23.59791  ? 46  ARG   A N   1 
ATOM   249  C  CA  . ARG   A 1 39  ? -2.48964  34.92722 37.20412 1.000 26.94120  ? 46  ARG   A CA  1 
ATOM   250  C  C   . ARG   A 1 39  ? -1.67983  35.35183 35.98653 1.000 31.96410  ? 46  ARG   A C   1 
ATOM   251  O  O   . ARG   A 1 39  ? -2.16794  36.10963 35.14020 1.000 29.28344  ? 46  ARG   A O   1 
ATOM   252  C  CB  . ARG   A 1 39  ? -2.08011  35.74178 38.43200 1.000 25.97501  ? 46  ARG   A CB  1 
ATOM   253  C  CG  . ARG   A 1 39  ? -1.88052  37.22514 38.15841 1.000 38.23589  ? 46  ARG   A CG  1 
ATOM   254  C  CD  . ARG   A 1 39  ? -1.34222  37.94990 39.38243 1.000 31.15422  ? 46  ARG   A CD  1 
ATOM   255  N  NE  . ARG   A 1 39  ? 0.11086   37.86658 39.46693 1.000 40.44697  ? 46  ARG   A NE  1 
ATOM   256  C  CZ  . ARG   A 1 39  ? 0.79830   37.88356 40.60078 1.000 56.41785  ? 46  ARG   A CZ  1 
ATOM   257  N  NH1 . ARG   A 1 39  ? 0.19458   37.98027 41.77426 1.000 51.05404  ? 46  ARG   A NH1 1 
ATOM   258  N  NH2 . ARG   A 1 39  ? 2.12504   37.80122 40.55636 1.000 51.77308  ? 46  ARG   A NH2 1 
ATOM   259  N  N   . GLU   A 1 40  ? -0.44298  34.86102 35.87465 1.000 27.14469  ? 47  GLU   A N   1 
ATOM   260  C  CA  . GLU   A 1 40  ? 0.42219   35.27106 34.77314 1.000 27.68060  ? 47  GLU   A CA  1 
ATOM   261  C  C   . GLU   A 1 40  ? -0.09971  34.76188 33.43557 1.000 30.22995  ? 47  GLU   A C   1 
ATOM   262  O  O   . GLU   A 1 40  ? -0.04467  35.47766 32.42824 1.000 32.04791  ? 47  GLU   A O   1 
ATOM   263  C  CB  . GLU   A 1 40  ? 1.84830   34.77472 35.01395 1.000 25.14896  ? 47  GLU   A CB  1 
ATOM   264  C  CG  . GLU   A 1 40  ? 2.49363   35.30241 36.28968 1.000 29.56756  ? 47  GLU   A CG  1 
ATOM   265  C  CD  . GLU   A 1 40  ? 2.43691   36.81738 36.39952 1.000 43.30098  ? 47  GLU   A CD  1 
ATOM   266  O  OE1 . GLU   A 1 40  ? 2.65237   37.50065 35.37654 1.000 34.46375  ? 47  GLU   A OE1 1 
ATOM   267  O  OE2 . GLU   A 1 40  ? 2.18013   37.32674 37.51158 1.000 44.47274  ? 47  GLU   A OE2 1 
ATOM   268  N  N   . LEU   A 1 41  ? -0.60555  33.52799 33.40331 1.000 27.68548  ? 48  LEU   A N   1 
ATOM   269  C  CA  . LEU   A 1 41  ? -1.10217  32.96866 32.15071 1.000 26.88941  ? 48  LEU   A CA  1 
ATOM   270  C  C   . LEU   A 1 41  ? -2.41647  33.62124 31.74119 1.000 31.25780  ? 48  LEU   A C   1 
ATOM   271  O  O   . LEU   A 1 41  ? -2.60989  33.96520 30.56900 1.000 30.59383  ? 48  LEU   A O   1 
ATOM   272  C  CB  . LEU   A 1 41  ? -1.26102  31.45454 32.28026 1.000 27.54820  ? 48  LEU   A CB  1 
ATOM   273  C  CG  . LEU   A 1 41  ? 0.04135   30.67122 32.46726 1.000 29.79763  ? 48  LEU   A CG  1 
ATOM   274  C  CD1 . LEU   A 1 41  ? -0.21477  29.16776 32.43125 1.000 31.09090  ? 48  LEU   A CD1 1 
ATOM   275  C  CD2 . LEU   A 1 41  ? 1.07352   31.07192 31.41736 1.000 20.86757  ? 48  LEU   A CD2 1 
ATOM   276  N  N   . ILE   A 1 42  ? -3.33415  33.79726 32.69631 1.000 28.02725  ? 49  ILE   A N   1 
ATOM   277  C  CA  . ILE   A 1 42  ? -4.58197  34.50202 32.41172 1.000 28.50416  ? 49  ILE   A CA  1 
ATOM   278  C  C   . ILE   A 1 42  ? -4.28962  35.91704 31.92992 1.000 34.30817  ? 49  ILE   A C   1 
ATOM   279  O  O   . ILE   A 1 42  ? -4.91899  36.41220 30.98619 1.000 30.39845  ? 49  ILE   A O   1 
ATOM   280  C  CB  . ILE   A 1 42  ? -5.49337  34.49946 33.65481 1.000 26.53317  ? 49  ILE   A CB  1 
ATOM   281  C  CG1 . ILE   A 1 42  ? -6.06461  33.10010 33.89798 1.000 26.08209  ? 49  ILE   A CG1 1 
ATOM   282  C  CG2 . ILE   A 1 42  ? -6.61507  35.52155 33.51142 1.000 27.22725  ? 49  ILE   A CG2 1 
ATOM   283  C  CD1 . ILE   A 1 42  ? -7.01118  33.02192 35.08118 1.000 28.61576  ? 49  ILE   A CD1 1 
ATOM   284  N  N   . SER   A 1 43  ? -3.32112  36.58465 32.56241 1.000 22.30487  ? 50  SER   A N   1 
ATOM   285  C  CA  . SER   A 1 43  ? -2.91975  37.91331 32.11236 1.000 34.62673  ? 50  SER   A CA  1 
ATOM   286  C  C   . SER   A 1 43  ? -2.34361  37.86582 30.70329 1.000 30.84108  ? 50  SER   A C   1 
ATOM   287  O  O   . SER   A 1 43  ? -2.56770  38.78089 29.90187 1.000 32.20064  ? 50  SER   A O   1 
ATOM   288  C  CB  . SER   A 1 43  ? -1.90685  38.51430 33.08772 1.000 25.54308  ? 50  SER   A CB  1 
ATOM   289  O  OG  . SER   A 1 43  ? -1.26664  39.64617 32.52569 1.000 33.08015  ? 50  SER   A OG  1 
ATOM   290  N  N   . ASN   A 1 44  ? -1.59066  36.80919 30.38542 1.000 28.75233  ? 51  ASN   A N   1 
ATOM   291  C  CA  . ASN   A 1 44  ? -1.08343  36.64683 29.02708 1.000 28.22573  ? 51  ASN   A CA  1 
ATOM   292  C  C   . ASN   A 1 44  ? -2.22403  36.45134 28.03838 1.000 32.39467  ? 51  ASN   A C   1 
ATOM   293  O  O   . ASN   A 1 44  ? -2.19622  36.99809 26.92950 1.000 28.90570  ? 51  ASN   A O   1 
ATOM   294  C  CB  . ASN   A 1 44  ? -0.11351  35.46777 28.96434 1.000 27.53067  ? 51  ASN   A CB  1 
ATOM   295  C  CG  . ASN   A 1 44  ? 1.30391   35.85884 29.33040 1.000 37.94162  ? 51  ASN   A CG  1 
ATOM   296  O  OD1 . ASN   A 1 44  ? 1.56069   36.98761 29.75227 1.000 35.61459  ? 51  ASN   A OD1 1 
ATOM   297  N  ND2 . ASN   A 1 44  ? 2.23504   34.92441 29.16984 1.000 24.99192  ? 51  ASN   A ND2 1 
ATOM   298  N  N   . SER   A 1 45  ? -3.23620  35.66997 28.42272 1.000 28.19751  ? 52  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 45  ? -4.40617  35.49978 27.56797 1.000 28.81194  ? 52  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 45  ? -5.15338  36.81571 27.39074 1.000 28.65476  ? 52  SER   A C   1 
ATOM   301  O  O   . SER   A 1 45  ? -5.60727  37.13736 26.28613 1.000 28.00137  ? 52  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 45  ? -5.33095  34.43357 28.15457 1.000 21.81210  ? 52  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 45  ? -4.76532  33.14110 28.02928 1.000 36.73435  ? 52  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 46  ? -5.28715  37.59160 28.46988 1.000 29.02227  ? 53  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 46  ? -5.98691  38.86958 28.38491 1.000 25.63220  ? 53  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 46  ? -5.28170  39.82541 27.43098 1.000 35.83396  ? 53  SER   A C   1 
ATOM   307  O  O   . SER   A 1 46  ? -5.93513  40.59570 26.71731 1.000 30.50233  ? 53  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 46  ? -6.10977  39.49163 29.77558 1.000 26.55274  ? 53  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 46  ? -6.89003  40.67375 29.74031 1.000 32.05489  ? 53  SER   A OG  1 
ATOM   310  N  N   . ASP   A 1 47  ? -3.94726  39.78559 27.39801 1.000 27.85552  ? 54  ASP   A N   1 
ATOM   311  C  CA  . ASP   A 1 47  ? -3.20707  40.65394 26.48833 1.000 30.35471  ? 54  ASP   A CA  1 
ATOM   312  C  C   . ASP   A 1 47  ? -3.41194  40.23847 25.03711 1.000 28.59929  ? 54  ASP   A C   1 
ATOM   313  O  O   . ASP   A 1 47  ? -3.58739  41.09241 24.15993 1.000 24.81039  ? 54  ASP   A O   1 
ATOM   314  C  CB  . ASP   A 1 47  ? -1.72165  40.64228 26.84504 1.000 29.63918  ? 54  ASP   A CB  1 
ATOM   315  C  CG  . ASP   A 1 47  ? -1.42687  41.38876 28.13092 1.000 40.75475  ? 54  ASP   A CG  1 
ATOM   316  O  OD1 . ASP   A 1 47  ? -2.33327  42.08848 28.63230 1.000 40.59131  ? 54  ASP   A OD1 1 
ATOM   317  O  OD2 . ASP   A 1 47  ? -0.28962  41.28030 28.63638 1.000 35.55782  ? 54  ASP   A OD2 1 
ATOM   318  N  N   . ALA   A 1 48  ? -3.38998  38.93136 24.76451 1.000 24.97371  ? 55  ALA   A N   1 
ATOM   319  C  CA  . ALA   A 1 48  ? -3.59975  38.45877 23.40061 1.000 29.61868  ? 55  ALA   A CA  1 
ATOM   320  C  C   . ALA   A 1 48  ? -5.00085  38.78709 22.90423 1.000 30.24529  ? 55  ALA   A C   1 
ATOM   321  O  O   . ALA   A 1 48  ? -5.19267  39.04247 21.70950 1.000 26.60426  ? 55  ALA   A O   1 
ATOM   322  C  CB  . ALA   A 1 48  ? -3.34471  36.95370 23.32120 1.000 23.87606  ? 55  ALA   A CB  1 
ATOM   323  N  N   . LEU   A 1 49  ? -5.98906  38.78753 23.80180 1.000 29.05893  ? 56  LEU   A N   1 
ATOM   324  C  CA  . LEU   A 1 49  ? -7.34898  39.13221 23.40239 1.000 26.78610  ? 56  LEU   A CA  1 
ATOM   325  C  C   . LEU   A 1 49  ? -7.47552  40.62248 23.11382 1.000 24.16738  ? 56  LEU   A C   1 
ATOM   326  O  O   . LEU   A 1 49  ? -8.17115  41.02063 22.17227 1.000 22.84450  ? 56  LEU   A O   1 
ATOM   327  C  CB  . LEU   A 1 49  ? -8.33721  38.70117 24.48590 1.000 26.31739  ? 56  LEU   A CB  1 
ATOM   328  C  CG  . LEU   A 1 49  ? -8.58645  37.19589 24.60672 1.000 26.26295  ? 56  LEU   A CG  1 
ATOM   329  C  CD1 . LEU   A 1 49  ? -9.12346  36.84884 25.98257 1.000 24.65148  ? 56  LEU   A CD1 1 
ATOM   330  C  CD2 . LEU   A 1 49  ? -9.55166  36.73091 23.53038 1.000 21.21858  ? 56  LEU   A CD2 1 
ATOM   331  N  N   . ASP   A 1 50  ? -6.80973  41.46023 23.91324 1.000 24.84420  ? 57  ASP   A N   1 
ATOM   332  C  CA  . ASP   A 1 50  ? -6.78562  42.89247 23.63242 1.000 36.52274  ? 57  ASP   A CA  1 
ATOM   333  C  C   . ASP   A 1 50  ? -6.20547  43.17131 22.25225 1.000 32.48398  ? 57  ASP   A C   1 
ATOM   334  O  O   . ASP   A 1 50  ? -6.66789  44.07436 21.54454 1.000 27.51347  ? 57  ASP   A O   1 
ATOM   335  C  CB  . ASP   A 1 50  ? -5.97494  43.62338 24.70309 1.000 30.37530  ? 57  ASP   A CB  1 
ATOM   336  C  CG  . ASP   A 1 50  ? -6.70806  43.72452 26.02267 1.000 40.63579  ? 57  ASP   A CG  1 
ATOM   337  O  OD1 . ASP   A 1 50  ? -7.95533  43.67421 26.01707 1.000 44.20259  ? 57  ASP   A OD1 1 
ATOM   338  O  OD2 . ASP   A 1 50  ? -6.03582  43.85302 27.06695 1.000 43.83284  ? 57  ASP   A OD2 1 
ATOM   339  N  N   . LYS   A 1 51  ? -5.19465  42.39833 21.85136 1.000 26.76840  ? 58  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 51  ? -4.53243  42.63819 20.57407 1.000 31.15748  ? 58  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 51  ? -5.48405  42.40761 19.40596 1.000 24.51975  ? 58  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 51  ? -5.57848  43.23738 18.49443 1.000 31.55212  ? 58  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 51  ? -3.30039  41.74157 20.45396 1.000 33.38902  ? 58  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 51  ? -1.98573  42.49682 20.44687 1.000 40.88166  ? 58  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 51  ? -0.83129  41.59859 20.85762 1.000 45.61546  ? 58  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 51  ? -0.48026  41.78333 22.32652 1.000 61.64179  ? 58  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 51  ? 0.82761   41.15414 22.65976 1.000 55.93247  ? 58  LYS   A NZ  1 
ATOM   348  N  N   . ILE   A 1 52  ? -6.20712  41.28574 19.42060 1.000 28.00270  ? 59  ILE   A N   1 
ATOM   349  C  CA  . ILE   A 1 52  ? -7.07136  40.95202 18.29243 1.000 28.90093  ? 59  ILE   A CA  1 
ATOM   350  C  C   . ILE   A 1 52  ? -8.30399  41.84929 18.26990 1.000 25.32006  ? 59  ILE   A C   1 
ATOM   351  O  O   . ILE   A 1 52  ? -8.81123  42.19778 17.19687 1.000 28.63519  ? 59  ILE   A O   1 
ATOM   352  C  CB  . ILE   A 1 52  ? -7.44554  39.45714 18.32365 1.000 31.70284  ? 59  ILE   A CB  1 
ATOM   353  C  CG1 . ILE   A 1 52  ? -8.13217  39.05882 17.01627 1.000 33.76324  ? 59  ILE   A CG1 1 
ATOM   354  C  CG2 . ILE   A 1 52  ? -8.31931  39.12383 19.53210 1.000 21.81224  ? 59  ILE   A CG2 1 
ATOM   355  C  CD1 . ILE   A 1 52  ? -7.26034  39.25780 15.79103 1.000 28.26043  ? 59  ILE   A CD1 1 
ATOM   356  N  N   . ARG   A 1 53  ? -8.80050  42.24779 19.44511 1.000 26.76187  ? 60  ARG   A N   1 
ATOM   357  C  CA  . ARG   A 1 53  ? -9.94243  43.15638 19.48912 1.000 27.06359  ? 60  ARG   A CA  1 
ATOM   358  C  C   . ARG   A 1 53  ? -9.57782  44.51949 18.91787 1.000 29.26393  ? 60  ARG   A C   1 
ATOM   359  O  O   . ARG   A 1 53  ? -10.35105 45.11060 18.15473 1.000 27.61630  ? 60  ARG   A O   1 
ATOM   360  C  CB  . ARG   A 1 53  ? -10.45139 43.30554 20.92271 1.000 28.65841  ? 60  ARG   A CB  1 
ATOM   361  C  CG  . ARG   A 1 53  ? -11.55278 44.34719 21.06776 1.000 32.03923  ? 60  ARG   A CG  1 
ATOM   362  C  CD  . ARG   A 1 53  ? -12.09703 44.42037 22.48815 1.000 39.87611  ? 60  ARG   A CD  1 
ATOM   363  N  NE  . ARG   A 1 53  ? -11.03549 44.61452 23.46787 1.000 56.85983  ? 60  ARG   A NE  1 
ATOM   364  C  CZ  . ARG   A 1 53  ? -11.10970 45.44772 24.49634 1.000 55.03445  ? 60  ARG   A CZ  1 
ATOM   365  N  NH1 . ARG   A 1 53  ? -12.17681 46.20351 24.69791 1.000 48.88947  ? 60  ARG   A NH1 1 
ATOM   366  N  NH2 . ARG   A 1 53  ? -10.08386 45.53124 25.33856 1.000 42.05338  ? 60  ARG   A NH2 1 
ATOM   367  N  N   . TYR   A 1 54  ? -8.39764  45.03011 19.27331 1.000 30.39296  ? 61  TYR   A N   1 
ATOM   368  C  CA  . TYR   A 1 54  ? -7.96387  46.32709 18.76660 1.000 34.28826  ? 61  TYR   A CA  1 
ATOM   369  C  C   . TYR   A 1 54  ? -7.75419  46.28742 17.25775 1.000 30.61578  ? 61  TYR   A C   1 
ATOM   370  O  O   . TYR   A 1 54  ? -8.17042  47.20225 16.53768 1.000 33.66726  ? 61  TYR   A O   1 
ATOM   371  C  CB  . TYR   A 1 54  ? -6.68372  46.76253 19.47785 1.000 31.95031  ? 61  TYR   A CB  1 
ATOM   372  C  CG  . TYR   A 1 54  ? -6.09020  48.03258 18.92236 1.000 35.73711  ? 61  TYR   A CG  1 
ATOM   373  C  CD1 . TYR   A 1 54  ? -5.01670  47.99445 18.04252 1.000 40.71498  ? 61  TYR   A CD1 1 
ATOM   374  C  CD2 . TYR   A 1 54  ? -6.60478  49.27143 19.27529 1.000 40.39706  ? 61  TYR   A CD2 1 
ATOM   375  C  CE1 . TYR   A 1 54  ? -4.47213  49.15713 17.52846 1.000 49.04817  ? 61  TYR   A CE1 1 
ATOM   376  C  CE2 . TYR   A 1 54  ? -6.06672  50.43836 18.76877 1.000 53.37600  ? 61  TYR   A CE2 1 
ATOM   377  C  CZ  . TYR   A 1 54  ? -5.00060  50.37511 17.89600 1.000 40.47931  ? 61  TYR   A CZ  1 
ATOM   378  O  OH  . TYR   A 1 54  ? -4.46035  51.53283 17.38746 1.000 56.38986  ? 61  TYR   A OH  1 
ATOM   379  N  N   . GLU   A 1 55  ? -7.10113  45.23354 16.76054 1.000 27.31813  ? 62  GLU   A N   1 
ATOM   380  C  CA  . GLU   A 1 55  ? -6.86140  45.12550 15.32516 1.000 29.75210  ? 62  GLU   A CA  1 
ATOM   381  C  C   . GLU   A 1 55  ? -8.16448  45.00283 14.54698 1.000 35.94483  ? 62  GLU   A C   1 
ATOM   382  O  O   . GLU   A 1 55  ? -8.25804  45.48516 13.41189 1.000 36.75765  ? 62  GLU   A O   1 
ATOM   383  C  CB  . GLU   A 1 55  ? -5.95365  43.93087 15.03090 1.000 26.89959  ? 62  GLU   A CB  1 
ATOM   384  C  CG  . GLU   A 1 55  ? -4.49707  44.13558 15.41995 1.000 30.63442  ? 62  GLU   A CG  1 
ATOM   385  C  CD  . GLU   A 1 55  ? -3.60389  43.02776 14.89793 1.000 42.17087  ? 62  GLU   A CD  1 
ATOM   386  O  OE1 . GLU   A 1 55  ? -4.10529  42.18069 14.12887 1.000 42.25665  ? 62  GLU   A OE1 1 
ATOM   387  O  OE2 . GLU   A 1 55  ? -2.40452  43.00478 15.24870 1.000 47.94465  ? 62  GLU   A OE2 1 
ATOM   388  N  N   . SER   A 1 56  ? -9.17988  44.36975 15.13829 1.000 31.73470  ? 63  SER   A N   1 
ATOM   389  C  CA  . SER   A 1 56  ? -10.47066 44.22515 14.47636 1.000 41.52234  ? 63  SER   A CA  1 
ATOM   390  C  C   . SER   A 1 56  ? -11.23737 45.53788 14.37592 1.000 42.10119  ? 63  SER   A C   1 
ATOM   391  O  O   . SER   A 1 56  ? -12.24086 45.59258 13.65657 1.000 43.78106  ? 63  SER   A O   1 
ATOM   392  C  CB  . SER   A 1 56  ? -11.32370 43.18703 15.20837 1.000 34.27170  ? 63  SER   A CB  1 
ATOM   393  O  OG  . SER   A 1 56  ? -11.83695 43.71150 16.42023 1.000 40.86450  ? 63  SER   A OG  1 
ATOM   394  N  N   . LEU   A 1 57  ? -10.80358 46.58644 15.07982 1.000 41.92232  ? 64  LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 57  ? -11.47109 47.87852 14.95764 1.000 44.52871  ? 64  LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 57  ? -11.24517 48.48530 13.58011 1.000 39.85999  ? 64  LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 57  ? -12.14927 49.11021 13.01366 1.000 44.97312  ? 64  LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 57  ? -10.97999 48.83275 16.04491 1.000 37.76974  ? 64  LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 57  ? -11.34027 48.49183 17.49003 1.000 38.90506  ? 64  LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 57  ? -11.01663 49.66664 18.38811 1.000 37.35690  ? 64  LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 57  ? -12.80838 48.11457 17.60686 1.000 46.38745  ? 64  LEU   A CD2 1 
ATOM   402  N  N   . THR   A 1 58  ? -10.04557 48.31719 13.03005 1.000 44.04914  ? 65  THR   A N   1 
ATOM   403  C  CA  . THR   A 1 58  ? -9.71018  48.82705 11.70950 1.000 49.38822  ? 65  THR   A CA  1 
ATOM   404  C  C   . THR   A 1 58  ? -9.80939  47.76412 10.62478 1.000 46.53433  ? 65  THR   A C   1 
ATOM   405  O  O   . THR   A 1 58  ? -9.66190  48.08938 9.44305  1.000 49.79034  ? 65  THR   A O   1 
ATOM   406  C  CB  . THR   A 1 58  ? -8.29996  49.42712 11.71908 1.000 39.96614  ? 65  THR   A CB  1 
ATOM   407  O  OG1 . THR   A 1 58  ? -7.34160  48.39433 11.97528 1.000 44.22880  ? 65  THR   A OG1 1 
ATOM   408  C  CG2 . THR   A 1 58  ? -8.18266  50.48990 12.80457 1.000 45.84039  ? 65  THR   A CG2 1 
ATOM   409  N  N   . ASP   A 1 59  ? -10.06230 46.50927 10.99495 1.000 48.15851  ? 66  ASP   A N   1 
ATOM   410  C  CA  . ASP   A 1 59  ? -10.16044 45.41760 10.02670 1.000 41.46803  ? 66  ASP   A CA  1 
ATOM   411  C  C   . ASP   A 1 59  ? -11.05517 44.33486 10.61317 1.000 44.45945  ? 66  ASP   A C   1 
ATOM   412  O  O   . ASP   A 1 59  ? -10.57755 43.39063 11.25595 1.000 39.01378  ? 66  ASP   A O   1 
ATOM   413  C  CB  . ASP   A 1 59  ? -8.78342  44.85780 9.67302  1.000 42.30696  ? 66  ASP   A CB  1 
ATOM   414  C  CG  . ASP   A 1 59  ? -8.81292  43.96524 8.45023  1.000 52.57564  ? 66  ASP   A CG  1 
ATOM   415  O  OD1 . ASP   A 1 59  ? -9.86651  43.90409 7.78199  1.000 56.03720  ? 66  ASP   A OD1 1 
ATOM   416  O  OD2 . ASP   A 1 59  ? -7.78040  43.32679 8.15551  1.000 53.23893  ? 66  ASP   A OD2 1 
ATOM   417  N  N   . PRO   A 1 60  ? -12.37311 44.44073 10.40845 1.000 41.25288  ? 67  PRO   A N   1 
ATOM   418  C  CA  . PRO   A 1 60  ? -13.29538 43.46885 11.02398 1.000 42.18667  ? 67  PRO   A CA  1 
ATOM   419  C  C   . PRO   A 1 60  ? -13.13385 42.04850 10.50970 1.000 44.64777  ? 67  PRO   A C   1 
ATOM   420  O  O   . PRO   A 1 60  ? -13.58353 41.11288 11.18398 1.000 38.97080  ? 67  PRO   A O   1 
ATOM   421  C  CB  . PRO   A 1 60  ? -14.68287 44.02738 10.67182 1.000 42.14384  ? 67  PRO   A CB  1 
ATOM   422  C  CG  . PRO   A 1 60  ? -14.44714 45.47271 10.34685 1.000 41.11177  ? 67  PRO   A CG  1 
ATOM   423  C  CD  . PRO   A 1 60  ? -13.09179 45.51814 9.71077  1.000 40.90469  ? 67  PRO   A CD  1 
ATOM   424  N  N   . SER   A 1 61  ? -12.51373 41.85288 9.34363  1.000 36.60364  ? 68  SER   A N   1 
ATOM   425  C  CA  . SER   A 1 61  ? -12.35096 40.50741 8.80663  1.000 46.12488  ? 68  SER   A CA  1 
ATOM   426  C  C   . SER   A 1 61  ? -11.40273 39.66019 9.64434  1.000 41.26986  ? 68  SER   A C   1 
ATOM   427  O  O   . SER   A 1 61  ? -11.37687 38.43654 9.47830  1.000 33.04152  ? 68  SER   A O   1 
ATOM   428  C  CB  . SER   A 1 61  ? -11.84943 40.56987 7.36436  1.000 37.85495  ? 68  SER   A CB  1 
ATOM   429  O  OG  . SER   A 1 61  ? -10.54337 41.11324 7.30834  1.000 47.58643  ? 68  SER   A OG  1 
ATOM   430  N  N   . LYS   A 1 62  ? -10.62797 40.27895 10.53878 1.000 38.28527  ? 69  LYS   A N   1 
ATOM   431  C  CA  . LYS   A 1 62  ? -9.73940  39.53443 11.42251 1.000 37.77387  ? 69  LYS   A CA  1 
ATOM   432  C  C   . LYS   A 1 62  ? -10.49226 38.70523 12.45453 1.000 37.11751  ? 69  LYS   A C   1 
ATOM   433  O  O   . LYS   A 1 62  ? -9.85860  37.93396 13.18306 1.000 35.47950  ? 69  LYS   A O   1 
ATOM   434  C  CB  . LYS   A 1 62  ? -8.77772  40.49296 12.12866 1.000 34.37428  ? 69  LYS   A CB  1 
ATOM   435  C  CG  . LYS   A 1 62  ? -7.91829  41.31345 11.17936 1.000 36.34814  ? 69  LYS   A CG  1 
ATOM   436  C  CD  . LYS   A 1 62  ? -6.54563  41.59150 11.77033 1.000 37.58360  ? 69  LYS   A CD  1 
ATOM   437  C  CE  . LYS   A 1 62  ? -5.72555  42.48651 10.85334 1.000 35.68480  ? 69  LYS   A CE  1 
ATOM   438  N  NZ  . LYS   A 1 62  ? -4.27020  42.43255 11.16662 1.000 36.53531  ? 69  LYS   A NZ  1 
ATOM   439  N  N   . LEU   A 1 63  ? -11.81429 38.84876 12.53969 1.000 36.45191  ? 70  LEU   A N   1 
ATOM   440  C  CA  . LEU   A 1 63  ? -12.64593 38.02585 13.40535 1.000 36.74100  ? 70  LEU   A CA  1 
ATOM   441  C  C   . LEU   A 1 63  ? -13.39762 36.94548 12.63680 1.000 43.04537  ? 70  LEU   A C   1 
ATOM   442  O  O   . LEU   A 1 63  ? -14.25750 36.27228 13.21541 1.000 33.20308  ? 70  LEU   A O   1 
ATOM   443  C  CB  . LEU   A 1 63  ? -13.63154 38.90277 14.18016 1.000 37.15129  ? 70  LEU   A CB  1 
ATOM   444  C  CG  . LEU   A 1 63  ? -13.00678 39.91741 15.14028 1.000 45.06891  ? 70  LEU   A CG  1 
ATOM   445  C  CD1 . LEU   A 1 63  ? -14.08112 40.72204 15.85171 1.000 45.63968  ? 70  LEU   A CD1 1 
ATOM   446  C  CD2 . LEU   A 1 63  ? -12.11745 39.20861 16.15162 1.000 28.87579  ? 70  LEU   A CD2 1 
ATOM   447  N  N   . ASP   A 1 64  ? -13.09471 36.76762 11.34630 1.000 32.75287  ? 71  ASP   A N   1 
ATOM   448  C  CA  . ASP   A 1 64  ? -13.69222 35.67247 10.58874 1.000 38.48282  ? 71  ASP   A CA  1 
ATOM   449  C  C   . ASP   A 1 64  ? -13.33986 34.32216 11.19509 1.000 37.82699  ? 71  ASP   A C   1 
ATOM   450  O  O   . ASP   A 1 64  ? -14.11499 33.36676 11.07718 1.000 43.48487  ? 71  ASP   A O   1 
ATOM   451  C  CB  . ASP   A 1 64  ? -13.23963 35.72663 9.12807  1.000 34.06579  ? 71  ASP   A CB  1 
ATOM   452  C  CG  . ASP   A 1 64  ? -13.81550 36.91360 8.37956  1.000 40.74990  ? 71  ASP   A CG  1 
ATOM   453  O  OD1 . ASP   A 1 64  ? -14.72169 37.58028 8.92233  1.000 37.67784  ? 71  ASP   A OD1 1 
ATOM   454  O  OD2 . ASP   A 1 64  ? -13.35825 37.18162 7.24770  1.000 36.58731  ? 71  ASP   A OD2 1 
ATOM   455  N  N   . SER   A 1 65  ? -12.18325 34.22540 11.84680 1.000 35.67077  ? 72  SER   A N   1 
ATOM   456  C  CA  . SER   A 1 65  ? -11.74581 33.00559 12.51070 1.000 35.01159  ? 72  SER   A CA  1 
ATOM   457  C  C   . SER   A 1 65  ? -12.36672 32.82429 13.89126 1.000 41.86288  ? 72  SER   A C   1 
ATOM   458  O  O   . SER   A 1 65  ? -11.94152 31.93099 14.63160 1.000 40.24770  ? 72  SER   A O   1 
ATOM   459  C  CB  . SER   A 1 65  ? -10.21940 32.99583 12.62462 1.000 40.02828  ? 72  SER   A CB  1 
ATOM   460  O  OG  . SER   A 1 65  ? -9.73859  34.23884 13.10932 1.000 38.80777  ? 72  SER   A OG  1 
ATOM   461  N  N   . GLY   A 1 66  ? -13.35439 33.64026 14.25083 1.000 36.34104  ? 73  GLY   A N   1 
ATOM   462  C  CA  . GLY   A 1 66  ? -13.98000 33.55038 15.55497 1.000 35.40219  ? 73  GLY   A CA  1 
ATOM   463  C  C   . GLY   A 1 66  ? -14.23414 34.91086 16.16928 1.000 40.11480  ? 73  GLY   A C   1 
ATOM   464  O  O   . GLY   A 1 66  ? -13.29856 35.69000 16.37504 1.000 42.16501  ? 73  GLY   A O   1 
ATOM   465  N  N   . LYS   A 1 67  ? -15.49844 35.21073 16.46571 1.000 40.22800  ? 74  LYS   A N   1 
ATOM   466  C  CA  . LYS   A 1 67  ? -15.86414 36.50793 17.01820 1.000 48.98239  ? 74  LYS   A CA  1 
ATOM   467  C  C   . LYS   A 1 67  ? -15.84704 36.54225 18.53957 1.000 46.11614  ? 74  LYS   A C   1 
ATOM   468  O  O   . LYS   A 1 67  ? -15.77202 37.63259 19.11784 1.000 46.40355  ? 74  LYS   A O   1 
ATOM   469  C  CB  . LYS   A 1 67  ? -17.25363 36.91992 16.52379 1.000 46.00216  ? 74  LYS   A CB  1 
ATOM   470  C  CG  . LYS   A 1 67  ? -17.33684 37.14531 15.02358 1.000 52.67317  ? 74  LYS   A CG  1 
ATOM   471  C  CD  . LYS   A 1 67  ? -18.23423 38.32726 14.70075 1.000 61.25965  ? 74  LYS   A CD  1 
ATOM   472  C  CE  . LYS   A 1 67  ? -17.44397 39.62759 14.67639 1.000 55.68441  ? 74  LYS   A CE  1 
ATOM   473  N  NZ  . LYS   A 1 67  ? -17.55612 40.31650 13.36228 1.000 57.24055  ? 74  LYS   A NZ  1 
ATOM   474  N  N   . GLU   A 1 68  ? -15.91109 35.38767 19.19756 1.000 36.85704  ? 75  GLU   A N   1 
ATOM   475  C  CA  . GLU   A 1 68  ? -15.94855 35.34288 20.65254 1.000 39.20263  ? 75  GLU   A CA  1 
ATOM   476  C  C   . GLU   A 1 68  ? -14.55659 35.56695 21.22842 1.000 40.84144  ? 75  GLU   A C   1 
ATOM   477  O  O   . GLU   A 1 68  ? -13.57827 34.97226 20.76529 1.000 36.78293  ? 75  GLU   A O   1 
ATOM   478  C  CB  . GLU   A 1 68  ? -16.50571 34.00326 21.13201 1.000 38.35635  ? 75  GLU   A CB  1 
ATOM   479  C  CG  . GLU   A 1 68  ? -18.01524 33.97721 21.28645 1.000 60.28977  ? 75  GLU   A CG  1 
ATOM   480  C  CD  . GLU   A 1 68  ? -18.73724 34.08497 19.95894 1.000 73.14168  ? 75  GLU   A CD  1 
ATOM   481  O  OE1 . GLU   A 1 68  ? -19.60876 34.96930 19.82790 1.000 76.04376  ? 75  GLU   A OE1 1 
ATOM   482  O  OE2 . GLU   A 1 68  ? -18.43592 33.28572 19.04710 1.000 75.90371  ? 75  GLU   A OE2 1 
ATOM   483  N  N   . LEU   A 1 69  ? -14.47419 36.42584 22.24128 1.000 33.17314  ? 76  LEU   A N   1 
ATOM   484  C  CA  . LEU   A 1 69  ? -13.23637 36.70655 22.96104 1.000 38.20106  ? 76  LEU   A CA  1 
ATOM   485  C  C   . LEU   A 1 69  ? -13.43418 36.26261 24.40567 1.000 34.89777  ? 76  LEU   A C   1 
ATOM   486  O  O   . LEU   A 1 69  ? -14.14668 36.92297 25.16953 1.000 31.33161  ? 76  LEU   A O   1 
ATOM   487  C  CB  . LEU   A 1 69  ? -12.88353 38.19033 22.88065 1.000 29.20119  ? 76  LEU   A CB  1 
ATOM   488  C  CG  . LEU   A 1 69  ? -12.83088 38.80620 21.48106 1.000 33.41293  ? 76  LEU   A CG  1 
ATOM   489  C  CD1 . LEU   A 1 69  ? -12.44736 40.27489 21.56022 1.000 32.81321  ? 76  LEU   A CD1 1 
ATOM   490  C  CD2 . LEU   A 1 69  ? -11.86094 38.04714 20.59185 1.000 27.46576  ? 76  LEU   A CD2 1 
ATOM   491  N  N   . HIS   A 1 70  ? -12.81238 35.14682 24.77974 1.000 29.86400  ? 77  HIS   A N   1 
ATOM   492  C  CA  . HIS   A 1 70  ? -13.04258 34.57183 26.09834 1.000 33.19426  ? 77  HIS   A CA  1 
ATOM   493  C  C   . HIS   A 1 70  ? -11.82593 33.75866 26.51664 1.000 31.89915  ? 77  HIS   A C   1 
ATOM   494  O  O   . HIS   A 1 70  ? -10.89067 33.54942 25.74002 1.000 26.40902  ? 77  HIS   A O   1 
ATOM   495  C  CB  . HIS   A 1 70  ? -14.31140 33.71046 26.11203 1.000 31.34153  ? 77  HIS   A CB  1 
ATOM   496  C  CG  . HIS   A 1 70  ? -14.28053 32.57102 25.14005 1.000 36.06153  ? 77  HIS   A CG  1 
ATOM   497  N  ND1 . HIS   A 1 70  ? -15.12567 32.49702 24.05370 1.000 46.94416  ? 77  HIS   A ND1 1 
ATOM   498  C  CD2 . HIS   A 1 70  ? -13.50992 31.45823 25.09261 1.000 38.26772  ? 77  HIS   A CD2 1 
ATOM   499  C  CE1 . HIS   A 1 70  ? -14.87613 31.38916 23.37845 1.000 41.00749  ? 77  HIS   A CE1 1 
ATOM   500  N  NE2 . HIS   A 1 70  ? -13.89969 30.74112 23.98762 1.000 39.39262  ? 77  HIS   A NE2 1 
ATOM   501  N  N   . ILE   A 1 71  ? -11.85816 33.30221 27.76766 1.000 28.16032  ? 78  ILE   A N   1 
ATOM   502  C  CA  . ILE   A 1 71  ? -10.81849 32.46184 28.34874 1.000 27.59636  ? 78  ILE   A CA  1 
ATOM   503  C  C   . ILE   A 1 71  ? -11.48807 31.25342 28.98620 1.000 26.32211  ? 78  ILE   A C   1 
ATOM   504  O  O   . ILE   A 1 71  ? -12.46695 31.40064 29.72570 1.000 30.70431  ? 78  ILE   A O   1 
ATOM   505  C  CB  . ILE   A 1 71  ? -9.97819  33.22154 29.39373 1.000 26.98066  ? 78  ILE   A CB  1 
ATOM   506  C  CG1 . ILE   A 1 71  ? -9.35076  34.47239 28.77651 1.000 30.52062  ? 78  ILE   A CG1 1 
ATOM   507  C  CG2 . ILE   A 1 71  ? -8.91092  32.31319 29.98247 1.000 25.14051  ? 78  ILE   A CG2 1 
ATOM   508  C  CD1 . ILE   A 1 71  ? -8.76020  35.42155 29.79457 1.000 25.94680  ? 78  ILE   A CD1 1 
ATOM   509  N  N   . ASN   A 1 72  ? -10.96687 30.06439 28.69985 1.000 27.81804  ? 79  ASN   A N   1 
ATOM   510  C  CA  . ASN   A 1 72  ? -11.47506 28.82758 29.27434 1.000 26.30597  ? 79  ASN   A CA  1 
ATOM   511  C  C   . ASN   A 1 72  ? -10.39449 28.17035 30.12068 1.000 27.22813  ? 79  ASN   A C   1 
ATOM   512  O  O   . ASN   A 1 72  ? -9.22126  28.14859 29.73751 1.000 32.81670  ? 79  ASN   A O   1 
ATOM   513  C  CB  . ASN   A 1 72  ? -11.94615 27.85693 28.18536 1.000 27.68879  ? 79  ASN   A CB  1 
ATOM   514  C  CG  . ASN   A 1 72  ? -13.17693 28.35344 27.45534 1.000 31.41316  ? 79  ASN   A CG  1 
ATOM   515  O  OD1 . ASN   A 1 72  ? -13.91136 29.20338 27.95998 1.000 32.07023  ? 79  ASN   A OD1 1 
ATOM   516  N  ND2 . ASN   A 1 72  ? -13.41410 27.81850 26.26337 1.000 30.38107  ? 79  ASN   A ND2 1 
ATOM   517  N  N   . LEU   A 1 73  ? -10.79398 27.64251 31.27582 1.000 29.13573  ? 80  LEU   A N   1 
ATOM   518  C  CA  . LEU   A 1 73  ? -9.90766  26.88458 32.15193 1.000 29.47379  ? 80  LEU   A CA  1 
ATOM   519  C  C   . LEU   A 1 73  ? -10.41596 25.45244 32.22365 1.000 29.77634  ? 80  LEU   A C   1 
ATOM   520  O  O   . LEU   A 1 73  ? -11.56030 25.21698 32.62515 1.000 28.69754  ? 80  LEU   A O   1 
ATOM   521  C  CB  . LEU   A 1 73  ? -9.83790  27.51071 33.54607 1.000 25.14065  ? 80  LEU   A CB  1 
ATOM   522  C  CG  . LEU   A 1 73  ? -9.54848  29.01222 33.59559 1.000 29.45171  ? 80  LEU   A CG  1 
ATOM   523  C  CD1 . LEU   A 1 73  ? -9.57363  29.51614 35.03210 1.000 25.52267  ? 80  LEU   A CD1 1 
ATOM   524  C  CD2 . LEU   A 1 73  ? -8.21819  29.32441 32.92905 1.000 23.57713  ? 80  LEU   A CD2 1 
ATOM   525  N  N   . ILE   A 1 74  ? -9.57082  24.50249 31.83327 1.000 29.16234  ? 81  ILE   A N   1 
ATOM   526  C  CA  . ILE   A 1 74  ? -9.99548  23.11244 31.68313 1.000 27.12900  ? 81  ILE   A CA  1 
ATOM   527  C  C   . ILE   A 1 74  ? -9.11688  22.19829 32.52682 1.000 31.13095  ? 81  ILE   A C   1 
ATOM   528  O  O   . ILE   A 1 74  ? -8.02791  21.80180 32.08220 1.000 33.59169  ? 81  ILE   A O   1 
ATOM   529  C  CB  . ILE   A 1 74  ? -9.96388  22.67959 30.20833 1.000 27.65060  ? 81  ILE   A CB  1 
ATOM   530  C  CG1 . ILE   A 1 74  ? -10.69066 23.70589 29.33405 1.000 34.63695  ? 81  ILE   A CG1 1 
ATOM   531  C  CG2 . ILE   A 1 74  ? -10.58115 21.29821 30.04908 1.000 29.77400  ? 81  ILE   A CG2 1 
ATOM   532  C  CD1 . ILE   A 1 74  ? -10.65607 23.38602 27.85556 1.000 30.37472  ? 81  ILE   A CD1 1 
ATOM   533  N  N   . PRO   A 1 75  ? -9.54437  21.82098 33.73001 1.000 29.04753  ? 82  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 75  ? -8.80126  20.81307 34.49130 1.000 29.75183  ? 82  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 75  ? -9.15539  19.40726 34.03559 1.000 30.79135  ? 82  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 75  ? -10.30271 19.11415 33.68996 1.000 31.36241  ? 82  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 75  ? -9.25166  21.05995 35.93452 1.000 31.45018  ? 82  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 75  ? -10.63599 21.59507 35.78895 1.000 29.31386  ? 82  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 75  ? -10.65287 22.39869 34.51037 1.000 35.65453  ? 82  PRO   A CD  1 
ATOM   540  N  N   . ASN   A 1 76  ? -8.14728  18.53521 34.02626 1.000 35.26785  ? 83  ASN   A N   1 
ATOM   541  C  CA  . ASN   A 1 76  ? -8.32205  17.14080 33.61675 1.000 33.84666  ? 83  ASN   A CA  1 
ATOM   542  C  C   . ASN   A 1 76  ? -7.57011  16.26961 34.61806 1.000 35.90136  ? 83  ASN   A C   1 
ATOM   543  O  O   . ASN   A 1 76  ? -6.35061  16.10728 34.51508 1.000 39.95483  ? 83  ASN   A O   1 
ATOM   544  C  CB  . ASN   A 1 76  ? -7.82523  16.91593 32.19326 1.000 39.64972  ? 83  ASN   A CB  1 
ATOM   545  C  CG  . ASN   A 1 76  ? -8.30886  15.60269 31.60517 1.000 38.42067  ? 83  ASN   A CG  1 
ATOM   546  O  OD1 . ASN   A 1 76  ? -8.10568  14.53548 32.18298 1.000 43.22870  ? 83  ASN   A OD1 1 
ATOM   547  N  ND2 . ASN   A 1 76  ? -8.95800  15.67764 30.44942 1.000 41.11758  ? 83  ASN   A ND2 1 
ATOM   548  N  N   . LYS   A 1 77  ? -8.30426  15.70928 35.58218 1.000 36.82380  ? 84  LYS   A N   1 
ATOM   549  C  CA  . LYS   A 1 77  ? -7.67622  14.89046 36.61335 1.000 44.41542  ? 84  LYS   A CA  1 
ATOM   550  C  C   . LYS   A 1 77  ? -7.11108  13.59491 36.04643 1.000 44.06196  ? 84  LYS   A C   1 
ATOM   551  O  O   . LYS   A 1 77  ? -6.08360  13.10711 36.53070 1.000 45.99345  ? 84  LYS   A O   1 
ATOM   552  C  CB  . LYS   A 1 77  ? -8.68138  14.58420 37.72195 1.000 45.58474  ? 84  LYS   A CB  1 
ATOM   553  C  CG  . LYS   A 1 77  ? -8.90704  15.72908 38.69543 1.000 44.51015  ? 84  LYS   A CG  1 
ATOM   554  C  CD  . LYS   A 1 77  ? -9.73275  15.26813 39.88585 1.000 43.57437  ? 84  LYS   A CD  1 
ATOM   555  C  CE  . LYS   A 1 77  ? -9.63474  16.24599 41.04400 1.000 53.60530  ? 84  LYS   A CE  1 
ATOM   556  N  NZ  . LYS   A 1 77  ? -10.97374 16.73197 41.47830 1.000 61.81976  ? 84  LYS   A NZ  1 
ATOM   557  N  N   . GLN   A 1 78  ? -7.76079  13.02482 35.02919 1.000 45.35392  ? 85  GLN   A N   1 
ATOM   558  C  CA  . GLN   A 1 78  ? -7.28583  11.76512 34.46578 1.000 46.91980  ? 85  GLN   A CA  1 
ATOM   559  C  C   . GLN   A 1 78  ? -5.92700  11.93613 33.79677 1.000 45.75530  ? 85  GLN   A C   1 
ATOM   560  O  O   . GLN   A 1 78  ? -5.02975  11.10512 33.97997 1.000 46.15045  ? 85  GLN   A O   1 
ATOM   561  C  CB  . GLN   A 1 78  ? -8.31015  11.21276 33.47361 1.000 61.25556  ? 85  GLN   A CB  1 
ATOM   562  C  CG  . GLN   A 1 78  ? -9.52851  10.55568 34.11768 1.000 82.17725  ? 85  GLN   A CG  1 
ATOM   563  C  CD  . GLN   A 1 78  ? -10.40922 11.54386 34.85761 1.000 89.78468  ? 85  GLN   A CD  1 
ATOM   564  O  OE1 . GLN   A 1 78  ? -10.68497 12.63750 34.36272 1.000 78.34367  ? 85  GLN   A OE1 1 
ATOM   565  N  NE2 . GLN   A 1 78  ? -10.85912 11.16159 36.04838 1.000 84.60594  ? 85  GLN   A NE2 1 
ATOM   566  N  N   . ASP   A 1 79  ? -5.75408  13.00719 33.02403 1.000 42.12764  ? 86  ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 79  ? -4.48874  13.28391 32.35816 1.000 49.33308  ? 86  ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 79  ? -3.52346  14.08799 33.21838 1.000 49.12940  ? 86  ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 79  ? -2.35181  14.21794 32.84475 1.000 51.35052  ? 86  ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 79  ? -4.73461  14.03494 31.04445 1.000 49.59609  ? 86  ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 79  ? -5.67462  13.29434 30.11731 1.000 53.03227  ? 86  ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 79  ? -6.02387  12.13602 30.42592 1.000 60.58928  ? 86  ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 79  ? -6.06648  13.87191 29.08156 1.000 66.46052  ? 86  ASP   A OD2 1 
ATOM   574  N  N   . ARG   A 1 80  ? -3.98421  14.61985 34.35321 1.000 35.50469  ? 87  ARG   A N   1 
ATOM   575  C  CA  . ARG   A 1 80  ? -3.17939  15.49155 35.20999 1.000 38.76161  ? 87  ARG   A CA  1 
ATOM   576  C  C   . ARG   A 1 80  ? -2.68322  16.70445 34.41996 1.000 34.97977  ? 87  ARG   A C   1 
ATOM   577  O  O   . ARG   A 1 80  ? -1.49601  17.03691 34.41110 1.000 34.45772  ? 87  ARG   A O   1 
ATOM   578  C  CB  . ARG   A 1 80  ? -2.02018  14.71851 35.85251 1.000 41.96510  ? 87  ARG   A CB  1 
ATOM   579  C  CG  . ARG   A 1 80  ? -1.28438  15.47082 36.95622 1.000 40.21796  ? 87  ARG   A CG  1 
ATOM   580  C  CD  . ARG   A 1 80  ? -1.03600  14.59497 38.17313 1.000 35.91237  ? 87  ARG   A CD  1 
ATOM   581  N  NE  . ARG   A 1 80  ? -0.43073  13.31118 37.84080 1.000 60.70694  ? 87  ARG   A NE  1 
ATOM   582  C  CZ  . ARG   A 1 80  ? 0.86978   13.12132 37.66478 1.000 64.16299  ? 87  ARG   A CZ  1 
ATOM   583  N  NH1 . ARG   A 1 80  ? 1.73141   14.12232 37.74431 1.000 56.97721  ? 87  ARG   A NH1 1 
ATOM   584  N  NH2 . ARG   A 1 80  ? 1.31774   11.89597 37.40639 1.000 61.61188  ? 87  ARG   A NH2 1 
ATOM   585  N  N   . THR   A 1 81  ? -3.61417  17.36070 33.72951 1.000 29.30697  ? 88  THR   A N   1 
ATOM   586  C  CA  . THR   A 1 81  ? -3.30996  18.53875 32.93274 1.000 33.36320  ? 88  THR   A CA  1 
ATOM   587  C  C   . THR   A 1 81  ? -4.30671  19.64598 33.24202 1.000 32.93877  ? 88  THR   A C   1 
ATOM   588  O  O   . THR   A 1 81  ? -5.47741  19.38914 33.53621 1.000 31.28083  ? 88  THR   A O   1 
ATOM   589  C  CB  . THR   A 1 81  ? -3.33625  18.24110 31.42072 1.000 28.04060  ? 88  THR   A CB  1 
ATOM   590  O  OG1 . THR   A 1 81  ? -4.68153  17.97338 31.00420 1.000 37.13679  ? 88  THR   A OG1 1 
ATOM   591  C  CG2 . THR   A 1 81  ? -2.45115  17.04750 31.08162 1.000 32.24343  ? 88  THR   A CG2 1 
ATOM   592  N  N   . LEU   A 1 82  ? -3.81978  20.88307 33.18374 1.000 32.18569  ? 89  LEU   A N   1 
ATOM   593  C  CA  . LEU   A 1 82  ? -4.64763  22.07821 33.28289 1.000 31.31092  ? 89  LEU   A CA  1 
ATOM   594  C  C   . LEU   A 1 82  ? -4.43189  22.89809 32.02141 1.000 29.90301  ? 89  LEU   A C   1 
ATOM   595  O  O   . LEU   A 1 82  ? -3.29912  23.28814 31.71840 1.000 29.77631  ? 89  LEU   A O   1 
ATOM   596  C  CB  . LEU   A 1 82  ? -4.30288  22.89884 34.52733 1.000 28.10519  ? 89  LEU   A CB  1 
ATOM   597  C  CG  . LEU   A 1 82  ? -5.01783  24.24916 34.62218 1.000 33.94173  ? 89  LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A 1 82  ? -6.51888  24.05406 34.77572 1.000 24.27896  ? 89  LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A 1 82  ? -4.46011  25.08527 35.76425 1.000 29.32556  ? 89  LEU   A CD2 1 
ATOM   600  N  N   . THR   A 1 83  ? -5.51045  23.15654 31.29101 1.000 27.03771  ? 90  THR   A N   1 
ATOM   601  C  CA  . THR   A 1 83  ? -5.44308  23.82904 30.00204 1.000 26.16323  ? 90  THR   A CA  1 
ATOM   602  C  C   . THR   A 1 83  ? -6.06271  25.21563 30.10155 1.000 26.95554  ? 90  THR   A C   1 
ATOM   603  O  O   . THR   A 1 83  ? -7.17655  25.36661 30.61426 1.000 26.50248  ? 90  THR   A O   1 
ATOM   604  C  CB  . THR   A 1 83  ? -6.16051  23.01562 28.92416 1.000 26.17307  ? 90  THR   A CB  1 
ATOM   605  O  OG1 . THR   A 1 83  ? -5.60080  21.69783 28.86276 1.000 31.73862  ? 90  THR   A OG1 1 
ATOM   606  C  CG2 . THR   A 1 83  ? -6.00708  23.68707 27.57506 1.000 26.34019  ? 90  THR   A CG2 1 
ATOM   607  N  N   . ILE   A 1 84  ? -5.34277  26.21894 29.60533 1.000 37.01910  ? 91  ILE   A N   1 
ATOM   608  C  CA  . ILE   A 1 84  ? -5.82922  27.59190 29.52514 1.000 31.23717  ? 91  ILE   A CA  1 
ATOM   609  C  C   . ILE   A 1 84  ? -5.98508  27.93169 28.05014 1.000 32.70579  ? 91  ILE   A C   1 
ATOM   610  O  O   . ILE   A 1 84  ? -4.99704  27.98924 27.30738 1.000 25.99634  ? 91  ILE   A O   1 
ATOM   611  C  CB  . ILE   A 1 84  ? -4.88744  28.58011 30.22521 1.000 25.60183  ? 91  ILE   A CB  1 
ATOM   612  C  CG1 . ILE   A 1 84  ? -4.83968  28.29797 31.72671 1.000 31.45574  ? 91  ILE   A CG1 1 
ATOM   613  C  CG2 . ILE   A 1 84  ? -5.33419  30.00867 29.96576 1.000 21.27354  ? 91  ILE   A CG2 1 
ATOM   614  C  CD1 . ILE   A 1 84  ? -3.54167  27.68309 32.18883 1.000 33.67799  ? 91  ILE   A CD1 1 
ATOM   615  N  N   . VAL   A 1 85  ? -7.22311  28.15428 27.62099 1.000 24.31346  ? 92  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 85  ? -7.53721  28.45521 26.23053 1.000 24.90051  ? 92  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 85  ? -8.03747  29.88840 26.14929 1.000 29.40577  ? 92  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 85  ? -8.86279  30.31300 26.96723 1.000 28.37286  ? 92  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 85  ? -8.58051  27.47770 25.66169 1.000 30.08652  ? 92  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 85  ? -8.74634  27.68528 24.16168 1.000 28.36911  ? 92  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 85  ? -8.18383  26.04219 25.96217 1.000 41.63633  ? 92  VAL   A CG2 1 
ATOM   622  N  N   . ASP   A 1 86  ? -7.52943  30.63302 25.17111 1.000 30.21320  ? 93  ASP   A N   1 
ATOM   623  C  CA  . ASP   A 1 86  ? -8.04147  31.95208 24.84138 1.000 27.40187  ? 93  ASP   A CA  1 
ATOM   624  C  C   . ASP   A 1 86  ? -8.22758  32.04347 23.33416 1.000 28.25419  ? 93  ASP   A C   1 
ATOM   625  O  O   . ASP   A 1 86  ? -7.59557  31.31669 22.56189 1.000 29.60238  ? 93  ASP   A O   1 
ATOM   626  C  CB  . ASP   A 1 86  ? -7.11155  33.07649 25.33452 1.000 26.70740  ? 93  ASP   A CB  1 
ATOM   627  C  CG  . ASP   A 1 86  ? -5.75698  33.06975 24.64394 1.000 30.73078  ? 93  ASP   A CG  1 
ATOM   628  O  OD1 . ASP   A 1 86  ? -5.68332  33.47240 23.46257 1.000 28.95247  ? 93  ASP   A OD1 1 
ATOM   629  O  OD2 . ASP   A 1 86  ? -4.76164  32.67294 25.28782 1.000 35.68986  ? 93  ASP   A OD2 1 
ATOM   630  N  N   . THR   A 1 87  ? -9.11498  32.94428 22.92183 1.000 28.48990  ? 94  THR   A N   1 
ATOM   631  C  CA  . THR   A 1 87  ? -9.34155  33.23013 21.50758 1.000 29.19136  ? 94  THR   A CA  1 
ATOM   632  C  C   . THR   A 1 87  ? -8.64021  34.51057 21.07966 1.000 30.79442  ? 94  THR   A C   1 
ATOM   633  O  O   . THR   A 1 87  ? -9.19037  35.31403 20.32025 1.000 27.54735  ? 94  THR   A O   1 
ATOM   634  C  CB  . THR   A 1 87  ? -10.83467 33.30953 21.21572 1.000 28.74860  ? 94  THR   A CB  1 
ATOM   635  O  OG1 . THR   A 1 87  ? -11.49685 33.97273 22.30015 1.000 28.41252  ? 94  THR   A OG1 1 
ATOM   636  C  CG2 . THR   A 1 87  ? -11.41346 31.90989 21.04402 1.000 35.19877  ? 94  THR   A CG2 1 
ATOM   637  N  N   . GLY   A 1 88  ? -7.42073  34.72030 21.56675 1.000 24.69480  ? 95  GLY   A N   1 
ATOM   638  C  CA  . GLY   A 1 88  ? -6.65678  35.90925 21.25943 1.000 29.54730  ? 95  GLY   A CA  1 
ATOM   639  C  C   . GLY   A 1 88  ? -6.08317  35.88370 19.86113 1.000 27.62630  ? 95  GLY   A C   1 
ATOM   640  O  O   . GLY   A 1 88  ? -6.48067  35.08820 19.00612 1.000 28.44066  ? 95  GLY   A O   1 
ATOM   641  N  N   . ILE   A 1 89  ? -5.11722  36.77588 19.63408 1.000 30.03903  ? 96  ILE   A N   1 
ATOM   642  C  CA  . ILE   A 1 89  ? -4.52747  36.92277 18.31156 1.000 28.56153  ? 96  ILE   A CA  1 
ATOM   643  C  C   . ILE   A 1 89  ? -3.71107  35.70292 17.90667 1.000 26.22438  ? 96  ILE   A C   1 
ATOM   644  O  O   . ILE   A 1 89  ? -3.44433  35.51040 16.71493 1.000 26.84977  ? 96  ILE   A O   1 
ATOM   645  C  CB  . ILE   A 1 89  ? -3.66628  38.19751 18.26652 1.000 31.10275  ? 96  ILE   A CB  1 
ATOM   646  C  CG1 . ILE   A 1 89  ? -3.42425  38.63558 16.82114 1.000 31.19310  ? 96  ILE   A CG1 1 
ATOM   647  C  CG2 . ILE   A 1 89  ? -2.34777  37.98458 19.00481 1.000 26.03707  ? 96  ILE   A CG2 1 
ATOM   648  C  CD1 . ILE   A 1 89  ? -2.71895  39.96347 16.70135 1.000 38.40649  ? 96  ILE   A CD1 1 
ATOM   649  N  N   . GLY   A 1 90  ? -3.31536  34.86414 18.85813 1.000 25.31268  ? 97  GLY   A N   1 
ATOM   650  C  CA  . GLY   A 1 90  ? -2.51017  33.70208 18.54037 1.000 27.16859  ? 97  GLY   A CA  1 
ATOM   651  C  C   . GLY   A 1 90  ? -1.06977  34.08202 18.24236 1.000 27.91198  ? 97  GLY   A C   1 
ATOM   652  O  O   . GLY   A 1 90  ? -0.65069  35.23410 18.35162 1.000 25.12674  ? 97  GLY   A O   1 
ATOM   653  N  N   . MET   A 1 91  ? -0.30166  33.07305 17.84639 1.000 23.40605  ? 98  MET   A N   1 
ATOM   654  C  CA  . MET   A 1 91  ? 1.12141   33.23391 17.59619 1.000 24.48413  ? 98  MET   A CA  1 
ATOM   655  C  C   . MET   A 1 91  ? 1.49587   32.56985 16.28135 1.000 26.99987  ? 98  MET   A C   1 
ATOM   656  O  O   . MET   A 1 91  ? 1.00938   31.48054 15.96419 1.000 28.53550  ? 98  MET   A O   1 
ATOM   657  C  CB  . MET   A 1 91  ? 1.95198   32.63281 18.73365 1.000 25.75056  ? 98  MET   A CB  1 
ATOM   658  C  CG  . MET   A 1 91  ? 2.14830   33.56240 19.92086 1.000 25.81813  ? 98  MET   A CG  1 
ATOM   659  S  SD  . MET   A 1 91  ? 2.75471   32.70247 21.38676 1.000 29.52080  ? 98  MET   A SD  1 
ATOM   660  C  CE  . MET   A 1 91  ? 1.63835   31.30573 21.45640 1.000 23.37298  ? 98  MET   A CE  1 
ATOM   661  N  N   . THR   A 1 92  ? 2.36124   33.23374 15.52106 1.000 29.59823  ? 99  THR   A N   1 
ATOM   662  C  CA  . THR   A 1 92  ? 2.91716   32.65051 14.31248 1.000 30.75782  ? 99  THR   A CA  1 
ATOM   663  C  C   . THR   A 1 92  ? 4.12179   31.77579 14.65706 1.000 30.38839  ? 99  THR   A C   1 
ATOM   664  O  O   . THR   A 1 92  ? 4.57064   31.70957 15.80532 1.000 27.36200  ? 99  THR   A O   1 
ATOM   665  C  CB  . THR   A 1 92  ? 3.32308   33.74273 13.32239 1.000 31.26689  ? 99  THR   A CB  1 
ATOM   666  O  OG1 . THR   A 1 92  ? 4.40814   34.50341 13.86774 1.000 29.90908  ? 99  THR   A OG1 1 
ATOM   667  C  CG2 . THR   A 1 92  ? 2.15601   34.67397 13.04356 1.000 32.43079  ? 99  THR   A CG2 1 
ATOM   668  N  N   . LYS   A 1 93  ? 4.65129   31.09481 13.63766 1.000 25.49253  ? 100 LYS   A N   1 
ATOM   669  C  CA  . LYS   A 1 93  ? 5.82816   30.25928 13.85378 1.000 32.99554  ? 100 LYS   A CA  1 
ATOM   670  C  C   . LYS   A 1 93  ? 7.03866   31.10262 14.23251 1.000 31.39006  ? 100 LYS   A C   1 
ATOM   671  O  O   . LYS   A 1 93  ? 7.83570   30.70633 15.09108 1.000 35.32079  ? 100 LYS   A O   1 
ATOM   672  C  CB  . LYS   A 1 93  ? 6.12685   29.42395 12.60988 1.000 27.72412  ? 100 LYS   A CB  1 
ATOM   673  C  CG  . LYS   A 1 93  ? 6.99772   28.21194 12.89892 1.000 39.02590  ? 100 LYS   A CG  1 
ATOM   674  C  CD  . LYS   A 1 93  ? 7.56440   27.59746 11.62931 1.000 37.76908  ? 100 LYS   A CD  1 
ATOM   675  C  CE  . LYS   A 1 93  ? 8.39169   26.36027 11.95198 1.000 45.00434  ? 100 LYS   A CE  1 
ATOM   676  N  NZ  . LYS   A 1 93  ? 8.94923   25.70601 10.73445 1.000 53.88202  ? 100 LYS   A NZ  1 
ATOM   677  N  N   . ALA   A 1 94  ? 7.19272   32.27136 13.60328 1.000 26.62643  ? 101 ALA   A N   1 
ATOM   678  C  CA  . ALA   A 1 94  ? 8.28430   33.16787 13.96871 1.000 27.25269  ? 101 ALA   A CA  1 
ATOM   679  C  C   . ALA   A 1 94  ? 8.11648   33.70202 15.38457 1.000 34.39411  ? 101 ALA   A C   1 
ATOM   680  O  O   . ALA   A 1 94  ? 9.11108   33.94773 16.07704 1.000 32.57694  ? 101 ALA   A O   1 
ATOM   681  C  CB  . ALA   A 1 94  ? 8.37618   34.32021 12.96937 1.000 27.96155  ? 101 ALA   A CB  1 
ATOM   682  N  N   . ASP   A 1 95  ? 6.87118   33.89165 15.82790 1.000 36.38471  ? 102 ASP   A N   1 
ATOM   683  C  CA  . ASP   A 1 95  ? 6.61983   34.25103 17.21996 1.000 28.75077  ? 102 ASP   A CA  1 
ATOM   684  C  C   . ASP   A 1 95  ? 7.16665   33.18948 18.16468 1.000 28.46594  ? 102 ASP   A C   1 
ATOM   685  O  O   . ASP   A 1 95  ? 7.84183   33.50487 19.15119 1.000 27.47896  ? 102 ASP   A O   1 
ATOM   686  C  CB  . ASP   A 1 95  ? 5.11993   34.43645 17.45129 1.000 30.20277  ? 102 ASP   A CB  1 
ATOM   687  C  CG  . ASP   A 1 95  ? 4.59231   35.72324 16.86059 1.000 39.54974  ? 102 ASP   A CG  1 
ATOM   688  O  OD1 . ASP   A 1 95  ? 5.36070   36.70576 16.79334 1.000 35.79613  ? 102 ASP   A OD1 1 
ATOM   689  O  OD2 . ASP   A 1 95  ? 3.40593   35.75376 16.46931 1.000 36.29838  ? 102 ASP   A OD2 1 
ATOM   690  N  N   . LEU   A 1 96  ? 6.88558   31.91750 17.86929 1.000 26.22923  ? 103 LEU   A N   1 
ATOM   691  C  CA  . LEU   A 1 96  ? 7.24793   30.83533 18.77840 1.000 27.32282  ? 103 LEU   A CA  1 
ATOM   692  C  C   . LEU   A 1 96  ? 8.75710   30.65561 18.88409 1.000 26.37351  ? 103 LEU   A C   1 
ATOM   693  O  O   . LEU   A 1 96  ? 9.26241   30.27728 19.94754 1.000 32.45826  ? 103 LEU   A O   1 
ATOM   694  C  CB  . LEU   A 1 96  ? 6.59525   29.53079 18.31684 1.000 25.46385  ? 103 LEU   A CB  1 
ATOM   695  C  CG  . LEU   A 1 96  ? 5.07492   29.41271 18.45701 1.000 25.59250  ? 103 LEU   A CG  1 
ATOM   696  C  CD1 . LEU   A 1 96  ? 4.58764   28.10477 17.85847 1.000 25.03589  ? 103 LEU   A CD1 1 
ATOM   697  C  CD2 . LEU   A 1 96  ? 4.63827   29.52867 19.91110 1.000 23.63973  ? 103 LEU   A CD2 1 
ATOM   698  N  N   . ILE   A 1 97  ? 9.49198   30.92798 17.81042 1.000 26.82486  ? 104 ILE   A N   1 
ATOM   699  C  CA  . ILE   A 1 97  ? 10.90882  30.60009 17.71951 1.000 30.67275  ? 104 ILE   A CA  1 
ATOM   700  C  C   . ILE   A 1 97  ? 11.78796  31.83985 17.86807 1.000 40.49996  ? 104 ILE   A C   1 
ATOM   701  O  O   . ILE   A 1 97  ? 12.74989  31.83688 18.63760 1.000 36.86335  ? 104 ILE   A O   1 
ATOM   702  C  CB  . ILE   A 1 97  ? 11.21658  29.85214 16.40274 1.000 35.08666  ? 104 ILE   A CB  1 
ATOM   703  C  CG1 . ILE   A 1 97  ? 10.44224  28.53284 16.35747 1.000 32.56219  ? 104 ILE   A CG1 1 
ATOM   704  C  CG2 . ILE   A 1 97  ? 12.70707  29.59325 16.27028 1.000 36.60278  ? 104 ILE   A CG2 1 
ATOM   705  C  CD1 . ILE   A 1 97  ? 10.21481  28.00082 14.96380 1.000 40.63589  ? 104 ILE   A CD1 1 
ATOM   706  N  N   . ASN   A 1 98  ? 11.46826  32.91501 17.14517 1.000 29.77791  ? 105 ASN   A N   1 
ATOM   707  C  CA  . ASN   A 1 98  ? 12.33807  34.08845 17.08859 1.000 35.16511  ? 105 ASN   A CA  1 
ATOM   708  C  C   . ASN   A 1 98  ? 11.84332  35.24135 17.95788 1.000 34.77163  ? 105 ASN   A C   1 
ATOM   709  O  O   . ASN   A 1 98  ? 12.53694  35.65727 18.89056 1.000 42.51213  ? 105 ASN   A O   1 
ATOM   710  C  CB  . ASN   A 1 98  ? 12.49341  34.55774 15.63521 1.000 31.68954  ? 105 ASN   A CB  1 
ATOM   711  C  CG  . ASN   A 1 98  ? 12.83083  33.42343 14.69006 1.000 51.81296  ? 105 ASN   A CG  1 
ATOM   712  O  OD1 . ASN   A 1 98  ? 13.87800  32.78781 14.81525 1.000 63.82213  ? 105 ASN   A OD1 1 
ATOM   713  N  ND2 . ASN   A 1 98  ? 11.94638  33.16675 13.73217 1.000 48.62448  ? 105 ASN   A ND2 1 
ATOM   714  N  N   . ASN   A 1 99  ? 10.64738  35.76131 17.66854 1.000 32.24141  ? 106 ASN   A N   1 
ATOM   715  C  CA  . ASN   A 1 99  ? 10.23788  37.05666 18.20869 1.000 35.21850  ? 106 ASN   A CA  1 
ATOM   716  C  C   . ASN   A 1 99  ? 10.15439  37.03927 19.73133 1.000 34.21401  ? 106 ASN   A C   1 
ATOM   717  O  O   . ASN   A 1 99  ? 10.75606  37.88341 20.40566 1.000 32.30775  ? 106 ASN   A O   1 
ATOM   718  C  CB  . ASN   A 1 99  ? 8.89861   37.47341 17.60039 1.000 31.19621  ? 106 ASN   A CB  1 
ATOM   719  C  CG  . ASN   A 1 99  ? 8.91651   37.45246 16.08303 1.000 40.95456  ? 106 ASN   A CG  1 
ATOM   720  O  OD1 . ASN   A 1 99  ? 9.96323   37.63454 15.46090 1.000 33.81435  ? 106 ASN   A OD1 1 
ATOM   721  N  ND2 . ASN   A 1 99  ? 7.75342   37.23559 15.47947 1.000 35.78530  ? 106 ASN   A ND2 1 
ATOM   722  N  N   . LEU   A 1 100 ? 9.40729   36.08746 20.29374 1.000 34.03435  ? 107 LEU   A N   1 
ATOM   723  C  CA  . LEU   A 1 100 ? 9.19317   36.08914 21.73738 1.000 39.71414  ? 107 LEU   A CA  1 
ATOM   724  C  C   . LEU   A 1 100 ? 10.46749  35.75464 22.50276 1.000 39.72057  ? 107 LEU   A C   1 
ATOM   725  O  O   . LEU   A 1 100 ? 10.66896  36.25820 23.61438 1.000 33.83110  ? 107 LEU   A O   1 
ATOM   726  C  CB  . LEU   A 1 100 ? 8.07712   35.11306 22.10340 1.000 29.91690  ? 107 LEU   A CB  1 
ATOM   727  C  CG  . LEU   A 1 100 ? 6.67739   35.55841 21.68114 1.000 31.37770  ? 107 LEU   A CG  1 
ATOM   728  C  CD1 . LEU   A 1 100 ? 5.64426   34.54408 22.12898 1.000 31.42747  ? 107 LEU   A CD1 1 
ATOM   729  C  CD2 . LEU   A 1 100 ? 6.36617   36.93599 22.24146 1.000 29.58745  ? 107 LEU   A CD2 1 
ATOM   730  N  N   . GLY   A 1 101 ? 11.33413  34.91568 21.93200 1.000 29.77314  ? 108 GLY   A N   1 
ATOM   731  C  CA  . GLY   A 1 101 ? 12.59074  34.60796 22.59474 1.000 34.71538  ? 108 GLY   A CA  1 
ATOM   732  C  C   . GLY   A 1 101 ? 13.49079  35.82128 22.72420 1.000 37.73239  ? 108 GLY   A C   1 
ATOM   733  O  O   . GLY   A 1 101 ? 14.18826  35.98503 23.72835 1.000 36.89334  ? 108 GLY   A O   1 
ATOM   734  N  N   . THR   A 1 102 ? 13.48448  36.69112 21.71074 1.000 33.74736  ? 109 THR   A N   1 
ATOM   735  C  CA  . THR   A 1 102 ? 14.26610  37.92130 21.78541 1.000 38.23066  ? 109 THR   A CA  1 
ATOM   736  C  C   . THR   A 1 102 ? 13.75297  38.83338 22.89307 1.000 40.15589  ? 109 THR   A C   1 
ATOM   737  O  O   . THR   A 1 102 ? 14.54489  39.43261 23.62974 1.000 40.26010  ? 109 THR   A O   1 
ATOM   738  C  CB  . THR   A 1 102 ? 14.23654  38.64649 20.44049 1.000 31.11655  ? 109 THR   A CB  1 
ATOM   739  O  OG1 . THR   A 1 102 ? 14.46897  37.70809 19.38273 1.000 39.04592  ? 109 THR   A OG1 1 
ATOM   740  C  CG2 . THR   A 1 102 ? 15.30315  39.72500 20.39740 1.000 39.76335  ? 109 THR   A CG2 1 
ATOM   741  N  N   . ILE   A 1 103 ? 12.42866  38.95217 23.02517 1.000 42.75547  ? 110 ILE   A N   1 
ATOM   742  C  CA  . ILE   A 1 103 ? 11.85501  39.72996 24.12167 1.000 46.71291  ? 110 ILE   A CA  1 
ATOM   743  C  C   . ILE   A 1 103 ? 12.18698  39.08385 25.46093 1.000 40.68328  ? 110 ILE   A C   1 
ATOM   744  O  O   . ILE   A 1 103 ? 12.55076  39.76864 26.42580 1.000 43.25564  ? 110 ILE   A O   1 
ATOM   745  C  CB  . ILE   A 1 103 ? 10.33290  39.89142 23.92886 1.000 49.34729  ? 110 ILE   A CB  1 
ATOM   746  C  CG1 . ILE   A 1 103 ? 10.00890  41.22849 23.25840 1.000 50.81448  ? 110 ILE   A CG1 1 
ATOM   747  C  CG2 . ILE   A 1 103 ? 9.59103   39.78375 25.25893 1.000 54.96585  ? 110 ILE   A CG2 1 
ATOM   748  C  CD1 . ILE   A 1 103 ? 10.50441  41.34649 21.84222 1.000 45.60504  ? 110 ILE   A CD1 1 
ATOM   749  N  N   . ALA   A 1 104 ? 12.08145  37.75428 25.53781 1.000 34.14982  ? 111 ALA   A N   1 
ATOM   750  C  CA  . ALA   A 1 104 ? 12.31736  37.05543 26.79450 1.000 39.50253  ? 111 ALA   A CA  1 
ATOM   751  C  C   . ALA   A 1 104 ? 13.77887  37.09305 27.21781 1.000 43.23760  ? 111 ALA   A C   1 
ATOM   752  O  O   . ALA   A 1 104 ? 14.06616  36.91542 28.40463 1.000 43.33728  ? 111 ALA   A O   1 
ATOM   753  C  CB  . ALA   A 1 104 ? 11.84319  35.60435 26.69006 1.000 33.73757  ? 111 ALA   A CB  1 
ATOM   754  N  N   . LYS   A 1 105 ? 14.70409  37.31670 26.28239 1.000 38.29137  ? 112 LYS   A N   1 
ATOM   755  C  CA  . LYS   A 1 105 ? 16.11833  37.38912 26.63604 1.000 37.74129  ? 112 LYS   A CA  1 
ATOM   756  C  C   . LYS   A 1 105 ? 16.38884  38.56601 27.56594 1.000 36.47161  ? 112 LYS   A C   1 
ATOM   757  O  O   . LYS   A 1 105 ? 16.95523  38.40239 28.65244 1.000 41.76205  ? 112 LYS   A O   1 
ATOM   758  C  CB  . LYS   A 1 105 ? 16.97036  37.49307 25.36960 1.000 39.38577  ? 112 LYS   A CB  1 
ATOM   759  C  CG  . LYS   A 1 105 ? 18.42353  37.09383 25.56663 1.000 43.08172  ? 112 LYS   A CG  1 
ATOM   760  C  CD  . LYS   A 1 105 ? 19.14307  36.94260 24.23515 1.000 48.99406  ? 112 LYS   A CD  1 
ATOM   761  C  CE  . LYS   A 1 105 ? 20.64544  37.12787 24.38955 1.000 55.73919  ? 112 LYS   A CE  1 
ATOM   762  N  NZ  . LYS   A 1 105 ? 20.98298  38.15647 25.41100 1.000 57.33045  ? 112 LYS   A NZ  1 
ATOM   763  N  N   . SER   A 1 106 ? 15.98246  39.76818 27.15232 1.000 33.58333  ? 113 SER   A N   1 
ATOM   764  C  CA  . SER   A 1 106 ? 16.22236  40.95120 27.97086 1.000 37.19169  ? 113 SER   A CA  1 
ATOM   765  C  C   . SER   A 1 106 ? 15.32120  40.98010 29.19810 1.000 37.16044  ? 113 SER   A C   1 
ATOM   766  O  O   . SER   A 1 106 ? 15.72336  41.49575 30.24709 1.000 44.61072  ? 113 SER   A O   1 
ATOM   767  C  CB  . SER   A 1 106 ? 16.02647  42.21558 27.13428 1.000 42.88291  ? 113 SER   A CB  1 
ATOM   768  O  OG  . SER   A 1 106 ? 15.38378  41.91815 25.90671 1.000 42.23951  ? 113 SER   A OG  1 
ATOM   769  N  N   . GLY   A 1 107 ? 14.10662  40.43923 29.09039 1.000 37.44977  ? 114 GLY   A N   1 
ATOM   770  C  CA  . GLY   A 1 107 ? 13.23377  40.37938 30.25101 1.000 37.31175  ? 114 GLY   A CA  1 
ATOM   771  C  C   . GLY   A 1 107 ? 13.74080  39.41694 31.30745 1.000 34.87900  ? 114 GLY   A C   1 
ATOM   772  O  O   . GLY   A 1 107 ? 13.63046  39.68210 32.50803 1.000 34.51123  ? 114 GLY   A O   1 
ATOM   773  N  N   . THR   A 1 108 ? 14.30673  38.28867 30.87684 1.000 31.41362  ? 115 THR   A N   1 
ATOM   774  C  CA  . THR   A 1 108 ? 14.89199  37.34324 31.82088 1.000 36.66054  ? 115 THR   A CA  1 
ATOM   775  C  C   . THR   A 1 108 ? 16.09672  37.95296 32.52536 1.000 38.63188  ? 115 THR   A C   1 
ATOM   776  O  O   . THR   A 1 108 ? 16.24877  37.82664 33.74620 1.000 35.55254  ? 115 THR   A O   1 
ATOM   777  C  CB  . THR   A 1 108 ? 15.29155  36.06103 31.09242 1.000 33.47274  ? 115 THR   A CB  1 
ATOM   778  O  OG1 . THR   A 1 108 ? 14.12205  35.28135 30.81806 1.000 46.56098  ? 115 THR   A OG1 1 
ATOM   779  C  CG2 . THR   A 1 108 ? 16.24429  35.25128 31.93148 1.000 49.07767  ? 115 THR   A CG2 1 
ATOM   780  N  N   . LYS   A 1 109 ? 16.96665  38.61890 31.76236 1.000 35.03364  ? 116 LYS   A N   1 
ATOM   781  C  CA  . LYS   A 1 109 ? 18.15180  39.24713 32.33834 1.000 36.54788  ? 116 LYS   A CA  1 
ATOM   782  C  C   . LYS   A 1 109 ? 17.77620  40.24202 33.42975 1.000 37.25499  ? 116 LYS   A C   1 
ATOM   783  O  O   . LYS   A 1 109 ? 18.38715  40.26475 34.50451 1.000 44.40054  ? 116 LYS   A O   1 
ATOM   784  C  CB  . LYS   A 1 109 ? 18.95534  39.93695 31.23625 1.000 40.17679  ? 116 LYS   A CB  1 
ATOM   785  C  CG  . LYS   A 1 109 ? 20.25215  40.56873 31.70671 1.000 48.10852  ? 116 LYS   A CG  1 
ATOM   786  C  CD  . LYS   A 1 109 ? 21.05353  41.10930 30.53428 1.000 48.75332  ? 116 LYS   A CD  1 
ATOM   787  C  CE  . LYS   A 1 109 ? 22.45298  41.51932 30.96307 1.000 59.12683  ? 116 LYS   A CE  1 
ATOM   788  N  NZ  . LYS   A 1 109 ? 22.61766  42.99885 30.98842 1.000 67.93627  ? 116 LYS   A NZ  1 
ATOM   789  N  N   . ALA   A 1 110 ? 16.76660  41.07423 33.17084 1.000 36.42015  ? 117 ALA   A N   1 
ATOM   790  C  CA  . ALA   A 1 110 ? 16.35818  42.06593 34.15961 1.000 39.83423  ? 117 ALA   A CA  1 
ATOM   791  C  C   . ALA   A 1 110 ? 15.69772  41.40859 35.36405 1.000 42.02415  ? 117 ALA   A C   1 
ATOM   792  O  O   . ALA   A 1 110 ? 15.85437  41.87726 36.49810 1.000 42.14408  ? 117 ALA   A O   1 
ATOM   793  C  CB  . ALA   A 1 110 ? 15.41613  43.08497 33.52112 1.000 34.04683  ? 117 ALA   A CB  1 
ATOM   794  N  N   . PHE   A 1 111 ? 14.96310  40.31728 35.13967 1.000 32.50118  ? 118 PHE   A N   1 
ATOM   795  C  CA  . PHE   A 1 111 ? 14.26356  39.66139 36.23874 1.000 35.37688  ? 118 PHE   A CA  1 
ATOM   796  C  C   . PHE   A 1 111 ? 15.24049  39.05689 37.24021 1.000 35.67953  ? 118 PHE   A C   1 
ATOM   797  O  O   . PHE   A 1 111 ? 15.05629  39.19511 38.45496 1.000 38.59190  ? 118 PHE   A O   1 
ATOM   798  C  CB  . PHE   A 1 111 ? 13.31876  38.59076 35.69330 1.000 32.67299  ? 118 PHE   A CB  1 
ATOM   799  C  CG  . PHE   A 1 111 ? 12.52679  37.88567 36.75625 1.000 33.41786  ? 118 PHE   A CG  1 
ATOM   800  C  CD1 . PHE   A 1 111 ? 11.91326  38.60283 37.76946 1.000 30.76241  ? 118 PHE   A CD1 1 
ATOM   801  C  CD2 . PHE   A 1 111 ? 12.39921  36.50625 36.74581 1.000 29.88960  ? 118 PHE   A CD2 1 
ATOM   802  C  CE1 . PHE   A 1 111 ? 11.18462  37.95946 38.75105 1.000 34.98378  ? 118 PHE   A CE1 1 
ATOM   803  C  CE2 . PHE   A 1 111 ? 11.67137  35.85703 37.72374 1.000 30.83472  ? 118 PHE   A CE2 1 
ATOM   804  C  CZ  . PHE   A 1 111 ? 11.06384  36.58442 38.72815 1.000 34.04211  ? 118 PHE   A CZ  1 
ATOM   805  N  N   . MET   A 1 112 ? 16.28534  38.38435 36.75359 1.000 35.02520  ? 119 MET   A N   1 
ATOM   806  C  CA  . MET   A 1 112 ? 17.23548  37.75039 37.66135 1.000 39.98634  ? 119 MET   A CA  1 
ATOM   807  C  C   . MET   A 1 112 ? 18.11114  38.77688 38.36598 1.000 39.37809  ? 119 MET   A C   1 
ATOM   808  O  O   . MET   A 1 112 ? 18.59623  38.51859 39.47341 1.000 46.23648  ? 119 MET   A O   1 
ATOM   809  C  CB  . MET   A 1 112 ? 18.10138  36.75411 36.89878 1.000 37.29823  ? 119 MET   A CB  1 
ATOM   810  C  CG  . MET   A 1 112 ? 17.31980  35.81681 36.00714 1.000 39.04038  ? 119 MET   A CG  1 
ATOM   811  S  SD  . MET   A 1 112 ? 18.16492  34.24659 35.80860 1.000 58.96694  ? 119 MET   A SD  1 
ATOM   812  C  CE  . MET   A 1 112 ? 18.82146  34.49741 34.15989 1.000 53.17543  ? 119 MET   A CE  1 
ATOM   813  N  N   . GLU   A 1 113 ? 18.33694  39.93342 37.73955 1.000 40.84661  ? 120 GLU   A N   1 
ATOM   814  C  CA  . GLU   A 1 113 ? 19.03275  41.01879 38.42266 1.000 51.37505  ? 120 GLU   A CA  1 
ATOM   815  C  C   . GLU   A 1 113 ? 18.23504  41.49353 39.62915 1.000 45.69306  ? 120 GLU   A C   1 
ATOM   816  O  O   . GLU   A 1 113 ? 18.78953  41.70515 40.71400 1.000 50.97020  ? 120 GLU   A O   1 
ATOM   817  C  CB  . GLU   A 1 113 ? 19.28147  42.17715 37.45575 1.000 49.98942  ? 120 GLU   A CB  1 
ATOM   818  C  CG  . GLU   A 1 113 ? 20.54844  42.05043 36.63034 1.000 57.51167  ? 120 GLU   A CG  1 
ATOM   819  C  CD  . GLU   A 1 113 ? 20.76243  43.23888 35.71064 1.000 74.52693  ? 120 GLU   A CD  1 
ATOM   820  O  OE1 . GLU   A 1 113 ? 19.93201  44.17307 35.73417 1.000 79.03269  ? 120 GLU   A OE1 1 
ATOM   821  O  OE2 . GLU   A 1 113 ? 21.76028  43.23659 34.96001 1.000 77.07616  ? 120 GLU   A OE2 1 
ATOM   822  N  N   . ALA   A 1 114 ? 16.92128  41.65722 39.45585 1.000 39.86395  ? 121 ALA   A N   1 
ATOM   823  C  CA  . ALA   A 1 114 ? 16.07418  42.10709 40.55397 1.000 41.25331  ? 121 ALA   A CA  1 
ATOM   824  C  C   . ALA   A 1 114 ? 15.96345  41.04455 41.63985 1.000 40.42094  ? 121 ALA   A C   1 
ATOM   825  O  O   . ALA   A 1 114 ? 15.90703  41.37268 42.83088 1.000 51.54199  ? 121 ALA   A O   1 
ATOM   826  C  CB  . ALA   A 1 114 ? 14.69049  42.48313 40.02472 1.000 44.12861  ? 121 ALA   A CB  1 
ATOM   827  N  N   . LEU   A 1 115 ? 15.94030  39.76550 41.24979 1.000 40.08692  ? 122 LEU   A N   1 
ATOM   828  C  CA  . LEU   A 1 115 ? 15.81035  38.68464 42.22287 1.000 44.48081  ? 122 LEU   A CA  1 
ATOM   829  C  C   . LEU   A 1 115 ? 16.95488  38.66605 43.22803 1.000 56.99823  ? 122 LEU   A C   1 
ATOM   830  O  O   . LEU   A 1 115 ? 16.77939  38.16030 44.34276 1.000 54.42155  ? 122 LEU   A O   1 
ATOM   831  C  CB  . LEU   A 1 115 ? 15.72721  37.33413 41.50767 1.000 39.89001  ? 122 LEU   A CB  1 
ATOM   832  C  CG  . LEU   A 1 115 ? 14.41027  37.02936 40.79178 1.000 46.84351  ? 122 LEU   A CG  1 
ATOM   833  C  CD1 . LEU   A 1 115 ? 14.57322  35.85324 39.84036 1.000 34.66178  ? 122 LEU   A CD1 1 
ATOM   834  C  CD2 . LEU   A 1 115 ? 13.30000  36.77002 41.79855 1.000 45.00167  ? 122 LEU   A CD2 1 
ATOM   835  N  N   . GLN   A 1 116 ? 18.12087  39.19764 42.86026 1.000 60.67503  ? 123 GLN   A N   1 
ATOM   836  C  CA  . GLN   A 1 116 ? 19.22908  39.33402 43.79589 1.000 64.49401  ? 123 GLN   A CA  1 
ATOM   837  C  C   . GLN   A 1 116 ? 19.16594  40.62466 44.60160 1.000 61.87399  ? 123 GLN   A C   1 
ATOM   838  O  O   . GLN   A 1 116 ? 19.83035  40.72481 45.64011 1.000 73.92748  ? 123 GLN   A O   1 
ATOM   839  C  CB  . GLN   A 1 116 ? 20.56683  39.26273 43.04937 1.000 68.14128  ? 123 GLN   A CB  1 
ATOM   840  C  CG  . GLN   A 1 116 ? 20.84772  37.91340 42.39854 1.000 73.16392  ? 123 GLN   A CG  1 
ATOM   841  C  CD  . GLN   A 1 116 ? 22.05013  37.94632 41.47115 1.000 88.97694  ? 123 GLN   A CD  1 
ATOM   842  O  OE1 . GLN   A 1 116 ? 21.99286  38.51772 40.38126 1.000 87.67678  ? 123 GLN   A OE1 1 
ATOM   843  N  NE2 . GLN   A 1 116 ? 23.14663  37.33008 41.90013 1.000 83.59778  ? 123 GLN   A NE2 1 
ATOM   844  N  N   . ALA   A 1 117 ? 18.38824  41.60721 44.15037 1.000 62.88149  ? 124 ALA   A N   1 
ATOM   845  C  CA  . ALA   A 1 117 ? 18.20053  42.86009 44.86772 1.000 57.03023  ? 124 ALA   A CA  1 
ATOM   846  C  C   . ALA   A 1 117 ? 17.05256  42.79902 45.86804 1.000 67.46987  ? 124 ALA   A C   1 
ATOM   847  O  O   . ALA   A 1 117 ? 16.61226  43.84679 46.35234 1.000 83.16810  ? 124 ALA   A O   1 
ATOM   848  C  CB  . ALA   A 1 117 ? 17.96703  44.00616 43.87906 1.000 52.42181  ? 124 ALA   A CB  1 
ATOM   849  N  N   . GLY   A 1 118 ? 16.55993  41.60343 46.18614 1.000 58.26661  ? 125 GLY   A N   1 
ATOM   850  C  CA  . GLY   A 1 118 ? 15.49224  41.42758 47.15015 1.000 62.03766  ? 125 GLY   A CA  1 
ATOM   851  C  C   . GLY   A 1 118 ? 14.15413  41.05357 46.55296 1.000 57.68219  ? 125 GLY   A C   1 
ATOM   852  O  O   . GLY   A 1 118 ? 13.25389  40.65238 47.30224 1.000 71.95623  ? 125 GLY   A O   1 
ATOM   853  N  N   . ALA   A 1 119 ? 13.98849  41.17131 45.23772 1.000 48.04293  ? 126 ALA   A N   1 
ATOM   854  C  CA  . ALA   A 1 119 ? 12.72688  40.81591 44.60761 1.000 50.45369  ? 126 ALA   A CA  1 
ATOM   855  C  C   . ALA   A 1 119 ? 12.45630  39.32010 44.75135 1.000 61.35736  ? 126 ALA   A C   1 
ATOM   856  O  O   . ALA   A 1 119 ? 13.35666  38.51807 45.01459 1.000 59.18889  ? 126 ALA   A O   1 
ATOM   857  C  CB  . ALA   A 1 119 ? 12.73731  41.20880 43.13061 1.000 40.14669  ? 126 ALA   A CB  1 
ATOM   858  N  N   . ASP   A 1 120 ? 11.19020  38.94931 44.58587 1.000 57.64922  ? 127 ASP   A N   1 
ATOM   859  C  CA  . ASP   A 1 120 ? 10.77412  37.55593 44.61991 1.000 52.03284  ? 127 ASP   A CA  1 
ATOM   860  C  C   . ASP   A 1 120 ? 10.08674  37.18876 43.30915 1.000 47.79924  ? 127 ASP   A C   1 
ATOM   861  O  O   . ASP   A 1 120 ? 9.83205   38.03762 42.45042 1.000 46.14593  ? 127 ASP   A O   1 
ATOM   862  C  CB  . ASP   A 1 120 ? 9.85805   37.27370 45.82089 1.000 59.75347  ? 127 ASP   A CB  1 
ATOM   863  C  CG  . ASP   A 1 120 ? 8.50484   37.94312 45.69987 1.000 63.84879  ? 127 ASP   A CG  1 
ATOM   864  O  OD1 . ASP   A 1 120 ? 8.44637   39.18924 45.74771 1.000 65.37219  ? 127 ASP   A OD1 1 
ATOM   865  O  OD2 . ASP   A 1 120 ? 7.49671   37.21911 45.56571 1.000 60.90581  ? 127 ASP   A OD2 1 
ATOM   866  N  N   . ILE   A 1 121 ? 9.78884   35.89364 43.17062 1.000 45.09794  ? 128 ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 121 ? 9.32665   35.34242 41.89821 1.000 50.85659  ? 128 ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 121 ? 7.99176   35.94758 41.47859 1.000 47.43084  ? 128 ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 121 ? 7.71655   36.09395 40.28027 1.000 38.17637  ? 128 ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 121 ? 9.25327   33.80364 42.00248 1.000 52.06396  ? 128 ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 121 ? 10.66038  33.20391 42.02351 1.000 54.05179  ? 128 ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 121 ? 8.45463   33.20540 40.85526 1.000 48.37438  ? 128 ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 121 ? 10.72159  31.81469 42.62041 1.000 57.50632  ? 128 ILE   A CD1 1 
ATOM   874  N  N   . SER   A 1 122 ? 7.15729   36.33711 42.44621 1.000 41.02587  ? 129 SER   A N   1 
ATOM   875  C  CA  . SER   A 1 122 ? 5.80874   36.80447 42.13835 1.000 44.22464  ? 129 SER   A CA  1 
ATOM   876  C  C   . SER   A 1 122 ? 5.79509   38.03553 41.23892 1.000 45.19869  ? 129 SER   A C   1 
ATOM   877  O  O   . SER   A 1 122 ? 4.78002   38.29433 40.58319 1.000 42.88332  ? 129 SER   A O   1 
ATOM   878  C  CB  . SER   A 1 122 ? 5.05128   37.10654 43.43172 1.000 40.10099  ? 129 SER   A CB  1 
ATOM   879  O  OG  . SER   A 1 122 ? 5.58484   38.25044 44.07535 1.000 47.08707  ? 129 SER   A OG  1 
ATOM   880  N  N   . MET   A 1 123 ? 6.88556   38.79848 41.19006 1.000 45.93658  ? 130 MET   A N   1 
ATOM   881  C  CA  . MET   A 1 123 ? 6.96799   39.98396 40.34634 1.000 39.90171  ? 130 MET   A CA  1 
ATOM   882  C  C   . MET   A 1 123 ? 7.44961   39.67731 38.93245 1.000 35.49001  ? 130 MET   A C   1 
ATOM   883  O  O   . MET   A 1 123 ? 7.84870   40.60102 38.21553 1.000 39.77984  ? 130 MET   A O   1 
ATOM   884  C  CB  . MET   A 1 123 ? 7.88892   41.02595 40.98611 1.000 35.87548  ? 130 MET   A CB  1 
ATOM   885  C  CG  . MET   A 1 123 ? 7.16846   42.03311 41.86378 1.000 45.90181  ? 130 MET   A CG  1 
ATOM   886  S  SD  . MET   A 1 123 ? 8.27596   42.85445 43.02478 1.000 70.88197  ? 130 MET   A SD  1 
ATOM   887  C  CE  . MET   A 1 123 ? 9.18566   41.45642 43.66453 1.000 44.35056  ? 130 MET   A CE  1 
ATOM   888  N  N   . ILE   A 1 124 ? 7.40934   38.40883 38.51476 1.000 34.50654  ? 131 ILE   A N   1 
ATOM   889  C  CA  . ILE   A 1 124 ? 7.94331   38.01959 37.21102 1.000 30.01971  ? 131 ILE   A CA  1 
ATOM   890  C  C   . ILE   A 1 124 ? 7.19322   38.70413 36.07385 1.000 31.52369  ? 131 ILE   A C   1 
ATOM   891  O  O   . ILE   A 1 124 ? 7.76953   38.96942 35.01129 1.000 27.46935  ? 131 ILE   A O   1 
ATOM   892  C  CB  . ILE   A 1 124 ? 7.90855   36.48312 37.07112 1.000 26.42489  ? 131 ILE   A CB  1 
ATOM   893  C  CG1 . ILE   A 1 124 ? 8.55957   36.03832 35.75991 1.000 31.05050  ? 131 ILE   A CG1 1 
ATOM   894  C  CG2 . ILE   A 1 124 ? 6.47971   35.96269 37.17987 1.000 29.39372  ? 131 ILE   A CG2 1 
ATOM   895  C  CD1 . ILE   A 1 124 ? 8.79007   34.54595 35.67284 1.000 27.48762  ? 131 ILE   A CD1 1 
ATOM   896  N  N   . GLY   A 1 125 ? 5.91007   39.01418 36.27488 1.000 37.53511  ? 132 GLY   A N   1 
ATOM   897  C  CA  . GLY   A 1 125 ? 5.12088   39.60177 35.20463 1.000 36.02934  ? 132 GLY   A CA  1 
ATOM   898  C  C   . GLY   A 1 125 ? 5.55018   41.00762 34.83442 1.000 46.03123  ? 132 GLY   A C   1 
ATOM   899  O  O   . GLY   A 1 125 ? 5.33614   41.44694 33.70091 1.000 37.93963  ? 132 GLY   A O   1 
ATOM   900  N  N   . GLN   A 1 126 ? 6.15852   41.73268 35.77639 1.000 32.11616  ? 133 GLN   A N   1 
ATOM   901  C  CA  . GLN   A 1 126 ? 6.64869   43.07791 35.50009 1.000 36.94121  ? 133 GLN   A CA  1 
ATOM   902  C  C   . GLN   A 1 126 ? 7.79799   43.09310 34.50160 1.000 38.95630  ? 133 GLN   A C   1 
ATOM   903  O  O   . GLN   A 1 126 ? 8.18430   44.17403 34.04375 1.000 37.87586  ? 133 GLN   A O   1 
ATOM   904  C  CB  . GLN   A 1 126 ? 7.09181   43.75382 36.79939 1.000 35.43701  ? 133 GLN   A CB  1 
ATOM   905  C  CG  . GLN   A 1 126 ? 5.96469   44.01936 37.78526 1.000 38.20309  ? 133 GLN   A CG  1 
ATOM   906  C  CD  . GLN   A 1 126 ? 6.41741   44.84657 38.97203 1.000 53.97699  ? 133 GLN   A CD  1 
ATOM   907  O  OE1 . GLN   A 1 126 ? 6.13284   44.51407 40.12283 1.000 59.77949  ? 133 GLN   A OE1 1 
ATOM   908  N  NE2 . GLN   A 1 126 ? 7.12829   45.93407 38.69597 1.000 51.44722  ? 133 GLN   A NE2 1 
ATOM   909  N  N   . PHE   A 1 127 ? 8.34982   41.93126 34.15656 1.000 31.36737  ? 134 PHE   A N   1 
ATOM   910  C  CA  . PHE   A 1 127 ? 9.45849   41.83299 33.21871 1.000 34.83303  ? 134 PHE   A CA  1 
ATOM   911  C  C   . PHE   A 1 127 ? 9.06328   41.12039 31.93219 1.000 37.28614  ? 134 PHE   A C   1 
ATOM   912  O  O   . PHE   A 1 127 ? 9.93146   40.82505 31.10408 1.000 34.95591  ? 134 PHE   A O   1 
ATOM   913  C  CB  . PHE   A 1 127 ? 10.64338  41.12834 33.88293 1.000 30.90254  ? 134 PHE   A CB  1 
ATOM   914  C  CG  . PHE   A 1 127 ? 11.06887  41.75853 35.18228 1.000 36.50290  ? 134 PHE   A CG  1 
ATOM   915  C  CD1 . PHE   A 1 127 ? 10.46053  41.39641 36.37418 1.000 29.15058  ? 134 PHE   A CD1 1 
ATOM   916  C  CD2 . PHE   A 1 127 ? 12.07014  42.71699 35.21223 1.000 35.23961  ? 134 PHE   A CD2 1 
ATOM   917  C  CE1 . PHE   A 1 127 ? 10.84314  41.97375 37.56968 1.000 33.95688  ? 134 PHE   A CE1 1 
ATOM   918  C  CE2 . PHE   A 1 127 ? 12.45757  43.29763 36.40719 1.000 34.08146  ? 134 PHE   A CE2 1 
ATOM   919  C  CZ  . PHE   A 1 127 ? 11.84207  42.92486 37.58640 1.000 32.04926  ? 134 PHE   A CZ  1 
ATOM   920  N  N   . GLY   A 1 128 ? 7.77525   40.83553 31.74914 1.000 32.03651  ? 135 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 128 ? 7.27215   40.29037 30.50586 1.000 34.03166  ? 135 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 128 ? 7.52522   38.81843 30.27911 1.000 39.98751  ? 135 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 128 ? 7.22992   38.32201 29.18725 1.000 37.91935  ? 135 GLY   A O   1 
ATOM   924  N  N   . VAL   A 1 129 ? 8.05114   38.09995 31.26923 1.000 34.05057  ? 136 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 129 ? 8.37617   36.68743 31.10315 1.000 32.43394  ? 136 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 129 ? 7.53574   35.84582 32.05360 1.000 33.09806  ? 136 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 129 ? 8.00051   34.82509 32.57424 1.000 30.16378  ? 136 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 129 ? 9.87718   36.43866 31.32983 1.000 29.35883  ? 136 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 129 ? 10.68697  37.05472 30.20176 1.000 32.34165  ? 136 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 129 ? 10.30747  37.00971 32.67166 1.000 25.59067  ? 136 VAL   A CG2 1 
ATOM   931  N  N   . GLY   A 1 130 ? 6.28693   36.26101 32.27345 1.000 25.78749  ? 137 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 130 ? 5.43783   35.56107 33.22287 1.000 24.08246  ? 137 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 130 ? 5.07186   34.15196 32.79671 1.000 27.87536  ? 137 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 130 ? 4.70949   33.32258 33.63648 1.000 22.43620  ? 137 GLY   A O   1 
ATOM   935  N  N   . PHE   A 1 131 ? 5.16491   33.85851 31.49558 1.000 22.77087  ? 138 PHE   A N   1 
ATOM   936  C  CA  . PHE   A 1 131 ? 4.79133   32.53684 30.99699 1.000 26.15733  ? 138 PHE   A CA  1 
ATOM   937  C  C   . PHE   A 1 131 ? 5.60582   31.43499 31.66233 1.000 24.71843  ? 138 PHE   A C   1 
ATOM   938  O  O   . PHE   A 1 131 ? 5.07854   30.35708 31.96196 1.000 26.66782  ? 138 PHE   A O   1 
ATOM   939  C  CB  . PHE   A 1 131 ? 4.97055   32.47893 29.48001 1.000 25.70296  ? 138 PHE   A CB  1 
ATOM   940  C  CG  . PHE   A 1 131 ? 4.97858   31.08312 28.92522 1.000 28.29627  ? 138 PHE   A CG  1 
ATOM   941  C  CD1 . PHE   A 1 131 ? 3.79055   30.42540 28.66569 1.000 26.77903  ? 138 PHE   A CD1 1 
ATOM   942  C  CD2 . PHE   A 1 131 ? 6.17382   30.42682 28.66726 1.000 27.06149  ? 138 PHE   A CD2 1 
ATOM   943  C  CE1 . PHE   A 1 131 ? 3.79020   29.14191 28.15835 1.000 28.86927  ? 138 PHE   A CE1 1 
ATOM   944  C  CE2 . PHE   A 1 131 ? 6.18075   29.14406 28.15920 1.000 30.96005  ? 138 PHE   A CE2 1 
ATOM   945  C  CZ  . PHE   A 1 131 ? 4.98684   28.49992 27.90499 1.000 30.28839  ? 138 PHE   A CZ  1 
ATOM   946  N  N   . TYR   A 1 132 ? 6.89623   31.68261 31.89206 1.000 25.31596  ? 139 TYR   A N   1 
ATOM   947  C  CA  . TYR   A 1 132 ? 7.77786   30.66149 32.44300 1.000 21.63730  ? 139 TYR   A CA  1 
ATOM   948  C  C   . TYR   A 1 132 ? 7.44326   30.30383 33.88368 1.000 31.23467  ? 139 TYR   A C   1 
ATOM   949  O  O   . TYR   A 1 132 ? 7.95761   29.29967 34.38894 1.000 28.49319  ? 139 TYR   A O   1 
ATOM   950  C  CB  . TYR   A 1 132 ? 9.22893   31.12362 32.33301 1.000 20.20473  ? 139 TYR   A CB  1 
ATOM   951  C  CG  . TYR   A 1 132 ? 9.65721   31.34585 30.90309 1.000 28.89977  ? 139 TYR   A CG  1 
ATOM   952  C  CD1 . TYR   A 1 132 ? 9.79310   30.27741 30.02694 1.000 23.65878  ? 139 TYR   A CD1 1 
ATOM   953  C  CD2 . TYR   A 1 132 ? 9.90305   32.62394 30.42147 1.000 24.01180  ? 139 TYR   A CD2 1 
ATOM   954  C  CE1 . TYR   A 1 132 ? 10.17512  30.47397 28.71508 1.000 20.93264  ? 139 TYR   A CE1 1 
ATOM   955  C  CE2 . TYR   A 1 132 ? 10.28633  32.83105 29.10904 1.000 32.77828  ? 139 TYR   A CE2 1 
ATOM   956  C  CZ  . TYR   A 1 132 ? 10.42051  31.75167 28.26112 1.000 25.99746  ? 139 TYR   A CZ  1 
ATOM   957  O  OH  . TYR   A 1 132 ? 10.80210  31.94956 26.95439 1.000 30.27770  ? 139 TYR   A OH  1 
ATOM   958  N  N   . SER   A 1 133 ? 6.59480   31.08796 34.55246 1.000 26.75703  ? 140 SER   A N   1 
ATOM   959  C  CA  . SER   A 1 133 ? 6.08742   30.68981 35.85920 1.000 23.91122  ? 140 SER   A CA  1 
ATOM   960  C  C   . SER   A 1 133 ? 5.22729   29.43603 35.78744 1.000 25.15594  ? 140 SER   A C   1 
ATOM   961  O  O   . SER   A 1 133 ? 4.89739   28.86987 36.83576 1.000 26.32918  ? 140 SER   A O   1 
ATOM   962  C  CB  . SER   A 1 133 ? 5.28187   31.82940 36.48285 1.000 23.58076  ? 140 SER   A CB  1 
ATOM   963  O  OG  . SER   A 1 133 ? 4.11291   32.09242 35.72731 1.000 29.42956  ? 140 SER   A OG  1 
ATOM   964  N  N   . ALA   A 1 134 ? 4.84948   28.99931 34.58272 1.000 24.42397  ? 141 ALA   A N   1 
ATOM   965  C  CA  . ALA   A 1 134 ? 4.12460   27.74247 34.43633 1.000 27.61973  ? 141 ALA   A CA  1 
ATOM   966  C  C   . ALA   A 1 134 ? 4.92317   26.57749 35.00106 1.000 24.10114  ? 141 ALA   A C   1 
ATOM   967  O  O   . ALA   A 1 134 ? 4.34959   25.60788 35.50988 1.000 24.76929  ? 141 ALA   A O   1 
ATOM   968  C  CB  . ALA   A 1 134 ? 3.79577   27.49703 32.96477 1.000 24.75164  ? 141 ALA   A CB  1 
ATOM   969  N  N   . TYR   A 1 135 ? 6.24956   26.66460 34.93689 1.000 23.98697  ? 142 TYR   A N   1 
ATOM   970  C  CA  . TYR   A 1 135 ? 7.13179   25.61557 35.42643 1.000 25.33170  ? 142 TYR   A CA  1 
ATOM   971  C  C   . TYR   A 1 135 ? 7.26808   25.61343 36.94392 1.000 32.19594  ? 142 TYR   A C   1 
ATOM   972  O  O   . TYR   A 1 135 ? 8.07456   24.84427 37.47891 1.000 35.38696  ? 142 TYR   A O   1 
ATOM   973  C  CB  . TYR   A 1 135 ? 8.50122   25.74311 34.75655 1.000 23.34677  ? 142 TYR   A CB  1 
ATOM   974  C  CG  . TYR   A 1 135 ? 8.44099   25.44282 33.27494 1.000 29.13325  ? 142 TYR   A CG  1 
ATOM   975  C  CD1 . TYR   A 1 135 ? 8.58704   24.14428 32.80582 1.000 24.63998  ? 142 TYR   A CD1 1 
ATOM   976  C  CD2 . TYR   A 1 135 ? 8.21431   26.45289 32.34808 1.000 27.22919  ? 142 TYR   A CD2 1 
ATOM   977  C  CE1 . TYR   A 1 135 ? 8.52165   23.86022 31.45842 1.000 25.29926  ? 142 TYR   A CE1 1 
ATOM   978  C  CE2 . TYR   A 1 135 ? 8.14727   26.17831 30.99483 1.000 26.67061  ? 142 TYR   A CE2 1 
ATOM   979  C  CZ  . TYR   A 1 135 ? 8.30113   24.87943 30.55595 1.000 30.13507  ? 142 TYR   A CZ  1 
ATOM   980  O  OH  . TYR   A 1 135 ? 8.23491   24.59463 29.21007 1.000 32.54237  ? 142 TYR   A OH  1 
ATOM   981  N  N   . LEU   A 1 136 ? 6.50652   26.45863 37.64345 1.000 26.81126  ? 143 LEU   A N   1 
ATOM   982  C  CA  . LEU   A 1 136 ? 6.34265   26.28258 39.08096 1.000 26.80023  ? 143 LEU   A CA  1 
ATOM   983  C  C   . LEU   A 1 136 ? 5.50619   25.04948 39.38856 1.000 30.89147  ? 143 LEU   A C   1 
ATOM   984  O  O   . LEU   A 1 136 ? 5.74761   24.36805 40.39128 1.000 30.39432  ? 143 LEU   A O   1 
ATOM   985  C  CB  . LEU   A 1 136 ? 5.68653   27.51801 39.70031 1.000 28.68696  ? 143 LEU   A CB  1 
ATOM   986  C  CG  . LEU   A 1 136 ? 6.48995   28.81376 39.82357 1.000 33.86872  ? 143 LEU   A CG  1 
ATOM   987  C  CD1 . LEU   A 1 136 ? 5.57350   29.96524 40.20357 1.000 30.01003  ? 143 LEU   A CD1 1 
ATOM   988  C  CD2 . LEU   A 1 136 ? 7.60829   28.66205 40.83853 1.000 24.99929  ? 143 LEU   A CD2 1 
ATOM   989  N  N   . VAL   A 1 137 ? 4.52783   24.74858 38.53852 1.000 29.51174  ? 144 VAL   A N   1 
ATOM   990  C  CA  . VAL   A 1 137 ? 3.58643   23.66310 38.78645 1.000 30.35437  ? 144 VAL   A CA  1 
ATOM   991  C  C   . VAL   A 1 137 ? 3.62894   22.58096 37.71942 1.000 29.63984  ? 144 VAL   A C   1 
ATOM   992  O  O   . VAL   A 1 137 ? 3.07623   21.49418 37.94571 1.000 33.64430  ? 144 VAL   A O   1 
ATOM   993  C  CB  . VAL   A 1 137 ? 2.14480   24.19683 38.93000 1.000 29.22384  ? 144 VAL   A CB  1 
ATOM   994  C  CG1 . VAL   A 1 137 ? 2.05064   25.16627 40.09966 1.000 32.09571  ? 144 VAL   A CG1 1 
ATOM   995  C  CG2 . VAL   A 1 137 ? 1.70014   24.86448 37.63642 1.000 26.19292  ? 144 VAL   A CG2 1 
ATOM   996  N  N   . ALA   A 1 138 ? 4.26018   22.82394 36.57385 1.000 27.61039  ? 145 ALA   A N   1 
ATOM   997  C  CA  . ALA   A 1 138 ? 4.25620   21.88597 35.46104 1.000 28.11688  ? 145 ALA   A CA  1 
ATOM   998  C  C   . ALA   A 1 138 ? 5.65812   21.35428 35.19466 1.000 27.56801  ? 145 ALA   A C   1 
ATOM   999  O  O   . ALA   A 1 138 ? 6.64049   22.10064 35.25656 1.000 32.84513  ? 145 ALA   A O   1 
ATOM   1000 C  CB  . ALA   A 1 138 ? 3.70513   22.54529 34.19354 1.000 28.60352  ? 145 ALA   A CB  1 
ATOM   1001 N  N   . GLU   A 1 139 ? 5.74081   20.05583 34.90012 1.000 30.52982  ? 146 GLU   A N   1 
ATOM   1002 C  CA  . GLU   A 1 139 ? 6.98059   19.44372 34.44220 1.000 37.31782  ? 146 GLU   A CA  1 
ATOM   1003 C  C   . GLU   A 1 139 ? 7.13653   19.50798 32.93021 1.000 39.08629  ? 146 GLU   A C   1 
ATOM   1004 O  O   . GLU   A 1 139 ? 8.25018   19.32663 32.42476 1.000 36.11294  ? 146 GLU   A O   1 
ATOM   1005 C  CB  . GLU   A 1 139 ? 7.05583   17.98203 34.90243 1.000 33.80744  ? 146 GLU   A CB  1 
ATOM   1006 C  CG  . GLU   A 1 139 ? 6.04613   17.05849 34.23292 1.000 37.46498  ? 146 GLU   A CG  1 
ATOM   1007 C  CD  . GLU   A 1 139 ? 6.04533   15.66178 34.82904 1.000 58.60376  ? 146 GLU   A CD  1 
ATOM   1008 O  OE1 . GLU   A 1 139 ? 6.59733   15.48936 35.93584 1.000 65.88114  ? 146 GLU   A OE1 1 
ATOM   1009 O  OE2 . GLU   A 1 139 ? 5.49391   14.73680 34.19377 1.000 69.57162  ? 146 GLU   A OE2 1 
ATOM   1010 N  N   . LYS   A 1 140 ? 6.04944   19.75975 32.20523 1.000 32.26280  ? 147 LYS   A N   1 
ATOM   1011 C  CA  . LYS   A 1 140 ? 6.08110   19.90256 30.75867 1.000 28.28987  ? 147 LYS   A CA  1 
ATOM   1012 C  C   . LYS   A 1 140 ? 4.95100   20.83471 30.35102 1.000 29.42038  ? 147 LYS   A C   1 
ATOM   1013 O  O   . LYS   A 1 140 ? 3.84638   20.75218 30.89430 1.000 30.95540  ? 147 LYS   A O   1 
ATOM   1014 C  CB  . LYS   A 1 140 ? 5.94212   18.54631 30.05639 1.000 30.74498  ? 147 LYS   A CB  1 
ATOM   1015 C  CG  . LYS   A 1 140 ? 5.61295   18.64219 28.57712 1.000 33.04026  ? 147 LYS   A CG  1 
ATOM   1016 C  CD  . LYS   A 1 140 ? 5.84294   17.31802 27.87144 1.000 38.09695  ? 147 LYS   A CD  1 
ATOM   1017 C  CE  . LYS   A 1 140 ? 4.60918   16.88491 27.10111 1.000 38.84788  ? 147 LYS   A CE  1 
ATOM   1018 N  NZ  . LYS   A 1 140 ? 4.56330   15.40746 26.92284 1.000 56.00411  ? 147 LYS   A NZ  1 
ATOM   1019 N  N   . VAL   A 1 141 ? 5.23425   21.72772 29.40654 1.000 28.50480  ? 148 VAL   A N   1 
ATOM   1020 C  CA  . VAL   A 1 141 ? 4.25316   22.68737 28.91607 1.000 25.70904  ? 148 VAL   A CA  1 
ATOM   1021 C  C   . VAL   A 1 141 ? 4.13190   22.53400 27.40729 1.000 27.93339  ? 148 VAL   A C   1 
ATOM   1022 O  O   . VAL   A 1 141 ? 5.13986   22.56651 26.69273 1.000 28.71734  ? 148 VAL   A O   1 
ATOM   1023 C  CB  . VAL   A 1 141 ? 4.63224   24.13574 29.27963 1.000 26.34309  ? 148 VAL   A CB  1 
ATOM   1024 C  CG1 . VAL   A 1 141 ? 3.61492   25.10725 28.69944 1.000 25.49318  ? 148 VAL   A CG1 1 
ATOM   1025 C  CG2 . VAL   A 1 141 ? 4.72914   24.29812 30.78716 1.000 23.48090  ? 148 VAL   A CG2 1 
ATOM   1026 N  N   . THR   A 1 142 ? 2.90278   22.36309 26.92755 1.000 28.10558  ? 149 THR   A N   1 
ATOM   1027 C  CA  . THR   A 1 142 ? 2.60096   22.34834 25.50386 1.000 27.10713  ? 149 THR   A CA  1 
ATOM   1028 C  C   . THR   A 1 142 ? 1.77470   23.57700 25.14959 1.000 36.41514  ? 149 THR   A C   1 
ATOM   1029 O  O   . THR   A 1 142 ? 0.83911   23.93642 25.87178 1.000 29.98061  ? 149 THR   A O   1 
ATOM   1030 C  CB  . THR   A 1 142 ? 1.83648   21.08304 25.10200 1.000 28.26024  ? 149 THR   A CB  1 
ATOM   1031 O  OG1 . THR   A 1 142 ? 2.49023   19.92879 25.64308 1.000 36.79328  ? 149 THR   A OG1 1 
ATOM   1032 C  CG2 . THR   A 1 142 ? 1.77963   20.95915 23.58793 1.000 26.64665  ? 149 THR   A CG2 1 
ATOM   1033 N  N   . VAL   A 1 143 ? 2.12305   24.21849 24.03758 1.000 25.04465  ? 150 VAL   A N   1 
ATOM   1034 C  CA  . VAL   A 1 143 ? 1.42456   25.40478 23.55652 1.000 25.78841  ? 150 VAL   A CA  1 
ATOM   1035 C  C   . VAL   A 1 143 ? 0.92040   25.12814 22.14853 1.000 29.60592  ? 150 VAL   A C   1 
ATOM   1036 O  O   . VAL   A 1 143 ? 1.71890   24.96142 21.21793 1.000 31.95477  ? 150 VAL   A O   1 
ATOM   1037 C  CB  . VAL   A 1 143 ? 2.32401   26.65052 23.57193 1.000 29.37530  ? 150 VAL   A CB  1 
ATOM   1038 C  CG1 . VAL   A 1 143 ? 1.59209   27.83374 22.95651 1.000 20.52233  ? 150 VAL   A CG1 1 
ATOM   1039 C  CG2 . VAL   A 1 143 ? 2.76803   26.97261 24.98599 1.000 32.55401  ? 150 VAL   A CG2 1 
ATOM   1040 N  N   . ILE   A 1 144 ? -0.39796  25.07909 21.99370 1.000 29.28958  ? 151 ILE   A N   1 
ATOM   1041 C  CA  . ILE   A 1 144 ? -1.04145  25.03029 20.68705 1.000 25.77621  ? 151 ILE   A CA  1 
ATOM   1042 C  C   . ILE   A 1 144 ? -1.55480  26.42830 20.37450 1.000 26.91109  ? 151 ILE   A C   1 
ATOM   1043 O  O   . ILE   A 1 144 ? -2.23404  27.04494 21.20453 1.000 31.98798  ? 151 ILE   A O   1 
ATOM   1044 C  CB  . ILE   A 1 144 ? -2.18021  23.99660 20.66264 1.000 30.28326  ? 151 ILE   A CB  1 
ATOM   1045 C  CG1 . ILE   A 1 144 ? -1.79997  22.76986 21.49612 1.000 32.98779  ? 151 ILE   A CG1 1 
ATOM   1046 C  CG2 . ILE   A 1 144 ? -2.50924  23.59622 19.23375 1.000 31.02146  ? 151 ILE   A CG2 1 
ATOM   1047 C  CD1 . ILE   A 1 144 ? -0.87178  21.81001 20.78612 1.000 32.61540  ? 151 ILE   A CD1 1 
ATOM   1048 N  N   . THR   A 1 145 ? -1.21887  26.94023 19.19137 1.000 25.61354  ? 152 THR   A N   1 
ATOM   1049 C  CA  . THR   A 1 145 ? -1.55336  28.31379 18.84039 1.000 30.05425  ? 152 THR   A CA  1 
ATOM   1050 C  C   . THR   A 1 145 ? -1.86097  28.40707 17.35135 1.000 31.33843  ? 152 THR   A C   1 
ATOM   1051 O  O   . THR   A 1 145 ? -1.28691  27.68183 16.53373 1.000 31.01637  ? 152 THR   A O   1 
ATOM   1052 C  CB  . THR   A 1 145 ? -0.42107  29.28110 19.22186 1.000 23.76256  ? 152 THR   A CB  1 
ATOM   1053 O  OG1 . THR   A 1 145 ? -0.82368  30.63191 18.95855 1.000 32.09183  ? 152 THR   A OG1 1 
ATOM   1054 C  CG2 . THR   A 1 145 ? 0.84941   28.96529 18.44442 1.000 26.55538  ? 152 THR   A CG2 1 
ATOM   1055 N  N   . LYS   A 1 146 ? -2.78434  29.30574 17.01039 1.000 28.21093  ? 153 LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 146 ? -3.19547  29.51948 15.62673 1.000 30.00502  ? 153 LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 146 ? -3.34712  31.01312 15.38734 1.000 28.85950  ? 153 LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 146 ? -4.16447  31.66872 16.03969 1.000 27.65116  ? 153 LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 146 ? -4.50558  28.78691 15.31385 1.000 27.89752  ? 153 LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 146 ? -5.09624  29.12030 13.94925 1.000 33.52145  ? 153 LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 146 ? -4.19693  28.62930 12.82411 1.000 28.46986  ? 153 LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 146 ? -4.89915  28.70873 11.47805 1.000 38.67525  ? 153 LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 146 ? -4.91291  30.09449 10.93013 1.000 37.02028  ? 153 LYS   A NZ  1 
ATOM   1064 N  N   . HIS   A 1 147 ? -2.56587  31.54471 14.45342 1.000 30.49376  ? 154 HIS   A N   1 
ATOM   1065 C  CA  . HIS   A 1 147 ? -2.59838  32.95460 14.09566 1.000 32.75428  ? 154 HIS   A CA  1 
ATOM   1066 C  C   . HIS   A 1 147 ? -3.22713  33.11072 12.71760 1.000 30.61484  ? 154 HIS   A C   1 
ATOM   1067 O  O   . HIS   A 1 147 ? -3.06586  32.24323 11.85411 1.000 27.96128  ? 154 HIS   A O   1 
ATOM   1068 C  CB  . HIS   A 1 147 ? -1.18696  33.54557 14.11133 1.000 28.67260  ? 154 HIS   A CB  1 
ATOM   1069 C  CG  . HIS   A 1 147 ? -1.14545  35.02866 13.92114 1.000 30.64208  ? 154 HIS   A CG  1 
ATOM   1070 N  ND1 . HIS   A 1 147 ? -1.18992  35.62256 12.67847 1.000 32.70498  ? 154 HIS   A ND1 1 
ATOM   1071 C  CD2 . HIS   A 1 147 ? -1.05564  36.03888 14.81801 1.000 31.23949  ? 154 HIS   A CD2 1 
ATOM   1072 C  CE1 . HIS   A 1 147 ? -1.13043  36.93487 12.81783 1.000 34.11462  ? 154 HIS   A CE1 1 
ATOM   1073 N  NE2 . HIS   A 1 147 ? -1.04941  37.21360 14.10632 1.000 36.86831  ? 154 HIS   A NE2 1 
ATOM   1074 N  N   . ASN   A 1 148 ? -3.93937  34.22418 12.51399 1.000 29.37085  ? 155 ASN   A N   1 
ATOM   1075 C  CA  . ASN   A 1 148 ? -4.67382  34.42750 11.26676 1.000 28.72934  ? 155 ASN   A CA  1 
ATOM   1076 C  C   . ASN   A 1 148 ? -3.78111  34.30877 10.03907 1.000 30.76923  ? 155 ASN   A C   1 
ATOM   1077 O  O   . ASN   A 1 148 ? -4.26187  33.96096 8.95449  1.000 34.14959  ? 155 ASN   A O   1 
ATOM   1078 C  CB  . ASN   A 1 148 ? -5.36064  35.79486 11.27608 1.000 36.04906  ? 155 ASN   A CB  1 
ATOM   1079 C  CG  . ASN   A 1 148 ? -6.74036  35.74999 11.90141 1.000 32.54428  ? 155 ASN   A CG  1 
ATOM   1080 O  OD1 . ASN   A 1 148 ? -7.34246  34.68452 12.02677 1.000 32.14380  ? 155 ASN   A OD1 1 
ATOM   1081 N  ND2 . ASN   A 1 148 ? -7.25191  36.91110 12.29139 1.000 33.58501  ? 155 ASN   A ND2 1 
ATOM   1082 N  N   . ASP   A 1 149 ? -2.48387  34.56582 10.19142 1.000 32.02762  ? 156 ASP   A N   1 
ATOM   1083 C  CA  . ASP   A 1 149 ? -1.55470  34.62011 9.07263  1.000 38.39574  ? 156 ASP   A CA  1 
ATOM   1084 C  C   . ASP   A 1 149 ? -0.69534  33.36980 8.93525  1.000 32.83604  ? 156 ASP   A C   1 
ATOM   1085 O  O   . ASP   A 1 149 ? 0.19315   33.34129 8.07851  1.000 37.23469  ? 156 ASP   A O   1 
ATOM   1086 C  CB  . ASP   A 1 149 ? -0.64661  35.84555 9.21476  1.000 34.97639  ? 156 ASP   A CB  1 
ATOM   1087 C  CG  . ASP   A 1 149 ? -1.41551  37.14931 9.15027  1.000 46.65484  ? 156 ASP   A CG  1 
ATOM   1088 O  OD1 . ASP   A 1 149 ? -2.53561  37.15656 8.59645  1.000 47.82200  ? 156 ASP   A OD1 1 
ATOM   1089 O  OD2 . ASP   A 1 149 ? -0.90565  38.16645 9.66484  1.000 46.52433  ? 156 ASP   A OD2 1 
ATOM   1090 N  N   . ASP   A 1 150 ? -0.93007  32.33869 9.74264  1.000 31.01850  ? 157 ASP   A N   1 
ATOM   1091 C  CA  . ASP   A 1 150 ? -0.04003  31.18779 9.75238  1.000 28.65630  ? 157 ASP   A CA  1 
ATOM   1092 C  C   . ASP   A 1 150 ? -0.83237  29.93043 10.08108 1.000 39.50925  ? 157 ASP   A C   1 
ATOM   1093 O  O   . ASP   A 1 150 ? -2.01229  29.98501 10.43547 1.000 37.72979  ? 157 ASP   A O   1 
ATOM   1094 C  CB  . ASP   A 1 150 ? 1.10546   31.38967 10.75050 1.000 29.70237  ? 157 ASP   A CB  1 
ATOM   1095 C  CG  . ASP   A 1 150 ? 2.39921   30.75404 10.28977 1.000 31.26780  ? 157 ASP   A CG  1 
ATOM   1096 O  OD1 . ASP   A 1 150 ? 2.36127   29.94895 9.33607  1.000 39.61651  ? 157 ASP   A OD1 1 
ATOM   1097 O  OD2 . ASP   A 1 150 ? 3.45494   31.05859 10.88292 1.000 36.90627  ? 157 ASP   A OD2 1 
ATOM   1098 N  N   . GLU   A 1 151 ? -0.16025  28.78874 9.95807  1.000 37.23476  ? 158 GLU   A N   1 
ATOM   1099 C  CA  . GLU   A 1 151 ? -0.75568  27.49726 10.25576 1.000 31.70800  ? 158 GLU   A CA  1 
ATOM   1100 C  C   . GLU   A 1 151 ? -0.78603  27.26075 11.76564 1.000 34.30364  ? 158 GLU   A C   1 
ATOM   1101 O  O   . GLU   A 1 151 ? -0.19572  28.00420 12.55369 1.000 33.86081  ? 158 GLU   A O   1 
ATOM   1102 C  CB  . GLU   A 1 151 ? 0.02170   26.38319 9.55419  1.000 40.90999  ? 158 GLU   A CB  1 
ATOM   1103 C  CG  . GLU   A 1 151 ? -0.24780  26.27336 8.05793  1.000 45.10141  ? 158 GLU   A CG  1 
ATOM   1104 C  CD  . GLU   A 1 151 ? -1.72464  26.14521 7.73225  1.000 81.02876  ? 158 GLU   A CD  1 
ATOM   1105 O  OE1 . GLU   A 1 151 ? -2.34750  25.14627 8.15301  1.000 89.80215  ? 158 GLU   A OE1 1 
ATOM   1106 O  OE2 . GLU   A 1 151 ? -2.26730  27.05036 7.06475  1.000 80.40378  ? 158 GLU   A OE2 1 
ATOM   1107 N  N   . GLN   A 1 152 ? -1.49515  26.20934 12.16744 1.000 31.65275  ? 159 GLN   A N   1 
ATOM   1108 C  CA  . GLN   A 1 152 ? -1.55655  25.82484 13.57086 1.000 30.17498  ? 159 GLN   A CA  1 
ATOM   1109 C  C   . GLN   A 1 152 ? -0.29017  25.06742 13.95117 1.000 28.88330  ? 159 GLN   A C   1 
ATOM   1110 O  O   . GLN   A 1 152 ? 0.10632   24.12070 13.26446 1.000 34.11018  ? 159 GLN   A O   1 
ATOM   1111 C  CB  . GLN   A 1 152 ? -2.79333  24.96670 13.83261 1.000 29.62307  ? 159 GLN   A CB  1 
ATOM   1112 C  CG  . GLN   A 1 152 ? -3.05056  24.66451 15.29920 1.000 33.16212  ? 159 GLN   A CG  1 
ATOM   1113 C  CD  . GLN   A 1 152 ? -4.46064  24.16896 15.54474 1.000 32.51520  ? 159 GLN   A CD  1 
ATOM   1114 O  OE1 . GLN   A 1 152 ? -5.42205  24.69263 14.98266 1.000 44.90107  ? 159 GLN   A OE1 1 
ATOM   1115 N  NE2 . GLN   A 1 152 ? -4.59022  23.14541 16.37828 1.000 35.57513  ? 159 GLN   A NE2 1 
ATOM   1116 N  N   . TYR   A 1 153 ? 0.34500   25.48505 15.04444 1.000 27.75010  ? 160 TYR   A N   1 
ATOM   1117 C  CA  . TYR   A 1 153 ? 1.62114   24.92425 15.46131 1.000 30.03698  ? 160 TYR   A CA  1 
ATOM   1118 C  C   . TYR   A 1 153 ? 1.55097   24.46529 16.90947 1.000 33.91472  ? 160 TYR   A C   1 
ATOM   1119 O  O   . TYR   A 1 153 ? 0.73275   24.95072 17.69579 1.000 28.96098  ? 160 TYR   A O   1 
ATOM   1120 C  CB  . TYR   A 1 153 ? 2.76246   25.93678 15.29994 1.000 27.08552  ? 160 TYR   A CB  1 
ATOM   1121 C  CG  . TYR   A 1 153 ? 3.19387   26.13963 13.86756 1.000 36.31836  ? 160 TYR   A CG  1 
ATOM   1122 C  CD1 . TYR   A 1 153 ? 4.03497   25.22971 13.24296 1.000 31.17144  ? 160 TYR   A CD1 1 
ATOM   1123 C  CD2 . TYR   A 1 153 ? 2.76491   27.24207 13.14121 1.000 37.71226  ? 160 TYR   A CD2 1 
ATOM   1124 C  CE1 . TYR   A 1 153 ? 4.43261   25.40725 11.93401 1.000 38.56383  ? 160 TYR   A CE1 1 
ATOM   1125 C  CE2 . TYR   A 1 153 ? 3.15819   27.42968 11.83122 1.000 32.61476  ? 160 TYR   A CE2 1 
ATOM   1126 C  CZ  . TYR   A 1 153 ? 3.99230   26.50862 11.23288 1.000 41.79549  ? 160 TYR   A CZ  1 
ATOM   1127 O  OH  . TYR   A 1 153 ? 4.38933   26.68867 9.92842  1.000 54.93133  ? 160 TYR   A OH  1 
ATOM   1128 N  N   . ALA   A 1 154 ? 2.43357   23.52914 17.25543 1.000 40.75210  ? 161 ALA   A N   1 
ATOM   1129 C  CA  . ALA   A 1 154 ? 2.51561   22.96820 18.60019 1.000 30.85995  ? 161 ALA   A CA  1 
ATOM   1130 C  C   . ALA   A 1 154 ? 3.92628   23.18067 19.13444 1.000 35.22597  ? 161 ALA   A C   1 
ATOM   1131 O  O   . ALA   A 1 154 ? 4.88577   22.59110 18.62502 1.000 35.13341  ? 161 ALA   A O   1 
ATOM   1132 C  CB  . ALA   A 1 154 ? 2.14589   21.48562 18.60216 1.000 36.36317  ? 161 ALA   A CB  1 
ATOM   1133 N  N   . TRP   A 1 155 ? 4.04518   24.02620 20.15124 1.000 30.09906  ? 162 TRP   A N   1 
ATOM   1134 C  CA  . TRP   A 1 155 ? 5.28569   24.25944 20.87342 1.000 25.79544  ? 162 TRP   A CA  1 
ATOM   1135 C  C   . TRP   A 1 155 ? 5.27808   23.42769 22.15112 1.000 29.35714  ? 162 TRP   A C   1 
ATOM   1136 O  O   . TRP   A 1 155 ? 4.22204   23.17849 22.73770 1.000 31.46241  ? 162 TRP   A O   1 
ATOM   1137 C  CB  . TRP   A 1 155 ? 5.43293   25.75144 21.18789 1.000 28.85605  ? 162 TRP   A CB  1 
ATOM   1138 C  CG  . TRP   A 1 155 ? 6.69750   26.16332 21.87848 1.000 26.00432  ? 162 TRP   A CG  1 
ATOM   1139 C  CD1 . TRP   A 1 155 ? 7.81541   26.68354 21.29458 1.000 26.65246  ? 162 TRP   A CD1 1 
ATOM   1140 C  CD2 . TRP   A 1 155 ? 6.95491   26.14156 23.28799 1.000 24.82870  ? 162 TRP   A CD2 1 
ATOM   1141 N  NE1 . TRP   A 1 155 ? 8.75960   26.96773 22.24966 1.000 26.04332  ? 162 TRP   A NE1 1 
ATOM   1142 C  CE2 . TRP   A 1 155 ? 8.25671   26.64372 23.48186 1.000 26.01065  ? 162 TRP   A CE2 1 
ATOM   1143 C  CE3 . TRP   A 1 155 ? 6.21521   25.73714 24.40330 1.000 24.77906  ? 162 TRP   A CE3 1 
ATOM   1144 C  CZ2 . TRP   A 1 155 ? 8.83509   26.75142 24.74412 1.000 26.00158  ? 162 TRP   A CZ2 1 
ATOM   1145 C  CZ3 . TRP   A 1 155 ? 6.79127   25.84441 25.65611 1.000 25.52617  ? 162 TRP   A CZ3 1 
ATOM   1146 C  CH2 . TRP   A 1 155 ? 8.08786   26.34762 25.81607 1.000 31.51818  ? 162 TRP   A CH2 1 
ATOM   1147 N  N   . GLU   A 1 156 ? 6.46065   22.98330 22.57409 1.000 26.98426  ? 163 GLU   A N   1 
ATOM   1148 C  CA  . GLU   A 1 156 ? 6.53666   22.07459 23.71011 1.000 27.77205  ? 163 GLU   A CA  1 
ATOM   1149 C  C   . GLU   A 1 156 ? 7.93051   22.12145 24.31828 1.000 33.16112  ? 163 GLU   A C   1 
ATOM   1150 O  O   . GLU   A 1 156 ? 8.92743   22.17360 23.59408 1.000 31.66247  ? 163 GLU   A O   1 
ATOM   1151 C  CB  . GLU   A 1 156 ? 6.19662   20.63864 23.29097 1.000 36.16527  ? 163 GLU   A CB  1 
ATOM   1152 C  CG  . GLU   A 1 156 ? 5.83786   19.71764 24.44645 1.000 39.26754  ? 163 GLU   A CG  1 
ATOM   1153 C  CD  . GLU   A 1 156 ? 5.27262   18.38831 23.97579 1.000 65.13779  ? 163 GLU   A CD  1 
ATOM   1154 O  OE1 . GLU   A 1 156 ? 6.05591   17.55833 23.46661 1.000 67.00768  ? 163 GLU   A OE1 1 
ATOM   1155 O  OE2 . GLU   A 1 156 ? 4.04898   18.17076 24.11324 1.000 57.65159  ? 163 GLU   A OE2 1 
ATOM   1156 N  N   . SER   A 1 157 ? 7.98957   22.07543 25.64851 1.000 29.28616  ? 164 SER   A N   1 
ATOM   1157 C  CA  . SER   A 1 157 ? 9.25918   22.04266 26.35950 1.000 32.22090  ? 164 SER   A CA  1 
ATOM   1158 C  C   . SER   A 1 157 ? 9.05464   21.47165 27.75424 1.000 31.49644  ? 164 SER   A C   1 
ATOM   1159 O  O   . SER   A 1 157 ? 8.11777   21.85490 28.45989 1.000 33.37948  ? 164 SER   A O   1 
ATOM   1160 C  CB  . SER   A 1 157 ? 9.88628   23.43704 26.46198 1.000 30.81179  ? 164 SER   A CB  1 
ATOM   1161 O  OG  . SER   A 1 157 ? 11.10451  23.38959 27.18484 1.000 34.42866  ? 164 SER   A OG  1 
ATOM   1162 N  N   . SER   A 1 158 ? 9.93984   20.55097 28.13893 1.000 32.29874  ? 165 SER   A N   1 
ATOM   1163 C  CA  . SER   A 1 158 ? 10.04915  20.06595 29.50895 1.000 35.86548  ? 165 SER   A CA  1 
ATOM   1164 C  C   . SER   A 1 158 ? 11.23669  20.68959 30.23137 1.000 34.98745  ? 165 SER   A C   1 
ATOM   1165 O  O   . SER   A 1 158 ? 11.81191  20.06873 31.13250 1.000 38.56119  ? 165 SER   A O   1 
ATOM   1166 C  CB  . SER   A 1 158 ? 10.16354  18.54180 29.52716 1.000 31.30530  ? 165 SER   A CB  1 
ATOM   1167 O  OG  . SER   A 1 158 ? 9.05856   17.93844 28.87936 1.000 43.77156  ? 165 SER   A OG  1 
ATOM   1168 N  N   . ALA   A 1 159 ? 11.61002  21.90463 29.84297 1.000 33.29038  ? 166 ALA   A N   1 
ATOM   1169 C  CA  . ALA   A 1 159 ? 12.83977  22.57208 30.28745 1.000 35.96430  ? 166 ALA   A CA  1 
ATOM   1170 C  C   . ALA   A 1 159 ? 14.02424  21.70718 29.84583 1.000 35.57168  ? 166 ALA   A C   1 
ATOM   1171 O  O   . ALA   A 1 159 ? 13.94436  20.98761 28.84128 1.000 38.95518  ? 166 ALA   A O   1 
ATOM   1172 C  CB  . ALA   A 1 159 ? 12.78106  22.86622 31.77721 1.000 28.82631  ? 166 ALA   A CB  1 
ATOM   1173 N  N   . GLY   A 1 160 ? 15.13294  21.76829 30.57691 1.000 36.41374  ? 167 GLY   A N   1 
ATOM   1174 C  CA  . GLY   A 1 160 ? 16.31346  21.02021 30.20833 1.000 33.24793  ? 167 GLY   A CA  1 
ATOM   1175 C  C   . GLY   A 1 160 ? 17.15577  21.64428 29.11859 1.000 32.24732  ? 167 GLY   A C   1 
ATOM   1176 O  O   . GLY   A 1 160 ? 18.17266  21.05403 28.73237 1.000 36.79163  ? 167 GLY   A O   1 
ATOM   1177 N  N   . GLY   A 1 161 ? 16.76666  22.80685 28.60051 1.000 36.19737  ? 168 GLY   A N   1 
ATOM   1178 C  CA  . GLY   A 1 161 ? 17.57367  23.54435 27.64983 1.000 34.23911  ? 168 GLY   A CA  1 
ATOM   1179 C  C   . GLY   A 1 161 ? 17.03976  23.58213 26.23432 1.000 35.77361  ? 168 GLY   A C   1 
ATOM   1180 O  O   . GLY   A 1 161 ? 17.61320  24.29538 25.40046 1.000 32.56876  ? 168 GLY   A O   1 
ATOM   1181 N  N   . SER   A 1 162 ? 15.96660  22.85588 25.92643 1.000 33.75753  ? 169 SER   A N   1 
ATOM   1182 C  CA  . SER   A 1 162 ? 15.49068  22.76571 24.55408 1.000 38.58258  ? 169 SER   A CA  1 
ATOM   1183 C  C   . SER   A 1 162 ? 13.96869  22.75449 24.51488 1.000 33.67500  ? 169 SER   A C   1 
ATOM   1184 O  O   . SER   A 1 162 ? 13.29647  22.47846 25.51184 1.000 27.15600  ? 169 SER   A O   1 
ATOM   1185 C  CB  . SER   A 1 162 ? 16.03585  21.51396 23.84968 1.000 32.34252  ? 169 SER   A CB  1 
ATOM   1186 O  OG  . SER   A 1 162 ? 15.53950  20.33240 24.45366 1.000 34.83096  ? 169 SER   A OG  1 
ATOM   1187 N  N   . PHE   A 1 163 ? 13.43711  23.05960 23.33213 1.000 26.98867  ? 170 PHE   A N   1 
ATOM   1188 C  CA  . PHE   A 1 163 ? 12.01229  22.97279 23.05237 1.000 26.20493  ? 170 PHE   A CA  1 
ATOM   1189 C  C   . PHE   A 1 163 ? 11.82410  22.49057 21.62158 1.000 31.93714  ? 170 PHE   A C   1 
ATOM   1190 O  O   . PHE   A 1 163 ? 12.73617  22.56976 20.79526 1.000 33.23237  ? 170 PHE   A O   1 
ATOM   1191 C  CB  . PHE   A 1 163 ? 11.30089  24.31818 23.25847 1.000 29.53248  ? 170 PHE   A CB  1 
ATOM   1192 C  CG  . PHE   A 1 163 ? 11.83223  25.43171 22.39630 1.000 32.52367  ? 170 PHE   A CG  1 
ATOM   1193 C  CD1 . PHE   A 1 163 ? 12.86950  26.23437 22.84241 1.000 30.29266  ? 170 PHE   A CD1 1 
ATOM   1194 C  CD2 . PHE   A 1 163 ? 11.28964  25.68267 21.14503 1.000 24.41819  ? 170 PHE   A CD2 1 
ATOM   1195 C  CE1 . PHE   A 1 163 ? 13.35787  27.26366 22.05686 1.000 32.58481  ? 170 PHE   A CE1 1 
ATOM   1196 C  CE2 . PHE   A 1 163 ? 11.77239  26.71044 20.35665 1.000 26.49856  ? 170 PHE   A CE2 1 
ATOM   1197 C  CZ  . PHE   A 1 163 ? 12.80581  27.50356 20.81438 1.000 26.64580  ? 170 PHE   A CZ  1 
ATOM   1198 N  N   . THR   A 1 164 ? 10.62434  21.99185 21.33269 1.000 29.06368  ? 171 THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 164 ? 10.28861  21.48740 20.01008 1.000 28.90483  ? 171 THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 164 ? 9.10892   22.25631 19.43139 1.000 28.53715  ? 171 THR   A C   1 
ATOM   1201 O  O   . THR   A 1 164 ? 8.23345   22.73061 20.16175 1.000 30.31188  ? 171 THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 164 ? 9.95146   19.98989 20.04149 1.000 33.46759  ? 171 THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 164 ? 8.76969   19.77756 20.82427 1.000 36.29287  ? 171 THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 164 ? 11.10588  19.19128 20.63243 1.000 28.57190  ? 171 THR   A CG2 1 
ATOM   1205 N  N   . VAL   A 1 165 ? 9.09969   22.37454 18.10546 1.000 27.55719  ? 172 VAL   A N   1 
ATOM   1206 C  CA  . VAL   A 1 165 ? 8.01286   23.00069 17.36288 1.000 31.05438  ? 172 VAL   A CA  1 
ATOM   1207 C  C   . VAL   A 1 165 ? 7.64029   22.07868 16.21122 1.000 32.35775  ? 172 VAL   A C   1 
ATOM   1208 O  O   . VAL   A 1 165 ? 8.51923   21.59400 15.48998 1.000 30.51155  ? 172 VAL   A O   1 
ATOM   1209 C  CB  . VAL   A 1 165 ? 8.40077   24.39677 16.83563 1.000 26.81618  ? 172 VAL   A CB  1 
ATOM   1210 C  CG1 . VAL   A 1 165 ? 7.31866   24.93857 15.91452 1.000 26.79438  ? 172 VAL   A CG1 1 
ATOM   1211 C  CG2 . VAL   A 1 165 ? 8.64182   25.35661 17.98934 1.000 25.02772  ? 172 VAL   A CG2 1 
ATOM   1212 N  N   . ARG   A 1 166 ? 6.34393   21.82875 16.04554 1.000 32.69144  ? 173 ARG   A N   1 
ATOM   1213 C  CA  . ARG   A 1 166 ? 5.86828   20.99654 14.95216 1.000 36.89591  ? 173 ARG   A CA  1 
ATOM   1214 C  C   . ARG   A 1 166 ? 4.51350   21.51088 14.49324 1.000 38.22104  ? 173 ARG   A C   1 
ATOM   1215 O  O   . ARG   A 1 166 ? 3.78335   22.15637 15.25009 1.000 30.06566  ? 173 ARG   A O   1 
ATOM   1216 C  CB  . ARG   A 1 166 ? 5.76401   19.52224 15.36380 1.000 37.20463  ? 173 ARG   A CB  1 
ATOM   1217 C  CG  . ARG   A 1 166 ? 4.66249   19.23930 16.37657 1.000 44.09936  ? 173 ARG   A CG  1 
ATOM   1218 C  CD  . ARG   A 1 166 ? 4.85295   17.88920 17.04839 1.000 41.56390  ? 173 ARG   A CD  1 
ATOM   1219 N  NE  . ARG   A 1 166 ? 5.90248   17.92107 18.06021 1.000 50.04919  ? 173 ARG   A NE  1 
ATOM   1220 C  CZ  . ARG   A 1 166 ? 6.33791   16.85754 18.72259 1.000 55.88090  ? 173 ARG   A CZ  1 
ATOM   1221 N  NH1 . ARG   A 1 166 ? 5.83963   15.65203 18.50001 1.000 38.37295  ? 173 ARG   A NH1 1 
ATOM   1222 N  NH2 . ARG   A 1 166 ? 7.29913   17.00671 19.62971 1.000 46.47237  ? 173 ARG   A NH2 1 
ATOM   1223 N  N   . THR   A 1 167 ? 4.18861   21.22233 13.23579 1.000 33.88310  ? 174 THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 167 ? 2.85186   21.50106 12.73164 1.000 36.26592  ? 174 THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 167 ? 1.84486   20.61376 13.45281 1.000 38.12761  ? 174 THR   A C   1 
ATOM   1226 O  O   . THR   A 1 167 ? 2.02973   19.39618 13.54580 1.000 47.38262  ? 174 THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 167 ? 2.79018   21.26697 11.22225 1.000 45.46042  ? 174 THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 167 ? 3.68778   22.16806 10.56197 1.000 52.12945  ? 174 THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 167 ? 1.37951   21.49950 10.69854 1.000 47.69407  ? 174 THR   A CG2 1 
ATOM   1230 N  N   . ASP   A 1 168 ? 0.78423   21.22364 13.97440 1.000 39.69398  ? 175 ASP   A N   1 
ATOM   1231 C  CA  . ASP   A 1 168 ? -0.19285  20.50507 14.78023 1.000 49.07590  ? 175 ASP   A CA  1 
ATOM   1232 C  C   . ASP   A 1 168 ? -1.22338  19.82933 13.88546 1.000 49.90320  ? 175 ASP   A C   1 
ATOM   1233 O  O   . ASP   A 1 168 ? -1.82812  20.47419 13.02264 1.000 47.17759  ? 175 ASP   A O   1 
ATOM   1234 C  CB  . ASP   A 1 168 ? -0.88587  21.44725 15.76403 1.000 40.34013  ? 175 ASP   A CB  1 
ATOM   1235 C  CG  . ASP   A 1 168 ? -1.82094  20.71495 16.70684 1.000 50.71370  ? 175 ASP   A CG  1 
ATOM   1236 O  OD1 . ASP   A 1 168 ? -1.39523  19.70148 17.30053 1.000 61.91139  ? 175 ASP   A OD1 1 
ATOM   1237 O  OD2 . ASP   A 1 168 ? -2.98117  21.15219 16.85561 1.000 52.35220  ? 175 ASP   A OD2 1 
ATOM   1238 N  N   . THR   A 1 169 ? -1.41791  18.52975 14.09794 1.000 59.38205  ? 176 THR   A N   1 
ATOM   1239 C  CA  . THR   A 1 169 ? -2.40369  17.74703 13.36655 1.000 71.08616  ? 176 THR   A CA  1 
ATOM   1240 C  C   . THR   A 1 169 ? -3.65992  17.47516 14.18251 1.000 70.11061  ? 176 THR   A C   1 
ATOM   1241 O  O   . THR   A 1 169 ? -4.53277  16.73042 13.72581 1.000 67.36611  ? 176 THR   A O   1 
ATOM   1242 C  CB  . THR   A 1 169 ? -1.79456  16.41675 12.91224 1.000 68.83525  ? 176 THR   A CB  1 
ATOM   1243 O  OG1 . THR   A 1 169 ? -1.26257  15.72034 14.04633 1.000 67.68904  ? 176 THR   A OG1 1 
ATOM   1244 C  CG2 . THR   A 1 169 ? -0.68075  16.65470 11.90155 1.000 63.17258  ? 176 THR   A CG2 1 
ATOM   1245 N  N   . GLY   A 1 170 ? -3.77314  18.05617 15.37247 1.000 65.81112  ? 177 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 170 ? -4.91945  17.83900 16.23123 1.000 56.63743  ? 177 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 170 ? -6.12475  18.65673 15.81130 1.000 58.86069  ? 177 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 170 ? -6.28438  19.02579 14.64547 1.000 55.19518  ? 177 GLY   A O   1 
ATOM   1249 N  N   . GLU   A 1 171 ? -6.98146  18.94782 16.78826 1.000 65.06514  ? 178 GLU   A N   1 
ATOM   1250 C  CA  . GLU   A 1 171 ? -8.20410  19.69110 16.53030 1.000 61.86940  ? 178 GLU   A CA  1 
ATOM   1251 C  C   . GLU   A 1 171 ? -7.88132  21.11027 16.07475 1.000 56.12847  ? 178 GLU   A C   1 
ATOM   1252 O  O   . GLU   A 1 171 ? -7.14440  21.82975 16.76614 1.000 42.47225  ? 178 GLU   A O   1 
ATOM   1253 C  CB  . GLU   A 1 171 ? -9.06073  19.73535 17.78988 1.000 64.76563  ? 178 GLU   A CB  1 
ATOM   1254 C  CG  . GLU   A 1 171 ? -10.47872 20.22075 17.55856 1.000 73.14436  ? 178 GLU   A CG  1 
ATOM   1255 C  CD  . GLU   A 1 171 ? -11.51701 19.39559 18.28141 1.000 96.55512  ? 178 GLU   A CD  1 
ATOM   1256 O  OE1 . GLU   A 1 171 ? -11.41184 19.26062 19.51256 1.000 101.14553 ? 178 GLU   A OE1 1 
ATOM   1257 O  OE2 . GLU   A 1 171 ? -12.44069 18.88135 17.61779 1.000 99.88277  ? 178 GLU   A OE2 1 
ATOM   1258 N  N   . PRO   A 1 172 ? -8.39664  21.54837 14.92645 1.000 51.94481  ? 179 PRO   A N   1 
ATOM   1259 C  CA  . PRO   A 1 172 ? -8.25424  22.95813 14.54853 1.000 51.97274  ? 179 PRO   A CA  1 
ATOM   1260 C  C   . PRO   A 1 172 ? -8.87333  23.86294 15.60340 1.000 48.85867  ? 179 PRO   A C   1 
ATOM   1261 O  O   . PRO   A 1 172 ? -9.86001  23.51023 16.25029 1.000 59.27196  ? 179 PRO   A O   1 
ATOM   1262 C  CB  . PRO   A 1 172 ? -9.00885  23.05281 13.21325 1.000 44.17144  ? 179 PRO   A CB  1 
ATOM   1263 C  CG  . PRO   A 1 172 ? -9.06252  21.67917 12.68355 1.000 47.50145  ? 179 PRO   A CG  1 
ATOM   1264 C  CD  . PRO   A 1 172 ? -8.88976  20.71488 13.81699 1.000 49.84492  ? 179 PRO   A CD  1 
ATOM   1265 N  N   . MET   A 1 173 ? -8.28319  25.04591 15.76658 1.000 46.29477  ? 180 MET   A N   1 
ATOM   1266 C  CA  . MET   A 1 173 ? -8.64477  25.95423 16.84186 1.000 52.87454  ? 180 MET   A CA  1 
ATOM   1267 C  C   . MET   A 1 173 ? -9.32271  27.23056 16.36848 1.000 46.70383  ? 180 MET   A C   1 
ATOM   1268 O  O   . MET   A 1 173 ? -9.85230  27.97091 17.20428 1.000 58.97766  ? 180 MET   A O   1 
ATOM   1269 C  CB  . MET   A 1 173 ? -7.39426  26.32933 17.64992 1.000 45.41614  ? 180 MET   A CB  1 
ATOM   1270 C  CG  . MET   A 1 173 ? -7.28737  25.65768 19.01404 1.000 52.05162  ? 180 MET   A CG  1 
ATOM   1271 S  SD  . MET   A 1 173 ? -5.98984  26.40837 20.01527 1.000 59.05107  ? 180 MET   A SD  1 
ATOM   1272 C  CE  . MET   A 1 173 ? -4.68629  26.52967 18.80007 1.000 31.59999  ? 180 MET   A CE  1 
ATOM   1273 N  N   . GLY   A 1 174 ? -9.32167  27.51166 15.06802 1.000 39.97305  ? 181 GLY   A N   1 
ATOM   1274 C  CA  . GLY   A 1 174 ? -9.87041  28.75825 14.57073 1.000 46.57921  ? 181 GLY   A CA  1 
ATOM   1275 C  C   . GLY   A 1 174 ? -8.91072  29.91841 14.73974 1.000 38.07752  ? 181 GLY   A C   1 
ATOM   1276 O  O   . GLY   A 1 174 ? -8.41369  30.47108 13.75300 1.000 40.55397  ? 181 GLY   A O   1 
ATOM   1277 N  N   . ARG   A 1 175 ? -8.64258  30.28932 15.99150 1.000 31.57462  ? 182 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 175 ? -7.69790  31.34553 16.32970 1.000 29.34033  ? 182 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 175 ? -7.50865  31.36346 17.83843 1.000 29.17716  ? 182 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 175 ? -8.47161  31.18147 18.58589 1.000 35.11265  ? 182 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 175 ? -8.18772  32.71866 15.85081 1.000 29.58933  ? 182 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 175 ? -7.11845  33.79669 15.89379 1.000 27.91036  ? 182 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 175 ? -7.72203  35.19115 15.88559 1.000 28.24225  ? 182 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 175 ? -8.64675  35.39704 16.99412 1.000 32.09991  ? 182 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 175 ? -9.96240  35.50026 16.86418 1.000 32.52531  ? 182 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 175 ? -10.54935 35.41183 15.68157 1.000 31.85532  ? 182 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 175 ? -10.70731 35.70054 17.94759 1.000 30.80027  ? 182 ARG   A NH2 1 
ATOM   1288 N  N   . GLY   A 1 176 ? -6.26912  31.57988 18.27984 1.000 26.29607  ? 183 GLY   A N   1 
ATOM   1289 C  CA  . GLY   A 1 176 ? -5.99503  31.73765 19.68952 1.000 25.29033  ? 183 GLY   A CA  1 
ATOM   1290 C  C   . GLY   A 1 176 ? -4.82391  30.88622 20.12841 1.000 26.89688  ? 183 GLY   A C   1 
ATOM   1291 O  O   . GLY   A 1 176 ? -4.03634  30.40137 19.30797 1.000 28.25817  ? 183 GLY   A O   1 
ATOM   1292 N  N   . THR   A 1 177 ? -4.71893  30.70560 21.44491 1.000 28.23812  ? 184 THR   A N   1 
ATOM   1293 C  CA  . THR   A 1 177 ? -3.60577  30.00301 22.06562 1.000 26.58690  ? 184 THR   A CA  1 
ATOM   1294 C  C   . THR   A 1 177 ? -4.13318  29.06682 23.14306 1.000 28.64050  ? 184 THR   A C   1 
ATOM   1295 O  O   . THR   A 1 177 ? -5.01932  29.43643 23.91869 1.000 26.73378  ? 184 THR   A O   1 
ATOM   1296 C  CB  . THR   A 1 177 ? -2.59787  30.98971 22.67711 1.000 31.07457  ? 184 THR   A CB  1 
ATOM   1297 O  OG1 . THR   A 1 177 ? -2.03338  31.80311 21.64097 1.000 28.38212  ? 184 THR   A OG1 1 
ATOM   1298 C  CG2 . THR   A 1 177 ? -1.47766  30.24697 23.39736 1.000 30.19818  ? 184 THR   A CG2 1 
ATOM   1299 N  N   . LYS   A 1 178 ? -3.58306  27.85536 23.18437 1.000 25.17692  ? 185 LYS   A N   1 
ATOM   1300 C  CA  . LYS   A 1 178 ? -3.93413  26.85024 24.17980 1.000 24.52891  ? 185 LYS   A CA  1 
ATOM   1301 C  C   . LYS   A 1 178 ? -2.66814  26.43551 24.91507 1.000 28.64632  ? 185 LYS   A C   1 
ATOM   1302 O  O   . LYS   A 1 178 ? -1.72026  25.94220 24.29466 1.000 30.54116  ? 185 LYS   A O   1 
ATOM   1303 C  CB  . LYS   A 1 178 ? -4.60419  25.64255 23.52032 1.000 26.24963  ? 185 LYS   A CB  1 
ATOM   1304 C  CG  . LYS   A 1 178 ? -4.51743  24.35118 24.31980 1.000 42.26520  ? 185 LYS   A CG  1 
ATOM   1305 C  CD  . LYS   A 1 178 ? -5.67717  23.41342 23.99618 1.000 34.98303  ? 185 LYS   A CD  1 
ATOM   1306 C  CE  . LYS   A 1 178 ? -6.02916  23.44784 22.51801 1.000 39.69127  ? 185 LYS   A CE  1 
ATOM   1307 N  NZ  . LYS   A 1 178 ? -6.63595  22.16645 22.06380 1.000 54.22558  ? 185 LYS   A NZ  1 
ATOM   1308 N  N   . VAL   A 1 179 ? -2.65027  26.63935 26.22803 1.000 25.24543  ? 186 VAL   A N   1 
ATOM   1309 C  CA  . VAL   A 1 179 ? -1.50475  26.30351 27.06551 1.000 23.81745  ? 186 VAL   A CA  1 
ATOM   1310 C  C   . VAL   A 1 179 ? -1.89106  25.10191 27.91746 1.000 26.43321  ? 186 VAL   A C   1 
ATOM   1311 O  O   . VAL   A 1 179 ? -2.78355  25.19256 28.76933 1.000 27.21215  ? 186 VAL   A O   1 
ATOM   1312 C  CB  . VAL   A 1 179 ? -1.06554  27.49009 27.93251 1.000 22.36645  ? 186 VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A 1 179 ? 0.13457   27.10658 28.78738 1.000 21.98393  ? 186 VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A 1 179 ? -0.73661  28.68602 27.05107 1.000 21.81481  ? 186 VAL   A CG2 1 
ATOM   1315 N  N   . ILE   A 1 180 ? -1.22315  23.97433 27.68822 1.000 24.15466  ? 187 ILE   A N   1 
ATOM   1316 C  CA  . ILE   A 1 180 ? -1.49653  22.72835 28.39514 1.000 26.89973  ? 187 ILE   A CA  1 
ATOM   1317 C  C   . ILE   A 1 180 ? -0.37964  22.50833 29.40493 1.000 29.37989  ? 187 ILE   A C   1 
ATOM   1318 O  O   . ILE   A 1 180 ? 0.78974   22.36313 29.02716 1.000 31.13236  ? 187 ILE   A O   1 
ATOM   1319 C  CB  . ILE   A 1 180 ? -1.61318  21.54167 27.42647 1.000 31.46239  ? 187 ILE   A CB  1 
ATOM   1320 C  CG1 . ILE   A 1 180 ? -2.57204  21.88411 26.28330 1.000 32.40604  ? 187 ILE   A CG1 1 
ATOM   1321 C  CG2 . ILE   A 1 180 ? -2.08083  20.29144 28.16261 1.000 28.54549  ? 187 ILE   A CG2 1 
ATOM   1322 C  CD1 . ILE   A 1 180 ? -2.60464  20.84834 25.18086 1.000 40.82536  ? 187 ILE   A CD1 1 
ATOM   1323 N  N   . LEU   A 1 181 ? -0.73786  22.48433 30.68677 1.000 27.36853  ? 188 LEU   A N   1 
ATOM   1324 C  CA  . LEU   A 1 181 ? 0.22274   22.31578 31.77171 1.000 26.26185  ? 188 LEU   A CA  1 
ATOM   1325 C  C   . LEU   A 1 181 ? 0.15899   20.87631 32.26871 1.000 27.13936  ? 188 LEU   A C   1 
ATOM   1326 O  O   . LEU   A 1 181 ? -0.82672  20.47239 32.89348 1.000 28.74049  ? 188 LEU   A O   1 
ATOM   1327 C  CB  . LEU   A 1 181 ? -0.05909  23.29538 32.90966 1.000 26.81696  ? 188 LEU   A CB  1 
ATOM   1328 C  CG  . LEU   A 1 181 ? -0.31917  24.76050 32.55798 1.000 29.51923  ? 188 LEU   A CG  1 
ATOM   1329 C  CD1 . LEU   A 1 181 ? -0.82922  25.50280 33.77866 1.000 34.77590  ? 188 LEU   A CD1 1 
ATOM   1330 C  CD2 . LEU   A 1 181 ? 0.93892   25.41916 32.01812 1.000 25.44637  ? 188 LEU   A CD2 1 
ATOM   1331 N  N   . HIS   A 1 182 ? 1.20740   20.10532 31.98890 1.000 26.86342  ? 189 HIS   A N   1 
ATOM   1332 C  CA  . HIS   A 1 182 ? 1.34807   18.75933 32.54032 1.000 28.33835  ? 189 HIS   A CA  1 
ATOM   1333 C  C   . HIS   A 1 182 ? 1.90328   18.90229 33.95155 1.000 28.60589  ? 189 HIS   A C   1 
ATOM   1334 O  O   . HIS   A 1 182 ? 3.10748   19.08251 34.14665 1.000 33.10163  ? 189 HIS   A O   1 
ATOM   1335 C  CB  . HIS   A 1 182 ? 2.24473   17.90362 31.65310 1.000 28.22258  ? 189 HIS   A CB  1 
ATOM   1336 C  CG  . HIS   A 1 182 ? 1.86036   17.93359 30.20619 1.000 33.24767  ? 189 HIS   A CG  1 
ATOM   1337 N  ND1 . HIS   A 1 182 ? 1.13189   16.92804 29.60841 1.000 31.03147  ? 189 HIS   A ND1 1 
ATOM   1338 C  CD2 . HIS   A 1 182 ? 2.09685   18.85202 29.23923 1.000 31.83940  ? 189 HIS   A CD2 1 
ATOM   1339 C  CE1 . HIS   A 1 182 ? 0.93791   17.22424 28.33555 1.000 37.33165  ? 189 HIS   A CE1 1 
ATOM   1340 N  NE2 . HIS   A 1 182 ? 1.51313   18.38686 28.08607 1.000 34.29494  ? 189 HIS   A NE2 1 
ATOM   1341 N  N   . LEU   A 1 183 ? 1.01616   18.82608 34.93958 1.000 30.05398  ? 190 LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 183 ? 1.35568   19.20754 36.30235 1.000 30.59450  ? 190 LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 183 ? 2.31752   18.21450 36.94397 1.000 37.27273  ? 190 LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 183 ? 2.34608   17.02794 36.60545 1.000 40.52899  ? 190 LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 183 ? 0.08957   19.31100 37.15205 1.000 32.40431  ? 190 LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 183 ? -0.92809  20.37726 36.74330 1.000 32.07794  ? 190 LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 183 ? -2.01455  20.51329 37.79731 1.000 34.27449  ? 190 LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 183 ? -0.24415  21.71573 36.49597 1.000 30.97293  ? 190 LEU   A CD2 1 
ATOM   1349 N  N   . LYS   A 1 184 ? 3.11180   18.71971 37.88467 1.000 32.83931  ? 191 LYS   A N   1 
ATOM   1350 C  CA  . LYS   A 1 184 ? 3.92029   17.85705 38.72859 1.000 37.35533  ? 191 LYS   A CA  1 
ATOM   1351 C  C   . LYS   A 1 184 ? 3.01922   17.02088 39.63357 1.000 37.75010  ? 191 LYS   A C   1 
ATOM   1352 O  O   . LYS   A 1 184 ? 1.86189   17.36440 39.89135 1.000 39.86181  ? 191 LYS   A O   1 
ATOM   1353 C  CB  . LYS   A 1 184 ? 4.89459   18.68481 39.56866 1.000 34.26303  ? 191 LYS   A CB  1 
ATOM   1354 C  CG  . LYS   A 1 184 ? 5.95943   19.41468 38.75888 1.000 38.97629  ? 191 LYS   A CG  1 
ATOM   1355 C  CD  . LYS   A 1 184 ? 6.70923   20.43045 39.61154 1.000 34.95100  ? 191 LYS   A CD  1 
ATOM   1356 C  CE  . LYS   A 1 184 ? 7.36118   21.51094 38.75798 1.000 44.15525  ? 191 LYS   A CE  1 
ATOM   1357 N  NZ  . LYS   A 1 184 ? 8.10039   22.49602 39.59661 1.000 41.32518  ? 191 LYS   A NZ  1 
ATOM   1358 N  N   . GLU   A 1 185 ? 3.57078   15.90684 40.12166 1.000 41.93285  ? 192 GLU   A N   1 
ATOM   1359 C  CA  . GLU   A 1 185 ? 2.77877   14.97277 40.91759 1.000 46.83998  ? 192 GLU   A CA  1 
ATOM   1360 C  C   . GLU   A 1 185 ? 2.22671   15.63325 42.17609 1.000 46.72146  ? 192 GLU   A C   1 
ATOM   1361 O  O   . GLU   A 1 185 ? 1.08609   15.36942 42.57506 1.000 49.73474  ? 192 GLU   A O   1 
ATOM   1362 C  CB  . GLU   A 1 185 ? 3.62217   13.74964 41.27901 1.000 45.09593  ? 192 GLU   A CB  1 
ATOM   1363 C  CG  . GLU   A 1 185 ? 2.98604   12.83831 42.31889 1.000 60.32288  ? 192 GLU   A CG  1 
ATOM   1364 C  CD  . GLU   A 1 185 ? 2.90194   11.39399 41.86295 1.000 76.88736  ? 192 GLU   A CD  1 
ATOM   1365 O  OE1 . GLU   A 1 185 ? 1.80400   10.80567 41.95551 1.000 76.47617  ? 192 GLU   A OE1 1 
ATOM   1366 O  OE2 . GLU   A 1 185 ? 3.93174   10.84548 41.41596 1.000 84.80423  ? 192 GLU   A OE2 1 
ATOM   1367 N  N   . ASP   A 1 186 ? 3.01118   16.50361 42.80593 1.000 41.77331  ? 193 ASP   A N   1 
ATOM   1368 C  CA  . ASP   A 1 186 ? 2.62729   17.13113 44.06266 1.000 48.94488  ? 193 ASP   A CA  1 
ATOM   1369 C  C   . ASP   A 1 186 ? 1.85061   18.42911 43.87311 1.000 43.84764  ? 193 ASP   A C   1 
ATOM   1370 O  O   . ASP   A 1 186 ? 1.65457   19.16364 44.84669 1.000 43.54669  ? 193 ASP   A O   1 
ATOM   1371 C  CB  . ASP   A 1 186 ? 3.86950   17.39530 44.91809 1.000 46.71727  ? 193 ASP   A CB  1 
ATOM   1372 C  CG  . ASP   A 1 186 ? 4.81879   18.39261 44.27835 1.000 46.72562  ? 193 ASP   A CG  1 
ATOM   1373 O  OD1 . ASP   A 1 186 ? 4.72879   18.60685 43.05054 1.000 50.01523  ? 193 ASP   A OD1 1 
ATOM   1374 O  OD2 . ASP   A 1 186 ? 5.65945   18.96174 45.00539 1.000 62.12419  ? 193 ASP   A OD2 1 
ATOM   1375 N  N   . GLN   A 1 187 ? 1.40616   18.73133 42.65284 1.000 35.12616  ? 194 GLN   A N   1 
ATOM   1376 C  CA  . GLN   A 1 187 ? 0.68233   19.96649 42.37369 1.000 33.42031  ? 194 GLN   A CA  1 
ATOM   1377 C  C   . GLN   A 1 187 ? -0.70665  19.69248 41.80469 1.000 33.93061  ? 194 GLN   A C   1 
ATOM   1378 O  O   . GLN   A 1 187 ? -1.21788  20.47275 40.99967 1.000 38.20139  ? 194 GLN   A O   1 
ATOM   1379 C  CB  . GLN   A 1 187 ? 1.47966   20.86164 41.42414 1.000 33.47124  ? 194 GLN   A CB  1 
ATOM   1380 C  CG  . GLN   A 1 187 ? 2.89480   21.17422 41.89142 1.000 34.38873  ? 194 GLN   A CG  1 
ATOM   1381 C  CD  . GLN   A 1 187 ? 2.92746   21.97578 43.17975 1.000 35.40766  ? 194 GLN   A CD  1 
ATOM   1382 O  OE1 . GLN   A 1 187 ? 2.00599   22.73651 43.47839 1.000 44.39575  ? 194 GLN   A OE1 1 
ATOM   1383 N  NE2 . GLN   A 1 187 ? 3.99352   21.80549 43.95276 1.000 34.72623  ? 194 GLN   A NE2 1 
ATOM   1384 N  N   . THR   A 1 188 ? -1.33403  18.58999 42.22058 1.000 33.55988  ? 195 THR   A N   1 
ATOM   1385 C  CA  . THR   A 1 188 ? -2.66216  18.24757 41.72369 1.000 38.96507  ? 195 THR   A CA  1 
ATOM   1386 C  C   . THR   A 1 188 ? -3.75791  19.13499 42.29854 1.000 34.23073  ? 195 THR   A C   1 
ATOM   1387 O  O   . THR   A 1 188 ? -4.90289  19.04408 41.84227 1.000 34.76489  ? 195 THR   A O   1 
ATOM   1388 C  CB  . THR   A 1 188 ? -2.98507  16.78414 42.03422 1.000 36.11927  ? 195 THR   A CB  1 
ATOM   1389 O  OG1 . THR   A 1 188 ? -2.94549  16.57613 43.45113 1.000 37.25902  ? 195 THR   A OG1 1 
ATOM   1390 C  CG2 . THR   A 1 188 ? -1.97362  15.86549 41.37238 1.000 42.13865  ? 195 THR   A CG2 1 
ATOM   1391 N  N   . GLU   A 1 189 ? -3.43992  19.98234 43.28130 1.000 29.53885  ? 196 GLU   A N   1 
ATOM   1392 C  CA  . GLU   A 1 189 ? -4.45103  20.83821 43.89242 1.000 37.13142  ? 196 GLU   A CA  1 
ATOM   1393 C  C   . GLU   A 1 189 ? -5.03085  21.84652 42.90966 1.000 32.11619  ? 196 GLU   A C   1 
ATOM   1394 O  O   . GLU   A 1 189 ? -6.15327  22.32111 43.11546 1.000 33.81398  ? 196 GLU   A O   1 
ATOM   1395 C  CB  . GLU   A 1 189 ? -3.85946  21.56891 45.10026 1.000 32.52045  ? 196 GLU   A CB  1 
ATOM   1396 C  CG  . GLU   A 1 189 ? -2.99649  22.77077 44.74173 1.000 37.49557  ? 196 GLU   A CG  1 
ATOM   1397 C  CD  . GLU   A 1 189 ? -2.25532  23.33911 45.93646 1.000 43.83106  ? 196 GLU   A CD  1 
ATOM   1398 O  OE1 . GLU   A 1 189 ? -1.13857  22.86175 46.22914 1.000 50.50332  ? 196 GLU   A OE1 1 
ATOM   1399 O  OE2 . GLU   A 1 189 ? -2.78898  24.26649 46.58128 1.000 45.29284  ? 196 GLU   A OE2 1 
ATOM   1400 N  N   . TYR   A 1 190 ? -4.29966  22.17959 41.84947 1.000 30.37640  ? 197 TYR   A N   1 
ATOM   1401 C  CA  . TYR   A 1 190 ? -4.76243  23.13303 40.85128 1.000 30.71751  ? 197 TYR   A CA  1 
ATOM   1402 C  C   . TYR   A 1 190 ? -5.66333  22.49439 39.80487 1.000 33.14465  ? 197 TYR   A C   1 
ATOM   1403 O  O   . TYR   A 1 190 ? -5.98131  23.13657 38.79797 1.000 31.15820  ? 197 TYR   A O   1 
ATOM   1404 C  CB  . TYR   A 1 190 ? -3.55909  23.81363 40.19661 1.000 25.97972  ? 197 TYR   A CB  1 
ATOM   1405 C  CG  . TYR   A 1 190 ? -2.68070  24.49866 41.21540 1.000 24.75244  ? 197 TYR   A CG  1 
ATOM   1406 C  CD1 . TYR   A 1 190 ? -3.11526  25.64200 41.86998 1.000 26.33618  ? 197 TYR   A CD1 1 
ATOM   1407 C  CD2 . TYR   A 1 190 ? -1.43373  23.98568 41.54914 1.000 24.00342  ? 197 TYR   A CD2 1 
ATOM   1408 C  CE1 . TYR   A 1 190 ? -2.32661  26.26837 42.81464 1.000 29.15668  ? 197 TYR   A CE1 1 
ATOM   1409 C  CE2 . TYR   A 1 190 ? -0.63717  24.60548 42.49421 1.000 31.28834  ? 197 TYR   A CE2 1 
ATOM   1410 C  CZ  . TYR   A 1 190 ? -1.09017  25.74724 43.12318 1.000 31.38750  ? 197 TYR   A CZ  1 
ATOM   1411 O  OH  . TYR   A 1 190 ? -0.30708  26.37303 44.06512 1.000 33.22416  ? 197 TYR   A OH  1 
ATOM   1412 N  N   . LEU   A 1 191 ? -6.07521  21.24731 40.02621 1.000 33.36447  ? 198 LEU   A N   1 
ATOM   1413 C  CA  . LEU   A 1 191 ? -7.13079  20.61575 39.25140 1.000 34.11446  ? 198 LEU   A CA  1 
ATOM   1414 C  C   . LEU   A 1 191 ? -8.46966  20.62578 39.97497 1.000 41.34031  ? 198 LEU   A C   1 
ATOM   1415 O  O   . LEU   A 1 191 ? -9.47546  20.21012 39.39031 1.000 39.32762  ? 198 LEU   A O   1 
ATOM   1416 C  CB  . LEU   A 1 191 ? -6.75107  19.16898 38.90916 1.000 37.39700  ? 198 LEU   A CB  1 
ATOM   1417 C  CG  . LEU   A 1 191 ? -5.41773  18.94721 38.19469 1.000 40.45422  ? 198 LEU   A CG  1 
ATOM   1418 C  CD1 . LEU   A 1 191 ? -5.07959  17.46132 38.13743 1.000 35.54700  ? 198 LEU   A CD1 1 
ATOM   1419 C  CD2 . LEU   A 1 191 ? -5.45771  19.55100 36.80146 1.000 33.15449  ? 198 LEU   A CD2 1 
ATOM   1420 N  N   . GLU   A 1 192 ? -8.50402  21.07856 41.22639 1.000 38.81967  ? 199 GLU   A N   1 
ATOM   1421 C  CA  . GLU   A 1 192 ? -9.73553  21.13216 41.99996 1.000 40.93453  ? 199 GLU   A CA  1 
ATOM   1422 C  C   . GLU   A 1 192 ? -10.49855 22.41129 41.68538 1.000 37.29390  ? 199 GLU   A C   1 
ATOM   1423 O  O   . GLU   A 1 192 ? -9.90499  23.48293 41.53393 1.000 35.15484  ? 199 GLU   A O   1 
ATOM   1424 C  CB  . GLU   A 1 192 ? -9.43875  21.04881 43.49819 1.000 44.89890  ? 199 GLU   A CB  1 
ATOM   1425 C  CG  . GLU   A 1 192 ? -8.85454  19.71376 43.93778 1.000 61.04739  ? 199 GLU   A CG  1 
ATOM   1426 C  CD  . GLU   A 1 192 ? -8.09914  19.80200 45.25157 1.000 79.75996  ? 199 GLU   A CD  1 
ATOM   1427 O  OE1 . GLU   A 1 192 ? -7.89453  20.92792 45.75303 1.000 79.89517  ? 199 GLU   A OE1 1 
ATOM   1428 O  OE2 . GLU   A 1 192 ? -7.71130  18.74089 45.78524 1.000 75.39787  ? 199 GLU   A OE2 1 
ATOM   1429 N  N   . GLU   A 1 193 ? -11.82436 22.28776 41.59469 1.000 42.62166  ? 200 GLU   A N   1 
ATOM   1430 C  CA  . GLU   A 1 193 ? -12.65310 23.40635 41.15456 1.000 42.97113  ? 200 GLU   A CA  1 
ATOM   1431 C  C   . GLU   A 1 193 ? -12.61218 24.55950 42.15175 1.000 47.00077  ? 200 GLU   A C   1 
ATOM   1432 O  O   . GLU   A 1 193 ? -12.47961 25.72625 41.76299 1.000 35.77036  ? 200 GLU   A O   1 
ATOM   1433 C  CB  . GLU   A 1 193 ? -14.08942 22.93179 40.93612 1.000 41.30290  ? 200 GLU   A CB  1 
ATOM   1434 C  CG  . GLU   A 1 193 ? -15.05262 24.03941 40.55303 1.000 56.55003  ? 200 GLU   A CG  1 
ATOM   1435 C  CD  . GLU   A 1 193 ? -16.41279 23.51000 40.14822 1.000 62.64698  ? 200 GLU   A CD  1 
ATOM   1436 O  OE1 . GLU   A 1 193 ? -16.66904 22.30677 40.36418 1.000 64.91195  ? 200 GLU   A OE1 1 
ATOM   1437 O  OE2 . GLU   A 1 193 ? -17.22710 24.29599 39.61929 1.000 73.48239  ? 200 GLU   A OE2 1 
ATOM   1438 N  N   . ARG   A 1 194 ? -12.72826 24.25202 43.44722 1.000 36.80760  ? 201 ARG   A N   1 
ATOM   1439 C  CA  . ARG   A 1 194 ? -12.74618 25.30613 44.45705 1.000 42.72734  ? 201 ARG   A CA  1 
ATOM   1440 C  C   . ARG   A 1 194 ? -11.40882 26.03118 44.54428 1.000 35.39886  ? 201 ARG   A C   1 
ATOM   1441 O  O   . ARG   A 1 194 ? -11.37674 27.23300 44.83238 1.000 39.12610  ? 201 ARG   A O   1 
ATOM   1442 C  CB  . ARG   A 1 194 ? -13.12268 24.72617 45.82118 1.000 44.52685  ? 201 ARG   A CB  1 
ATOM   1443 C  CG  . ARG   A 1 194 ? -12.58746 23.32628 46.07304 1.000 59.89498  ? 201 ARG   A CG  1 
ATOM   1444 C  CD  . ARG   A 1 194 ? -13.11366 22.76450 47.38601 1.000 61.20378  ? 201 ARG   A CD  1 
ATOM   1445 N  NE  . ARG   A 1 194 ? -12.09346 22.01454 48.10944 1.000 77.48440  ? 201 ARG   A NE  1 
ATOM   1446 C  CZ  . ARG   A 1 194 ? -12.21651 21.59983 49.36319 1.000 78.20366  ? 201 ARG   A CZ  1 
ATOM   1447 N  NH1 . ARG   A 1 194 ? -13.30557 21.85186 50.07121 1.000 69.42397  ? 201 ARG   A NH1 1 
ATOM   1448 N  NH2 . ARG   A 1 194 ? -11.22032 20.91840 49.92213 1.000 73.83225  ? 201 ARG   A NH2 1 
ATOM   1449 N  N   . ARG   A 1 195 ? -10.30138 25.32636 44.30231 1.000 37.29058  ? 202 ARG   A N   1 
ATOM   1450 C  CA  . ARG   A 1 195 ? -8.99112  25.96737 44.35305 1.000 32.75615  ? 202 ARG   A CA  1 
ATOM   1451 C  C   . ARG   A 1 195 ? -8.80918  26.93780 43.19228 1.000 32.06433  ? 202 ARG   A C   1 
ATOM   1452 O  O   . ARG   A 1 195 ? -8.31019  28.05382 43.37742 1.000 36.38126  ? 202 ARG   A O   1 
ATOM   1453 C  CB  . ARG   A 1 195 ? -7.88698  24.91033 44.35046 1.000 31.62104  ? 202 ARG   A CB  1 
ATOM   1454 C  CG  . ARG   A 1 195 ? -6.48239  25.48250 44.43077 1.000 26.37900  ? 202 ARG   A CG  1 
ATOM   1455 C  CD  . ARG   A 1 195 ? -6.24006  26.18523 45.75946 1.000 36.78328  ? 202 ARG   A CD  1 
ATOM   1456 N  NE  . ARG   A 1 195 ? -4.82963  26.49435 45.96443 1.000 34.44128  ? 202 ARG   A NE  1 
ATOM   1457 C  CZ  . ARG   A 1 195 ? -4.35330  27.71459 46.17122 1.000 40.51590  ? 202 ARG   A CZ  1 
ATOM   1458 N  NH1 . ARG   A 1 195 ? -5.15073  28.76928 46.21735 1.000 32.23550  ? 202 ARG   A NH1 1 
ATOM   1459 N  NH2 . ARG   A 1 195 ? -3.04444  27.88077 46.33888 1.000 33.41792  ? 202 ARG   A NH2 1 
ATOM   1460 N  N   . ILE   A 1 196 ? -9.20857  26.52921 41.98488 1.000 27.60564  ? 203 ILE   A N   1 
ATOM   1461 C  CA  . ILE   A 1 196 ? -9.09494  27.41181 40.82563 1.000 30.74686  ? 203 ILE   A CA  1 
ATOM   1462 C  C   . ILE   A 1 196 ? -9.98206  28.63860 41.00051 1.000 35.69369  ? 203 ILE   A C   1 
ATOM   1463 O  O   . ILE   A 1 196 ? -9.58236  29.76475 40.67724 1.000 29.57403  ? 203 ILE   A O   1 
ATOM   1464 C  CB  . ILE   A 1 196 ? -9.43766  26.64658 39.53372 1.000 31.15847  ? 203 ILE   A CB  1 
ATOM   1465 C  CG1 . ILE   A 1 196 ? -8.49626  25.45649 39.34548 1.000 30.49480  ? 203 ILE   A CG1 1 
ATOM   1466 C  CG2 . ILE   A 1 196 ? -9.37793  27.57222 38.32937 1.000 31.10184  ? 203 ILE   A CG2 1 
ATOM   1467 C  CD1 . ILE   A 1 196 ? -8.97866  24.46190 38.30908 1.000 34.77046  ? 203 ILE   A CD1 1 
ATOM   1468 N  N   . LYS   A 1 197 ? -11.20034 28.44007 41.51209 1.000 29.75237  ? 204 LYS   A N   1 
ATOM   1469 C  CA  . LYS   A 1 197 ? -12.09502 29.56591 41.76420 1.000 35.82861  ? 204 LYS   A CA  1 
ATOM   1470 C  C   . LYS   A 1 197 ? -11.47819 30.54775 42.75012 1.000 32.97638  ? 204 LYS   A C   1 
ATOM   1471 O  O   . LYS   A 1 197 ? -11.57310 31.76749 42.56817 1.000 31.30726  ? 204 LYS   A O   1 
ATOM   1472 C  CB  . LYS   A 1 197 ? -13.43569 29.06046 42.29350 1.000 33.45973  ? 204 LYS   A CB  1 
ATOM   1473 C  CG  . LYS   A 1 197 ? -14.43423 28.67444 41.22023 1.000 36.21500  ? 204 LYS   A CG  1 
ATOM   1474 C  CD  . LYS   A 1 197 ? -15.71190 28.13958 41.85033 1.000 41.00276  ? 204 LYS   A CD  1 
ATOM   1475 C  CE  . LYS   A 1 197 ? -16.54154 27.35158 40.85276 1.000 45.47246  ? 204 LYS   A CE  1 
ATOM   1476 N  NZ  . LYS   A 1 197 ? -17.63884 26.60444 41.52931 1.000 57.37218  ? 204 LYS   A NZ  1 
ATOM   1477 N  N   . GLU   A 1 198 ? -10.84230 30.02937 43.80275 1.000 36.03673  ? 205 GLU   A N   1 
ATOM   1478 C  CA  . GLU   A 1 198 ? -10.20484 30.89024 44.79247 1.000 35.26858  ? 205 GLU   A CA  1 
ATOM   1479 C  C   . GLU   A 1 198 ? -9.08011  31.70919 44.17261 1.000 34.29312  ? 205 GLU   A C   1 
ATOM   1480 O  O   . GLU   A 1 198 ? -8.91795  32.89354 44.48820 1.000 36.00656  ? 205 GLU   A O   1 
ATOM   1481 C  CB  . GLU   A 1 198 ? -9.67847  30.04105 45.94800 1.000 34.49935  ? 205 GLU   A CB  1 
ATOM   1482 C  CG  . GLU   A 1 198 ? -8.90492  30.81106 47.00213 1.000 42.48699  ? 205 GLU   A CG  1 
ATOM   1483 C  CD  . GLU   A 1 198 ? -8.27480  29.89251 48.02864 1.000 46.82703  ? 205 GLU   A CD  1 
ATOM   1484 O  OE1 . GLU   A 1 198 ? -7.74827  28.83399 47.62589 1.000 42.79213  ? 205 GLU   A OE1 1 
ATOM   1485 O  OE2 . GLU   A 1 198 ? -8.30992  30.22252 49.23324 1.000 47.62572  ? 205 GLU   A OE2 1 
ATOM   1486 N  N   . ILE   A 1 199 ? -8.29833  31.09797 43.28083 1.000 30.62472  ? 206 ILE   A N   1 
ATOM   1487 C  CA  . ILE   A 1 199 ? -7.17450  31.80140 42.67120 1.000 30.41788  ? 206 ILE   A CA  1 
ATOM   1488 C  C   . ILE   A 1 199 ? -7.66851  32.83969 41.67046 1.000 32.68616  ? 206 ILE   A C   1 
ATOM   1489 O  O   . ILE   A 1 199 ? -7.15198  33.96271 41.61589 1.000 33.81130  ? 206 ILE   A O   1 
ATOM   1490 C  CB  . ILE   A 1 199 ? -6.21333  30.79231 42.01810 1.000 30.72052  ? 206 ILE   A CB  1 
ATOM   1491 C  CG1 . ILE   A 1 199 ? -5.59819  29.88474 43.08324 1.000 29.30028  ? 206 ILE   A CG1 1 
ATOM   1492 C  CG2 . ILE   A 1 199 ? -5.12214  31.51423 41.24468 1.000 25.92339  ? 206 ILE   A CG2 1 
ATOM   1493 C  CD1 . ILE   A 1 199 ? -4.85406  28.70327 42.51561 1.000 36.16682  ? 206 ILE   A CD1 1 
ATOM   1494 N  N   . VAL   A 1 200 ? -8.67155  32.48454 40.86289 1.000 31.05153  ? 207 VAL   A N   1 
ATOM   1495 C  CA  . VAL   A 1 200 ? -9.20785  33.42493 39.88039 1.000 28.49745  ? 207 VAL   A CA  1 
ATOM   1496 C  C   . VAL   A 1 200 ? -9.80989  34.63673 40.58058 1.000 33.34183  ? 207 VAL   A C   1 
ATOM   1497 O  O   . VAL   A 1 200 ? -9.57991  35.78557 40.18361 1.000 35.13821  ? 207 VAL   A O   1 
ATOM   1498 C  CB  . VAL   A 1 200 ? -10.23761 32.72698 38.97272 1.000 34.84045  ? 207 VAL   A CB  1 
ATOM   1499 C  CG1 . VAL   A 1 200 ? -11.05063 33.75459 38.20303 1.000 28.52024  ? 207 VAL   A CG1 1 
ATOM   1500 C  CG2 . VAL   A 1 200 ? -9.53801  31.77618 38.01219 1.000 29.48061  ? 207 VAL   A CG2 1 
ATOM   1501 N  N   . LYS   A 1 201 ? -10.58339 34.39691 41.64263 1.000 31.87647  ? 208 LYS   A N   1 
ATOM   1502 C  CA  . LYS   A 1 201 ? -11.20758 35.49587 42.37166 1.000 35.04889  ? 208 LYS   A CA  1 
ATOM   1503 C  C   . LYS   A 1 201 ? -10.17679 36.35169 43.09563 1.000 40.55365  ? 208 LYS   A C   1 
ATOM   1504 O  O   . LYS   A 1 201 ? -10.42084 37.53827 43.34317 1.000 41.90714  ? 208 LYS   A O   1 
ATOM   1505 C  CB  . LYS   A 1 201 ? -12.22978 34.95048 43.36911 1.000 36.65793  ? 208 LYS   A CB  1 
ATOM   1506 C  CG  . LYS   A 1 201 ? -13.26155 35.97348 43.81991 1.000 48.43907  ? 208 LYS   A CG  1 
ATOM   1507 C  CD  . LYS   A 1 201 ? -14.14099 35.43711 44.94099 1.000 59.49711  ? 208 LYS   A CD  1 
ATOM   1508 C  CE  . LYS   A 1 201 ? -13.40300 35.42090 46.27050 1.000 67.47851  ? 208 LYS   A CE  1 
ATOM   1509 N  NZ  . LYS   A 1 201 ? -13.46274 34.08896 46.93504 1.000 70.63413  ? 208 LYS   A NZ  1 
ATOM   1510 N  N   . LYS   A 1 202 ? -9.02453  35.77506 43.43734 1.000 34.54781  ? 209 LYS   A N   1 
ATOM   1511 C  CA  . LYS   A 1 202 ? -8.01333  36.51976 44.17729 1.000 36.28922  ? 209 LYS   A CA  1 
ATOM   1512 C  C   . LYS   A 1 202 ? -7.14717  37.37117 43.25604 1.000 36.79895  ? 209 LYS   A C   1 
ATOM   1513 O  O   . LYS   A 1 202 ? -6.84152  38.52400 43.58049 1.000 36.11933  ? 209 LYS   A O   1 
ATOM   1514 C  CB  . LYS   A 1 202 ? -7.14047  35.55560 44.98188 1.000 39.52360  ? 209 LYS   A CB  1 
ATOM   1515 C  CG  . LYS   A 1 202 ? -6.14782  36.23613 45.91157 1.000 41.34008  ? 209 LYS   A CG  1 
ATOM   1516 C  CD  . LYS   A 1 202 ? -5.20901  35.22071 46.54485 1.000 42.01512  ? 209 LYS   A CD  1 
ATOM   1517 C  CE  . LYS   A 1 202 ? -4.39845  35.84004 47.66964 1.000 48.00853  ? 209 LYS   A CE  1 
ATOM   1518 N  NZ  . LYS   A 1 202 ? -3.46657  34.85239 48.28281 1.000 49.28815  ? 209 LYS   A NZ  1 
ATOM   1519 N  N   . HIS   A 1 203 ? -6.75070  36.82997 42.10296 1.000 36.31126  ? 210 HIS   A N   1 
ATOM   1520 C  CA  . HIS   A 1 203 ? -5.74400  37.46326 41.26358 1.000 31.59059  ? 210 HIS   A CA  1 
ATOM   1521 C  C   . HIS   A 1 203 ? -6.26739  37.96487 39.92374 1.000 33.64111  ? 210 HIS   A C   1 
ATOM   1522 O  O   . HIS   A 1 203 ? -5.56299  38.73145 39.25765 1.000 40.26941  ? 210 HIS   A O   1 
ATOM   1523 C  CB  . HIS   A 1 203 ? -4.58310  36.48817 41.00799 1.000 30.77676  ? 210 HIS   A CB  1 
ATOM   1524 C  CG  . HIS   A 1 203 ? -3.82074  36.11390 42.24200 1.000 35.00070  ? 210 HIS   A CG  1 
ATOM   1525 N  ND1 . HIS   A 1 203 ? -3.17525  37.04235 43.03024 1.000 41.84447  ? 210 HIS   A ND1 1 
ATOM   1526 C  CD2 . HIS   A 1 203 ? -3.59922  34.91012 42.82188 1.000 35.71054  ? 210 HIS   A CD2 1 
ATOM   1527 C  CE1 . HIS   A 1 203 ? -2.59042  36.42725 44.04286 1.000 41.61416  ? 210 HIS   A CE1 1 
ATOM   1528 N  NE2 . HIS   A 1 203 ? -2.83275  35.13289 43.94013 1.000 45.61566  ? 210 HIS   A NE2 1 
ATOM   1529 N  N   . SER   A 1 204 ? -7.47228  37.56662 39.50622 1.000 31.27551  ? 211 SER   A N   1 
ATOM   1530 C  CA  . SER   A 1 204 ? -7.93679  37.90433 38.16511 1.000 30.78363  ? 211 SER   A CA  1 
ATOM   1531 C  C   . SER   A 1 204 ? -9.39808  38.33919 38.15788 1.000 33.28727  ? 211 SER   A C   1 
ATOM   1532 O  O   . SER   A 1 204 ? -10.11326 38.09876 37.17909 1.000 39.11713  ? 211 SER   A O   1 
ATOM   1533 C  CB  . SER   A 1 204 ? -7.74782  36.72249 37.21013 1.000 37.47956  ? 211 SER   A CB  1 
ATOM   1534 O  OG  . SER   A 1 204 ? -6.39322  36.30631 37.16681 1.000 35.27404  ? 211 SER   A OG  1 
ATOM   1535 N  N   . GLN   A 1 205 ? -9.85408  38.99558 39.22708 1.000 36.62945  ? 212 GLN   A N   1 
ATOM   1536 C  CA  . GLN   A 1 205 ? -11.27431 39.31015 39.34984 1.000 36.61197  ? 212 GLN   A CA  1 
ATOM   1537 C  C   . GLN   A 1 205 ? -11.72824 40.34655 38.32844 1.000 31.86416  ? 212 GLN   A C   1 
ATOM   1538 O  O   . GLN   A 1 205 ? -12.89820 40.34718 37.92843 1.000 39.45589  ? 212 GLN   A O   1 
ATOM   1539 C  CB  . GLN   A 1 205 ? -11.58230 39.79489 40.76764 1.000 40.73573  ? 212 GLN   A CB  1 
ATOM   1540 C  CG  . GLN   A 1 205 ? -10.98612 41.15130 41.11860 1.000 52.50170  ? 212 GLN   A CG  1 
ATOM   1541 C  CD  . GLN   A 1 205 ? -9.84208  41.04768 42.10783 1.000 65.82601  ? 212 GLN   A CD  1 
ATOM   1542 O  OE1 . GLN   A 1 205 ? -8.90831  40.26805 41.91639 1.000 62.95877  ? 212 GLN   A OE1 1 
ATOM   1543 N  NE2 . GLN   A 1 205 ? -9.91125  41.83439 43.17645 1.000 50.17864  ? 212 GLN   A NE2 1 
ATOM   1544 N  N   . PHE   A 1 206 ? -10.83018 41.22724 37.89024 1.000 34.96865  ? 213 PHE   A N   1 
ATOM   1545 C  CA  . PHE   A 1 206 ? -11.19468 42.34515 37.03085 1.000 35.35387  ? 213 PHE   A CA  1 
ATOM   1546 C  C   . PHE   A 1 206 ? -10.77865 42.14544 35.57905 1.000 32.02344  ? 213 PHE   A C   1 
ATOM   1547 O  O   . PHE   A 1 206 ? -10.80595 43.10732 34.80360 1.000 30.22209  ? 213 PHE   A O   1 
ATOM   1548 C  CB  . PHE   A 1 206 ? -10.58944 43.64315 37.57130 1.000 33.91323  ? 213 PHE   A CB  1 
ATOM   1549 C  CG  . PHE   A 1 206 ? -11.09629 44.02857 38.93350 1.000 36.57202  ? 213 PHE   A CG  1 
ATOM   1550 C  CD1 . PHE   A 1 206 ? -12.45134 43.99293 39.21703 1.000 37.68686  ? 213 PHE   A CD1 1 
ATOM   1551 C  CD2 . PHE   A 1 206 ? -10.21964 44.43186 39.92796 1.000 42.00333  ? 213 PHE   A CD2 1 
ATOM   1552 C  CE1 . PHE   A 1 206 ? -12.92364 44.34775 40.46782 1.000 41.73198  ? 213 PHE   A CE1 1 
ATOM   1553 C  CE2 . PHE   A 1 206 ? -10.68602 44.78755 41.18084 1.000 43.56650  ? 213 PHE   A CE2 1 
ATOM   1554 C  CZ  . PHE   A 1 206 ? -12.03990 44.74536 41.45047 1.000 50.61058  ? 213 PHE   A CZ  1 
ATOM   1555 N  N   . ILE   A 1 207 ? -10.39255 40.92591 35.19338 1.000 33.92844  ? 214 ILE   A N   1 
ATOM   1556 C  CA  . ILE   A 1 207 ? -10.05331 40.66384 33.80000 1.000 30.08254  ? 214 ILE   A CA  1 
ATOM   1557 C  C   . ILE   A 1 207 ? -11.27315 40.93218 32.93241 1.000 32.43178  ? 214 ILE   A C   1 
ATOM   1558 O  O   . ILE   A 1 207 ? -12.37379 40.43663 33.20584 1.000 40.16883  ? 214 ILE   A O   1 
ATOM   1559 C  CB  . ILE   A 1 207 ? -9.54008  39.22636 33.62917 1.000 26.78059  ? 214 ILE   A CB  1 
ATOM   1560 C  CG1 . ILE   A 1 207 ? -8.22153  39.03887 34.38424 1.000 27.20568  ? 214 ILE   A CG1 1 
ATOM   1561 C  CG2 . ILE   A 1 207 ? -9.37640  38.89041 32.15226 1.000 33.54417  ? 214 ILE   A CG2 1 
ATOM   1562 C  CD1 . ILE   A 1 207 ? -7.02779  39.67910 33.70628 1.000 23.26022  ? 214 ILE   A CD1 1 
ATOM   1563 N  N   . GLY   A 1 208 ? -11.08361 41.72880 31.88261 1.000 28.77684  ? 215 GLY   A N   1 
ATOM   1564 C  CA  . GLY   A 1 208 ? -12.19253 42.19921 31.07469 1.000 29.32750  ? 215 GLY   A CA  1 
ATOM   1565 C  C   . GLY   A 1 208 ? -12.67435 41.23728 30.00748 1.000 34.88127  ? 215 GLY   A C   1 
ATOM   1566 O  O   . GLY   A 1 208 ? -13.09583 41.66535 28.92918 1.000 38.18726  ? 215 GLY   A O   1 
ATOM   1567 N  N   . TYR   A 1 209 ? -12.62505 39.93871 30.29095 1.000 28.81912  ? 216 TYR   A N   1 
ATOM   1568 C  CA  . TYR   A 1 209 ? -13.12001 38.92177 29.37496 1.000 26.50643  ? 216 TYR   A CA  1 
ATOM   1569 C  C   . TYR   A 1 209 ? -13.72429 37.79923 30.20108 1.000 30.67306  ? 216 TYR   A C   1 
ATOM   1570 O  O   . TYR   A 1 209 ? -13.28960 37.56924 31.33599 1.000 33.51212  ? 216 TYR   A O   1 
ATOM   1571 C  CB  . TYR   A 1 209 ? -12.00422 38.38272 28.46406 1.000 26.61016  ? 216 TYR   A CB  1 
ATOM   1572 C  CG  . TYR   A 1 209 ? -11.41475 39.42018 27.52644 1.000 29.24380  ? 216 TYR   A CG  1 
ATOM   1573 C  CD1 . TYR   A 1 209 ? -12.08721 39.80942 26.37327 1.000 23.21240  ? 216 TYR   A CD1 1 
ATOM   1574 C  CD2 . TYR   A 1 209 ? -10.18810 40.01372 27.79855 1.000 29.75232  ? 216 TYR   A CD2 1 
ATOM   1575 C  CE1 . TYR   A 1 209 ? -11.55119 40.75910 25.51507 1.000 27.13362  ? 216 TYR   A CE1 1 
ATOM   1576 C  CE2 . TYR   A 1 209 ? -9.64628  40.96292 26.94873 1.000 31.08395  ? 216 TYR   A CE2 1 
ATOM   1577 C  CZ  . TYR   A 1 209 ? -10.33152 41.33230 25.80848 1.000 29.63063  ? 216 TYR   A CZ  1 
ATOM   1578 O  OH  . TYR   A 1 209 ? -9.79621  42.27651 24.95935 1.000 35.22367  ? 216 TYR   A OH  1 
ATOM   1579 N  N   . PRO   A 1 210 ? -14.73365 37.10064 29.68009 1.000 34.65868  ? 217 PRO   A N   1 
ATOM   1580 C  CA  . PRO   A 1 210 ? -15.35091 36.01393 30.45514 1.000 24.44879  ? 217 PRO   A CA  1 
ATOM   1581 C  C   . PRO   A 1 210 ? -14.37314 34.86571 30.66049 1.000 24.50336  ? 217 PRO   A C   1 
ATOM   1582 O  O   . PRO   A 1 210 ? -13.74097 34.39152 29.71457 1.000 27.56956  ? 217 PRO   A O   1 
ATOM   1583 C  CB  . PRO   A 1 210 ? -16.55099 35.58623 29.59965 1.000 25.81316  ? 217 PRO   A CB  1 
ATOM   1584 C  CG  . PRO   A 1 210 ? -16.35162 36.19783 28.26442 1.000 38.90501  ? 217 PRO   A CG  1 
ATOM   1585 C  CD  . PRO   A 1 210 ? -15.41605 37.35137 28.39937 1.000 26.29376  ? 217 PRO   A CD  1 
ATOM   1586 N  N   . ILE   A 1 211 ? -14.24924 34.42782 31.90890 1.000 27.34031  ? 218 ILE   A N   1 
ATOM   1587 C  CA  . ILE   A 1 211 ? -13.42447 33.28198 32.27303 1.000 28.03190  ? 218 ILE   A CA  1 
ATOM   1588 C  C   . ILE   A 1 211 ? -14.36498 32.16203 32.69641 1.000 33.83443  ? 218 ILE   A C   1 
ATOM   1589 O  O   . ILE   A 1 211 ? -15.02142 32.25118 33.74149 1.000 34.08822  ? 218 ILE   A O   1 
ATOM   1590 C  CB  . ILE   A 1 211 ? -12.42718 33.62229 33.38853 1.000 35.00608  ? 218 ILE   A CB  1 
ATOM   1591 C  CG1 . ILE   A 1 211 ? -11.54799 34.80552 32.97764 1.000 28.25431  ? 218 ILE   A CG1 1 
ATOM   1592 C  CG2 . ILE   A 1 211 ? -11.57654 32.40784 33.73177 1.000 25.93836  ? 218 ILE   A CG2 1 
ATOM   1593 C  CD1 . ILE   A 1 211 ? -10.60493 35.27020 34.06597 1.000 20.84736  ? 218 ILE   A CD1 1 
ATOM   1594 N  N   . THR   A 1 212 ? -14.43313 31.10603 31.89045 1.000 30.87207  ? 219 THR   A N   1 
ATOM   1595 C  CA  . THR   A 1 212 ? -15.30211 29.96670 32.15920 1.000 31.26738  ? 219 THR   A CA  1 
ATOM   1596 C  C   . THR   A 1 212 ? -14.46765 28.80742 32.69101 1.000 30.49511  ? 219 THR   A C   1 
ATOM   1597 O  O   . THR   A 1 212 ? -13.49927 28.38593 32.04862 1.000 25.11785  ? 219 THR   A O   1 
ATOM   1598 C  CB  . THR   A 1 212 ? -16.05896 29.54600 30.89976 1.000 32.96381  ? 219 THR   A CB  1 
ATOM   1599 O  OG1 . THR   A 1 212 ? -16.65350 30.69915 30.29244 1.000 32.65399  ? 219 THR   A OG1 1 
ATOM   1600 C  CG2 . THR   A 1 212 ? -17.15216 28.54441 31.24320 1.000 31.33341  ? 219 THR   A CG2 1 
ATOM   1601 N  N   . LEU   A 1 213 ? -14.84304 28.29975 33.86181 1.000 25.18336  ? 220 LEU   A N   1 
ATOM   1602 C  CA  . LEU   A 1 213 ? -14.16082 27.17623 34.49255 1.000 29.98873  ? 220 LEU   A CA  1 
ATOM   1603 C  C   . LEU   A 1 213 ? -14.93973 25.90585 34.16833 1.000 33.80792  ? 220 LEU   A C   1 
ATOM   1604 O  O   . LEU   A 1 213 ? -16.01204 25.66561 34.73205 1.000 40.74286  ? 220 LEU   A O   1 
ATOM   1605 C  CB  . LEU   A 1 213 ? -14.04348 27.39015 36.00028 1.000 27.00294  ? 220 LEU   A CB  1 
ATOM   1606 C  CG  . LEU   A 1 213 ? -13.41117 26.25805 36.81141 1.000 39.03630  ? 220 LEU   A CG  1 
ATOM   1607 C  CD1 . LEU   A 1 213 ? -12.09058 25.82306 36.19648 1.000 42.10365  ? 220 LEU   A CD1 1 
ATOM   1608 C  CD2 . LEU   A 1 213 ? -13.21751 26.68554 38.25803 1.000 31.51430  ? 220 LEU   A CD2 1 
ATOM   1609 N  N   . PHE   A 1 214 ? -14.39928 25.09764 33.26054 1.000 35.91917  ? 221 PHE   A N   1 
ATOM   1610 C  CA  . PHE   A 1 214 ? -15.07927 23.88311 32.83248 1.000 34.23062  ? 221 PHE   A CA  1 
ATOM   1611 C  C   . PHE   A 1 214 ? -15.10278 22.85789 33.95863 1.000 42.40420  ? 221 PHE   A C   1 
ATOM   1612 O  O   . PHE   A 1 214 ? -14.11255 22.66949 34.67009 1.000 45.98383  ? 221 PHE   A O   1 
ATOM   1613 C  CB  . PHE   A 1 214 ? -14.38763 23.28906 31.60419 1.000 32.33029  ? 221 PHE   A CB  1 
ATOM   1614 C  CG  . PHE   A 1 214 ? -14.74578 23.96692 30.30782 1.000 28.91000  ? 221 PHE   A CG  1 
ATOM   1615 C  CD1 . PHE   A 1 214 ? -14.98225 25.33171 30.25569 1.000 33.98488  ? 221 PHE   A CD1 1 
ATOM   1616 C  CD2 . PHE   A 1 214 ? -14.83827 23.23350 29.13726 1.000 37.12084  ? 221 PHE   A CD2 1 
ATOM   1617 C  CE1 . PHE   A 1 214 ? -15.30667 25.94935 29.06245 1.000 33.64831  ? 221 PHE   A CE1 1 
ATOM   1618 C  CE2 . PHE   A 1 214 ? -15.16295 23.84476 27.94138 1.000 36.41485  ? 221 PHE   A CE2 1 
ATOM   1619 C  CZ  . PHE   A 1 214 ? -15.39786 25.20474 27.90407 1.000 32.31023  ? 221 PHE   A CZ  1 
ATOM   1620 N  N   . VAL   A 1 215 ? -16.24210 22.19222 34.11667 1.000 36.33389  ? 222 VAL   A N   1 
ATOM   1621 C  CA  . VAL   A 1 215 ? -16.41938 21.15934 35.13069 1.000 32.28629  ? 222 VAL   A CA  1 
ATOM   1622 C  C   . VAL   A 1 215 ? -16.20734 19.79916 34.48284 1.000 42.88811  ? 222 VAL   A C   1 
ATOM   1623 O  O   . VAL   A 1 215 ? -16.59636 19.58024 33.32778 1.000 36.15490  ? 222 VAL   A O   1 
ATOM   1624 C  CB  . VAL   A 1 215 ? -17.81199 21.25418 35.78438 1.000 37.90632  ? 222 VAL   A CB  1 
ATOM   1625 C  CG1 . VAL   A 1 215 ? -17.90370 20.32726 36.98696 1.000 44.58079  ? 222 VAL   A CG1 1 
ATOM   1626 C  CG2 . VAL   A 1 215 ? -18.11152 22.68794 36.19096 1.000 37.15900  ? 222 VAL   A CG2 1 
ATOM   1627 N  N   . GLU   A 1 216 ? -15.57751 18.88631 35.21891 1.000 35.84616  ? 223 GLU   A N   1 
ATOM   1628 C  CA  . GLU   A 1 216 ? -15.35402 17.54221 34.71335 1.000 45.87423  ? 223 GLU   A CA  1 
ATOM   1629 C  C   . GLU   A 1 216 ? -16.59049 16.67353 34.93024 1.000 40.70624  ? 223 GLU   A C   1 
ATOM   1630 O  O   . GLU   A 1 216 ? -17.49082 17.00310 35.70768 1.000 41.34571  ? 223 GLU   A O   1 
ATOM   1631 C  CB  . GLU   A 1 216 ? -14.13416 16.90493 35.38155 1.000 42.42891  ? 223 GLU   A CB  1 
ATOM   1632 C  CG  . GLU   A 1 216 ? -12.90224 17.79719 35.40624 1.000 46.15703  ? 223 GLU   A CG  1 
ATOM   1633 C  CD  . GLU   A 1 216 ? -11.66552 17.07043 35.90052 1.000 49.27603  ? 223 GLU   A CD  1 
ATOM   1634 O  OE1 . GLU   A 1 216 ? -11.19311 16.15261 35.19574 1.000 46.35427  ? 223 GLU   A OE1 1 
ATOM   1635 O  OE2 . GLU   A 1 216 ? -11.16644 17.41609 36.99255 1.000 53.36605  ? 223 GLU   A OE2 1 
ATOM   1636 N  N   . LYS   A 1 217 ? -16.62069 15.54658 34.22700 1.000 51.56786  ? 224 LYS   A N   1 
ATOM   1637 C  CA  . LYS   A 1 217 ? -17.78023 14.66269 34.23773 1.000 55.17208  ? 224 LYS   A CA  1 
ATOM   1638 C  C   . LYS   A 1 217 ? -17.47936 13.34306 34.94551 1.000 48.38666  ? 224 LYS   A C   1 
ATOM   1639 O  O   . LYS   A 1 217 ? -16.36687 13.12395 35.42511 1.000 62.52688  ? 224 LYS   A O   1 
ATOM   1640 C  CB  . LYS   A 1 217 ? -18.24813 14.39947 32.80508 1.000 44.93551  ? 224 LYS   A CB  1 
ATOM   1641 C  CG  . LYS   A 1 217 ? -18.32125 15.65013 31.94142 1.000 42.70410  ? 224 LYS   A CG  1 
ATOM   1642 C  CD  . LYS   A 1 217 ? -18.54752 15.30321 30.48026 1.000 42.13242  ? 224 LYS   A CD  1 
ATOM   1643 C  CE  . LYS   A 1 217 ? -17.35187 14.57068 29.89514 1.000 42.14299  ? 224 LYS   A CE  1 
ATOM   1644 N  NZ  . LYS   A 1 217 ? -16.27703 15.51466 29.47913 1.000 38.76423  ? 224 LYS   A NZ  1 
HETATM 1645 C  C10 . A1AYH B 2 .   ? 12.33992  30.98257 23.97401 0.927 20.08567  ? 301 A1AYH A C10 1 
HETATM 1646 C  C13 . A1AYH B 2 .   ? 4.97809   33.93340 25.61049 0.927 30.13466  ? 301 A1AYH A C13 1 
HETATM 1647 C  C11 . A1AYH B 2 .   ? 13.42200  31.18069 23.08333 0.927 30.26643  ? 301 A1AYH A C11 1 
HETATM 1648 C  C12 . A1AYH B 2 .   ? 12.92819  30.95241 21.81896 0.927 28.61597  ? 301 A1AYH A C12 1 
HETATM 1649 C  C14 . A1AYH B 2 .   ? 5.63445   35.10069 25.95704 0.927 42.47830  ? 301 A1AYH A C14 1 
HETATM 1650 C  C1  . A1AYH B 2 .   ? 6.89437   35.02294 26.50063 0.927 36.47823  ? 301 A1AYH A C1  1 
HETATM 1651 C  C2  . A1AYH B 2 .   ? 7.51020   33.81302 26.70406 0.927 26.16481  ? 301 A1AYH A C2  1 
HETATM 1652 C  C3  . A1AYH B 2 .   ? 6.84035   32.65595 26.35430 0.927 32.86646  ? 301 A1AYH A C3  1 
HETATM 1653 C  C4  . A1AYH B 2 .   ? 5.57245   32.69769 25.79886 0.927 36.71629  ? 301 A1AYH A C4  1 
HETATM 1654 C  C5  . A1AYH B 2 .   ? 4.85435   31.42467 25.42308 0.927 33.13294  ? 301 A1AYH A C5  1 
HETATM 1655 C  C6  . A1AYH B 2 .   ? 6.87964   31.08746 23.48109 0.927 34.48026  ? 301 A1AYH A C6  1 
HETATM 1656 C  C7  . A1AYH B 2 .   ? 7.59380   29.99062 22.70739 0.927 25.59771  ? 301 A1AYH A C7  1 
HETATM 1657 C  C8  . A1AYH B 2 .   ? 9.88290   30.33636 23.57876 0.927 26.46323  ? 301 A1AYH A C8  1 
HETATM 1658 C  C9  . A1AYH B 2 .   ? 11.27396  30.65445 23.22215 0.927 26.42434  ? 301 A1AYH A C9  1 
HETATM 1659 N  N1  . A1AYH B 2 .   ? 9.01762   30.23822 22.56021 0.927 28.12901  ? 301 A1AYH A N1  1 
HETATM 1660 O  O1  . A1AYH B 2 .   ? 9.54226   30.18682 24.75360 0.927 30.47065  ? 301 A1AYH A O1  1 
HETATM 1661 O  O2  . A1AYH B 2 .   ? 11.60708  30.62829 21.89620 0.927 34.16004  ? 301 A1AYH A O2  1 
HETATM 1662 S  S1  . A1AYH B 2 .   ? 5.09744   30.86274 23.70801 0.927 31.74196  ? 301 A1AYH A S1  1 
HETATM 1663 CL CL1 . A1AYH B 2 .   ? 7.72886   36.48546 26.93854 0.927 54.29144  ? 301 A1AYH A CL1 1 
HETATM 1664 O  O   . HOH   C 3 .   ? -3.29973  24.84048 10.00468 1.000 52.76782  ? 401 HOH   A O   1 
HETATM 1665 O  O   . HOH   C 3 .   ? -13.82878 33.30188 19.00719 1.000 36.62037  ? 402 HOH   A O   1 
HETATM 1666 O  O   . HOH   C 3 .   ? 17.59323  43.04725 30.45572 1.000 44.27575  ? 403 HOH   A O   1 
HETATM 1667 O  O   . HOH   C 3 .   ? 9.49490   17.20095 26.59115 1.000 40.22431  ? 404 HOH   A O   1 
HETATM 1668 O  O   . HOH   C 3 .   ? -0.69394  16.79176 44.41058 1.000 44.54504  ? 405 HOH   A O   1 
HETATM 1669 O  O   . HOH   C 3 .   ? 6.01927   19.69802 11.45904 1.000 37.22193  ? 406 HOH   A O   1 
HETATM 1670 O  O   . HOH   C 3 .   ? 13.78369  16.93881 20.42309 1.000 31.38152  ? 407 HOH   A O   1 
HETATM 1671 O  O   . HOH   C 3 .   ? 10.71224  28.37781 42.69657 1.000 44.70971  ? 408 HOH   A O   1 
HETATM 1672 O  O   . HOH   C 3 .   ? -12.18252 32.11147 47.90078 1.000 53.93146  ? 409 HOH   A O   1 
HETATM 1673 O  O   . HOH   C 3 .   ? -10.53947 31.12210 50.10292 1.000 44.08161  ? 410 HOH   A O   1 
HETATM 1674 O  O   . HOH   C 3 .   ? -6.32464  45.96909 11.80599 1.000 31.88069  ? 411 HOH   A O   1 
HETATM 1675 O  O   . HOH   C 3 .   ? -17.51802 33.35053 24.43256 1.000 41.17085  ? 412 HOH   A O   1 
HETATM 1676 O  O   . HOH   C 3 .   ? -14.88168 31.75211 28.75727 1.000 25.00817  ? 413 HOH   A O   1 
HETATM 1677 O  O   . HOH   C 3 .   ? 8.78837   22.43666 12.81057 1.000 43.50913  ? 414 HOH   A O   1 
HETATM 1678 O  O   . HOH   C 3 .   ? -3.89194  34.03132 21.68745 1.000 19.31167  ? 415 HOH   A O   1 
HETATM 1679 O  O   . HOH   C 3 .   ? 7.00416   24.74098 9.32870  1.000 40.75833  ? 416 HOH   A O   1 
HETATM 1680 O  O   . HOH   C 3 .   ? -6.68554  31.89057 12.42534 1.000 32.57726  ? 417 HOH   A O   1 
HETATM 1681 O  O   . HOH   C 3 .   ? 5.56842   39.32269 27.45321 1.000 56.82534  ? 418 HOH   A O   1 
HETATM 1682 O  O   . HOH   C 3 .   ? 10.36827  33.17717 20.24810 1.000 34.72705  ? 419 HOH   A O   1 
HETATM 1683 O  O   . HOH   C 3 .   ? -6.52247  19.85249 30.46736 1.000 29.55809  ? 420 HOH   A O   1 
HETATM 1684 O  O   . HOH   C 3 .   ? -15.71427 18.56277 31.07684 1.000 31.42987  ? 421 HOH   A O   1 
HETATM 1685 O  O   . HOH   C 3 .   ? -4.51200  13.86729 38.49258 1.000 46.17046  ? 422 HOH   A O   1 
HETATM 1686 O  O   . HOH   C 3 .   ? -4.42653  36.34058 14.42197 1.000 29.51615  ? 423 HOH   A O   1 
HETATM 1687 O  O   . HOH   C 3 .   ? 8.66018   26.88543 43.60900 1.000 46.21413  ? 424 HOH   A O   1 
HETATM 1688 O  O   . HOH   C 3 .   ? -8.68108  42.43957 31.04691 1.000 26.35246  ? 425 HOH   A O   1 
HETATM 1689 O  O   . HOH   C 3 .   ? 0.60504   39.55430 30.65949 1.000 30.43241  ? 426 HOH   A O   1 
HETATM 1690 O  O   . HOH   C 3 .   ? -11.83940 16.51728 18.64302 1.000 58.69464  ? 427 HOH   A O   1 
HETATM 1691 O  O   . HOH   C 3 .   ? 4.00878   39.13460 38.19455 1.000 38.54337  ? 428 HOH   A O   1 
HETATM 1692 O  O   . HOH   C 3 .   ? -4.95331  42.82703 29.25388 1.000 36.59177  ? 429 HOH   A O   1 
HETATM 1693 O  O   . HOH   C 3 .   ? 9.15223   18.73920 23.23231 1.000 37.82922  ? 430 HOH   A O   1 
HETATM 1694 O  O   . HOH   C 3 .   ? -5.18173  21.08944 13.37739 1.000 48.71868  ? 431 HOH   A O   1 
HETATM 1695 O  O   . HOH   C 3 .   ? -0.05987  30.48471 13.52224 1.000 29.70341  ? 432 HOH   A O   1 
HETATM 1696 O  O   . HOH   C 3 .   ? 9.18840   25.10310 41.22152 1.000 31.30313  ? 433 HOH   A O   1 
HETATM 1697 O  O   . HOH   C 3 .   ? 15.40121  19.44750 14.93938 1.000 27.15919  ? 434 HOH   A O   1 
HETATM 1698 O  O   . HOH   C 3 .   ? 14.50080  33.48131 19.86245 1.000 35.05278  ? 435 HOH   A O   1 
HETATM 1699 O  O   . HOH   C 3 .   ? 2.53108   37.39504 32.68091 1.000 30.73170  ? 436 HOH   A O   1 
HETATM 1700 O  O   . HOH   C 3 .   ? 1.20446   24.66493 45.51543 1.000 39.25562  ? 437 HOH   A O   1 
HETATM 1701 O  O   . HOH   C 3 .   ? -19.71794 16.75324 37.22479 1.000 48.57666  ? 438 HOH   A O   1 
HETATM 1702 O  O   . HOH   C 3 .   ? 0.93262   18.39147 17.84954 1.000 49.96974  ? 439 HOH   A O   1 
HETATM 1703 O  O   . HOH   C 3 .   ? 5.23419   36.74121 12.53623 1.000 43.36285  ? 440 HOH   A O   1 
HETATM 1704 O  O   . HOH   C 3 .   ? 14.25557  17.41627 16.10262 1.000 29.14714  ? 441 HOH   A O   1 
HETATM 1705 O  O   . HOH   C 3 .   ? 15.39850  24.92096 29.67627 1.000 32.27898  ? 442 HOH   A O   1 
HETATM 1706 O  O   . HOH   C 3 .   ? -4.60419  37.59979 35.54130 1.000 25.58306  ? 443 HOH   A O   1 
HETATM 1707 O  O   . HOH   C 3 .   ? -12.73834 19.70587 41.45568 1.000 38.30411  ? 444 HOH   A O   1 
HETATM 1708 O  O   . HOH   C 3 .   ? 1.32583   43.21185 29.73845 1.000 39.33439  ? 445 HOH   A O   1 
HETATM 1709 O  O   . HOH   C 3 .   ? 9.26637   25.16184 46.23877 1.000 42.81272  ? 446 HOH   A O   1 
HETATM 1710 O  O   . HOH   C 3 .   ? -6.43036  20.34830 26.59749 1.000 40.53379  ? 447 HOH   A O   1 
HETATM 1711 O  O   . HOH   C 3 .   ? 23.34201  45.49873 34.74745 1.000 62.63552  ? 448 HOH   A O   1 
HETATM 1712 O  O   . HOH   C 3 .   ? 0.03659   37.47071 25.36147 1.000 34.42842  ? 449 HOH   A O   1 
HETATM 1713 O  O   . HOH   C 3 .   ? 12.29964  20.01591 26.78183 1.000 31.26099  ? 450 HOH   A O   1 
HETATM 1714 O  O   . HOH   C 3 .   ? 19.52409  28.79452 37.55597 1.000 44.60110  ? 451 HOH   A O   1 
HETATM 1715 O  O   . HOH   C 3 .   ? 6.39279   20.43178 19.52742 1.000 23.25020  ? 452 HOH   A O   1 
HETATM 1716 O  O   . HOH   C 3 .   ? -13.82755 37.73608 34.06966 1.000 47.97557  ? 453 HOH   A O   1 
HETATM 1717 O  O   . HOH   C 3 .   ? -8.79327  18.05872 29.00069 1.000 49.82375  ? 454 HOH   A O   1 
HETATM 1718 O  O   . HOH   C 3 .   ? 5.82854   32.52956 10.77322 1.000 34.44837  ? 455 HOH   A O   1 
HETATM 1719 O  O   . HOH   C 3 .   ? -3.55514  30.33044 26.75173 1.000 28.20112  ? 456 HOH   A O   1 
HETATM 1720 O  O   . HOH   C 3 .   ? 1.57555   37.17529 18.06008 1.000 37.60554  ? 457 HOH   A O   1 
HETATM 1721 O  O   . HOH   C 3 .   ? -0.33774  12.63016 42.14390 1.000 49.36554  ? 458 HOH   A O   1 
HETATM 1722 O  O   . HOH   C 3 .   ? -7.87006  46.35378 22.70232 1.000 39.16072  ? 459 HOH   A O   1 
HETATM 1723 O  O   . HOH   C 3 .   ? -0.39758  40.23662 7.80957  1.000 53.84007  ? 460 HOH   A O   1 
HETATM 1724 O  O   . HOH   C 3 .   ? -12.11620 25.90122 24.63344 1.000 29.94246  ? 461 HOH   A O   1 
HETATM 1725 O  O   . HOH   C 3 .   ? -5.02159  16.55099 28.57477 1.000 43.59906  ? 462 HOH   A O   1 
HETATM 1726 O  O   . HOH   C 3 .   ? -12.77990 20.29342 32.97091 1.000 43.43764  ? 463 HOH   A O   1 
HETATM 1727 O  O   . HOH   C 3 .   ? 16.85695  24.78900 31.84928 1.000 30.71228  ? 464 HOH   A O   1 
HETATM 1728 O  O   . HOH   C 3 .   ? 22.62358  32.02515 24.74332 1.000 40.97325  ? 465 HOH   A O   1 
HETATM 1729 O  O   . HOH   C 3 .   ? -17.77011 33.73052 15.56104 1.000 52.89450  ? 466 HOH   A O   1 
HETATM 1730 O  O   . HOH   C 3 .   ? -1.07348  19.88581 45.34015 1.000 40.83522  ? 467 HOH   A O   1 
HETATM 1731 O  O   . HOH   C 3 .   ? -1.30999  12.92405 30.50255 1.000 51.99767  ? 468 HOH   A O   1 
HETATM 1732 O  O   . HOH   C 3 .   ? 12.89327  26.34234 11.42369 1.000 47.19091  ? 469 HOH   A O   1 
HETATM 1733 O  O   . HOH   C 3 .   ? -2.13077  32.00506 28.30918 1.000 37.61291  ? 470 HOH   A O   1 
HETATM 1734 O  O   . HOH   C 3 .   ? -6.69120  16.83939 42.35151 1.000 50.06552  ? 471 HOH   A O   1 
HETATM 1735 O  O   . HOH   C 3 .   ? 19.59878  18.58370 29.19015 1.000 43.53260  ? 472 HOH   A O   1 
HETATM 1736 O  O   . HOH   C 3 .   ? -2.08288  33.75492 25.30404 1.000 31.30857  ? 473 HOH   A O   1 
HETATM 1737 O  O   . HOH   C 3 .   ? 1.27135   40.04025 35.26890 1.000 45.54071  ? 474 HOH   A O   1 
HETATM 1738 O  O   . HOH   C 3 .   ? -12.05515 44.17487 27.93492 1.000 39.54433  ? 475 HOH   A O   1 
HETATM 1739 O  O   . HOH   C 3 .   ? -0.23521  38.45760 22.69474 1.000 38.87038  ? 476 HOH   A O   1 
HETATM 1740 O  O   . HOH   C 3 .   ? 6.31383   14.92210 38.76864 1.000 39.84345  ? 477 HOH   A O   1 
HETATM 1741 O  O   . HOH   C 3 .   ? 1.65967   39.06105 44.03782 1.000 52.57404  ? 478 HOH   A O   1 
HETATM 1742 O  O   . HOH   C 3 .   ? 7.66443   48.79324 38.57728 1.000 40.66110  ? 479 HOH   A O   1 
HETATM 1743 O  O   . HOH   C 3 .   ? -6.03846  31.85588 50.04449 1.000 48.12646  ? 480 HOH   A O   1 
HETATM 1744 O  O   . HOH   C 3 .   ? 11.47884  37.80116 12.97557 1.000 41.88374  ? 481 HOH   A O   1 
HETATM 1745 O  O   . HOH   C 3 .   ? -8.69673  29.26926 20.79666 1.000 36.12394  ? 482 HOH   A O   1 
HETATM 1746 O  O   . HOH   C 3 .   ? 4.35221   38.22997 31.32259 1.000 26.30205  ? 483 HOH   A O   1 
HETATM 1747 O  O   . HOH   C 3 .   ? -9.15343  44.17877 28.63371 1.000 33.97265  ? 484 HOH   A O   1 
HETATM 1748 O  O   . HOH   C 3 .   ? -16.64321 38.33952 22.70623 1.000 44.39451  ? 485 HOH   A O   1 
HETATM 1749 O  O   . HOH   C 3 .   ? 6.09855   24.29108 50.04472 1.000 42.76873  ? 486 HOH   A O   1 
HETATM 1750 O  O   . HOH   C 3 .   ? 5.06454   36.12113 29.58437 1.000 29.41158  ? 487 HOH   A O   1 
HETATM 1751 O  O   . HOH   C 3 .   ? 4.38021   18.39757 20.57068 1.000 46.34644  ? 488 HOH   A O   1 
HETATM 1752 O  O   . HOH   C 3 .   ? 2.09107   15.40878 34.09506 1.000 42.06679  ? 489 HOH   A O   1 
HETATM 1753 O  O   . HOH   C 3 .   ? 6.71882   13.29673 9.69061  1.000 56.61834  ? 490 HOH   A O   1 
HETATM 1754 O  O   . HOH   C 3 .   ? -17.25197 29.31724 35.38190 1.000 37.37692  ? 491 HOH   A O   1 
HETATM 1755 O  O   . HOH   C 3 .   ? -10.13306 34.29913 46.87784 1.000 41.39038  ? 492 HOH   A O   1 
HETATM 1756 O  O   . HOH   C 3 .   ? -3.27966  45.02514 26.57679 1.000 41.15468  ? 493 HOH   A O   1 
HETATM 1757 O  O   . HOH   C 3 .   ? -5.80062  33.77676 38.74087 1.000 43.04760  ? 494 HOH   A O   1 
HETATM 1758 O  O   . HOH   C 3 .   ? -5.02558  20.64968 19.04995 1.000 48.16626  ? 495 HOH   A O   1 
HETATM 1759 O  O   . HOH   C 3 .   ? -4.69565  40.43017 36.86429 1.000 45.82869  ? 496 HOH   A O   1 
HETATM 1760 O  O   . HOH   C 3 .   ? 0.46400   23.40177 48.78580 1.000 47.40992  ? 497 HOH   A O   1 
HETATM 1761 O  O   . HOH   C 3 .   ? 4.21879   23.06036 46.74734 1.000 47.66655  ? 498 HOH   A O   1 
HETATM 1762 O  O   . HOH   C 3 .   ? 6.98011   47.51816 36.06230 1.000 56.29731  ? 499 HOH   A O   1 
HETATM 1763 O  O   . HOH   C 3 .   ? -14.46969 15.88101 31.94393 1.000 40.46762  ? 500 HOH   A O   1 
HETATM 1764 O  O   . HOH   C 3 .   ? 18.57245  35.98417 20.60832 1.000 52.26239  ? 501 HOH   A O   1 
HETATM 1765 O  O   . HOH   C 3 .   ? -4.66137  39.11289 9.72143  1.000 44.48247  ? 502 HOH   A O   1 
HETATM 1766 O  O   . HOH   C 3 .   ? 10.65934  41.55067 28.16801 1.000 49.26130  ? 503 HOH   A O   1 
HETATM 1767 O  O   . HOH   C 3 .   ? -13.74766 32.84024 40.60017 1.000 34.82737  ? 504 HOH   A O   1 
HETATM 1768 O  O   . HOH   C 3 .   ? -13.46816 22.47110 37.72761 1.000 47.50175  ? 505 HOH   A O   1 
HETATM 1769 O  O   . HOH   C 3 .   ? -11.52269 32.11673 17.72923 1.000 38.28379  ? 506 HOH   A O   1 
HETATM 1770 O  O   . HOH   C 3 .   ? 5.77360   47.10405 41.86415 1.000 59.89992  ? 507 HOH   A O   1 
HETATM 1771 O  O   . HOH   C 3 .   ? -4.79694  30.44670 7.79936  1.000 44.40961  ? 508 HOH   A O   1 
HETATM 1772 O  O   . HOH   C 3 .   ? 10.98976  18.73049 33.87775 1.000 38.53282  ? 509 HOH   A O   1 
HETATM 1773 O  O   . HOH   C 3 .   ? -15.68100 35.83330 34.35649 1.000 43.72019  ? 510 HOH   A O   1 
HETATM 1774 O  O   . HOH   C 3 .   ? 11.26440  24.29397 8.40569  1.000 54.92664  ? 511 HOH   A O   1 
HETATM 1775 O  O   . HOH   C 3 .   ? 12.37113  42.80923 27.84078 1.000 45.79909  ? 512 HOH   A O   1 
HETATM 1776 O  O   . HOH   C 3 .   ? -7.22999  26.34349 12.92067 1.000 46.35353  ? 513 HOH   A O   1 
HETATM 1777 O  O   . HOH   C 3 .   ? -14.34687 19.75574 38.04784 1.000 41.77872  ? 514 HOH   A O   1 
HETATM 1778 O  O   . HOH   C 3 .   ? -16.14181 39.48642 25.55579 1.000 42.42263  ? 515 HOH   A O   1 
HETATM 1779 O  O   . HOH   C 3 .   ? -8.83440  29.46525 10.66373 1.000 50.80475  ? 516 HOH   A O   1 
HETATM 1780 O  O   . HOH   C 3 .   ? -1.92372  43.94694 24.37072 1.000 44.35119  ? 517 HOH   A O   1 
HETATM 1781 O  O   . HOH   C 3 .   ? 7.897     44.219   30.741   1.000 46.19093  ? 518 HOH   A O   1 
HETATM 1782 O  O   . HOH   C 3 .   ? 15.75548  22.69681 33.71162 1.000 39.84265  ? 519 HOH   A O   1 
HETATM 1783 O  O   . HOH   C 3 .   ? -15.20520 41.48668 26.35909 1.000 42.49154  ? 520 HOH   A O   1 
HETATM 1784 O  O   . HOH   C 3 .   ? 0.75064   32.35250 27.65974 1.000 31.34801  ? 521 HOH   A O   1 
HETATM 1785 O  O   . HOH   C 3 .   ? -5.34444  24.41714 11.65093 1.000 49.48806  ? 522 HOH   A O   1 
HETATM 1786 O  O   . HOH   C 3 .   ? 19.18819  44.33667 32.40792 1.000 46.34057  ? 523 HOH   A O   1 
HETATM 1787 O  O   . HOH   C 3 .   ? -9.00143  26.79993 11.70724 1.000 50.89288  ? 524 HOH   A O   1 
HETATM 1788 O  O   . HOH   C 3 .   ? -4.48695  38.94886 12.93638 1.000 35.63859  ? 525 HOH   A O   1 
HETATM 1789 O  O   . HOH   C 3 .   ? 19.35943  23.57904 30.82384 1.000 42.66699  ? 526 HOH   A O   1 
HETATM 1790 O  O   . HOH   C 3 .   ? -8.187    47.527   27.509   1.000 45.51620  ? 527 HOH   A O   1 
HETATM 1791 O  O   . HOH   C 3 .   ? -12.17240 28.08433 22.25983 1.000 45.80185  ? 528 HOH   A O   1 
HETATM 1792 O  O   . HOH   C 3 .   ? 1.27740   33.31802 26.00842 1.000 43.09005  ? 529 HOH   A O   1 
HETATM 1793 O  O   . HOH   C 3 .   ? -3.088    53.088   20.425   1.000 47.90802  ? 530 HOH   A O   1 
HETATM 1794 O  O   . HOH   C 3 .   ? -17.53644 32.52620 27.09681 1.000 35.14151  ? 531 HOH   A O   1 
HETATM 1795 O  O   . HOH   C 3 .   ? 8.10944   15.04328 25.57673 1.000 54.44747  ? 532 HOH   A O   1 
HETATM 1796 O  O   . HOH   C 3 .   ? -11.33527 18.26073 28.71049 1.000 42.79630  ? 533 HOH   A O   1 
HETATM 1797 O  O   . HOH   C 3 .   ? -13.01707 18.47128 30.93170 1.000 39.11303  ? 534 HOH   A O   1 
HETATM 1798 O  O   . HOH   C 3 .   ? 12.891    44.204   29.475   1.000 44.72545  ? 535 HOH   A O   1 
HETATM 1799 O  O   . HOH   C 3 .   ? -1.08868  40.60132 36.83753 1.000 48.03505  ? 536 HOH   A O   1 
HETATM 1800 O  O   . HOH   C 3 .   ? -2.70856  18.55237 47.01542 1.000 51.56663  ? 537 HOH   A O   1 
HETATM 1801 O  O   . HOH   C 3 .   ? 12.115    44.250   31.682   1.000 32.65671  ? 538 HOH   A O   1 
HETATM 1802 O  O   . HOH   C 3 .   ? -5.90212  14.38384 41.37076 1.000 40.04846  ? 539 HOH   A O   1 
HETATM 1803 O  O   . HOH   C 3 .   ? -8.62247  34.45509 49.14663 1.000 45.98129  ? 540 HOH   A O   1 
HETATM 1804 O  O   . HOH   C 3 .   ? -1.12287  16.76957 47.39662 1.000 59.17258  ? 541 HOH   A O   1 
HETATM 1805 O  O   . HOH   C 3 .   ? 14.36539  20.47130 34.67994 1.000 51.78987  ? 542 HOH   A O   1 
HETATM 1806 O  O   . HOH   C 3 .   ? 8.44616   31.47714 9.47996  1.000 46.96985  ? 543 HOH   A O   1 
HETATM 1807 O  O   . HOH   C 3 .   ? -5.88408  47.79282 23.84868 1.000 41.14515  ? 544 HOH   A O   1 
HETATM 1808 O  O   . HOH   C 3 .   ? 20.76889  31.07175 38.69379 1.000 44.87444  ? 545 HOH   A O   1 
HETATM 1809 O  O   . HOH   C 3 .   ? 19.00530  43.73560 28.12752 1.000 42.47370  ? 546 HOH   A O   1 
HETATM 1810 O  O   . HOH   C 3 .   ? 1.67274   17.40783 19.76852 1.000 50.10132  ? 547 HOH   A O   1 
HETATM 1811 O  O   . HOH   C 3 .   ? -15.22861 42.74328 23.80810 1.000 49.28524  ? 548 HOH   A O   1 
HETATM 1812 O  O   . HOH   C 3 .   ? 3.258     47.126   36.101   1.000 52.36550  ? 549 HOH   A O   1 
HETATM 1813 O  O   . HOH   C 3 .   ? 23.013    25.133   23.274   1.000 45.24416  ? 550 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   . GLU A 9   ? 0.71926 0.92454 0.71089 -0.04095 0.03721  -0.43148 16  GLU A N   
2    C CA  . GLU A 9   ? 0.71648 0.88328 0.68862 0.00207  0.03508  -0.39693 16  GLU A CA  
3    C C   . GLU A 9   ? 0.67486 0.82727 0.66990 0.01662  0.02370  -0.35143 16  GLU A C   
4    O O   . GLU A 9   ? 0.68975 0.90629 0.70217 0.01951  0.00055  -0.34930 16  GLU A O   
5    C CB  . GLU A 9   ? 0.73017 0.96635 0.68042 0.03828  0.01213  -0.39016 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.86641 1.05017 0.79415 0.07118  0.02280  -0.35168 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.08581 1.17416 1.00358 0.05722  0.05900  -0.35950 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.00194 1.07735 0.89677 0.04254  0.07591  -0.39604 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.13456 1.15956 1.06464 0.06342  0.07095  -0.32358 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.55633 0.62793 0.54991 0.02809  0.04040  -0.31360 17  VAL A N   
11   C CA  . VAL A 10  ? 0.51211 0.56344 0.52509 0.03791  0.03274  -0.27176 17  VAL A CA  
12   C C   . VAL A 10  ? 0.48717 0.52206 0.49293 0.07386  0.02699  -0.22283 17  VAL A C   
13   O O   . VAL A 10  ? 0.51379 0.50670 0.50464 0.08562  0.04510  -0.21384 17  VAL A O   
14   C CB  . VAL A 10  ? 0.53814 0.51625 0.55772 0.01461  0.06003  -0.27433 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.49354 0.46414 0.53148 0.02371  0.04902  -0.23610 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.57722 0.56520 0.60285 -0.02928 0.07430  -0.32889 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.44238 0.51021 0.45821 0.09029  0.00485  -0.19290 18  GLU A N   
18   C CA  . GLU A 11  ? 0.44302 0.49961 0.45656 0.11572  0.00112  -0.14937 18  GLU A CA  
19   C C   . GLU A 11  ? 0.39579 0.42083 0.42735 0.11222  0.00172  -0.12200 18  GLU A C   
20   O O   . GLU A 11  ? 0.37809 0.41156 0.42228 0.10029  -0.00723 -0.12582 18  GLU A O   
21   C CB  . GLU A 11  ? 0.40363 0.50912 0.40821 0.13575  -0.01785 -0.13511 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.47277 0.61807 0.45351 0.14715  -0.01995 -0.15652 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.60411 0.78981 0.56805 0.17458  -0.03410 -0.13476 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.41767 0.63522 0.38454 0.17912  -0.04841 -0.13566 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.57200 0.75495 0.51725 0.19407  -0.02774 -0.11496 18  GLU A OE2 
26   N N   . THR A 12  ? 0.39676 0.39374 0.42901 0.12442  0.01200  -0.09549 19  THR A N   
27   C CA  . THR A 12  ? 0.37876 0.35580 0.42522 0.12410  0.01228  -0.07035 19  THR A CA  
28   C C   . THR A 12  ? 0.36989 0.37159 0.42389 0.13497  0.00070  -0.03999 19  THR A C   
29   O O   . THR A 12  ? 0.36981 0.38352 0.41921 0.14844  0.00558  -0.02821 19  THR A O   
30   C CB  . THR A 12  ? 0.41025 0.34420 0.45100 0.13192  0.03514  -0.06421 19  THR A CB  
31   O OG1 . THR A 12  ? 0.44844 0.34500 0.47903 0.11550  0.05267  -0.09420 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.39410 0.32206 0.44642 0.13755  0.03294  -0.03628 19  THR A CG2 
33   N N   . PHE A 13  ? 0.32682 0.33438 0.39145 0.12658  -0.01151 -0.02958 20  PHE A N   
34   C CA  . PHE A 13  ? 0.33636 0.35992 0.40688 0.12816  -0.01870 -0.00639 20  PHE A CA  
35   C C   . PHE A 13  ? 0.37052 0.39097 0.45547 0.12121  -0.02060 0.00754  20  PHE A C   
36   O O   . PHE A 13  ? 0.38850 0.39195 0.47541 0.11662  -0.01953 0.00133  20  PHE A O   
37   C CB  . PHE A 13  ? 0.33220 0.36327 0.39455 0.12603  -0.02922 -0.00787 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.33624 0.38339 0.38099 0.13779  -0.03058 -0.02187 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.36712 0.42510 0.41025 0.13396  -0.03479 -0.04905 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.33479 0.39240 0.36381 0.15178  -0.02659 -0.00914 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.36583 0.45465 0.39286 0.14501  -0.03864 -0.06572 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.37904 0.45906 0.38694 0.16725  -0.02895 -0.02128 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.35514 0.45580 0.36243 0.16446  -0.03686 -0.05081 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.33116 0.37205 0.42508 0.11893  -0.02206 0.02498  21  ALA A N   
45   C CA  . ALA A 14  ? 0.39088 0.44563 0.49851 0.11081  -0.02654 0.03529  21  ALA A CA  
46   C C   . ALA A 14  ? 0.44205 0.49107 0.54881 0.09212  -0.03516 0.03383  21  ALA A C   
47   O O   . ALA A 14  ? 0.37192 0.41311 0.46987 0.08788  -0.03317 0.03500  21  ALA A O   
48   C CB  . ALA A 14  ? 0.28132 0.37578 0.40327 0.11594  -0.02157 0.05019  21  ALA A CB  
49   N N   . PHE A 15  ? 0.35783 0.40545 0.46848 0.08381  -0.04167 0.03223  22  PHE A N   
50   C CA  . PHE A 15  ? 0.34980 0.38938 0.45739 0.06545  -0.04713 0.02937  22  PHE A CA  
51   C C   . PHE A 15  ? 0.30468 0.37131 0.42262 0.04853  -0.04443 0.03566  22  PHE A C   
52   O O   . PHE A 15  ? 0.33617 0.44487 0.47013 0.05142  -0.04379 0.04249  22  PHE A O   
53   C CB  . PHE A 15  ? 0.34595 0.38104 0.45290 0.06130  -0.05382 0.02458  22  PHE A CB  
54   C CG  . PHE A 15  ? 0.41421 0.42067 0.51167 0.06687  -0.05410 0.01407  22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.27861 0.26667 0.36585 0.06456  -0.05555 0.00696  22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.32606 0.32514 0.42373 0.07539  -0.04963 0.01139  22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.40730 0.38631 0.49088 0.06990  -0.05652 -0.00476 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.38276 0.36350 0.47626 0.07395  -0.04736 -0.00224 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.28596 0.26485 0.37556 0.07084  -0.05279 -0.01140 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.38678 0.42980 0.49460 0.03098  -0.03984 0.03261  23  GLN A N   
61   C CA  . GLN A 16  ? 0.36624 0.43099 0.48413 0.00334  -0.03429 0.03150  23  GLN A CA  
62   C C   . GLN A 16  ? 0.39394 0.49849 0.52531 -0.00790 -0.04626 0.02427  23  GLN A C   
63   O O   . GLN A 16  ? 0.35244 0.44284 0.47534 0.00031  -0.05514 0.02003  23  GLN A O   
64   C CB  . GLN A 16  ? 0.46971 0.48245 0.56586 -0.01450 -0.02114 0.02777  23  GLN A CB  
65   C CG  . GLN A 16  ? 0.43703 0.41765 0.51534 -0.00181 -0.00544 0.03943  23  GLN A CG  
66   C CD  . GLN A 16  ? 0.48999 0.43246 0.54331 0.02735  -0.00838 0.04156  23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.41498 0.37093 0.47429 0.04265  -0.02317 0.03537  23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.46468 0.36190 0.48850 0.03588  0.00804  0.05039  23  GLN A NE2 
69   N N   . ALA A 17  ? 0.37653 0.53948 0.52906 -0.02573 -0.04596 0.02265  24  ALA A N   
70   C CA  . ALA A 17  ? 0.38152 0.60301 0.54663 -0.02998 -0.05948 0.01694  24  ALA A CA  
71   C C   . ALA A 17  ? 0.43568 0.62875 0.58412 -0.04882 -0.06482 0.00148  24  ALA A C   
72   O O   . ALA A 17  ? 0.36772 0.58267 0.51255 -0.03757 -0.07701 0.00045  24  ALA A O   
73   C CB  . ALA A 17  ? 0.32733 0.62996 0.52035 -0.05185 -0.05813 0.01234  24  ALA A CB  
74   N N   . GLU A 18  ? 0.36341 0.50238 0.49668 -0.07428 -0.05263 -0.00915 25  GLU A N   
75   C CA  . GLU A 18  ? 0.42425 0.52881 0.53762 -0.09124 -0.05388 -0.02535 25  GLU A CA  
76   C C   . GLU A 18  ? 0.48257 0.54877 0.57905 -0.06089 -0.06129 -0.01914 25  GLU A C   
77   O O   . GLU A 18  ? 0.40560 0.48333 0.49541 -0.06040 -0.07097 -0.02646 25  GLU A O   
78   C CB  . GLU A 18  ? 0.48065 0.52063 0.57469 -0.11949 -0.03207 -0.03514 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.63751 0.70868 0.74804 -0.15910 -0.01781 -0.04483 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.66030 0.74447 0.78505 -0.14603 -0.00864 -0.02583 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.67418 0.74212 0.79390 -0.10630 -0.01439 -0.00714 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.77126 0.88577 0.91257 -0.17793 0.00558  -0.03208 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.36710 0.39447 0.45674 -0.03659 -0.05616 -0.00731 26  ILE A N   
84   C CA  . ILE A 19  ? 0.35195 0.35300 0.43082 -0.01290 -0.06119 -0.00540 26  ILE A CA  
85   C C   . ILE A 19  ? 0.40216 0.44076 0.49202 0.00320  -0.07099 0.00076  26  ILE A C   
86   O O   . ILE A 19  ? 0.40268 0.43272 0.48375 0.00978  -0.07469 -0.00216 26  ILE A O   
87   C CB  . ILE A 19  ? 0.39906 0.36785 0.47068 0.00743  -0.05454 0.00165  26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.40566 0.32585 0.45492 0.00190  -0.04126 0.00010  26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.42764 0.38954 0.49723 0.02741  -0.05976 -0.00043 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.63191 0.54623 0.68013 -0.00552 -0.02811 0.00854  26  ILE A CD1 
91   N N   . ALA A 20  ? 0.37797 0.45510 0.48373 0.01230  -0.07174 0.01110  27  ALA A N   
92   C CA  . ALA A 20  ? 0.37246 0.47338 0.48123 0.03511  -0.07470 0.02149  27  ALA A CA  
93   C C   . ALA A 20  ? 0.36521 0.49887 0.46856 0.03191  -0.08335 0.01941  27  ALA A C   
94   O O   . ALA A 20  ? 0.34229 0.46363 0.43311 0.04857  -0.08232 0.02505  27  ALA A O   
95   C CB  . ALA A 20  ? 0.30546 0.44344 0.42925 0.04924  -0.07138 0.03381  27  ALA A CB  
96   N N   . GLN A 21  ? 0.29760 0.47489 0.40842 0.00874  -0.09005 0.00967  28  GLN A N   
97   C CA  . GLN A 21  ? 0.40914 0.63296 0.51359 0.00557  -0.10065 0.00435  28  GLN A CA  
98   C C   . GLN A 21  ? 0.38371 0.56555 0.46655 -0.00838 -0.10136 -0.01028 28  GLN A C   
99   O O   . GLN A 21  ? 0.35275 0.56200 0.42258 -0.00316 -0.10874 -0.01228 28  GLN A O   
100  C CB  . GLN A 21  ? 0.42727 0.72784 0.55050 -0.01907 -0.10777 -0.00719 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.47987 0.76804 0.59781 -0.06396 -0.10654 -0.03483 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.64569 0.98528 0.78762 -0.09882 -0.10298 -0.04866 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.56636 0.92530 0.72827 -0.09048 -0.09749 -0.03580 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.58168 0.94415 0.72119 -0.14080 -0.10366 -0.07740 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.37516 0.49388 0.45069 -0.02128 -0.09276 -0.01907 29  LEU A N   
106  C CA  . LEU A 22  ? 0.42459 0.50024 0.47847 -0.02425 -0.09067 -0.02924 29  LEU A CA  
107  C C   . LEU A 22  ? 0.45008 0.50562 0.49806 0.00350  -0.08804 -0.01661 29  LEU A C   
108  O O   . LEU A 22  ? 0.38172 0.43269 0.41386 0.00764  -0.08870 -0.01948 29  LEU A O   
109  C CB  . LEU A 22  ? 0.39824 0.41437 0.44253 -0.03766 -0.07951 -0.03906 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.53005 0.49898 0.55430 -0.02818 -0.07447 -0.04446 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.43976 0.41365 0.44518 -0.04374 -0.07719 -0.06091 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.64784 0.56194 0.66154 -0.02512 -0.06180 -0.04575 29  LEU A CD2 
113  N N   . MET A 23  ? 0.38177 0.42439 0.44094 0.01997  -0.08238 -0.00469 30  MET A N   
114  C CA  . MET A 23  ? 0.44204 0.46226 0.49668 0.03869  -0.07470 0.00271  30  MET A CA  
115  C C   . MET A 23  ? 0.46000 0.50394 0.50426 0.05456  -0.07400 0.01568  30  MET A C   
116  O O   . MET A 23  ? 0.41390 0.43826 0.44364 0.06152  -0.06667 0.01769  30  MET A O   
117  C CB  . MET A 23  ? 0.36657 0.37224 0.43338 0.04891  -0.06732 0.00797  30  MET A CB  
118  C CG  . MET A 23  ? 0.35039 0.32756 0.41919 0.04523  -0.06392 -0.00331 30  MET A CG  
119  S SD  . MET A 23  ? 0.41898 0.39658 0.49946 0.05188  -0.06097 -0.00134 30  MET A SD  
120  C CE  . MET A 23  ? 0.40642 0.36933 0.48888 0.06077  -0.04841 -0.00457 30  MET A CE  
121  N N   . SER A 24  ? 0.33680 0.42651 0.38664 0.06346  -0.07970 0.02623  31  SER A N   
122  C CA  . SER A 24  ? 0.39850 0.51885 0.43294 0.08738  -0.07901 0.04256  31  SER A CA  
123  C C   . SER A 24  ? 0.38937 0.53341 0.40629 0.07841  -0.08857 0.03328  31  SER A C   
124  O O   . SER A 24  ? 0.45001 0.59733 0.44397 0.09977  -0.08337 0.04637  31  SER A O   
125  C CB  . SER A 24  ? 0.33646 0.51721 0.38264 0.10277  -0.08489 0.05497  31  SER A CB  
126  O OG  . SER A 24  ? 0.63958 0.89086 0.68980 0.08835  -0.10220 0.04423  31  SER A OG  
127  N N   . LEU A 25  ? 0.42447 0.58016 0.44718 0.04763  -0.09925 0.01070  32  LEU A N   
128  C CA  . LEU A 25  ? 0.36619 0.53791 0.36887 0.03536  -0.10648 -0.00395 32  LEU A CA  
129  C C   . LEU A 25  ? 0.44063 0.55533 0.42469 0.04066  -0.09515 -0.00449 32  LEU A C   
130  O O   . LEU A 25  ? 0.47533 0.60144 0.43548 0.04976  -0.09518 -0.00269 32  LEU A O   
131  C CB  . LEU A 25  ? 0.38192 0.56290 0.39166 -0.00278 -0.11354 -0.03129 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.52808 0.74311 0.51796 -0.02193 -0.12257 -0.05343 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.62068 0.93470 0.61959 -0.02483 -0.13799 -0.05687 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.56910 0.73687 0.55335 -0.05868 -0.11603 -0.08155 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.38949 0.45066 0.38408 0.03641  -0.08508 -0.00726 33  ILE A N   
136  C CA  . ILE A 26  ? 0.45813 0.47793 0.44168 0.04079  -0.07324 -0.00933 33  ILE A CA  
137  C C   . ILE A 26  ? 0.43719 0.44814 0.41191 0.06342  -0.05930 0.01087  33  ILE A C   
138  O O   . ILE A 26  ? 0.41733 0.41169 0.37470 0.06825  -0.04872 0.01240  33  ILE A O   
139  C CB  . ILE A 26  ? 0.46574 0.44840 0.46492 0.03303  -0.06770 -0.01894 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.44129 0.41222 0.43446 0.01537  -0.07270 -0.03681 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.43405 0.39081 0.43214 0.03990  -0.05392 -0.01973 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.45974 0.40134 0.46367 0.01571  -0.06780 -0.04053 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.45442 0.47124 0.43716 0.07828  -0.05506 0.02722  34  ILE A N   
144  C CA  . ILE A 27  ? 0.50802 0.49895 0.47642 0.10034  -0.03407 0.04736  34  ILE A CA  
145  C C   . ILE A 27  ? 0.53143 0.55106 0.46906 0.12446  -0.03376 0.06601  34  ILE A C   
146  O O   . ILE A 27  ? 0.69251 0.68180 0.60533 0.13929  -0.01332 0.08003  34  ILE A O   
147  C CB  . ILE A 27  ? 0.59310 0.57048 0.57535 0.11046  -0.02540 0.05713  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.44697 0.39738 0.45362 0.08979  -0.02313 0.03834  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.67038 0.61252 0.62923 0.13652  0.00155  0.08026  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.58198 0.48545 0.58734 0.08632  0.00220  0.03510  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.56496 0.64794 0.50232 0.12859  -0.05481 0.06583  35  ASN A N   
152  C CA  . ASN A 28  ? 0.65188 0.78134 0.56032 0.15968  -0.05710 0.08588  35  ASN A CA  
153  C C   . ASN A 28  ? 0.70518 0.87179 0.59209 0.15114  -0.07058 0.07242  35  ASN A C   
154  O O   . ASN A 28  ? 0.72761 0.92712 0.58187 0.18099  -0.06904 0.09044  35  ASN A O   
155  C CB  . ASN A 28  ? 0.60007 0.79818 0.52230 0.17453  -0.07189 0.09401  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.68614 0.84946 0.62540 0.18671  -0.05751 0.10733  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.77951 0.87427 0.70528 0.20118  -0.03130 0.12179  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.62059 0.83008 0.58846 0.17815  -0.07189 0.10021  35  ASN A ND2 
159  N N   . THR A 29  ? 0.58190 0.74208 0.48094 0.11488  -0.08148 0.04212  36  THR A N   
160  C CA  . THR A 29  ? 0.66587 0.85877 0.54213 0.10351  -0.09315 0.02391  36  THR A CA  
161  C C   . THR A 29  ? 0.60270 0.75078 0.44967 0.11453  -0.07500 0.03119  36  THR A C   
162  O O   . THR A 29  ? 0.50839 0.59403 0.36528 0.10880  -0.05694 0.03247  36  THR A O   
163  C CB  . THR A 29  ? 0.75542 0.94350 0.64912 0.06181  -0.10473 -0.01128 36  THR A CB  
164  O OG1 . THR A 29  ? 0.59407 0.82631 0.51411 0.04784  -0.11805 -0.01843 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.66011 0.87360 0.52597 0.04688  -0.11333 -0.03523 36  THR A CG2 
166  N N   . PHE A 30  ? 0.57087 0.75931 0.38179 0.13015  -0.07948 0.03474  37  PHE A N   
167  C CA  . PHE A 30  ? 0.61945 0.77253 0.39777 0.14070  -0.06132 0.04142  37  PHE A CA  
168  C C   . PHE A 30  ? 0.66449 0.79343 0.44684 0.10768  -0.06461 0.00774  37  PHE A C   
169  O O   . PHE A 30  ? 0.70832 0.87629 0.47721 0.09175  -0.08163 -0.01748 37  PHE A O   
170  C CB  . PHE A 30  ? 0.62404 0.83385 0.35690 0.17300  -0.06547 0.05764  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.74786 0.92261 0.44160 0.18680  -0.04379 0.06789  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.77733 0.89137 0.45713 0.21043  -0.01008 0.10053  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.73425 0.93396 0.40289 0.17420  -0.05351 0.04340  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.76808 0.85003 0.41222 0.22075  0.01405  0.11065  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.72325 0.89331 0.35482 0.18828  -0.03178 0.05369  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.74677 0.85966 0.36729 0.21145  0.00226  0.08847  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.56277 0.62998 0.36227 0.09800  -0.04673 0.00552  38  TYR A N   
178  C CA  . TYR A 31  ? 0.63076 0.67139 0.43338 0.07533  -0.04596 -0.02232 38  TYR A CA  
179  C C   . TYR A 31  ? 0.61728 0.61437 0.42029 0.08196  -0.02010 -0.01378 38  TYR A C   
180  O O   . TYR A 31  ? 0.52715 0.49743 0.35773 0.08124  -0.00757 -0.00455 38  TYR A O   
181  C CB  . TYR A 31  ? 0.58562 0.61190 0.42139 0.05235  -0.05610 -0.04068 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.57493 0.56851 0.40716 0.03597  -0.05256 -0.06664 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.62090 0.62415 0.42888 0.01950  -0.06130 -0.09238 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.54475 0.50000 0.39606 0.03817  -0.03877 -0.06696 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.74472 0.70531 0.54273 0.00889  -0.05255 -0.11473 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.61776 0.54392 0.46197 0.03238  -0.03321 -0.08688 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.68802 0.60949 0.50329 0.01934  -0.03827 -0.10919 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.80104 0.68119 0.60282 0.01778  -0.02738 -0.12761 38  TYR A OH  
189  N N   . SER A 32  ? 0.58100 0.57630 0.35399 0.08604  -0.01116 -0.01976 39  SER A N   
190  C CA  . SER A 32  ? 0.65237 0.61777 0.42307 0.09279  0.01695  -0.00950 39  SER A CA  
191  C C   . SER A 32  ? 0.69956 0.64210 0.50096 0.07812  0.02411  -0.02875 39  SER A C   
192  O O   . SER A 32  ? 0.61407 0.54113 0.43405 0.07705  0.04603  -0.02244 39  SER A O   
193  C CB  . SER A 32  ? 0.64524 0.62213 0.36925 0.10624  0.02597  -0.00627 39  SER A CB  
194  O OG  . SER A 32  ? 0.70086 0.69809 0.39325 0.13008  0.02794  0.02088  39  SER A OG  
195  N N   . ASN A 33  ? 0.62472 0.56639 0.43015 0.06753  0.00870  -0.05254 40  ASN A N   
196  C CA  . ASN A 33  ? 0.65885 0.58249 0.48496 0.06382  0.01625  -0.06826 40  ASN A CA  
197  C C   . ASN A 33  ? 0.59408 0.51394 0.46220 0.05901  0.01277  -0.06531 40  ASN A C   
198  O O   . ASN A 33  ? 0.66009 0.57047 0.53898 0.05533  0.00217  -0.07646 40  ASN A O   
199  C CB  . ASN A 33  ? 0.59048 0.50081 0.39400 0.05912  0.00775  -0.09232 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.66536 0.55576 0.48010 0.06649  0.01957  -0.10464 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.63370 0.53463 0.46123 0.07602  0.03605  -0.10025 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.58312 0.44610 0.39179 0.06342  0.01394  -0.11967 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.43587 0.38917 0.33794 -0.01528 -0.06497 -0.02103 41  LYS A N   
204  C CA  . LYS A 34  ? 0.47742 0.47543 0.42605 -0.01739 -0.04644 -0.01254 41  LYS A CA  
205  C C   . LYS A 34  ? 0.49068 0.47406 0.43644 -0.00794 -0.03322 -0.02728 41  LYS A C   
206  O O   . LYS A 34  ? 0.40783 0.41545 0.38289 -0.01269 -0.02624 -0.02121 41  LYS A O   
207  C CB  . LYS A 34  ? 0.42813 0.46274 0.39766 -0.00472 -0.02040 -0.00698 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.46465 0.52957 0.44637 -0.00969 -0.02868 0.01384  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.43947 0.52465 0.42649 0.00947  -0.00236 0.01657  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.37853 0.49975 0.37712 0.01068  -0.00793 0.04047  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.34899 0.52200 0.38232 0.00854  -0.00975 0.06969  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.38464 0.33268 0.29421 0.00881  -0.02879 -0.04333 42  GLU A N   
213  C CA  . GLU A 35  ? 0.36513 0.31282 0.27713 0.02150  -0.01291 -0.05164 42  GLU A CA  
214  C C   . GLU A 35  ? 0.44922 0.38270 0.36406 0.01100  -0.02777 -0.05150 42  GLU A C   
215  O O   . GLU A 35  ? 0.37317 0.31946 0.30325 0.01716  -0.01453 -0.05420 42  GLU A O   
216  C CB  . GLU A 35  ? 0.46279 0.38259 0.33178 0.04863  -0.00460 -0.06135 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.53545 0.38877 0.34166 0.05658  -0.03055 -0.07039 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.57995 0.40306 0.33052 0.09517  -0.01834 -0.07800 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.65297 0.50863 0.41464 0.10759  0.00328  -0.07272 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.75720 0.52169 0.44787 0.11627  -0.03001 -0.08712 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.37915 0.28707 0.28027 -0.00767 -0.05783 -0.04514 43  ILE A N   
222  C CA  . ILE A 36  ? 0.40078 0.28887 0.30032 -0.02048 -0.07579 -0.04207 43  ILE A CA  
223  C C   . ILE A 36  ? 0.46783 0.40986 0.42230 -0.03029 -0.06216 -0.02963 43  ILE A C   
224  O O   . ILE A 36  ? 0.42401 0.35773 0.38287 -0.03749 -0.07041 -0.02689 43  ILE A O   
225  C CB  . ILE A 36  ? 0.45167 0.29875 0.32427 -0.04658 -0.11841 -0.03108 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.46701 0.36894 0.38414 -0.06986 -0.12590 -0.00554 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.53279 0.30236 0.32832 -0.03154 -0.13645 -0.04767 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.52543 0.47048 0.48966 -0.09629 -0.13836 0.02324  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.30234 0.29219 0.29019 -0.02743 -0.04215 -0.02188 44  PHE A N   
230  C CA  . PHE A 37  ? 0.34736 0.37614 0.37019 -0.02738 -0.02740 -0.01229 44  PHE A CA  
231  C C   . PHE A 37  ? 0.32303 0.34132 0.34349 -0.01777 -0.01566 -0.02602 44  PHE A C   
232  O O   . PHE A 37  ? 0.30041 0.33049 0.33686 -0.02165 -0.01548 -0.02003 44  PHE A O   
233  C CB  . PHE A 37  ? 0.23211 0.29141 0.26781 -0.01684 -0.00796 -0.00643 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.29327 0.34143 0.31818 -0.00358 0.01080  -0.02219 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.31574 0.34984 0.32325 0.00212  0.01422  -0.03067 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.33038 0.38197 0.36104 0.00107  0.02195  -0.02470 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.27401 0.30688 0.27853 0.00904  0.02869  -0.03649 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.23651 0.27827 0.25934 0.00471  0.03151  -0.03261 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.30158 0.33858 0.31557 0.00710  0.03503  -0.03605 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.30281 0.30544 0.30537 -0.00422 -0.00556 -0.04018 45  LEU A N   
241  C CA  . LEU A 38  ? 0.36876 0.37406 0.37525 0.00451  0.00516  -0.04650 45  LEU A CA  
242  C C   . LEU A 38  ? 0.36846 0.34749 0.35945 0.00584  -0.00766 -0.04989 45  LEU A C   
243  O O   . LEU A 38  ? 0.32686 0.31533 0.33120 0.00628  -0.00387 -0.04928 45  LEU A O   
244  C CB  . LEU A 38  ? 0.31949 0.32913 0.31677 0.01918  0.01919  -0.05052 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.38204 0.41288 0.39454 0.02480  0.03023  -0.04750 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.21454 0.25989 0.25015 0.00988  0.03039  -0.04348 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.32264 0.37402 0.33551 0.03603  0.04382  -0.04036 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.33472 0.27205 0.28984 0.00664  -0.02589 -0.05345 46  ARG A N   
249  C CA  . ARG A 39  ? 0.40138 0.29517 0.32709 0.00784  -0.04355 -0.05672 46  ARG A CA  
250  C C   . ARG A 39  ? 0.45016 0.35885 0.40548 -0.01607 -0.05602 -0.04339 46  ARG A C   
251  O O   . ARG A 39  ? 0.41985 0.31892 0.37387 -0.01352 -0.05762 -0.04423 46  ARG A O   
252  C CB  . ARG A 39  ? 0.43098 0.25876 0.29719 0.01039  -0.06869 -0.06258 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.62147 0.38513 0.44619 0.00266  -0.09874 -0.06296 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.58308 0.26469 0.33595 0.00003  -0.13284 -0.06806 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.68981 0.38120 0.46579 -0.04192 -0.16251 -0.04915 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.91791 0.56972 0.65599 -0.05241 -0.18858 -0.04798 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.89391 0.48502 0.56089 -0.02085 -0.18789 -0.06785 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.83925 0.51707 0.61082 -0.09350 -0.21593 -0.02270 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.36982 0.30837 0.35318 -0.03632 -0.06300 -0.02710 47  GLU A N   
260  C CA  . GLU A 40  ? 0.35782 0.32211 0.37181 -0.05606 -0.07312 -0.00584 47  GLU A CA  
261  C C   . GLU A 40  ? 0.36831 0.36965 0.41064 -0.04485 -0.04923 -0.00592 47  GLU A C   
262  O O   . GLU A 40  ? 0.38681 0.39166 0.43920 -0.05114 -0.05457 0.00303  47  GLU A O   
263  C CB  . GLU A 40  ? 0.30401 0.30694 0.34460 -0.07357 -0.08186 0.01920  47  GLU A CB  
264  C CG  . GLU A 40  ? 0.38205 0.34720 0.39418 -0.09164 -0.11347 0.02367  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.59158 0.48956 0.56410 -0.10937 -0.14949 0.02350  47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.46968 0.37816 0.46163 -0.12383 -0.15819 0.03966  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.64931 0.47695 0.56349 -0.10668 -0.17024 0.00769  47  GLU A OE2 
268  N N   . LEU A 41  ? 0.32638 0.34915 0.37639 -0.02981 -0.02622 -0.01477 48  LEU A N   
269  C CA  . LEU A 41  ? 0.30458 0.34838 0.36872 -0.02090 -0.00998 -0.01541 48  LEU A CA  
270  C C   . LEU A 41  ? 0.36857 0.39495 0.42414 -0.01442 -0.00874 -0.02793 48  LEU A C   
271  O O   . LEU A 41  ? 0.35486 0.38849 0.41908 -0.01420 -0.00765 -0.02415 48  LEU A O   
272  C CB  . LEU A 41  ? 0.30945 0.36487 0.37238 -0.01093 0.00611  -0.01975 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.32880 0.40595 0.39742 -0.00862 0.00988  -0.00469 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.35214 0.42366 0.40551 0.00465  0.02406  -0.01076 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.19997 0.30717 0.28573 -0.00836 0.00903  0.01863  48  LEU A CD2 
276  N N   . ILE A 42  ? 0.33986 0.34764 0.37740 -0.00516 -0.00728 -0.03977 49  ILE A N   
277  C CA  . ILE A 42  ? 0.35155 0.35082 0.38065 0.00714  -0.00438 -0.04587 49  ILE A CA  
278  C C   . ILE A 42  ? 0.43939 0.40971 0.45445 0.00378  -0.01995 -0.04381 49  ILE A C   
279  O O   . ILE A 42  ? 0.38677 0.36110 0.40713 0.00859  -0.01777 -0.04321 49  ILE A O   
280  C CB  . ILE A 42  ? 0.33668 0.32705 0.34441 0.02588  0.00283  -0.05210 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.31206 0.33818 0.34077 0.02538  0.01751  -0.04831 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.35510 0.33441 0.34501 0.04719  0.00549  -0.05361 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.34603 0.37972 0.36152 0.04564  0.02843  -0.04621 49  ILE A CD1 
284  N N   . SER A 43  ? 0.30487 0.24267 0.29995 -0.00750 -0.03956 -0.04038 50  SER A N   
285  C CA  . SER A 43  ? 0.47840 0.38048 0.45678 -0.01840 -0.06155 -0.03388 50  SER A CA  
286  C C   . SER A 43  ? 0.40448 0.34543 0.42190 -0.03308 -0.05965 -0.01720 50  SER A C   
287  O O   . SER A 43  ? 0.42812 0.35436 0.44100 -0.03465 -0.06697 -0.01334 50  SER A O   
288  C CB  . SER A 43  ? 0.38824 0.24554 0.33674 -0.03640 -0.09095 -0.02806 50  SER A CB  
289  O OG  . SER A 43  ? 0.49567 0.32449 0.43674 -0.05886 -0.11834 -0.01302 50  SER A OG  
290  N N   . ASN A 44  ? 0.35140 0.33968 0.40138 -0.03914 -0.04869 -0.00576 51  ASN A N   
291  C CA  . ASN A 44  ? 0.32239 0.34923 0.40083 -0.04217 -0.04146 0.01162  51  ASN A CA  
292  C C   . ASN A 44  ? 0.37408 0.40478 0.45199 -0.02624 -0.02655 -0.00069 51  ASN A C   
293  O O   . ASN A 44  ? 0.32494 0.36300 0.41034 -0.02690 -0.02755 0.00852  51  ASN A O   
294  C CB  . ASN A 44  ? 0.29228 0.36250 0.39125 -0.03985 -0.02924 0.02613  51  ASN A CB  
295  C CG  . ASN A 44  ? 0.41076 0.50316 0.52769 -0.05978 -0.04578 0.05564  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.39319 0.45757 0.50244 -0.08168 -0.07232 0.06328  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.22412 0.36459 0.36087 -0.05198 -0.03270 0.07560  51  ASN A ND2 
298  N N   . SER A 45  ? 0.32401 0.35281 0.39455 -0.01415 -0.01486 -0.01766 52  SER A N   
299  C CA  . SER A 45  ? 0.32950 0.36406 0.40117 -0.00462 -0.00696 -0.02490 52  SER A CA  
300  C C   . SER A 45  ? 0.33733 0.35234 0.39907 0.00062  -0.01395 -0.02786 52  SER A C   
301  O O   . SER A 45  ? 0.32501 0.34695 0.39197 0.00381  -0.01288 -0.02533 52  SER A O   
302  C CB  . SER A 45  ? 0.23874 0.28073 0.30929 0.00047  0.00155  -0.03390 52  SER A CB  
303  O OG  . SER A 45  ? 0.42548 0.47464 0.49562 -0.00195 0.00671  -0.03196 52  SER A OG  
304  N N   . SER A 46  ? 0.36016 0.34367 0.39888 0.00527  -0.02186 -0.03334 53  SER A N   
305  C CA  . SER A 46  ? 0.33628 0.28761 0.35002 0.01798  -0.02866 -0.03658 53  SER A CA  
306  C C   . SER A 46  ? 0.47071 0.40601 0.48482 0.00421  -0.04311 -0.02582 53  SER A C   
307  O O   . SER A 46  ? 0.40936 0.33422 0.41537 0.01390  -0.04387 -0.02580 53  SER A O   
308  C CB  . SER A 46  ? 0.37886 0.28170 0.34832 0.03113  -0.03691 -0.04492 53  SER A CB  
309  O OG  . SER A 46  ? 0.47482 0.33728 0.40584 0.05355  -0.04123 -0.04880 53  SER A OG  
310  N N   . ASP A 47  ? 0.36404 0.30378 0.39057 -0.01835 -0.05455 -0.01185 54  ASP A N   
311  C CA  . ASP A 47  ? 0.39413 0.33054 0.42867 -0.03500 -0.06879 0.00738  54  ASP A CA  
312  C C   . ASP A 47  ? 0.34822 0.32828 0.41014 -0.02806 -0.05219 0.01411  54  ASP A C   
313  O O   . ASP A 47  ? 0.30400 0.27515 0.36353 -0.02844 -0.05755 0.02135  54  ASP A O   
314  C CB  . ASP A 47  ? 0.37615 0.32401 0.42600 -0.06183 -0.08510 0.03054  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.55061 0.43657 0.56132 -0.07535 -0.11359 0.02727  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.58494 0.40986 0.54748 -0.05886 -0.12011 0.00730  54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.47722 0.37366 0.50015 -0.09981 -0.13046 0.04666  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.28369 0.30214 0.36306 -0.02031 -0.03414 0.01164  55  ALA A N   
319  C CA  . ALA A 48  ? 0.33066 0.37535 0.41936 -0.01013 -0.02168 0.01575  55  ALA A CA  
320  C C   . ALA A 48  ? 0.34576 0.37859 0.42482 0.00117  -0.01996 0.00180  55  ALA A C   
321  O O   . ALA A 48  ? 0.29656 0.33720 0.37709 0.00615  -0.01813 0.00758  55  ALA A O   
322  C CB  . ALA A 48  ? 0.25046 0.31657 0.34015 -0.00140 -0.00777 0.01330  55  ALA A CB  
323  N N   . LEU A 49  ? 0.33812 0.35804 0.40794 0.00778  -0.01964 -0.01264 56  LEU A N   
324  C CA  . LEU A 49  ? 0.30968 0.33192 0.37615 0.02079  -0.01725 -0.01828 56  LEU A CA  
325  C C   . LEU A 49  ? 0.29134 0.28500 0.34191 0.02662  -0.02595 -0.01470 56  LEU A C   
326  O O   . LEU A 49  ? 0.27141 0.27277 0.32381 0.03495  -0.02470 -0.01225 56  LEU A O   
327  C CB  . LEU A 49  ? 0.30177 0.33177 0.36639 0.03072  -0.01129 -0.02575 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.28722 0.34409 0.36656 0.02297  -0.00591 -0.02672 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.26437 0.32897 0.34331 0.02953  -0.00012 -0.02872 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.21257 0.29159 0.30205 0.02085  -0.00840 -0.02194 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.32050 0.27396 0.34951 0.02120  -0.03837 -0.01357 57  ASP A N   
332  C CA  . ASP A 50  ? 0.49214 0.40103 0.49453 0.02299  -0.05297 -0.00869 57  ASP A CA  
333  C C   . ASP A 50  ? 0.42787 0.35544 0.45093 0.00989  -0.05579 0.00770  57  ASP A C   
334  O O   . ASP A 50  ? 0.37494 0.28483 0.38562 0.01764  -0.06004 0.01091  57  ASP A O   
335  C CB  . ASP A 50  ? 0.44519 0.29576 0.41317 0.01077  -0.07487 -0.00741 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.60152 0.41452 0.52793 0.03493  -0.07314 -0.02412 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.64368 0.47160 0.56422 0.06524  -0.05626 -0.03148 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.66477 0.43696 0.56371 0.02509  -0.08890 -0.02639 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.33352 0.29854 0.38501 -0.00517 -0.05146 0.02053  58  LYS A N   
340  C CA  . LYS A 51  ? 0.37517 0.36450 0.44417 -0.01217 -0.05091 0.04190  58  LYS A CA  
341  C C   . LYS A 51  ? 0.28494 0.29182 0.35488 0.00610  -0.03854 0.03504  58  LYS A C   
342  O O   . LYS A 51  ? 0.37685 0.37810 0.44389 0.00779  -0.04248 0.04518  58  LYS A O   
343  C CB  . LYS A 51  ? 0.38079 0.41328 0.47456 -0.02071 -0.04345 0.06024  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.46740 0.50879 0.57712 -0.04502 -0.05928 0.09409  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.50459 0.59048 0.63811 -0.05119 -0.05295 0.11274  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.71976 0.77633 0.84602 -0.07193 -0.07281 0.10867  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.62045 0.72821 0.77652 -0.08301 -0.07152 0.13771  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.32234 0.34748 0.39415 0.01711  -0.02715 0.01990  59  ILE A N   
349  C CA  . ILE A 52  ? 0.32996 0.36882 0.39932 0.02901  -0.02206 0.01603  59  ILE A CA  
350  C C   . ILE A 52  ? 0.29077 0.31775 0.35353 0.03893  -0.02647 0.01013  59  ILE A C   
351  O O   . ILE A 52  ? 0.33153 0.36435 0.39213 0.04629  -0.02722 0.01416  59  ILE A O   
352  C CB  . ILE A 52  ? 0.36187 0.41398 0.42871 0.03126  -0.01686 0.00574  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.39091 0.44659 0.44535 0.03881  -0.01917 0.00501  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.23453 0.28759 0.30665 0.02934  -0.01780 -0.00577 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.32493 0.38144 0.36740 0.04789  -0.01456 0.01816  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.31734 0.32746 0.37203 0.04425  -0.02829 0.00233  60  ARG A N   
357  C CA  . ARG A 53  ? 0.32910 0.32874 0.37045 0.06370  -0.02895 0.00065  60  ARG A CA  
358  C C   . ARG A 53  ? 0.37603 0.33838 0.39748 0.06545  -0.03839 0.00840  60  ARG A C   
359  O O   . ARG A 53  ? 0.35594 0.32098 0.37238 0.07986  -0.03769 0.01184  60  ARG A O   
360  C CB  . ARG A 53  ? 0.35994 0.34428 0.38466 0.07835  -0.02604 -0.00679 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.41626 0.38540 0.41569 0.10976  -0.02347 -0.00505 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.52782 0.48470 0.50259 0.13465  -0.01617 -0.00950 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.77174 0.67274 0.71594 0.12387  -0.02678 -0.01872 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.78882 0.62687 0.67537 0.14796  -0.03208 -0.02501 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.72862 0.55103 0.57794 0.19140  -0.02341 -0.02283 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.65075 0.43701 0.51007 0.13096  -0.04763 -0.03195 60  ARG A NH2 
367  N N   . TYR A 54  ? 0.40537 0.33348 0.41594 0.04817  -0.05008 0.01476  61  TYR A N   
368  C CA  . TYR A 54  ? 0.47514 0.36212 0.46553 0.04215  -0.06501 0.02728  61  TYR A CA  
369  C C   . TYR A 54  ? 0.40931 0.33121 0.42274 0.03796  -0.05987 0.04175  61  TYR A C   
370  O O   . TYR A 54  ? 0.45877 0.36226 0.45817 0.04675  -0.06429 0.04739  61  TYR A O   
371  C CB  . TYR A 54  ? 0.46168 0.31115 0.44114 0.01519  -0.08499 0.03843  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.52935 0.33692 0.49157 -0.00158 -0.10681 0.05894  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.56754 0.41416 0.56528 -0.02613 -0.10971 0.08796  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.63394 0.36127 0.53969 0.00978  -0.12470 0.05284  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.68767 0.50142 0.67451 -0.04614 -0.13182 0.11334  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.82164 0.50044 0.70597 -0.00958 -0.14954 0.07341  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.62750 0.35325 0.55728 -0.04119 -0.15400 0.10510  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.84860 0.53182 0.76214 -0.06503 -0.18069 0.13199  61  TYR A OH  
379  N N   . GLU A 55  ? 0.34287 0.31077 0.38433 0.02917  -0.04990 0.04847  62  GLU A N   
380  C CA  . GLU A 55  ? 0.36024 0.35748 0.41273 0.03248  -0.04309 0.06280  62  GLU A CA  
381  C C   . GLU A 55  ? 0.43797 0.44425 0.48352 0.05206  -0.03774 0.05095  62  GLU A C   
382  O O   . GLU A 55  ? 0.44803 0.45851 0.49009 0.05837  -0.03758 0.06128  62  GLU A O   
383  C CB  . GLU A 55  ? 0.30597 0.34203 0.37406 0.03022  -0.03142 0.07127  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.34358 0.39183 0.42856 0.01120  -0.03580 0.09703  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.47090 0.56483 0.56657 0.02102  -0.01896 0.11200  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.47568 0.57594 0.55394 0.04294  -0.00693 0.09978  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.52828 0.64894 0.64445 0.00854  -0.01951 0.13820  62  GLU A OE2 
388  N N   . SER A 56  ? 0.38191 0.39612 0.42774 0.06028  -0.03481 0.03372  63  SER A N   
389  C CA  . SER A 56  ? 0.49980 0.53227 0.54560 0.07386  -0.03424 0.02924  63  SER A CA  
390  C C   . SER A 56  ? 0.51722 0.53178 0.55065 0.08983  -0.03758 0.03275  63  SER A C   
391  O O   . SER A 56  ? 0.53051 0.56620 0.56677 0.10180  -0.03788 0.03513  63  SER A O   
392  C CB  . SER A 56  ? 0.39660 0.45243 0.45314 0.07357  -0.03280 0.01938  63  SER A CB  
393  O OG  . SER A 56  ? 0.48346 0.53147 0.53774 0.08378  -0.03029 0.01593  63  SER A OG  
394  N N   . LEU A 57  ? 0.53623 0.50682 0.54981 0.09092  -0.04292 0.03432  64  LEU A N   
395  C CA  . LEU A 57  ? 0.58946 0.52660 0.57583 0.11131  -0.04736 0.03742  64  LEU A CA  
396  C C   . LEU A 57  ? 0.53085 0.46678 0.51687 0.10887  -0.05110 0.05060  64  LEU A C   
397  O O   . LEU A 57  ? 0.59927 0.53496 0.57454 0.12944  -0.05031 0.05338  64  LEU A O   
398  C CB  . LEU A 57  ? 0.54001 0.40798 0.48709 0.11182  -0.05891 0.03496  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.56320 0.41982 0.49520 0.12458  -0.05481 0.02189  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.59439 0.36040 0.46461 0.13274  -0.07144 0.01869  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.63850 0.54285 0.58116 0.15599  -0.03866 0.01982  64  LEU A CD2 
402  N N   . THR A 58  ? 0.57822 0.51898 0.57646 0.08693  -0.05363 0.06261  65  THR A N   
403  C CA  . THR A 58  ? 0.64360 0.58995 0.64297 0.08551  -0.05475 0.07992  65  THR A CA  
404  C C   . THR A 58  ? 0.58637 0.58076 0.60097 0.09049  -0.04423 0.08032  65  THR A C   
405  O O   . THR A 58  ? 0.62618 0.62856 0.63707 0.09577  -0.04276 0.09379  65  THR A O   
406  C CB  . THR A 58  ? 0.52995 0.45694 0.53165 0.06083  -0.06467 0.10307  65  THR A CB  
407  O OG1 . THR A 58  ? 0.56377 0.52674 0.58998 0.04666  -0.05763 0.10857  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.63757 0.49585 0.60831 0.05195  -0.08426 0.10190  65  THR A CG2 
409  N N   . ASP A 59  ? 0.59608 0.61421 0.61952 0.08988  -0.03921 0.06639  66  ASP A N   
410  C CA  . ASP A 59  ? 0.50454 0.54707 0.52399 0.09499  -0.03548 0.06431  66  ASP A CA  
411  C C   . ASP A 59  ? 0.53701 0.59191 0.56033 0.09269  -0.03923 0.04758  66  ASP A C   
412  O O   . ASP A 59  ? 0.46676 0.52320 0.49238 0.08418  -0.03659 0.04089  66  ASP A O   
413  C CB  . ASP A 59  ? 0.51297 0.56425 0.53026 0.09199  -0.02675 0.07684  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.64970 0.70735 0.64058 0.10782  -0.02333 0.07678  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.70002 0.75273 0.67640 0.11466  -0.03237 0.06843  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.65934 0.72484 0.63866 0.11601  -0.01266 0.08708  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.49081 0.55936 0.51726 0.09911  -0.04654 0.04505  67  PRO A N   
418  C CA  . PRO A 60  ? 0.49136 0.58182 0.52972 0.09170  -0.05330 0.03831  67  PRO A CA  
419  C C   . PRO A 60  ? 0.53033 0.61500 0.55108 0.08024  -0.06297 0.03271  67  PRO A C   
420  O O   . PRO A 60  ? 0.45264 0.54679 0.48128 0.06724  -0.07035 0.02859  67  PRO A O   
421  C CB  . PRO A 60  ? 0.47818 0.59588 0.52722 0.10213  -0.06014 0.04742  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.47489 0.57286 0.51431 0.11925  -0.05298 0.05304  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.48684 0.55716 0.51019 0.11300  -0.04933 0.05342  67  PRO A CD  
424  N N   . SER A 61  ? 0.44564 0.50960 0.43554 0.08722  -0.06395 0.03400  68  SER A N   
425  C CA  . SER A 61  ? 0.58748 0.62612 0.53894 0.08403  -0.07528 0.02703  68  SER A CA  
426  C C   . SER A 61  ? 0.53232 0.55786 0.47789 0.08070  -0.06592 0.02012  68  SER A C   
427  O O   . SER A 61  ? 0.45032 0.44617 0.35893 0.07783  -0.07735 0.01238  68  SER A O   
428  C CB  . SER A 61  ? 0.50530 0.51998 0.41303 0.10323  -0.07458 0.03142  68  SER A CB  
429  O OG  . SER A 61  ? 0.62585 0.64527 0.53695 0.11772  -0.05166 0.04141  68  SER A OG  
430  N N   . LYS A 62  ? 0.47972 0.52015 0.45480 0.08059  -0.04873 0.02359  69  LYS A N   
431  C CA  . LYS A 62  ? 0.47497 0.51013 0.45014 0.07683  -0.04010 0.01955  69  LYS A CA  
432  C C   . LYS A 62  ? 0.46235 0.49937 0.44857 0.06008  -0.04995 0.00892  69  LYS A C   
433  O O   . LYS A 62  ? 0.44579 0.47465 0.42762 0.05673  -0.04484 0.00414  69  LYS A O   
434  C CB  . LYS A 62  ? 0.41729 0.46718 0.42160 0.07521  -0.02613 0.02968  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.44125 0.49759 0.44222 0.08638  -0.01760 0.04904  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.44523 0.51695 0.46583 0.08084  -0.00751 0.06655  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.41346 0.50261 0.43979 0.08695  -0.00118 0.09531  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.40771 0.52723 0.45324 0.08333  0.00850  0.12299  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.44252 0.49678 0.44570 0.05046  -0.06315 0.00980  70  LEU A N   
440  C CA  . LEU A 63  ? 0.43683 0.50424 0.45492 0.03293  -0.07424 0.00853  70  LEU A CA  
441  C C   . LEU A 63  ? 0.53267 0.58103 0.52184 0.01779  -0.10174 0.00992  70  LEU A C   
442  O O   . LEU A 63  ? 0.39686 0.46215 0.40256 -0.00329 -0.11738 0.01661  70  LEU A O   
443  C CB  . LEU A 63  ? 0.41350 0.52444 0.47364 0.03440  -0.06978 0.01768  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.50952 0.62007 0.58283 0.04772  -0.05011 0.01459  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.49860 0.64093 0.59457 0.06016  -0.04533 0.02371  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.30966 0.40650 0.38099 0.04017  -0.04321 0.00607  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.43057 0.44118 0.37270 0.02744  -0.11062 0.00663  71  ASP A N   
448  C CA  . ASP A 64  ? 0.53305 0.50195 0.42718 0.01260  -0.14372 0.00566  71  ASP A CA  
449  C C   . ASP A 64  ? 0.54944 0.47656 0.41126 0.00076  -0.15374 -0.00254 71  ASP A C   
450  O O   . ASP A 64  ? 0.63887 0.53766 0.47570 -0.02542 -0.18811 0.00112  71  ASP A O   
451  C CB  . ASP A 64  ? 0.51321 0.43545 0.34568 0.03470  -0.14811 0.00107  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.57804 0.53487 0.43541 0.04145  -0.14676 0.01093  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.50117 0.51350 0.41692 0.02877  -0.14722 0.02198  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.54869 0.47770 0.36377 0.06385  -0.14353 0.00957  71  ASP A OD2 
455  N N   . SER A 65  ? 0.52424 0.44592 0.38517 0.01732  -0.12736 -0.01059 72  SER A N   
456  C CA  . SER A 65  ? 0.53859 0.42225 0.36944 0.01125  -0.13215 -0.01820 72  SER A CA  
457  C C   . SER A 65  ? 0.59240 0.51858 0.47961 -0.01533 -0.13371 -0.01213 72  SER A C   
458  O O   . SER A 65  ? 0.58464 0.48768 0.45691 -0.02023 -0.13317 -0.01742 72  SER A O   
459  C CB  . SER A 65  ? 0.61305 0.48436 0.42348 0.04306  -0.10179 -0.02374 72  SER A CB  
460  O OG  . SER A 65  ? 0.55798 0.48773 0.42881 0.05018  -0.07479 -0.01680 72  SER A OG  
461  N N   . GLY A 66  ? 0.48176 0.46994 0.42909 -0.02760 -0.13377 0.00096  73  GLY A N   
462  C CA  . GLY A 66  ? 0.43641 0.47313 0.43559 -0.04435 -0.13067 0.01160  73  GLY A CA  
463  C C   . GLY A 66  ? 0.45810 0.55497 0.51110 -0.02851 -0.10605 0.01837  73  GLY A C   
464  O O   . GLY A 66  ? 0.48615 0.57669 0.53924 -0.00758 -0.08287 0.00804  73  GLY A O   
465  N N   . LYS A 67  ? 0.42680 0.58032 0.52136 -0.03722 -0.11283 0.03930  74  LYS A N   
466  C CA  . LYS A 67  ? 0.50983 0.71090 0.64038 -0.01349 -0.09016 0.04692  74  LYS A CA  
467  C C   . LYS A 67  ? 0.45711 0.68403 0.61105 -0.00536 -0.07141 0.04969  74  LYS A C   
468  O O   . LYS A 67  ? 0.45528 0.69237 0.61548 0.02165  -0.05081 0.04775  74  LYS A O   
469  C CB  . LYS A 67  ? 0.44344 0.70057 0.60386 -0.01568 -0.10229 0.07317  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.54398 0.77731 0.68005 -0.01831 -0.11949 0.07079  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.62653 0.91087 0.79019 0.00197  -0.11264 0.08874  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.57059 0.82707 0.71810 0.03529  -0.08666 0.07151  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.59921 0.84440 0.73127 0.04385  -0.09351 0.07211  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.33753 0.56674 0.49613 -0.02658 -0.07991 0.05421  75  GLU A N   
475  C CA  . GLU A 68  ? 0.35147 0.60758 0.53047 -0.01791 -0.06228 0.05906  75  GLU A CA  
476  C C   . GLU A 68  ? 0.39729 0.60446 0.55003 -0.00434 -0.04521 0.03263  75  GLU A C   
477  O O   . GLU A 68  ? 0.37088 0.53125 0.49546 -0.01401 -0.05115 0.01677  75  GLU A O   
478  C CB  . GLU A 68  ? 0.32859 0.60552 0.52326 -0.04880 -0.07952 0.07716  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.56276 0.92247 0.80551 -0.05808 -0.08841 0.11803  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.72045 1.09168 0.96692 -0.07399 -0.11404 0.13226  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.72584 1.15947 1.00401 -0.05491 -0.10554 0.15482  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.78638 1.10019 0.99743 -0.10205 -0.14315 0.12145  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.29544 0.51237 0.45261 0.02031  -0.02545 0.03091  76  LEU A N   
484  C CA  . LEU A 69  ? 0.38066 0.55531 0.51549 0.02904  -0.01439 0.01135  76  LEU A CA  
485  C C   . LEU A 69  ? 0.33010 0.52291 0.47294 0.03362  -0.00470 0.01614  76  LEU A C   
486  O O   . LEU A 69  ? 0.27515 0.49340 0.42191 0.05852  0.00747  0.02659  76  LEU A O   
487  C CB  . LEU A 69  ? 0.28130 0.43037 0.39784 0.05225  -0.00703 0.00413  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.34001 0.47829 0.45124 0.05181  -0.01428 0.00398  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.35134 0.45553 0.43988 0.07163  -0.01016 -0.00089 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.27552 0.39072 0.37733 0.03267  -0.02224 -0.00371 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.28708 0.43984 0.40777 0.01063  0.00350  0.12357  77  HIS A N   
492  C CA  . HIS A 70  ? 0.32874 0.47992 0.45257 0.01102  0.00518  0.12210  77  HIS A CA  
493  C C   . HIS A 70  ? 0.33269 0.44438 0.43495 -0.00533 -0.00711 0.08578  77  HIS A C   
494  O O   . HIS A 70  ? 0.27523 0.36544 0.36275 -0.01771 -0.01793 0.06485  77  HIS A O   
495  C CB  . HIS A 70  ? 0.27670 0.48504 0.42909 -0.00028 -0.00972 0.15324  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.33158 0.55472 0.48387 -0.03369 -0.04138 0.14787  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.44753 0.72001 0.61613 -0.04573 -0.05631 0.17273  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.37640 0.56836 0.50923 -0.05712 -0.05965 0.12082  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.37930 0.64459 0.53420 -0.07808 -0.08353 0.15789  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.38359 0.59706 0.51609 -0.08374 -0.08405 0.12698  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.28801 0.39347 0.38848 -0.00212 -0.00344 0.08170  78  ILE A N   
502  C CA  . ILE A 71  ? 0.29625 0.37342 0.37886 -0.01321 -0.01297 0.05368  78  ILE A CA  
503  C C   . ILE A 71  ? 0.26901 0.36737 0.36374 -0.02240 -0.02322 0.06659  78  ILE A C   
504  O O   . ILE A 71  ? 0.31097 0.43376 0.42189 -0.01028 -0.01267 0.08986  78  ILE A O   
505  C CB  . ILE A 71  ? 0.30665 0.34996 0.36853 0.00145  0.00444  0.03244  78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.36373 0.38182 0.41409 0.00716  0.01676  0.02081  78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.29390 0.32068 0.34065 -0.00845 -0.00653 0.00839  78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.32509 0.30821 0.35256 0.01832  0.03591  0.00279  78  ILE A CD1 
509  N N   . ASN A 72  ? 0.29504 0.38138 0.38054 -0.04224 -0.04096 0.05345  79  ASN A N   
510  C CA  . ASN A 72  ? 0.27015 0.36632 0.36303 -0.05371 -0.04930 0.06342  79  ASN A CA  
511  C C   . ASN A 72  ? 0.29929 0.36435 0.37091 -0.04985 -0.04725 0.04115  79  ASN A C   
512  O O   . ASN A 72  ? 0.38570 0.42426 0.43693 -0.05115 -0.05017 0.01809  79  ASN A O   
513  C CB  . ASN A 72  ? 0.28396 0.38847 0.37961 -0.08265 -0.07058 0.07079  79  ASN A CB  
514  C CG  . ASN A 72  ? 0.30693 0.45815 0.42848 -0.08874 -0.07574 0.09929  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.29763 0.47989 0.44100 -0.06914 -0.06089 0.12124  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.29357 0.45080 0.40996 -0.11478 -0.09599 0.10058  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.31864 0.39191 0.39648 -0.04304 -0.04106 0.05132  80  LEU A N   
518  C CA  . LEU A 73  ? 0.33604 0.38809 0.39574 -0.03748 -0.03875 0.03646  80  LEU A CA  
519  C C   . LEU A 73  ? 0.33882 0.38918 0.40337 -0.05332 -0.04627 0.04933  80  LEU A C   
520  O O   . LEU A 73  ? 0.30914 0.38499 0.39625 -0.05643 -0.04418 0.07402  80  LEU A O   
521  C CB  . LEU A 73  ? 0.28055 0.33848 0.33620 -0.01344 -0.02253 0.03594  80  LEU A CB  
522  C CG  . LEU A 73  ? 0.33985 0.39228 0.38691 0.00004  -0.01161 0.02504  80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.29491 0.34608 0.32875 0.02150  0.00435  0.02365  80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.27841 0.30913 0.30828 -0.00707 -0.01807 -0.00171 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.34891 0.36763 0.39150 -0.06288 -0.05285 0.03449  81  ILE A N   
526  C CA  . ILE A 74  ? 0.33003 0.33200 0.36875 -0.08235 -0.05894 0.04376  81  ILE A CA  
527  C C   . ILE A 74  ? 0.39626 0.37214 0.41443 -0.06910 -0.04937 0.03631  81  ILE A C   
528  O O   . ILE A 74  ? 0.44650 0.39158 0.43825 -0.06650 -0.04958 0.01940  81  ILE A O   
529  C CB  . ILE A 74  ? 0.34998 0.32788 0.37274 -0.10840 -0.07404 0.03589  81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.42127 0.43164 0.46314 -0.11680 -0.08306 0.04381  81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.38699 0.34209 0.40219 -0.13477 -0.08041 0.04552  81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.38035 0.37110 0.40264 -0.14121 -0.09911 0.03553  81  ILE A CD1 
533  N N   . PRO A 75  ? 0.36186 0.35101 0.39080 -0.05779 -0.03908 0.05133  82  PRO A N   
534  C CA  . PRO A 75  ? 0.38504 0.35103 0.39436 -0.04464 -0.02891 0.04915  82  PRO A CA  
535  C C   . PRO A 75  ? 0.41468 0.34271 0.41254 -0.06681 -0.03037 0.05706  82  PRO A C   
536  O O   . PRO A 75  ? 0.41432 0.34798 0.42933 -0.09219 -0.03767 0.07224  82  PRO A O   
537  C CB  . PRO A 75  ? 0.39102 0.38810 0.41584 -0.02332 -0.01660 0.06428  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.34379 0.37059 0.39942 -0.03508 -0.01990 0.08374  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.42274 0.45121 0.48076 -0.05026 -0.03293 0.07280  82  PRO A CD  
540  N N   . ASN A 76  ? 0.49486 0.38344 0.46172 -0.05772 -0.02244 0.04774  83  ASN A N   
541  C CA  . ASN A 76  ? 0.50222 0.33775 0.44605 -0.07632 -0.01885 0.05237  83  ASN A CA  
542  C C   . ASN A 76  ? 0.54052 0.35704 0.46653 -0.04878 0.00162  0.05855  83  ASN A C   
543  O O   . ASN A 76  ? 0.60608 0.40551 0.50652 -0.02788 0.00931  0.04760  83  ASN A O   
544  C CB  . ASN A 76  ? 0.60123 0.39240 0.51288 -0.09341 -0.02757 0.03420  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.61553 0.34531 0.49897 -0.12300 -0.02710 0.03707  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.69556 0.38696 0.55998 -0.11527 -0.01004 0.04479  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.65543 0.37384 0.53301 -0.15800 -0.04536 0.03110  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.54466 0.36861 0.48587 -0.04706 0.01166  0.07943  84  LYS A N   
549  C CA  . LYS A 77  ? 0.65016 0.46122 0.57620 -0.01781 0.03299  0.08964  84  LYS A CA  
550  C C   . LYS A 77  ? 0.68377 0.42215 0.56824 -0.02147 0.04572  0.08712  84  LYS A C   
551  O O   . LYS A 77  ? 0.71971 0.44594 0.58189 0.01051  0.06330  0.08946  84  LYS A O   
552  C CB  . LYS A 77  ? 0.64866 0.48256 0.60080 -0.01557 0.04242  0.11508  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.60398 0.50352 0.58368 0.00630  0.04068  0.11992  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.57976 0.49744 0.57842 0.01678  0.05555  0.14775  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.68567 0.65684 0.69424 0.04908  0.05990  0.15032  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.76680 0.77305 0.80902 0.04345  0.06070  0.17122  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.72131 0.41039 0.59154 -0.05943 0.03809  0.08334  85  GLN A N   
558  C CA  . GLN A 78  ? 0.78560 0.39085 0.60629 -0.06452 0.05310  0.07944  85  GLN A CA  
559  C C   . GLN A 78  ? 0.78868 0.37419 0.57562 -0.04121 0.05719  0.06168  85  GLN A C   
560  O O   . GLN A 78  ? 0.81936 0.36272 0.57142 -0.01427 0.08059  0.06592  85  GLN A O   
561  C CB  . GLN A 78  ? 0.98775 0.54419 0.79550 -0.11642 0.04030  0.07568  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.24537 0.80059 1.07640 -0.14153 0.04394  0.09830  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.29115 0.93657 1.18369 -0.14031 0.03167  0.11446  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.12187 0.81657 1.03825 -0.14860 0.01078  0.10663  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.21132 0.87607 1.12725 -0.12712 0.04751  0.13898  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.72852 0.34586 0.52627 -0.04878 0.03706  0.04495  86  ASP A N   
567  C CA  . ASP A 79  ? 0.83155 0.43913 0.60375 -0.02770 0.04014  0.03040  86  ASP A CA  
568  C C   . ASP A 79  ? 0.79895 0.47320 0.59454 0.00992  0.04379  0.03278  86  ASP A C   
569  O O   . ASP A 79  ? 0.83286 0.50702 0.61121 0.03155  0.04975  0.02629  86  ASP A O   
570  C CB  . ASP A 79  ? 0.83561 0.44278 0.60603 -0.05468 0.01793  0.01224  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.90829 0.45489 0.65181 -0.09685 0.00962  0.00780  86  ASP A CG  
572  O OD1 . ASP A 79  ? 1.02921 0.52276 0.75015 -0.10614 0.02334  0.01674  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 1.07652 0.62864 0.82003 -0.12205 -0.01065 -0.00418 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.59524 0.32639 0.42739 0.01721  0.04054  0.04262  87  ARG A N   
575  C CA  . ARG A 80  ? 0.60839 0.40446 0.45991 0.04587  0.03991  0.04186  87  ARG A CA  
576  C C   . ARG A 80  ? 0.54837 0.37169 0.40901 0.03932  0.02340  0.02288  87  ARG A C   
577  O O   . ARG A 80  ? 0.53595 0.38181 0.39147 0.05917  0.02586  0.01766  87  ARG A O   
578  C CB  . ARG A 80  ? 0.65656 0.45091 0.48701 0.08273  0.06103  0.05324  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.60359 0.47145 0.45306 0.10925  0.05910  0.05575  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.54815 0.42612 0.39023 0.13977  0.07913  0.07787  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.89079 0.71623 0.69957 0.15812  0.10261  0.09082  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.93573 0.77344 0.72873 0.18548  0.11275  0.09525  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.81701 0.72060 0.62726 0.19262  0.09851  0.08662  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.93360 0.71547 0.69190 0.20612  0.13940  0.11041  87  ARG A NH2 
585  N N   . THR A 81  ? 0.47128 0.29516 0.34709 0.01087  0.00721  0.01518  88  THR A N   
586  C CA  . THR A 81  ? 0.51231 0.35772 0.39762 0.00320  -0.00667 -0.00064 88  THR A CA  
587  C C   . THR A 81  ? 0.48290 0.36766 0.40097 -0.00903 -0.01824 -0.00016 88  THR A C   
588  O O   . THR A 81  ? 0.45718 0.34234 0.38901 -0.02206 -0.01966 0.01225  88  THR A O   
589  C CB  . THR A 81  ? 0.46854 0.26686 0.33002 -0.01644 -0.01249 -0.01011 88  THR A CB  
590  O OG1 . THR A 81  ? 0.58826 0.36823 0.45453 -0.04692 -0.02224 -0.00553 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.55284 0.29889 0.37337 -0.00216 0.00384  -0.00874 88  THR A CG2 
592  N N   . LEU A 82  ? 0.45863 0.37577 0.38850 -0.00394 -0.02432 -0.01179 89  LEU A N   
593  C CA  . LEU A 82  ? 0.42999 0.37559 0.38410 -0.01243 -0.03166 -0.01260 89  LEU A CA  
594  C C   . LEU A 82  ? 0.41366 0.35451 0.36801 -0.02443 -0.04060 -0.02485 89  LEU A C   
595  O O   . LEU A 82  ? 0.41390 0.35745 0.36002 -0.01666 -0.04002 -0.03695 89  LEU A O   
596  C CB  . LEU A 82  ? 0.37475 0.35644 0.33668 0.00556  -0.02702 -0.01560 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.43677 0.43781 0.41506 0.00133  -0.02949 -0.01801 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.30723 0.31222 0.30304 -0.00571 -0.02799 0.00159  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.37231 0.39670 0.34522 0.01656  -0.02480 -0.02720 89  LEU A CD2 
600  N N   . THR A 83  ? 0.37433 0.31318 0.33980 -0.04285 -0.04851 -0.01904 90  THR A N   
601  C CA  . THR A 83  ? 0.36546 0.29918 0.32945 -0.05398 -0.05661 -0.02716 90  THR A CA  
602  C C   . THR A 83  ? 0.35752 0.32162 0.34504 -0.05260 -0.05678 -0.02409 90  THR A C   
603  O O   . THR A 83  ? 0.33923 0.32260 0.34514 -0.05434 -0.05558 -0.00876 90  THR A O   
604  C CB  . THR A 83  ? 0.37813 0.28584 0.33049 -0.07706 -0.06635 -0.02207 90  THR A CB  
605  O OG1 . THR A 83  ? 0.47232 0.33881 0.39479 -0.07702 -0.06175 -0.02525 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.38354 0.28745 0.32982 -0.08542 -0.07437 -0.03014 90  THR A CG2 
607  N N   . ILE A 84  ? 0.48455 0.45122 0.47078 -0.04816 -0.05572 -0.03638 91  ILE A N   
608  C CA  . ILE A 84  ? 0.40032 0.38427 0.40228 -0.04562 -0.05201 -0.03423 91  ILE A CA  
609  C C   . ILE A 84  ? 0.42107 0.39920 0.42240 -0.05620 -0.05870 -0.03367 91  ILE A C   
610  O O   . ILE A 84  ? 0.34544 0.30872 0.33358 -0.05642 -0.05989 -0.04602 91  ILE A O   
611  C CB  . ILE A 84  ? 0.32874 0.31666 0.32735 -0.03393 -0.04326 -0.04891 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.40064 0.39843 0.39610 -0.02299 -0.03774 -0.04861 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.26991 0.26110 0.27729 -0.03170 -0.03568 -0.04773 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.43287 0.43184 0.41490 -0.01773 -0.03923 -0.05975 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.30433 0.29901 0.32046 -0.06361 -0.06263 -0.01673 92  VAL A N   
616  C CA  . VAL A 85  ? 0.31129 0.30820 0.32662 -0.07350 -0.07046 -0.01244 92  VAL A CA  
617  C C   . VAL A 85  ? 0.35551 0.37308 0.38869 -0.06198 -0.05989 -0.00245 92  VAL A C   
618  O O   . VAL A 85  ? 0.33030 0.36756 0.38018 -0.05298 -0.05116 0.01213  92  VAL A O   
619  C CB  . VAL A 85  ? 0.37427 0.37873 0.39015 -0.09465 -0.08577 0.00181  92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.35523 0.36094 0.36172 -0.10609 -0.09657 0.00317  92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.53780 0.51176 0.53243 -0.10448 -0.09069 -0.00664 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.37014 0.38021 0.39761 -0.05960 -0.05760 -0.00853 93  ASP A N   
623  C CA  . ASP A 86  ? 0.32536 0.34965 0.36614 -0.04824 -0.04560 0.00386  93  ASP A CA  
624  C C   . ASP A 86  ? 0.33475 0.36679 0.37199 -0.05502 -0.05447 0.01105  93  ASP A C   
625  O O   . ASP A 86  ? 0.36394 0.37892 0.38190 -0.06592 -0.06626 -0.00099 93  ASP A O   
626  C CB  . ASP A 86  ? 0.32561 0.32806 0.36109 -0.03531 -0.02754 -0.01147 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.38827 0.36957 0.40979 -0.04016 -0.03010 -0.03078 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.36647 0.34704 0.38656 -0.04016 -0.03000 -0.02653 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.45781 0.42755 0.47069 -0.04223 -0.03129 -0.04760 93  ASP A OD2 
630  N N   . THR A 87  ? 0.32385 0.38176 0.37687 -0.04580 -0.04695 0.03266  94  THR A N   
631  C CA  . THR A 87  ? 0.32898 0.40100 0.37917 -0.04809 -0.05317 0.04294  94  THR A CA  
632  C C   . THR A 87  ? 0.35651 0.40989 0.40365 -0.03093 -0.03326 0.03842  94  THR A C   
633  O O   . THR A 87  ? 0.30618 0.37929 0.36121 -0.02004 -0.02552 0.05804  94  THR A O   
634  C CB  . THR A 87  ? 0.29912 0.42237 0.37082 -0.04920 -0.05910 0.07562  94  THR A CB  
635  O OG1 . THR A 87  ? 0.28304 0.42087 0.37563 -0.03118 -0.04021 0.09205  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.37625 0.51636 0.44478 -0.07700 -0.08576 0.07846  94  THR A CG2 
637  N N   . GLY A 88  ? 0.29459 0.31246 0.33124 -0.02890 -0.02416 0.01464  95  GLY A N   
638  C CA  . GLY A 88  ? 0.36422 0.36002 0.39842 -0.01782 -0.00483 0.00847  95  GLY A CA  
639  C C   . GLY A 88  ? 0.34462 0.33672 0.36833 -0.01983 -0.00996 0.00696  95  GLY A C   
640  O O   . GLY A 88  ? 0.35244 0.36056 0.36761 -0.02795 -0.02787 0.01344  95  GLY A O   
641  N N   . ILE A 89  ? 0.38372 0.35223 0.40540 -0.01372 0.00650  -0.00204 96  ILE A N   
642  C CA  . ILE A 89  ? 0.36937 0.33367 0.38217 -0.01122 0.00684  -0.00065 96  ILE A CA  
643  C C   . ILE A 89  ? 0.34841 0.30516 0.34284 -0.02190 -0.01071 -0.01551 96  ILE A C   
644  O O   . ILE A 89  ? 0.36171 0.31711 0.34134 -0.01953 -0.01475 -0.01235 96  ILE A O   
645  C CB  . ILE A 89  ? 0.40795 0.34768 0.42613 -0.00396 0.03119  -0.00516 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.41019 0.35135 0.42365 0.00538  0.03771  0.00642  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.35041 0.27166 0.36721 -0.01568 0.03074  -0.02881 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.50752 0.42340 0.52835 0.01200  0.06463  0.00654  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.34017 0.29005 0.33155 -0.03079 -0.01912 -0.03005 97  GLY A N   
650  C CA  . GLY A 90  ? 0.37466 0.31215 0.34547 -0.03630 -0.03057 -0.04174 97  GLY A CA  
651  C C   . GLY A 90  ? 0.38826 0.31372 0.35855 -0.03091 -0.01903 -0.05039 97  GLY A C   
652  O O   . GLY A 90  ? 0.34768 0.27254 0.33448 -0.02769 -0.00370 -0.04992 97  GLY A O   
653  N N   . MET A 91  ? 0.34190 0.25598 0.29144 -0.03009 -0.02502 -0.05683 98  MET A N   
654  C CA  . MET A 91  ? 0.35633 0.26672 0.30723 -0.02353 -0.01446 -0.06107 98  MET A CA  
655  C C   . MET A 91  ? 0.40378 0.29811 0.32398 -0.01456 -0.01556 -0.05761 98  MET A C   
656  O O   . MET A 91  ? 0.43897 0.31659 0.32866 -0.01693 -0.02732 -0.05971 98  MET A O   
657  C CB  . MET A 91  ? 0.36851 0.28480 0.32509 -0.02588 -0.01568 -0.07039 98  MET A CB  
658  C CG  . MET A 91  ? 0.35511 0.28665 0.33921 -0.03393 -0.01011 -0.07624 98  MET A CG  
659  S SD  . MET A 91  ? 0.39627 0.34259 0.38280 -0.03699 -0.01673 -0.08516 98  MET A SD  
660  C CE  . MET A 91  ? 0.33162 0.26206 0.29439 -0.03479 -0.02925 -0.08263 98  MET A CE  
661  N N   . THR A 92  ? 0.43449 0.33031 0.35979 -0.00511 -0.00213 -0.05231 99  THR A N   
662  C CA  . THR A 92  ? 0.46542 0.34434 0.35890 0.00781  0.00104  -0.04835 99  THR A CA  
663  C C   . THR A 92  ? 0.46517 0.33948 0.34997 0.01613  0.00617  -0.05159 99  THR A C   
664  O O   . THR A 92  ? 0.41355 0.30492 0.32116 0.01085  0.00613  -0.05591 99  THR A O   
665  C CB  . THR A 92  ? 0.46635 0.35139 0.37025 0.01770  0.01605  -0.03716 99  THR A CB  
666  O OG1 . THR A 92  ? 0.43174 0.33387 0.37080 0.01642  0.03007  -0.03591 99  THR A OG1 
667  C CG2 . THR A 92  ? 0.47491 0.36788 0.38943 0.01399  0.01495  -0.02973 99  THR A CG2 
668  N N   . LYS A 93  ? 0.42280 0.27462 0.27119 0.03163  0.01194  -0.04767 100 LYS A N   
669  C CA  . LYS A 93  ? 0.52280 0.37054 0.36034 0.04620  0.02172  -0.04530 100 LYS A CA  
670  C C   . LYS A 93  ? 0.47398 0.36195 0.35675 0.04980  0.03520  -0.03610 100 LYS A C   
671  O O   . LYS A 93  ? 0.51151 0.42078 0.40973 0.05240  0.03799  -0.03418 100 LYS A O   
672  C CB  . LYS A 93  ? 0.48758 0.29585 0.26997 0.06549  0.02926  -0.04171 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.64599 0.43519 0.40162 0.08304  0.03942  -0.03943 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.66165 0.41070 0.36270 0.10826  0.05471  -0.03281 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.77184 0.49622 0.44190 0.13024  0.06943  -0.02780 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.92140 0.59690 0.52897 0.15879  0.08844  -0.02106 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.40190 0.30309 0.30669 0.04878  0.04378  -0.02879 101 ALA A N   
678  C CA  . ALA A 94  ? 0.38219 0.32103 0.33226 0.04476  0.05546  -0.02055 101 ALA A CA  
679  C C   . ALA A 94  ? 0.45317 0.41535 0.43830 0.02145  0.04657  -0.03114 101 ALA A C   
680  O O   . ALA A 94  ? 0.40859 0.40532 0.42386 0.01428  0.04988  -0.02810 101 ALA A O   
681  C CB  . ALA A 94  ? 0.38649 0.32627 0.34966 0.04722  0.06854  -0.01022 101 ALA A CB  
682  N N   . ASP A 95  ? 0.48525 0.43166 0.46555 0.00946  0.03536  -0.04226 102 ASP A N   
683  C CA  . ASP A 95  ? 0.37613 0.33718 0.37909 -0.00909 0.02763  -0.05332 102 ASP A CA  
684  C C   . ASP A 95  ? 0.36791 0.34575 0.36791 -0.00685 0.02032  -0.05646 102 ASP A C   
685  O O   . ASP A 95  ? 0.33685 0.34536 0.36187 -0.01827 0.01897  -0.05947 102 ASP A O   
686  C CB  . ASP A 95  ? 0.40426 0.34551 0.39780 -0.01570 0.01905  -0.05999 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.52203 0.45439 0.52629 -0.01813 0.02922  -0.05483 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.46478 0.40422 0.49109 -0.02380 0.04231  -0.05217 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.48929 0.40932 0.48057 -0.01476 0.02492  -0.05152 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.35784 0.31448 0.32427 0.00734  0.01611  -0.05530 103 LEU A N   
691  C CA  . LEU A 96  ? 0.37105 0.33688 0.33021 0.01298  0.01189  -0.05626 103 LEU A CA  
692  C C   . LEU A 96  ? 0.34178 0.34364 0.31666 0.02452  0.02216  -0.04368 103 LEU A C   
693  O O   . LEU A 96  ? 0.40428 0.43681 0.39217 0.02383  0.01885  -0.04250 103 LEU A O   
694  C CB  . LEU A 96  ? 0.37676 0.30020 0.29055 0.02447  0.00863  -0.05748 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.39097 0.28971 0.29172 0.01047  -0.00500 -0.06699 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.41500 0.26900 0.26724 0.01686  -0.00807 -0.06834 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.35182 0.27093 0.27545 -0.00181 -0.01320 -0.07342 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.34644 0.35090 0.32188 0.03637  0.03508  -0.03143 104 ILE A N   
699  C CA  . ILE A 97  ? 0.37911 0.41951 0.36681 0.05304  0.04764  -0.01319 104 ILE A CA  
700  C C   . ILE A 97  ? 0.47048 0.56097 0.50736 0.03614  0.05112  -0.00626 104 ILE A C   
701  O O   . ILE A 97  ? 0.39699 0.54066 0.46299 0.03166  0.05029  0.00252  104 ILE A O   
702  C CB  . ILE A 97  ? 0.45948 0.46604 0.40761 0.08278  0.06327  -0.00054 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.46363 0.41565 0.35794 0.09481  0.05999  -0.00894 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.45905 0.50822 0.42347 0.10432  0.08026  0.02387  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.60219 0.49869 0.44309 0.11347  0.06971  -0.00711 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.33648 0.41207 0.38287 0.02514  0.05515  -0.00894 105 ASN A N   
707  C CA  . ASN A 98  ? 0.37787 0.49121 0.46703 0.00837  0.06233  -0.00068 105 ASN A CA  
708  C C   . ASN A 98  ? 0.36534 0.47894 0.47689 -0.02577 0.05315  -0.01849 105 ASN A C   
709  O O   . ASN A 98  ? 0.44003 0.59453 0.58071 -0.04778 0.04735  -0.02067 105 ASN A O   
710  C CB  . ASN A 98  ? 0.34174 0.43648 0.42583 0.02224  0.07906  0.01259  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.61381 0.69287 0.66197 0.05840  0.09012  0.02745  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.75214 0.86520 0.80761 0.07449  0.09802  0.04446  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.60465 0.63212 0.61074 0.07199  0.09163  0.02227  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.35401 0.35595 0.51507 -0.01893 0.00749  0.01312  106 ASN A N   
715  C CA  . ASN A 99  ? 0.39948 0.38145 0.55722 -0.01602 -0.02559 0.01567  106 ASN A CA  
716  C C   . ASN A 99  ? 0.37366 0.36260 0.56371 -0.01031 -0.02392 0.01053  106 ASN A C   
717  O O   . ASN A 99  ? 0.35235 0.33267 0.54253 -0.01649 -0.03536 0.02575  106 ASN A O   
718  C CB  . ASN A 99  ? 0.35750 0.32734 0.50047 -0.00470 -0.05175 -0.00441 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.49699 0.45880 0.60029 -0.00831 -0.05550 -0.00050 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.41905 0.36935 0.49639 -0.02133 -0.04568 0.02288  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.43032 0.40099 0.52837 0.00247  -0.06958 -0.02492 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.35926 0.36088 0.57302 -0.00073 -0.00807 -0.01224 107 LEU A N   
723  C CA  . LEU A 100 ? 0.42363 0.42494 0.66039 0.00579  -0.00611 -0.01881 107 LEU A CA  
724  C C   . LEU A 100 ? 0.41708 0.43094 0.66118 0.00311  0.01112  0.00270  107 LEU A C   
725  O O   . LEU A 100 ? 0.34108 0.35171 0.59263 0.00415  0.00167  0.00733  107 LEU A O   
726  C CB  . LEU A 100 ? 0.29111 0.29850 0.54709 0.01395  0.01192  -0.04957 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.30782 0.31548 0.56891 0.01931  -0.01011 -0.07646 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.29620 0.31587 0.58203 0.02157  0.01310  -0.11008 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.29149 0.28151 0.55119 0.02584  -0.04276 -0.07240 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.28636 0.31686 0.52802 0.00119  0.03574  0.01503  108 GLY A N   
731  C CA  . GLY A 101 ? 0.33829 0.39049 0.59025 0.00315  0.04968  0.03592  108 GLY A CA  
732  C C   . GLY A 101 ? 0.37443 0.43481 0.62441 -0.01134 0.02632  0.05575  108 GLY A C   
733  O O   . GLY A 101 ? 0.35348 0.43209 0.61620 -0.01066 0.02334  0.06557  108 GLY A O   
734  N N   . THR A 102 ? 0.33574 0.38072 0.56579 -0.02570 0.01017  0.06090  109 THR A N   
735  C CA  . THR A 102 ? 0.39615 0.43821 0.61823 -0.04463 -0.00867 0.07713  109 THR A CA  
736  C C   . THR A 102 ? 0.42736 0.44826 0.65012 -0.04503 -0.03247 0.06950  109 THR A C   
737  O O   . THR A 102 ? 0.42272 0.45520 0.65179 -0.05777 -0.04023 0.07896  109 THR A O   
738  C CB  . THR A 102 ? 0.32615 0.34101 0.51512 -0.05812 -0.01761 0.08398  109 THR A CB  
739  O OG1 . THR A 102 ? 0.42382 0.45238 0.60738 -0.05572 0.00562  0.08601  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.43984 0.45223 0.61876 -0.08330 -0.02522 0.10232  109 THR A CG2 
741  N N   . ILE A 103 ? 0.47140 0.46427 0.68885 -0.03201 -0.04363 0.05031  110 ILE A N   
742  C CA  . ILE A 103 ? 0.52846 0.49927 0.74715 -0.02930 -0.06211 0.04053  110 ILE A CA  
743  C C   . ILE A 103 ? 0.43702 0.43147 0.67729 -0.02291 -0.05004 0.03832  110 ILE A C   
744  O O   . ILE A 103 ? 0.47118 0.46191 0.71043 -0.03080 -0.06220 0.04144  110 ILE A O   
745  C CB  . ILE A 103 ? 0.57171 0.51666 0.78660 -0.01333 -0.07382 0.01817  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.61394 0.51872 0.79805 -0.01680 -0.09991 0.02293  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.63852 0.57900 0.87094 -0.00217 -0.07350 -0.00010 110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.55876 0.45785 0.71617 -0.02568 -0.09948 0.03839  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.34286 0.35755 0.59713 -0.00856 -0.02491 0.03291  111 ALA A N   
750  C CA  . ALA A 104 ? 0.40249 0.43073 0.66770 0.00281  -0.01123 0.03199  111 ALA A CA  
751  C C   . ALA A 104 ? 0.43562 0.50007 0.70713 -0.00321 -0.01138 0.05379  111 ALA A C   
752  O O   . ALA A 104 ? 0.43263 0.50727 0.70672 0.00462  -0.01129 0.05525  111 ALA A O   
753  C CB  . ALA A 104 ? 0.32705 0.35715 0.59768 0.01964  0.02040  0.02141  111 ALA A CB  
754  N N   . LYS A 105 ? 0.36467 0.45176 0.63847 -0.01679 -0.01145 0.06955  112 LYS A N   
755  C CA  . LYS A 105 ? 0.33736 0.47132 0.62532 -0.02438 -0.01202 0.08733  112 LYS A CA  
756  C C   . LYS A 105 ? 0.32296 0.45523 0.60757 -0.04227 -0.03816 0.08643  112 LYS A C   
757  O O   . LYS A 105 ? 0.37696 0.53914 0.67067 -0.03679 -0.04197 0.08945  112 LYS A O   
758  C CB  . LYS A 105 ? 0.34959 0.50567 0.64122 -0.03975 -0.00425 0.10107  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.36643 0.58674 0.68374 -0.03970 0.00576  0.11723  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.43322 0.67337 0.75497 -0.05099 0.02255  0.12828  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.48583 0.79448 0.83752 -0.06366 0.02400  0.14167  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.49881 0.82259 0.85689 -0.08354 -0.00280 0.13858  112 LYS A NZ  
763  N N   . SER A 106 ? 0.30518 0.39899 0.57185 -0.06291 -0.05618 0.08194  113 SER A N   
764  C CA  . SER A 106 ? 0.35782 0.43990 0.61540 -0.08370 -0.07799 0.07917  113 SER A CA  
765  C C   . SER A 106 ? 0.36909 0.42381 0.61903 -0.06917 -0.08572 0.06359  113 SER A C   
766  O O   . SER A 106 ? 0.46196 0.52423 0.70881 -0.07965 -0.09834 0.06120  113 SER A O   
767  C CB  . SER A 106 ? 0.45395 0.48955 0.68585 -0.10735 -0.09047 0.08010  113 SER A CB  
768  O OG  . SER A 106 ? 0.45736 0.46932 0.67823 -0.09667 -0.08272 0.08086  113 SER A OG  
769  N N   . GLY A 107 ? 0.38380 0.40871 0.63041 -0.04733 -0.07727 0.05082  114 GLY A N   
770  C CA  . GLY A 107 ? 0.39216 0.39239 0.63313 -0.03384 -0.07901 0.03450  114 GLY A CA  
771  C C   . GLY A 107 ? 0.34873 0.38043 0.59609 -0.01911 -0.06661 0.03833  114 GLY A C   
772  O O   . GLY A 107 ? 0.35126 0.37258 0.58743 -0.01794 -0.07411 0.03141  114 GLY A O   
773  N N   . THR A 108 ? 0.28897 0.35536 0.54925 -0.00563 -0.04668 0.04993  115 THR A N   
774  C CA  . THR A 108 ? 0.34593 0.44034 0.60667 0.01413  -0.03445 0.05772  115 THR A CA  
775  C C   . THR A 108 ? 0.35542 0.49271 0.61971 0.00136  -0.05522 0.06875  115 THR A C   
776  O O   . THR A 108 ? 0.31870 0.46151 0.57062 0.01132  -0.06070 0.06753  115 THR A O   
777  C CB  . THR A 108 ? 0.29406 0.41214 0.56561 0.03289  -0.00699 0.06889  115 THR A CB  
778  O OG1 . THR A 108 ? 0.47567 0.55378 0.73966 0.04618  0.01615  0.05395  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.47917 0.63490 0.75065 0.05509  0.00132  0.08375  115 THR A CG2 
780  N N   . LYS A 109 ? 0.29423 0.46327 0.57362 -0.02252 -0.06622 0.07813  116 LYS A N   
781  C CA  . LYS A 109 ? 0.29356 0.51270 0.58240 -0.04138 -0.08551 0.08463  116 LYS A CA  
782  C C   . LYS A 109 ? 0.32017 0.50859 0.58676 -0.05723 -0.10724 0.07061  116 LYS A C   
783  O O   . LYS A 109 ? 0.40034 0.62250 0.66418 -0.05639 -0.11966 0.07078  116 LYS A O   
784  C CB  . LYS A 109 ? 0.32534 0.57030 0.63090 -0.07194 -0.08923 0.09231  116 LYS A CB  
785  C CG  . LYS A 109 ? 0.39918 0.70661 0.72211 -0.09768 -0.10604 0.09570  116 LYS A CG  
786  C CD  . LYS A 109 ? 0.39334 0.72556 0.73350 -0.12878 -0.10146 0.10282  116 LYS A CD  
787  C CE  . LYS A 109 ? 0.48810 0.90158 0.85687 -0.15406 -0.11338 0.10409  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.61367 1.00051 0.96708 -0.20349 -0.12805 0.09298  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.33704 0.46140 0.58535 -0.06987 -0.11237 0.05784  117 ALA A N   
790  C CA  . ALA A 110 ? 0.40090 0.48755 0.62508 -0.08463 -0.12976 0.04325  117 ALA A CA  
791  C C   . ALA A 110 ? 0.43975 0.50897 0.64800 -0.05827 -0.12377 0.03426  117 ALA A C   
792  O O   . ALA A 110 ? 0.44872 0.51443 0.63814 -0.06626 -0.13734 0.02660  117 ALA A O   
793  C CB  . ALA A 110 ? 0.35541 0.37517 0.56304 -0.09797 -0.13451 0.03319  117 ALA A CB  
794  N N   . PHE A 111 ? 0.32265 0.37794 0.53431 -0.02907 -0.10137 0.03379  118 PHE A N   
795  C CA  . PHE A 111 ? 0.37444 0.40361 0.56611 -0.00587 -0.08939 0.02437  118 PHE A CA  
796  C C   . PHE A 111 ? 0.36733 0.43922 0.54912 0.00767  -0.09227 0.03620  118 PHE A C   
797  O O   . PHE A 111 ? 0.41965 0.47327 0.57339 0.01168  -0.09812 0.02841  118 PHE A O   
798  C CB  . PHE A 111 ? 0.34591 0.35168 0.54384 0.01733  -0.06053 0.01947  118 PHE A CB  
799  C CG  . PHE A 111 ? 0.37443 0.34575 0.54955 0.03790  -0.04136 0.00796  118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.36042 0.29483 0.51358 0.03134  -0.05010 -0.00812 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.33168 0.30127 0.50272 0.06271  -0.01096 0.01267  118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.43374 0.33303 0.56245 0.04832  -0.02884 -0.01932 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.36595 0.29579 0.50984 0.07903  0.01137  0.00190  118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.42469 0.32082 0.54793 0.07143  0.00245  -0.01409 118 PHE A CZ  
805  N N   . MET A 112 ? 0.33288 0.46252 0.53539 0.01719  -0.08843 0.05494  119 MET A N   
806  C CA  . MET A 112 ? 0.38261 0.55973 0.57696 0.03755  -0.09288 0.06776  119 MET A CA  
807  C C   . MET A 112 ? 0.36156 0.57981 0.55482 0.01172  -0.12588 0.06501  119 MET A C   
808  O O   . MET A 112 ? 0.44653 0.69026 0.61998 0.02620  -0.13674 0.06817  119 MET A O   
809  C CB  . MET A 112 ? 0.32216 0.55241 0.54259 0.05840  -0.07826 0.08778  119 MET A CB  
810  C CG  . MET A 112 ? 0.35642 0.54763 0.57930 0.07598  -0.04484 0.08821  119 MET A CG  
811  S SD  . MET A 112 ? 0.59425 0.82402 0.82221 0.11836  -0.01849 0.11109  119 MET A SD  
812  C CE  . MET A 112 ? 0.49122 0.76527 0.76393 0.09731  -0.01670 0.11842  119 MET A CE  
813  N N   . GLU A 113 ? 0.37279 0.59623 0.58296 -0.02704 -0.14132 0.05856  120 GLU A N   
814  C CA  . GLU A 113 ? 0.49889 0.74951 0.70362 -0.05968 -0.16966 0.05007  120 GLU A CA  
815  C C   . GLU A 113 ? 0.46037 0.65348 0.62228 -0.06159 -0.17727 0.03298  120 GLU A C   
816  O O   . GLU A 113 ? 0.52388 0.74527 0.66748 -0.06628 -0.19609 0.02865  120 GLU A O   
817  C CB  . GLU A 113 ? 0.47710 0.72333 0.69895 -0.10268 -0.17724 0.04540  120 GLU A CB  
818  C CG  . GLU A 113 ? 0.53217 0.85812 0.79490 -0.11547 -0.17821 0.05859  120 GLU A CG  
819  C CD  . GLU A 113 ? 0.75113 1.05991 1.02064 -0.16110 -0.18152 0.05355  120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.84355 1.07600 1.08333 -0.17940 -0.18481 0.04113  120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.75264 1.12113 1.05477 -0.17741 -0.17860 0.06221  120 GLU A OE2 
822  N N   . ALA A 114 ? 0.41787 0.53314 0.56364 -0.05730 -0.16271 0.02174  121 ALA A N   
823  C CA  . ALA A 114 ? 0.46811 0.52456 0.57477 -0.05819 -0.16512 0.00381  121 ALA A CA  
824  C C   . ALA A 114 ? 0.46653 0.52373 0.54555 -0.02384 -0.15505 0.00756  121 ALA A C   
825  O O   . ALA A 114 ? 0.62541 0.66535 0.66760 -0.02710 -0.16543 -0.00262 121 ALA A O   
826  C CB  . ALA A 114 ? 0.52985 0.51279 0.63405 -0.05795 -0.15049 -0.00972 121 ALA A CB  
827  N N   . LEU A 115 ? 0.45409 0.52504 0.54399 0.00915  -0.13293 0.02215  122 LEU A N   
828  C CA  . LEU A 115 ? 0.52528 0.58428 0.58052 0.04472  -0.11779 0.02812  122 LEU A CA  
829  C C   . LEU A 115 ? 0.67222 0.78631 0.70714 0.05084  -0.14266 0.03731  122 LEU A C   
830  O O   . LEU A 115 ? 0.66297 0.75319 0.65161 0.07406  -0.13777 0.03792  122 LEU A O   
831  C CB  . LEU A 115 ? 0.46111 0.52406 0.53047 0.07673  -0.08758 0.04328  122 LEU A CB  
832  C CG  . LEU A 115 ? 0.56587 0.56993 0.64404 0.07821  -0.05779 0.03058  122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.39967 0.41920 0.49812 0.10000  -0.03180 0.04480  122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.57854 0.51515 0.61617 0.08899  -0.03757 0.01445  122 LEU A CD2 
835  N N   . GLN A 116 ? 0.68306 0.87207 0.75024 0.03034  -0.16871 0.04346  123 GLN A N   
836  C CA  . GLN A 116 ? 0.71360 0.96857 0.76831 0.03075  -0.19805 0.04727  123 GLN A CA  
837  C C   . GLN A 116 ? 0.69449 0.93235 0.72408 -0.00841 -0.22315 0.02500  123 GLN A C   
838  O O   . GLN A 116 ? 0.84262 1.11979 0.84650 -0.00715 -0.24697 0.02284  123 GLN A O   
839  C CB  . GLN A 116 ? 0.70880 1.06419 0.81607 0.02522  -0.21264 0.06101  123 GLN A CB  
840  C CG  . GLN A 116 ? 0.75695 1.13837 0.88458 0.06881  -0.18913 0.08442  123 GLN A CG  
841  C CD  . GLN A 116 ? 0.90633 1.38157 1.09281 0.05903  -0.19814 0.09509  123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.87962 1.35172 1.09997 0.02734  -0.19242 0.09055  123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.80645 1.36611 1.00378 0.08809  -0.21158 0.10937  123 GLN A NE2 
844  N N   . ALA A 117 ? 0.77072 0.83645 0.78204 -0.14121 -0.22587 -0.18285 124 ALA A N   
845  C CA  . ALA A 117 ? 0.70679 0.75261 0.70749 -0.15690 -0.22684 -0.22862 124 ALA A CA  
846  C C   . ALA A 117 ? 0.87062 0.89931 0.79362 -0.15216 -0.21179 -0.25344 124 ALA A C   
847  O O   . ALA A 117 ? 1.08271 1.08210 0.99519 -0.15916 -0.19909 -0.28729 124 ALA A O   
848  C CB  . ALA A 117 ? 0.63900 0.64979 0.70300 -0.16111 -0.20325 -0.23452 124 ALA A CB  
849  N N   . GLY A 118 ? 0.77014 0.80768 0.63605 -0.13881 -0.20357 -0.22739 125 GLY A N   
850  C CA  . GLY A 118 ? 0.84853 0.87193 0.63669 -0.13638 -0.18212 -0.24544 125 GLY A CA  
851  C C   . GLY A 118 ? 0.79591 0.80472 0.59102 -0.12333 -0.13990 -0.23137 125 GLY A C   
852  O O   . GLY A 118 ? 0.99911 1.00253 0.73236 -0.12172 -0.11685 -0.23935 125 GLY A O   
853  N N   . ALA A 119 ? 0.65123 0.65600 0.51818 -0.11549 -0.12888 -0.21156 126 ALA A N   
854  C CA  . ALA A 119 ? 0.67911 0.67870 0.55921 -0.10375 -0.09477 -0.19951 126 ALA A CA  
855  C C   . ALA A 119 ? 0.82902 0.83960 0.66268 -0.10040 -0.08523 -0.16721 126 ALA A C   
856  O O   . ALA A 119 ? 0.80843 0.82685 0.61362 -0.10143 -0.10659 -0.14393 126 ALA A O   
857  C CB  . ALA A 119 ? 0.52481 0.51839 0.48219 -0.09628 -0.09193 -0.18157 126 ALA A CB  
858  N N   . ASP A 120 ? 0.78315 0.79398 0.61328 -0.09607 -0.05218 -0.16643 127 ASP A N   
859  C CA  . ASP A 120 ? 0.72334 0.73760 0.51608 -0.09675 -0.03566 -0.13778 127 ASP A CA  
860  C C   . ASP A 120 ? 0.64855 0.67001 0.49759 -0.09135 -0.01913 -0.11984 127 ASP A C   
861  O O   . ASP A 120 ? 0.60634 0.63111 0.51588 -0.08446 -0.02035 -0.12851 127 ASP A O   
862  C CB  . ASP A 120 ? 0.84488 0.85614 0.56933 -0.10383 -0.00753 -0.15572 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.88148 0.90250 0.64198 -0.10155 0.02588  -0.18571 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.89099 0.90921 0.68364 -0.09638 0.02187  -0.21748 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.84050 0.87229 0.60136 -0.10488 0.05688  -0.17847 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.62308 0.64348 0.44696 -0.09507 -0.00432 -0.09420 128 ILE A N   
867  C CA  . ILE A 121 ? 0.67881 0.70583 0.54769 -0.09356 0.00602  -0.07586 128 ILE A CA  
868  C C   . ILE A 121 ? 0.61358 0.66103 0.52755 -0.09142 0.02641  -0.09819 128 ILE A C   
869  O O   . ILE A 121 ? 0.47569 0.53336 0.44148 -0.08569 0.02261  -0.09087 128 ILE A O   
870  C CB  . ILE A 121 ? 0.71243 0.72679 0.53897 -0.10143 0.02110  -0.04888 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.75055 0.74763 0.55554 -0.09523 -0.00382 -0.02081 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.64976 0.67296 0.51529 -0.10615 0.03852  -0.04077 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.82324 0.79534 0.56640 -0.09901 0.00881  0.00470  128 ILE A CD1 
874  N N   . SER A 122 ? 0.53583 0.59163 0.43134 -0.09425 0.04753  -0.12617 129 SER A N   
875  C CA  . SER A 122 ? 0.55040 0.63394 0.49600 -0.08962 0.06973  -0.14826 129 SER A CA  
876  C C   . SER A 122 ? 0.53892 0.62671 0.55172 -0.07142 0.05154  -0.15690 129 SER A C   
877  O O   . SER A 122 ? 0.48272 0.59707 0.54958 -0.06224 0.06028  -0.16418 129 SER A O   
878  C CB  . SER A 122 ? 0.50655 0.59682 0.42028 -0.09439 0.09888  -0.18041 129 SER A CB  
879  O OG  . SER A 122 ? 0.60481 0.67792 0.50636 -0.08682 0.08593  -0.20485 129 SER A OG  
880  N N   . MET A 123 ? 0.55683 0.61943 0.56913 -0.06625 0.02620  -0.15539 130 MET A N   
881  C CA  . MET A 123 ? 0.46445 0.51822 0.53342 -0.05070 0.01129  -0.15918 130 MET A CA  
882  C C   . MET A 123 ? 0.40053 0.45140 0.49652 -0.04792 -0.00611 -0.12560 130 MET A C   
883  O O   . MET A 123 ? 0.44984 0.48250 0.57911 -0.03820 -0.02069 -0.12051 130 MET A O   
884  C CB  . MET A 123 ? 0.42688 0.45123 0.48500 -0.05165 -0.00318 -0.17776 130 MET A CB  
885  C CG  . MET A 123 ? 0.55412 0.57304 0.61690 -0.04435 0.01365  -0.21938 130 MET A CG  
886  S SD  . MET A 123 ? 0.89504 0.88202 0.91613 -0.05698 -0.00075 -0.24905 130 MET A SD  
887  C CE  . MET A 123 ? 0.57931 0.57852 0.52729 -0.07589 -0.01430 -0.22519 130 MET A CE  
888  N N   . ILE A 124 ? 0.38971 0.45299 0.46839 -0.05733 -0.00175 -0.10345 131 ILE A N   
889  C CA  . ILE A 124 ? 0.32978 0.38748 0.42335 -0.05689 -0.01497 -0.07449 131 ILE A CA  
890  C C   . ILE A 124 ? 0.32963 0.39746 0.47067 -0.04237 -0.02058 -0.07209 131 ILE A C   
891  O O   . ILE A 124 ? 0.27940 0.33180 0.43251 -0.03806 -0.03443 -0.05169 131 ILE A O   
892  C CB  . ILE A 124 ? 0.29210 0.35641 0.35551 -0.07034 -0.00441 -0.05732 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.35107 0.40564 0.42307 -0.07073 -0.01473 -0.03133 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.31708 0.41090 0.38885 -0.07584 0.01679  -0.07038 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.31876 0.36680 0.35885 -0.08307 -0.00383 -0.01558 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.38753 0.48261 0.55603 -0.03336 -0.00983 -0.09184 132 GLY A N   
897  C CA  . GLY A 125 ? 0.34752 0.45871 0.56272 -0.01528 -0.02004 -0.08726 132 GLY A CA  
898  C C   . GLY A 125 ? 0.47772 0.55502 0.71624 0.00366  -0.03480 -0.08375 132 GLY A C   
899  O O   . GLY A 125 ? 0.36874 0.44267 0.63012 0.01840  -0.04960 -0.06571 132 GLY A O   
900  N N   . GLN A 126 ? 0.31432 0.36260 0.54335 0.00225  -0.03111 -0.10077 133 GLN A N   
901  C CA  . GLN A 126 ? 0.38228 0.38848 0.63284 0.01519  -0.04137 -0.09983 133 GLN A CA  
902  C C   . GLN A 126 ? 0.42112 0.39756 0.66148 0.00723  -0.05548 -0.06782 133 GLN A C   
903  O O   . GLN A 126 ? 0.41446 0.35154 0.67311 0.01585  -0.06195 -0.06035 133 GLN A O   
904  C CB  . GLN A 126 ? 0.37506 0.35774 0.61364 0.00876  -0.03363 -0.13133 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.39956 0.40285 0.64913 0.01917  -0.01398 -0.16741 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.61543 0.58749 0.84796 0.01324  -0.00696 -0.20215 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.69430 0.68207 0.89497 0.00397  0.00939  -0.22914 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.59355 0.51815 0.84306 0.01614  -0.01787 -0.20262 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.32957 0.32019 0.54205 -0.00913 -0.05661 -0.04930 134 PHE A N   
910  C CA  . PHE A 127 ? 0.38394 0.35177 0.58778 -0.01764 -0.06399 -0.02127 134 PHE A CA  
911  C C   . PHE A 127 ? 0.41296 0.39512 0.60863 -0.01480 -0.06698 0.00332  134 PHE A C   
912  O O   . PHE A 127 ? 0.39330 0.36019 0.57467 -0.02332 -0.06778 0.02580  134 PHE A O   
913  C CB  . PHE A 127 ? 0.34151 0.31045 0.52219 -0.03734 -0.06268 -0.02191 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.41561 0.37545 0.59588 -0.04317 -0.06460 -0.04868 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.32326 0.30226 0.48207 -0.04440 -0.05778 -0.07272 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.40307 0.33444 0.60143 -0.05035 -0.07168 -0.05167 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.39088 0.36067 0.53865 -0.05096 -0.06051 -0.09998 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.39167 0.31615 0.58712 -0.05889 -0.07607 -0.08127 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.36926 0.31289 0.53557 -0.05831 -0.07175 -0.10586 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.33235 0.34673 0.53817 -0.00447 -0.06786 -0.00329 135 GLY A N   
921  C CA  . GLY A 128 ? 0.35430 0.38561 0.55314 -0.00191 -0.07570 0.01511  135 GLY A CA  
922  C C   . GLY A 128 ? 0.43478 0.48191 0.60265 -0.02243 -0.06754 0.01989  135 GLY A C   
923  O O   . GLY A 128 ? 0.40962 0.46652 0.56462 -0.02438 -0.07367 0.03245  135 GLY A O   
924  N N   . VAL A 129 ? 0.36503 0.41173 0.51701 -0.03698 -0.05454 0.01019  136 VAL A N   
925  C CA  . VAL A 129 ? 0.35312 0.40351 0.47571 -0.05399 -0.04425 0.01659  136 VAL A CA  
926  C C   . VAL A 129 ? 0.35498 0.43028 0.47232 -0.06368 -0.03058 -0.00197 136 VAL A C   
927  O O   . VAL A 129 ? 0.33023 0.39576 0.42009 -0.07648 -0.01825 0.00059  136 VAL A O   
928  C CB  . VAL A 129 ? 0.32873 0.35180 0.43498 -0.06084 -0.04046 0.02877  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.37264 0.37310 0.48310 -0.05728 -0.04606 0.04846  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.28059 0.29905 0.39269 -0.05939 -0.04231 0.01531  136 VAL A CG2 
931  N N   . GLY A 130 ? 0.31962 0.34060 0.31959 -0.00583 -0.03654 -0.02477 137 GLY A N   
932  C CA  . GLY A 130 ? 0.29020 0.33125 0.29357 0.01141  -0.02893 -0.02996 137 GLY A CA  
933  C C   . GLY A 130 ? 0.32575 0.38749 0.34590 0.01199  -0.01118 -0.02265 137 GLY A C   
934  O O   . GLY A 130 ? 0.24884 0.32983 0.27380 0.01845  -0.00382 -0.02013 137 GLY A O   
935  N N   . PHE A 131 ? 0.26149 0.31665 0.28705 0.00417  -0.00582 -0.01865 138 PHE A N   
936  C CA  . PHE A 131 ? 0.29707 0.36244 0.33435 0.00521  0.00667  -0.01450 138 PHE A CA  
937  C C   . PHE A 131 ? 0.27056 0.35006 0.31856 0.00663  0.01284  -0.00736 138 PHE A C   
938  O O   . PHE A 131 ? 0.29297 0.37552 0.34477 0.00944  0.01826  -0.00325 138 PHE A O   
939  C CB  . PHE A 131 ? 0.29475 0.35049 0.33136 -0.00147 0.00952  -0.01373 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.32280 0.38362 0.36870 0.00044  0.01912  -0.01173 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.30480 0.36100 0.35168 0.00227  0.02066  -0.01402 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.30134 0.37222 0.35466 0.00136  0.02432  -0.00898 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.33179 0.38223 0.38289 0.00284  0.02480  -0.01329 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.35079 0.41793 0.40763 0.00786  0.02911  -0.01056 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.34859 0.39991 0.40232 0.00754  0.02813  -0.01255 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.27398 0.36159 0.32632 0.00370  0.00993  -0.00489 139 TYR A N   
947  C CA  . TYR A 132 ? 0.21929 0.32104 0.28178 0.00930  0.01287  0.00063  139 TYR A CA  
948  C C   . TYR A 132 ? 0.34167 0.44680 0.39830 0.01567  0.01030  0.00447  139 TYR A C   
949  O O   . TYR A 132 ? 0.30446 0.41354 0.36462 0.02189  0.01077  0.01110  139 TYR A O   
950  C CB  . TYR A 132 ? 0.19152 0.31246 0.26371 0.00427  0.00936  0.00143  139 TYR A CB  
951  C CG  . TYR A 132 ? 0.29793 0.42550 0.37463 -0.00380 0.01472  0.00066  139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.22766 0.36107 0.31020 0.00509  0.02379  -0.00105 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.23897 0.36384 0.30952 -0.02051 0.00910  0.00185  139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.18894 0.33454 0.27186 -0.00068 0.03008  -0.00256 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.34681 0.48123 0.41739 -0.03077 0.01500  0.00442  139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.25379 0.40308 0.33091 -0.01990 0.02700  0.00169  139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.30392 0.46886 0.37764 -0.02845 0.03422  0.00340  139 TYR A OH  
958  N N   . SER A 133 ? 0.28919 0.39337 0.33409 0.01640  0.00664  0.00012  140 SER A N   
959  C CA  . SER A 133 ? 0.25262 0.36741 0.28849 0.02211  0.00730  0.00442  140 SER A CA  
960  C C   . SER A 133 ? 0.26811 0.38211 0.30560 0.01935  0.01598  0.01416  140 SER A C   
961  O O   . SER A 133 ? 0.28255 0.40643 0.31141 0.01960  0.01767  0.02339  140 SER A O   
962  C CB  . SER A 133 ? 0.25128 0.37168 0.27300 0.02775  0.00218  -0.00630 140 SER A CB  
963  O OG  . SER A 133 ? 0.32575 0.44408 0.34835 0.02819  0.00569  -0.01226 140 SER A OG  
964  N N   . ALA A 134 ? 0.26031 0.36176 0.30593 0.01448  0.02000  0.01325  141 ALA A N   
965  C CA  . ALA A 134 ? 0.30321 0.39643 0.34978 0.00796  0.02408  0.02272  141 ALA A CA  
966  C C   . ALA A 134 ? 0.26467 0.34387 0.30720 0.01046  0.02061  0.03474  141 ALA A C   
967  O O   . ALA A 134 ? 0.27848 0.34916 0.31348 0.00261  0.02037  0.04800  141 ALA A O   
968  C CB  . ALA A 134 ? 0.26985 0.34726 0.32334 0.00428  0.02532  0.01661  141 ALA A CB  
969  N N   . TYR A 135 ? 0.26225 0.34013 0.30901 0.02067  0.01625  0.03128  142 TYR A N   
970  C CA  . TYR A 135 ? 0.28473 0.34987 0.32790 0.02962  0.00965  0.03982  142 TYR A CA  
971  C C   . TYR A 135 ? 0.37255 0.44784 0.40292 0.03097  0.00536  0.05061  142 TYR A C   
972  O O   . TYR A 135 ? 0.41832 0.48313 0.44309 0.04067  -0.00305 0.05837  142 TYR A O   
973  C CB  . TYR A 135 ? 0.25219 0.32618 0.30870 0.04232  0.00702  0.03017  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.32684 0.39018 0.38991 0.04404  0.01113  0.02089  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.28077 0.31631 0.33913 0.05471  0.00609  0.02063  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.29646 0.37264 0.36549 0.03603  0.01763  0.01204  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.29168 0.31773 0.35185 0.05882  0.00879  0.00938  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.29141 0.35996 0.36199 0.03795  0.02138  0.00393  142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.34416 0.39019 0.41065 0.05003  0.01765  0.00143  142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.37787 0.41657 0.44202 0.05454  0.02032  -0.00946 142 TYR A OH  
981  N N   . LEU A 136 ? 0.29977 0.39598 0.32295 0.02460  0.00961  0.04985  143 LEU A N   
982  C CA  . LEU A 136 ? 0.30205 0.40946 0.30678 0.02442  0.00754  0.06167  143 LEU A CA  
983  C C   . LEU A 136 ? 0.36315 0.45537 0.35522 0.01192  0.00963  0.08145  143 LEU A C   
984  O O   . LEU A 136 ? 0.36530 0.45067 0.33888 0.01161  0.00407  0.09796  143 LEU A O   
985  C CB  . LEU A 136 ? 0.31829 0.45566 0.31602 0.02488  0.01146  0.05184  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.38029 0.52624 0.38033 0.03404  0.00365  0.03524  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.32894 0.49281 0.31849 0.03765  0.00508  0.02196  143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.26943 0.41963 0.26080 0.04168  -0.00676 0.04002  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.34534 0.43064 0.34532 -0.00070 0.01555  0.08152  144 VAL A N   
990  C CA  . VAL A 137 ? 0.36342 0.43706 0.35286 -0.02027 0.01646  0.10154  144 VAL A CA  
991  C C   . VAL A 137 ? 0.36874 0.39542 0.36202 -0.02563 0.00864  0.10398  144 VAL A C   
992  O O   . VAL A 137 ? 0.43231 0.43345 0.41258 -0.04378 0.00317  0.12331  144 VAL A O   
993  C CB  . VAL A 137 ? 0.33314 0.44992 0.32732 -0.03465 0.02873  0.10108  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.35799 0.51977 0.34173 -0.02527 0.03466  0.09694  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.28624 0.40756 0.30142 -0.03181 0.03207  0.08113  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.34276 0.35608 0.35023 -0.01166 0.00664  0.08556  145 ALA A N   
997  C CA  . ALA A 138 ? 0.36278 0.33414 0.37140 -0.01248 -0.00102 0.08222  145 ALA A CA  
998  C C   . ALA A 138 ? 0.36593 0.30978 0.37175 0.01183  -0.01173 0.07548  145 ALA A C   
999  O O   . ALA A 138 ? 0.42058 0.39090 0.43649 0.02856  -0.00887 0.06490  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.35919 0.34359 0.38402 -0.01472 0.00610  0.06464  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.42557 0.31703 0.41739 0.01387  -0.02602 0.08101  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.52111 0.38644 0.51035 0.04306  -0.03795 0.06950  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.54052 0.40389 0.54069 0.05458  -0.03518 0.04657  146 GLU A C   
1004 O O   . GLU A 139 ? 0.50054 0.36660 0.50498 0.08253  -0.03924 0.03147  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.50759 0.30746 0.46949 0.04538  -0.05980 0.08476  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.57623 0.32277 0.52450 0.02554  -0.07008 0.08903  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.87978 0.55186 0.79504 0.02143  -0.09550 0.10905  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.97771 0.64608 0.87940 0.02852  -0.10207 0.12489  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 1.04357 0.65641 0.94342 0.01040  -0.11149 0.10944  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.45231 0.31689 0.45664 0.03487  -0.02849 0.04328  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.39971 0.26486 0.41031 0.04356  -0.02541 0.02249  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.40074 0.29482 0.42227 0.02131  -0.01319 0.02154  147 LYS A C   
1013 O O   . LYS A 140 ? 0.42081 0.31430 0.44105 -0.00232 -0.01316 0.03529  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.45788 0.26069 0.44960 0.05018  -0.04357 0.01631  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.48726 0.28808 0.48004 0.05313  -0.04133 -0.00392 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.57965 0.31779 0.55008 0.07090  -0.06217 -0.01695 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.60388 0.30724 0.56492 0.04806  -0.07133 -0.01970 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.85805 0.47916 0.79069 0.05394  -0.09972 -0.02305 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.37622 0.29906 0.40777 0.02912  -0.00348 0.00616  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.33034 0.27696 0.36952 0.01371  0.00492  0.00317  148 VAL A CA  
1021 C C   . VAL A 141 ? 0.36428 0.29845 0.39860 0.01907  0.00323  -0.01282 148 VAL A C   
1022 O O   . VAL A 141 ? 0.37298 0.31317 0.40498 0.03750  0.00570  -0.02470 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.32090 0.30972 0.37029 0.01507  0.01546  0.00256  148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.30376 0.30834 0.35652 0.00430  0.01972  -0.00221 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.28006 0.28173 0.33038 0.01181  0.01580  0.01568  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.37070 0.29373 0.40346 0.00303  -0.00099 -0.01337 149 THR A N   
1027 C CA  . THR A 142 ? 0.36335 0.27735 0.38924 0.00603  -0.00369 -0.02861 149 THR A CA  
1028 C C   . THR A 142 ? 0.46797 0.41382 0.50181 -0.00406 0.00295  -0.02963 149 THR A C   
1029 O O   . THR A 142 ? 0.37712 0.34060 0.42141 -0.01840 0.00385  -0.02046 149 THR A O   
1030 C CB  . THR A 142 ? 0.39635 0.26582 0.41160 -0.00367 -0.01969 -0.03091 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.52157 0.35085 0.52556 0.00503  -0.03056 -0.02707 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.38449 0.24096 0.38700 0.00588  -0.02449 -0.05060 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.32334 0.27819 0.35005 0.00498  0.00678  -0.04077 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.32558 0.30090 0.35336 -0.00104 0.00900  -0.04221 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.38320 0.34422 0.39747 -0.00009 0.00210  -0.05439 150 VAL A C   
1036 O O   . VAL A 143 ? 0.41985 0.37521 0.41908 0.01189  0.00437  -0.06368 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.36443 0.36126 0.39045 0.00463  0.01765  -0.03986 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.25208 0.25604 0.27163 0.00028  0.01476  -0.04137 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.39633 0.40655 0.43403 0.00371  0.02154  -0.02991 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.37728 0.33866 0.39692 -0.01201 -0.00640 -0.05513 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.33988 0.29247 0.34703 -0.01222 -0.01537 -0.06668 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.34689 0.32236 0.35325 -0.01121 -0.01474 -0.06557 151 ILE A C   
1043 O O   . ILE A 144 ? 0.39865 0.39567 0.42108 -0.01578 -0.01469 -0.05922 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.39923 0.33769 0.41371 -0.02769 -0.02938 -0.06876 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.44149 0.35323 0.45867 -0.03352 -0.03234 -0.06220 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.42173 0.33980 0.41715 -0.02461 -0.04153 -0.08451 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.45797 0.32872 0.45254 -0.01787 -0.03846 -0.07501 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.33951 0.30977 0.32392 -0.00351 -0.01535 -0.07184 152 THR A N   
1049 C CA  . THR A 145 ? 0.39527 0.37559 0.37107 -0.00150 -0.01803 -0.06868 152 THR A CA  
1050 C C   . THR A 145 ? 0.42349 0.39335 0.37387 0.00200  -0.02655 -0.07711 152 THR A C   
1051 O O   . THR A 145 ? 0.42874 0.38774 0.36201 0.00632  -0.02434 -0.08495 152 THR A O   
1052 C CB  . THR A 145 ? 0.31616 0.30112 0.28559 0.00080  -0.00793 -0.05892 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.42665 0.40908 0.38361 0.00158  -0.01570 -0.05474 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.35774 0.34157 0.30967 0.00442  0.00168  -0.06024 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.38413 0.35797 0.32979 0.00321  -0.03784 -0.07692 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.41920 0.38305 0.33780 0.00704  -0.04897 -0.08338 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.41235 0.37118 0.31300 0.01158  -0.05623 -0.07488 153 LYS A C   
1058 O O   . LYS A 146 ? 0.38918 0.35629 0.30515 0.01596  -0.06523 -0.07418 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.38659 0.35569 0.31770 0.00401  -0.06439 -0.09501 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.46959 0.43090 0.37318 0.00957  -0.07988 -0.10234 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.42354 0.36652 0.29167 0.01324  -0.07487 -0.10814 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.56493 0.50037 0.40418 0.01798  -0.09234 -0.11767 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.55474 0.48595 0.36592 0.02336  -0.09753 -0.10616 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.41023 0.42365 0.32474 -0.03528 -0.00572 0.02852  154 HIS A N   
1065 C CA  . HIS A 147 ? 0.44966 0.46233 0.33252 -0.04108 -0.00352 0.03443  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.43076 0.43708 0.29538 -0.04262 -0.01362 0.02521  154 HIS A C   
1067 O O   . HIS A 147 ? 0.39857 0.40346 0.26038 -0.03654 -0.01974 0.00936  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.39941 0.42403 0.26599 -0.04564 0.00518  0.03625  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.43480 0.45391 0.27555 -0.05466 0.00153  0.04780  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.46783 0.49057 0.28424 -0.06124 -0.00004 0.04797  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.44996 0.45475 0.28225 -0.05646 -0.00531 0.05968  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.49452 0.50693 0.29475 -0.07059 -0.00798 0.06189  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.53091 0.52992 0.33999 -0.06692 -0.01363 0.06737  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.42378 0.42138 0.27079 -0.04726 -0.01883 0.03332  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.42597 0.41182 0.25380 -0.04798 -0.03226 0.02557  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.46195 0.45306 0.25408 -0.04541 -0.02871 0.01392  155 ASN A C   
1077 O O   . ASN A 148 ? 0.51592 0.49301 0.28859 -0.03835 -0.04215 0.00069  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.52823 0.50351 0.33796 -0.05301 -0.03856 0.03660  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.47442 0.44574 0.31638 -0.04761 -0.04638 0.04407  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.45491 0.43035 0.33605 -0.04444 -0.05120 0.04328  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.49414 0.45878 0.32315 -0.04535 -0.04939 0.05356  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.47365 0.48591 0.25735 -0.04814 -0.01159 0.01990  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.55907 0.58935 0.31044 -0.04334 -0.00050 0.01722  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.48022 0.52785 0.23955 -0.02688 0.00886  0.00166  156 ASP A C   
1085 O O   . ASP A 149 ? 0.53635 0.60833 0.27007 -0.01657 0.02374  0.00085  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.51120 0.56099 0.25676 -0.05860 0.01126  0.04131  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.67234 0.69968 0.40065 -0.07191 -0.00298 0.05472  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.70058 0.70490 0.41154 -0.06746 -0.01682 0.04513  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.66804 0.69700 0.40267 -0.08584 -0.00507 0.07416  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.44908 0.48670 0.24278 -0.02197 0.00090  -0.00871 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.41142 0.46219 0.21520 -0.00599 0.00627  -0.02375 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.54970 0.57168 0.37979 0.00147  -0.01698 -0.03933 157 ASP A C   
1093 O O   . ASP A 150 ? 0.52753 0.52831 0.37772 -0.00824 -0.03254 -0.03260 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.40657 0.48419 0.23779 -0.01361 0.02348  -0.01015 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.41644 0.52602 0.24558 0.00372  0.03849  -0.01946 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.53211 0.63758 0.33556 0.02700  0.03399  -0.04113 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.47045 0.60820 0.32362 -0.00302 0.05230  -0.00561 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.51897 0.54240 0.35338 0.01948  -0.02064 -0.05780 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.44928 0.44234 0.31314 0.02588  -0.04840 -0.07100 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.46450 0.46096 0.37793 0.01061  -0.04435 -0.05268 158 GLU A C   
1101 O O   . GLU A 151 ? 0.45006 0.46852 0.36797 0.00067  -0.02229 -0.03636 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.57437 0.56198 0.41804 0.05537  -0.05832 -0.10011 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.65255 0.62045 0.44065 0.07978  -0.07381 -0.12321 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.11989 1.04305 0.91578 0.07160  -0.11073 -0.12546 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.22758 1.11890 1.06560 0.06863  -0.14411 -0.12997 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.12309 1.04349 0.88839 0.06671  -0.10851 -0.11979 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.42706 0.39829 0.37731 0.00967  -0.06935 -0.05354 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.39305 0.36661 0.38686 -0.00117 -0.06569 -0.03356 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.37382 0.35314 0.37047 0.01038  -0.06195 -0.04624 159 GLN A C   
1110 O O   . GLN A 152 ? 0.44717 0.41242 0.43645 0.02814  -0.08049 -0.07134 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.37825 0.32794 0.41935 -0.00898 -0.09401 -0.02173 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.40604 0.36325 0.49073 -0.01988 -0.08565 0.00829  159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.38225 0.33112 0.52206 -0.03197 -0.10568 0.03386  159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.53705 0.48677 0.68221 -0.03723 -0.11226 0.03951  159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.40765 0.35010 0.59394 -0.03722 -0.11693 0.05261  159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.35110 0.34746 0.35582 0.00373  -0.04158 -0.03076 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.37541 0.38046 0.38541 0.01374  -0.03729 -0.04099 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.41820 0.41202 0.45838 0.00655  -0.03981 -0.02228 160 TYR A C   
1119 O O   . TYR A 153 ? 0.35398 0.34472 0.40169 -0.00439 -0.03344 0.00254  160 TYR A O   
1120 C CB  . TYR A 153 ? 0.33413 0.37211 0.32289 0.01482  -0.01274 -0.04057 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.45460 0.51211 0.41322 0.02842  -0.00583 -0.05769 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.38815 0.45488 0.34134 0.05289  -0.00906 -0.08154 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.47832 0.54505 0.40952 0.02065  0.00415  -0.04931 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.48656 0.57483 0.40386 0.07249  0.00134  -0.09527 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.41871 0.50442 0.31608 0.03556  0.01294  -0.06095 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.53371 0.63206 0.42227 0.06307  0.01350  -0.08323 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.70645 0.82737 0.55332 0.08487  0.02626  -0.09302 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.50200 0.49065 0.55574 0.01649  -0.04842 -0.03398 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.37353 0.34806 0.45095 0.01248  -0.05303 -0.01734 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.42622 0.41447 0.49774 0.01948  -0.04276 -0.02399 161 ALA A C   
1131 O O   . ALA A 154 ? 0.42105 0.41746 0.49641 0.03348  -0.04863 -0.04701 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.44263 0.38837 0.55063 0.01575  -0.08338 -0.02226 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.36391 0.35364 0.42608 0.01286  -0.03016 -0.00433 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.30793 0.30226 0.36992 0.01730  -0.02799 -0.00592 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.35908 0.32521 0.43115 0.02066  -0.03974 0.00535  162 TRP A C   
1136 O O   . TRP A 155 ? 0.39123 0.34072 0.46348 0.01679  -0.04025 0.02616  162 TRP A O   
1137 C CB  . TRP A 155 ? 0.35150 0.35369 0.39121 0.01050  -0.01633 0.00713  162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.31353 0.31709 0.35743 0.01278  -0.02116 0.00751  162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.30658 0.34048 0.36562 0.01051  -0.01803 0.00145  162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.31181 0.28509 0.34648 0.01829  -0.03224 0.01770  162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.29923 0.32261 0.36768 0.01148  -0.03066 0.00680  162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.31965 0.30125 0.36738 0.01788  -0.04111 0.01402  162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.32779 0.26920 0.34451 0.02517  -0.03553 0.03237  162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.33290 0.28311 0.37193 0.02480  -0.05888 0.01950  162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.35249 0.26517 0.35222 0.03505  -0.04791 0.03865  162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.42536 0.33815 0.43404 0.03513  -0.06226 0.02971  162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.32605 0.28992 0.40931 0.02864  -0.04869 -0.00544 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.34361 0.27719 0.43441 0.03312  -0.06311 0.00370  163 GLU A CA  
1149 C C   . GLU A 156 ? 0.41093 0.34270 0.50634 0.04115  -0.07149 -0.00554 163 GLU A C   
1150 O O   . GLU A 156 ? 0.37666 0.33609 0.49028 0.04597  -0.07107 -0.02509 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.44577 0.36546 0.56289 0.03563  -0.08177 -0.00537 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.49296 0.37925 0.61979 0.03441  -0.09624 0.01609  163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.81629 0.68372 0.97493 0.03192  -0.12131 0.01319  163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.83800 0.69757 1.01042 0.04346  -0.14250 -0.01554 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.71914 0.57936 0.89200 0.01989  -0.12268 0.04044  163 GLU A OE2 
1156 N N   . SER A 157 ? 0.37741 0.27819 0.45714 0.04488  -0.07934 0.01045  164 SER A N   
1157 C CA  . SER A 157 ? 0.41660 0.30618 0.50147 0.05304  -0.09462 0.00272  164 SER A CA  
1158 C C   . SER A 157 ? 0.42916 0.27464 0.49292 0.06071  -0.10724 0.02008  164 SER A C   
1159 O O   . SER A 157 ? 0.47052 0.29844 0.49931 0.06259  -0.09744 0.04411  164 SER A O   
1160 C CB  . SER A 157 ? 0.39915 0.29893 0.47263 0.05057  -0.09251 0.00416  164 SER A CB  
1161 O OG  . SER A 157 ? 0.44549 0.33143 0.53120 0.05753  -0.11346 -0.00151 164 SER A OG  
1162 N N   . SER A 158 ? 0.40854 0.37130 0.44736 0.05984  0.04473  0.01734  165 SER A N   
1163 C CA  . SER A 158 ? 0.45271 0.41931 0.49071 0.06978  0.04767  0.02506  165 SER A CA  
1164 C C   . SER A 158 ? 0.42931 0.42429 0.47576 0.07787  0.03834  0.03180  165 SER A C   
1165 O O   . SER A 158 ? 0.47328 0.47489 0.51697 0.09201  0.04250  0.04060  165 SER A O   
1166 C CB  . SER A 158 ? 0.40586 0.34904 0.43456 0.07973  0.06379  0.03103  165 SER A CB  
1167 O OG  . SER A 158 ? 0.57522 0.48860 0.59929 0.06875  0.06729  0.02392  165 SER A OG  
1168 N N   . ALA A 159 ? 0.39828 0.40987 0.45673 0.06864  0.02448  0.02874  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.41721 0.45667 0.49259 0.07058  0.01086  0.03585  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.40424 0.45801 0.48931 0.08226  0.02356  0.05032  166 ALA A C   
1171 O O   . ALA A 159 ? 0.45486 0.49379 0.53146 0.08661  0.04012  0.05175  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.32830 0.37223 0.39474 0.07756  -0.00304 0.03334  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.40035 0.48247 0.50074 0.08964  0.01496  0.06131  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.34928 0.45224 0.46175 0.10377  0.02774  0.07915  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.31844 0.44729 0.45952 0.09822  0.02794  0.09188  167 GLY A C   
1176 O O   . GLY A 160 ? 0.36491 0.51574 0.51726 0.11351  0.04129  0.11083  167 GLY A O   
1177 N N   . GLY A 161 ? 0.36479 0.49263 0.51792 0.07963  0.01605  0.08514  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.31951 0.47547 0.50595 0.07362  0.01591  0.10147  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.34970 0.48745 0.52208 0.07522  0.03256  0.09925  168 GLY A C   
1180 O O   . GLY A 161 ? 0.29247 0.45323 0.49176 0.07174  0.03456  0.11485  168 GLY A O   
1181 N N   . SER A 162 ? 0.35036 0.44884 0.48343 0.08049  0.04342  0.08192  169 SER A N   
1182 C CA  . SER A 162 ? 0.42426 0.50383 0.53787 0.08547  0.05672  0.07801  169 SER A CA  
1183 C C   . SER A 162 ? 0.38347 0.42629 0.46974 0.07455  0.05138  0.05395  169 SER A C   
1184 O O   . SER A 162 ? 0.30811 0.33722 0.38648 0.06852  0.04438  0.04325  169 SER A O   
1185 C CB  . SER A 162 ? 0.35634 0.42577 0.44676 0.11155  0.07906  0.08662  169 SER A CB  
1186 O OG  . SER A 162 ? 0.40808 0.44496 0.47038 0.11799  0.08337  0.07467  169 SER A OG  
1187 N N   . PHE A 163 ? 0.30718 0.33796 0.38030 0.07423  0.05552  0.04831  170 PHE A N   
1188 C CA  . PHE A 163 ? 0.31522 0.31584 0.36461 0.06544  0.05079  0.02800  170 PHE A CA  
1189 C C   . PHE A 163 ? 0.40394 0.38468 0.42485 0.07851  0.06079  0.02333  170 PHE A C   
1190 O O   . PHE A 163 ? 0.41599 0.41017 0.43652 0.09478  0.07220  0.03743  170 PHE A O   
1191 C CB  . PHE A 163 ? 0.34990 0.35909 0.41311 0.04787  0.03664  0.02244  170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.37550 0.40471 0.45554 0.04714  0.03722  0.03400  170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.32657 0.38340 0.44101 0.04182  0.03124  0.05025  170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.28120 0.30197 0.34461 0.05163  0.04252  0.03004  170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.34203 0.41720 0.47884 0.03929  0.03271  0.06510  170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.29570 0.33552 0.37560 0.05326  0.04605  0.04447  170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.27551 0.34230 0.39461 0.04620  0.04220  0.06338  170 PHE A CZ  
1198 N N   . THR A 164 ? 0.38590 0.33550 0.38289 0.07271  0.05554  0.00463  171 THR A N   
1199 C CA  . THR A 164 ? 0.40418 0.32735 0.36672 0.08471  0.05872  -0.00548 171 THR A CA  
1200 C C   . THR A 164 ? 0.40108 0.32306 0.36014 0.07190  0.04667  -0.01786 171 THR A C   
1201 O O   . THR A 164 ? 0.41530 0.34433 0.39208 0.05302  0.03627  -0.02281 171 THR A O   
1202 C CB  . THR A 164 ? 0.48592 0.36587 0.41982 0.09010  0.05948  -0.01805 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.52157 0.39033 0.46706 0.06796  0.04743  -0.02878 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.42365 0.30397 0.35798 0.10630  0.07349  -0.00436 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.39985 0.31418 0.33302 0.08630  0.04928  -0.02121 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.44784 0.36077 0.37132 0.07935  0.03811  -0.03290 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.49218 0.36822 0.36905 0.09435  0.03346  -0.04987 172 VAL A C   
1208 O O   . VAL A 165 ? 0.48284 0.34595 0.33052 0.12070  0.04543  -0.04538 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.37857 0.32353 0.31679 0.08437  0.04431  -0.01775 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.38512 0.32725 0.30569 0.08366  0.03489  -0.02909 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.33297 0.30464 0.31333 0.06681  0.04226  -0.00572 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.50475 0.36359 0.37379 0.07911  0.01498  -0.06861 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.58625 0.40575 0.40987 0.09002  0.00282  -0.08888 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.59940 0.42696 0.42587 0.07480  -0.01746 -0.10151 173 ARG A C   
1215 O O   . ARG A 166 ? 0.47403 0.32948 0.33885 0.05269  -0.02223 -0.09604 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.60973 0.38391 0.41997 0.08475  -0.00387 -0.10125 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.68413 0.45964 0.53181 0.05168  -0.01781 -0.10516 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.66566 0.40258 0.51100 0.04755  -0.01642 -0.10779 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.76057 0.51631 0.62476 0.05517  0.00512  -0.08840 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.84427 0.57311 0.70584 0.05831  0.01286  -0.08506 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.64675 0.32296 0.48828 0.05322  0.00166  -0.09952 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.71076 0.46452 0.59046 0.06667  0.03071  -0.06655 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.56734 0.37059 0.34947 0.09020  -0.02960 -0.11793 174 THR A N   
1224 C CA  . THR A 167 ? 0.59578 0.40432 0.37784 0.07624  -0.05355 -0.13219 174 THR A CA  
1225 C C   . THR A 167 ? 0.61682 0.40784 0.42401 0.04498  -0.07415 -0.14333 174 THR A C   
1226 O O   . THR A 167 ? 0.75458 0.50103 0.54472 0.04370  -0.08037 -0.15435 174 THR A O   
1227 C CB  . THR A 167 ? 0.74123 0.52275 0.46331 0.10281  -0.06525 -0.14958 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.82381 0.62843 0.52845 0.13347  -0.04228 -0.13288 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.76634 0.55603 0.48979 0.08756  -0.09432 -0.16506 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.61106 0.43703 0.46010 0.02123  -0.08314 -0.13760 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.71913 0.54067 0.60486 -0.00891 -0.09830 -0.13934 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.74249 0.53989 0.61372 -0.02016 -0.13170 -0.16077 175 ASP A C   
1233 O O   . ASP A 168 ? 0.70536 0.52216 0.56501 -0.01541 -0.14549 -0.16735 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.57475 0.44698 0.51101 -0.02505 -0.09141 -0.12016 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.69098 0.56547 0.67044 -0.05242 -0.10081 -0.11415 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.84181 0.68603 0.82451 -0.05739 -0.09604 -0.11357 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.68954 0.59821 0.70140 -0.06727 -0.11124 -0.10693 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.87676 0.63044 0.74905 -0.03523 -0.14621 -0.17131 176 THR A N   
1239 C CA  . THR A 169 ? 1.03769 0.76110 0.90216 -0.05205 -0.18376 -0.19269 176 THR A CA  
1240 C C   . THR A 169 ? 0.99415 0.74294 0.92680 -0.09067 -0.19890 -0.18072 176 THR A C   
1241 O O   . THR A 169 ? 0.96459 0.68999 0.90503 -0.11215 -0.23319 -0.19517 176 THR A O   
1242 C CB  . THR A 169 ? 1.05134 0.69769 0.86639 -0.04238 -0.19404 -0.21425 176 THR A CB  
1243 O OG1 . THR A 169 ? 1.03452 0.66402 0.87333 -0.05012 -0.17414 -0.20039 176 THR A OG1 
1244 C CG2 . THR A 169 ? 1.01152 0.63462 0.75413 0.00089  -0.18139 -0.22519 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.90760 0.70333 0.88959 -0.09883 -0.17519 -0.15357 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.75905 0.58547 0.80745 -0.12973 -0.18283 -0.13519 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.76035 0.63937 0.83672 -0.13997 -0.20034 -0.13009 177 GLY A C   
1248 O O   . GLY A 170 ? 0.72581 0.60329 0.76807 -0.12999 -0.21905 -0.14834 177 GLY A O   
1249 N N   . GLU A 171 ? 0.80215 0.73042 0.93960 -0.15641 -0.19246 -0.10271 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.73118 0.71648 0.90309 -0.16549 -0.20634 -0.09172 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.66025 0.67465 0.79773 -0.13711 -0.19171 -0.09291 178 GLU A C   
1252 O O   . GLU A 171 ? 0.48800 0.51094 0.61481 -0.11863 -0.16095 -0.08150 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.72884 0.76204 0.96992 -0.18131 -0.19297 -0.05661 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.79881 0.89291 1.08743 -0.19488 -0.21043 -0.04063 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.06183 1.18033 1.42649 -0.22579 -0.21906 -0.01402 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.10681 1.23644 1.49981 -0.22363 -0.19121 0.01214  178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.09667 1.22123 1.47720 -0.24197 -0.24251 -0.01878 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.60880 0.63693 0.72794 -0.13263 -0.21399 -0.10613 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.60639 0.66725 0.70109 -0.10661 -0.19850 -0.10146 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.53431 0.64975 0.67235 -0.10617 -0.17712 -0.07076 179 PRO A C   
1261 O O   . PRO A 172 ? 0.63785 0.78424 0.82998 -0.12625 -0.18332 -0.05215 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.50945 0.58097 0.58789 -0.10637 -0.23152 -0.11781 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.57123 0.59382 0.63980 -0.12468 -0.26406 -0.14147 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.59592 0.59635 0.70161 -0.14648 -0.25502 -0.13084 179 PRO A CD  
1265 N N   . MET A 173 ? 0.50674 0.63227 0.61999 -0.08147 -0.15170 -0.06407 180 MET A N   
1266 C CA  . MET A 173 ? 0.56923 0.73181 0.70796 -0.07412 -0.12868 -0.03821 180 MET A CA  
1267 C C   . MET A 173 ? 0.47930 0.68218 0.61305 -0.05789 -0.12671 -0.02910 180 MET A C   
1268 O O   . MET A 173 ? 0.61734 0.85227 0.77127 -0.05000 -0.11053 -0.00682 180 MET A O   
1269 C CB  . MET A 173 ? 0.49130 0.62714 0.60716 -0.05943 -0.10146 -0.03631 180 MET A CB  
1270 C CG  . MET A 173 ? 0.56790 0.69825 0.71157 -0.06888 -0.08924 -0.02285 180 MET A CG  
1271 S SD  . MET A 173 ? 0.67193 0.78239 0.78934 -0.04858 -0.06153 -0.01887 180 MET A SD  
1272 C CE  . MET A 173 ? 0.35117 0.42618 0.42330 -0.03877 -0.06428 -0.04151 180 MET A CE  
1273 N N   . GLY A 174 ? 0.40498 0.60551 0.50831 -0.04892 -0.14141 -0.04468 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.48013 0.71587 0.57381 -0.02977 -0.13701 -0.03533 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.38935 0.60811 0.44931 -0.00534 -0.10925 -0.03147 181 GLY A C   
1276 O O   . GLY A 174 ? 0.43658 0.64417 0.46012 0.01194  -0.10777 -0.04026 181 GLY A O   
1277 N N   . ARG A 175 ? 0.30406 0.51960 0.37603 -0.00318 -0.08818 -0.01739 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.29183 0.48567 0.33730 0.01510  -0.06582 -0.01398 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.28716 0.47386 0.34758 0.01298  -0.05108 -0.00266 182 ARG A C   
1280 O O   . ARG A 175 ? 0.34366 0.55822 0.43225 0.00911  -0.05053 0.01219  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.29302 0.50764 0.32361 0.03626  -0.05833 -0.00363 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.29122 0.47573 0.29352 0.05247  -0.03991 -0.00237 182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.29392 0.49315 0.28601 0.07304  -0.02885 0.01251  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.33010 0.54976 0.33979 0.07593  -0.02368 0.02717  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.31521 0.57912 0.34149 0.08144  -0.02812 0.04022  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.29671 0.58912 0.32453 0.08242  -0.04155 0.03788  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.28238 0.56464 0.32325 0.08861  -0.01901 0.05749  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.26827 0.42036 0.31049 0.01723  -0.03952 -0.00782 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.25739 0.39904 0.30448 0.01989  -0.02748 0.00063  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.28822 0.39989 0.33385 0.01027  -0.02627 -0.00877 183 GLY A C   
1291 O O   . GLY A 176 ? 0.31459 0.40911 0.34998 0.00555  -0.03098 -0.02096 183 GLY A O   
1292 N N   . THR A 177 ? 0.30449 0.41095 0.35748 0.01131  -0.01877 -0.00147 184 THR A N   
1293 C CA  . THR A 177 ? 0.29273 0.37373 0.34373 0.00590  -0.01600 -0.00743 184 THR A CA  
1294 C C   . THR A 177 ? 0.30848 0.39863 0.38109 0.00075  -0.01282 0.00256  184 THR A C   
1295 O O   . THR A 177 ? 0.27509 0.38516 0.35551 0.01005  -0.00651 0.01744  184 THR A O   
1296 C CB  . THR A 177 ? 0.36361 0.42258 0.39451 0.01720  -0.00982 -0.00845 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.33666 0.38736 0.35438 0.02028  -0.01096 -0.01349 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.35860 0.39827 0.39053 0.01269  -0.00835 -0.01249 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.26683 0.34192 0.34786 -0.01114 -0.01516 -0.00320 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.24987 0.32916 0.35296 -0.01644 -0.01032 0.00805  185 LYS A CA  
1301 C C   . LYS A 178 ? 0.31513 0.36829 0.40501 -0.01193 -0.00368 0.00371  185 LYS A C   
1302 O O   . LYS A 178 ? 0.34946 0.38132 0.42964 -0.01730 -0.00727 -0.00880 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.26145 0.34493 0.39099 -0.03683 -0.02151 0.00689  185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.46121 0.53344 0.61123 -0.04578 -0.01685 0.01492  185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.35088 0.43760 0.54072 -0.06702 -0.02829 0.02344  185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.41266 0.49795 0.59748 -0.07891 -0.04985 0.00611  185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.59054 0.66547 0.80431 -0.10409 -0.06836 0.00366  185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.27205 0.32819 0.35897 0.00120  0.00611  0.01502  186 VAL A N   
1309 C CA  . VAL A 179 ? 0.26481 0.30117 0.33898 0.00816  0.01086  0.01251  186 VAL A CA  
1310 C C   . VAL A 179 ? 0.28991 0.33044 0.38399 0.00676  0.01963  0.02680  186 VAL A C   
1311 O O   . VAL A 179 ? 0.29014 0.34995 0.39384 0.01687  0.02831  0.04460  186 VAL A O   
1312 C CB  . VAL A 179 ? 0.25698 0.28753 0.30531 0.02704  0.01188  0.01208  186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.26134 0.27536 0.29859 0.03345  0.01266  0.00912  186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.25687 0.28085 0.29114 0.02614  0.00381  0.00119  186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.26539 0.28736 0.36501 -0.00315 0.01933  0.02160  187 ILE A N   
1316 C CA  . ILE A 180 ? 0.29420 0.31369 0.41418 -0.00622 0.02816  0.03573  187 ILE A CA  
1317 C C   . ILE A 180 ? 0.33615 0.34265 0.43751 0.00985  0.03660  0.03716  187 ILE A C   
1318 O O   . ILE A 180 ? 0.36948 0.35788 0.45553 0.00964  0.03290  0.02417  187 ILE A O   
1319 C CB  . ILE A 180 ? 0.35277 0.35355 0.48911 -0.02761 0.02047  0.02870  187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.35646 0.36978 0.50504 -0.04262 0.00614  0.02230  187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.30782 0.30463 0.47214 -0.03361 0.02941  0.04707  187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.47042 0.45728 0.62348 -0.06165 -0.00793 0.00856  187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.30631 0.32503 0.40854 0.02647  0.04830  0.05492  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.30205 0.31207 0.38371 0.04568  0.05483  0.05747  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.30899 0.31242 0.40976 0.04448  0.06811  0.07348  188 LEU A C   
1326 O O   . LEU A 181 ? 0.31717 0.33581 0.43903 0.04859  0.08032  0.09610  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.31260 0.33511 0.37121 0.07171  0.05827  0.06516  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.35194 0.37769 0.39197 0.07544  0.04732  0.05396  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.42517 0.45758 0.43858 0.10581  0.05338  0.06474  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.31218 0.32017 0.33450 0.06911  0.03164  0.03198  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.31484 0.29620 0.40965 0.04042  0.06737  0.06472  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.33404 0.30237 0.44032 0.04330  0.08102  0.07947  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.34124 0.31903 0.42662 0.07240  0.09099  0.09059  189 HIS A C   
1334 O O   . HIS A 182 ? 0.40777 0.37989 0.47005 0.08320  0.08588  0.07997  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.34425 0.28231 0.44577 0.03235  0.07715  0.06578  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.40979 0.33531 0.51815 0.00962  0.06339  0.04954  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.38169 0.28620 0.51116 -0.00976 0.06063  0.05129  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.39485 0.32461 0.49029 0.00442  0.05038  0.03159  189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.46582 0.36219 0.59042 -0.02413 0.04481  0.03280  189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.42865 0.34167 0.53273 -0.01453 0.04054  0.02205  189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.35101 0.34593 0.44497 0.08690  0.10480  0.11382  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.36397 0.36968 0.42880 0.12049  0.11203  0.12314  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.45554 0.44925 0.51140 0.13431  0.12175  0.13004  190 LEU A C   
1344 O O   . LEU A 183 ? 0.49451 0.47238 0.57302 0.12154  0.13137  0.13841  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.37580 0.40465 0.45077 0.13762  0.12858  0.15090  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.36423 0.41090 0.44368 0.13305  0.12223  0.14929  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.38237 0.45563 0.46427 0.16095  0.14232  0.18114  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.36635 0.40386 0.40662 0.13814  0.10147  0.12047  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.48453 0.40050 0.36271 0.10889  0.00137  0.05835  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.53594 0.45538 0.42801 0.13304  0.00260  0.08008  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.55739 0.43248 0.44446 0.12055  -0.00525 0.09710  191 LYS A C   
1352 O O   . LYS A 184 ? 0.58642 0.45517 0.47297 0.08907  -0.01039 0.09521  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.45906 0.46088 0.38190 0.13680  0.00042  0.09460  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.49444 0.54596 0.44051 0.14804  0.01368  0.08538  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.40187 0.53582 0.39029 0.13742  0.00467  0.09328  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.49391 0.67158 0.51221 0.12883  0.02080  0.08432  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.41514 0.66916 0.48587 0.11256  0.00758  0.08718  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.62023 0.46560 0.50742 0.14779  -0.00309 0.11750  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.70221 0.49309 0.58440 0.13804  -0.00407 0.14103  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.68481 0.52260 0.56780 0.11574  -0.00627 0.16370  192 GLU A C   
1361 O O   . GLU A 185 ? 0.73258 0.54052 0.61659 0.08937  -0.00167 0.17468  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.69445 0.44541 0.57358 0.17843  -0.00022 0.16514  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.90677 0.60555 0.77967 0.17225  0.00333  0.20319  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.15291 0.74482 1.02364 0.18760  0.00890  0.20549  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.16700 0.69363 1.04511 0.15614  0.01276  0.21217  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.26078 0.83355 1.12785 0.23104  0.01029  0.19982  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.59645 0.50943 0.48132 0.12577  -0.01277 0.16874  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.67690 0.63326 0.54951 0.11305  -0.01666 0.18541  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.59937 0.58956 0.47708 0.08038  -0.01746 0.16055  193 ASP A C   
1370 O O   . ASP A 186 ? 0.58598 0.61795 0.45065 0.07357  -0.02111 0.16513  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.62890 0.64730 0.49885 0.14167  -0.03129 0.19809  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.59823 0.67722 0.49990 0.14239  -0.04031 0.16992  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.64067 0.70205 0.55763 0.13268  -0.03018 0.14747  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.76807 0.91274 0.67963 0.15241  -0.05791 0.17093  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.49131 0.46166 0.38166 0.06456  -0.01522 0.13376  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.45889 0.45620 0.35473 0.03935  -0.01679 0.11249  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.47603 0.43374 0.37943 0.01633  -0.01387 0.10405  194 GLN A C   
1378 O O   . GLN A 187 ? 0.52608 0.49039 0.43501 0.00360  -0.01832 0.08178  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.44762 0.47137 0.35276 0.04344  -0.01947 0.09040  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.43794 0.51222 0.35646 0.06132  -0.02434 0.09592  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.43620 0.55718 0.35195 0.05333  -0.03571 0.09871  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.55272 0.67528 0.45884 0.03367  -0.03520 0.08947  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.41210 0.57266 0.33468 0.07227  -0.04810 0.10906  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.48310 0.40055 0.39147 0.01052  -0.00755 0.12350  195 THR A N   
1385 C CA  . THR A 188 ? 0.55392 0.44023 0.48635 -0.01609 -0.00809 0.11483  195 THR A CA  
1386 C C   . THR A 188 ? 0.47346 0.40398 0.42317 -0.03744 -0.00188 0.11651  195 THR A C   
1387 O O   . THR A 188 ? 0.47192 0.39462 0.45436 -0.06008 -0.00512 0.10666  195 THR A O   
1388 C CB  . THR A 188 ? 0.53373 0.36004 0.47860 -0.02083 -0.00042 0.13783  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.54611 0.38867 0.48090 -0.01558 0.01703  0.17792  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.63343 0.40624 0.56141 0.00522  -0.00632 0.13135  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.40447 0.38268 0.33519 -0.02887 0.00506  0.12567  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.48390 0.50176 0.42516 -0.04200 0.01496  0.12521  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.40892 0.44175 0.36959 -0.05169 0.00314  0.09437  196 GLU A C   
1394 O O   . GLU A 189 ? 0.41369 0.47140 0.39968 -0.06348 0.01017  0.09216  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.42454 0.48231 0.32878 -0.02573 0.02009  0.13270  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.48320 0.56569 0.37577 -0.01770 0.00351  0.10467  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.56351 0.68047 0.42141 -0.00275 -0.00052 0.10620  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.65161 0.77213 0.49516 0.01318  -0.01089 0.11627  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.57824 0.71964 0.42304 -0.00428 0.00430  0.09465  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.39497 0.41501 0.34418 -0.04353 -0.01211 0.07390  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.39445 0.42179 0.35088 -0.04717 -0.02336 0.05033  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.42688 0.42744 0.40503 -0.05832 -0.03736 0.03833  197 TYR A C   
1403 O O   . TYR A 190 ? 0.40284 0.40374 0.37729 -0.05564 -0.05184 0.01957  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.34307 0.36959 0.27445 -0.03290 -0.02814 0.03945  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.32037 0.37803 0.24208 -0.02679 -0.02212 0.04502  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.33127 0.41496 0.25443 -0.03109 -0.01985 0.03774  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.31247 0.37420 0.22535 -0.01456 -0.02183 0.05452  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.36271 0.47099 0.27412 -0.02670 -0.02075 0.03518  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.39462 0.49112 0.30308 -0.01009 -0.02461 0.05523  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.38993 0.50729 0.29537 -0.01791 -0.02569 0.04333  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.40553 0.55338 0.30345 -0.01459 -0.03456 0.03646  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.43107 0.40567 0.43096 -0.07052 -0.03541 0.04889  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.43518 0.38983 0.47119 -0.08905 -0.05259 0.03465  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.49455 0.48604 0.59015 -0.11229 -0.04274 0.04758  198 LEU A C   
1415 O O   . LEU A 191 ? 0.45347 0.44336 0.59744 -0.13236 -0.06008 0.03464  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.49895 0.39078 0.53119 -0.09152 -0.05808 0.03392  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.56781 0.42311 0.54616 -0.06379 -0.06223 0.02218  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.52810 0.31681 0.50572 -0.06199 -0.06214 0.02529  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.48576 0.33783 0.43613 -0.05338 -0.08344 -0.00995 198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.45081 0.47880 0.54536 -0.10896 -0.01565 0.07126  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.44533 0.51587 0.59412 -0.12581 0.00382  0.08759  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.37575 0.49620 0.54505 -0.11968 -0.00400 0.06837  199 GLU A C   
1423 O O   . GLU A 192 ? 0.36128 0.48734 0.48710 -0.09871 -0.00936 0.05496  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.49909 0.58452 0.62235 -0.11752 0.03918  0.12133  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.72483 0.76109 0.83360 -0.12087 0.05003  0.14993  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.97790 1.02380 1.02882 -0.09840 0.07314  0.17834  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.97732 1.06372 0.99461 -0.08125 0.07612  0.16779  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.93970 0.94888 0.97620 -0.09614 0.08586  0.21028  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.40642 0.56326 0.64976 -0.13822 -0.00434 0.06856  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.38508 0.58974 0.65788 -0.12846 -0.01682 0.05014  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.43319 0.67311 0.67952 -0.10540 0.01185  0.05710  200 GLU A C   
1432 O O   . GLU A 193 ? 0.29774 0.54272 0.51865 -0.08400 0.00007  0.03894  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.31594 0.56407 0.68931 -0.15365 -0.02360 0.05047  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.47503 0.78294 0.89067 -0.13880 -0.03669 0.03498  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.49811 0.85669 1.02550 -0.16493 -0.05427 0.03058  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.51328 0.86118 1.09190 -0.19972 -0.04748 0.04325  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.60442 1.01359 1.17398 -0.15087 -0.07606 0.01526  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.29765 0.55654 0.54434 -0.10755 0.05031  0.08334  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.37334 0.66321 0.58690 -0.08277 0.07718  0.08429  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.32076 0.57415 0.45009 -0.06255 0.06566  0.06898  201 ARG A C   
1441 O O   . ARG A 194 ? 0.37243 0.63735 0.47684 -0.04175 0.06895  0.05204  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.38606 0.70178 0.60397 -0.08593 0.12262  0.11790  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.59788 0.87325 0.80460 -0.10500 0.12926  0.14701  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.60356 0.90523 0.81668 -0.10723 0.17959  0.18864  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.84812 1.10591 0.99003 -0.09986 0.18930  0.21559  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.87000 1.12710 0.97428 -0.08900 0.22414  0.24455  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.73737 1.03411 0.86631 -0.08599 0.25640  0.24968  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.85248 1.06392 0.88889 -0.07727 0.22146  0.26357  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.37174 0.58153 0.46361 -0.06826 0.05227  0.07361  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.34315 0.52884 0.37260 -0.05293 0.04044  0.06017  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.33894 0.51096 0.36840 -0.04711 0.01613  0.03479  202 ARG A C   
1452 O O   . ARG A 195 ? 0.40419 0.57319 0.40495 -0.03425 0.01419  0.01984  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.34951 0.50108 0.35087 -0.05670 0.03412  0.07419  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.30295 0.44281 0.25652 -0.04310 0.02147  0.06236  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.43927 0.60368 0.35465 -0.02917 0.03260  0.06021  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.42276 0.58197 0.30388 -0.02080 0.01588  0.05062  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.50252 0.66886 0.36804 -0.01571 0.00553  0.02502  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.39428 0.56497 0.26555 -0.01309 0.01167  0.00634  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.41682 0.58580 0.26711 -0.01303 -0.01215 0.01728  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.27701 0.43643 0.33545 -0.05605 -0.00336 0.02979  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.32508 0.46935 0.37382 -0.04612 -0.02458 0.01203  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.37214 0.54351 0.44054 -0.03218 -0.02041 0.00323  203 ILE A C   
1463 O O   . ILE A 196 ? 0.30898 0.46240 0.35230 -0.01814 -0.02532 -0.00696 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.33072 0.45746 0.39570 -0.05401 -0.04958 0.00615  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.34262 0.43274 0.38330 -0.06184 -0.05156 0.01131  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.34263 0.45402 0.38508 -0.03796 -0.06975 -0.00686 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.39831 0.46630 0.45651 -0.07208 -0.07536 0.00075  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.26587 0.47987 0.38471 -0.03494 -0.00860 0.00880  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.32452 0.56949 0.46732 -0.01536 -0.00060 0.00055  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.30845 0.54082 0.40368 0.00099  0.01852  -0.00804 204 LYS A C   
1471 O O   . LYS A 197 ? 0.29461 0.51433 0.38060 0.02067  0.01497  -0.02255 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.25106 0.55527 0.46499 -0.02170 0.01685  0.01150  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.25413 0.58538 0.53649 -0.03065 -0.01105 0.00846  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.26254 0.66220 0.63317 -0.04271 0.01082  0.02208  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.28496 0.70990 0.73288 -0.06515 -0.02314 0.01794  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.38091 0.87110 0.92787 -0.08849 0.00256  0.03636  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.35841 0.58993 0.42089 -0.00545 0.03617  -0.00029 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.36939 0.58957 0.38109 0.00921  0.04708  -0.01466 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.38246 0.55717 0.36335 0.00913  0.02513  -0.03113 205 GLU A C   
1480 O O   . GLU A 198 ? 0.41647 0.57326 0.37836 0.02236  0.02560  -0.05189 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.36838 0.59808 0.34436 0.00444  0.06312  -0.00031 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.49337 0.71287 0.40807 0.01931  0.06533  -0.01984 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.56002 0.78842 0.43077 0.01864  0.07345  -0.00211 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.50914 0.72808 0.38869 0.00371  0.06468  0.01955  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.58191 0.82382 0.40384 0.03709  0.08819  -0.00991 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.34390 0.49734 0.32237 -0.00552 0.00839  -0.02217 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.36034 0.47756 0.31784 -0.00798 -0.00530 -0.03130 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.39250 0.48700 0.36242 0.00280  -0.01270 -0.03683 206 ILE A C   
1489 O O   . ILE A 199 ? 0.42116 0.48469 0.37882 0.00658  -0.01399 -0.04792 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.36995 0.47662 0.32066 -0.02083 -0.01427 -0.01803 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.35169 0.47530 0.28628 -0.02552 -0.00860 -0.01004 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.32232 0.40005 0.26260 -0.02354 -0.02154 -0.02204 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.44230 0.55608 0.37579 -0.03206 -0.01447 0.00466  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.35873 0.46625 0.35484 0.00803  -0.01994 -0.02859 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.33057 0.41898 0.33322 0.02494  -0.03073 -0.02961 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.38968 0.47644 0.40072 0.04485  -0.01965 -0.04293 207 VAL A C   
1497 O O   . VAL A 200 ? 0.43077 0.47554 0.42879 0.05700  -0.02204 -0.04686 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.39276 0.50626 0.42476 0.02835  -0.04827 -0.02236 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.31149 0.41842 0.35373 0.05451  -0.06112 -0.02249 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.33930 0.43331 0.34751 0.01564  -0.06257 -0.01571 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.35048 0.47878 0.38190 0.05032  -0.00384 -0.04883 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.38936 0.51757 0.42476 0.07554  0.01065  -0.06543 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.48914 0.57141 0.48031 0.07403  0.01525  -0.08639 208 LYS A C   
1504 O O   . LYS A 201 ? 0.51850 0.56993 0.50386 0.09506  0.01995  -0.10487 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.37957 0.56928 0.44398 0.08311  0.03378  -0.06417 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.51689 0.72142 0.60215 0.11844  0.05024  -0.07835 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.62727 0.89700 0.73635 0.12660  0.08348  -0.07461 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.75501 1.01075 0.79811 0.12583  0.10351  -0.08794 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.77940 1.08004 0.82433 0.10668  0.12285  -0.06368 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.42409 0.50045 0.38811 0.05037  0.01121  -0.08596 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.46838 0.51103 0.39942 0.04489  0.00850  -0.10992 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.49209 0.47955 0.42655 0.03362  -0.00436 -0.11012 209 LYS A C   
1513 O O   . LYS A 202 ? 0.50080 0.44407 0.42750 0.03667  -0.00607 -0.13317 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.50879 0.57763 0.41529 0.02782  0.00628  -0.10807 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.54954 0.59752 0.42367 0.02288  -0.00377 -0.13818 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.55492 0.63380 0.40766 0.00964  -0.01249 -0.13089 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.64542 0.71670 0.46198 0.00953  -0.02836 -0.16606 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.65686 0.76353 0.45234 0.00226  -0.04175 -0.15637 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.48311 0.46847 0.42808 0.02111  -0.01114 -0.08467 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.43775 0.37838 0.38417 0.00728  -0.01559 -0.07706 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.47321 0.38191 0.42309 0.02232  -0.01569 -0.05541 210 HIS A C   
1522 O O   . HIS A 203 ? 0.57304 0.43517 0.52185 0.01503  -0.01241 -0.04503 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.42042 0.38260 0.36635 -0.01541 -0.01887 -0.06372 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.46666 0.45606 0.40715 -0.02839 -0.02404 -0.08159 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.55936 0.52962 0.50092 -0.03800 -0.03112 -0.10856 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.46471 0.49630 0.39583 -0.03128 -0.02630 -0.07633 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.54853 0.55496 0.47766 -0.04416 -0.04078 -0.12034 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.58974 0.63235 0.51110 -0.03866 -0.03593 -0.09778 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.48395 0.42399 0.28039 -0.02881 -0.10550 -0.04190 211 SER A N   
1530 C CA  . SER A 204 ? 0.44522 0.41761 0.30681 -0.01847 -0.08068 -0.04160 211 SER A CA  
1531 C C   . SER A 204 ? 0.48419 0.45499 0.32558 -0.00642 -0.04239 -0.05466 211 SER A C   
1532 O O   . SER A 204 ? 0.53291 0.53486 0.41850 0.00224  -0.02051 -0.04815 211 SER A O   
1533 C CB  . SER A 204 ? 0.49897 0.51015 0.41493 -0.01596 -0.07647 -0.02063 211 SER A CB  
1534 O OG  . SER A 204 ? 0.45815 0.47575 0.40635 -0.02327 -0.10750 -0.00792 211 SER A OG  
1535 N N   . GLN A 205 ? 0.56065 0.49429 0.33682 -0.00494 -0.03449 -0.07375 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.56417 0.49998 0.32694 0.00898  0.00705  -0.08519 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.48125 0.42879 0.30065 0.02171  0.01914  -0.09348 212 GLN A C   
1538 O O   . GLN A 205 ? 0.56042 0.53130 0.40743 0.03460  0.04972  -0.09318 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.66283 0.55006 0.33488 0.00978  0.01712  -0.10620 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.83735 0.67653 0.48095 0.00897  -0.00396 -0.13138 212 GLN A CG  
1541 C CD  . GLN A 205 ? 1.04207 0.83922 0.61980 -0.00887 -0.04699 -0.13434 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.99071 0.80685 0.59459 -0.02174 -0.07941 -0.11290 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.89264 0.62979 0.38412 -0.00882 -0.04908 -0.16167 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.51815 0.45034 0.36016 0.01742  -0.00604 -0.09811 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.50877 0.44014 0.39438 0.02841  0.00216  -0.10466 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.43242 0.39870 0.38562 0.02629  -0.00623 -0.08335 213 PHE A C   
1547 O O   . PHE A 206 ? 0.40053 0.36081 0.38696 0.03150  -0.00691 -0.08363 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.51667 0.39629 0.37559 0.02450  -0.01671 -0.12564 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.59178 0.42565 0.37213 0.03001  -0.00438 -0.15254 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.60812 0.44873 0.37508 0.04879  0.03760  -0.16180 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.69779 0.48081 0.41733 0.01630  -0.03442 -0.16876 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.70015 0.49657 0.38891 0.05585  0.05697  -0.18762 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.76402 0.49628 0.39503 0.02186  -0.02157 -0.19608 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.85728 0.59564 0.47005 0.04270  0.02799  -0.20600 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.44081 0.43818 0.41014 0.01943  -0.01150 -0.06490 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.36521 0.39113 0.38666 0.01942  -0.01366 -0.04726 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.38206 0.42315 0.42705 0.03323  0.00601  -0.04545 214 ILE A C   
1558 O O   . ILE A 207 ? 0.47758 0.53215 0.51650 0.04037  0.02296  -0.04776 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.31277 0.36301 0.34176 0.01304  -0.01931 -0.03213 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.32521 0.36324 0.34524 0.00045  -0.04523 -0.03009 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.37656 0.45116 0.44680 0.01621  -0.01439 -0.01796 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.25942 0.30042 0.32394 -0.00630 -0.05996 -0.02301 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.32640 0.36554 0.40144 0.03604  0.00244  -0.03878 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.32355 0.37021 0.42055 0.04955  0.01311  -0.03576 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.37809 0.45511 0.49214 0.05140  0.01556  -0.02082 215 GLY A C   
1566 O O   . GLY A 208 ? 0.41295 0.49253 0.54546 0.05783  0.01316  -0.01129 215 GLY A O   
1567 N N   . TYR A 209 ? 0.29882 0.39337 0.40280 0.04526  0.01730  -0.01838 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.25859 0.37492 0.37362 0.04542  0.01707  -0.00806 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.30908 0.43942 0.41693 0.04170  0.02431  -0.01041 216 TYR A C   
1570 O O   . TYR A 209 ? 0.35575 0.47709 0.44047 0.03633  0.02677  -0.01567 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.26088 0.37680 0.37339 0.03925  0.01027  0.00179  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.29624 0.39957 0.41532 0.04068  0.00796  0.00933  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.21998 0.32125 0.34074 0.04706  0.00568  0.01762  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.30447 0.39672 0.42926 0.03389  0.00580  0.01077  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.27506 0.36038 0.39551 0.04707  0.00502  0.02868  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.32195 0.40248 0.45662 0.03250  0.00658  0.02131  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.30720 0.38270 0.43593 0.03933  0.00808  0.03100  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.38216 0.44170 0.51448 0.03676  0.01022  0.04547  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.34709 0.49674 0.47304 0.04268  0.02561  -0.00503 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.21362 0.37651 0.33881 0.03621  0.03420  -0.00367 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.22439 0.37871 0.32792 0.02606  0.02684  0.00099  217 PRO A C   
1582 O O   . PRO A 210 ? 0.26418 0.41449 0.36885 0.02481  0.01614  0.00491  217 PRO A O   
1583 C CB  . PRO A 210 ? 0.21187 0.39670 0.37222 0.03699  0.02995  0.00280  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.37861 0.55627 0.54333 0.04283  0.01426  0.00569  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.23102 0.38873 0.37929 0.04833  0.01654  0.00146  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.26976 0.41821 0.35083 0.02018  0.03363  0.00089  218 ILE A N   
1587 C CA  . ILE A 211 ? 0.28738 0.42620 0.35150 0.01159  0.02443  0.00827  218 ILE A CA  
1588 C C   . ILE A 211 ? 0.35695 0.50427 0.42433 0.00343  0.03295  0.01690  218 ILE A C   
1589 O O   . ILE A 211 ? 0.36454 0.51366 0.41699 0.00059  0.04950  0.01788  218 ILE A O   
1590 C CB  . ILE A 211 ? 0.39332 0.51254 0.42421 0.00878  0.01792  0.00581  218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.30791 0.41972 0.34590 0.01355  0.00871  -0.00156 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.28463 0.39473 0.30618 0.00181  0.00389  0.01690  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.23077 0.32133 0.24000 0.00842  -0.00456 -0.00575 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.31294 0.46222 0.39784 -0.00100 0.02353  0.02303  219 THR A N   
1595 C CA  . THR A 212 ? 0.31244 0.46700 0.40858 -0.01210 0.02776  0.03309  219 THR A CA  
1596 C C   . THR A 212 ? 0.31708 0.44937 0.39223 -0.01911 0.01835  0.04281  219 THR A C   
1597 O O   . THR A 212 ? 0.25328 0.37186 0.32922 -0.01461 0.00384  0.04077  219 THR A O   
1598 C CB  . THR A 212 ? 0.31932 0.48400 0.44915 -0.01423 0.01797  0.03217  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.30304 0.48511 0.45256 -0.00521 0.01979  0.02530  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.28717 0.46189 0.44146 -0.02887 0.02245  0.04340  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.25753 0.38500 0.31432 -0.02894 0.02847  0.05469  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.33381 0.43645 0.36917 -0.03627 0.01737  0.06874  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.37450 0.47459 0.43546 -0.04870 0.01660  0.08013  220 LEU A C   
1604 O O   . LEU A 213 ? 0.45626 0.56763 0.52415 -0.06065 0.03400  0.09101  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.31658 0.40643 0.30298 -0.04127 0.02615  0.07768  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.48846 0.54884 0.44590 -0.04980 0.01168  0.09758  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.52572 0.57287 0.50116 -0.04097 -0.01666 0.09614  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.42091 0.46293 0.31356 -0.05388 0.01641  0.10410  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.40145 0.48510 0.47821 -0.04615 -0.00186 0.07717  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.37587 0.44833 0.47640 -0.05869 -0.00822 0.08424  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.49168 0.54257 0.57691 -0.07232 -0.00709 0.10759  221 PHE A C   
1612 O O   . PHE A 214 ? 0.55363 0.58394 0.60960 -0.06740 -0.01506 0.11610  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.35650 0.40617 0.46573 -0.04970 -0.02671 0.07113  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.30471 0.36819 0.42555 -0.04285 -0.02930 0.05247  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.35925 0.45182 0.48021 -0.03593 -0.01909 0.04628  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.41481 0.45538 0.54024 -0.04313 -0.04390 0.04109  221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.34996 0.45082 0.47771 -0.02985 -0.02474 0.03329  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.40439 0.45137 0.52783 -0.03773 -0.04963 0.02586  221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.34120 0.41953 0.46691 -0.03127 -0.04071 0.02405  221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.40567 0.46106 0.51380 -0.09079 0.00078  0.12059  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.36631 0.39898 0.46144 -0.10753 0.00445  0.14744  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.50580 0.50168 0.62208 -0.11383 -0.01913 0.15067  222 VAL A C   
1623 O O   . VAL A 215 ? 0.40962 0.40589 0.55821 -0.11480 -0.03085 0.13461  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.42208 0.48299 0.53520 -0.12602 0.03331  0.16334  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.52459 0.55952 0.60976 -0.14364 0.04299  0.19535  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.40567 0.50155 0.50465 -0.11494 0.05864  0.15235  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.43655 0.39498 0.53046 -0.11747 -0.02871 0.17087  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.57145 0.48653 0.68503 -0.12211 -0.05052 0.17470  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.49868 0.40739 0.64058 -0.15126 -0.04500 0.19512  223 GLU A C   
1630 O O   . GLU A 216 ? 0.49685 0.43421 0.63989 -0.16745 -0.02030 0.21308  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.54988 0.42529 0.63694 -0.11191 -0.06687 0.19022  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.59936 0.48733 0.66706 -0.08701 -0.07244 0.17663  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.65388 0.50480 0.71359 -0.07517 -0.09550 0.19173  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.61800 0.43716 0.70609 -0.06534 -0.11007 0.18519  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.71743 0.56828 0.74196 -0.07482 -0.10073 0.20953  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.64108 0.51002 0.80824 -0.15797 -0.06672 0.19178  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.67711 0.53643 0.88275 -0.18851 -0.06793 0.20883  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.61239 0.42011 0.80597 -0.19686 -0.07719 0.23365  224 LYS A C   
1639 O O   . LYS A 217 ? 0.81269 0.58991 0.97313 -0.18112 -0.08622 0.24219  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.53834 0.38921 0.77979 -0.19167 -0.08981 0.18025  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.49610 0.38984 0.73662 -0.17463 -0.08652 0.15031  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.49233 0.36193 0.74658 -0.17471 -0.11426 0.12096  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.52352 0.33215 0.74557 -0.15452 -0.13086 0.10214  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.48743 0.31019 0.67524 -0.12223 -0.12126 0.08117  224 LYS A NZ  
# 
