data_8PS6
# 
_entry.id   8PS6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8PS6         pdb_00008ps6 10.2210/pdb8ps6/pdb 
WWPDB D_1292129965 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-22 
2 'Structure model' 1 1 2025-02-19 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.year'           
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8PS6 
_pdbx_database_status.recvd_initial_deposition_date   2023-07-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jinek@bioc.uzh.ch 
_pdbx_contact_author.name_first         Martin 
_pdbx_contact_author.name_last          Jinek 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7601-210X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Loeff, L.'  1 0000-0002-1805-7844 
'Walter, A.' 2 0009-0003-9030-0698 
'Jinek, M.'  3 0000-0002-7601-210X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Cell 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1097-4172 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            188 
_citation.language                  ? 
_citation.page_first                721 
_citation.page_last                 ? 
_citation.title                     'DNA end sensing and cleavage by the Shedu anti-phage defense system.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.cell.2024.11.030 
_citation.pdbx_database_id_PubMed   39742808 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Loeff, L.'     1 ? 
primary 'Walter, A.'    2 ? 
primary 'Rosalen, G.T.' 3 ? 
primary 'Jinek, M.'     4 ? 
# 
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 'Shedu effector protein' 22070.945 1  ? ? ? ? 
2 non-polymer syn 'SULFATE ION'            96.063    2  ? ? ? ? 
3 water       nat water                    18.015    33 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Shedu protein,DUF4263 domain-containing protein' 
# 
_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       
;SNAMLQFSFVSNDVVMTYDGDSGEQIIWVWESLNKFQTVCISRIFNFQLQDLRNPPSTVQDFNDYEYSFNFGTLNNEYIT
VPGRILSINRDVLIHKSIKLERKVFASERNVSIFGRLSKLLDHTNPIIIGGDKPEAIPKSVFQELQSKFPNTGELDRYAN
ARVHAILAGYLDGMKDARERYEHYLNRKTVI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNAMLQFSFVSNDVVMTYDGDSGEQIIWVWESLNKFQTVCISRIFNFQLQDLRNPPSTVQDFNDYEYSFNFGTLNNEYIT
VPGRILSINRDVLIHKSIKLERKVFASERNVSIFGRLSKLLDHTNPIIIGGDKPEAIPKSVFQELQSKFPNTGELDRYAN
ARVHAILAGYLDGMKDARERYEHYLNRKTVI
;
_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 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASN n 
1 3   ALA n 
1 4   MET n 
1 5   LEU n 
1 6   GLN n 
1 7   PHE n 
1 8   SER n 
1 9   PHE n 
1 10  VAL n 
1 11  SER n 
1 12  ASN n 
1 13  ASP n 
1 14  VAL n 
1 15  VAL n 
1 16  MET n 
1 17  THR n 
1 18  TYR n 
1 19  ASP n 
1 20  GLY n 
1 21  ASP n 
1 22  SER n 
1 23  GLY n 
1 24  GLU n 
1 25  GLN n 
1 26  ILE n 
1 27  ILE n 
1 28  TRP n 
1 29  VAL n 
1 30  TRP n 
1 31  GLU n 
1 32  SER n 
1 33  LEU n 
1 34  ASN n 
1 35  LYS n 
1 36  PHE n 
1 37  GLN n 
1 38  THR n 
1 39  VAL n 
1 40  CYS n 
1 41  ILE n 
1 42  SER n 
1 43  ARG n 
1 44  ILE n 
1 45  PHE n 
1 46  ASN n 
1 47  PHE n 
1 48  GLN n 
1 49  LEU n 
1 50  GLN n 
1 51  ASP n 
1 52  LEU n 
1 53  ARG n 
1 54  ASN n 
1 55  PRO n 
1 56  PRO n 
1 57  SER n 
1 58  THR n 
1 59  VAL n 
1 60  GLN n 
1 61  ASP n 
1 62  PHE n 
1 63  ASN n 
1 64  ASP n 
1 65  TYR n 
1 66  GLU n 
1 67  TYR n 
1 68  SER n 
1 69  PHE n 
1 70  ASN n 
1 71  PHE n 
1 72  GLY n 
1 73  THR n 
1 74  LEU n 
1 75  ASN n 
1 76  ASN n 
1 77  GLU n 
1 78  TYR n 
1 79  ILE n 
1 80  THR n 
1 81  VAL n 
1 82  PRO n 
1 83  GLY n 
1 84  ARG n 
1 85  ILE n 
1 86  LEU n 
1 87  SER n 
1 88  ILE n 
1 89  ASN n 
1 90  ARG n 
1 91  ASP n 
1 92  VAL n 
1 93  LEU n 
1 94  ILE n 
1 95  HIS n 
1 96  LYS n 
1 97  SER n 
1 98  ILE n 
1 99  LYS n 
1 100 LEU n 
1 101 GLU n 
1 102 ARG n 
1 103 LYS n 
1 104 VAL n 
1 105 PHE n 
1 106 ALA n 
1 107 SER n 
1 108 GLU n 
1 109 ARG n 
1 110 ASN n 
1 111 VAL n 
1 112 SER n 
1 113 ILE n 
1 114 PHE n 
1 115 GLY n 
1 116 ARG n 
1 117 LEU n 
1 118 SER n 
1 119 LYS n 
1 120 LEU n 
1 121 LEU n 
1 122 ASP n 
1 123 HIS n 
1 124 THR n 
1 125 ASN n 
1 126 PRO n 
1 127 ILE n 
1 128 ILE n 
1 129 ILE n 
1 130 GLY n 
1 131 GLY n 
1 132 ASP n 
1 133 LYS n 
1 134 PRO n 
1 135 GLU n 
1 136 ALA n 
1 137 ILE n 
1 138 PRO n 
1 139 LYS n 
1 140 SER n 
1 141 VAL n 
1 142 PHE n 
1 143 GLN n 
1 144 GLU n 
1 145 LEU n 
1 146 GLN n 
1 147 SER n 
1 148 LYS n 
1 149 PHE n 
1 150 PRO n 
1 151 ASN n 
1 152 THR n 
1 153 GLY n 
1 154 GLU n 
1 155 LEU n 
1 156 ASP n 
1 157 ARG n 
1 158 TYR n 
1 159 ALA n 
1 160 ASN n 
1 161 ALA n 
1 162 ARG n 
1 163 VAL n 
1 164 HIS n 
1 165 ALA n 
1 166 ILE n 
1 167 LEU n 
1 168 ALA n 
1 169 GLY n 
1 170 TYR n 
1 171 LEU n 
1 172 ASP n 
1 173 GLY n 
1 174 MET n 
1 175 LYS n 
1 176 ASP n 
1 177 ALA n 
1 178 ARG n 
1 179 GLU n 
1 180 ARG n 
1 181 TYR n 
1 182 GLU n 
1 183 HIS n 
1 184 TYR n 
1 185 LEU n 
1 186 ASN n 
1 187 ARG n 
1 188 LYS n 
1 189 THR n 
1 190 VAL n 
1 191 ILE 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                   191 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SduA 
_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      'Escherichia coli KTE10' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1169330 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
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   SER 1   -2  ?   ?   ?   A . n 
A 1 2   ASN 2   -1  ?   ?   ?   A . n 
A 1 3   ALA 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   LEU 5   2   2   LEU LEU A . n 
A 1 6   GLN 6   3   3   GLN GLN A . n 
A 1 7   PHE 7   4   4   PHE PHE A . n 
A 1 8   SER 8   5   5   SER SER A . n 
A 1 9   PHE 9   6   6   PHE PHE A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  SER 11  8   8   SER SER A . n 
A 1 12  ASN 12  9   9   ASN ASN A . n 
A 1 13  ASP 13  10  10  ASP ASP A . n 
A 1 14  VAL 14  11  11  VAL VAL A . n 
A 1 15  VAL 15  12  12  VAL VAL A . n 
A 1 16  MET 16  13  13  MET MET A . n 
A 1 17  THR 17  14  14  THR THR A . n 
A 1 18  TYR 18  15  15  TYR TYR A . n 
A 1 19  ASP 19  16  16  ASP ASP A . n 
A 1 20  GLY 20  17  ?   ?   ?   A . n 
A 1 21  ASP 21  18  ?   ?   ?   A . n 
A 1 22  SER 22  19  ?   ?   ?   A . n 
A 1 23  GLY 23  20  ?   ?   ?   A . n 
A 1 24  GLU 24  21  21  GLU GLU A . n 
A 1 25  GLN 25  22  22  GLN GLN A . n 
A 1 26  ILE 26  23  23  ILE ILE A . n 
A 1 27  ILE 27  24  24  ILE ILE A . n 
A 1 28  TRP 28  25  25  TRP TRP A . n 
A 1 29  VAL 29  26  26  VAL VAL A . n 
A 1 30  TRP 30  27  27  TRP TRP A . n 
A 1 31  GLU 31  28  28  GLU GLU A . n 
A 1 32  SER 32  29  29  SER SER A . n 
A 1 33  LEU 33  30  30  LEU LEU A . n 
A 1 34  ASN 34  31  31  ASN ASN A . n 
A 1 35  LYS 35  32  32  LYS LYS A . n 
A 1 36  PHE 36  33  33  PHE PHE A . n 
A 1 37  GLN 37  34  34  GLN GLN A . n 
A 1 38  THR 38  35  35  THR THR A . n 
A 1 39  VAL 39  36  36  VAL VAL A . n 
A 1 40  CYS 40  37  37  CYS CYS A . n 
A 1 41  ILE 41  38  38  ILE ILE A . n 
A 1 42  SER 42  39  39  SER SER A . n 
A 1 43  ARG 43  40  40  ARG ARG A . n 
A 1 44  ILE 44  41  41  ILE ILE A . n 
A 1 45  PHE 45  42  42  PHE PHE A . n 
A 1 46  ASN 46  43  43  ASN ASN A . n 
A 1 47  PHE 47  44  44  PHE PHE A . n 
A 1 48  GLN 48  45  45  GLN GLN A . n 
A 1 49  LEU 49  46  46  LEU LEU A . n 
A 1 50  GLN 50  47  47  GLN GLN A . n 
A 1 51  ASP 51  48  48  ASP ASP A . n 
A 1 52  LEU 52  49  49  LEU LEU A . n 
A 1 53  ARG 53  50  50  ARG ARG A . n 
A 1 54  ASN 54  51  51  ASN ASN A . n 
A 1 55  PRO 55  52  52  PRO PRO A . n 
A 1 56  PRO 56  53  53  PRO PRO A . n 
A 1 57  SER 57  54  54  SER SER A . n 
A 1 58  THR 58  55  55  THR THR A . n 
A 1 59  VAL 59  56  56  VAL VAL A . n 
A 1 60  GLN 60  57  57  GLN GLN A . n 
A 1 61  ASP 61  58  58  ASP ASP A . n 
A 1 62  PHE 62  59  59  PHE PHE A . n 
A 1 63  ASN 63  60  60  ASN ASN A . n 
A 1 64  ASP 64  61  61  ASP ASP A . n 
A 1 65  TYR 65  62  62  TYR TYR A . n 
A 1 66  GLU 66  63  63  GLU GLU A . n 
A 1 67  TYR 67  64  64  TYR TYR A . n 
A 1 68  SER 68  65  65  SER SER A . n 
A 1 69  PHE 69  66  66  PHE PHE A . n 
A 1 70  ASN 70  67  67  ASN ASN A . n 
A 1 71  PHE 71  68  68  PHE PHE A . n 
A 1 72  GLY 72  69  69  GLY GLY A . n 
A 1 73  THR 73  70  70  THR THR A . n 
A 1 74  LEU 74  71  71  LEU LEU A . n 
A 1 75  ASN 75  72  72  ASN ASN A . n 
A 1 76  ASN 76  73  73  ASN ASN A . n 
A 1 77  GLU 77  74  74  GLU GLU A . n 
A 1 78  TYR 78  75  75  TYR TYR A . n 
A 1 79  ILE 79  76  76  ILE ILE A . n 
A 1 80  THR 80  77  77  THR THR A . n 
A 1 81  VAL 81  78  78  VAL VAL A . n 
A 1 82  PRO 82  79  79  PRO PRO A . n 
A 1 83  GLY 83  80  80  GLY GLY A . n 
A 1 84  ARG 84  81  81  ARG ARG A . n 
A 1 85  ILE 85  82  82  ILE ILE A . n 
A 1 86  LEU 86  83  83  LEU LEU A . n 
A 1 87  SER 87  84  84  SER SER A . n 
A 1 88  ILE 88  85  85  ILE ILE A . n 
A 1 89  ASN 89  86  86  ASN ASN A . n 
A 1 90  ARG 90  87  87  ARG ARG A . n 
A 1 91  ASP 91  88  88  ASP ASP A . n 
A 1 92  VAL 92  89  89  VAL VAL A . n 
A 1 93  LEU 93  90  90  LEU LEU A . n 
A 1 94  ILE 94  91  91  ILE ILE A . n 
A 1 95  HIS 95  92  92  HIS HIS A . n 
A 1 96  LYS 96  93  93  LYS LYS A . n 
A 1 97  SER 97  94  94  SER SER A . n 
A 1 98  ILE 98  95  95  ILE ILE A . n 
A 1 99  LYS 99  96  96  LYS LYS A . n 
A 1 100 LEU 100 97  97  LEU LEU A . n 
A 1 101 GLU 101 98  98  GLU GLU A . n 
A 1 102 ARG 102 99  99  ARG ARG A . n 
A 1 103 LYS 103 100 100 LYS LYS A . n 
A 1 104 VAL 104 101 101 VAL VAL A . n 
A 1 105 PHE 105 102 102 PHE PHE A . n 
A 1 106 ALA 106 103 103 ALA ALA A . n 
A 1 107 SER 107 104 104 SER SER A . n 
A 1 108 GLU 108 105 105 GLU GLU A . n 
A 1 109 ARG 109 106 106 ARG ARG A . n 
A 1 110 ASN 110 107 107 ASN ASN A . n 
A 1 111 VAL 111 108 108 VAL VAL A . n 
A 1 112 SER 112 109 109 SER SER A . n 
A 1 113 ILE 113 110 110 ILE ILE A . n 
A 1 114 PHE 114 111 111 PHE PHE A . n 
A 1 115 GLY 115 112 112 GLY GLY A . n 
A 1 116 ARG 116 113 113 ARG ARG A . n 
A 1 117 LEU 117 114 114 LEU LEU A . n 
A 1 118 SER 118 115 115 SER SER A . n 
A 1 119 LYS 119 116 116 LYS LYS A . n 
A 1 120 LEU 120 117 117 LEU LEU A . n 
A 1 121 LEU 121 118 118 LEU LEU A . n 
A 1 122 ASP 122 119 119 ASP ASP A . n 
A 1 123 HIS 123 120 120 HIS HIS A . n 
A 1 124 THR 124 121 121 THR THR A . n 
A 1 125 ASN 125 122 122 ASN ASN A . n 
A 1 126 PRO 126 123 123 PRO PRO A . n 
A 1 127 ILE 127 124 124 ILE ILE A . n 
A 1 128 ILE 128 125 125 ILE ILE A . n 
A 1 129 ILE 129 126 126 ILE ILE A . n 
A 1 130 GLY 130 127 127 GLY GLY A . n 
A 1 131 GLY 131 128 128 GLY GLY A . n 
A 1 132 ASP 132 129 129 ASP ASP A . n 
A 1 133 LYS 133 130 130 LYS LYS A . n 
A 1 134 PRO 134 131 131 PRO PRO A . n 
A 1 135 GLU 135 132 132 GLU GLU A . n 
A 1 136 ALA 136 133 133 ALA ALA A . n 
A 1 137 ILE 137 134 134 ILE ILE A . n 
A 1 138 PRO 138 135 135 PRO PRO A . n 
A 1 139 LYS 139 136 136 LYS LYS A . n 
A 1 140 SER 140 137 137 SER SER A . n 
A 1 141 VAL 141 138 138 VAL VAL A . n 
A 1 142 PHE 142 139 139 PHE PHE A . n 
A 1 143 GLN 143 140 140 GLN GLN A . n 
A 1 144 GLU 144 141 141 GLU GLU A . n 
A 1 145 LEU 145 142 142 LEU LEU A . n 
A 1 146 GLN 146 143 143 GLN GLN A . n 
A 1 147 SER 147 144 144 SER SER A . n 
A 1 148 LYS 148 145 145 LYS LYS A . n 
A 1 149 PHE 149 146 146 PHE PHE A . n 
A 1 150 PRO 150 147 147 PRO PRO A . n 
A 1 151 ASN 151 148 148 ASN ASN A . n 
A 1 152 THR 152 149 149 THR THR A . n 
A 1 153 GLY 153 150 150 GLY GLY A . n 
A 1 154 GLU 154 151 151 GLU GLU A . n 
A 1 155 LEU 155 152 152 LEU LEU A . n 
A 1 156 ASP 156 153 153 ASP ASP A . n 
A 1 157 ARG 157 154 154 ARG ARG A . n 
A 1 158 TYR 158 155 155 TYR TYR A . n 
A 1 159 ALA 159 156 156 ALA ALA A . n 
A 1 160 ASN 160 157 157 ASN ASN A . n 
A 1 161 ALA 161 158 158 ALA ALA A . n 
A 1 162 ARG 162 159 159 ARG ARG A . n 
A 1 163 VAL 163 160 160 VAL VAL A . n 
A 1 164 HIS 164 161 161 HIS HIS A . n 
A 1 165 ALA 165 162 162 ALA ALA A . n 
A 1 166 ILE 166 163 163 ILE ILE A . n 
A 1 167 LEU 167 164 164 LEU LEU A . n 
A 1 168 ALA 168 165 165 ALA ALA A . n 
A 1 169 GLY 169 166 166 GLY GLY A . n 
A 1 170 TYR 170 167 167 TYR TYR A . n 
A 1 171 LEU 171 168 168 LEU LEU A . n 
A 1 172 ASP 172 169 169 ASP ASP A . n 
A 1 173 GLY 173 170 170 GLY GLY A . n 
A 1 174 MET 174 171 171 MET MET A . n 
A 1 175 LYS 175 172 172 LYS LYS A . n 
A 1 176 ASP 176 173 173 ASP ASP A . n 
A 1 177 ALA 177 174 174 ALA ALA A . n 
A 1 178 ARG 178 175 175 ARG ARG A . n 
A 1 179 GLU 179 176 176 GLU GLU A . n 
A 1 180 ARG 180 177 177 ARG ARG A . n 
A 1 181 TYR 181 178 178 TYR TYR A . n 
A 1 182 GLU 182 179 179 GLU GLU A . n 
A 1 183 HIS 183 180 180 HIS HIS A . n 
A 1 184 TYR 184 181 181 TYR TYR A . n 
A 1 185 LEU 185 182 182 LEU LEU A . n 
A 1 186 ASN 186 183 183 ASN ASN A . n 
A 1 187 ARG 187 184 184 ARG ARG A . n 
A 1 188 LYS 188 185 ?   ?   ?   A . n 
A 1 189 THR 189 186 ?   ?   ?   A . n 
A 1 190 VAL 190 187 ?   ?   ?   A . n 
A 1 191 ILE 191 188 ?   ?   ?   A . n 
# 
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 SO4 1  201 1  SO4 SO4 A . 
C 2 SO4 1  202 2  SO4 SO4 A . 
D 3 HOH 1  301 30 HOH HOH A . 
D 3 HOH 2  302 28 HOH HOH A . 
D 3 HOH 3  303 8  HOH HOH A . 
D 3 HOH 4  304 3  HOH HOH A . 
D 3 HOH 5  305 6  HOH HOH A . 
D 3 HOH 6  306 9  HOH HOH A . 
D 3 HOH 7  307 10 HOH HOH A . 
D 3 HOH 8  308 4  HOH HOH A . 
D 3 HOH 9  309 5  HOH HOH A . 
D 3 HOH 10 310 26 HOH HOH A . 
D 3 HOH 11 311 7  HOH HOH A . 
D 3 HOH 12 312 1  HOH HOH A . 
D 3 HOH 13 313 18 HOH HOH A . 
D 3 HOH 14 314 11 HOH HOH A . 
D 3 HOH 15 315 2  HOH HOH A . 
D 3 HOH 16 316 12 HOH HOH A . 
D 3 HOH 17 317 23 HOH HOH A . 
D 3 HOH 18 318 32 HOH HOH A . 
D 3 HOH 19 319 24 HOH HOH A . 
D 3 HOH 20 320 22 HOH HOH A . 
D 3 HOH 21 321 15 HOH HOH A . 
D 3 HOH 22 322 29 HOH HOH A . 
D 3 HOH 23 323 33 HOH HOH A . 
D 3 HOH 24 324 16 HOH HOH A . 
D 3 HOH 25 325 19 HOH HOH A . 
D 3 HOH 26 326 31 HOH HOH A . 
D 3 HOH 27 327 17 HOH HOH A . 
D 3 HOH 28 328 27 HOH HOH A . 
D 3 HOH 29 329 13 HOH HOH A . 
D 3 HOH 30 330 25 HOH HOH A . 
D 3 HOH 31 331 20 HOH HOH A . 
D 3 HOH 32 332 14 HOH HOH A . 
D 3 HOH 33 333 21 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8PS6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     225.543 
_cell.length_a_esd                 ? 
_cell.length_b                     225.543 
_cell.length_b_esd                 ? 
_cell.length_c                     32.029 
_cell.length_c_esd                 ? 
_cell.volume                       1411018.529 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8PS6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_symmetry.space_group_name_Hall            
;R 3 2"
;
_symmetry.space_group_name_H-M             'H 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8PS6 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.70 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          66.79 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'HEPES 100 mM, Ammonium Sulfate 550 mM, protein concentration: 4.5 mg /ml, 1 uL reservoir + 1 uL protein solution.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-08-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99999 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.99999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          49.15 
_reflns.entry_id                                       8PS6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.518 
_reflns.d_resolution_low                               112.772 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     10123 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           95.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                20.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.178 
_reflns.pdbx_Rpim_I_all                                0.039 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.174 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.518 
_reflns_shell.d_res_low                                     2.561 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             518 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               21.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.748 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               59.81 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8PS6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.52 
_refine.ls_d_res_low                             42.62 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     10117 
_refine.ls_number_reflns_R_free                  461 
_refine.ls_number_reflns_R_work                  9656 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.77 
_refine.ls_percent_reflns_R_free                 4.56 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2235 
_refine.ls_R_factor_R_free                       0.2445 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2224 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.1651 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3953 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.52 
_refine_hist.d_res_low                        42.62 
_refine_hist.number_atoms_solvent             33 
_refine_hist.number_atoms_total               1528 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1485 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0087  ? 1526 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1951  ? 2064 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0911  ? 222  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0045  ? 267  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.9547 ? 566  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.52 2.56  . . 135 3222 96.00 . . . . 0.2809 . . . . . . . . . . . 0.3358 
'X-RAY DIFFRACTION' 2.88 3.63  . . 171 3222 97.03 . . . . 0.2596 . . . . . . . . . . . 0.2788 
'X-RAY DIFFRACTION' 3.63 42.62 . . 155 3212 94.31 . . . . 0.1907 . . . . . . . . . . . 0.2116 
# 
_struct.entry_id                     8PS6 
_struct.title                        'Crystal structure of the N-terminal domain of SduA' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8PS6 
_struct_keywords.text            'SduA, Shedu, Prokaryotic immune system, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8PS6 
_struct_ref.pdbx_db_accession          8PS6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8PS6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 191 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             8PS6 
_struct_ref_seq.db_align_beg                  -2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  188 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       -2 
_struct_ref_seq.pdbx_auth_seq_align_end       188 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3810  ? 
1 MORE         -77   ? 
1 'SSA (A^2)'  21110 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z        1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 6_556 -x,-x+y,-z+1 -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 -0.8660254038 0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 32.0290000000 
# 
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 ILE A 26  ? GLN A 37  ? ILE A 23  GLN A 34  1 ? 12 
HELX_P HELX_P2 AA2 GLN A 50  ? LEU A 52  ? GLN A 47  LEU A 49  5 ? 3  
HELX_P HELX_P3 AA3 PRO A 82  ? SER A 87  ? PRO A 79  SER A 84  5 ? 6  
HELX_P HELX_P4 AA4 GLU A 101 ? PHE A 105 ? GLU A 98  PHE A 102 1 ? 5  
HELX_P HELX_P5 AA5 ILE A 113 ? LEU A 121 ? ILE A 110 LEU A 118 1 ? 9  
HELX_P HELX_P6 AA6 PRO A 138 ? PHE A 149 ? PRO A 135 PHE A 146 1 ? 12 
HELX_P HELX_P7 AA7 ASN A 151 ? HIS A 183 ? ASN A 148 HIS A 180 1 ? 33 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
# 
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 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 5   ? VAL A 10  ? LEU A 2   VAL A 7   
AA1 2 ASP A 13  ? TYR A 18  ? ASP A 10  TYR A 15  
AA1 3 TYR A 67  ? ASN A 75  ? TYR A 64  ASN A 72  
AA1 4 TYR A 78  ? VAL A 81  ? TYR A 75  VAL A 78  
AA1 5 VAL A 92  ? HIS A 95  ? VAL A 89  HIS A 92  
AA1 6 ILE A 127 ? ILE A 129 ? ILE A 124 ILE A 126 
AA2 1 THR A 38  ? ILE A 41  ? THR A 35  ILE A 38  
AA2 2 PHE A 45  ? GLN A 48  ? PHE A 42  GLN A 45  
AA3 1 ALA A 106 ? SER A 107 ? ALA A 103 SER A 104 
AA3 2 VAL A 111 ? SER A 112 ? VAL A 108 SER A 109 
# 
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 GLN A 6   ? N GLN A 3   O THR A 17  ? O THR A 14  
AA1 2 3 N TYR A 18  ? N TYR A 15  O TYR A 67  ? O TYR A 64  
AA1 3 4 N THR A 73  ? N THR A 70  O THR A 80  ? O THR A 77  
AA1 4 5 N VAL A 81  ? N VAL A 78  O VAL A 92  ? O VAL A 89  
AA1 5 6 N LEU A 93  ? N LEU A 90  O ILE A 127 ? O ILE A 124 
AA2 1 2 N ILE A 41  ? N ILE A 38  O PHE A 45  ? O PHE A 42  
AA3 1 2 N SER A 107 ? N SER A 104 O VAL A 111 ? O VAL A 108 
# 
_pdbx_entry_details.entry_id                   8PS6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 8  ? ? 56.54 -127.52 
2 1 GLN A 34 ? ? 55.86 18.39   
3 1 ARG A 40 ? ? 77.00 -4.36   
4 1 ASN A 73 ? ? 57.53 -128.08 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     332 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                  
2  -y,x-y,z               
3  -x+y,-x,z              
4  x-y,-y,-z              
5  -x,-x+y,-z             
6  y,x,-z                 
7  x+1/3,y+2/3,z+2/3      
8  -y+1/3,x-y+2/3,z+2/3   
9  -x+y+1/3,-x+2/3,z+2/3  
10 x-y+1/3,-y+2/3,-z+2/3  
11 -x+1/3,-x+y+2/3,-z+2/3 
12 y+1/3,x+2/3,-z+2/3     
13 x+2/3,y+1/3,z+1/3      
14 -y+2/3,x-y+1/3,z+1/3   
15 -x+y+2/3,-x+1/3,z+1/3  
16 x-y+2/3,-y+1/3,-z+1/3  
17 -x+2/3,-x+y+1/3,-z+1/3 
18 y+2/3,x+1/3,-z+1/3     
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -12.2948894442  56.7096587251 16.2828883918 0.495613324931 ? -0.0324396627114 ? 0.00392564290976 ? 
0.370158983276 ? -0.0764734566121 ? 0.315223877215 ? 4.65927755323 ? -1.47477695843 ? -2.71360257658 ? 4.39905944151 ? 
1.00636796103  ? 8.6645042451  ? -0.289147168343 ? 0.0218675515062 ? -0.0829645205804 ? 0.256036377948  ? -0.0348912797107 ? 
0.48377456538   ? 0.177846863002 ? -0.812588188256 ? 0.338793632361 ? 
2 'X-RAY DIFFRACTION' ? refined -0.320422539333 41.5243506431 7.90992399754 0.364412403515 ? 0.0735206606803  ? 0.107176899246   ? 
0.280326481597 ? 0.0103250643407  ? 0.304005368086 ? 4.54921893936 ? 0.384918466493 ? -1.07840623029 ? 8.35614055671 ? 
0.39754482762  ? 5.12885118892 ? -0.260862731732 ? 0.187974326233  ? -0.34248484508   ? -0.314635210319 ? -0.0837634425982 ? 
-0.244551992346 ? 0.219825199865 ? 0.0806784150566 ? 0.320480717039 ? 
3 'X-RAY DIFFRACTION' ? refined -26.258034068   9.11217649963 22.0782235116 0.572029028966 ? 0.0580370934786  ? 0.0885024525454  ? 
0.422939693613 ? 0.109035703552   ? 0.665712173884 ? 3.80047399218 ? 4.65746687501  ? -2.76172809312 ? 3.95210314015 ? 
-4.44779411392 ? 4.2292760505  ? -0.333625757473 ? 0.21205371681   ? -0.451886255882  ? -0.680571852456 ? 0.287791225647   ? 
-0.486941525861 ? 0.604811635645 ? -0.510291363414 ? 0.080869567771 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 1   ? A 68  A 72  ? ? 
;chain 'A' and (resid 1 through 72 )
;
2 'X-RAY DIFFRACTION' 2 A 69  A 73  ? A 144 A 148 ? ? 
;chain 'A' and (resid 73 through 148 )
;
3 'X-RAY DIFFRACTION' 3 A 145 A 149 ? A 180 A 184 ? ? 
;chain 'A' and (resid 149 through 185 )
;
# 
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 SER -2  ? A SER 1   
2  1 Y 1 A ASN -1  ? A ASN 2   
3  1 Y 1 A ALA 0   ? A ALA 3   
4  1 Y 1 A GLY 17  ? A GLY 20  
5  1 Y 1 A ASP 18  ? A ASP 21  
6  1 Y 1 A SER 19  ? A SER 22  
7  1 Y 1 A GLY 20  ? A GLY 23  
8  1 Y 1 A LYS 185 ? A LYS 188 
9  1 Y 1 A THR 186 ? A THR 189 
10 1 Y 1 A VAL 187 ? A VAL 190 
11 1 Y 1 A ILE 188 ? A ILE 191 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'European Research Council (ERC)'                      'European Union' 820152 1 
'H2020 Marie Curie Actions of the European Commission' 'European Union' 845268 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-A0A2X1JPY1-F1 
_pdbx_initial_refinement_model.details          'Residues 1-188' 
# 
_space_group.name_H-M_alt     'R 3 2 :H' 
_space_group.name_Hall        
;R 3 2"
;
_space_group.IT_number        155 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8PS6 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.004434 
_atom_sites.fract_transf_matrix[1][2]   0.002560 
_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]   0.005120 
_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]   0.031222 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 4   ? -19.42700 49.72800  11.67900 1.000 97.59784  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 4   ? -18.78100 49.47600  10.39700 1.000 95.49667  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 4   ? -17.41400 50.15500  10.34000 1.000 94.00948  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 4   ? -17.23000 51.23900  10.89300 1.000 84.77080  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 4   ? -19.66400 49.96400  9.24600  1.000 97.10881  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 4   ? -19.19000 49.51300  7.87900  1.000 98.96268  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 4   ? -19.17800 47.71500  7.74600  1.000 115.95889 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 4   ? -17.97000 47.47700  6.44600  1.000 103.48417 ? 1   MET A CE  1 
ATOM   9    N N   . LEU A 1 5   ? -16.45600 49.51200  9.67600  1.000 73.33578  ? 2   LEU A N   1 
ATOM   10   C CA  . LEU A 1 5   ? -15.10900 50.04300  9.52100  1.000 59.59316  ? 2   LEU A CA  1 
ATOM   11   C C   . LEU A 1 5   ? -14.88500 50.43900  8.07000  1.000 63.40712  ? 2   LEU A C   1 
ATOM   12   O O   . LEU A 1 5   ? -15.12000 49.63800  7.16000  1.000 69.21169  ? 2   LEU A O   1 
ATOM   13   C CB  . LEU A 1 5   ? -14.05900 49.02000  9.95800  1.000 56.88955  ? 2   LEU A CB  1 
ATOM   14   C CG  . LEU A 1 5   ? -14.10400 48.63600  11.43600 1.000 56.75358  ? 2   LEU A CG  1 
ATOM   15   C CD1 . LEU A 1 5   ? -12.91700 47.76100  11.79200 1.000 59.94265  ? 2   LEU A CD1 1 
ATOM   16   C CD2 . LEU A 1 5   ? -14.14300 49.88100  12.30500 1.000 62.34051  ? 2   LEU A CD2 1 
ATOM   17   N N   . GLN A 1 6   ? -14.42600 51.67100  7.85900  1.000 60.92015  ? 3   GLN A N   1 
ATOM   18   C CA  . GLN A 1 6   ? -14.19600 52.20900  6.52500  1.000 54.95841  ? 3   GLN A CA  1 
ATOM   19   C C   . GLN A 1 6   ? -12.81900 52.85400  6.49200  1.000 50.87753  ? 3   GLN A C   1 
ATOM   20   O O   . GLN A 1 6   ? -12.52600 53.74000  7.30100  1.000 56.03176  ? 3   GLN A O   1 
ATOM   21   C CB  . GLN A 1 6   ? -15.28800 53.21900  6.15000  1.000 60.84387  ? 3   GLN A CB  1 
ATOM   22   C CG  . GLN A 1 6   ? -16.67100 52.61600  5.97600  1.000 80.44117  ? 3   GLN A CG  1 
ATOM   23   C CD  . GLN A 1 6   ? -17.72500 53.66100  5.67800  1.000 95.46791  ? 3   GLN A CD  1 
ATOM   24   O OE1 . GLN A 1 6   ? -17.57500 54.83200  6.03100  1.000 92.25895  ? 3   GLN A OE1 1 
ATOM   25   N NE2 . GLN A 1 6   ? -18.80000 53.24400  5.02300  1.000 96.40950  ? 3   GLN A NE2 1 
ATOM   26   N N   . PHE A 1 7   ? -11.97400 52.37800  5.57300  1.000 47.95878  ? 4   PHE A N   1 
ATOM   27   C CA  . PHE A 1 7   ? -10.59500 52.91300  5.45000  1.000 46.94187  ? 4   PHE A CA  1 
ATOM   28   C C   . PHE A 1 7   ? -10.55000 53.90800  4.28900  1.000 43.33628  ? 4   PHE A C   1 
ATOM   29   O O   . PHE A 1 7   ? -11.14900 53.62500  3.23600  1.000 49.77446  ? 4   PHE A O   1 
ATOM   30   C CB  . PHE A 1 7   ? -9.59500  51.77300  5.24200  1.000 41.72868  ? 4   PHE A CB  1 
ATOM   31   C CG  . PHE A 1 7   ? -9.44200  50.82500  6.40500  1.000 51.17696  ? 4   PHE A CG  1 
ATOM   32   C CD1 . PHE A 1 7   ? -10.31600 49.76400  6.57900  1.000 48.43652  ? 4   PHE A CD1 1 
ATOM   33   C CD2 . PHE A 1 7   ? -8.41100  50.98100  7.31600  1.000 39.65217  ? 4   PHE A CD2 1 
ATOM   34   C CE1 . PHE A 1 7   ? -10.17100 48.88900  7.64400  1.000 51.22911  ? 4   PHE A CE1 1 
ATOM   35   C CE2 . PHE A 1 7   ? -8.26500  50.10500  8.37900  1.000 43.17337  ? 4   PHE A CE2 1 
ATOM   36   C CZ  . PHE A 1 7   ? -9.14400  49.06000  8.54200  1.000 49.92102  ? 4   PHE A CZ  1 
ATOM   37   N N   . SER A 1 8   ? -9.87700  55.04300  4.48700  1.000 38.62222  ? 5   SER A N   1 
ATOM   38   C CA  . SER A 1 8   ? -9.76400  56.07500  3.42500  1.000 40.10608  ? 5   SER A CA  1 
ATOM   39   C C   . SER A 1 8   ? -8.35800  56.67300  3.45400  1.000 38.98814  ? 5   SER A C   1 
ATOM   40   O O   . SER A 1 8   ? -7.68900  56.54700  4.49200  1.000 35.96643  ? 5   SER A O   1 
ATOM   41   C CB  . SER A 1 8   ? -10.80300 57.14700  3.59700  1.000 41.56213  ? 5   SER A CB  1 
ATOM   42   O OG  . SER A 1 8   ? -10.37900 58.11100  4.54900  1.000 40.04447  ? 5   SER A OG  1 
ATOM   43   N N   . PHE A 1 9   ? -7.92000  57.27200  2.34700  1.000 44.80665  ? 6   PHE A N   1 
ATOM   44   C CA  . PHE A 1 9   ? -6.60700  57.96000  2.35900  1.000 46.28025  ? 6   PHE A CA  1 
ATOM   45   C C   . PHE A 1 9   ? -6.83700  59.46800  2.28300  1.000 48.20808  ? 6   PHE A C   1 
ATOM   46   O O   . PHE A 1 9   ? -7.37500  59.93500  1.26400  1.000 51.77337  ? 6   PHE A O   1 
ATOM   47   C CB  . PHE A 1 9   ? -5.75300  57.53400  1.16300  1.000 44.53201  ? 6   PHE A CB  1 
ATOM   48   C CG  . PHE A 1 9   ? -5.32700  56.08900  1.14700  1.000 52.73014  ? 6   PHE A CG  1 
ATOM   49   C CD1 . PHE A 1 9   ? -5.05100  55.41400  2.32400  1.000 52.53450  ? 6   PHE A CD1 1 
ATOM   50   C CD2 . PHE A 1 9   ? -5.19200  55.40700  -0.05100 1.000 51.22130  ? 6   PHE A CD2 1 
ATOM   51   C CE1 . PHE A 1 9   ? -4.65800  54.08600  2.30300  1.000 47.65892  ? 6   PHE A CE1 1 
ATOM   52   C CE2 . PHE A 1 9   ? -4.79700  54.07900  -0.07100 1.000 55.98323  ? 6   PHE A CE2 1 
ATOM   53   C CZ  . PHE A 1 9   ? -4.53100  53.42200  1.10600  1.000 51.22713  ? 6   PHE A CZ  1 
ATOM   54   N N   . VAL A 1 10  ? -6.44400  60.20500  3.32400  1.000 36.40972  ? 7   VAL A N   1 
ATOM   55   C CA  . VAL A 1 10  ? -6.52100  61.69200  3.25700  1.000 38.33987  ? 7   VAL A CA  1 
ATOM   56   C C   . VAL A 1 10  ? -5.07000  62.15900  3.19400  1.000 40.92402  ? 7   VAL A C   1 
ATOM   57   O O   . VAL A 1 10  ? -4.35300  61.93000  4.18400  1.000 40.70770  ? 7   VAL A O   1 
ATOM   58   C CB  . VAL A 1 10  ? -7.26200  62.28100  4.47200  1.000 43.82237  ? 7   VAL A CB  1 
ATOM   59   C CG1 . VAL A 1 10  ? -7.36900  63.79600  4.38900  1.000 40.54199  ? 7   VAL A CG1 1 
ATOM   60   C CG2 . VAL A 1 10  ? -8.63800  61.65900  4.64900  1.000 37.80390  ? 7   VAL A CG2 1 
ATOM   61   N N   . SER A 1 11  ? -4.65800  62.78000  2.08400  1.000 55.61260  ? 8   SER A N   1 
ATOM   62   C CA  . SER A 1 11  ? -3.22500  63.13800  1.91700  1.000 56.89672  ? 8   SER A CA  1 
ATOM   63   C C   . SER A 1 11  ? -2.39300  61.85800  2.05700  1.000 51.92211  ? 8   SER A C   1 
ATOM   64   O O   . SER A 1 11  ? -2.70100  60.87600  1.35600  1.000 52.16674  ? 8   SER A O   1 
ATOM   65   C CB  . SER A 1 11  ? -2.78500  64.21900  2.87400  1.000 60.55119  ? 8   SER A CB  1 
ATOM   66   O OG  . SER A 1 11  ? -1.63700  64.89200  2.38000  1.000 68.31067  ? 8   SER A OG  1 
ATOM   67   N N   . ASN A 1 12  ? -1.38500  61.87200  2.93100  1.000 46.32370  ? 9   ASN A N   1 
ATOM   68   C CA  . ASN A 1 12  ? -0.54100  60.67000  3.16500  1.000 46.25149  ? 9   ASN A CA  1 
ATOM   69   C C   . ASN A 1 12  ? -0.98500  59.97100  4.45500  1.000 52.63242  ? 9   ASN A C   1 
ATOM   70   O O   . ASN A 1 12  ? -0.22700  59.12500  4.95300  1.000 51.99164  ? 9   ASN A O   1 
ATOM   71   C CB  . ASN A 1 12  ? 0.94900   61.01300  3.17100  1.000 63.67706  ? 9   ASN A CB  1 
ATOM   72   C CG  . ASN A 1 12  ? 1.57000   60.93400  1.79300  1.000 66.69152  ? 9   ASN A CG  1 
ATOM   73   O OD1 . ASN A 1 12  ? 0.89400   60.60800  0.82000  1.000 68.45184  ? 9   ASN A OD1 1 
ATOM   74   N ND2 . ASN A 1 12  ? 2.85700   61.22900  1.69900  1.000 79.65981  ? 9   ASN A ND2 1 
ATOM   75   N N   . ASP A 1 13  ? -2.15000  60.34000  4.99300  1.000 45.32068  ? 10  ASP A N   1 
ATOM   76   C CA  . ASP A 1 13  ? -2.61900  59.75700  6.27700  1.000 39.69035  ? 10  ASP A CA  1 
ATOM   77   C C   . ASP A 1 13  ? -3.70600  58.71400  6.00800  1.000 41.76620  ? 10  ASP A C   1 
ATOM   78   O O   . ASP A 1 13  ? -4.67300  59.03700  5.29800  1.000 38.05508  ? 10  ASP A O   1 
ATOM   79   C CB  . ASP A 1 13  ? -3.12600  60.84400  7.22700  1.000 44.83903  ? 10  ASP A CB  1 
ATOM   80   C CG  . ASP A 1 13  ? -2.01400  61.65500  7.86700  1.000 53.99234  ? 10  ASP A CG  1 
ATOM   81   O OD1 . ASP A 1 13  ? -0.90400  61.11000  8.01500  1.000 64.21232  ? 10  ASP A OD1 1 
ATOM   82   O OD2 . ASP A 1 13  ? -2.27000  62.82500  8.21000  1.000 56.61600  ? 10  ASP A OD2 1 
ATOM   83   N N   . VAL A 1 14  ? -3.54200  57.50700  6.55700  1.000 39.92404  ? 11  VAL A N   1 
ATOM   84   C CA  . VAL A 1 14  ? -4.58700  56.45200  6.41300  1.000 37.56773  ? 11  VAL A CA  1 
ATOM   85   C C   . VAL A 1 14  ? -5.61000  56.66300  7.52900  1.000 36.78564  ? 11  VAL A C   1 
ATOM   86   O O   . VAL A 1 14  ? -5.19100  56.76100  8.69500  1.000 36.93987  ? 11  VAL A O   1 
ATOM   87   C CB  . VAL A 1 14  ? -3.96800  55.04400  6.45300  1.000 40.71742  ? 11  VAL A CB  1 
ATOM   88   C CG1 . VAL A 1 14  ? -5.01700  53.95800  6.28900  1.000 34.77230  ? 11  VAL A CG1 1 
ATOM   89   C CG2 . VAL A 1 14  ? -2.86400  54.89600  5.42000  1.000 36.06829  ? 11  VAL A CG2 1 
ATOM   90   N N   . VAL A 1 15  ? -6.89700  56.73300  7.18300  1.000 37.26475  ? 12  VAL A N   1 
ATOM   91   C CA  . VAL A 1 15  ? -7.93700  57.05200  8.20200  1.000 40.54908  ? 12  VAL A CA  1 
ATOM   92   C C   . VAL A 1 15  ? -8.90800  55.87900  8.34200  1.000 45.62083  ? 12  VAL A C   1 
ATOM   93   O O   . VAL A 1 15  ? -9.40800  55.40600  7.30900  1.000 42.19762  ? 12  VAL A O   1 
ATOM   94   C CB  . VAL A 1 15  ? -8.68100  58.34900  7.83300  1.000 41.43335  ? 12  VAL A CB  1 
ATOM   95   C CG1 . VAL A 1 15  ? -9.76300  58.69900  8.84200  1.000 43.74361  ? 12  VAL A CG1 1 
ATOM   96   C CG2 . VAL A 1 15  ? -7.72300  59.51300  7.64200  1.000 43.66526  ? 12  VAL A CG2 1 
ATOM   97   N N   . MET A 1 16  ? -9.16000  55.43300  9.57600  1.000 45.37009  ? 13  MET A N   1 
ATOM   98   C CA  . MET A 1 16  ? -10.16900 54.36800  9.80700  1.000 37.89177  ? 13  MET A CA  1 
ATOM   99   C C   . MET A 1 16  ? -11.39400 55.01100  10.46300 1.000 46.08262  ? 13  MET A C   1 
ATOM   100  O O   . MET A 1 16  ? -11.25600 55.52200  11.58700 1.000 42.17445  ? 13  MET A O   1 
ATOM   101  C CB  . MET A 1 16  ? -9.62300  53.25900  10.71000 1.000 37.35009  ? 13  MET A CB  1 
ATOM   102  C CG  . MET A 1 16  ? -10.44000 51.98500  10.64100 1.000 40.37786  ? 13  MET A CG  1 
ATOM   103  S SD  . MET A 1 16  ? -10.61400 51.18100  12.24900 1.000 47.07176  ? 13  MET A SD  1 
ATOM   104  C CE  . MET A 1 16  ? -11.58900 52.40400  13.12300 1.000 57.59707  ? 13  MET A CE  1 
ATOM   105  N N   . THR A 1 17  ? -12.53700 54.99700  9.77600  1.000 39.99139  ? 14  THR A N   1 
ATOM   106  C CA  . THR A 1 17  ? -13.75500 55.59900  10.30000 1.000 46.91670  ? 14  THR A CA  1 
ATOM   107  C C   . THR A 1 17  ? -14.61700 54.52500  10.95300 1.000 48.12323  ? 14  THR A C   1 
ATOM   108  O O   . THR A 1 17  ? -14.89200 53.48600  10.34300 1.000 48.44071  ? 14  THR A O   1 
ATOM   109  C CB  . THR A 1 17  ? -14.53600 56.30600  9.19000  1.000 48.94613  ? 14  THR A CB  1 
ATOM   110  O OG1 . THR A 1 17  ? -13.74000 57.36700  8.65100  1.000 50.06775  ? 14  THR A OG1 1 
ATOM   111  C CG2 . THR A 1 17  ? -15.82900 56.89200  9.73700  1.000 51.42633  ? 14  THR A CG2 1 
ATOM   112  N N   . TYR A 1 18  ? -15.04100 54.77800  12.18900 1.000 43.75784  ? 15  TYR A N   1 
ATOM   113  C CA  . TYR A 1 18  ? -15.87900 53.84900  12.93400 1.000 49.33193  ? 15  TYR A CA  1 
ATOM   114  C C   . TYR A 1 18  ? -17.30100 54.38600  13.00000 1.000 46.86893  ? 15  TYR A C   1 
ATOM   115  O O   . TYR A 1 18  ? -17.52100 55.52300  13.42700 1.000 46.78947  ? 15  TYR A O   1 
ATOM   116  C CB  . TYR A 1 18  ? -15.33600 53.62100  14.34500 1.000 43.08519  ? 15  TYR A CB  1 
ATOM   117  C CG  . TYR A 1 18  ? -16.15200 52.63300  15.14800 1.000 49.05455  ? 15  TYR A CG  1 
ATOM   118  C CD1 . TYR A 1 18  ? -16.33500 51.33100  14.70300 1.000 52.16230  ? 15  TYR A CD1 1 
ATOM   119  C CD2 . TYR A 1 18  ? -16.73300 53.00000  16.35400 1.000 47.47384  ? 15  TYR A CD2 1 
ATOM   120  C CE1 . TYR A 1 18  ? -17.07600 50.42200  15.43300 1.000 57.89112  ? 15  TYR A CE1 1 
ATOM   121  C CE2 . TYR A 1 18  ? -17.47600 52.09600  17.09400 1.000 59.16197  ? 15  TYR A CE2 1 
ATOM   122  C CZ  . TYR A 1 18  ? -17.64500 50.80900  16.62800 1.000 59.04908  ? 15  TYR A CZ  1 
ATOM   123  O OH  . TYR A 1 18  ? -18.38300 49.90700  17.36100 1.000 67.86019  ? 15  TYR A OH  1 
ATOM   124  N N   . ASP A 1 19  ? -18.26800 53.55500  12.64000 1.000 55.66085  ? 16  ASP A N   1 
ATOM   125  C CA  . ASP A 1 19  ? -19.69300 53.94500  12.72500 1.000 64.60165  ? 16  ASP A CA  1 
ATOM   126  C C   . ASP A 1 19  ? -20.36400 53.05800  13.77200 1.000 57.89449  ? 16  ASP A C   1 
ATOM   127  O O   . ASP A 1 19  ? -21.39400 53.48400  14.27200 1.000 62.83011  ? 16  ASP A O   1 
ATOM   128  C CB  . ASP A 1 19  ? -20.34900 53.87100  11.34700 1.000 71.17926  ? 16  ASP A CB  1 
ATOM   129  C CG  . ASP A 1 19  ? -21.54100 54.79600  11.19100 1.000 81.27137  ? 16  ASP A CG  1 
ATOM   130  O OD1 . ASP A 1 19  ? -21.87600 55.48600  12.17000 1.000 78.91861  ? 16  ASP A OD1 1 
ATOM   131  O OD2 . ASP A 1 19  ? -22.12000 54.82200  10.09200 1.000 78.61329  ? 16  ASP A OD2 1 
ATOM   132  N N   . GLU A 1 24  ? -25.12100 51.34700  17.18400 1.000 102.48328 ? 21  GLU A N   1 
ATOM   133  C CA  . GLU A 1 24  ? -25.10400 51.20200  18.65600 1.000 97.36482  ? 21  GLU A CA  1 
ATOM   134  C C   . GLU A 1 24  ? -24.83400 52.55800  19.29600 1.000 99.32953  ? 21  GLU A C   1 
ATOM   135  O O   . GLU A 1 24  ? -24.62600 53.53300  18.56400 1.000 100.95533 ? 21  GLU A O   1 
ATOM   136  C CB  . GLU A 1 24  ? -23.98200 50.24000  19.03900 1.000 96.60803  ? 21  GLU A CB  1 
ATOM   137  C CG  . GLU A 1 24  ? -22.59600 50.77600  18.73400 1.000 97.12906  ? 21  GLU A CG  1 
ATOM   138  C CD  . GLU A 1 24  ? -21.53300 49.71700  18.50700 1.000 98.49290  ? 21  GLU A CD  1 
ATOM   139  O OE1 . GLU A 1 24  ? -21.57300 49.05900  17.45200 1.000 104.02365 ? 21  GLU A OE1 1 
ATOM   140  O OE2 . GLU A 1 24  ? -20.66700 49.55600  19.38400 1.000 98.38229  ? 21  GLU A OE2 1 
ATOM   141  N N   . GLN A 1 25  ? -24.92400 52.63000  20.61600 1.000 107.26193 ? 22  GLN A N   1 
ATOM   142  C CA  . GLN A 1 25  ? -24.54300 53.88600  21.29600 1.000 101.32078 ? 22  GLN A CA  1 
ATOM   143  C C   . GLN A 1 25  ? -23.02100 53.97000  21.18700 1.000 102.19301 ? 22  GLN A C   1 
ATOM   144  O O   . GLN A 1 25  ? -22.35000 53.20700  21.90100 1.000 97.14846  ? 22  GLN A O   1 
ATOM   145  C CB  . GLN A 1 25  ? -25.07600 53.85500  22.71900 1.000 93.97051  ? 22  GLN A CB  1 
ATOM   146  C CG  . GLN A 1 25  ? -26.39100 54.60600  22.88100 1.000 107.89255 ? 22  GLN A CG  1 
ATOM   147  C CD  . GLN A 1 25  ? -27.51400 54.02900  22.05300 1.000 119.17973 ? 22  GLN A CD  1 
ATOM   148  O OE1 . GLN A 1 25  ? -27.76500 52.82600  22.06100 1.000 117.62469 ? 22  GLN A OE1 1 
ATOM   149  N NE2 . GLN A 1 25  ? -28.20800 54.89200  21.32900 1.000 118.80717 ? 22  GLN A NE2 1 
ATOM   150  N N   . ILE A 1 26  ? -22.50500 54.83600  20.31300 1.000 77.75727  ? 23  ILE A N   1 
ATOM   151  C CA  . ILE A 1 26  ? -21.04500 54.89800  20.04200 1.000 70.47434  ? 23  ILE A CA  1 
ATOM   152  C C   . ILE A 1 26  ? -20.37700 55.76900  21.10100 1.000 69.50547  ? 23  ILE A C   1 
ATOM   153  O O   . ILE A 1 26  ? -19.16100 55.95600  21.01500 1.000 63.16407  ? 23  ILE A O   1 
ATOM   154  C CB  . ILE A 1 26  ? -20.83000 55.41900  18.61100 1.000 70.69392  ? 23  ILE A CB  1 
ATOM   155  C CG1 . ILE A 1 26  ? -21.63600 56.68300  18.32300 1.000 67.56947  ? 23  ILE A CG1 1 
ATOM   156  C CG2 . ILE A 1 26  ? -21.11900 54.33100  17.59500 1.000 67.65380  ? 23  ILE A CG2 1 
ATOM   157  C CD1 . ILE A 1 26  ? -21.03200 57.51900  17.23300 1.000 73.86574  ? 23  ILE A CD1 1 
ATOM   158  N N   . ILE A 1 27  ? -21.15800 56.28800  22.04400 1.000 66.60218  ? 24  ILE A N   1 
ATOM   159  C CA  . ILE A 1 27  ? -20.62000 57.13700  23.14100 1.000 65.16242  ? 24  ILE A CA  1 
ATOM   160  C C   . ILE A 1 27  ? -19.55900 56.36300  23.92500 1.000 60.69432  ? 24  ILE A C   1 
ATOM   161  O O   . ILE A 1 27  ? -18.65000 57.00600  24.43600 1.000 59.15688  ? 24  ILE A O   1 
ATOM   162  C CB  . ILE A 1 27  ? -21.78200 57.64100  24.02300 1.000 70.71937  ? 24  ILE A CB  1 
ATOM   163  C CG1 . ILE A 1 27  ? -21.30100 58.49600  25.19600 1.000 79.74289  ? 24  ILE A CG1 1 
ATOM   164  C CG2 . ILE A 1 27  ? -22.65400 56.48800  24.49000 1.000 70.05477  ? 24  ILE A CG2 1 
ATOM   165  C CD1 . ILE A 1 27  ? -20.93400 59.90300  24.81500 1.000 74.87223  ? 24  ILE A CD1 1 
ATOM   166  N N   . TRP A 1 28  ? -19.65800 55.03700  23.98800 1.000 63.61562  ? 25  TRP A N   1 
ATOM   167  C CA  . TRP A 1 28  ? -18.69800 54.30200  24.80500 1.000 63.67957  ? 25  TRP A CA  1 
ATOM   168  C C   . TRP A 1 28  ? -17.26600 54.50600  24.32400 1.000 57.99148  ? 25  TRP A C   1 
ATOM   169  O O   . TRP A 1 28  ? -16.32700 54.41700  25.12300 1.000 59.73969  ? 25  TRP A O   1 
ATOM   170  C CB  . TRP A 1 28  ? -19.04600 52.81300  24.80600 1.000 60.26677  ? 25  TRP A CB  1 
ATOM   171  C CG  . TRP A 1 28  ? -18.76700 52.15300  23.49000 1.000 74.40788  ? 25  TRP A CG  1 
ATOM   172  C CD1 . TRP A 1 28  ? -19.59900 52.08900  22.40800 1.000 73.75795  ? 25  TRP A CD1 1 
ATOM   173  C CD2 . TRP A 1 28  ? -17.56200 51.47800  23.10900 1.000 68.41629  ? 25  TRP A CD2 1 
ATOM   174  N NE1 . TRP A 1 28  ? -18.98900 51.40800  21.38100 1.000 72.61855  ? 25  TRP A NE1 1 
ATOM   175  C CE2 . TRP A 1 28  ? -17.73800 51.02300  21.78600 1.000 73.30904  ? 25  TRP A CE2 1 
ATOM   176  C CE3 . TRP A 1 28  ? -16.35400 51.21100  23.76000 1.000 59.13878  ? 25  TRP A CE3 1 
ATOM   177  C CZ2 . TRP A 1 28  ? -16.75000 50.31700  21.10200 1.000 69.03755  ? 25  TRP A CZ2 1 
ATOM   178  C CZ3 . TRP A 1 28  ? -15.37500 50.50900  23.08000 1.000 62.98215  ? 25  TRP A CZ3 1 
ATOM   179  C CH2 . TRP A 1 28  ? -15.57800 50.07100  21.76500 1.000 63.31647  ? 25  TRP A CH2 1 
ATOM   180  N N   . VAL A 1 29  ? -17.09700 54.79500  23.03000 1.000 50.67483  ? 26  VAL A N   1 
ATOM   181  C CA  . VAL A 1 29  ? -15.73400 55.03400  22.46700 1.000 45.65550  ? 26  VAL A CA  1 
ATOM   182  C C   . VAL A 1 29  ? -15.17100 56.29900  23.11600 1.000 42.98026  ? 26  VAL A C   1 
ATOM   183  O O   . VAL A 1 29  ? -14.04600 56.24200  23.64600 1.000 38.65997  ? 26  VAL A O   1 
ATOM   184  C CB  . VAL A 1 29  ? -15.77600 55.16500  20.93300 1.000 45.37366  ? 26  VAL A CB  1 
ATOM   185  C CG1 . VAL A 1 29  ? -14.40100 55.43400  20.34200 1.000 41.14892  ? 26  VAL A CG1 1 
ATOM   186  C CG2 . VAL A 1 29  ? -16.42000 53.95800  20.27300 1.000 48.06102  ? 26  VAL A CG2 1 
ATOM   187  N N   . TRP A 1 30  ? -15.94400 57.38700  23.09000 1.000 44.69418  ? 27  TRP A N   1 
ATOM   188  C CA  . TRP A 1 30  ? -15.49500 58.67400  23.68300 1.000 47.23201  ? 27  TRP A CA  1 
ATOM   189  C C   . TRP A 1 30  ? -15.28200 58.49800  25.18800 1.000 49.26921  ? 27  TRP A C   1 
ATOM   190  O O   . TRP A 1 30  ? -14.29700 59.04300  25.70700 1.000 46.03456  ? 27  TRP A O   1 
ATOM   191  C CB  . TRP A 1 30  ? -16.51200 59.78000  23.37500 1.000 45.48742  ? 27  TRP A CB  1 
ATOM   192  C CG  . TRP A 1 30  ? -16.08800 61.16000  23.77300 1.000 46.59389  ? 27  TRP A CG  1 
ATOM   193  C CD1 . TRP A 1 30  ? -16.81700 62.05700  24.49900 1.000 46.73660  ? 27  TRP A CD1 1 
ATOM   194  C CD2 . TRP A 1 30  ? -14.84700 61.81700  23.45700 1.000 51.89035  ? 27  TRP A CD2 1 
ATOM   195  N NE1 . TRP A 1 30  ? -16.11600 63.22100  24.66100 1.000 48.41636  ? 27  TRP A NE1 1 
ATOM   196  C CE2 . TRP A 1 30  ? -14.90400 63.10400  24.03300 1.000 47.66582  ? 27  TRP A CE2 1 
ATOM   197  C CE3 . TRP A 1 30  ? -13.69600 61.45000  22.74900 1.000 42.36754  ? 27  TRP A CE3 1 
ATOM   198  C CZ2 . TRP A 1 30  ? -13.85700 64.01700  23.92300 1.000 41.86220  ? 27  TRP A CZ2 1 
ATOM   199  C CZ3 . TRP A 1 30  ? -12.66200 62.35300  22.64300 1.000 47.23944  ? 27  TRP A CZ3 1 
ATOM   200  C CH2 . TRP A 1 30  ? -12.74400 63.61800  23.22200 1.000 39.53099  ? 27  TRP A CH2 1 
ATOM   201  N N   . GLU A 1 31  ? -16.17200 57.75700  25.85100 1.000 56.82560  ? 28  GLU A N   1 
ATOM   202  C CA  . GLU A 1 31  ? -16.06000 57.54600  27.31700 1.000 61.95456  ? 28  GLU A CA  1 
ATOM   203  C C   . GLU A 1 31  ? -14.76000 56.80100  27.63300 1.000 55.14429  ? 28  GLU A C   1 
ATOM   204  O O   . GLU A 1 31  ? -14.07300 57.20600  28.58600 1.000 58.36700  ? 28  GLU A O   1 
ATOM   205  C CB  . GLU A 1 31  ? -17.27600 56.77900  27.83700 1.000 66.54136  ? 28  GLU A CB  1 
ATOM   206  C CG  . GLU A 1 31  ? -17.27200 56.58600  29.34300 1.000 75.02321  ? 28  GLU A CG  1 
ATOM   207  C CD  . GLU A 1 31  ? -18.48900 55.86900  29.90100 1.000 104.58774 ? 28  GLU A CD  1 
ATOM   208  O OE1 . GLU A 1 31  ? -19.35700 55.46900  29.09900 1.000 111.21063 ? 28  GLU A OE1 1 
ATOM   209  O OE2 . GLU A 1 31  ? -18.56500 55.70700  31.13500 1.000 103.65749 ? 28  GLU A OE2 1 
ATOM   210  N N   . SER A 1 32  ? -14.42800 55.77500  26.84600 1.000 46.09487  ? 29  SER A N   1 
ATOM   211  C CA  . SER A 1 32  ? -13.17100 55.01200  27.06200 1.000 45.76777  ? 29  SER A CA  1 
ATOM   212  C C   . SER A 1 32  ? -11.96900 55.93500  26.85000 1.000 48.14583  ? 29  SER A C   1 
ATOM   213  O O   . SER A 1 32  ? -11.01400 55.85000  27.64000 1.000 45.21184  ? 29  SER A O   1 
ATOM   214  C CB  . SER A 1 32  ? -13.10300 53.80800  26.16400 1.000 44.98198  ? 29  SER A CB  1 
ATOM   215  O OG  . SER A 1 32  ? -11.90200 53.08500  26.38000 1.000 50.54519  ? 29  SER A OG  1 
ATOM   216  N N   . LEU A 1 33  ? -12.02400 56.78100  25.81900 1.000 42.56105  ? 30  LEU A N   1 
ATOM   217  C CA  . LEU A 1 33  ? -10.92100 57.73800  25.54500 1.000 41.74607  ? 30  LEU A CA  1 
ATOM   218  C C   . LEU A 1 33  ? -10.79900 58.73600  26.70100 1.000 41.21538  ? 30  LEU A C   1 
ATOM   219  O O   . LEU A 1 33  ? -9.67300  59.10200  27.04600 1.000 43.70390  ? 30  LEU A O   1 
ATOM   220  C CB  . LEU A 1 33  ? -11.19300 58.45000  24.21800 1.000 40.52373  ? 30  LEU A CB  1 
ATOM   221  C CG  . LEU A 1 33  ? -10.90600 57.62300  22.96700 1.000 45.97615  ? 30  LEU A CG  1 
ATOM   222  C CD1 . LEU A 1 33  ? -11.46700 58.29900  21.72700 1.000 41.47699  ? 30  LEU A CD1 1 
ATOM   223  C CD2 . LEU A 1 33  ? -9.41400  57.37700  22.81200 1.000 37.61279  ? 30  LEU A CD2 1 
ATOM   224  N N   . ASN A 1 34  ? -11.92000 59.20300  27.24700 1.000 54.80544  ? 31  ASN A N   1 
ATOM   225  C CA  . ASN A 1 34  ? -11.83800 60.10900  28.42100 1.000 58.70224  ? 31  ASN A CA  1 
ATOM   226  C C   . ASN A 1 34  ? -11.23400 59.36500  29.61800 1.000 59.44315  ? 31  ASN A C   1 
ATOM   227  O O   . ASN A 1 34  ? -10.37300 59.95400  30.29300 1.000 65.25051  ? 31  ASN A O   1 
ATOM   228  C CB  . ASN A 1 34  ? -13.20400 60.71000  28.75900 1.000 62.99912  ? 31  ASN A CB  1 
ATOM   229  C CG  . ASN A 1 34  ? -13.81100 61.47700  27.60400 1.000 71.67288  ? 31  ASN A CG  1 
ATOM   230  O OD1 . ASN A 1 34  ? -13.09300 62.01000  26.76100 1.000 69.14875  ? 31  ASN A OD1 1 
ATOM   231  N ND2 . ASN A 1 34  ? -15.13100 61.53000  27.55100 1.000 75.64394  ? 31  ASN A ND2 1 
ATOM   232  N N   . LYS A 1 35  ? -11.68300 58.13400  29.87800 1.000 46.68600  ? 32  LYS A N   1 
ATOM   233  C CA  . LYS A 1 35  ? -11.21400 57.36400  31.06400 1.000 49.40904  ? 32  LYS A CA  1 
ATOM   234  C C   . LYS A 1 35  ? -9.75600  56.89500  30.96500 1.000 49.09585  ? 32  LYS A C   1 
ATOM   235  O O   . LYS A 1 35  ? -9.04200  57.03600  31.97300 1.000 51.66679  ? 32  LYS A O   1 
ATOM   236  C CB  . LYS A 1 35  ? -12.15600 56.18700  31.33300 1.000 50.97704  ? 32  LYS A CB  1 
ATOM   237  C CG  . LYS A 1 35  ? -13.59700 56.57100  31.64300 1.000 52.45319  ? 32  LYS A CG  1 
ATOM   238  C CD  . LYS A 1 35  ? -13.74700 57.36800  32.92000 1.000 60.11182  ? 32  LYS A CD  1 
ATOM   239  C CE  . LYS A 1 35  ? -15.18800 57.68300  33.25800 1.000 64.85173  ? 32  LYS A CE  1 
ATOM   240  N NZ  . LYS A 1 35  ? -15.29700 58.48400  34.50000 1.000 60.50585  ? 32  LYS A NZ  1 
ATOM   241  N N   . PHE A 1 36  ? -9.31600  56.37700  29.81100 1.000 50.25172  ? 33  PHE A N   1 
ATOM   242  C CA  . PHE A 1 36  ? -7.95500  55.77300  29.73400 1.000 50.33679  ? 33  PHE A CA  1 
ATOM   243  C C   . PHE A 1 36  ? -7.16100  56.28800  28.53200 1.000 48.78098  ? 33  PHE A C   1 
ATOM   244  O O   . PHE A 1 36  ? -6.06800  55.74300  28.28800 1.000 52.42324  ? 33  PHE A O   1 
ATOM   245  C CB  . PHE A 1 36  ? -8.05400  54.24800  29.64100 1.000 51.18788  ? 33  PHE A CB  1 
ATOM   246  C CG  . PHE A 1 36  ? -9.11000  53.61400  30.50900 1.000 54.45887  ? 33  PHE A CG  1 
ATOM   247  C CD1 . PHE A 1 36  ? -8.94000  53.52300  31.88100 1.000 58.56934  ? 33  PHE A CD1 1 
ATOM   248  C CD2 . PHE A 1 36  ? -10.27000 53.09900  29.95400 1.000 53.94759  ? 33  PHE A CD2 1 
ATOM   249  C CE1 . PHE A 1 36  ? -9.91100  52.94000  32.67900 1.000 59.17103  ? 33  PHE A CE1 1 
ATOM   250  C CE2 . PHE A 1 36  ? -11.23900 52.51300  30.75300 1.000 68.07610  ? 33  PHE A CE2 1 
ATOM   251  C CZ  . PHE A 1 36  ? -11.05800 52.43500  32.11300 1.000 65.65900  ? 33  PHE A CZ  1 
ATOM   252  N N   . GLN A 1 37  ? -7.68400  57.28500  27.81700 1.000 46.47555  ? 34  GLN A N   1 
ATOM   253  C CA  . GLN A 1 37  ? -7.00000  57.87100  26.66400 1.000 45.02537  ? 34  GLN A CA  1 
ATOM   254  C C   . GLN A 1 37  ? -6.64400  56.82600  25.61200 1.000 45.47855  ? 34  GLN A C   1 
ATOM   255  O O   . GLN A 1 37  ? -5.78100  57.06600  24.76200 1.000 48.49593  ? 34  GLN A O   1 
ATOM   256  C CB  . GLN A 1 37  ? -5.75400  58.65700  27.09200 1.000 50.21101  ? 34  GLN A CB  1 
ATOM   257  C CG  . GLN A 1 37  ? -6.05700  59.84700  28.00200 1.000 46.75535  ? 34  GLN A CG  1 
ATOM   258  C CD  . GLN A 1 37  ? -6.32300  59.43700  29.44400 1.000 53.90961  ? 34  GLN A CD  1 
ATOM   259  O OE1 . GLN A 1 37  ? -7.38100  59.73300  30.00600 1.000 52.45197  ? 34  GLN A OE1 1 
ATOM   260  N NE2 . GLN A 1 37  ? -5.35700  58.75800  30.05000 1.000 53.73990  ? 34  GLN A NE2 1 
ATOM   261  N N   . THR A 1 38  ? -7.29800  55.66500  25.67300 1.000 44.39311  ? 35  THR A N   1 
ATOM   262  C CA  . THR A 1 38  ? -7.21600  54.62800  24.65500 1.000 50.15631  ? 35  THR A CA  1 
ATOM   263  C C   . THR A 1 38  ? -8.60200  54.02200  24.48300 1.000 45.93728  ? 35  THR A C   1 
ATOM   264  O O   . THR A 1 38  ? -9.48600  54.19700  25.32600 1.000 46.00963  ? 35  THR A O   1 
ATOM   265  C CB  . THR A 1 38  ? -6.20800  53.51900  25.01400 1.000 52.92544  ? 35  THR A CB  1 
ATOM   266  O OG1 . THR A 1 38  ? -6.54700  52.95100  26.28500 1.000 55.31266  ? 35  THR A OG1 1 
ATOM   267  C CG2 . THR A 1 38  ? -4.78000  54.05500  25.07000 1.000 50.96555  ? 35  THR A CG2 1 
ATOM   268  N N   . VAL A 1 39  ? -8.81700  53.36700  23.34600 1.000 46.01306  ? 36  VAL A N   1 
ATOM   269  C CA  . VAL A 1 39  ? -10.10700 52.68100  23.05300 1.000 44.54103  ? 36  VAL A CA  1 
ATOM   270  C C   . VAL A 1 39  ? -9.81900  51.48800  22.14700 1.000 47.22631  ? 36  VAL A C   1 
ATOM   271  O O   . VAL A 1 39  ? -8.88300  51.57300  21.36100 1.000 46.77132  ? 36  VAL A O   1 
ATOM   272  C CB  . VAL A 1 39  ? -11.14800 53.61300  22.42000 1.000 44.94724  ? 36  VAL A CB  1 
ATOM   273  C CG1 . VAL A 1 39  ? -10.71300 54.14700  21.06800 1.000 38.43451  ? 36  VAL A CG1 1 
ATOM   274  C CG2 . VAL A 1 39  ? -12.51500 52.96000  22.33700 1.000 42.85639  ? 36  VAL A CG2 1 
ATOM   275  N N   . CYS A 1 40  ? -10.57800 50.40800  22.28800 1.000 49.56576  ? 37  CYS A N   1 
ATOM   276  C CA  . CYS A 1 40  ? -10.45300 49.23900  21.39600 1.000 49.62478  ? 37  CYS A CA  1 
ATOM   277  C C   . CYS A 1 40  ? -11.64700 49.20900  20.45600 1.000 52.27727  ? 37  CYS A C   1 
ATOM   278  O O   . CYS A 1 40  ? -12.75500 49.09100  20.94500 1.000 52.65063  ? 37  CYS A O   1 
ATOM   279  C CB  . CYS A 1 40  ? -10.41800 47.92800  22.16800 1.000 51.17359  ? 37  CYS A CB  1 
ATOM   280  S SG  . CYS A 1 40  ? -9.60300  46.56000  21.30500 1.000 55.87953  ? 37  CYS A SG  1 
ATOM   281  N N   . ILE A 1 41  ? -11.39000 49.24600  19.15100 1.000 49.56950  ? 38  ILE A N   1 
ATOM   282  C CA  . ILE A 1 41  ? -12.47300 49.25400  18.13500 1.000 50.69299  ? 38  ILE A CA  1 
ATOM   283  C C   . ILE A 1 41  ? -12.46000 47.91800  17.39200 1.000 54.42017  ? 38  ILE A C   1 
ATOM   284  O O   . ILE A 1 41  ? -11.36900 47.47700  17.04300 1.000 53.86670  ? 38  ILE A O   1 
ATOM   285  C CB  . ILE A 1 41  ? -12.27800 50.46400  17.21400 1.000 49.31908  ? 38  ILE A CB  1 
ATOM   286  C CG1 . ILE A 1 41  ? -12.19200 51.77100  18.00300 1.000 50.23114  ? 38  ILE A CG1 1 
ATOM   287  C CG2 . ILE A 1 41  ? -13.35000 50.51600  16.14500 1.000 52.14152  ? 38  ILE A CG2 1 
ATOM   288  C CD1 . ILE A 1 41  ? -13.53100 52.35900  18.34700 1.000 50.82027  ? 38  ILE A CD1 1 
ATOM   289  N N   . SER A 1 42  ? -13.60500 47.23800  17.30700 1.000 58.79957  ? 39  SER A N   1 
ATOM   290  C CA  . SER A 1 42  ? -13.75100 45.93400  16.59800 1.000 68.16463  ? 39  SER A CA  1 
ATOM   291  C C   . SER A 1 42  ? -12.90100 44.86200  17.26800 1.000 65.92178  ? 39  SER A C   1 
ATOM   292  O O   . SER A 1 42  ? -12.60700 43.88700  16.59800 1.000 68.22682  ? 39  SER A O   1 
ATOM   293  C CB  . SER A 1 42  ? -13.58600 45.99900  15.10200 1.000 63.23035  ? 39  SER A CB  1 
ATOM   294  O OG  . SER A 1 42  ? -14.61900 46.77000  14.51400 1.000 70.54890  ? 39  SER A OG  1 
ATOM   295  N N   . ARG A 1 43  ? -12.44900 45.10500  18.48900 1.000 63.54023  ? 40  ARG A N   1 
ATOM   296  C CA  . ARG A 1 43  ? -11.73600 44.09800  19.30900 1.000 62.70844  ? 40  ARG A CA  1 
ATOM   297  C C   . ARG A 1 43  ? -10.28600 43.90400  18.87600 1.000 66.67469  ? 40  ARG A C   1 
ATOM   298  O O   . ARG A 1 43  ? -9.57700  43.20200  19.60000 1.000 64.75831  ? 40  ARG A O   1 
ATOM   299  C CB  . ARG A 1 43  ? -12.57200 42.82300  19.45200 1.000 63.48783  ? 40  ARG A CB  1 
ATOM   300  C CG  . ARG A 1 43  ? -13.84300 43.00900  20.26400 1.000 70.78198  ? 40  ARG A CG  1 
ATOM   301  C CD  . ARG A 1 43  ? -14.60900 41.71100  20.41700 1.000 82.44878  ? 40  ARG A CD  1 
ATOM   302  N NE  . ARG A 1 43  ? -15.86100 41.89600  21.13200 1.000 92.18999  ? 40  ARG A NE  1 
ATOM   303  C CZ  . ARG A 1 43  ? -16.77600 40.94900  21.30500 1.000 100.02497 ? 40  ARG A CZ  1 
ATOM   304  N NH1 . ARG A 1 43  ? -16.57500 39.73900  20.81400 1.000 90.65545  ? 40  ARG A NH1 1 
ATOM   305  N NH2 . ARG A 1 43  ? -17.88500 41.21400  21.97000 1.000 103.84329 ? 40  ARG A NH2 1 
ATOM   306  N N   . ILE A 1 44  ? -9.84300  44.55500  17.79900 1.000 70.59769  ? 41  ILE A N   1 
ATOM   307  C CA  . ILE A 1 44  ? -8.46400  44.31900  17.26800 1.000 64.87350  ? 41  ILE A CA  1 
ATOM   308  C C   . ILE A 1 44  ? -7.68900  45.62500  17.19300 1.000 62.49808  ? 41  ILE A C   1 
ATOM   309  O O   . ILE A 1 44  ? -6.46600  45.58200  17.35200 1.000 65.29665  ? 41  ILE A O   1 
ATOM   310  C CB  . ILE A 1 44  ? -8.54200  43.60600  15.90300 1.000 65.49576  ? 41  ILE A CB  1 
ATOM   311  C CG1 . ILE A 1 44  ? -8.81800  42.11400  16.07500 1.000 68.13817  ? 41  ILE A CG1 1 
ATOM   312  C CG2 . ILE A 1 44  ? -7.30200  43.83000  15.05500 1.000 64.52892  ? 41  ILE A CG2 1 
ATOM   313  C CD1 . ILE A 1 44  ? -10.22700 41.73900  15.74100 1.000 80.36499  ? 41  ILE A CD1 1 
ATOM   314  N N   . PHE A 1 45  ? -8.38600  46.74300  17.06100 1.000 50.84412  ? 42  PHE A N   1 
ATOM   315  C CA  . PHE A 1 45  ? -7.69700  48.03100  16.83100 1.000 45.20088  ? 42  PHE A CA  1 
ATOM   316  C C   . PHE A 1 45  ? -7.60000  48.82200  18.13300 1.000 54.86265  ? 42  PHE A C   1 
ATOM   317  O O   . PHE A 1 45  ? -8.61900  49.06800  18.75300 1.000 55.73153  ? 42  PHE A O   1 
ATOM   318  C CB  . PHE A 1 45  ? -8.39800  48.74200  15.67600 1.000 42.25673  ? 42  PHE A CB  1 
ATOM   319  C CG  . PHE A 1 45  ? -8.41600  47.96500  14.38900 1.000 48.66190  ? 42  PHE A CG  1 
ATOM   320  C CD1 . PHE A 1 45  ? -7.24100  47.50100  13.82800 1.000 46.83187  ? 42  PHE A CD1 1 
ATOM   321  C CD2 . PHE A 1 45  ? -9.60800  47.68600  13.74700 1.000 47.61003  ? 42  PHE A CD2 1 
ATOM   322  C CE1 . PHE A 1 45  ? -7.25700  46.78400  12.64500 1.000 46.66526  ? 42  PHE A CE1 1 
ATOM   323  C CE2 . PHE A 1 45  ? -9.62100  46.96500  12.56700 1.000 45.92720  ? 42  PHE A CE2 1 
ATOM   324  C CZ  . PHE A 1 45  ? -8.44700  46.51800  12.01800 1.000 51.56665  ? 42  PHE A CZ  1 
ATOM   325  N N   . ASN A 1 46  ? -6.38800  49.18900  18.52400 1.000 49.17703  ? 43  ASN A N   1 
ATOM   326  C CA  . ASN A 1 46  ? -6.17200  49.97500  19.75800 1.000 47.01598  ? 43  ASN A CA  1 
ATOM   327  C C   . ASN A 1 46  ? -5.78000  51.40400  19.40300 1.000 46.90117  ? 43  ASN A C   1 
ATOM   328  O O   . ASN A 1 46  ? -4.65900  51.62600  18.96900 1.000 45.09549  ? 43  ASN A O   1 
ATOM   329  C CB  . ASN A 1 46  ? -5.19200  49.30000  20.70800 1.000 51.86803  ? 43  ASN A CB  1 
ATOM   330  C CG  . ASN A 1 46  ? -5.35100  49.76700  22.13800 1.000 67.49705  ? 43  ASN A CG  1 
ATOM   331  O OD1 . ASN A 1 46  ? -6.40900  49.59600  22.73800 1.000 64.02966  ? 43  ASN A OD1 1 
ATOM   332  N ND2 . ASN A 1 46  ? -4.30800  50.36400  22.68800 1.000 60.57623  ? 43  ASN A ND2 1 
ATOM   333  N N   . PHE A 1 47  ? -6.67600  52.33900  19.66300 1.000 43.80450  ? 44  PHE A N   1 
ATOM   334  C CA  . PHE A 1 47  ? -6.42200  53.74200  19.27900 1.000 43.54348  ? 44  PHE A CA  1 
ATOM   335  C C   . PHE A 1 47  ? -6.20900  54.62500  20.50300 1.000 47.84704  ? 44  PHE A C   1 
ATOM   336  O O   . PHE A 1 47  ? -6.91500  54.47100  21.48500 1.000 46.35307  ? 44  PHE A O   1 
ATOM   337  C CB  . PHE A 1 47  ? -7.57300  54.26700  18.42100 1.000 38.56027  ? 44  PHE A CB  1 
ATOM   338  C CG  . PHE A 1 47  ? -7.69100  53.68400  17.04000 1.000 43.41040  ? 44  PHE A CG  1 
ATOM   339  C CD1 . PHE A 1 47  ? -6.73500  53.94400  16.07600 1.000 38.57505  ? 44  PHE A CD1 1 
ATOM   340  C CD2 . PHE A 1 47  ? -8.77500  52.89700  16.70100 1.000 42.89962  ? 44  PHE A CD2 1 
ATOM   341  C CE1 . PHE A 1 47  ? -6.85400  53.41300  14.80400 1.000 42.19455  ? 44  PHE A CE1 1 
ATOM   342  C CE2 . PHE A 1 47  ? -8.89200  52.36700  15.42900 1.000 40.81514  ? 44  PHE A CE2 1 
ATOM   343  C CZ  . PHE A 1 47  ? -7.93100  52.62400  14.48400 1.000 38.11351  ? 44  PHE A CZ  1 
ATOM   344  N N   . GLN A 1 48  ? -5.22800  55.50400  20.44100 1.000 41.62254  ? 45  GLN A N   1 
ATOM   345  C CA  . GLN A 1 48  ? -5.00600  56.49000  21.48700 1.000 45.02732  ? 45  GLN A CA  1 
ATOM   346  C C   . GLN A 1 48  ? -5.78200  57.76200  21.16800 1.000 38.93242  ? 45  GLN A C   1 
ATOM   347  O O   . GLN A 1 48  ? -6.21900  57.98200  20.03600 1.000 41.66315  ? 45  GLN A O   1 
ATOM   348  C CB  . GLN A 1 48  ? -3.51400  56.80700  21.63900 1.000 43.91108  ? 45  GLN A CB  1 
ATOM   349  C CG  . GLN A 1 48  ? -2.69200  55.66600  22.21100 1.000 40.82289  ? 45  GLN A CG  1 
ATOM   350  C CD  . GLN A 1 48  ? -1.20600  55.97000  22.22900 1.000 49.33156  ? 45  GLN A CD  1 
ATOM   351  O OE1 . GLN A 1 48  ? -0.78000  57.06700  21.86400 1.000 50.31029  ? 45  GLN A OE1 1 
ATOM   352  N NE2 . GLN A 1 48  ? -0.40800  54.99600  22.65000 1.000 48.98726  ? 45  GLN A NE2 1 
ATOM   353  N N   . LEU A 1 49  ? -5.94800  58.60500  22.19100 1.000 37.71347  ? 46  LEU A N   1 
ATOM   354  C CA  . LEU A 1 49  ? -6.68900  59.85000  22.00800 1.000 38.53396  ? 46  LEU A CA  1 
ATOM   355  C C   . LEU A 1 49  ? -6.04000  60.73400  20.94900 1.000 40.47864  ? 46  LEU A C   1 
ATOM   356  O O   . LEU A 1 49  ? -6.73800  61.40900  20.18200 1.000 37.17100  ? 46  LEU A O   1 
ATOM   357  C CB  . LEU A 1 49  ? -6.80100  60.59400  23.33800 1.000 39.92576  ? 46  LEU A CB  1 
ATOM   358  C CG  . LEU A 1 49  ? -7.49700  61.95600  23.28300 1.000 38.19627  ? 46  LEU A CG  1 
ATOM   359  C CD1 . LEU A 1 49  ? -8.88800  61.82000  22.68800 1.000 37.18289  ? 46  LEU A CD1 1 
ATOM   360  C CD2 . LEU A 1 49  ? -7.56300  62.57700  24.66500 1.000 39.80678  ? 46  LEU A CD2 1 
ATOM   361  N N   . GLN A 1 50  ? -4.70500  60.72800  20.87600 1.000 42.39435  ? 47  GLN A N   1 
ATOM   362  C CA  . GLN A 1 50  ? -4.00600  61.51200  19.86300 1.000 47.43934  ? 47  GLN A CA  1 
ATOM   363  C C   . GLN A 1 50  ? -4.35800  61.07900  18.44400 1.000 46.69051  ? 47  GLN A C   1 
ATOM   364  O O   . GLN A 1 50  ? -4.13100  61.84500  17.50100 1.000 51.28375  ? 47  GLN A O   1 
ATOM   365  C CB  . GLN A 1 50  ? -2.49400  61.40700  20.06300 1.000 43.30440  ? 47  GLN A CB  1 
ATOM   366  C CG  . GLN A 1 50  ? -1.94700  60.01500  19.80800 1.000 52.89873  ? 47  GLN A CG  1 
ATOM   367  C CD  . GLN A 1 50  ? -0.44900  60.01000  19.60200 1.000 61.77933  ? 47  GLN A CD  1 
ATOM   368  O OE1 . GLN A 1 50  ? 0.16100   61.05700  19.38100 1.000 62.38832  ? 47  GLN A OE1 1 
ATOM   369  N NE2 . GLN A 1 50  ? 0.15600   58.82900  19.67700 1.000 64.42721  ? 47  GLN A NE2 1 
ATOM   370  N N   . ASP A 1 51  ? -4.98700  59.92800  18.27500 1.000 36.57221  ? 48  ASP A N   1 
ATOM   371  C CA  . ASP A 1 51  ? -5.27800  59.39100  16.92500 1.000 38.41921  ? 48  ASP A CA  1 
ATOM   372  C C   . ASP A 1 51  ? -6.65700  59.84000  16.43100 1.000 37.11305  ? 48  ASP A C   1 
ATOM   373  O O   . ASP A 1 51  ? -6.91400  59.68100  15.25200 1.000 37.37000  ? 48  ASP A O   1 
ATOM   374  C CB  . ASP A 1 51  ? -5.11200  57.86800  16.89600 1.000 36.04595  ? 48  ASP A CB  1 
ATOM   375  C CG  . ASP A 1 51  ? -3.72400  57.35800  17.20700 1.000 39.87775  ? 48  ASP A CG  1 
ATOM   376  O OD1 . ASP A 1 51  ? -2.76300  57.95600  16.71800 1.000 51.48774  ? 48  ASP A OD1 1 
ATOM   377  O OD2 . ASP A 1 51  ? -3.63000  56.35400  17.91500 1.000 38.13498  ? 48  ASP A OD2 1 
ATOM   378  N N   . LEU A 1 52  ? -7.47700  60.42200  17.30300 1.000 29.22908  ? 49  LEU A N   1 
ATOM   379  C CA  . LEU A 1 52  ? -8.82900  60.86900  16.90200 1.000 35.58475  ? 49  LEU A CA  1 
ATOM   380  C C   . LEU A 1 52  ? -8.75000  62.22500  16.21600 1.000 31.99432  ? 49  LEU A C   1 
ATOM   381  O O   . LEU A 1 52  ? -8.41100  63.19300  16.86500 1.000 36.01334  ? 49  LEU A O   1 
ATOM   382  C CB  . LEU A 1 52  ? -9.80400  60.85700  18.08100 1.000 30.85944  ? 49  LEU A CB  1 
ATOM   383  C CG  . LEU A 1 52  ? -11.26400 61.13000  17.74200 1.000 36.71906  ? 49  LEU A CG  1 
ATOM   384  C CD1 . LEU A 1 52  ? -11.78200 60.12200  16.73800 1.000 33.08674  ? 49  LEU A CD1 1 
ATOM   385  C CD2 . LEU A 1 52  ? -12.11000 61.10500  19.00000 1.000 37.77545  ? 49  LEU A CD2 1 
ATOM   386  N N   . ARG A 1 53  ? -9.02700  62.24600  14.92500 1.000 31.19592  ? 50  ARG A N   1 
ATOM   387  C CA  . ARG A 1 53  ? -8.95000  63.46200  14.09100 1.000 34.65949  ? 50  ARG A CA  1 
ATOM   388  C C   . ARG A 1 53  ? -10.11200 64.39300  14.38700 1.000 37.19731  ? 50  ARG A C   1 
ATOM   389  O O   . ARG A 1 53  ? -9.93700  65.59700  14.26100 1.000 35.94844  ? 50  ARG A O   1 
ATOM   390  C CB  . ARG A 1 53  ? -8.89800  63.00300  12.63700 1.000 31.48621  ? 50  ARG A CB  1 
ATOM   391  C CG  . ARG A 1 53  ? -7.80700  61.98800  12.34300 1.000 29.96459  ? 50  ARG A CG  1 
ATOM   392  C CD  . ARG A 1 53  ? -7.99400  61.32800  10.99300 1.000 30.12072  ? 50  ARG A CD  1 
ATOM   393  N NE  . ARG A 1 53  ? -8.19200  62.26100  9.89400  1.000 39.31226  ? 50  ARG A NE  1 
ATOM   394  C CZ  . ARG A 1 53  ? -7.22900  62.82600  9.17900  1.000 32.27227  ? 50  ARG A CZ  1 
ATOM   395  N NH1 . ARG A 1 53  ? -5.96100  62.56500  9.43300  1.000 31.57050  ? 50  ARG A NH1 1 
ATOM   396  N NH2 . ARG A 1 53  ? -7.53900  63.65400  8.20400  1.000 34.29117  ? 50  ARG A NH2 1 
ATOM   397  N N   . ASN A 1 54  ? -11.24000 63.83200  14.78100 1.000 35.36819  ? 51  ASN A N   1 
ATOM   398  C CA  . ASN A 1 54  ? -12.45700 64.63800  14.98700 1.000 37.79144  ? 51  ASN A CA  1 
ATOM   399  C C   . ASN A 1 54  ? -12.94300 64.48000  16.41800 1.000 41.18316  ? 51  ASN A C   1 
ATOM   400  O O   . ASN A 1 54  ? -14.01600 63.94500  16.61200 1.000 39.81838  ? 51  ASN A O   1 
ATOM   401  C CB  . ASN A 1 54  ? -13.57700 64.23500  14.02900 1.000 40.20992  ? 51  ASN A CB  1 
ATOM   402  C CG  . ASN A 1 54  ? -13.85700 62.75400  13.92100 1.000 42.03978  ? 51  ASN A CG  1 
ATOM   403  O OD1 . ASN A 1 54  ? -13.01800 61.92400  14.23500 1.000 38.38621  ? 51  ASN A OD1 1 
ATOM   404  N ND2 . ASN A 1 54  ? -15.04800 62.42400  13.46600 1.000 40.76769  ? 51  ASN A ND2 1 
ATOM   405  N N   . PRO A 1 55  ? -12.25400 65.05700  17.41400 1.000 43.77867  ? 52  PRO A N   1 
ATOM   406  C CA  . PRO A 1 55  ? -12.74800 64.96000  18.75500 1.000 42.75495  ? 52  PRO A CA  1 
ATOM   407  C C   . PRO A 1 55  ? -14.17600 65.51800  18.82100 1.000 49.82252  ? 52  PRO A C   1 
ATOM   408  O O   . PRO A 1 55  ? -14.44000 66.57800  18.33000 1.000 47.98458  ? 52  PRO A O   1 
ATOM   409  C CB  . PRO A 1 55  ? -11.67600 65.69700  19.55100 1.000 40.82709  ? 52  PRO A CB  1 
ATOM   410  C CG  . PRO A 1 55  ? -10.98000 66.57600  18.56400 1.000 48.90793  ? 52  PRO A CG  1 
ATOM   411  C CD  . PRO A 1 55  ? -10.99200 65.76800  17.29600 1.000 44.01783  ? 52  PRO A CD  1 
ATOM   412  N N   . PRO A 1 56  ? -15.11600 64.77700  19.42900 1.000 44.35154  ? 53  PRO A N   1 
ATOM   413  C CA  . PRO A 1 56  ? -16.49500 65.20700  19.49300 1.000 44.84590  ? 53  PRO A CA  1 
ATOM   414  C C   . PRO A 1 56  ? -16.82900 66.38600  20.41600 1.000 50.77492  ? 53  PRO A C   1 
ATOM   415  O O   . PRO A 1 56  ? -16.08900 66.66000  21.32400 1.000 47.88359  ? 53  PRO A O   1 
ATOM   416  C CB  . PRO A 1 56  ? -17.21100 63.96000  19.98900 1.000 47.24793  ? 53  PRO A CB  1 
ATOM   417  C CG  . PRO A 1 56  ? -16.18400 63.18400  20.73500 1.000 42.71677  ? 53  PRO A CG  1 
ATOM   418  C CD  . PRO A 1 56  ? -14.89100 63.46700  20.01400 1.000 42.59087  ? 53  PRO A CD  1 
ATOM   419  N N   . SER A 1 57  ? -17.92500 67.07800  20.12400 1.000 66.21504  ? 54  SER A N   1 
ATOM   420  C CA  . SER A 1 57  ? -18.37200 68.23000  20.94900 1.000 63.97583  ? 54  SER A CA  1 
ATOM   421  C C   . SER A 1 57  ? -18.98200 67.76300  22.26300 1.000 70.64749  ? 54  SER A C   1 
ATOM   422  O O   . SER A 1 57  ? -19.44000 66.62100  22.33900 1.000 68.27174  ? 54  SER A O   1 
ATOM   423  C CB  . SER A 1 57  ? -19.32700 69.10800  20.21500 1.000 61.35737  ? 54  SER A CB  1 
ATOM   424  O OG  . SER A 1 57  ? -19.61300 70.27300  20.96400 1.000 78.00256  ? 54  SER A OG  1 
ATOM   425  N N   . THR A 1 58  ? -18.98100 68.63800  23.26000 1.000 88.15314  ? 55  THR A N   1 
ATOM   426  C CA  . THR A 1 58  ? -19.58100 68.32000  24.57900 1.000 85.12579  ? 55  THR A CA  1 
ATOM   427  C C   . THR A 1 58  ? -21.07300 68.09500  24.37800 1.000 86.68723  ? 55  THR A C   1 
ATOM   428  O O   . THR A 1 58  ? -21.66200 67.35800  25.17000 1.000 95.88552  ? 55  THR A O   1 
ATOM   429  C CB  . THR A 1 58  ? -19.27400 69.44400  25.56400 1.000 84.06541  ? 55  THR A CB  1 
ATOM   430  O OG1 . THR A 1 58  ? -19.57000 70.67100  24.90100 1.000 94.15677  ? 55  THR A OG1 1 
ATOM   431  C CG2 . THR A 1 58  ? -17.82900 69.44200  26.01000 1.000 79.20694  ? 55  THR A CG2 1 
ATOM   432  N N   . VAL A 1 59  ? -21.65000 68.74500  23.37700 1.000 88.99816  ? 56  VAL A N   1 
ATOM   433  C CA  . VAL A 1 59  ? -23.11300 68.64900  23.12100 1.000 99.10854  ? 56  VAL A CA  1 
ATOM   434  C C   . VAL A 1 59  ? -23.39800 67.76900  21.90500 1.000 95.88413  ? 56  VAL A C   1 
ATOM   435  O O   . VAL A 1 59  ? -24.53600 67.80200  21.43100 1.000 104.20306 ? 56  VAL A O   1 
ATOM   436  C CB  . VAL A 1 59  ? -23.66700 70.06300  22.89100 1.000 99.65039  ? 56  VAL A CB  1 
ATOM   437  C CG1 . VAL A 1 59  ? -23.52400 70.92500  24.13500 1.000 92.40552  ? 56  VAL A CG1 1 
ATOM   438  C CG2 . VAL A 1 59  ? -23.00300 70.73800  21.70100 1.000 91.37625  ? 56  VAL A CG2 1 
ATOM   439  N N   . GLN A 1 60  ? -22.43400 66.99000  21.43400 1.000 84.83528  ? 57  GLN A N   1 
ATOM   440  C CA  . GLN A 1 60  ? -22.60900 66.24300  20.16400 1.000 81.55970  ? 57  GLN A CA  1 
ATOM   441  C C   . GLN A 1 60  ? -23.73500 65.22300  20.20200 1.000 85.06795  ? 57  GLN A C   1 
ATOM   442  O O   . GLN A 1 60  ? -23.90900 64.57000  21.22900 1.000 87.84416  ? 57  GLN A O   1 
ATOM   443  C CB  . GLN A 1 60  ? -21.33000 65.48200  19.81500 1.000 73.06337  ? 57  GLN A CB  1 
ATOM   444  C CG  . GLN A 1 60  ? -21.35100 64.78700  18.46500 1.000 70.92603  ? 57  GLN A CG  1 
ATOM   445  C CD  . GLN A 1 60  ? -20.82700 65.69400  17.38300 1.000 78.92936  ? 57  GLN A CD  1 
ATOM   446  O OE1 . GLN A 1 60  ? -19.84400 66.40400  17.56800 1.000 70.71155  ? 57  GLN A OE1 1 
ATOM   447  N NE2 . GLN A 1 60  ? -21.49200 65.68200  16.24100 1.000 77.30282  ? 57  GLN A NE2 1 
ATOM   448  N N   . ASP A 1 61  ? -24.48000 65.11500  19.10500 1.000 101.27976 ? 58  ASP A N   1 
ATOM   449  C CA  . ASP A 1 61  ? -25.45600 64.01300  18.99000 1.000 100.09628 ? 58  ASP A CA  1 
ATOM   450  C C   . ASP A 1 61  ? -24.65800 62.92000  18.30200 1.000 100.99258 ? 58  ASP A C   1 
ATOM   451  O O   . ASP A 1 61  ? -24.17900 63.15800  17.19400 1.000 100.72041 ? 58  ASP A O   1 
ATOM   452  C CB  . ASP A 1 61  ? -26.66500 64.40900  18.15400 1.000 106.05465 ? 58  ASP A CB  1 
ATOM   453  C CG  . ASP A 1 61  ? -27.70500 63.30900  18.04500 1.000 113.91168 ? 58  ASP A CG  1 
ATOM   454  O OD1 . ASP A 1 61  ? -27.67600 62.39100  18.88500 1.000 112.39123 ? 58  ASP A OD1 1 
ATOM   455  O OD2 . ASP A 1 61  ? -28.53400 63.38300  17.12000 1.000 116.43495 ? 58  ASP A OD2 1 
ATOM   456  N N   . PHE A 1 62  ? -24.52200 61.77300  18.94500 1.000 90.57959  ? 59  PHE A N   1 
ATOM   457  C CA  . PHE A 1 62  ? -23.63200 60.72900  18.39600 1.000 85.41624  ? 59  PHE A CA  1 
ATOM   458  C C   . PHE A 1 62  ? -24.35400 59.93100  17.31100 1.000 94.04831  ? 59  PHE A C   1 
ATOM   459  O O   . PHE A 1 62  ? -23.72100 59.10000  16.65800 1.000 92.02834  ? 59  PHE A O   1 
ATOM   460  C CB  . PHE A 1 62  ? -23.03300 59.92500  19.54600 1.000 83.88475  ? 59  PHE A CB  1 
ATOM   461  C CG  . PHE A 1 62  ? -21.99000 60.65500  20.35200 1.000 80.70999  ? 59  PHE A CG  1 
ATOM   462  C CD1 . PHE A 1 62  ? -22.35500 61.54100  21.35000 1.000 79.29979  ? 59  PHE A CD1 1 
ATOM   463  C CD2 . PHE A 1 62  ? -20.64300 60.45100  20.11600 1.000 77.72809  ? 59  PHE A CD2 1 
ATOM   464  C CE1 . PHE A 1 62  ? -21.39600 62.21500  22.08700 1.000 81.29770  ? 59  PHE A CE1 1 
ATOM   465  C CE2 . PHE A 1 62  ? -19.68600 61.12100  20.85800 1.000 76.97784  ? 59  PHE A CE2 1 
ATOM   466  C CZ  . PHE A 1 62  ? -20.06300 62.00100  21.84200 1.000 76.31625  ? 59  PHE A CZ  1 
ATOM   467  N N   . ASN A 1 63  ? -25.65500 60.15900  17.14600 1.000 109.98237 ? 60  ASN A N   1 
ATOM   468  C CA  . ASN A 1 63  ? -26.38400 59.48200  16.04900 1.000 111.20968 ? 60  ASN A CA  1 
ATOM   469  C C   . ASN A 1 63  ? -25.80800 59.97900  14.72900 1.000 110.22406 ? 60  ASN A C   1 
ATOM   470  O O   . ASN A 1 63  ? -25.57700 59.15800  13.83100 1.000 108.81783 ? 60  ASN A O   1 
ATOM   471  C CB  . ASN A 1 63  ? -27.88300 59.75800  16.14900 1.000 120.34667 ? 60  ASN A CB  1 
ATOM   472  C CG  . ASN A 1 63  ? -28.70200 58.87000  15.24000 1.000 127.03198 ? 60  ASN A CG  1 
ATOM   473  O OD1 . ASN A 1 63  ? -28.32300 57.73300  14.97000 1.000 126.74330 ? 60  ASN A OD1 1 
ATOM   474  N ND2 . ASN A 1 63  ? -29.82700 59.37900  14.76700 1.000 125.94749 ? 60  ASN A ND2 1 
ATOM   475  N N   . ASP A 1 64  ? -25.61800 61.28300  14.62200 1.000 131.04534 ? 61  ASP A N   1 
ATOM   476  C CA  . ASP A 1 64  ? -24.99300 61.87900  13.41900 1.000 135.85742 ? 61  ASP A CA  1 
ATOM   477  C C   . ASP A 1 64  ? -23.49200 61.58100  13.35500 1.000 130.52423 ? 61  ASP A C   1 
ATOM   478  O O   . ASP A 1 64  ? -22.98600 61.42100  12.23900 1.000 133.79079 ? 61  ASP A O   1 
ATOM   479  C CB  . ASP A 1 64  ? -25.23200 63.38800  13.41900 1.000 139.96650 ? 61  ASP A CB  1 
ATOM   480  C CG  . ASP A 1 64  ? -26.67000 63.78200  13.14100 1.000 153.53569 ? 61  ASP A CG  1 
ATOM   481  O OD1 . ASP A 1 64  ? -27.43000 62.91500  12.66800 1.000 156.05306 ? 61  ASP A OD1 1 
ATOM   482  O OD2 . ASP A 1 64  ? -27.01800 64.95100  13.40500 1.000 160.16399 ? 61  ASP A OD2 1 
ATOM   483  N N   . TYR A 1 65  ? -22.79900 61.52700  14.48800 1.000 79.66778  ? 62  TYR A N   1 
ATOM   484  C CA  . TYR A 1 65  ? -21.31500 61.43700  14.51200 1.000 70.80717  ? 62  TYR A CA  1 
ATOM   485  C C   . TYR A 1 65  ? -20.68600 60.12200  14.05200 1.000 62.72040  ? 62  TYR A C   1 
ATOM   486  O O   . TYR A 1 65  ? -21.28600 59.06800  14.24100 1.000 64.34350  ? 62  TYR A O   1 
ATOM   487  C CB  . TYR A 1 65  ? -20.83700 61.84600  15.91000 1.000 61.31291  ? 62  TYR A CB  1 
ATOM   488  C CG  . TYR A 1 65  ? -19.35900 61.88400  16.15800 1.000 53.24577  ? 62  TYR A CG  1 
ATOM   489  C CD1 . TYR A 1 65  ? -18.60400 63.00100  15.85600 1.000 52.02667  ? 62  TYR A CD1 1 
ATOM   490  C CD2 . TYR A 1 65  ? -18.73200 60.80600  16.74100 1.000 54.60376  ? 62  TYR A CD2 1 
ATOM   491  C CE1 . TYR A 1 65  ? -17.24300 63.03100  16.09800 1.000 49.77919  ? 62  TYR A CE1 1 
ATOM   492  C CE2 . TYR A 1 65  ? -17.37700 60.82000  16.98700 1.000 53.59509  ? 62  TYR A CE2 1 
ATOM   493  C CZ  . TYR A 1 65  ? -16.63100 61.93200  16.66700 1.000 51.49660  ? 62  TYR A CZ  1 
ATOM   494  O OH  . TYR A 1 65  ? -15.29900 61.89900  16.92700 1.000 53.56804  ? 62  TYR A OH  1 
ATOM   495  N N   . GLU A 1 66  ? -19.50000 60.21600  13.44600 1.000 61.12678  ? 63  GLU A N   1 
ATOM   496  C CA  . GLU A 1 66  ? -18.68600 59.03400  13.08700 1.000 52.95255  ? 63  GLU A CA  1 
ATOM   497  C C   . GLU A 1 66  ? -17.27900 59.35900  13.58100 1.000 51.69591  ? 63  GLU A C   1 
ATOM   498  O O   . GLU A 1 66  ? -16.90600 60.51200  13.50800 1.000 54.62707  ? 63  GLU A O   1 
ATOM   499  C CB  . GLU A 1 66  ? -18.63900 58.84100  11.57500 1.000 52.48147  ? 63  GLU A CB  1 
ATOM   500  C CG  . GLU A 1 66  ? -19.55300 57.75500  11.05900 1.000 66.19292  ? 63  GLU A CG  1 
ATOM   501  C CD  . GLU A 1 66  ? -19.77100 57.79600  9.55700  1.000 73.34156  ? 63  GLU A CD  1 
ATOM   502  O OE1 . GLU A 1 66  ? -18.89600 58.32100  8.85000  1.000 70.45032  ? 63  GLU A OE1 1 
ATOM   503  O OE2 . GLU A 1 66  ? -20.81800 57.30800  9.10300  1.000 84.16562  ? 63  GLU A OE2 1 
ATOM   504  N N   . TYR A 1 67  ? -16.53300 58.37400  14.04900 1.000 47.09075  ? 64  TYR A N   1 
ATOM   505  C CA  . TYR A 1 67  ? -15.18900 58.61000  14.61100 1.000 41.00063  ? 64  TYR A CA  1 
ATOM   506  C C   . TYR A 1 67  ? -14.14600 58.35400  13.53200 1.000 42.54627  ? 64  TYR A C   1 
ATOM   507  O O   . TYR A 1 67  ? -14.12500 57.27100  12.97100 1.000 46.14178  ? 64  TYR A O   1 
ATOM   508  C CB  . TYR A 1 67  ? -14.92600 57.66100  15.77800 1.000 41.63952  ? 64  TYR A CB  1 
ATOM   509  C CG  . TYR A 1 67  ? -15.68800 57.88300  17.05600 1.000 45.66513  ? 64  TYR A CG  1 
ATOM   510  C CD1 . TYR A 1 67  ? -16.93300 57.31600  17.24300 1.000 51.61241  ? 64  TYR A CD1 1 
ATOM   511  C CD2 . TYR A 1 67  ? -15.13900 58.60200  18.10100 1.000 43.84478  ? 64  TYR A CD2 1 
ATOM   512  C CE1 . TYR A 1 67  ? -17.63700 57.49800  18.41800 1.000 60.77847  ? 64  TYR A CE1 1 
ATOM   513  C CE2 . TYR A 1 67  ? -15.83000 58.79600  19.28400 1.000 50.69121  ? 64  TYR A CE2 1 
ATOM   514  C CZ  . TYR A 1 67  ? -17.08400 58.24000  19.44100 1.000 53.88430  ? 64  TYR A CZ  1 
ATOM   515  O OH  . TYR A 1 67  ? -17.78500 58.40500  20.59500 1.000 51.07261  ? 64  TYR A OH  1 
ATOM   516  N N   . SER A 1 68  ? -13.29600 59.33000  13.27900 1.000 40.57898  ? 65  SER A N   1 
ATOM   517  C CA  . SER A 1 68  ? -12.25100 59.19700  12.24800 1.000 44.00172  ? 65  SER A CA  1 
ATOM   518  C C   . SER A 1 68  ? -10.89000 59.10300  12.92500 1.000 40.26872  ? 65  SER A C   1 
ATOM   519  O O   . SER A 1 68  ? -10.46900 60.05000  13.57200 1.000 38.34890  ? 65  SER A O   1 
ATOM   520  C CB  . SER A 1 68  ? -12.32900 60.30000  11.23700 1.000 42.66315  ? 65  SER A CB  1 
ATOM   521  O OG  . SER A 1 68  ? -13.59100 60.32300  10.59800 1.000 54.96500  ? 65  SER A OG  1 
ATOM   522  N N   . PHE A 1 69  ? -10.20700 57.99800  12.70300 1.000 33.68739  ? 66  PHE A N   1 
ATOM   523  C CA  . PHE A 1 69  ? -8.96000  57.78700  13.44600 1.000 32.93425  ? 66  PHE A CA  1 
ATOM   524  C C   . PHE A 1 69  ? -7.76900  57.62200  12.53500 1.000 34.51918  ? 66  PHE A C   1 
ATOM   525  O O   . PHE A 1 69  ? -7.88800  57.04500  11.47200 1.000 35.20954  ? 66  PHE A O   1 
ATOM   526  C CB  . PHE A 1 69  ? -9.04600  56.49500  14.25500 1.000 35.28086  ? 66  PHE A CB  1 
ATOM   527  C CG  . PHE A 1 69  ? -9.84000  56.50600  15.53400 1.000 33.33756  ? 66  PHE A CG  1 
ATOM   528  C CD1 . PHE A 1 69  ? -9.31500  57.04600  16.69300 1.000 31.98521  ? 66  PHE A CD1 1 
ATOM   529  C CD2 . PHE A 1 69  ? -11.08900 55.91400  15.59300 1.000 34.11469  ? 66  PHE A CD2 1 
ATOM   530  C CE1 . PHE A 1 69  ? -10.03700 57.02300  17.87400 1.000 40.01012  ? 66  PHE A CE1 1 
ATOM   531  C CE2 . PHE A 1 69  ? -11.80900 55.89200  16.77400 1.000 42.39500  ? 66  PHE A CE2 1 
ATOM   532  C CZ  . PHE A 1 69  ? -11.28300 56.44800  17.91300 1.000 38.34729  ? 66  PHE A CZ  1 
ATOM   533  N N   . ASN A 1 70  ? -6.64700  58.16100  12.95900 1.000 35.70066  ? 67  ASN A N   1 
ATOM   534  C CA  . ASN A 1 70  ? -5.39600  57.91500  12.25500 1.000 36.75134  ? 67  ASN A CA  1 
ATOM   535  C C   . ASN A 1 70  ? -4.98100  56.46300  12.46400 1.000 39.04592  ? 67  ASN A C   1 
ATOM   536  O O   . ASN A 1 70  ? -4.74100  56.03100  13.59800 1.000 35.79400  ? 67  ASN A O   1 
ATOM   537  C CB  . ASN A 1 70  ? -4.30900  58.86500  12.74700 1.000 33.22359  ? 67  ASN A CB  1 
ATOM   538  C CG  . ASN A 1 70  ? -4.47400  60.27000  12.20200 1.000 36.44750  ? 67  ASN A CG  1 
ATOM   539  O OD1 . ASN A 1 70  ? -4.97000  60.46200  11.09000 1.000 37.19882  ? 67  ASN A OD1 1 
ATOM   540  N ND2 . ASN A 1 70  ? -4.05500  61.26000  12.98100 1.000 34.21970  ? 67  ASN A ND2 1 
ATOM   541  N N   . PHE A 1 71  ? -4.90700  55.71000  11.37200 1.000 33.37483  ? 68  PHE A N   1 
ATOM   542  C CA  . PHE A 1 71  ? -4.62600  54.28200  11.41000 1.000 34.43911  ? 68  PHE A CA  1 
ATOM   543  C C   . PHE A 1 71  ? -3.22100  53.93800  10.94800 1.000 38.13977  ? 68  PHE A C   1 
ATOM   544  O O   . PHE A 1 71  ? -2.58800  53.04400  11.51600 1.000 38.82819  ? 68  PHE A O   1 
ATOM   545  C CB  . PHE A 1 71  ? -5.64900  53.53700  10.54600 1.000 31.12886  ? 68  PHE A CB  1 
ATOM   546  C CG  . PHE A 1 71  ? -5.50800  52.04600  10.58000 1.000 34.32405  ? 68  PHE A CG  1 
ATOM   547  C CD1 . PHE A 1 71  ? -5.89900  51.32500  11.69600 1.000 36.88858  ? 68  PHE A CD1 1 
ATOM   548  C CD2 . PHE A 1 71  ? -5.00400  51.36000  9.48500  1.000 35.50597  ? 68  PHE A CD2 1 
ATOM   549  C CE1 . PHE A 1 71  ? -5.77500  49.94700  11.72800 1.000 35.26559  ? 68  PHE A CE1 1 
ATOM   550  C CE2 . PHE A 1 71  ? -4.88100  49.98000  9.51000  1.000 37.61904  ? 68  PHE A CE2 1 
ATOM   551  C CZ  . PHE A 1 71  ? -5.26700  49.27300  10.63500 1.000 34.10529  ? 68  PHE A CZ  1 
ATOM   552  N N   . GLY A 1 72  ? -2.74600  54.65200  9.92800  1.000 43.47219  ? 69  GLY A N   1 
ATOM   553  C CA  . GLY A 1 72  ? -1.39900  54.38900  9.39300  1.000 41.04701  ? 69  GLY A CA  1 
ATOM   554  C C   . GLY A 1 72  ? -0.87100  55.56100  8.59400  1.000 44.63232  ? 69  GLY A C   1 
ATOM   555  O O   . GLY A 1 72  ? -1.58100  56.57800  8.49700  1.000 45.11212  ? 69  GLY A O   1 
ATOM   556  N N   . THR A 1 73  ? 0.34000   55.42600  8.05500  1.000 44.19959  ? 70  THR A N   1 
ATOM   557  C CA  . THR A 1 73  ? 0.94700   56.50400  7.23500  1.000 48.25409  ? 70  THR A CA  1 
ATOM   558  C C   . THR A 1 73  ? 1.28300   55.93700  5.85300  1.000 46.78337  ? 70  THR A C   1 
ATOM   559  O O   . THR A 1 73  ? 1.85300   54.83400  5.79300  1.000 46.18967  ? 70  THR A O   1 
ATOM   560  C CB  . THR A 1 73  ? 2.18200   57.09000  7.92700  1.000 47.62435  ? 70  THR A CB  1 
ATOM   561  O OG1 . THR A 1 73  ? 3.11600   56.02900  8.12500  1.000 66.02864  ? 70  THR A OG1 1 
ATOM   562  C CG2 . THR A 1 73  ? 1.85700   57.74100  9.25400  1.000 54.22309  ? 70  THR A CG2 1 
ATOM   563  N N   . LEU A 1 74  ? 0.94000   56.67000  4.79300  1.000 48.35471  ? 71  LEU A N   1 
ATOM   564  C CA  . LEU A 1 74  ? 1.26400   56.21200  3.42000  1.000 55.51689  ? 71  LEU A CA  1 
ATOM   565  C C   . LEU A 1 74  ? 2.64900   56.73800  3.04300  1.000 56.90251  ? 71  LEU A C   1 
ATOM   566  O O   . LEU A 1 74  ? 2.77000   57.94600  2.77600  1.000 61.71785  ? 71  LEU A O   1 
ATOM   567  C CB  . LEU A 1 74  ? 0.19700   56.74500  2.46100  1.000 46.89658  ? 71  LEU A CB  1 
ATOM   568  C CG  . LEU A 1 74  ? 0.11000   56.03600  1.11200  1.000 64.89882  ? 71  LEU A CG  1 
ATOM   569  C CD1 . LEU A 1 74  ? 0.50300   54.57400  1.24600  1.000 65.06004  ? 71  LEU A CD1 1 
ATOM   570  C CD2 . LEU A 1 74  ? -1.28900  56.16200  0.53200  1.000 66.41226  ? 71  LEU A CD2 1 
ATOM   571  N N   . ASN A 1 75  ? 3.64900   55.85600  3.02300  1.000 62.69264  ? 72  ASN A N   1 
ATOM   572  C CA  . ASN A 1 75  ? 5.02100   56.25100  2.61200  1.000 66.54338  ? 72  ASN A CA  1 
ATOM   573  C C   . ASN A 1 75  ? 5.41500   55.35300  1.44200  1.000 73.84900  ? 72  ASN A C   1 
ATOM   574  O O   . ASN A 1 75  ? 5.25000   54.12600  1.57600  1.000 69.56646  ? 72  ASN A O   1 
ATOM   575  C CB  . ASN A 1 75  ? 6.01700   56.14400  3.76800  1.000 75.92472  ? 72  ASN A CB  1 
ATOM   576  C CG  . ASN A 1 75  ? 7.44400   56.41600  3.34200  1.000 83.57261  ? 72  ASN A CG  1 
ATOM   577  O OD1 . ASN A 1 75  ? 7.75500   57.49800  2.85000  1.000 86.58220  ? 72  ASN A OD1 1 
ATOM   578  N ND2 . ASN A 1 75  ? 8.31800   55.43900  3.52300  1.000 81.75196  ? 72  ASN A ND2 1 
ATOM   579  N N   . ASN A 1 76  ? 5.89900   55.94000  0.34500  1.000 96.52799  ? 73  ASN A N   1 
ATOM   580  C CA  . ASN A 1 76  ? 6.20200   55.12700  -0.86200 1.000 98.77308  ? 73  ASN A CA  1 
ATOM   581  C C   . ASN A 1 76  ? 4.91300   54.40800  -1.27200 1.000 93.26346  ? 73  ASN A C   1 
ATOM   582  O O   . ASN A 1 76  ? 3.88000   55.08900  -1.42300 1.000 92.48649  ? 73  ASN A O   1 
ATOM   583  C CB  . ASN A 1 76  ? 7.38100   54.17300  -0.64500 1.000 103.02083 ? 73  ASN A CB  1 
ATOM   584  C CG  . ASN A 1 76  ? 8.71200   54.88800  -0.55600 1.000 111.60527 ? 73  ASN A CG  1 
ATOM   585  O OD1 . ASN A 1 76  ? 8.85900   56.00200  -1.05400 1.000 111.88671 ? 73  ASN A OD1 1 
ATOM   586  N ND2 . ASN A 1 76  ? 9.68800   54.25600  0.07600  1.000 114.22059 ? 73  ASN A ND2 1 
ATOM   587  N N   . GLU A 1 77  ? 4.98000   53.08900  -1.45200 1.000 74.37602  ? 74  GLU A N   1 
ATOM   588  C CA  . GLU A 1 77  ? 3.78700   52.30300  -1.85900 1.000 74.44634  ? 74  GLU A CA  1 
ATOM   589  C C   . GLU A 1 77  ? 3.28300   51.46100  -0.68200 1.000 70.62202  ? 74  GLU A C   1 
ATOM   590  O O   . GLU A 1 77  ? 2.48700   50.54300  -0.92800 1.000 64.99771  ? 74  GLU A O   1 
ATOM   591  C CB  . GLU A 1 77  ? 4.14200   51.42400  -3.05700 1.000 80.94131  ? 74  GLU A CB  1 
ATOM   592  C CG  . GLU A 1 77  ? 3.87400   52.08500  -4.39500 1.000 84.73455  ? 74  GLU A CG  1 
ATOM   593  C CD  . GLU A 1 77  ? 4.36200   51.27900  -5.58600 1.000 90.60586  ? 74  GLU A CD  1 
ATOM   594  O OE1 . GLU A 1 77  ? 5.34400   50.52800  -5.42400 1.000 88.10973  ? 74  GLU A OE1 1 
ATOM   595  O OE2 . GLU A 1 77  ? 3.75700   51.40000  -6.66900 1.000 101.97006 ? 74  GLU A OE2 1 
ATOM   596  N N   . TYR A 1 78  ? 3.73600   51.74600  0.54100  1.000 66.52525  ? 75  TYR A N   1 
ATOM   597  C CA  . TYR A 1 78  ? 3.36600   50.88000  1.69300  1.000 59.03683  ? 75  TYR A CA  1 
ATOM   598  C C   . TYR A 1 78  ? 2.60700   51.64700  2.77800  1.000 58.62451  ? 75  TYR A C   1 
ATOM   599  O O   . TYR A 1 78  ? 3.02200   52.76700  3.12500  1.000 55.68522  ? 75  TYR A O   1 
ATOM   600  C CB  . TYR A 1 78  ? 4.61600   50.25400  2.31100  1.000 56.23004  ? 75  TYR A CB  1 
ATOM   601  C CG  . TYR A 1 78  ? 5.20200   49.10900  1.52700  1.000 59.63678  ? 75  TYR A CG  1 
ATOM   602  C CD1 . TYR A 1 78  ? 4.75100   47.81400  1.71200  1.000 56.29879  ? 75  TYR A CD1 1 
ATOM   603  C CD2 . TYR A 1 78  ? 6.21200   49.32200  0.60500  1.000 62.01588  ? 75  TYR A CD2 1 
ATOM   604  C CE1 . TYR A 1 78  ? 5.28600   46.75800  0.99600  1.000 57.95324  ? 75  TYR A CE1 1 
ATOM   605  C CE2 . TYR A 1 78  ? 6.75800   48.27700  -0.11900 1.000 61.43636  ? 75  TYR A CE2 1 
ATOM   606  C CZ  . TYR A 1 78  ? 6.29500   46.99000  0.07900  1.000 58.42958  ? 75  TYR A CZ  1 
ATOM   607  O OH  . TYR A 1 78  ? 6.83500   45.95700  -0.62700 1.000 63.68022  ? 75  TYR A OH  1 
ATOM   608  N N   . ILE A 1 79  ? 1.52800   51.05500  3.29700  1.000 47.87408  ? 76  ILE A N   1 
ATOM   609  C CA  . ILE A 1 79  ? 0.78200   51.67100  4.43300  1.000 45.11439  ? 76  ILE A CA  1 
ATOM   610  C C   . ILE A 1 79  ? 1.42600   51.15600  5.72500  1.000 45.29868  ? 76  ILE A C   1 
ATOM   611  O O   . ILE A 1 79  ? 1.32600   49.94400  5.98700  1.000 46.67818  ? 76  ILE A O   1 
ATOM   612  C CB  . ILE A 1 79  ? -0.71400  51.30500  4.36100  1.000 45.06179  ? 76  ILE A CB  1 
ATOM   613  C CG1 . ILE A 1 79  ? -1.41100  51.98400  3.18000  1.000 40.81616  ? 76  ILE A CG1 1 
ATOM   614  C CG2 . ILE A 1 79  ? -1.41500  51.60100  5.67900  1.000 45.69347  ? 76  ILE A CG2 1 
ATOM   615  C CD1 . ILE A 1 79  ? -1.94500  51.02000  2.15000  1.000 46.05875  ? 76  ILE A CD1 1 
ATOM   616  N N   . THR A 1 80  ? 2.08100   52.03600  6.48400  1.000 44.09729  ? 77  THR A N   1 
ATOM   617  C CA  . THR A 1 80  ? 2.75900   51.62600  7.73300  1.000 44.70873  ? 77  THR A CA  1 
ATOM   618  C C   . THR A 1 80  ? 1.78300   51.76500  8.89700  1.000 45.09740  ? 77  THR A C   1 
ATOM   619  O O   . THR A 1 80  ? 1.45300   52.89300  9.24800  1.000 46.54473  ? 77  THR A O   1 
ATOM   620  C CB  . THR A 1 80  ? 4.07800   52.37500  7.95200  1.000 46.23575  ? 77  THR A CB  1 
ATOM   621  O OG1 . THR A 1 80  ? 4.90100   52.17000  6.80500  1.000 52.75957  ? 77  THR A OG1 1 
ATOM   622  C CG2 . THR A 1 80  ? 4.80900   51.92900  9.19800  1.000 47.89776  ? 77  THR A CG2 1 
ATOM   623  N N   . VAL A 1 81  ? 1.35300   50.63800  9.45900  1.000 38.63564  ? 78  VAL A N   1 
ATOM   624  C CA  . VAL A 1 81  ? 0.45000   50.66100  10.63700 1.000 39.03638  ? 78  VAL A CA  1 
ATOM   625  C C   . VAL A 1 81  ? 1.31100   50.61500  11.91300 1.000 36.32047  ? 78  VAL A C   1 
ATOM   626  O O   . VAL A 1 81  ? 2.09000   49.67000  12.01700 1.000 40.95491  ? 78  VAL A O   1 
ATOM   627  C CB  . VAL A 1 81  ? -0.60400  49.54400  10.58400 1.000 37.79564  ? 78  VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 81  ? -1.62100  49.66800  11.70300 1.000 37.78908  ? 78  VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 81  ? -1.29000  49.48600  9.23100  1.000 32.12950  ? 78  VAL A CG2 1 
ATOM   630  N N   . PRO A 1 82  ? 1.25300   51.57900  12.87600 1.000 51.99240  ? 79  PRO A N   1 
ATOM   631  C CA  . PRO A 1 82  ? 2.02500   51.45500  14.11900 1.000 50.27981  ? 79  PRO A CA  1 
ATOM   632  C C   . PRO A 1 82  ? 1.64000   50.19400  14.87500 1.000 54.18381  ? 79  PRO A C   1 
ATOM   633  O O   . PRO A 1 82  ? 0.47000   49.80500  14.91800 1.000 49.18214  ? 79  PRO A O   1 
ATOM   634  C CB  . PRO A 1 82  ? 1.64800   52.71700  14.90200 1.000 46.96602  ? 79  PRO A CB  1 
ATOM   635  C CG  . PRO A 1 82  ? 1.16100   53.67600  13.86900 1.000 52.10084  ? 79  PRO A CG  1 
ATOM   636  C CD  . PRO A 1 82  ? 0.49800   52.84000  12.81700 1.000 49.02209  ? 79  PRO A CD  1 
ATOM   637  N N   . GLY A 1 83  ? 2.64700   49.55100  15.47100 1.000 41.52709  ? 80  GLY A N   1 
ATOM   638  C CA  . GLY A 1 83  ? 2.40100   48.30000  16.17300 1.000 40.97689  ? 80  GLY A CA  1 
ATOM   639  C C   . GLY A 1 83  ? 1.40400   48.43800  17.30600 1.000 38.85399  ? 80  GLY A C   1 
ATOM   640  O O   . GLY A 1 83  ? 0.65400   47.50500  17.60400 1.000 38.20324  ? 80  GLY A O   1 
ATOM   641  N N   . ARG A 1 84  ? 1.38000   49.60700  17.95300 1.000 45.54522  ? 81  ARG A N   1 
ATOM   642  C CA  . ARG A 1 84  ? 0.45800   49.82500  19.06300 1.000 46.11373  ? 81  ARG A CA  1 
ATOM   643  C C   . ARG A 1 84  ? -0.99900  49.75500  18.61600 1.000 47.01774  ? 81  ARG A C   1 
ATOM   644  O O   . ARG A 1 84  ? -1.87500  49.39200  19.41200 1.000 48.26687  ? 81  ARG A O   1 
ATOM   645  C CB  . ARG A 1 84  ? 0.74800   51.17200  19.72500 1.000 44.67478  ? 81  ARG A CB  1 
ATOM   646  C CG  . ARG A 1 84  ? 0.75300   52.34700  18.75900 1.000 45.58528  ? 81  ARG A CG  1 
ATOM   647  C CD  . ARG A 1 84  ? 1.00200   53.65100  19.49000 1.000 45.72030  ? 81  ARG A CD  1 
ATOM   648  N NE  . ARG A 1 84  ? 0.79200   54.80200  18.62100 1.000 48.02572  ? 81  ARG A NE  1 
ATOM   649  C CZ  . ARG A 1 84  ? -0.39800  55.31600  18.34100 1.000 50.78651  ? 81  ARG A CZ  1 
ATOM   650  N NH1 . ARG A 1 84  ? -1.50800  54.80300  18.84800 1.000 43.19930  ? 81  ARG A NH1 1 
ATOM   651  N NH2 . ARG A 1 84  ? -0.47700  56.36700  17.52800 1.000 49.66049  ? 81  ARG A NH2 1 
ATOM   652  N N   . ILE A 1 85  ? -1.28000  50.09200  17.35300 1.000 42.84211  ? 82  ILE A N   1 
ATOM   653  C CA  . ILE A 1 85  ? -2.64100  49.97700  16.83300 1.000 42.88873  ? 82  ILE A CA  1 
ATOM   654  C C   . ILE A 1 85  ? -3.11900  48.52900  16.88100 1.000 44.06609  ? 82  ILE A C   1 
ATOM   655  O O   . ILE A 1 85  ? -4.32200  48.26600  17.01100 1.000 44.51994  ? 82  ILE A O   1 
ATOM   656  C CB  . ILE A 1 85  ? -2.71600  50.54500  15.40100 1.000 41.52295  ? 82  ILE A CB  1 
ATOM   657  C CG1 . ILE A 1 85  ? -2.08500  51.94000  15.33500 1.000 43.49466  ? 82  ILE A CG1 1 
ATOM   658  C CG2 . ILE A 1 85  ? -4.15800  50.59900  14.91900 1.000 41.23469  ? 82  ILE A CG2 1 
ATOM   659  C CD1 . ILE A 1 85  ? -2.98900  53.05400  15.81100 1.000 37.26138  ? 82  ILE A CD1 1 
ATOM   660  N N   . LEU A 1 86  ? -2.19500  47.57000  16.78700 1.000 43.88787  ? 83  LEU A N   1 
ATOM   661  C CA  . LEU A 1 86  ? -2.52600  46.15000  16.76700 1.000 42.42779  ? 83  LEU A CA  1 
ATOM   662  C C   . LEU A 1 86  ? -2.03200  45.40700  18.00400 1.000 45.03292  ? 83  LEU A C   1 
ATOM   663  O O   . LEU A 1 86  ? -2.07400  44.17200  18.02700 1.000 44.88573  ? 83  LEU A O   1 
ATOM   664  C CB  . LEU A 1 86  ? -1.95800  45.49800  15.50500 1.000 38.66601  ? 83  LEU A CB  1 
ATOM   665  C CG  . LEU A 1 86  ? -2.50500  46.02900  14.18000 1.000 37.05119  ? 83  LEU A CG  1 
ATOM   666  C CD1 . LEU A 1 86  ? -1.75500  45.42100  13.00900 1.000 38.91607  ? 83  LEU A CD1 1 
ATOM   667  C CD2 . LEU A 1 86  ? -3.99500  45.74900  14.07000 1.000 36.77239  ? 83  LEU A CD2 1 
ATOM   668  N N   . SER A 1 87  ? -1.56100  46.12800  19.02600 1.000 51.65895  ? 84  SER A N   1 
ATOM   669  C CA  . SER A 1 87  ? -1.10900  45.53300  20.28900 1.000 56.82248  ? 84  SER A CA  1 
ATOM   670  C C   . SER A 1 87  ? 0.07300   44.58700  20.08100 1.000 60.59080  ? 84  SER A C   1 
ATOM   671  O O   . SER A 1 87  ? 0.17700   43.54200  20.72900 1.000 56.36300  ? 84  SER A O   1 
ATOM   672  C CB  . SER A 1 87  ? -2.25400  44.81500  21.01200 1.000 47.76817  ? 84  SER A CB  1 
ATOM   673  O OG  . SER A 1 87  ? -3.23800  45.73400  21.45300 1.000 69.42149  ? 84  SER A OG  1 
ATOM   674  N N   . ILE A 1 88  ? 0.97700   44.95500  19.17200 1.000 49.88435  ? 85  ILE A N   1 
ATOM   675  C CA  . ILE A 1 88  ? 2.19000   44.19200  18.91000 1.000 49.94894  ? 85  ILE A CA  1 
ATOM   676  C C   . ILE A 1 88  ? 3.37900   45.14400  18.95400 1.000 52.26044  ? 85  ILE A C   1 
ATOM   677  O O   . ILE A 1 88  ? 3.22800   46.36500  18.94900 1.000 50.41751  ? 85  ILE A O   1 
ATOM   678  C CB  . ILE A 1 88  ? 2.14000   43.44400  17.56000 1.000 47.16290  ? 85  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 88  ? 2.07500   44.43600  16.39700 1.000 46.22412  ? 85  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 88  ? 0.95000   42.49400  17.51900 1.000 39.58040  ? 85  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 88  ? 2.17600   43.78700  15.03600 1.000 42.66591  ? 85  ILE A CD1 1 
ATOM   682  N N   . ASN A 1 89  ? 4.57600   44.56600  19.00000 1.000 77.31315  ? 86  ASN A N   1 
ATOM   683  C CA  . ASN A 1 89  ? 5.80400   45.39100  19.11400 1.000 82.47101  ? 86  ASN A CA  1 
ATOM   684  C C   . ASN A 1 89  ? 6.25300   45.83000  17.72100 1.000 84.34309  ? 86  ASN A C   1 
ATOM   685  O O   . ASN A 1 89  ? 6.59100   47.01100  17.55600 1.000 90.35041  ? 86  ASN A O   1 
ATOM   686  C CB  . ASN A 1 89  ? 6.88100   44.66900  19.92600 1.000 87.55975  ? 86  ASN A CB  1 
ATOM   687  C CG  . ASN A 1 89  ? 7.33700   43.35700  19.32700 1.000 93.46074  ? 86  ASN A CG  1 
ATOM   688  O OD1 . ASN A 1 89  ? 6.62600   42.36100  19.39500 1.000 83.89409  ? 86  ASN A OD1 1 
ATOM   689  N ND2 . ASN A 1 89  ? 8.52800   43.34200  18.75200 1.000 99.93052  ? 86  ASN A ND2 1 
ATOM   690  N N   . ARG A 1 90  ? 6.20400   44.92800  16.74800 1.000 67.91765  ? 87  ARG A N   1 
ATOM   691  C CA  . ARG A 1 90  ? 6.64700   45.24800  15.37400 1.000 64.36492  ? 87  ARG A CA  1 
ATOM   692  C C   . ARG A 1 90  ? 5.63100   46.16100  14.69400 1.000 63.37828  ? 87  ARG A C   1 
ATOM   693  O O   . ARG A 1 90  ? 4.49900   46.19800  15.14500 1.000 61.52729  ? 87  ARG A O   1 
ATOM   694  C CB  . ARG A 1 90  ? 6.70300   43.95200  14.56600 1.000 59.75148  ? 87  ARG A CB  1 
ATOM   695  C CG  . ARG A 1 90  ? 7.63100   42.89500  15.13700 1.000 76.29384  ? 87  ARG A CG  1 
ATOM   696  C CD  . ARG A 1 90  ? 7.16600   41.51400  14.72300 1.000 69.19255  ? 87  ARG A CD  1 
ATOM   697  N NE  . ARG A 1 90  ? 7.97900   40.44900  15.28600 1.000 67.93421  ? 87  ARG A NE  1 
ATOM   698  C CZ  . ARG A 1 90  ? 7.84000   39.97700  16.51700 1.000 77.26024  ? 87  ARG A CZ  1 
ATOM   699  N NH1 . ARG A 1 90  ? 6.91800   40.47300  17.32000 1.000 83.42162  ? 87  ARG A NH1 1 
ATOM   700  N NH2 . ARG A 1 90  ? 8.61500   38.99700  16.94300 1.000 83.52937  ? 87  ARG A NH2 1 
ATOM   701  N N   . ASP A 1 91  ? 6.02800   46.83600  13.62100 1.000 53.57212  ? 88  ASP A N   1 
ATOM   702  C CA  . ASP A 1 91  ? 5.07400   47.64900  12.82900 1.000 50.72455  ? 88  ASP A CA  1 
ATOM   703  C C   . ASP A 1 91  ? 4.53800   46.74800  11.71100 1.000 48.14806  ? 88  ASP A C   1 
ATOM   704  O O   . ASP A 1 91  ? 5.08000   45.66100  11.53200 1.000 49.99983  ? 88  ASP A O   1 
ATOM   705  C CB  . ASP A 1 91  ? 5.74900   48.92100  12.31200 1.000 54.72559  ? 88  ASP A CB  1 
ATOM   706  C CG  . ASP A 1 91  ? 5.79600   50.05700  13.31300 1.000 56.69602  ? 88  ASP A CG  1 
ATOM   707  O OD1 . ASP A 1 91  ? 5.35100   49.85200  14.45200 1.000 63.44982  ? 88  ASP A OD1 1 
ATOM   708  O OD2 . ASP A 1 91  ? 6.28000   51.13700  12.94000 1.000 58.00397  ? 88  ASP A OD2 1 
ATOM   709  N N   . VAL A 1 92  ? 3.47600   47.16200  11.02700 1.000 45.44728  ? 89  VAL A N   1 
ATOM   710  C CA  . VAL A 1 92  ? 2.87700   46.33600  9.94400  1.000 45.71037  ? 89  VAL A CA  1 
ATOM   711  C C   . VAL A 1 92  ? 2.81300   47.16700  8.66300  1.000 53.64222  ? 89  VAL A C   1 
ATOM   712  O O   . VAL A 1 92  ? 2.28500   48.27500  8.71000  1.000 49.90423  ? 89  VAL A O   1 
ATOM   713  C CB  . VAL A 1 92  ? 1.51400   45.73800  10.33700 1.000 44.51714  ? 89  VAL A CB  1 
ATOM   714  C CG1 . VAL A 1 92  ? 0.76300   45.18300  9.14100  1.000 42.97229  ? 89  VAL A CG1 1 
ATOM   715  C CG2 . VAL A 1 92  ? 1.66000   44.65800  11.39400 1.000 47.62324  ? 89  VAL A CG2 1 
ATOM   716  N N   . LEU A 1 93  ? 3.37000   46.64500  7.57400  1.000 41.35756  ? 90  LEU A N   1 
ATOM   717  C CA  . LEU A 1 93  ? 3.40500   47.38200  6.29400  1.000 45.13785  ? 90  LEU A CA  1 
ATOM   718  C C   . LEU A 1 93  ? 2.53000   46.65000  5.28300  1.000 44.98190  ? 90  LEU A C   1 
ATOM   719  O O   . LEU A 1 93  ? 2.83200   45.51000  4.96700  1.000 44.83252  ? 90  LEU A O   1 
ATOM   720  C CB  . LEU A 1 93  ? 4.85000   47.49800  5.80600  1.000 45.28606  ? 90  LEU A CB  1 
ATOM   721  C CG  . LEU A 1 93  ? 5.62000   48.74200  6.24100  1.000 49.99193  ? 90  LEU A CG  1 
ATOM   722  C CD1 . LEU A 1 93  ? 6.14400   48.59600  7.66000  1.000 41.92700  ? 90  LEU A CD1 1 
ATOM   723  C CD2 . LEU A 1 93  ? 6.77000   49.00800  5.28600  1.000 44.26111  ? 90  LEU A CD2 1 
ATOM   724  N N   . ILE A 1 94  ? 1.47200   47.30300  4.82300  1.000 40.48096  ? 91  ILE A N   1 
ATOM   725  C CA  . ILE A 1 94  ? 0.57000   46.70800  3.80800  1.000 37.19885  ? 91  ILE A CA  1 
ATOM   726  C C   . ILE A 1 94  ? 0.75400   47.49900  2.52500  1.000 41.57090  ? 91  ILE A C   1 
ATOM   727  O O   . ILE A 1 94  ? 0.55700   48.69700  2.54500  1.000 41.72809  ? 91  ILE A O   1 
ATOM   728  C CB  . ILE A 1 94  ? -0.89500  46.74000  4.27600  1.000 41.25166  ? 91  ILE A CB  1 
ATOM   729  C CG1 . ILE A 1 94  ? -1.03400  46.37800  5.75500  1.000 38.29299  ? 91  ILE A CG1 1 
ATOM   730  C CG2 . ILE A 1 94  ? -1.76300  45.85400  3.40200  1.000 39.25580  ? 91  ILE A CG2 1 
ATOM   731  C CD1 . ILE A 1 94  ? -1.18500  44.90100  5.99500  1.000 39.96197  ? 91  ILE A CD1 1 
ATOM   732  N N   . HIS A 1 95  ? 1.09800   46.82000  1.44600  1.000 46.86268  ? 92  HIS A N   1 
ATOM   733  C CA  . HIS A 1 95  ? 1.25700   47.47300  0.15600  1.000 46.22060  ? 92  HIS A CA  1 
ATOM   734  C C   . HIS A 1 95  ? -0.08800  47.99500  -0.34000 1.000 48.19256  ? 92  HIS A C   1 
ATOM   735  O O   . HIS A 1 95  ? -1.14300  47.42200  -0.05700 1.000 50.73872  ? 92  HIS A O   1 
ATOM   736  C CB  . HIS A 1 95  ? 1.86100   46.51100  -0.86500 1.000 47.64680  ? 92  HIS A CB  1 
ATOM   737  C CG  . HIS A 1 95  ? 2.33600   47.18500  -2.11300 1.000 51.37098  ? 92  HIS A CG  1 
ATOM   738  N ND1 . HIS A 1 95  ? 1.64200   47.12600  -3.30200 1.000 46.20729  ? 92  HIS A ND1 1 
ATOM   739  C CD2 . HIS A 1 95  ? 3.42800   47.94900  -2.35100 1.000 49.78611  ? 92  HIS A CD2 1 
ATOM   740  C CE1 . HIS A 1 95  ? 2.29100   47.81800  -4.22200 1.000 50.72375  ? 92  HIS A CE1 1 
ATOM   741  N NE2 . HIS A 1 95  ? 3.37800   48.32700  -3.67100 1.000 55.74247  ? 92  HIS A NE2 1 
ATOM   742  N N   . LYS A 1 96  ? -0.04000  49.10200  -1.08600 1.000 57.09722  ? 93  LYS A N   1 
ATOM   743  C CA  . LYS A 1 96  ? -1.26300  49.73800  -1.56900 1.000 61.47137  ? 93  LYS A CA  1 
ATOM   744  C C   . LYS A 1 96  ? -2.08000  48.82700  -2.47400 1.000 60.70416  ? 93  LYS A C   1 
ATOM   745  O O   . LYS A 1 96  ? -3.29800  49.01100  -2.58100 1.000 63.27506  ? 93  LYS A O   1 
ATOM   746  C CB  . LYS A 1 96  ? -0.92600  51.03100  -2.31300 1.000 65.09015  ? 93  LYS A CB  1 
ATOM   747  C CG  . LYS A 1 96  ? -0.30400  52.10400  -1.44200 1.000 76.17667  ? 93  LYS A CG  1 
ATOM   748  C CD  . LYS A 1 96  ? 0.01800   53.36000  -2.24600 1.000 90.69111  ? 93  LYS A CD  1 
ATOM   749  C CE  . LYS A 1 96  ? -1.24300  54.08100  -2.69200 1.000 88.77923  ? 93  LYS A CE  1 
ATOM   750  N NZ  . LYS A 1 96  ? -0.92900  55.40100  -3.30600 1.000 84.23086  ? 93  LYS A NZ  1 
ATOM   751  N N   . SER A 1 97  ? -1.44300  47.85400  -3.13200 1.000 48.66226  ? 94  SER A N   1 
ATOM   752  C CA  . SER A 1 97  ? -2.17500  46.93500  -3.99600 1.000 54.64271  ? 94  SER A CA  1 
ATOM   753  C C   . SER A 1 97  ? -3.16500  46.07500  -3.21900 1.000 56.51556  ? 94  SER A C   1 
ATOM   754  O O   . SER A 1 97  ? -4.07800  45.50400  -3.82500 1.000 62.04347  ? 94  SER A O   1 
ATOM   755  C CB  . SER A 1 97  ? -1.19600  46.04200  -4.76500 1.000 49.80860  ? 94  SER A CB  1 
ATOM   756  O OG  . SER A 1 97  ? -0.46100  45.21400  -3.88000 1.000 56.85124  ? 94  SER A OG  1 
ATOM   757  N N   . ILE A 1 98  ? -3.00300  45.96600  -1.90400 1.000 46.33287  ? 95  ILE A N   1 
ATOM   758  C CA  . ILE A 1 98  ? -3.92300  45.21300  -1.06100 1.000 49.92871  ? 95  ILE A CA  1 
ATOM   759  C C   . ILE A 1 98  ? -4.97400  46.16800  -0.50900 1.000 50.58648  ? 95  ILE A C   1 
ATOM   760  O O   . ILE A 1 98  ? -4.63900  47.19600  0.09400  1.000 45.25979  ? 95  ILE A O   1 
ATOM   761  C CB  . ILE A 1 98  ? -3.16700  44.50300  0.07300  1.000 43.37879  ? 95  ILE A CB  1 
ATOM   762  C CG1 . ILE A 1 98  ? -2.18700  43.48100  -0.50600 1.000 41.15139  ? 95  ILE A CG1 1 
ATOM   763  C CG2 . ILE A 1 98  ? -4.14600  43.83900  1.03200  1.000 39.25971  ? 95  ILE A CG2 1 
ATOM   764  C CD1 . ILE A 1 98  ? -0.86600  43.41600  0.22700  1.000 45.81325  ? 95  ILE A CD1 1 
ATOM   765  N N   . LYS A 1 99  ? -6.24500  45.83300  -0.72200 1.000 57.93323  ? 96  LYS A N   1 
ATOM   766  C CA  . LYS A 1 99  ? -7.33400  46.68600  -0.26200 1.000 60.27176  ? 96  LYS A CA  1 
ATOM   767  C C   . LYS A 1 99  ? -7.41300  46.66700  1.25700  1.000 51.72913  ? 96  LYS A C   1 
ATOM   768  O O   . LYS A 1 99  ? -7.45200  45.59900  1.87400  1.000 55.82762  ? 96  LYS A O   1 
ATOM   769  C CB  . LYS A 1 99  ? -8.66300  46.22500  -0.85600 1.000 57.38022  ? 96  LYS A CB  1 
ATOM   770  C CG  . LYS A 1 99  ? -8.72200  46.27500  -2.37000 1.000 85.46913  ? 96  LYS A CG  1 
ATOM   771  C CD  . LYS A 1 99  ? -10.06500 45.77900  -2.87300 1.000 95.45208  ? 96  LYS A CD  1 
ATOM   772  C CE  . LYS A 1 99  ? -10.12900 45.79900  -4.38900 1.000 90.08767  ? 96  LYS A CE  1 
ATOM   773  N NZ  . LYS A 1 99  ? -11.44900 45.32300  -4.88700 1.000 90.40975  ? 96  LYS A NZ  1 
ATOM   774  N N   . LEU A 1 100 ? -7.44100  47.85100  1.86000  1.000 52.19393  ? 97  LEU A N   1 
ATOM   775  C CA  . LEU A 1 100 ? -7.57300  47.96100  3.30800  1.000 49.15780  ? 97  LEU A CA  1 
ATOM   776  C C   . LEU A 1 100 ? -8.99800  47.61500  3.71400  1.000 47.12517  ? 97  LEU A C   1 
ATOM   777  O O   . LEU A 1 100 ? -9.94500  48.32800  3.37100  1.000 50.20438  ? 97  LEU A O   1 
ATOM   778  C CB  . LEU A 1 100 ? -7.19800  49.36200  3.77400  1.000 45.24051  ? 97  LEU A CB  1 
ATOM   779  C CG  . LEU A 1 100 ? -5.69400  49.61500  3.85600  1.000 49.53742  ? 97  LEU A CG  1 
ATOM   780  C CD1 . LEU A 1 100 ? -5.43000  51.05100  4.23600  1.000 49.20815  ? 97  LEU A CD1 1 
ATOM   781  C CD2 . LEU A 1 100 ? -5.04200  48.66600  4.85000  1.000 39.50637  ? 97  LEU A CD2 1 
ATOM   782  N N   . GLU A 1 101 ? -9.14600  46.51200  4.43900  1.000 55.27020  ? 98  GLU A N   1 
ATOM   783  C CA  . GLU A 1 101 ? -10.42900 46.08700  4.97300  1.000 56.08344  ? 98  GLU A CA  1 
ATOM   784  C C   . GLU A 1 101 ? -10.16600 45.38000  6.29400  1.000 52.08153  ? 98  GLU A C   1 
ATOM   785  O O   . GLU A 1 101 ? -9.01600  45.14000  6.67200  1.000 47.99376  ? 98  GLU A O   1 
ATOM   786  C CB  . GLU A 1 101 ? -11.17000 45.17900  3.98800  1.000 61.04977  ? 98  GLU A CB  1 
ATOM   787  C CG  . GLU A 1 101 ? -10.42300 43.89700  3.66700  1.000 59.84702  ? 98  GLU A CG  1 
ATOM   788  C CD  . GLU A 1 101 ? -11.12800 43.05000  2.63000  1.000 69.74640  ? 98  GLU A CD  1 
ATOM   789  O OE1 . GLU A 1 101 ? -12.08700 43.55000  2.00600  1.000 71.10183  ? 98  GLU A OE1 1 
ATOM   790  O OE2 . GLU A 1 101 ? -10.72300 41.88300  2.44100  1.000 78.95090  ? 98  GLU A OE2 1 
ATOM   791  N N   . ARG A 1 102 ? -11.24400 45.04000  6.99900  1.000 52.96347  ? 99  ARG A N   1 
ATOM   792  C CA  . ARG A 1 102 ? -11.07000 44.40700  8.30100  1.000 48.47998  ? 99  ARG A CA  1 
ATOM   793  C C   . ARG A 1 102 ? -10.47600 43.00800  8.16500  1.000 46.82522  ? 99  ARG A C   1 
ATOM   794  O O   . ARG A 1 102 ? -9.65100  42.59800  8.99100  1.000 44.48291  ? 99  ARG A O   1 
ATOM   795  C CB  . ARG A 1 102 ? -12.40000 44.35800  9.05000  1.000 45.38298  ? 99  ARG A CB  1 
ATOM   796  C CG  . ARG A 1 102 ? -12.21700 44.28400  10.55100 1.000 55.14222  ? 99  ARG A CG  1 
ATOM   797  C CD  . ARG A 1 102 ? -13.44800 43.75000  11.25600 1.000 52.26976  ? 99  ARG A CD  1 
ATOM   798  N NE  . ARG A 1 102 ? -13.13500 43.37200  12.62900 1.000 53.92686  ? 99  ARG A NE  1 
ATOM   799  C CZ  . ARG A 1 102 ? -13.69100 42.35500  13.27200 1.000 58.17683  ? 99  ARG A CZ  1 
ATOM   800  N NH1 . ARG A 1 102 ? -14.60100 41.58800  12.69500 1.000 65.95067  ? 99  ARG A NH1 1 
ATOM   801  N NH2 . ARG A 1 102 ? -13.31800 42.09500  14.52200 1.000 57.68350  ? 99  ARG A NH2 1 
ATOM   802  N N   . LYS A 1 103 ? -10.86900 42.26800  7.12400  1.000 51.16398  ? 100 LYS A N   1 
ATOM   803  C CA  . LYS A 1 103 ? -10.36600 40.91000  6.93000  1.000 47.44703  ? 100 LYS A CA  1 
ATOM   804  C C   . LYS A 1 103 ? -8.86300  40.87200  6.69200  1.000 50.56717  ? 100 LYS A C   1 
ATOM   805  O O   . LYS A 1 103 ? -8.25400  39.80500  6.82800  1.000 52.62517  ? 100 LYS A O   1 
ATOM   806  C CB  . LYS A 1 103 ? -11.09200 40.23900  5.76200  1.000 52.62223  ? 100 LYS A CB  1 
ATOM   807  C CG  . LYS A 1 103 ? -12.57500 40.01300  6.00700  1.000 67.74882  ? 100 LYS A CG  1 
ATOM   808  C CD  . LYS A 1 103 ? -13.24300 39.39800  4.79000  1.000 76.71139  ? 100 LYS A CD  1 
ATOM   809  C CE  . LYS A 1 103 ? -14.72300 39.14400  5.03400  1.000 80.03914  ? 100 LYS A CE  1 
ATOM   810  N NZ  . LYS A 1 103 ? -15.39000 38.59700  3.81800  1.000 88.58253  ? 100 LYS A NZ  1 
ATOM   811  N N   . VAL A 1 104 ? -8.25200  42.00200  6.33100  1.000 48.16019  ? 101 VAL A N   1 
ATOM   812  C CA  . VAL A 1 104 ? -6.79500  42.05900  6.24700  1.000 41.18678  ? 101 VAL A CA  1 
ATOM   813  C C   . VAL A 1 104 ? -6.17700  41.82100  7.61800  1.000 36.16006  ? 101 VAL A C   1 
ATOM   814  O O   . VAL A 1 104 ? -5.13700  41.16300  7.74500  1.000 38.34357  ? 101 VAL A O   1 
ATOM   815  C CB  . VAL A 1 104 ? -6.34600  43.40700  5.64900  1.000 42.89536  ? 101 VAL A CB  1 
ATOM   816  C CG1 . VAL A 1 104 ? -4.84500  43.60300  5.81700  1.000 35.11470  ? 101 VAL A CG1 1 
ATOM   817  C CG2 . VAL A 1 104 ? -6.73100  43.48700  4.18300  1.000 43.14119  ? 101 VAL A CG2 1 
ATOM   818  N N   . PHE A 1 105 ? -6.82000  42.33300  8.66900  1.000 43.55813  ? 102 PHE A N   1 
ATOM   819  C CA  . PHE A 1 105 ? -6.25900  42.29300  10.01000 1.000 40.59616  ? 102 PHE A CA  1 
ATOM   820  C C   . PHE A 1 105 ? -6.92900  41.28100  10.92800 1.000 44.07410  ? 102 PHE A C   1 
ATOM   821  O O   . PHE A 1 105 ? -6.27700  40.79200  11.85700 1.000 40.28636  ? 102 PHE A O   1 
ATOM   822  C CB  . PHE A 1 105 ? -6.33400  43.68900  10.65000 1.000 42.32622  ? 102 PHE A CB  1 
ATOM   823  C CG  . PHE A 1 105 ? -5.72400  44.76900  9.80000  1.000 37.02354  ? 102 PHE A CG  1 
ATOM   824  C CD1 . PHE A 1 105 ? -4.36800  45.04500  9.87400  1.000 36.26211  ? 102 PHE A CD1 1 
ATOM   825  C CD2 . PHE A 1 105 ? -6.50300  45.49500  8.91100  1.000 40.66105  ? 102 PHE A CD2 1 
ATOM   826  C CE1 . PHE A 1 105 ? -3.79900  46.02800  9.08700  1.000 37.54834  ? 102 PHE A CE1 1 
ATOM   827  C CE2 . PHE A 1 105 ? -5.94000  46.48500  8.11700  1.000 39.91727  ? 102 PHE A CE2 1 
ATOM   828  C CZ  . PHE A 1 105 ? -4.58600  46.75100  8.20600  1.000 41.28612  ? 102 PHE A CZ  1 
ATOM   829  N N   . ALA A 1 106 ? -8.19400  40.93800  10.68500 1.000 51.06998  ? 103 ALA A N   1 
ATOM   830  C CA  . ALA A 1 106 ? -8.94900  40.07400  11.58000 1.000 55.23488  ? 103 ALA A CA  1 
ATOM   831  C C   . ALA A 1 106 ? -9.50300  38.86700  10.83700 1.000 57.52361  ? 103 ALA A C   1 
ATOM   832  O O   . ALA A 1 106 ? -9.97400  38.98400  9.70100  1.000 54.21127  ? 103 ALA A O   1 
ATOM   833  C CB  . ALA A 1 106 ? -10.10200 40.83700  12.24200 1.000 48.45454  ? 103 ALA A CB  1 
ATOM   834  N N   . SER A 1 107 ? -9.43800  37.71100  11.48600 1.000 46.88114  ? 104 SER A N   1 
ATOM   835  C CA  . SER A 1 107 ? -10.16200 36.52300  11.06500 1.000 46.17892  ? 104 SER A CA  1 
ATOM   836  C C   . SER A 1 107 ? -11.44900 36.41200  11.87500 1.000 46.60309  ? 104 SER A C   1 
ATOM   837  O O   . SER A 1 107 ? -11.69600 37.19000  12.79800 1.000 47.96445  ? 104 SER A O   1 
ATOM   838  C CB  . SER A 1 107 ? -9.29600  35.27000  11.23400 1.000 40.65409  ? 104 SER A CB  1 
ATOM   839  O OG  . SER A 1 107 ? -9.96100  34.12100  10.74600 1.000 51.43261  ? 104 SER A OG  1 
ATOM   840  N N   . GLU A 1 108 ? -12.27500 35.43300  11.51400 1.000 66.52796  ? 105 GLU A N   1 
ATOM   841  C CA  . GLU A 1 108 ? -13.55100 35.24500  12.19400 1.000 67.81222  ? 105 GLU A CA  1 
ATOM   842  C C   . GLU A 1 108 ? -13.34500 35.04600  13.69300 1.000 65.78816  ? 105 GLU A C   1 
ATOM   843  O O   . GLU A 1 108 ? -12.33100 34.50200  14.13700 1.000 61.65085  ? 105 GLU A O   1 
ATOM   844  C CB  . GLU A 1 108 ? -14.29900 34.05500  11.59500 1.000 71.01737  ? 105 GLU A CB  1 
ATOM   845  C CG  . GLU A 1 108 ? -15.06600 34.39000  10.32800 1.000 81.89335  ? 105 GLU A CG  1 
ATOM   846  C CD  . GLU A 1 108 ? -16.28200 35.25300  10.60100 1.000 90.00081  ? 105 GLU A CD  1 
ATOM   847  O OE1 . GLU A 1 108 ? -17.07400 34.89800  11.50200 1.000 89.79493  ? 105 GLU A OE1 1 
ATOM   848  O OE2 . GLU A 1 108 ? -16.44700 36.28700  9.91700  1.000 91.34050  ? 105 GLU A OE2 1 
ATOM   849  N N   . ARG A 1 109 ? -14.32800 35.50800  14.47200 1.000 69.17214  ? 106 ARG A N   1 
ATOM   850  C CA  . ARG A 1 109 ? -14.26300 35.56500  15.93500 1.000 67.52158  ? 106 ARG A CA  1 
ATOM   851  C C   . ARG A 1 109 ? -13.19300 36.54000  16.42800 1.000 67.25907  ? 106 ARG A C   1 
ATOM   852  O O   . ARG A 1 109 ? -12.60400 36.33800  17.49400 1.000 61.52201  ? 106 ARG A O   1 
ATOM   853  C CB  . ARG A 1 109 ? -14.04800 34.17900  16.55800 1.000 60.10017  ? 106 ARG A CB  1 
ATOM   854  C CG  . ARG A 1 109 ? -15.17900 33.20000  16.30300 1.000 65.08094  ? 106 ARG A CG  1 
ATOM   855  C CD  . ARG A 1 109 ? -16.50900 33.77300  16.74700 1.000 77.34735  ? 106 ARG A CD  1 
ATOM   856  N NE  . ARG A 1 109 ? -16.61100 33.87000  18.19700 1.000 75.70676  ? 106 ARG A NE  1 
ATOM   857  C CZ  . ARG A 1 109 ? -17.54300 33.26800  18.92300 1.000 78.68814  ? 106 ARG A CZ  1 
ATOM   858  N NH1 . ARG A 1 109 ? -18.49000 32.53600  18.36100 1.000 87.63136  ? 106 ARG A NH1 1 
ATOM   859  N NH2 . ARG A 1 109 ? -17.53000 33.41200  20.24500 1.000 83.02058  ? 106 ARG A NH2 1 
ATOM   860  N N   . ASN A 1 110 ? -12.93400 37.59800  15.65300 1.000 50.88193  ? 107 ASN A N   1 
ATOM   861  C CA  . ASN A 1 110 ? -12.07500 38.70600  16.07900 1.000 51.40912  ? 107 ASN A CA  1 
ATOM   862  C C   . ASN A 1 110 ? -10.65100 38.24300  16.38300 1.000 47.18419  ? 107 ASN A C   1 
ATOM   863  O O   . ASN A 1 110 ? -10.03900 38.66200  17.36700 1.000 46.31826  ? 107 ASN A O   1 
ATOM   864  C CB  . ASN A 1 110 ? -12.67700 39.43000  17.28600 1.000 53.70634  ? 107 ASN A CB  1 
ATOM   865  C CG  . ASN A 1 110 ? -14.10200 39.88300  17.04200 1.000 59.69800  ? 107 ASN A CG  1 
ATOM   866  O OD1 . ASN A 1 110 ? -14.38100 40.60900  16.08700 1.000 59.18243  ? 107 ASN A OD1 1 
ATOM   867  N ND2 . ASN A 1 110 ? -15.01600 39.44700  17.90300 1.000 63.90772  ? 107 ASN A ND2 1 
ATOM   868  N N   . VAL A 1 111 ? -10.11300 37.37600  15.53200 1.000 47.25683  ? 108 VAL A N   1 
ATOM   869  C CA  . VAL A 1 111 ? -8.75300  36.87300  15.69700 1.000 45.55252  ? 108 VAL A CA  1 
ATOM   870  C C   . VAL A 1 111 ? -7.78800  37.84400  15.02900 1.000 46.80000  ? 108 VAL A C   1 
ATOM   871  O O   . VAL A 1 111 ? -7.85700  38.06600  13.81500 1.000 43.75512  ? 108 VAL A O   1 
ATOM   872  C CB  . VAL A 1 111 ? -8.60300  35.46200  15.11200 1.000 49.07729  ? 108 VAL A CB  1 
ATOM   873  C CG1 . VAL A 1 111 ? -7.15200  35.00900  15.20800 1.000 45.91939  ? 108 VAL A CG1 1 
ATOM   874  C CG2 . VAL A 1 111 ? -9.52000  34.49000  15.83500 1.000 47.66269  ? 108 VAL A CG2 1 
ATOM   875  N N   . SER A 1 112 ? -6.88400  38.41800  15.81900 1.000 42.02185  ? 109 SER A N   1 
ATOM   876  C CA  . SER A 1 112 ? -5.88600  39.34600  15.29800 1.000 39.25286  ? 109 SER A CA  1 
ATOM   877  C C   . SER A 1 112 ? -4.85900  38.55500  14.50000 1.000 38.11274  ? 109 SER A C   1 
ATOM   878  O O   . SER A 1 112 ? -4.04200  37.83000  15.07600 1.000 39.88357  ? 109 SER A O   1 
ATOM   879  C CB  . SER A 1 112 ? -5.22500  40.11900  16.43500 1.000 40.29801  ? 109 SER A CB  1 
ATOM   880  O OG  . SER A 1 112 ? -4.38000  41.13900  15.93300 1.000 38.46893  ? 109 SER A OG  1 
ATOM   881  N N   . ILE A 1 113 ? -4.90500  38.69200  13.17200 1.000 43.35792  ? 110 ILE A N   1 
ATOM   882  C CA  . ILE A 1 113 ? -3.99000  37.95300  12.30400 1.000 42.18965  ? 110 ILE A CA  1 
ATOM   883  C C   . ILE A 1 113 ? -2.54500  38.29500  12.63900 1.000 40.67205  ? 110 ILE A C   1 
ATOM   884  O O   . ILE A 1 113 ? -1.70300  37.40900  12.82700 1.000 41.29136  ? 110 ILE A O   1 
ATOM   885  C CB  . ILE A 1 113 ? -4.30200  38.23800  10.82500 1.000 38.69467  ? 110 ILE A CB  1 
ATOM   886  C CG1 . ILE A 1 113 ? -5.65600  37.64000  10.43900 1.000 44.49767  ? 110 ILE A CG1 1 
ATOM   887  C CG2 . ILE A 1 113 ? -3.18800  37.70400  9.93100  1.000 35.63231  ? 110 ILE A CG2 1 
ATOM   888  C CD1 . ILE A 1 113 ? -6.11600  38.02200  9.05100  1.000 43.81202  ? 110 ILE A CD1 1 
ATOM   889  N N   . PHE A 1 114 ? -2.23500  39.59000  12.71400 1.000 39.46953  ? 111 PHE A N   1 
ATOM   890  C CA  . PHE A 1 114 ? -0.86400  40.00500  12.97700 1.000 41.78790  ? 111 PHE A CA  1 
ATOM   891  C C   . PHE A 1 114 ? -0.50700  39.89700  14.45100 1.000 45.70565  ? 111 PHE A C   1 
ATOM   892  O O   . PHE A 1 114 ? 0.67700   39.78400  14.78800 1.000 49.08318  ? 111 PHE A O   1 
ATOM   893  C CB  . PHE A 1 114 ? -0.64500  41.42800  12.46200 1.000 36.56895  ? 111 PHE A CB  1 
ATOM   894  C CG  . PHE A 1 114 ? -0.90400  41.57000  10.99200 1.000 37.01476  ? 111 PHE A CG  1 
ATOM   895  C CD1 . PHE A 1 114 ? -0.02700  41.02100  10.06600 1.000 39.96786  ? 111 PHE A CD1 1 
ATOM   896  C CD2 . PHE A 1 114 ? -2.03100  42.22700  10.53200 1.000 33.21711  ? 111 PHE A CD2 1 
ATOM   897  C CE1 . PHE A 1 114 ? -0.26500  41.13400  8.70800  1.000 34.40518  ? 111 PHE A CE1 1 
ATOM   898  C CE2 . PHE A 1 114 ? -2.27300  42.34500  9.17200  1.000 42.50074  ? 111 PHE A CE2 1 
ATOM   899  C CZ  . PHE A 1 114 ? -1.38700  41.79700  8.25900  1.000 35.24651  ? 111 PHE A CZ  1 
ATOM   900  N N   . GLY A 1 115 ? -1.50600  39.92500  15.33800 1.000 50.85615  ? 112 GLY A N   1 
ATOM   901  C CA  . GLY A 1 115 ? -1.24200  39.62000  16.73400 1.000 42.36149  ? 112 GLY A CA  1 
ATOM   902  C C   . GLY A 1 115 ? -0.74400  38.20000  16.92600 1.000 44.67437  ? 112 GLY A C   1 
ATOM   903  O O   . GLY A 1 115 ? 0.14700   37.94800  17.74000 1.000 45.56745  ? 112 GLY A O   1 
ATOM   904  N N   . ARG A 1 116 ? -1.30900  37.25400  16.17000 1.000 52.09392  ? 113 ARG A N   1 
ATOM   905  C CA  . ARG A 1 116 ? -0.84900  35.87100  16.24800 1.000 54.28998  ? 113 ARG A CA  1 
ATOM   906  C C   . ARG A 1 116 ? 0.50300   35.69800  15.56800 1.000 52.62115  ? 113 ARG A C   1 
ATOM   907  O O   . ARG A 1 116 ? 1.38400   35.00700  16.09200 1.000 58.22527  ? 113 ARG A O   1 
ATOM   908  C CB  . ARG A 1 116 ? -1.88000  34.93300  15.61800 1.000 54.24684  ? 113 ARG A CB  1 
ATOM   909  C CG  . ARG A 1 116 ? -3.25400  34.98000  16.26400 1.000 57.56650  ? 113 ARG A CG  1 
ATOM   910  C CD  . ARG A 1 116 ? -3.78500  33.58000  16.54500 1.000 55.90270  ? 113 ARG A CD  1 
ATOM   911  N NE  . ARG A 1 116 ? -3.13700  32.97400  17.70200 1.000 62.15104  ? 113 ARG A NE  1 
ATOM   912  C CZ  . ARG A 1 116 ? -3.47100  33.22900  18.96000 1.000 62.82487  ? 113 ARG A CZ  1 
ATOM   913  N NH1 . ARG A 1 116 ? -4.43200  34.08700  19.25900 1.000 65.05035  ? 113 ARG A NH1 1 
ATOM   914  N NH2 . ARG A 1 116 ? -2.82400  32.60900  19.94300 1.000 66.83158  ? 113 ARG A NH2 1 
ATOM   915  N N   . LEU A 1 117 ? 0.68400   36.32100  14.40200 1.000 53.64244  ? 114 LEU A N   1 
ATOM   916  C CA  . LEU A 1 117 ? 1.92100   36.14500  13.64700 1.000 52.37062  ? 114 LEU A CA  1 
ATOM   917  C C   . LEU A 1 117 ? 3.12200   36.71300  14.39700 1.000 55.28654  ? 114 LEU A C   1 
ATOM   918  O O   . LEU A 1 117 ? 4.19700   36.10200  14.40900 1.000 59.28196  ? 114 LEU A O   1 
ATOM   919  C CB  . LEU A 1 117 ? 1.78300   36.79700  12.27100 1.000 48.04788  ? 114 LEU A CB  1 
ATOM   920  C CG  . LEU A 1 117 ? 3.01600   36.83400  11.36200 1.000 47.83362  ? 114 LEU A CG  1 
ATOM   921  C CD1 . LEU A 1 117 ? 3.49500   35.43300  11.03200 1.000 47.99055  ? 114 LEU A CD1 1 
ATOM   922  C CD2 . LEU A 1 117 ? 2.71300   37.61100  10.09100 1.000 48.67385  ? 114 LEU A CD2 1 
ATOM   923  N N   . SER A 1 118 ? 2.95700   37.87400  15.03700 1.000 55.45762  ? 115 SER A N   1 
ATOM   924  C CA  . SER A 1 118 ? 4.08900   38.53200  15.68500 1.000 60.43385  ? 115 SER A CA  1 
ATOM   925  C C   . SER A 1 118 ? 4.62200   37.71000  16.85200 1.000 57.19920  ? 115 SER A C   1 
ATOM   926  O O   . SER A 1 118 ? 5.83300   37.68700  17.10100 1.000 64.26842  ? 115 SER A O   1 
ATOM   927  C CB  . SER A 1 118 ? 3.68700   39.93000  16.15400 1.000 54.30308  ? 115 SER A CB  1 
ATOM   928  O OG  . SER A 1 118 ? 4.76000   40.56300  16.82400 1.000 66.35748  ? 115 SER A OG  1 
ATOM   929  N N   . LYS A 1 119 ? 3.73600   37.03000  17.58200 1.000 60.70071  ? 116 LYS A N   1 
ATOM   930  C CA  . LYS A 1 119 ? 4.19100   36.16000  18.66100 1.000 69.04779  ? 116 LYS A CA  1 
ATOM   931  C C   . LYS A 1 119 ? 4.97800   34.96500  18.13700 1.000 63.61874  ? 116 LYS A C   1 
ATOM   932  O O   . LYS A 1 119 ? 5.80800   34.41500  18.86900 1.000 72.03911  ? 116 LYS A O   1 
ATOM   933  C CB  . LYS A 1 119 ? 3.00000   35.68000  19.49800 1.000 60.65662  ? 116 LYS A CB  1 
ATOM   934  C CG  . LYS A 1 119 ? 3.40000   34.98100  20.78900 1.000 79.38822  ? 116 LYS A CG  1 
ATOM   935  C CD  . LYS A 1 119 ? 2.20200   34.62000  21.65400 1.000 81.22501  ? 116 LYS A CD  1 
ATOM   936  C CE  . LYS A 1 119 ? 2.66000   33.94700  22.94200 1.000 69.42425  ? 116 LYS A CE  1 
ATOM   937  N NZ  . LYS A 1 119 ? 1.53200   33.63300  23.85900 1.000 78.81053  ? 116 LYS A NZ  1 
ATOM   938  N N   . LEU A 1 120 ? 4.74800   34.56300  16.88900 1.000 56.01698  ? 117 LEU A N   1 
ATOM   939  C CA  . LEU A 1 120 ? 5.44800   33.42800  16.30600 1.000 56.23791  ? 117 LEU A CA  1 
ATOM   940  C C   . LEU A 1 120 ? 6.77600   33.80400  15.66700 1.000 65.04090  ? 117 LEU A C   1 
ATOM   941  O O   . LEU A 1 120 ? 7.60300   32.91700  15.42600 1.000 67.62423  ? 117 LEU A O   1 
ATOM   942  C CB  . LEU A 1 120 ? 4.56100   32.74600  15.26100 1.000 60.59407  ? 117 LEU A CB  1 
ATOM   943  C CG  . LEU A 1 120 ? 3.28700   32.10200  15.80100 1.000 56.47915  ? 117 LEU A CG  1 
ATOM   944  C CD1 . LEU A 1 120 ? 2.38800   31.65600  14.65900 1.000 58.42419  ? 117 LEU A CD1 1 
ATOM   945  C CD2 . LEU A 1 120 ? 3.64400   30.93000  16.69900 1.000 56.82977  ? 117 LEU A CD2 1 
ATOM   946  N N   . LEU A 1 121 ? 6.96800   35.09700  15.39100 1.000 66.04692  ? 118 LEU A N   1 
ATOM   947  C CA  . LEU A 1 121 ? 8.20900   35.56500  14.71700 1.000 67.75751  ? 118 LEU A CA  1 
ATOM   948  C C   . LEU A 1 121 ? 9.35300   35.63600  15.73300 1.000 77.57976  ? 118 LEU A C   1 
ATOM   949  O O   . LEU A 1 121 ? 9.09200   36.01500  16.89100 1.000 71.48006  ? 118 LEU A O   1 
ATOM   950  C CB  . LEU A 1 121 ? 7.94800   36.93400  14.08300 1.000 67.47162  ? 118 LEU A CB  1 
ATOM   951  C CG  . LEU A 1 121 ? 6.98600   36.93500  12.89700 1.000 64.75170  ? 118 LEU A CG  1 
ATOM   952  C CD1 . LEU A 1 121 ? 6.82100   38.33600  12.33100 1.000 53.93629  ? 118 LEU A CD1 1 
ATOM   953  C CD2 . LEU A 1 121 ? 7.45400   35.97200  11.81700 1.000 61.53067  ? 118 LEU A CD2 1 
ATOM   954  N N   . ASP A 1 122 ? 10.56900  35.28400  15.30800 1.000 100.16127 ? 119 ASP A N   1 
ATOM   955  C CA  . ASP A 1 122 ? 11.74800  35.30400  16.21400 1.000 105.82837 ? 119 ASP A CA  1 
ATOM   956  C C   . ASP A 1 122 ? 12.56200  36.57900  15.97200 1.000 105.32449 ? 119 ASP A C   1 
ATOM   957  O O   . ASP A 1 122 ? 13.66900  36.68200  16.53400 1.000 118.41111 ? 119 ASP A O   1 
ATOM   958  C CB  . ASP A 1 122 ? 12.59100  34.03700  16.05400 1.000 105.26403 ? 119 ASP A CB  1 
ATOM   959  C CG  . ASP A 1 122 ? 11.95300  32.81400  16.69000 1.000 113.29007 ? 119 ASP A CG  1 
ATOM   960  O OD1 . ASP A 1 122 ? 11.36100  32.96300  17.77700 1.000 118.51129 ? 119 ASP A OD1 1 
ATOM   961  O OD2 . ASP A 1 122 ? 12.05100  31.72500  16.09200 1.000 116.70529 ? 119 ASP A OD2 1 
ATOM   962  N N   . HIS A 1 123 ? 12.03700  37.50900  15.17100 1.000 92.81291  ? 120 HIS A N   1 
ATOM   963  C CA  . HIS A 1 123 ? 12.80300  38.73400  14.81900 1.000 85.00753  ? 120 HIS A CA  1 
ATOM   964  C C   . HIS A 1 123 ? 11.99000  39.98300  15.17200 1.000 90.75107  ? 120 HIS A C   1 
ATOM   965  O O   . HIS A 1 123 ? 10.75200  39.89200  15.17700 1.000 92.55578  ? 120 HIS A O   1 
ATOM   966  C CB  . HIS A 1 123 ? 13.18200  38.70900  13.33300 1.000 88.55244  ? 120 HIS A CB  1 
ATOM   967  C CG  . HIS A 1 123 ? 12.01800  38.53400  12.41600 1.000 92.45465  ? 120 HIS A CG  1 
ATOM   968  N ND1 . HIS A 1 123 ? 11.24000  39.59600  11.99900 1.000 84.48475  ? 120 HIS A ND1 1 
ATOM   969  C CD2 . HIS A 1 123 ? 11.49700  37.43300  11.83300 1.000 86.01305  ? 120 HIS A CD2 1 
ATOM   970  C CE1 . HIS A 1 123 ? 10.29100  39.15800  11.19900 1.000 79.42183  ? 120 HIS A CE1 1 
ATOM   971  N NE2 . HIS A 1 123 ? 10.42700  37.83300  11.08100 1.000 90.11395  ? 120 HIS A NE2 1 
ATOM   972  N N   . THR A 1 124 ? 12.66900  41.10000  15.44900 1.000 95.97002  ? 121 THR A N   1 
ATOM   973  C CA  . THR A 1 124 ? 11.98100  42.37400  15.79500 1.000 99.65734  ? 121 THR A CA  1 
ATOM   974  C C   . THR A 1 124 ? 11.65200  43.14200  14.51000 1.000 91.42380  ? 121 THR A C   1 
ATOM   975  O O   . THR A 1 124 ? 11.03600  44.22100  14.61000 1.000 87.30736  ? 121 THR A O   1 
ATOM   976  C CB  . THR A 1 124 ? 12.83300  43.20700  16.76100 1.000 104.59130 ? 121 THR A CB  1 
ATOM   977  O OG1 . THR A 1 124 ? 12.06000  44.32300  17.20400 1.000 110.02819 ? 121 THR A OG1 1 
ATOM   978  C CG2 . THR A 1 124 ? 14.12700  43.68700  16.14200 1.000 97.44326  ? 121 THR A CG2 1 
ATOM   979  N N   . ASN A 1 125 ? 12.04700  42.60400  13.35400 1.000 84.41684  ? 122 ASN A N   1 
ATOM   980  C CA  . ASN A 1 125 ? 11.80500  43.28400  12.05400 1.000 79.69905  ? 122 ASN A CA  1 
ATOM   981  C C   . ASN A 1 125 ? 10.29700  43.39200  11.80200 1.000 73.84798  ? 122 ASN A C   1 
ATOM   982  O O   . ASN A 1 125 ? 9.56700   42.44900  12.16000 1.000 75.63247  ? 122 ASN A O   1 
ATOM   983  C CB  . ASN A 1 125 ? 12.53600  42.58200  10.90700 1.000 80.99335  ? 122 ASN A CB  1 
ATOM   984  C CG  . ASN A 1 125 ? 13.91200  42.08600  11.29700 1.000 84.20453  ? 122 ASN A CG  1 
ATOM   985  O OD1 . ASN A 1 125 ? 14.60000  42.71400  12.09900 1.000 93.65981  ? 122 ASN A OD1 1 
ATOM   986  N ND2 . ASN A 1 125 ? 14.32300  40.96300  10.73300 1.000 90.85933  ? 122 ASN A ND2 1 
ATOM   987  N N   . PRO A 1 126 ? 9.80200   44.49600  11.20000 1.000 70.72334  ? 123 PRO A N   1 
ATOM   988  C CA  . PRO A 1 126 ? 8.36300   44.69400  10.99000 1.000 61.47618  ? 123 PRO A CA  1 
ATOM   989  C C   . PRO A 1 126 ? 7.73000   43.73700  9.97000  1.000 61.97348  ? 123 PRO A C   1 
ATOM   990  O O   . PRO A 1 126 ? 8.42600   43.27900  9.08400  1.000 67.02322  ? 123 PRO A O   1 
ATOM   991  C CB  . PRO A 1 126 ? 8.27500   46.13400  10.46300 1.000 60.48613  ? 123 PRO A CB  1 
ATOM   992  C CG  . PRO A 1 126 ? 9.62200   46.38100  9.82900  1.000 65.12119  ? 123 PRO A CG  1 
ATOM   993  C CD  . PRO A 1 126 ? 10.59600  45.62200  10.70300 1.000 68.21221  ? 123 PRO A CD  1 
ATOM   994  N N   . ILE A 1 127 ? 6.43500   43.45100  10.13100 1.000 55.98905  ? 124 ILE A N   1 
ATOM   995  C CA  . ILE A 1 127 ? 5.71300   42.57100  9.16400  1.000 54.40384  ? 124 ILE A CA  1 
ATOM   996  C C   . ILE A 1 127 ? 5.43700   43.36500  7.88600  1.000 54.46313  ? 124 ILE A C   1 
ATOM   997  O O   . ILE A 1 127 ? 4.84400   44.44700  7.99200  1.000 53.06888  ? 124 ILE A O   1 
ATOM   998  C CB  . ILE A 1 127 ? 4.41100   42.03000  9.78300  1.000 53.51142  ? 124 ILE A CB  1 
ATOM   999  C CG1 . ILE A 1 127 ? 4.63200   41.49800  11.20000 1.000 57.04089  ? 124 ILE A CG1 1 
ATOM   1000 C CG2 . ILE A 1 127 ? 3.77900   40.98400  8.87900  1.000 45.31644  ? 124 ILE A CG2 1 
ATOM   1001 C CD1 . ILE A 1 127 ? 3.38800   40.93100  11.83500 1.000 51.88666  ? 124 ILE A CD1 1 
ATOM   1002 N N   . ILE A 1 128 ? 5.86000   42.84800  6.73000  1.000 48.30601  ? 125 ILE A N   1 
ATOM   1003 C CA  . ILE A 1 128 ? 5.63900   43.51300  5.45100  1.000 45.80712  ? 125 ILE A CA  1 
ATOM   1004 C C   . ILE A 1 128 ? 4.83800   42.57200  4.56500  1.000 41.10834  ? 125 ILE A C   1 
ATOM   1005 O O   . ILE A 1 128 ? 5.24100   41.42200  4.34700  1.000 37.89383  ? 125 ILE A O   1 
ATOM   1006 C CB  . ILE A 1 128 ? 6.96100   43.91900  4.78200  1.000 48.00854  ? 125 ILE A CB  1 
ATOM   1007 C CG1 . ILE A 1 128 ? 7.80500   44.74400  5.75300  1.000 49.12740  ? 125 ILE A CG1 1 
ATOM   1008 C CG2 . ILE A 1 128 ? 6.69400   44.71200  3.51000  1.000 46.44279  ? 125 ILE A CG2 1 
ATOM   1009 C CD1 . ILE A 1 128 ? 9.07200   45.29900  5.14500  1.000 48.21347  ? 125 ILE A CD1 1 
ATOM   1010 N N   . ILE A 1 129 ? 3.71000   43.05900  4.05400  1.000 45.31155  ? 126 ILE A N   1 
ATOM   1011 C CA  . ILE A 1 129 ? 2.80000   42.27000  3.23300  1.000 43.30188  ? 126 ILE A CA  1 
ATOM   1012 C C   . ILE A 1 129 ? 2.73600   42.89400  1.84500  1.000 47.71528  ? 126 ILE A C   1 
ATOM   1013 O O   . ILE A 1 129 ? 2.31300   44.04800  1.69500  1.000 52.13637  ? 126 ILE A O   1 
ATOM   1014 C CB  . ILE A 1 129 ? 1.39800   42.18900  3.85700  1.000 45.36526  ? 126 ILE A CB  1 
ATOM   1015 C CG1 . ILE A 1 129 ? 1.48500   41.71000  5.31100  1.000 40.10057  ? 126 ILE A CG1 1 
ATOM   1016 C CG2 . ILE A 1 129 ? 0.51000   41.27300  3.03800  1.000 40.72504  ? 126 ILE A CG2 1 
ATOM   1017 C CD1 . ILE A 1 129 ? 1.96200   40.28100  5.46200  1.000 39.82821  ? 126 ILE A CD1 1 
ATOM   1018 N N   . GLY A 1 130 ? 3.12100   42.13400  0.82000  1.000 53.71006  ? 127 GLY A N   1 
ATOM   1019 C CA  . GLY A 1 130 ? 2.98400   42.59200  -0.57400 1.000 54.79872  ? 127 GLY A CA  1 
ATOM   1020 C C   . GLY A 1 130 ? 4.11000   43.46500  -1.07100 1.000 57.71683  ? 127 GLY A C   1 
ATOM   1021 O O   . GLY A 1 130 ? 5.05500   43.69000  -0.32900 1.000 61.76339  ? 127 GLY A O   1 
ATOM   1022 N N   . GLY A 1 131 ? 3.99300   43.94200  -2.30200 1.000 51.08300  ? 128 GLY A N   1 
ATOM   1023 C CA  . GLY A 1 131 ? 4.99200   44.86700  -2.85100 1.000 51.58602  ? 128 GLY A CA  1 
ATOM   1024 C C   . GLY A 1 131 ? 6.23500   44.22600  -3.41100 1.000 55.09301  ? 128 GLY A C   1 
ATOM   1025 O O   . GLY A 1 131 ? 6.16400   43.06300  -3.79700 1.000 58.14058  ? 128 GLY A O   1 
ATOM   1026 N N   . ASP A 1 132 ? 7.31600   44.99700  -3.51000 1.000 62.06844  ? 129 ASP A N   1 
ATOM   1027 C CA  . ASP A 1 132 ? 8.56600   44.50800  -4.14100 1.000 73.96387  ? 129 ASP A CA  1 
ATOM   1028 C C   . ASP A 1 132 ? 9.66900   44.41900  -3.09600 1.000 65.05436  ? 129 ASP A C   1 
ATOM   1029 O O   . ASP A 1 132 ? 10.76800  43.99900  -3.44100 1.000 76.46273  ? 129 ASP A O   1 
ATOM   1030 C CB  . ASP A 1 132 ? 8.97400   45.41400  -5.30300 1.000 71.18658  ? 129 ASP A CB  1 
ATOM   1031 C CG  . ASP A 1 132 ? 7.85400   45.64300  -6.29800 1.000 82.52059  ? 129 ASP A CG  1 
ATOM   1032 O OD1 . ASP A 1 132 ? 7.37100   44.65100  -6.87100 1.000 82.66023  ? 129 ASP A OD1 1 
ATOM   1033 O OD2 . ASP A 1 132 ? 7.47200   46.81000  -6.48400 1.000 93.77325  ? 129 ASP A OD2 1 
ATOM   1034 N N   . LYS A 1 133 ? 9.36300   44.77100  -1.86000 1.000 61.77052  ? 130 LYS A N   1 
ATOM   1035 C CA  . LYS A 1 133 ? 10.38200  44.61100  -0.80300 1.000 66.66379  ? 130 LYS A CA  1 
ATOM   1036 C C   . LYS A 1 133 ? 10.72300  43.13000  -0.69800 1.000 68.42732  ? 130 LYS A C   1 
ATOM   1037 O O   . LYS A 1 133 ? 9.81600   42.28800  -0.73300 1.000 60.58903  ? 130 LYS A O   1 
ATOM   1038 C CB  . LYS A 1 133 ? 9.93200   45.24900  0.51200  1.000 61.06885  ? 130 LYS A CB  1 
ATOM   1039 C CG  . LYS A 1 133 ? 9.81300   46.76300  0.48700  1.000 63.74329  ? 130 LYS A CG  1 
ATOM   1040 C CD  . LYS A 1 133 ? 9.34400   47.34900  1.79200  1.000 61.32260  ? 130 LYS A CD  1 
ATOM   1041 C CE  . LYS A 1 133 ? 9.25900   48.85700  1.74400  1.000 75.61854  ? 130 LYS A CE  1 
ATOM   1042 N NZ  . LYS A 1 133 ? 8.77500   49.41300  3.02600  1.000 85.90036  ? 130 LYS A NZ  1 
ATOM   1043 N N   . PRO A 1 134 ? 12.01600  42.78900  -0.61400 1.000 76.75174  ? 131 PRO A N   1 
ATOM   1044 C CA  . PRO A 1 134 ? 12.44600  41.40000  -0.59000 1.000 76.62038  ? 131 PRO A CA  1 
ATOM   1045 C C   . PRO A 1 134 ? 11.96700  40.63800  0.64700  1.000 72.36501  ? 131 PRO A C   1 
ATOM   1046 O O   . PRO A 1 134 ? 11.71100  39.47300  0.53100  1.000 75.67473  ? 131 PRO A O   1 
ATOM   1047 C CB  . PRO A 1 134 ? 13.97600  41.54100  -0.64300 1.000 77.06948  ? 131 PRO A CB  1 
ATOM   1048 C CG  . PRO A 1 134 ? 14.21300  42.89300  -1.25100 1.000 73.51789  ? 131 PRO A CG  1 
ATOM   1049 C CD  . PRO A 1 134 ? 13.13000  43.73300  -0.61800 1.000 82.11064  ? 131 PRO A CD  1 
ATOM   1050 N N   . GLU A 1 135 ? 11.91000  41.30000  1.79300  1.000 69.83052  ? 132 GLU A N   1 
ATOM   1051 C CA  . GLU A 1 135 ? 11.55200  40.62400  3.06500  1.000 68.83826  ? 132 GLU A CA  1 
ATOM   1052 C C   . GLU A 1 135 ? 10.03700  40.54700  3.23300  1.000 63.14866  ? 132 GLU A C   1 
ATOM   1053 O O   . GLU A 1 135 ? 9.59700   40.14900  4.30700  1.000 60.96245  ? 132 GLU A O   1 
ATOM   1054 C CB  . GLU A 1 135 ? 12.17200  41.43100  4.19600  1.000 67.16057  ? 132 GLU A CB  1 
ATOM   1055 C CG  . GLU A 1 135 ? 11.66100  42.85700  4.25400  1.000 72.51988  ? 132 GLU A CG  1 
ATOM   1056 C CD  . GLU A 1 135 ? 12.63800  43.93400  3.82400  1.000 77.06905  ? 132 GLU A CD  1 
ATOM   1057 O OE1 . GLU A 1 135 ? 13.16200  43.84400  2.70000  1.000 73.28106  ? 132 GLU A OE1 1 
ATOM   1058 O OE2 . GLU A 1 135 ? 12.86100  44.86600  4.61400  1.000 84.68373  ? 132 GLU A OE2 1 
ATOM   1059 N N   . ALA A 1 136 ? 9.28500   40.87100  2.19300  1.000 56.21482  ? 133 ALA A N   1 
ATOM   1060 C CA  . ALA A 1 136 ? 7.80900   40.94900  2.28900  1.000 52.44997  ? 133 ALA A CA  1 
ATOM   1061 C C   . ALA A 1 136 ? 7.11900   39.61200  2.01600  1.000 47.93390  ? 133 ALA A C   1 
ATOM   1062 O O   . ALA A 1 136 ? 7.49500   38.95300  1.03100  1.000 58.71616  ? 133 ALA A O   1 
ATOM   1063 C CB  . ALA A 1 136 ? 7.30100   41.99700  1.33500  1.000 50.84658  ? 133 ALA A CB  1 
ATOM   1064 N N   . ILE A 1 137 ? 6.16000   39.22400  2.86400  1.000 51.61886  ? 134 ILE A N   1 
ATOM   1065 C CA  . ILE A 1 137 ? 5.33800   38.04900  2.59700  1.000 48.72737  ? 134 ILE A CA  1 
ATOM   1066 C C   . ILE A 1 137 ? 4.63100   38.29900  1.27300  1.000 44.22194  ? 134 ILE A C   1 
ATOM   1067 O O   . ILE A 1 137 ? 3.92600   39.30900  1.13600  1.000 44.67547  ? 134 ILE A O   1 
ATOM   1068 C CB  . ILE A 1 137 ? 4.33700   37.78400  3.73100  1.000 45.73190  ? 134 ILE A CB  1 
ATOM   1069 C CG1 . ILE A 1 137 ? 5.06800   37.61600  5.06300  1.000 48.66391  ? 134 ILE A CG1 1 
ATOM   1070 C CG2 . ILE A 1 137 ? 3.49400   36.55000  3.42400  1.000 43.52158  ? 134 ILE A CG2 1 
ATOM   1071 C CD1 . ILE A 1 137 ? 4.14100   37.36200  6.23400  1.000 42.50391  ? 134 ILE A CD1 1 
ATOM   1072 N N   . PRO A 1 138 ? 4.80100   37.43500  0.27300  1.000 49.61559  ? 135 PRO A N   1 
ATOM   1073 C CA  . PRO A 1 138 ? 4.18200   37.69000  -1.03200 1.000 48.68828  ? 135 PRO A CA  1 
ATOM   1074 C C   . PRO A 1 138 ? 2.67200   37.84100  -0.91500 1.000 49.01399  ? 135 PRO A C   1 
ATOM   1075 O O   . PRO A 1 138 ? 2.02700   37.20400  -0.07800 1.000 47.55287  ? 135 PRO A O   1 
ATOM   1076 C CB  . PRO A 1 138 ? 4.56500   36.45300  -1.85100 1.000 49.98737  ? 135 PRO A CB  1 
ATOM   1077 C CG  . PRO A 1 138 ? 5.81900   35.96200  -1.20700 1.000 53.76618  ? 135 PRO A CG  1 
ATOM   1078 C CD  . PRO A 1 138 ? 5.64300   36.22700  0.25900  1.000 48.88679  ? 135 PRO A CD  1 
ATOM   1079 N N   . LYS A 1 139 ? 2.11900   38.72100  -1.75500 1.000 50.76561  ? 136 LYS A N   1 
ATOM   1080 C CA  . LYS A 1 139 ? 0.67400   38.92000  -1.78600 1.000 48.98416  ? 136 LYS A CA  1 
ATOM   1081 C C   . LYS A 1 139 ? -0.05500  37.59900  -1.99000 1.000 50.39764  ? 136 LYS A C   1 
ATOM   1082 O O   . LYS A 1 139 ? -1.11800  37.36700  -1.40300 1.000 53.86886  ? 136 LYS A O   1 
ATOM   1083 C CB  . LYS A 1 139 ? 0.31000   39.91500  -2.89100 1.000 48.24154  ? 136 LYS A CB  1 
ATOM   1084 C CG  . LYS A 1 139 ? -1.16000  40.29500  -2.94400 1.000 55.70538  ? 136 LYS A CG  1 
ATOM   1085 C CD  . LYS A 1 139 ? -1.44300  41.24100  -4.10200 1.000 55.78734  ? 136 LYS A CD  1 
ATOM   1086 C CE  . LYS A 1 139 ? -2.91600  41.62300  -4.15700 1.000 69.92078  ? 136 LYS A CE  1 
ATOM   1087 N NZ  . LYS A 1 139 ? -3.21300  42.55600  -5.27900 1.000 73.46208  ? 136 LYS A NZ  1 
ATOM   1088 N N   . SER A 1 140 ? 0.52100   36.70800  -2.80000 1.000 53.37737  ? 137 SER A N   1 
ATOM   1089 C CA  . SER A 1 140 ? -0.08600  35.40000  -3.02800 1.000 58.36277  ? 137 SER A CA  1 
ATOM   1090 C C   . SER A 1 140 ? -0.00700  34.52200  -1.78300 1.000 56.80718  ? 137 SER A C   1 
ATOM   1091 O O   . SER A 1 140 ? -0.92500  33.73900  -1.51200 1.000 59.56329  ? 137 SER A O   1 
ATOM   1092 C CB  . SER A 1 140 ? 0.59100   34.71200  -4.21300 1.000 59.53077  ? 137 SER A CB  1 
ATOM   1093 O OG  . SER A 1 140 ? 1.98800   34.60500  -4.00100 1.000 64.28166  ? 137 SER A OG  1 
ATOM   1094 N N   . VAL A 1 141 ? 1.08200   34.62700  -1.01900 1.000 50.53993  ? 138 VAL A N   1 
ATOM   1095 C CA  . VAL A 1 141 ? 1.19000   33.84600  0.21000  1.000 50.89376  ? 138 VAL A CA  1 
ATOM   1096 C C   . VAL A 1 141 ? 0.22000   34.37300  1.25900  1.000 50.92730  ? 138 VAL A C   1 
ATOM   1097 O O   . VAL A 1 141 ? -0.42600  33.59600  1.97400  1.000 49.09560  ? 138 VAL A O   1 
ATOM   1098 C CB  . VAL A 1 141 ? 2.64100   33.84600  0.72700  1.000 50.02184  ? 138 VAL A CB  1 
ATOM   1099 C CG1 . VAL A 1 141 ? 2.73600   33.10900  2.05900  1.000 44.95984  ? 138 VAL A CG1 1 
ATOM   1100 C CG2 . VAL A 1 141 ? 3.56700   33.21300  -0.29700 1.000 49.83523  ? 138 VAL A CG2 1 
ATOM   1101 N N   . PHE A 1 142 ? 0.09300   35.69900  1.36300  1.000 44.57540  ? 139 PHE A N   1 
ATOM   1102 C CA  . PHE A 1 142 ? -0.84000  36.27700  2.32400  1.000 47.03391  ? 139 PHE A CA  1 
ATOM   1103 C C   . PHE A 1 142 ? -2.28200  35.92900  1.97100  1.000 46.86485  ? 139 PHE A C   1 
ATOM   1104 O O   . PHE A 1 142 ? -3.07100  35.56800  2.85100  1.000 46.20091  ? 139 PHE A O   1 
ATOM   1105 C CB  . PHE A 1 142 ? -0.65300  37.79200  2.39400  1.000 41.58648  ? 139 PHE A CB  1 
ATOM   1106 C CG  . PHE A 1 142 ? -1.49300  38.45700  3.44500  1.000 41.80416  ? 139 PHE A CG  1 
ATOM   1107 C CD1 . PHE A 1 142 ? -1.12200  38.41200  4.78000  1.000 41.49756  ? 139 PHE A CD1 1 
ATOM   1108 C CD2 . PHE A 1 142 ? -2.65400  39.12900  3.10200  1.000 47.54465  ? 139 PHE A CD2 1 
ATOM   1109 C CE1 . PHE A 1 142 ? -1.89400  39.02300  5.75100  1.000 39.33384  ? 139 PHE A CE1 1 
ATOM   1110 C CE2 . PHE A 1 142 ? -3.43000  39.74200  4.07200  1.000 41.76783  ? 139 PHE A CE2 1 
ATOM   1111 C CZ  . PHE A 1 142 ? -3.04900  39.68800  5.39600  1.000 34.94757  ? 139 PHE A CZ  1 
ATOM   1112 N N   . GLN A 1 143 ? -2.64000  36.02100  0.68600  1.000 62.44209  ? 140 GLN A N   1 
ATOM   1113 C CA  . GLN A 1 143 ? -3.99500  35.67800  0.26200  1.000 64.98429  ? 140 GLN A CA  1 
ATOM   1114 C C   . GLN A 1 143 ? -4.30700  34.20900  0.50600  1.000 61.64373  ? 140 GLN A C   1 
ATOM   1115 O O   . GLN A 1 143 ? -5.45600  33.86100  0.80100  1.000 66.01656  ? 140 GLN A O   1 
ATOM   1116 C CB  . GLN A 1 143 ? -4.18700  36.01800  -1.21700 1.000 66.90462  ? 140 GLN A CB  1 
ATOM   1117 C CG  . GLN A 1 143 ? -4.32700  37.50400  -1.50600 1.000 71.06187  ? 140 GLN A CG  1 
ATOM   1118 C CD  . GLN A 1 143 ? -4.30300  37.81000  -2.99100 1.000 81.98171  ? 140 GLN A CD  1 
ATOM   1119 O OE1 . GLN A 1 143 ? -3.73100  37.05900  -3.78300 1.000 73.24555  ? 140 GLN A OE1 1 
ATOM   1120 N NE2 . GLN A 1 143 ? -4.92900  38.91600  -3.37800 1.000 94.89683  ? 140 GLN A NE2 1 
ATOM   1121 N N   . GLU A 1 144 ? -3.30500  33.33600  0.38700  1.000 56.61427  ? 141 GLU A N   1 
ATOM   1122 C CA  . GLU A 1 144 ? -3.53000  31.91700  0.64100  1.000 59.40079  ? 141 GLU A CA  1 
ATOM   1123 C C   . GLU A 1 144 ? -3.82600  31.66500  2.11400  1.000 55.62745  ? 141 GLU A C   1 
ATOM   1124 O O   . GLU A 1 144 ? -4.69800  30.85400  2.44900  1.000 58.12795  ? 141 GLU A O   1 
ATOM   1125 C CB  . GLU A 1 144 ? -2.31800  31.10600  0.18400  1.000 64.02916  ? 141 GLU A CB  1 
ATOM   1126 C CG  . GLU A 1 144 ? -2.50100  29.60100  0.26900  1.000 70.30242  ? 141 GLU A CG  1 
ATOM   1127 C CD  . GLU A 1 144 ? -1.30900  28.84400  -0.27900 1.000 80.12829  ? 141 GLU A CD  1 
ATOM   1128 O OE1 . GLU A 1 144 ? -0.34800  29.50100  -0.73300 1.000 78.29516  ? 141 GLU A OE1 1 
ATOM   1129 O OE2 . GLU A 1 144 ? -1.33300  27.59500  -0.25900 1.000 77.25042  ? 141 GLU A OE2 1 
ATOM   1130 N N   . LEU A 1 145 ? -3.11000  32.35200  3.00600  1.000 52.43331  ? 142 LEU A N   1 
ATOM   1131 C CA  . LEU A 1 145 ? -3.40400  32.24700  4.43100  1.000 54.37790  ? 142 LEU A CA  1 
ATOM   1132 C C   . LEU A 1 145 ? -4.80700  32.75500  4.73900  1.000 55.66087  ? 142 LEU A C   1 
ATOM   1133 O O   . LEU A 1 145 ? -5.52200  32.16600  5.55800  1.000 54.99316  ? 142 LEU A O   1 
ATOM   1134 C CB  . LEU A 1 145 ? -2.36000  33.02200  5.23500  1.000 52.61417  ? 142 LEU A CB  1 
ATOM   1135 C CG  . LEU A 1 145 ? -0.91900  32.52100  5.11800  1.000 52.47928  ? 142 LEU A CG  1 
ATOM   1136 C CD1 . LEU A 1 145 ? 0.05400   33.57700  5.61200  1.000 44.12669  ? 142 LEU A CD1 1 
ATOM   1137 C CD2 . LEU A 1 145 ? -0.74600  31.22300  5.89400  1.000 46.26509  ? 142 LEU A CD2 1 
ATOM   1138 N N   . GLN A 1 146 ? -5.21900  33.84500  4.08400  1.000 46.12711  ? 143 GLN A N   1 
ATOM   1139 C CA  . GLN A 1 146 ? -6.56200  34.37800  4.28900  1.000 47.69997  ? 143 GLN A CA  1 
ATOM   1140 C C   . GLN A 1 146 ? -7.62400  33.33700  3.96400  1.000 51.18523  ? 143 GLN A C   1 
ATOM   1141 O O   . GLN A 1 146 ? -8.59000  33.16800  4.71800  1.000 50.70808  ? 143 GLN A O   1 
ATOM   1142 C CB  . GLN A 1 146 ? -6.76600  35.62700  3.43200  1.000 50.30126  ? 143 GLN A CB  1 
ATOM   1143 C CG  . GLN A 1 146 ? -5.79800  36.76100  3.72100  1.000 48.62718  ? 143 GLN A CG  1 
ATOM   1144 C CD  . GLN A 1 146 ? -6.45200  37.91100  4.45700  1.000 58.70957  ? 143 GLN A CD  1 
ATOM   1145 O OE1 . GLN A 1 146 ? -6.99500  38.83200  3.84100  1.000 62.81534  ? 143 GLN A OE1 1 
ATOM   1146 N NE2 . GLN A 1 146 ? -6.40500  37.86700  5.78200  1.000 53.17981  ? 143 GLN A NE2 1 
ATOM   1147 N N   . SER A 1 147 ? -7.45700  32.62100  2.84900  1.000 49.30784  ? 144 SER A N   1 
ATOM   1148 C CA  . SER A 1 147 ? -8.44600  31.62900  2.44700  1.000 50.85510  ? 144 SER A CA  1 
ATOM   1149 C C   . SER A 1 147 ? -8.44100  30.40500  3.35200  1.000 51.25530  ? 144 SER A C   1 
ATOM   1150 O O   . SER A 1 147 ? -9.45500  29.70300  3.42700  1.000 53.51471  ? 144 SER A O   1 
ATOM   1151 C CB  . SER A 1 147 ? -8.20500  31.20300  0.99700  1.000 52.74123  ? 144 SER A CB  1 
ATOM   1152 O OG  . SER A 1 147 ? -7.00700  30.45500  0.88400  1.000 54.78674  ? 144 SER A OG  1 
ATOM   1153 N N   . LYS A 1 148 ? -7.32600  30.12700  4.03200  1.000 52.70000  ? 145 LYS A N   1 
ATOM   1154 C CA  . LYS A 1 148 ? -7.28300  28.98900  4.94300  1.000 52.86772  ? 145 LYS A CA  1 
ATOM   1155 C C   . LYS A 1 148 ? -7.85900  29.33300  6.31100  1.000 57.10874  ? 145 LYS A C   1 
ATOM   1156 O O   . LYS A 1 148 ? -8.37800  28.44500  6.99800  1.000 59.13977  ? 145 LYS A O   1 
ATOM   1157 C CB  . LYS A 1 148 ? -5.84800  28.48100  5.08500  1.000 52.05577  ? 145 LYS A CB  1 
ATOM   1158 C CG  . LYS A 1 148 ? -5.27100  27.88900  3.80900  1.000 54.00272  ? 145 LYS A CG  1 
ATOM   1159 C CD  . LYS A 1 148 ? -3.79800  27.55500  3.96700  1.000 53.61324  ? 145 LYS A CD  1 
ATOM   1160 C CE  . LYS A 1 148 ? -3.26600  26.84300  2.73300  1.000 69.66927  ? 145 LYS A CE  1 
ATOM   1161 N NZ  . LYS A 1 148 ? -1.81400  26.53300  2.84600  1.000 70.28669  ? 145 LYS A NZ  1 
ATOM   1162 N N   . PHE A 1 149 ? -7.78100  30.60000  6.71500  1.000 43.92914  ? 146 PHE A N   1 
ATOM   1163 C CA  . PHE A 1 149 ? -8.32200  31.02400  7.99600  1.000 42.91688  ? 146 PHE A CA  1 
ATOM   1164 C C   . PHE A 1 149 ? -9.80600  30.66800  8.08900  1.000 49.02829  ? 146 PHE A C   1 
ATOM   1165 O O   . PHE A 1 149 ? -10.51700 30.66700  7.07900  1.000 52.10789  ? 146 PHE A O   1 
ATOM   1166 C CB  . PHE A 1 149 ? -8.13700  32.53000  8.18300  1.000 39.58993  ? 146 PHE A CB  1 
ATOM   1167 C CG  . PHE A 1 149 ? -6.70300  32.95400  8.35100  1.000 37.04798  ? 146 PHE A CG  1 
ATOM   1168 C CD1 . PHE A 1 149 ? -5.75900  32.07600  8.85500  1.000 37.65735  ? 146 PHE A CD1 1 
ATOM   1169 C CD2 . PHE A 1 149 ? -6.30100  34.23500  8.00600  1.000 34.62045  ? 146 PHE A CD2 1 
ATOM   1170 C CE1 . PHE A 1 149 ? -4.44200  32.46600  9.01100  1.000 35.99293  ? 146 PHE A CE1 1 
ATOM   1171 C CE2 . PHE A 1 149 ? -4.98400  34.63200  8.16100  1.000 32.85740  ? 146 PHE A CE2 1 
ATOM   1172 C CZ  . PHE A 1 149 ? -4.05400  33.74500  8.66400  1.000 34.09672  ? 146 PHE A CZ  1 
ATOM   1173 N N   . PRO A 1 150 ? -10.30000 30.36000  9.28800  1.000 59.21165  ? 147 PRO A N   1 
ATOM   1174 C CA  . PRO A 1 150 ? -11.69600 29.92100  9.41800  1.000 61.74409  ? 147 PRO A CA  1 
ATOM   1175 C C   . PRO A 1 150 ? -12.67300 31.03100  9.05000  1.000 62.06091  ? 147 PRO A C   1 
ATOM   1176 O O   . PRO A 1 150 ? -12.53900 32.17700  9.49000  1.000 58.14930  ? 147 PRO A O   1 
ATOM   1177 C CB  . PRO A 1 150 ? -11.80800 29.53100  10.89700 1.000 57.05018  ? 147 PRO A CB  1 
ATOM   1178 C CG  . PRO A 1 150 ? -10.73400 30.31600  11.57700 1.000 56.46946  ? 147 PRO A CG  1 
ATOM   1179 C CD  . PRO A 1 150 ? -9.60600  30.39200  10.58800 1.000 56.40328  ? 147 PRO A CD  1 
ATOM   1180 N N   . ASN A 1 151 ? -13.65900 30.67700  8.23100  1.000 65.31185  ? 148 ASN A N   1 
ATOM   1181 C CA  . ASN A 1 151 ? -14.71300 31.57900  7.80200  1.000 68.08885  ? 148 ASN A CA  1 
ATOM   1182 C C   . ASN A 1 151 ? -15.97700 31.32500  8.62700  1.000 74.86807  ? 148 ASN A C   1 
ATOM   1183 O O   . ASN A 1 151 ? -15.97300 30.55600  9.59300  1.000 74.23696  ? 148 ASN A O   1 
ATOM   1184 C CB  . ASN A 1 151 ? -14.95900 31.41000  6.30100  1.000 65.57649  ? 148 ASN A CB  1 
ATOM   1185 C CG  . ASN A 1 151 ? -15.11000 29.95800  5.89400  1.000 73.29677  ? 148 ASN A CG  1 
ATOM   1186 O OD1 . ASN A 1 151 ? -14.12100 29.24600  5.71000  1.000 77.32984  ? 148 ASN A OD1 1 
ATOM   1187 N ND2 . ASN A 1 151 ? -16.35100 29.51000  5.74800  1.000 79.32409  ? 148 ASN A ND2 1 
ATOM   1188 N N   . THR A 1 152 ? -17.07700 31.98300  8.24800  1.000 64.24728  ? 149 THR A N   1 
ATOM   1189 C CA  . THR A 1 152 ? -18.32500 31.81700  8.98800  1.000 59.36061  ? 149 THR A CA  1 
ATOM   1190 C C   . THR A 1 152 ? -18.86800 30.40000  8.84900  1.000 62.16978  ? 149 THR A C   1 
ATOM   1191 O O   . THR A 1 152 ? -19.39800 29.83600  9.81300  1.000 60.02053  ? 149 THR A O   1 
ATOM   1192 C CB  . THR A 1 152 ? -19.37000 32.82700  8.51300  1.000 61.85004  ? 149 THR A CB  1 
ATOM   1193 O OG1 . THR A 1 152 ? -20.50600 32.79100  9.38500  1.000 65.93946  ? 149 THR A OG1 1 
ATOM   1194 C CG2 . THR A 1 152 ? -19.81200 32.51900  7.09400  1.000 66.43123  ? 149 THR A CG2 1 
ATOM   1195 N N   . GLY A 1 153 ? -18.74600 29.81100  7.65900  1.000 65.81821  ? 150 GLY A N   1 
ATOM   1196 C CA  . GLY A 1 153 ? -19.28200 28.47600  7.44800  1.000 65.30312  ? 150 GLY A CA  1 
ATOM   1197 C C   . GLY A 1 153 ? -18.54900 27.41500  8.24600  1.000 61.79669  ? 150 GLY A C   1 
ATOM   1198 O O   . GLY A 1 153 ? -19.16600 26.47800  8.76100  1.000 59.65313  ? 150 GLY A O   1 
ATOM   1199 N N   . GLU A 1 154 ? -17.22500 27.54600  8.36300  1.000 65.41581  ? 151 GLU A N   1 
ATOM   1200 C CA  . GLU A 1 154 ? -16.45700 26.57200  9.13200  1.000 59.40641  ? 151 GLU A CA  1 
ATOM   1201 C C   . GLU A 1 154 ? -16.82500 26.62600  10.60900 1.000 58.84166  ? 151 GLU A C   1 
ATOM   1202 O O   . GLU A 1 154 ? -16.96000 25.58500  11.26100 1.000 59.47655  ? 151 GLU A O   1 
ATOM   1203 C CB  . GLU A 1 154 ? -14.95900 26.80800  8.94200  1.000 51.48006  ? 151 GLU A CB  1 
ATOM   1204 C CG  . GLU A 1 154 ? -14.09800 25.80700  9.69000  1.000 54.57963  ? 151 GLU A CG  1 
ATOM   1205 C CD  . GLU A 1 154 ? -12.62400 26.14500  9.64900  1.000 61.15587  ? 151 GLU A CD  1 
ATOM   1206 O OE1 . GLU A 1 154 ? -12.16700 26.73200  8.64500  1.000 65.70575  ? 151 GLU A OE1 1 
ATOM   1207 O OE2 . GLU A 1 154 ? -11.92200 25.82400  10.62900 1.000 54.46284  ? 151 GLU A OE2 1 
ATOM   1208 N N   . LEU A 1 155 ? -16.99000 27.83300  11.15500 1.000 53.53783  ? 152 LEU A N   1 
ATOM   1209 C CA  . LEU A 1 155 ? -17.41300 27.96200  12.54500 1.000 58.58689  ? 152 LEU A CA  1 
ATOM   1210 C C   . LEU A 1 155 ? -18.85100 27.50200  12.73700 1.000 56.75706  ? 152 LEU A C   1 
ATOM   1211 O O   . LEU A 1 155 ? -19.19400 26.97400  13.80200 1.000 55.83670  ? 152 LEU A O   1 
ATOM   1212 C CB  . LEU A 1 155 ? -17.24800 29.40700  13.01000 1.000 53.74904  ? 152 LEU A CB  1 
ATOM   1213 C CG  . LEU A 1 155 ? -15.80300 29.89800  13.09200 1.000 64.50822  ? 152 LEU A CG  1 
ATOM   1214 C CD1 . LEU A 1 155 ? -15.78100 31.38900  13.31400 1.000 70.71671  ? 152 LEU A CD1 1 
ATOM   1215 C CD2 . LEU A 1 155 ? -15.06600 29.18400  14.20800 1.000 62.42482  ? 152 LEU A CD2 1 
ATOM   1216 N N   . ASP A 1 156 ? -19.70300 27.69100  11.72700 1.000 55.06709  ? 153 ASP A N   1 
ATOM   1217 C CA  . ASP A 1 156 ? -21.07200 27.19800  11.82500 1.000 56.13502  ? 153 ASP A CA  1 
ATOM   1218 C C   . ASP A 1 156 ? -21.10900 25.67600  11.80400 1.000 53.73904  ? 153 ASP A C   1 
ATOM   1219 O O   . ASP A 1 156 ? -21.87600 25.05800  12.55200 1.000 55.48140  ? 153 ASP A O   1 
ATOM   1220 C CB  . ASP A 1 156 ? -21.92100 27.77800  10.69400 1.000 58.91071  ? 153 ASP A CB  1 
ATOM   1221 C CG  . ASP A 1 156 ? -22.39500 29.18900  10.98300 1.000 58.15156  ? 153 ASP A CG  1 
ATOM   1222 O OD1 . ASP A 1 156 ? -22.25000 29.64900  12.13500 1.000 65.37586  ? 153 ASP A OD1 1 
ATOM   1223 O OD2 . ASP A 1 156 ? -22.91400 29.84100  10.05300 1.000 64.77885  ? 153 ASP A OD2 1 
ATOM   1224 N N   . ARG A 1 157 ? -20.28400 25.05300  10.96000 1.000 41.63830  ? 154 ARG A N   1 
ATOM   1225 C CA  . ARG A 1 157 ? -20.23800 23.59600  10.91400 1.000 45.23020  ? 154 ARG A CA  1 
ATOM   1226 C C   . ARG A 1 157 ? -19.61600 23.02200  12.17800 1.000 41.35433  ? 154 ARG A C   1 
ATOM   1227 O O   . ARG A 1 157 ? -20.06000 21.97900  12.67300 1.000 42.62992  ? 154 ARG A O   1 
ATOM   1228 C CB  . ARG A 1 157 ? -19.46500 23.12900  9.68200  1.000 49.23043  ? 154 ARG A CB  1 
ATOM   1229 C CG  . ARG A 1 157 ? -20.23800 23.23600  8.38100  1.000 56.21269  ? 154 ARG A CG  1 
ATOM   1230 C CD  . ARG A 1 157 ? -19.43100 22.67700  7.22100  1.000 60.32982  ? 154 ARG A CD  1 
ATOM   1231 N NE  . ARG A 1 157 ? -18.18800 23.41200  7.02100  1.000 62.25898  ? 154 ARG A NE  1 
ATOM   1232 C CZ  . ARG A 1 157 ? -18.07100 24.49400  6.26300  1.000 65.95653  ? 154 ARG A CZ  1 
ATOM   1233 N NH1 . ARG A 1 157 ? -19.10800 24.99900  5.61400  1.000 65.32745  ? 154 ARG A NH1 1 
ATOM   1234 N NH2 . ARG A 1 157 ? -16.88500 25.08400  6.15400  1.000 60.04755  ? 154 ARG A NH2 1 
ATOM   1235 N N   . TYR A 1 158 ? -18.58100 23.68000  12.70800 1.000 46.89121  ? 155 TYR A N   1 
ATOM   1236 C CA  . TYR A 1 158 ? -17.96800 23.21700  13.94900 1.000 46.79187  ? 155 TYR A CA  1 
ATOM   1237 C C   . TYR A 1 158 ? -18.98400 23.20000  15.08500 1.000 50.79312  ? 155 TYR A C   1 
ATOM   1238 O O   . TYR A 1 158 ? -19.11300 22.20100  15.80400 1.000 45.27632  ? 155 TYR A O   1 
ATOM   1239 C CB  . TYR A 1 158 ? -16.77100 24.10000  14.30700 1.000 42.34160  ? 155 TYR A CB  1 
ATOM   1240 C CG  . TYR A 1 158 ? -16.18800 23.79800  15.67000 1.000 41.97099  ? 155 TYR A CG  1 
ATOM   1241 C CD1 . TYR A 1 158 ? -15.28300 22.75900  15.84500 1.000 41.74308  ? 155 TYR A CD1 1 
ATOM   1242 C CD2 . TYR A 1 158 ? -16.54900 24.54700  16.78300 1.000 44.25878  ? 155 TYR A CD2 1 
ATOM   1243 C CE1 . TYR A 1 158 ? -14.75300 22.47600  17.09000 1.000 43.85612  ? 155 TYR A CE1 1 
ATOM   1244 C CE2 . TYR A 1 158 ? -16.02500 24.27200  18.03400 1.000 44.31930  ? 155 TYR A CE2 1 
ATOM   1245 C CZ  . TYR A 1 158 ? -15.12700 23.23600  18.18200 1.000 45.24269  ? 155 TYR A CZ  1 
ATOM   1246 O OH  . TYR A 1 158 ? -14.60200 22.95900  19.42600 1.000 49.80383  ? 155 TYR A OH  1 
ATOM   1247 N N   . ALA A 1 159 ? -19.73100 24.29500  15.22600 1.000 42.37945  ? 156 ALA A N   1 
ATOM   1248 C CA  . ALA A 1 159 ? -20.72700 24.38800  16.31500 1.000 47.29805  ? 156 ALA A CA  1 
ATOM   1249 C C   . ALA A 1 159 ? -21.81100 23.32700  16.11500 1.000 48.80105  ? 156 ALA A C   1 
ATOM   1250 O O   . ALA A 1 159 ? -22.16300 22.65700  17.09700 1.000 51.32258  ? 156 ALA A O   1 
ATOM   1251 C CB  . ALA A 1 159 ? -21.30400 25.77600  16.37100 1.000 44.34580  ? 156 ALA A CB  1 
ATOM   1252 N N   . ASN A 1 160 ? -22.31200 23.18600  14.88800 1.000 44.51074  ? 157 ASN A N   1 
ATOM   1253 C CA  . ASN A 1 160 ? -23.39300 22.20700  14.60900 1.000 50.06014  ? 157 ASN A CA  1 
ATOM   1254 C C   . ASN A 1 160 ? -22.88500 20.78600  14.86600 1.000 51.31629  ? 157 ASN A C   1 
ATOM   1255 O O   . ASN A 1 160 ? -23.62700 20.00200  15.47100 1.000 59.30271  ? 157 ASN A O   1 
ATOM   1256 C CB  . ASN A 1 160 ? -23.94700 22.35800  13.19100 1.000 51.84719  ? 157 ASN A CB  1 
ATOM   1257 C CG  . ASN A 1 160 ? -25.09400 23.34200  13.11100 1.000 64.16766  ? 157 ASN A CG  1 
ATOM   1258 O OD1 . ASN A 1 160 ? -26.25400 22.94500  13.04000 1.000 67.45440  ? 157 ASN A OD1 1 
ATOM   1259 N ND2 . ASN A 1 160 ? -24.78000 24.62700  13.12600 1.000 60.77196  ? 157 ASN A ND2 1 
ATOM   1260 N N   . ALA A 1 161 ? -21.66400 20.48100  14.43000 1.000 47.19289  ? 158 ALA A N   1 
ATOM   1261 C CA  . ALA A 1 161 ? -21.09200 19.13100  14.62600 1.000 51.69033  ? 158 ALA A CA  1 
ATOM   1262 C C   . ALA A 1 161 ? -20.92100 18.85800  16.11900 1.000 49.22373  ? 158 ALA A C   1 
ATOM   1263 O O   . ALA A 1 161 ? -21.20400 17.73000  16.54500 1.000 48.40108  ? 158 ALA A O   1 
ATOM   1264 C CB  . ALA A 1 161 ? -19.77600 19.02100  13.90300 1.000 47.28807  ? 158 ALA A CB  1 
ATOM   1265 N N   . ARG A 1 162 ? -20.45700 19.85800  16.86800 1.000 57.77763  ? 159 ARG A N   1 
ATOM   1266 C CA  . ARG A 1 162 ? -20.23500 19.68600  18.32400 1.000 57.85179  ? 159 ARG A CA  1 
ATOM   1267 C C   . ARG A 1 162 ? -21.58100 19.40100  18.99700 1.000 61.23337  ? 159 ARG A C   1 
ATOM   1268 O O   . ARG A 1 162 ? -21.64300 18.46500  19.80400 1.000 61.30538  ? 159 ARG A O   1 
ATOM   1269 C CB  . ARG A 1 162 ? -19.56200 20.94100  18.88400 1.000 52.95468  ? 159 ARG A CB  1 
ATOM   1270 C CG  . ARG A 1 162 ? -19.09900 20.82200  20.32700 1.000 73.81549  ? 159 ARG A CG  1 
ATOM   1271 C CD  . ARG A 1 162 ? -17.67000 20.32700  20.42500 1.000 63.35406  ? 159 ARG A CD  1 
ATOM   1272 N NE  . ARG A 1 162 ? -17.43500 19.61800  21.67400 1.000 64.19378  ? 159 ARG A NE  1 
ATOM   1273 C CZ  . ARG A 1 162 ? -17.62900 18.31700  21.85000 1.000 73.07388  ? 159 ARG A CZ  1 
ATOM   1274 N NH1 . ARG A 1 162 ? -18.06300 17.56900  20.85000 1.000 70.22639  ? 159 ARG A NH1 1 
ATOM   1275 N NH2 . ARG A 1 162 ? -17.38600 17.76600  23.02500 1.000 76.52228  ? 159 ARG A NH2 1 
ATOM   1276 N N   . VAL A 1 163 ? -22.62600 20.14200  18.62100 1.000 49.97430  ? 160 VAL A N   1 
ATOM   1277 C CA  . VAL A 1 163 ? -23.98200 19.92700  19.20400 1.000 51.85070  ? 160 VAL A CA  1 
ATOM   1278 C C   . VAL A 1 163 ? -24.46800 18.52900  18.81500 1.000 52.05492  ? 160 VAL A C   1 
ATOM   1279 O O   . VAL A 1 163 ? -25.00000 17.82800  19.68900 1.000 53.29035  ? 160 VAL A O   1 
ATOM   1280 C CB  . VAL A 1 163 ? -24.96400 21.02700  18.75700 1.000 48.35624  ? 160 VAL A CB  1 
ATOM   1281 C CG1 . VAL A 1 163 ? -26.41400 20.63900  19.00100 1.000 51.87990  ? 160 VAL A CG1 1 
ATOM   1282 C CG2 . VAL A 1 163 ? -24.65100 22.36000  19.41800 1.000 45.71735  ? 160 VAL A CG2 1 
ATOM   1283 N N   . HIS A 1 164 ? -24.25000 18.13400  17.56000 1.000 47.11086  ? 161 HIS A N   1 
ATOM   1284 C CA  . HIS A 1 164 ? -24.69900 16.80200  17.08200 1.000 58.09327  ? 161 HIS A CA  1 
ATOM   1285 C C   . HIS A 1 164 ? -23.97300 15.70900  17.86400 1.000 56.09082  ? 161 HIS A C   1 
ATOM   1286 O O   . HIS A 1 164 ? -24.63800 14.75600  18.28200 1.000 58.01396  ? 161 HIS A O   1 
ATOM   1287 C CB  . HIS A 1 164 ? -24.44600 16.66500  15.57600 1.000 60.40654  ? 161 HIS A CB  1 
ATOM   1288 C CG  . HIS A 1 164 ? -24.57400 15.27000  15.06400 1.000 58.72221  ? 161 HIS A CG  1 
ATOM   1289 N ND1 . HIS A 1 164 ? -25.80000 14.67400  14.84800 1.000 64.09706  ? 161 HIS A ND1 1 
ATOM   1290 C CD2 . HIS A 1 164 ? -23.64200 14.35500  14.72100 1.000 65.36925  ? 161 HIS A CD2 1 
ATOM   1291 C CE1 . HIS A 1 164 ? -25.61800 13.45100  14.39700 1.000 60.54856  ? 161 HIS A CE1 1 
ATOM   1292 N NE2 . HIS A 1 164 ? -24.30300 13.23100  14.31100 1.000 72.90274  ? 161 HIS A NE2 1 
ATOM   1293 N N   . ALA A 1 165 ? -22.66800 15.87100  18.07600 1.000 58.47033  ? 162 ALA A N   1 
ATOM   1294 C CA  . ALA A 1 165 ? -21.87500 14.83000  18.76500 1.000 61.63237  ? 162 ALA A CA  1 
ATOM   1295 C C   . ALA A 1 165 ? -22.33200 14.72500  20.22000 1.000 59.19085  ? 162 ALA A C   1 
ATOM   1296 O O   . ALA A 1 165 ? -22.35900 13.60200  20.75000 1.000 66.17664  ? 162 ALA A O   1 
ATOM   1297 C CB  . ALA A 1 165 ? -20.40800 15.15700  18.67300 1.000 57.41301  ? 162 ALA A CB  1 
ATOM   1298 N N   . ILE A 1 166 ? -22.67100 15.85800  20.83400 1.000 50.12724  ? 163 ILE A N   1 
ATOM   1299 C CA  . ILE A 1 166 ? -23.10100 15.84000  22.22900 1.000 50.83325  ? 163 ILE A CA  1 
ATOM   1300 C C   . ILE A 1 166 ? -24.47300 15.18900  22.35700 1.000 49.79885  ? 163 ILE A C   1 
ATOM   1301 O O   . ILE A 1 166 ? -24.70300 14.35500  23.24200 1.000 49.60493  ? 163 ILE A O   1 
ATOM   1302 C CB  . ILE A 1 166 ? -23.08900 17.26500  22.81000 1.000 53.26385  ? 163 ILE A CB  1 
ATOM   1303 C CG1 . ILE A 1 166 ? -21.65600 17.78900  22.88900 1.000 48.74376  ? 163 ILE A CG1 1 
ATOM   1304 C CG2 . ILE A 1 166 ? -23.74200 17.29600  24.18100 1.000 48.45841  ? 163 ILE A CG2 1 
ATOM   1305 C CD1 . ILE A 1 166 ? -21.57000 19.27600  23.08300 1.000 53.35952  ? 163 ILE A CD1 1 
ATOM   1306 N N   . LEU A 1 167 ? -25.40500 15.55300  21.47300 1.000 49.89554  ? 164 LEU A N   1 
ATOM   1307 C CA  . LEU A 1 167 ? -26.73300 14.95000  21.51800 1.000 53.27565  ? 164 LEU A CA  1 
ATOM   1308 C C   . LEU A 1 167 ? -26.68100 13.47600  21.13600 1.000 51.83993  ? 164 LEU A C   1 
ATOM   1309 O O   . LEU A 1 167 ? -27.40800 12.65400  21.70700 1.000 51.35338  ? 164 LEU A O   1 
ATOM   1310 C CB  . LEU A 1 167 ? -27.69000 15.71600  20.60300 1.000 49.83565  ? 164 LEU A CB  1 
ATOM   1311 C CG  . LEU A 1 167 ? -28.10200 17.11500  21.06200 1.000 46.54065  ? 164 LEU A CG  1 
ATOM   1312 C CD1 . LEU A 1 167 ? -29.06000 17.74700  20.06600 1.000 47.92946  ? 164 LEU A CD1 1 
ATOM   1313 C CD2 . LEU A 1 167 ? -28.72900 17.06000  22.44700 1.000 48.47186  ? 164 LEU A CD2 1 
ATOM   1314 N N   . ALA A 1 168 ? -25.82800 13.12100  20.17400 1.000 57.47576  ? 165 ALA A N   1 
ATOM   1315 C CA  . ALA A 1 168 ? -25.69100 11.72000  19.79500 1.000 57.27001  ? 165 ALA A CA  1 
ATOM   1316 C C   . ALA A 1 168 ? -25.05800 10.90000  20.91200 1.000 55.72008  ? 165 ALA A C   1 
ATOM   1317 O O   . ALA A 1 168 ? -25.42900 9.73800   21.11100 1.000 55.66724  ? 165 ALA A O   1 
ATOM   1318 C CB  . ALA A 1 168 ? -24.87200 11.60200  18.50900 1.000 55.53076  ? 165 ALA A CB  1 
ATOM   1319 N N   . GLY A 1 169 ? -24.11100 11.48500  21.64900 1.000 53.09760  ? 166 GLY A N   1 
ATOM   1320 C CA  . GLY A 1 169 ? -23.49900 10.77500  22.75700 1.000 52.53607  ? 166 GLY A CA  1 
ATOM   1321 C C   . GLY A 1 169 ? -24.45900 10.51200  23.89700 1.000 55.55644  ? 166 GLY A C   1 
ATOM   1322 O O   . GLY A 1 169 ? -24.32600 9.50700   24.60200 1.000 57.66489  ? 166 GLY A O   1 
ATOM   1323 N N   . TYR A 1 170 ? -25.43300 11.40200  24.09600 1.000 49.70395  ? 167 TYR A N   1 
ATOM   1324 C CA  . TYR A 1 170 ? -26.45100 11.16200  25.11300 1.000 55.63995  ? 167 TYR A CA  1 
ATOM   1325 C C   . TYR A 1 170 ? -27.40400 10.05500  24.68000 1.000 56.76822  ? 167 TYR A C   1 
ATOM   1326 O O   . TYR A 1 170 ? -27.72800 9.16300   25.47100 1.000 54.33786  ? 167 TYR A O   1 
ATOM   1327 C CB  . TYR A 1 170 ? -27.20200 12.46200  25.41000 1.000 47.26637  ? 167 TYR A CB  1 
ATOM   1328 C CG  . TYR A 1 170 ? -28.69500 12.30500  25.64200 1.000 50.38875  ? 167 TYR A CG  1 
ATOM   1329 C CD1 . TYR A 1 170 ? -29.18900 11.79300  26.83800 1.000 48.16931  ? 167 TYR A CD1 1 
ATOM   1330 C CD2 . TYR A 1 170 ? -29.61000 12.69100  24.67000 1.000 49.61138  ? 167 TYR A CD2 1 
ATOM   1331 C CE1 . TYR A 1 170 ? -30.55200 11.65600  27.05000 1.000 47.54025  ? 167 TYR A CE1 1 
ATOM   1332 C CE2 . TYR A 1 170 ? -30.97500 12.56000  24.87400 1.000 53.97333  ? 167 TYR A CE2 1 
ATOM   1333 C CZ  . TYR A 1 170 ? -31.44100 12.04100  26.06500 1.000 52.19954  ? 167 TYR A CZ  1 
ATOM   1334 O OH  . TYR A 1 170 ? -32.80000 11.90900  26.27000 1.000 53.28288  ? 167 TYR A OH  1 
ATOM   1335 N N   . LEU A 1 171 ? -27.84300 10.08300  23.41900 1.000 48.90056  ? 168 LEU A N   1 
ATOM   1336 C CA  . LEU A 1 171 ? -28.75700 9.05800   22.93000 1.000 52.15416  ? 168 LEU A CA  1 
ATOM   1337 C C   . LEU A 1 171 ? -28.07400 7.69900   22.83600 1.000 58.32518  ? 168 LEU A C   1 
ATOM   1338 O O   . LEU A 1 171 ? -28.67100 6.67400   23.18800 1.000 60.61025  ? 168 LEU A O   1 
ATOM   1339 C CB  . LEU A 1 171 ? -29.32300 9.47100   21.57400 1.000 50.58572  ? 168 LEU A CB  1 
ATOM   1340 C CG  . LEU A 1 171 ? -30.29100 10.65600  21.58400 1.000 54.50913  ? 168 LEU A CG  1 
ATOM   1341 C CD1 . LEU A 1 171 ? -30.52400 11.17600  20.17600 1.000 50.67407  ? 168 LEU A CD1 1 
ATOM   1342 C CD2 . LEU A 1 171 ? -31.61100 10.25800  22.23300 1.000 48.47206  ? 168 LEU A CD2 1 
ATOM   1343 N N   . ASP A 1 172 ? -26.82400 7.66500   22.36500 1.000 57.34153  ? 169 ASP A N   1 
ATOM   1344 C CA  . ASP A 1 172 ? -26.12600 6.39000   22.22400 1.000 57.87469  ? 169 ASP A CA  1 
ATOM   1345 C C   . ASP A 1 172 ? -25.82500 5.76900   23.58200 1.000 59.16968  ? 169 ASP A C   1 
ATOM   1346 O O   . ASP A 1 172 ? -25.98900 4.55700   23.76500 1.000 59.46583  ? 169 ASP A O   1 
ATOM   1347 C CB  . ASP A 1 172 ? -24.84000 6.57600   21.42000 1.000 60.17256  ? 169 ASP A CB  1 
ATOM   1348 C CG  . ASP A 1 172 ? -25.10400 6.80900   19.94500 1.000 66.41554  ? 169 ASP A CG  1 
ATOM   1349 O OD1 . ASP A 1 172 ? -26.19700 6.43100   19.47100 1.000 63.97771  ? 169 ASP A OD1 1 
ATOM   1350 O OD2 . ASP A 1 172 ? -24.21900 7.36400   19.25900 1.000 64.57433  ? 169 ASP A OD2 1 
ATOM   1351 N N   . GLY A 1 173 ? -25.37800 6.57800   24.54400 1.000 59.29143  ? 170 GLY A N   1 
ATOM   1352 C CA  . GLY A 1 173 ? -25.16200 6.06300   25.88500 1.000 55.56090  ? 170 GLY A CA  1 
ATOM   1353 C C   . GLY A 1 173 ? -26.45100 5.61100   26.54400 1.000 58.72862  ? 170 GLY A C   1 
ATOM   1354 O O   . GLY A 1 173 ? -26.47400 4.60500   27.25900 1.000 62.28339  ? 170 GLY A O   1 
ATOM   1355 N N   . MET A 1 174 ? -27.54200 6.33500   26.28400 1.000 60.61441  ? 171 MET A N   1 
ATOM   1356 C CA  . MET A 1 174 ? -28.86200 5.93100   26.83600 1.000 62.35897  ? 171 MET A CA  1 
ATOM   1357 C C   . MET A 1 174 ? -29.22700 4.55600   26.27200 1.000 69.60618  ? 171 MET A C   1 
ATOM   1358 O O   . MET A 1 174 ? -29.63500 3.68400   27.06000 1.000 68.25227  ? 171 MET A O   1 
ATOM   1359 C CB  . MET A 1 174 ? -29.95100 6.93500   26.45100 1.000 58.54818  ? 171 MET A CB  1 
ATOM   1360 C CG  . MET A 1 174 ? -31.32300 6.57800   26.98600 1.000 68.87917  ? 171 MET A CG  1 
ATOM   1361 S SD  . MET A 1 174 ? -32.52200 7.91000   26.73500 1.000 64.88109  ? 171 MET A SD  1 
ATOM   1362 C CE  . MET A 1 174 ? -34.02300 7.10600   27.29300 1.000 67.14721  ? 171 MET A CE  1 
ATOM   1363 N N   . LYS A 1 175 ? -29.07800 4.37600   24.95700 1.000 66.70504  ? 172 LYS A N   1 
ATOM   1364 C CA  . LYS A 1 175 ? -29.43900 3.08900   24.30800 1.000 70.14637  ? 172 LYS A CA  1 
ATOM   1365 C C   . LYS A 1 175 ? -28.54700 1.97000   24.85600 1.000 71.10402  ? 172 LYS A C   1 
ATOM   1366 O O   . LYS A 1 175 ? -29.07800 0.88100   25.13000 1.000 72.77301  ? 172 LYS A O   1 
ATOM   1367 C CB  . LYS A 1 175 ? -29.36500 3.23100   22.78300 1.000 69.30517  ? 172 LYS A CB  1 
ATOM   1368 C CG  . LYS A 1 175 ? -29.77900 2.01100   21.97100 1.000 82.29043  ? 172 LYS A CG  1 
ATOM   1369 C CD  . LYS A 1 175 ? -29.72400 2.24700   20.47700 1.000 78.61381  ? 172 LYS A CD  1 
ATOM   1370 C CE  . LYS A 1 175 ? -30.11100 1.02800   19.66900 1.000 91.82294  ? 172 LYS A CE  1 
ATOM   1371 N NZ  . LYS A 1 175 ? -30.04700 1.29300   18.21300 1.000 94.34787  ? 172 LYS A NZ  1 
ATOM   1372 N N   . ASP A 1 176 ? -27.24900 2.24000   25.02600 1.000 67.54903  ? 173 ASP A N   1 
ATOM   1373 C CA  . ASP A 1 176 ? -26.30700 1.21100   25.53700 1.000 72.15057  ? 173 ASP A CA  1 
ATOM   1374 C C   . ASP A 1 176 ? -26.69700 0.82000   26.96600 1.000 74.48349  ? 173 ASP A C   1 
ATOM   1375 O O   . ASP A 1 176 ? -26.71100 -0.38600  27.25800 1.000 75.58595  ? 173 ASP A O   1 
ATOM   1376 C CB  . ASP A 1 176 ? -24.85800 1.69400   25.46000 1.000 73.97668  ? 173 ASP A CB  1 
ATOM   1377 C CG  . ASP A 1 176 ? -24.32300 1.74900   24.04000 1.000 84.98010  ? 173 ASP A CG  1 
ATOM   1378 O OD1 . ASP A 1 176 ? -24.83600 0.99300   23.19400 1.000 88.18978  ? 173 ASP A OD1 1 
ATOM   1379 O OD2 . ASP A 1 176 ? -23.40100 2.55100   23.79300 1.000 92.93694  ? 173 ASP A OD2 1 
ATOM   1380 N N   . ALA A 1 177 ? -27.02400 1.80500   27.80700 1.000 66.38598  ? 174 ALA A N   1 
ATOM   1381 C CA  . ALA A 1 177 ? -27.41200 1.52400   29.20800 1.000 64.92156  ? 174 ALA A CA  1 
ATOM   1382 C C   . ALA A 1 177 ? -28.70300 0.70300   29.22200 1.000 62.77658  ? 174 ALA A C   1 
ATOM   1383 O O   . ALA A 1 177 ? -28.79600 -0.23900  30.02900 1.000 70.56329  ? 174 ALA A O   1 
ATOM   1384 C CB  . ALA A 1 177 ? -27.57100 2.81500   29.97100 1.000 58.27141  ? 174 ALA A CB  1 
ATOM   1385 N N   . ARG A 1 178 ? -29.65500 1.05400   28.35400 1.000 52.18722  ? 175 ARG A N   1 
ATOM   1386 C CA  . ARG A 1 178 ? -30.93400 0.30400   28.26900 1.000 59.46591  ? 175 ARG A CA  1 
ATOM   1387 C C   . ARG A 1 178 ? -30.63700 -1.12900  27.82000 1.000 67.12798  ? 175 ARG A C   1 
ATOM   1388 O O   . ARG A 1 178 ? -31.21700 -2.05600  28.40600 1.000 67.16218  ? 175 ARG A O   1 
ATOM   1389 C CB  . ARG A 1 178 ? -31.87700 1.00900   27.29000 1.000 59.47839  ? 175 ARG A CB  1 
ATOM   1390 C CG  . ARG A 1 178 ? -33.17100 0.26200   27.00600 1.000 63.63435  ? 175 ARG A CG  1 
ATOM   1391 C CD  . ARG A 1 178 ? -33.57900 0.37700   25.55000 1.000 60.07250  ? 175 ARG A CD  1 
ATOM   1392 N NE  . ARG A 1 178 ? -33.32500 1.70400   25.01100 1.000 73.57692  ? 175 ARG A NE  1 
ATOM   1393 C CZ  . ARG A 1 178 ? -33.21000 1.98300   23.71800 1.000 74.61474  ? 175 ARG A CZ  1 
ATOM   1394 N NH1 . ARG A 1 178 ? -33.32500 1.02000   22.82100 1.000 71.96970  ? 175 ARG A NH1 1 
ATOM   1395 N NH2 . ARG A 1 178 ? -32.97900 3.22400   23.32600 1.000 68.63667  ? 175 ARG A NH2 1 
ATOM   1396 N N   . GLU A 1 179 ? -29.73800 -1.29700  26.84900 1.000 66.36407  ? 176 GLU A N   1 
ATOM   1397 C CA  . GLU A 1 179 ? -29.43500 -2.64600  26.30400 1.000 65.00872  ? 176 GLU A CA  1 
ATOM   1398 C C   . GLU A 1 179 ? -28.83600 -3.52700  27.40500 1.000 66.48332  ? 176 GLU A C   1 
ATOM   1399 O O   . GLU A 1 179 ? -29.23600 -4.70200  27.49600 1.000 68.52373  ? 176 GLU A O   1 
ATOM   1400 C CB  . GLU A 1 179 ? -28.49600 -2.53100  25.10300 1.000 62.67181  ? 176 GLU A CB  1 
ATOM   1401 C CG  . GLU A 1 179 ? -29.22400 -2.30600  23.79200 1.000 64.39397  ? 176 GLU A CG  1 
ATOM   1402 C CD  . GLU A 1 179 ? -28.39600 -1.62000  22.72000 1.000 69.95498  ? 176 GLU A CD  1 
ATOM   1403 O OE1 . GLU A 1 179 ? -27.23400 -1.27200  23.00600 1.000 73.31868  ? 176 GLU A OE1 1 
ATOM   1404 O OE2 . GLU A 1 179 ? -28.91500 -1.43600  21.60200 1.000 71.16677  ? 176 GLU A OE2 1 
ATOM   1405 N N   . ARG A 1 180 ? -27.91300 -2.98000  28.20100 1.000 82.61901  ? 177 ARG A N   1 
ATOM   1406 C CA  . ARG A 1 180 ? -27.28400 -3.75800  29.26300 1.000 85.97697  ? 177 ARG A CA  1 
ATOM   1407 C C   . ARG A 1 180 ? -28.30200 -4.16100  30.32100 1.000 84.27647  ? 177 ARG A C   1 
ATOM   1408 O O   . ARG A 1 180 ? -28.25300 -5.28100  30.84300 1.000 89.72737  ? 177 ARG A O   1 
ATOM   1409 C CB  . ARG A 1 180 ? -26.14100 -2.96400  29.89100 1.000 81.26770  ? 177 ARG A CB  1 
ATOM   1410 C CG  . ARG A 1 180 ? -25.03800 -2.63300  28.91300 1.000 83.92659  ? 177 ARG A CG  1 
ATOM   1411 C CD  . ARG A 1 180 ? -24.18200 -1.48600  29.41200 1.000 92.38571  ? 177 ARG A CD  1 
ATOM   1412 N NE  . ARG A 1 180 ? -23.53800 -0.79200  28.30500 1.000 105.05717 ? 177 ARG A NE  1 
ATOM   1413 C CZ  . ARG A 1 180 ? -22.33900 -1.09500  27.82600 1.000 103.27061 ? 177 ARG A CZ  1 
ATOM   1414 N NH1 . ARG A 1 180 ? -21.60700 -2.06100  28.35500 1.000 85.77199  ? 177 ARG A NH1 1 
ATOM   1415 N NH2 . ARG A 1 180 ? -21.86500 -0.41100  26.78800 1.000 93.70921  ? 177 ARG A NH2 1 
ATOM   1416 N N   . TYR A 1 181 ? -29.23600 -3.26300  30.64600 1.000 63.64388  ? 178 TYR A N   1 
ATOM   1417 C CA  . TYR A 1 181 ? -30.29200 -3.60800  31.59100 1.000 65.70775  ? 178 TYR A CA  1 
ATOM   1418 C C   . TYR A 1 181 ? -31.21800 -4.67000  31.01300 1.000 66.49421  ? 178 TYR A C   1 
ATOM   1419 O O   . TYR A 1 181 ? -31.62400 -5.60100  31.71700 1.000 61.65790  ? 178 TYR A O   1 
ATOM   1420 C CB  . TYR A 1 181 ? -31.07700 -2.35400  31.97900 1.000 53.35184  ? 178 TYR A CB  1 
ATOM   1421 C CG  . TYR A 1 181 ? -32.16700 -2.60100  32.99800 1.000 58.12020  ? 178 TYR A CG  1 
ATOM   1422 C CD1 . TYR A 1 181 ? -31.93600 -3.39900  34.11100 1.000 58.86744  ? 178 TYR A CD1 1 
ATOM   1423 C CD2 . TYR A 1 181 ? -33.42200 -2.02500  32.85500 1.000 51.77180  ? 178 TYR A CD2 1 
ATOM   1424 C CE1 . TYR A 1 181 ? -32.92800 -3.62800  35.04600 1.000 55.99878  ? 178 TYR A CE1 1 
ATOM   1425 C CE2 . TYR A 1 181 ? -34.42200 -2.24400  33.78800 1.000 55.79752  ? 178 TYR A CE2 1 
ATOM   1426 C CZ  . TYR A 1 181 ? -34.16800 -3.04600  34.88200 1.000 56.34579  ? 178 TYR A CZ  1 
ATOM   1427 O OH  . TYR A 1 181 ? -35.15700 -3.26900  35.81200 1.000 65.38889  ? 178 TYR A OH  1 
ATOM   1428 N N   . GLU A 1 182 ? -31.55200 -4.55500  29.72500 1.000 65.12181  ? 179 GLU A N   1 
ATOM   1429 C CA  . GLU A 1 182 ? -32.44200 -5.52300  29.09500 1.000 65.79470  ? 179 GLU A CA  1 
ATOM   1430 C C   . GLU A 1 182 ? -31.78300 -6.88200  28.90200 1.000 65.69945  ? 179 GLU A C   1 
ATOM   1431 O O   . GLU A 1 182 ? -32.48700 -7.86600  28.64900 1.000 71.25151  ? 179 GLU A O   1 
ATOM   1432 C CB  . GLU A 1 182 ? -32.93300 -4.98400  27.75200 1.000 62.43356  ? 179 GLU A CB  1 
ATOM   1433 C CG  . GLU A 1 182 ? -33.89200 -3.81400  27.87600 1.000 65.00255  ? 179 GLU A CG  1 
ATOM   1434 C CD  . GLU A 1 182 ? -34.30100 -3.25400  26.53000 1.000 65.30884  ? 179 GLU A CD  1 
ATOM   1435 O OE1 . GLU A 1 182 ? -33.48400 -3.32400  25.58600 1.000 71.90555  ? 179 GLU A OE1 1 
ATOM   1436 O OE2 . GLU A 1 182 ? -35.43800 -2.74800  26.41300 1.000 59.91069  ? 179 GLU A OE2 1 
ATOM   1437 N N   . HIS A 1 183 ? -30.45200 -6.95400  29.00900 1.000 69.48289  ? 180 HIS A N   1 
ATOM   1438 C CA  . HIS A 1 183 ? -29.76800 -8.24200  28.96100 1.000 74.55958  ? 180 HIS A CA  1 
ATOM   1439 C C   . HIS A 1 183 ? -30.14200 -9.11400  30.15700 1.000 75.22934  ? 180 HIS A C   1 
ATOM   1440 O O   . HIS A 1 183 ? -30.07800 -10.34800 30.07600 1.000 73.14598  ? 180 HIS A O   1 
ATOM   1441 C CB  . HIS A 1 183 ? -28.25500 -8.01300  28.87800 1.000 70.30948  ? 180 HIS A CB  1 
ATOM   1442 C CG  . HIS A 1 183 ? -27.44100 -9.01600  29.63700 1.000 81.17002  ? 180 HIS A CG  1 
ATOM   1443 N ND1 . HIS A 1 183 ? -27.12400 -10.25800 29.13000 1.000 88.01099  ? 180 HIS A ND1 1 
ATOM   1444 C CD2 . HIS A 1 183 ? -26.86500 -8.95300  30.86100 1.000 82.35748  ? 180 HIS A CD2 1 
ATOM   1445 C CE1 . HIS A 1 183 ? -26.39700 -10.92000 30.01200 1.000 88.24775  ? 180 HIS A CE1 1 
ATOM   1446 N NE2 . HIS A 1 183 ? -26.22500 -10.15100 31.07200 1.000 81.88299  ? 180 HIS A NE2 1 
ATOM   1447 N N   . TYR A 1 184 ? -30.60700 -8.47700  31.23500 1.000 69.44144  ? 181 TYR A N   1 
ATOM   1448 C CA  . TYR A 1 184 ? -31.06500 -9.23500  32.42900 1.000 70.32280  ? 181 TYR A CA  1 
ATOM   1449 C C   . TYR A 1 184 ? -32.59500 -9.29600  32.43300 1.000 72.85881  ? 181 TYR A C   1 
ATOM   1450 O O   . TYR A 1 184 ? -33.16300 -9.77400  33.43200 1.000 76.28723  ? 181 TYR A O   1 
ATOM   1451 C CB  . TYR A 1 184 ? -30.63400 -8.52800  33.71600 1.000 70.80239  ? 181 TYR A CB  1 
ATOM   1452 C CG  . TYR A 1 184 ? -29.15700 -8.27300  33.87000 1.000 72.09069  ? 181 TYR A CG  1 
ATOM   1453 C CD1 . TYR A 1 184 ? -28.29600 -9.27900  34.27400 1.000 72.46536  ? 181 TYR A CD1 1 
ATOM   1454 C CD2 . TYR A 1 184 ? -28.62300 -7.01500  33.64600 1.000 64.70053  ? 181 TYR A CD2 1 
ATOM   1455 C CE1 . TYR A 1 184 ? -26.93900 -9.04800  34.43200 1.000 69.40811  ? 181 TYR A CE1 1 
ATOM   1456 C CE2 . TYR A 1 184 ? -27.27000 -6.76700  33.79700 1.000 62.68421  ? 181 TYR A CE2 1 
ATOM   1457 C CZ  . TYR A 1 184 ? -26.42400 -7.78700  34.19200 1.000 64.02598  ? 181 TYR A CZ  1 
ATOM   1458 O OH  . TYR A 1 184 ? -25.08900 -7.55100  34.34400 1.000 72.09134  ? 181 TYR A OH  1 
ATOM   1459 N N   . LEU A 1 185 ? -33.24200 -8.83100  31.36100 1.000 60.58628  ? 182 LEU A N   1 
ATOM   1460 C CA  . LEU A 1 185 ? -34.72900 -8.76400  31.34500 1.000 57.66100  ? 182 LEU A CA  1 
ATOM   1461 C C   . LEU A 1 185 ? -35.29600 -9.69100  30.26700 1.000 60.77673  ? 182 LEU A C   1 
ATOM   1462 O O   . LEU A 1 185 ? -34.79500 -9.64500  29.13100 1.000 66.42477  ? 182 LEU A O   1 
ATOM   1463 C CB  . LEU A 1 185 ? -35.15700 -7.31900  31.07600 1.000 59.56291  ? 182 LEU A CB  1 
ATOM   1464 C CG  . LEU A 1 185 ? -34.98300 -6.33800  32.23300 1.000 57.86768  ? 182 LEU A CG  1 
ATOM   1465 C CD1 . LEU A 1 185 ? -35.68500 -5.02700  31.92300 1.000 52.76166  ? 182 LEU A CD1 1 
ATOM   1466 C CD2 . LEU A 1 185 ? -35.50900 -6.92800  33.53200 1.000 54.13331  ? 182 LEU A CD2 1 
ATOM   1467 N N   . ASN A 1 186 ? -36.29500 -10.50500 30.61800 1.000 63.19206  ? 183 ASN A N   1 
ATOM   1468 C CA  . ASN A 1 186 ? -36.96100 -11.38500 29.61900 1.000 64.76588  ? 183 ASN A CA  1 
ATOM   1469 C C   . ASN A 1 186 ? -37.67400 -10.51900 28.57500 1.000 68.84550  ? 183 ASN A C   1 
ATOM   1470 O O   . ASN A 1 186 ? -37.61600 -10.87100 27.38100 1.000 78.53048  ? 183 ASN A O   1 
ATOM   1471 C CB  . ASN A 1 186 ? -37.93400 -12.36100 30.28500 1.000 65.35074  ? 183 ASN A CB  1 
ATOM   1472 C CG  . ASN A 1 186 ? -38.50500 -13.38100 29.32300 1.000 69.41305  ? 183 ASN A CG  1 
ATOM   1473 O OD1 . ASN A 1 186 ? -37.79500 -13.89300 28.46100 1.000 72.83308  ? 183 ASN A OD1 1 
ATOM   1474 N ND2 . ASN A 1 186 ? -39.78500 -13.68100 29.46300 1.000 69.45249  ? 183 ASN A ND2 1 
ATOM   1475 N N   . ARG A 1 187 ? -38.31100 -9.42700  29.00800 1.000 120.45191 ? 184 ARG A N   1 
ATOM   1476 C CA  . ARG A 1 187 ? -39.08800 -8.56700  28.07500 1.000 119.83250 ? 184 ARG A CA  1 
ATOM   1477 C C   . ARG A 1 187 ? -38.34600 -7.24700  27.84700 1.000 105.75044 ? 184 ARG A C   1 
ATOM   1478 O O   . ARG A 1 187 ? -37.93600 -6.62300  28.84400 1.000 107.90819 ? 184 ARG A O   1 
ATOM   1479 C CB  . ARG A 1 187 ? -40.48700 -8.30700  28.64200 1.000 120.64683 ? 184 ARG A CB  1 
ATOM   1480 C CG  . ARG A 1 187 ? -41.37700 -7.45300  27.75000 1.000 127.48802 ? 184 ARG A CG  1 
ATOM   1481 C CD  . ARG A 1 187 ? -42.75800 -7.24500  28.34300 1.000 125.99975 ? 184 ARG A CD  1 
ATOM   1482 N NE  . ARG A 1 187 ? -43.61400 -6.42900  27.49500 1.000 128.75337 ? 184 ARG A NE  1 
ATOM   1483 C CZ  . ARG A 1 187 ? -43.64400 -5.10200  27.51500 1.000 128.86515 ? 184 ARG A CZ  1 
ATOM   1484 N NH1 . ARG A 1 187 ? -42.86100 -4.43400  28.34500 1.000 118.58301 ? 184 ARG A NH1 1 
ATOM   1485 N NH2 . ARG A 1 187 ? -44.45700 -4.44600  26.70500 1.000 128.74023 ? 184 ARG A NH2 1 
HETATM 1486 S S   . SO4 B 2 .   ? -0.56300  57.22100  12.88500 1.000 129.75890 ? 201 SO4 A S   1 
HETATM 1487 O O1  . SO4 B 2 .   ? 0.61900   56.51400  12.39600 1.000 88.83890  ? 201 SO4 A O1  1 
HETATM 1488 O O2  . SO4 B 2 .   ? -1.23300  57.86700  11.75800 1.000 98.07890  ? 201 SO4 A O2  1 
HETATM 1489 O O3  . SO4 B 2 .   ? -1.47500  56.27000  13.52100 1.000 72.24890  ? 201 SO4 A O3  1 
HETATM 1490 O O4  . SO4 B 2 .   ? -0.16100  58.23300  13.86000 1.000 114.18890 ? 201 SO4 A O4  1 
HETATM 1491 S S   . SO4 C 2 .   ? -17.74200 27.84800  3.20900  1.000 129.28890 ? 202 SO4 A S   1 
HETATM 1492 O O1  . SO4 C 2 .   ? -16.31900 27.58600  3.01300  1.000 100.29890 ? 202 SO4 A O1  1 
HETATM 1493 O O2  . SO4 C 2 .   ? -18.51300 27.14100  2.18900  1.000 123.75890 ? 202 SO4 A O2  1 
HETATM 1494 O O3  . SO4 C 2 .   ? -18.14600 27.38200  4.53300  1.000 109.53890 ? 202 SO4 A O3  1 
HETATM 1495 O O4  . SO4 C 2 .   ? -17.99600 29.28200  3.10300  1.000 107.15890 ? 202 SO4 A O4  1 
HETATM 1496 O O   . HOH D 3 .   ? -5.45700  38.53100  2.23400  1.000 56.29890  ? 301 HOH A O   1 
HETATM 1497 O O   . HOH D 3 .   ? -22.55700 29.00100  7.92900  1.000 54.67890  ? 302 HOH A O   1 
HETATM 1498 O O   . HOH D 3 .   ? -9.74100  60.36100  1.26100  1.000 45.94890  ? 303 HOH A O   1 
HETATM 1499 O O   . HOH D 3 .   ? -14.09600 38.52300  13.64200 1.000 56.98890  ? 304 HOH A O   1 
HETATM 1500 O O   . HOH D 3 .   ? 2.00800   43.46500  -3.88400 1.000 54.16890  ? 305 HOH A O   1 
HETATM 1501 O O   . HOH D 3 .   ? -7.62900  63.74000  19.49900 1.000 42.64890  ? 306 HOH A O   1 
HETATM 1502 O O   . HOH D 3 .   ? 8.92800   46.74200  18.70900 1.000 50.50890  ? 307 HOH A O   1 
HETATM 1503 O O   . HOH D 3 .   ? -2.81100  52.98700  20.25600 1.000 44.85890  ? 308 HOH A O   1 
HETATM 1504 O O   . HOH D 3 .   ? -4.30700  42.26600  12.90000 1.000 39.24890  ? 309 HOH A O   1 
HETATM 1505 O O   . HOH D 3 .   ? -4.54100  49.94100  0.08700  1.000 54.75890  ? 310 HOH A O   1 
HETATM 1506 O O   . HOH D 3 .   ? -11.97400 56.34300  6.55500  1.000 36.72890  ? 311 HOH A O   1 
HETATM 1507 O O   . HOH D 3 .   ? -10.932   67.450    12.447   1.000 36.91890  ? 312 HOH A O   1 
HETATM 1508 O O   . HOH D 3 .   ? -14.36500 46.79700  20.89600 1.000 53.08890  ? 313 HOH A O   1 
HETATM 1509 O O   . HOH D 3 .   ? -36.93700 -16.60800 28.40900 1.000 46.62890  ? 314 HOH A O   1 
HETATM 1510 O O   . HOH D 3 .   ? -16.55300 47.91900  18.34500 1.000 56.39890  ? 315 HOH A O   1 
HETATM 1511 O O   . HOH D 3 .   ? -12.12600 34.63500  7.97900  1.000 51.83890  ? 316 HOH A O   1 
HETATM 1512 O O   . HOH D 3 .   ? 10.36600  37.22800  1.87800  1.000 57.24890  ? 317 HOH A O   1 
HETATM 1513 O O   . HOH D 3 .   ? 8.11300   52.66100  2.56000  1.000 68.39890  ? 318 HOH A O   1 
HETATM 1514 O O   . HOH D 3 .   ? 2.13800   52.66900  -8.81300 1.000 61.22890  ? 319 HOH A O   1 
HETATM 1515 O O   . HOH D 3 .   ? -40.17700 -5.87100  30.78700 1.000 63.66890  ? 320 HOH A O   1 
HETATM 1516 O O   . HOH D 3 .   ? -25.91400 27.02300  11.55700 1.000 61.78890  ? 321 HOH A O   1 
HETATM 1517 O O   . HOH D 3 .   ? 4.17800   51.29400  17.57300 1.000 48.01890  ? 322 HOH A O   1 
HETATM 1518 O O   . HOH D 3 .   ? -21.93100 20.70600  10.49900 1.000 55.19890  ? 323 HOH A O   1 
HETATM 1519 O O   . HOH D 3 .   ? -1.47100  52.26900  23.78800 1.000 48.25890  ? 324 HOH A O   1 
HETATM 1520 O O   . HOH D 3 .   ? -32.43800 -11.39100 27.90300 1.000 53.60890  ? 325 HOH A O   1 
HETATM 1521 O O   . HOH D 3 .   ? -21.08300 11.01000  19.40600 1.000 48.40890  ? 326 HOH A O   1 
HETATM 1522 O O   . HOH D 3 .   ? -14.71500 63.54700  10.20100 1.000 42.82890  ? 327 HOH A O   1 
HETATM 1523 O O   . HOH D 3 .   ? -35.498   10.221    27.710   1.000 50.89890  ? 328 HOH A O   1 
HETATM 1524 O O   . HOH D 3 .   ? -16.71500 38.80600  13.05800 1.000 66.47890  ? 329 HOH A O   1 
HETATM 1525 O O   . HOH D 3 .   ? -38.67200 -2.49000  28.47700 1.000 55.82890  ? 330 HOH A O   1 
HETATM 1526 O O   . HOH D 3 .   ? -37.10700 -1.22900  29.85400 1.000 58.72890  ? 331 HOH A O   1 
HETATM 1527 O O   . HOH D 3 .   ? -12.64400 65.10900  10.67600 0.500 57.79890  ? 332 HOH A O   1 
HETATM 1528 O O   . HOH D 3 .   ? -39.50300 -0.32000  27.91500 1.000 57.49890  ? 333 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 4   ? 1.18201 1.34145 1.18482 -0.31243 0.06876  -0.24761 1   MET A N   
2    C CA  . MET A 4   ? 1.17356 1.30917 1.14572 -0.31304 0.04798  -0.25765 1   MET A CA  
3    C C   . MET A 4   ? 1.19187 1.26132 1.11873 -0.26323 0.03431  -0.22437 1   MET A C   
4    O O   . MET A 4   ? 1.06862 1.15112 1.00116 -0.22369 0.02314  -0.20086 1   MET A O   
5    C CB  . MET A 4   ? 1.14283 1.39477 1.15209 -0.31451 0.01167  -0.28381 1   MET A CB  
6    C CG  . MET A 4   ? 1.18375 1.41774 1.15864 -0.32424 -0.00591 -0.30164 1   MET A CG  
7    S SD  . MET A 4   ? 1.43312 1.58579 1.38700 -0.37262 0.03377  -0.31669 1   MET A SD  
8    C CE  . MET A 4   ? 1.31744 1.40359 1.21090 -0.34938 0.01863  -0.31074 1   MET A CE  
9    N N   . LEU A 5   ? 0.96825 0.96727 0.85091 -0.26707 0.03757  -0.22476 2   LEU A N   
10   C CA  . LEU A 5   ? 0.82476 0.76965 0.66986 -0.22614 0.02749  -0.19690 2   LEU A CA  
11   C C   . LEU A 5   ? 0.86721 0.84198 0.69999 -0.21447 -0.00090 -0.20512 2   LEU A C   
12   O O   . LEU A 5   ? 0.94384 0.92095 0.76493 -0.24275 -0.00085 -0.23218 2   LEU A O   
13   C CB  . LEU A 5   ? 0.83962 0.68141 0.64051 -0.22966 0.05694  -0.18583 2   LEU A CB  
14   C CG  . LEU A 5   ? 0.85315 0.65285 0.65038 -0.23172 0.08652  -0.17046 2   LEU A CG  
15   C CD1 . LEU A 5   ? 0.94359 0.64432 0.68964 -0.21921 0.11066  -0.15330 2   LEU A CD1 
16   C CD2 . LEU A 5   ? 0.90375 0.74292 0.72198 -0.19908 0.07204  -0.14975 2   LEU A CD2 
17   N N   . GLN A 6   ? 0.83102 0.82276 0.66091 -0.17394 -0.02260 -0.18252 3   GLN A N   
18   C CA  . GLN A 6   ? 0.75353 0.76994 0.56470 -0.15590 -0.04702 -0.18308 3   GLN A CA  
19   C C   . GLN A 6   ? 0.73000 0.69117 0.51193 -0.12410 -0.04607 -0.15304 3   GLN A C   
20   O O   . GLN A 6   ? 0.79466 0.74750 0.58679 -0.10211 -0.04636 -0.13143 3   GLN A O   
21   C CB  . GLN A 6   ? 0.78816 0.89568 0.62794 -0.13759 -0.07415 -0.18644 3   GLN A CB  
22   C CG  . GLN A 6   ? 0.99703 1.18544 0.87392 -0.17043 -0.07979 -0.22120 3   GLN A CG  
23   C CD  . GLN A 6   ? 1.14315 1.43290 1.05130 -0.14183 -0.10766 -0.22149 3   GLN A CD  
24   O OE1 . GLN A 6   ? 1.10410 1.39011 1.01121 -0.09922 -0.11418 -0.19349 3   GLN A OE1 
25   N NE2 . GLN A 6   ? 1.11545 1.49728 1.05040 -0.16410 -0.12383 -0.25475 3   GLN A NE2 
26   N N   . PHE A 7   ? 0.71696 0.64200 0.46326 -0.12461 -0.04273 -0.15481 4   PHE A N   
27   C CA  . PHE A 7   ? 0.72616 0.60766 0.44976 -0.09897 -0.03837 -0.12861 4   PHE A CA  
28   C C   . PHE A 7   ? 0.67728 0.58601 0.38329 -0.07665 -0.05722 -0.11916 4   PHE A C   
29   O O   . PHE A 7   ? 0.75325 0.69451 0.44344 -0.08258 -0.06961 -0.13725 4   PHE A O   
30   C CB  . PHE A 7   ? 0.68930 0.51244 0.38377 -0.10732 -0.01701 -0.13262 4   PHE A CB  
31   C CG  . PHE A 7   ? 0.82201 0.60179 0.52069 -0.11942 0.00588  -0.13361 4   PHE A CG  
32   C CD1 . PHE A 7   ? 0.79060 0.56008 0.48969 -0.15088 0.01860  -0.15765 4   PHE A CD1 
33   C CD2 . PHE A 7   ? 0.68606 0.43535 0.38519 -0.09971 0.01607  -0.11081 4   PHE A CD2 
34   C CE1 . PHE A 7   ? 0.84549 0.56253 0.53846 -0.15920 0.04489  -0.15396 4   PHE A CE1 
35   C CE2 . PHE A 7   ? 0.74640 0.45434 0.43965 -0.10328 0.03699  -0.10795 4   PHE A CE2 
36   C CZ  . PHE A 7   ? 0.84167 0.52693 0.52818 -0.13139 0.05342  -0.12707 4   PHE A CZ  
37   N N   . SER A 8   ? 0.62276 0.51684 0.32787 -0.05277 -0.05819 -0.09259 5   SER A N   
38   C CA  . SER A 8   ? 0.64678 0.55048 0.32658 -0.02885 -0.06938 -0.07708 5   SER A CA  
39   C C   . SER A 8   ? 0.65183 0.50967 0.31988 -0.01922 -0.05417 -0.05301 5   SER A C   
40   O O   . SER A 8   ? 0.61389 0.44950 0.30317 -0.02657 -0.04277 -0.04896 5   SER A O   
41   C CB  . SER A 8   ? 0.64807 0.58951 0.34159 -0.00854 -0.08632 -0.07017 5   SER A CB  
42   O OG  . SER A 8   ? 0.63450 0.54540 0.34162 0.00278  -0.07875 -0.05083 5   SER A OG  
43   N N   . PHE A 9   ? 0.73976 0.58837 0.37432 -0.00419 -0.05307 -0.03842 6   PHE A N   
44   C CA  . PHE A 9   ? 0.77262 0.58369 0.40213 -0.00040 -0.03502 -0.01603 6   PHE A CA  
45   C C   . PHE A 9   ? 0.80513 0.60188 0.42468 0.01831  -0.03755 0.00606  6   PHE A C   
46   O O   . PHE A 9   ? 0.86017 0.66333 0.44365 0.03877  -0.04515 0.01524  6   PHE A O   
47   C CB  . PHE A 9   ? 0.76625 0.56514 0.36062 0.00091  -0.02143 -0.01252 6   PHE A CB  
48   C CG  . PHE A 9   ? 0.87077 0.66734 0.46540 -0.01254 -0.01227 -0.03224 6   PHE A CG  
49   C CD1 . PHE A 9   ? 0.85954 0.64942 0.48711 -0.02391 -0.00656 -0.04037 6   PHE A CD1 
50   C CD2 . PHE A 9   ? 0.86586 0.66037 0.41995 -0.01023 -0.00731 -0.04202 6   PHE A CD2 
51   C CE1 . PHE A 9   ? 0.80569 0.58019 0.42494 -0.03035 0.00597  -0.05529 6   PHE A CE1 
52   C CE2 . PHE A 9   ? 0.93345 0.71261 0.48105 -0.01999 0.00515  -0.06109 6   PHE A CE2 
53   C CZ  . PHE A 9   ? 0.86693 0.63269 0.44677 -0.02884 0.01286  -0.06633 6   PHE A CZ  
54   N N   . VAL A 10  ? 0.65479 0.42908 0.29953 0.01345  -0.03073 0.01370  7   VAL A N   
55   C CA  . VAL A 10  ? 0.69626 0.43612 0.32436 0.02923  -0.02590 0.03464  7   VAL A CA  
56   C C   . VAL A 10  ? 0.74106 0.44438 0.36948 0.01221  -0.00182 0.04708  7   VAL A C   
57   O O   . VAL A 10  ? 0.72484 0.43246 0.38940 -0.00835 0.00278  0.03696  7   VAL A O   
58   C CB  . VAL A 10  ? 0.75804 0.49636 0.41066 0.03462  -0.03444 0.02923  7   VAL A CB  
59   C CG1 . VAL A 10  ? 0.74149 0.42987 0.36905 0.05370  -0.02577 0.04952  7   VAL A CG1 
60   C CG2 . VAL A 10  ? 0.66013 0.45027 0.32598 0.04507  -0.05494 0.01325  7   VAL A CG2 
61   N N   . SER A 11  ? 0.94988 0.62377 0.53937 0.02057  0.01364  0.06797  8   SER A N   
62   C CA  . SER A 11  ? 0.97258 0.62150 0.56774 -0.00165 0.04142  0.07819  8   SER A CA  
63   C C   . SER A 11  ? 0.88558 0.57630 0.51092 -0.01809 0.04366  0.06196  8   SER A C   
64   O O   . SER A 11  ? 0.88765 0.60063 0.49382 -0.00771 0.03687  0.05495  8   SER A O   
65   C CB  . SER A 11  ? 1.02333 0.63639 0.64094 -0.01949 0.05246  0.07999  8   SER A CB  
66   O OG  . SER A 11  ? 1.13426 0.71587 0.74537 -0.03973 0.08308  0.09440  8   SER A OG  
67   N N   . ASN A 12  ? 0.79678 0.49830 0.46502 -0.04085 0.05265  0.05473  9   ASN A N   
68   C CA  . ASN A 12  ? 0.77246 0.51557 0.46931 -0.04788 0.05544  0.04185  9   ASN A CA  
69   C C   . ASN A 12  ? 0.83655 0.60110 0.56214 -0.04720 0.03530  0.02364  9   ASN A C   
70   O O   . ASN A 12  ? 0.81048 0.60397 0.56100 -0.04956 0.03776  0.01517  9   ASN A O   
71   C CB  . ASN A 12  ? 0.97818 0.73699 0.70426 -0.06827 0.07881  0.04636  9   ASN A CB  
72   C CG  . ASN A 12  ? 1.02670 0.78202 0.72525 -0.06505 0.10383  0.06080  9   ASN A CG  
73   O OD1 . ASN A 12  ? 1.07033 0.80881 0.72172 -0.04581 0.10140  0.06659  9   ASN A OD1 
74   N ND2 . ASN A 12  ? 1.17379 0.95125 0.90167 -0.08447 0.12831  0.06489  9   ASN A ND2 
75   N N   . ASP A 13  ? 0.75015 0.50147 0.47036 -0.04074 0.01849  0.01975  10  ASP A N   
76   C CA  . ASP A 13  ? 0.66557 0.43342 0.40907 -0.04091 0.00374  0.00451  10  ASP A CA  
77   C C   . ASP A 13  ? 0.69386 0.47085 0.42222 -0.03099 -0.00655 -0.00475 10  ASP A C   
78   O O   . ASP A 13  ? 0.65515 0.42902 0.36174 -0.02166 -0.01420 -0.00232 10  ASP A O   
79   C CB  . ASP A 13  ? 0.73341 0.48444 0.48582 -0.04325 -0.00392 0.00276  10  ASP A CB  
80   C CG  . ASP A 13  ? 0.84336 0.59011 0.61800 -0.06223 0.00444  0.00114  10  ASP A CG  
81   O OD1 . ASP A 13  ? 0.95498 0.73272 0.75208 -0.07175 0.01004  -0.00267 10  ASP A OD1 
82   O OD2 . ASP A 13  ? 0.88926 0.60338 0.65851 -0.06695 0.00585  0.00191  10  ASP A OD2 
83   N N   . VAL A 14  ? 0.66360 0.45171 0.40162 -0.03273 -0.00562 -0.01542 11  VAL A N   
84   C CA  . VAL A 14  ? 0.63721 0.42741 0.36278 -0.03239 -0.01085 -0.02858 11  VAL A CA  
85   C C   . VAL A 14  ? 0.61955 0.41663 0.36151 -0.03423 -0.02122 -0.03502 11  VAL A C   
86   O O   . VAL A 14  ? 0.61666 0.41203 0.37485 -0.03463 -0.01992 -0.03394 11  VAL A O   
87   C CB  . VAL A 14  ? 0.68223 0.46366 0.40118 -0.03245 0.00191  -0.03544 11  VAL A CB  
88   C CG1 . VAL A 14  ? 0.61506 0.38738 0.31874 -0.04053 0.00170  -0.05244 11  VAL A CG1 
89   C CG2 . VAL A 14  ? 0.62865 0.40794 0.33384 -0.02663 0.01538  -0.02888 11  VAL A CG2 
90   N N   . VAL A 15  ? 0.62199 0.43398 0.35992 -0.03375 -0.03132 -0.04249 12  VAL A N   
91   C CA  . VAL A 15  ? 0.65244 0.47897 0.40926 -0.03303 -0.03846 -0.04805 12  VAL A CA  
92   C C   . VAL A 15  ? 0.70927 0.55266 0.47145 -0.04689 -0.03658 -0.06554 12  VAL A C   
93   O O   . VAL A 15  ? 0.66391 0.52377 0.41563 -0.05329 -0.04108 -0.07629 12  VAL A O   
94   C CB  . VAL A 15  ? 0.66038 0.49862 0.41528 -0.01694 -0.04993 -0.04097 12  VAL A CB  
95   C CG1 . VAL A 15  ? 0.67640 0.53430 0.45136 -0.01135 -0.05479 -0.04728 12  VAL A CG1 
96   C CG2 . VAL A 15  ? 0.70295 0.50923 0.44690 -0.00921 -0.04522 -0.02415 12  VAL A CG2 
97   N N   . MET A 16  ? 0.70349 0.54194 0.47843 -0.05333 -0.02860 -0.06945 13  MET A N   
98   C CA  . MET A 16  ? 0.60268 0.45253 0.38451 -0.07256 -0.02055 -0.08604 13  MET A CA  
99   C C   . MET A 16  ? 0.68459 0.57410 0.49224 -0.07008 -0.02656 -0.09056 13  MET A C   
100  O O   . MET A 16  ? 0.63679 0.51627 0.44938 -0.05984 -0.02284 -0.08225 13  MET A O   
101  C CB  . MET A 16  ? 0.61363 0.42208 0.38343 -0.07999 0.00019  -0.08429 13  MET A CB  
102  C CG  . MET A 16  ? 0.65629 0.45535 0.42254 -0.10654 0.01638  -0.10177 13  MET A CG  
103  S SD  . MET A 16  ? 0.75577 0.51799 0.51475 -0.11221 0.04301  -0.09569 13  MET A SD  
104  C CE  . MET A 16  ? 0.86007 0.67634 0.65202 -0.10476 0.03144  -0.09422 13  MET A CE  
105  N N   . THR A 17  ? 0.58574 0.52485 0.40889 -0.07716 -0.03617 -0.10495 14  THR A N   
106  C CA  . THR A 17  ? 0.64627 0.63710 0.49925 -0.07029 -0.04135 -0.11006 14  THR A CA  
107  C C   . THR A 17  ? 0.64806 0.65810 0.52231 -0.10074 -0.02364 -0.12750 14  THR A C   
108  O O   . THR A 17  ? 0.65002 0.66626 0.52424 -0.12992 -0.01824 -0.14567 14  THR A O   
109  C CB  . THR A 17  ? 0.64976 0.69902 0.51095 -0.05388 -0.06380 -0.11443 14  THR A CB  
110  O OG1 . THR A 17  ? 0.68329 0.70108 0.51798 -0.02527 -0.07355 -0.09402 14  THR A OG1 
111  C CG2 . THR A 17  ? 0.64813 0.76134 0.54450 -0.04084 -0.06814 -0.12002 14  THR A CG2 
112  N N   . TYR A 18  ? 0.58625 0.60122 0.47513 -0.09609 -0.01160 -0.12331 15  TYR A N   
113  C CA  . TYR A 18  ? 0.64555 0.67540 0.55343 -0.12526 0.01180  -0.13627 15  TYR A CA  
114  C C   . TYR A 18  ? 0.56959 0.68815 0.52307 -0.12263 0.00602  -0.14898 15  TYR A C   
115  O O   . TYR A 18  ? 0.55928 0.69817 0.52034 -0.08909 -0.00259 -0.13881 15  TYR A O   
116  C CB  . TYR A 18  ? 0.59259 0.56597 0.47848 -0.12053 0.03439  -0.12125 15  TYR A CB  
117  C CG  . TYR A 18  ? 0.66411 0.63934 0.56040 -0.15067 0.06582  -0.12993 15  TYR A CG  
118  C CD1 . TYR A 18  ? 0.71202 0.66578 0.60413 -0.18957 0.08441  -0.14402 15  TYR A CD1 
119  C CD2 . TYR A 18  ? 0.63541 0.62710 0.54127 -0.14184 0.08102  -0.12472 15  TYR A CD2 
120  C CE1 . TYR A 18  ? 0.78512 0.73053 0.68395 -0.22242 0.11946  -0.15132 15  TYR A CE1 
121  C CE2 . TYR A 18  ? 0.78151 0.77199 0.69439 -0.17135 0.11554  -0.13031 15  TYR A CE2 
122  C CZ  . TYR A 18  ? 0.78925 0.75493 0.69941 -0.21335 0.13574  -0.14289 15  TYR A CZ  
123  O OH  . TYR A 18  ? 0.90293 0.85790 0.81755 -0.24777 0.17608  -0.14789 15  TYR A OH  
124  N N   . ASP A 19  ? 0.65290 0.82460 0.63735 -0.15849 0.01330  -0.17297 16  ASP A N   
125  C CA  . ASP A 19  ? 0.71312 0.98969 0.75176 -0.15876 0.00943  -0.18850 16  ASP A CA  
126  C C   . ASP A 19  ? 0.61917 0.90055 0.68001 -0.19672 0.04665  -0.19848 16  ASP A C   
127  O O   . ASP A 19  ? 0.64193 0.99966 0.74567 -0.19076 0.05229  -0.20469 16  ASP A O   
128  C CB  . ASP A 19  ? 0.76038 1.11982 0.82429 -0.16840 -0.01728 -0.21169 16  ASP A CB  
129  C CG  . ASP A 19  ? 0.83321 1.30938 0.94535 -0.13955 -0.03628 -0.21831 16  ASP A CG  
130  O OD1 . ASP A 19  ? 0.79526 1.28178 0.92151 -0.11321 -0.02513 -0.20560 16  ASP A OD1 
131  O OD2 . ASP A 19  ? 0.76572 1.32343 0.89780 -0.13993 -0.06237 -0.23654 16  ASP A OD2 
132  N N   . GLU A 24  ? 1.03593 1.56854 1.28943 -0.32503 0.18876  -0.25280 21  GLU A N   
133  C CA  . GLU A 24  ? 0.99882 1.47464 1.22596 -0.32197 0.23345  -0.23179 21  GLU A CA  
134  C C   . GLU A 24  ? 1.03050 1.50579 1.23778 -0.25143 0.21629  -0.20875 21  GLU A C   
135  O O   . GLU A 24  ? 1.03902 1.54564 1.25118 -0.20933 0.17359  -0.20770 21  GLU A O   
136  C CB  . GLU A 24  ? 1.06512 1.39072 1.21482 -0.33953 0.25761  -0.21276 21  GLU A CB  
137  C CG  . GLU A 24  ? 1.11940 1.36248 1.20859 -0.29204 0.22237  -0.19079 21  GLU A CG  
138  C CD  . GLU A 24  ? 1.19615 1.32083 1.22531 -0.31214 0.23357  -0.18205 21  GLU A CD  
139  O OE1 . GLU A 24  ? 1.26108 1.38937 1.30198 -0.34722 0.22583  -0.20332 21  GLU A OE1 
140  O OE2 . GLU A 24  ? 1.24600 1.27769 1.21439 -0.28950 0.24950  -0.15500 21  GLU A OE2 
141  N N   . GLN A 25  ? 1.14950 1.59212 1.33385 -0.23999 0.25143  -0.19268 22  GLN A N   
142  C CA  . GLN A 25  ? 1.09164 1.51415 1.24394 -0.17537 0.23704  -0.17392 22  GLN A CA  
143  C C   . GLN A 25  ? 1.16644 1.47120 1.24523 -0.15460 0.21432  -0.15447 22  GLN A C   
144  O O   . GLN A 25  ? 1.15026 1.36529 1.17566 -0.16822 0.23926  -0.13947 22  GLN A O   
145  C CB  . GLN A 25  ? 1.00147 1.42407 1.14491 -0.17176 0.28234  -0.16552 22  GLN A CB  
146  C CG  . GLN A 25  ? 1.11193 1.66318 1.32431 -0.15250 0.28876  -0.17997 22  GLN A CG  
147  C CD  . GLN A 25  ? 1.18466 1.85862 1.48500 -0.19895 0.29241  -0.20781 22  GLN A CD  
148  O OE1 . GLN A 25  ? 1.16297 1.82912 1.47711 -0.26233 0.32416  -0.21753 22  GLN A OE1 
149  N NE2 . GLN A 25  ? 1.12214 1.91110 1.48090 -0.16716 0.26042  -0.22199 22  GLN A NE2 
150  N N   . ILE A 26  ? 0.85683 1.16476 0.93283 -0.12239 0.17093  -0.15388 23  ILE A N   
151  C CA  . ILE A 26  ? 0.81640 1.02741 0.83390 -0.10856 0.14886  -0.13867 23  ILE A CA  
152  C C   . ILE A 26  ? 0.83854 0.99450 0.80785 -0.06731 0.14807  -0.12287 23  ILE A C   
153  O O   . ILE A 26  ? 0.79557 0.88309 0.72128 -0.05405 0.12983  -0.11199 23  ILE A O   
154  C CB  . ILE A 26  ? 0.80378 1.04344 0.83882 -0.09715 0.10827  -0.14531 23  ILE A CB  
155  C CG1 . ILE A 26  ? 0.72604 1.04468 0.79661 -0.05734 0.08882  -0.15036 23  ILE A CG1 
156  C CG2 . ILE A 26  ? 0.74748 1.01448 0.80857 -0.14334 0.10792  -0.16235 23  ILE A CG2 
157  C CD1 . ILE A 26  ? 0.81536 1.12011 0.87110 -0.02798 0.05148  -0.14444 23  ILE A CD1 
158  N N   . ILE A 27  ? 0.78690 0.97794 0.76574 -0.04896 0.16750  -0.12460 24  ILE A N   
159  C CA  . ILE A 27  ? 0.80231 0.94270 0.73086 -0.01119 0.16871  -0.11535 24  ILE A CA  
160  C C   . ILE A 27  ? 0.79528 0.84977 0.66105 -0.02123 0.18107  -0.10060 24  ILE A C   
161  O O   . ILE A 27  ? 0.80764 0.81265 0.62741 0.00517  0.16584  -0.09534 24  ILE A O   
162  C CB  . ILE A 27  ? 0.84672 1.04410 0.79620 0.00743  0.19488  -0.12187 24  ILE A CB  
163  C CG1 . ILE A 27  ? 0.99821 1.14185 0.88981 0.04487  0.19843  -0.11741 24  ILE A CG1 
164  C CG2 . ILE A 27  ? 0.81757 1.05173 0.79246 -0.03168 0.23737  -0.12359 24  ILE A CG2 
165  C CD1 . ILE A 27  ? 0.94524 1.07257 0.82699 0.08429  0.16690  -0.12265 24  ILE A CD1 
166  N N   . TRP A 28  ? 0.83924 0.87623 0.70163 -0.05740 0.20769  -0.09510 25  TRP A N   
167  C CA  . TRP A 28  ? 0.88990 0.84432 0.68531 -0.05647 0.22212  -0.07684 25  TRP A CA  
168  C C   . TRP A 28  ? 0.84502 0.74946 0.60893 -0.04091 0.18652  -0.07034 25  TRP A C   
169  O O   . TRP A 28  ? 0.90313 0.75594 0.61077 -0.02171 0.18517  -0.05765 25  TRP A O   
170  C CB  . TRP A 28  ? 0.85573 0.78539 0.64875 -0.09782 0.26040  -0.07064 25  TRP A CB  
171  C CG  . TRP A 28  ? 1.02922 0.95177 0.84618 -0.12683 0.24593  -0.07797 25  TRP A CG  
172  C CD1 . TRP A 28  ? 0.97723 0.96697 0.85827 -0.15601 0.23839  -0.09911 25  TRP A CD1 
173  C CD2 . TRP A 28  ? 0.99216 0.84075 0.76659 -0.12599 0.23638  -0.06603 25  TRP A CD2 
174  N NE1 . TRP A 28  ? 0.97606 0.93127 0.85184 -0.17590 0.22561  -0.10243 25  TRP A NE1 
175  C CE2 . TRP A 28  ? 1.03561 0.90240 0.84741 -0.15697 0.22599  -0.08157 25  TRP A CE2 
176  C CE3 . TRP A 28  ? 0.92101 0.69675 0.62924 -0.09896 0.23502  -0.04469 25  TRP A CE3 
177  C CZ2 . TRP A 28  ? 1.01124 0.81771 0.79416 -0.16140 0.21806  -0.07610 25  TRP A CZ2 
178  C CZ3 . TRP A 28  ? 0.99441 0.71866 0.67996 -0.10101 0.22607  -0.03776 25  TRP A CZ3 
179  C CH2 . TRP A 28  ? 0.98276 0.71848 0.70450 -0.13191 0.21951  -0.05322 25  TRP A CH2 
180  N N   . VAL A 29  ? 0.73295 0.65968 0.53278 -0.04763 0.15791  -0.07930 26  VAL A N   
181  C CA  . VAL A 29  ? 0.69027 0.57730 0.46714 -0.03542 0.12668  -0.07383 26  VAL A CA  
182  C C   . VAL A 29  ? 0.66716 0.54533 0.42056 -0.00272 0.10697  -0.07545 26  VAL A C   
183  O O   . VAL A 29  ? 0.63966 0.47793 0.35131 0.00926  0.09818  -0.06790 26  VAL A O   
184  C CB  . VAL A 29  ? 0.66422 0.57905 0.48072 -0.04802 0.10382  -0.08283 26  VAL A CB  
185  C CG1 . VAL A 29  ? 0.62976 0.50816 0.42555 -0.03709 0.07721  -0.07667 26  VAL A CG1 
186  C CG2 . VAL A 29  ? 0.68596 0.61398 0.52616 -0.08534 0.12223  -0.08921 26  VAL A CG2 
187  N N   . TRP A 30  ? 0.66805 0.58364 0.44649 0.01196  0.10130  -0.08664 27  TRP A N   
188  C CA  . TRP A 30  ? 0.71500 0.61168 0.46792 0.04024  0.08615  -0.09299 27  TRP A CA  
189  C C   . TRP A 30  ? 0.76590 0.63707 0.46904 0.05157  0.10282  -0.09058 27  TRP A C   
190  O O   . TRP A 30  ? 0.74775 0.58769 0.41367 0.06453  0.08595  -0.09458 27  TRP A O   
191  C CB  . TRP A 30  ? 0.66989 0.60427 0.45415 0.05909  0.08391  -0.10367 27  TRP A CB  
192  C CG  . TRP A 30  ? 0.70432 0.60504 0.46099 0.08563  0.07078  -0.11269 27  TRP A CG  
193  C CD1 . TRP A 30  ? 0.70753 0.61320 0.45505 0.11226  0.08255  -0.12281 27  TRP A CD1 
194  C CD2 . TRP A 30  ? 0.79458 0.64825 0.52877 0.08553  0.04689  -0.11512 27  TRP A CD2 
195  N NE1 . TRP A 30  ? 0.75637 0.61117 0.47206 0.12752  0.06787  -0.13275 27  TRP A NE1 
196  C CE2 . TRP A 30  ? 0.75884 0.58367 0.46857 0.10839  0.04611  -0.12870 27  TRP A CE2 
197  C CE3 . TRP A 30  ? 0.68086 0.51485 0.41406 0.06733  0.02896  -0.10862 27  TRP A CE3 
198  C CZ2 . TRP A 30  ? 0.71002 0.48475 0.39580 0.10679  0.02876  -0.13760 27  TRP A CZ2 
199  C CZ3 . TRP A 30  ? 0.76134 0.55729 0.47626 0.06794  0.01157  -0.11563 27  TRP A CZ3 
200  C CH2 . TRP A 30  ? 0.68145 0.44693 0.37363 0.08418  0.01173  -0.13074 27  TRP A CH2 
201  N N   . GLU A 31  ? 0.85680 0.74385 0.55846 0.04503  0.13570  -0.08532 28  GLU A N   
202  C CA  . GLU A 31  ? 0.94904 0.81074 0.59421 0.05934  0.15610  -0.07994 28  GLU A CA  
203  C C   . GLU A 31  ? 0.89455 0.71009 0.49059 0.06061  0.14676  -0.06602 28  GLU A C   
204  O O   . GLU A 31  ? 0.95877 0.75476 0.50415 0.08225  0.13695  -0.06869 28  GLU A O   
205  C CB  . GLU A 31  ? 0.99582 0.88140 0.65105 0.04693  0.19966  -0.07352 28  GLU A CB  
206  C CG  . GLU A 31  ? 1.13372 0.99239 0.72442 0.06472  0.22579  -0.06540 28  GLU A CG  
207  C CD  . GLU A 31  ? 1.49797 1.37851 1.09738 0.05002  0.27594  -0.05780 28  GLU A CD  
208  O OE1 . GLU A 31  ? 1.54609 1.47013 1.20928 0.02098  0.28936  -0.06193 28  GLU A OE1 
209  O OE2 . GLU A 31  ? 1.51303 1.37064 1.05485 0.06605  0.30232  -0.04891 28  GLU A OE2 
210  N N   . SER A 32  ? 0.78000 0.58202 0.38938 0.04068  0.14861  -0.05381 29  SER A N   
211  C CA  . SER A 32  ? 0.80450 0.56559 0.36888 0.04910  0.14074  -0.03825 29  SER A CA  
212  C C   . SER A 32  ? 0.83383 0.60003 0.39546 0.06313  0.09946  -0.04918 29  SER A C   
213  O O   . SER A 32  ? 0.81645 0.56983 0.33156 0.08312  0.08846  -0.04460 29  SER A O   
214  C CB  . SER A 32  ? 0.79647 0.53653 0.37610 0.02667  0.15328  -0.02619 29  SER A CB  
215  O OG  . SER A 32  ? 0.89501 0.59589 0.42958 0.04321  0.14777  -0.00948 29  SER A OG  
216  N N   . LEU A 33  ? 0.74051 0.52739 0.34923 0.05276  0.07871  -0.06311 30  LEU A N   
217  C CA  . LEU A 33  ? 0.72925 0.51723 0.33968 0.05835  0.04496  -0.07504 30  LEU A CA  
218  C C   . LEU A 33  ? 0.73461 0.52062 0.31077 0.07526  0.03748  -0.09140 30  LEU A C   
219  O O   . LEU A 33  ? 0.77326 0.55854 0.32874 0.08024  0.01476  -0.10007 30  LEU A O   
220  C CB  . LEU A 33  ? 0.69329 0.49354 0.35289 0.04537  0.03255  -0.08290 30  LEU A CB  
221  C CG  . LEU A 33  ? 0.75312 0.55462 0.43914 0.02901  0.03028  -0.07222 30  LEU A CG  
222  C CD1 . LEU A 33  ? 0.67691 0.49527 0.40375 0.02090  0.02175  -0.07840 30  LEU A CD1 
223  C CD2 . LEU A 33  ? 0.65498 0.44649 0.32765 0.03118  0.01283  -0.06748 30  LEU A CD2 
224  N N   . ASN A 34  ? 0.90654 0.69662 0.47920 0.08294  0.05578  -0.09876 31  ASN A N   
225  C CA  . ASN A 34  ? 0.97306 0.75419 0.50317 0.10074  0.05205  -0.11714 31  ASN A CA  
226  C C   . ASN A 34  ? 1.00442 0.77956 0.47459 0.11521  0.05519  -0.10879 31  ASN A C   
227  O O   . ASN A 34  ? 1.08994 0.86411 0.52518 0.12411  0.03302  -0.12580 31  ASN A O   
228  C CB  . ASN A 34  ? 1.02279 0.81106 0.55983 0.11163  0.07541  -0.12556 31  ASN A CB  
229  C CG  . ASN A 34  ? 1.11165 0.90993 0.70167 0.10748  0.07059  -0.13138 31  ASN A CG  
230  O OD1 . ASN A 34  ? 1.07858 0.86348 0.68528 0.09877  0.04742  -0.13604 31  ASN A OD1 
231  N ND2 . ASN A 34  ? 1.14401 0.97005 0.76007 0.11555  0.09359  -0.12998 31  ASN A ND2 
232  N N   . LYS A 35  ? 0.84943 0.61949 0.30493 0.11727  0.08284  -0.08447 32  LYS A N   
233  C CA  . LYS A 35  ? 0.91163 0.66780 0.29789 0.13898  0.09171  -0.06990 32  LYS A CA  
234  C C   . LYS A 35  ? 0.91297 0.67153 0.28092 0.14800  0.06356  -0.06221 32  LYS A C   
235  O O   . LYS A 35  ? 0.95705 0.72672 0.27933 0.16900  0.04750  -0.06673 32  LYS A O   
236  C CB  . LYS A 35  ? 0.94244 0.67972 0.31474 0.13646  0.13691  -0.04373 32  LYS A CB  
237  C CG  . LYS A 35  ? 0.95127 0.70164 0.34008 0.13086  0.16875  -0.05110 32  LYS A CG  
238  C CD  . LYS A 35  ? 1.06585 0.81742 0.40071 0.15663  0.17136  -0.06578 32  LYS A CD  
239  C CE  . LYS A 35  ? 1.11441 0.88376 0.46591 0.15588  0.20807  -0.07127 32  LYS A CE  
240  N NZ  . LYS A 35  ? 1.06849 0.84393 0.38652 0.17642  0.20437  -0.08537 32  LYS A NZ  
241  N N   . PHE A 36  ? 0.91364 0.67189 0.32381 0.13303  0.05621  -0.05197 33  PHE A N   
242  C CA  . PHE A 36  ? 0.91785 0.68352 0.31119 0.14776  0.03504  -0.04092 33  PHE A CA  
243  C C   . PHE A 36  ? 0.87107 0.66034 0.32205 0.12854  0.00646  -0.05395 33  PHE A C   
244  O O   . PHE A 36  ? 0.91316 0.71639 0.36229 0.13960  -0.00822 -0.04447 33  PHE A O   
245  C CB  . PHE A 36  ? 0.94930 0.67780 0.31781 0.15735  0.06478  -0.00717 33  PHE A CB  
246  C CG  . PHE A 36  ? 1.01783 0.71025 0.34111 0.16391  0.10691  0.01009  33  PHE A CG  
247  C CD1 . PHE A 36  ? 1.08665 0.78071 0.35801 0.19185  0.10879  0.01799  33  PHE A CD1 
248  C CD2 . PHE A 36  ? 1.00913 0.67793 0.36271 0.13585  0.14257  0.01704  33  PHE A CD2 
249  C CE1 . PHE A 36  ? 1.11316 0.77753 0.35753 0.19338  0.14857  0.03511  33  PHE A CE1 
250  C CE2 . PHE A 36  ? 1.21019 0.84944 0.52695 0.13617  0.18630  0.03214  33  PHE A CE2 
251  C CZ  . PHE A 36  ? 1.19851 0.83366 0.46258 0.16520  0.18947  0.04258  33  PHE A CZ  
252  N N   . GLN A 37  ? 0.82527 0.61849 0.32210 0.10480  0.00139  -0.07269 34  GLN A N   
253  C CA  . GLN A 37  ? 0.78565 0.59376 0.33134 0.08560  -0.02059 -0.08331 34  GLN A CA  
254  C C   . GLN A 37  ? 0.78531 0.58876 0.35391 0.08078  -0.01472 -0.06308 34  GLN A C   
255  O O   . GLN A 37  ? 0.80769 0.62794 0.40700 0.07107  -0.03196 -0.06728 34  GLN A O   
256  C CB  . GLN A 37  ? 0.84336 0.68157 0.38285 0.08659  -0.05204 -0.10438 34  GLN A CB  
257  C CG  . GLN A 37  ? 0.80864 0.64305 0.32479 0.08549  -0.05892 -0.13236 34  GLN A CG  
258  C CD  . GLN A 37  ? 0.92011 0.75469 0.37352 0.11243  -0.05113 -0.12961 34  GLN A CD  
259  O OE1 . GLN A 37  ? 0.91635 0.72861 0.34797 0.11836  -0.03141 -0.13353 34  GLN A OE1 
260  N NE2 . GLN A 37  ? 0.91904 0.78215 0.34069 0.13285  -0.06559 -0.12173 34  GLN A NE2 
261  N N   . THR A 38  ? 0.78627 0.56308 0.33739 0.08581  0.01289  -0.04247 35  THR A N   
262  C CA  . THR A 38  ? 0.86009 0.61825 0.42738 0.07779  0.02539  -0.02686 35  THR A CA  
263  C C   . THR A 38  ? 0.81368 0.54606 0.38567 0.06120  0.05767  -0.02079 35  THR A C   
264  O O   . THR A 38  ? 0.82062 0.55087 0.37666 0.06271  0.07384  -0.02249 35  THR A O   
265  C CB  . THR A 38  ? 0.91234 0.65747 0.44111 0.10477  0.02835  -0.00656 35  THR A CB  
266  O OG1 . THR A 38  ? 0.96981 0.69079 0.44103 0.12715  0.04782  0.00784  35  THR A OG1 
267  C CG2 . THR A 38  ? 0.86953 0.66064 0.40629 0.11910  -0.00535 -0.01507 35  THR A CG2 
268  N N   . VAL A 39  ? 0.81055 0.52970 0.40804 0.04243  0.06716  -0.01736 36  VAL A N   
269  C CA  . VAL A 39  ? 0.79333 0.49633 0.40270 0.01820  0.09754  -0.01663 36  VAL A CA  
270  C C   . VAL A 39  ? 0.84021 0.50739 0.44678 0.00655  0.11113  -0.00872 36  VAL A C   
271  O O   . VAL A 39  ? 0.82933 0.50173 0.44604 0.01255  0.09147  -0.00955 36  VAL A O   
272  C CB  . VAL A 39  ? 0.76784 0.51223 0.42772 -0.00140 0.08970  -0.03524 36  VAL A CB  
273  C CG1 . VAL A 39  ? 0.66726 0.43069 0.36240 -0.00920 0.06424  -0.04403 36  VAL A CG1 
274  C CG2 . VAL A 39  ? 0.73411 0.48270 0.41153 -0.02679 0.12002  -0.03840 36  VAL A CG2 
275  N N   . CYS A 40  ? 0.88827 0.51641 0.47860 -0.01064 0.14709  -0.00231 37  CYS A N   
276  C CA  . CYS A 40  ? 0.90654 0.48873 0.49024 -0.02746 0.16527  -0.00006 37  CYS A CA  
277  C C   . CYS A 40  ? 0.91545 0.52385 0.54701 -0.07093 0.17199  -0.02214 37  CYS A C   
278  O O   . CYS A 40  ? 0.91315 0.53199 0.55535 -0.09201 0.19477  -0.02710 37  CYS A O   
279  C CB  . CYS A 40  ? 0.97188 0.47665 0.49583 -0.01987 0.20632  0.02139  37  CYS A CB  
280  S SG  . CYS A 40  ? 1.06877 0.49556 0.55884 -0.01602 0.22448  0.03042  37  CYS A SG  
281  N N   . ILE A 41  ? 0.86828 0.48996 0.52518 -0.08274 0.15409  -0.03495 38  ILE A N   
282  C CA  . ILE A 41  ? 0.85480 0.51478 0.55653 -0.12116 0.15315  -0.05911 38  ILE A CA  
283  C C   . ILE A 41  ? 0.92705 0.53083 0.60983 -0.14799 0.17708  -0.06654 38  ILE A C   
284  O O   . ILE A 41  ? 0.94597 0.50375 0.59697 -0.12829 0.17507  -0.05665 38  ILE A O   
285  C CB  . ILE A 41  ? 0.80539 0.52522 0.54329 -0.11135 0.11336  -0.06907 38  ILE A CB  
286  C CG1 . ILE A 41  ? 0.80218 0.55743 0.54895 -0.08478 0.09443  -0.06283 38  ILE A CG1 
287  C CG2 . ILE A 41  ? 0.81071 0.58052 0.58991 -0.14207 0.10690  -0.09267 38  ILE A CG2 
288  C CD1 . ILE A 41  ? 0.78116 0.58842 0.56136 -0.09446 0.09819  -0.07391 38  ILE A CD1 
289  N N   . SER A 42  ? 0.97788 0.58051 0.67573 -0.19097 0.20391  -0.08323 39  SER A N   
290  C CA  . SER A 42  ? 1.12300 0.66519 0.80175 -0.22709 0.23135  -0.09785 39  SER A CA  
291  C C   . SER A 42  ? 1.15488 0.58594 0.76391 -0.20703 0.26602  -0.07258 39  SER A C   
292  O O   . SER A 42  ? 1.21593 0.58033 0.79604 -0.22107 0.28430  -0.08043 39  SER A O   
293  C CB  . SER A 42  ? 1.04575 0.61389 0.74283 -0.23945 0.20569  -0.12094 39  SER A CB  
294  O OG  . SER A 42  ? 1.08583 0.75308 0.84162 -0.26131 0.18109  -0.14494 39  SER A OG  
295  N N   . ARG A 43  ? 1.14028 0.55450 0.71946 -0.16919 0.27126  -0.04367 40  ARG A N   
296  C CA  . ARG A 43  ? 1.18824 0.50043 0.69396 -0.14136 0.30614  -0.01427 40  ARG A CA  
297  C C   . ARG A 43  ? 1.26028 0.53982 0.73323 -0.09635 0.28949  -0.00020 40  ARG A C   
298  O O   . ARG A 43  ? 1.27808 0.49052 0.69192 -0.05850 0.31061  0.02681  40  ARG A O   
299  C CB  . ARG A 43  ? 1.22434 0.47619 0.71172 -0.17832 0.35387  -0.02290 40  ARG A CB  
300  C CG  . ARG A 43  ? 1.29747 0.58169 0.81023 -0.21087 0.37599  -0.02782 40  ARG A CG  
301  C CD  . ARG A 43  ? 1.46496 0.70209 0.96563 -0.24218 0.41788  -0.03995 40  ARG A CD  
302  N NE  . ARG A 43  ? 1.56394 0.84168 1.09718 -0.27561 0.43911  -0.04709 40  ARG A NE  
303  C CZ  . ARG A 43  ? 1.66997 0.92413 1.20639 -0.31356 0.47587  -0.06164 40  ARG A CZ  
304  N NH1 . ARG A 43  ? 1.58609 0.76928 1.08912 -0.32352 0.49723  -0.07075 40  ARG A NH1 
305  N NH2 . ARG A 43  ? 1.69041 0.99296 1.26220 -0.34125 0.49347  -0.06711 40  ARG A NH2 
306  N N   . ILE A 44  ? 1.27851 0.61431 0.78956 -0.09442 0.25213  -0.01628 41  ILE A N   
307  C CA  . ILE A 44  ? 1.22238 0.53414 0.70838 -0.05494 0.24051  -0.00541 41  ILE A CA  
308  C C   . ILE A 44  ? 1.15118 0.54994 0.67352 -0.02656 0.19449  -0.00240 41  ILE A C   
309  O O   . ILE A 44  ? 1.19438 0.59009 0.69650 0.01603  0.18546  0.01463  41  ILE A O   
310  C CB  . ILE A 44  ? 1.24304 0.51816 0.72733 -0.08301 0.25072  -0.02861 41  ILE A CB  
311  C CG1 . ILE A 44  ? 1.31470 0.51625 0.75800 -0.09286 0.29403  -0.02651 41  ILE A CG1 
312  C CG2 . ILE A 44  ? 1.22492 0.51744 0.70944 -0.04960 0.22761  -0.02607 41  ILE A CG2 
313  C CD1 . ILE A 44  ? 1.45558 0.67080 0.92713 -0.15319 0.30994  -0.05491 41  ILE A CD1 
314  N N   . PHE A 45  ? 0.96226 0.43498 0.53461 -0.04776 0.16927  -0.01750 42  PHE A N   
315  C CA  . PHE A 45  ? 0.85621 0.39942 0.46180 -0.02866 0.12967  -0.01807 42  PHE A CA  
316  C C   . PHE A 45  ? 0.96864 0.54276 0.57313 -0.00752 0.11797  -0.00673 42  PHE A C   
317  O O   . PHE A 45  ? 0.97373 0.55807 0.58575 -0.02318 0.12611  -0.01100 42  PHE A O   
318  C CB  . PHE A 45  ? 0.78774 0.37978 0.43805 -0.05864 0.11061  -0.04077 42  PHE A CB  
319  C CG  . PHE A 45  ? 0.88011 0.44490 0.52392 -0.07763 0.11940  -0.05503 42  PHE A CG  
320  C CD1 . PHE A 45  ? 0.87456 0.40983 0.49501 -0.05519 0.12146  -0.04775 42  PHE A CD1 
321  C CD2 . PHE A 45  ? 0.85789 0.43222 0.51886 -0.11745 0.12581  -0.07835 42  PHE A CD2 
322  C CE1 . PHE A 45  ? 0.88681 0.39198 0.49427 -0.07126 0.13137  -0.06343 42  PHE A CE1 
323  C CE2 . PHE A 45  ? 0.84875 0.39812 0.49816 -0.13683 0.13244  -0.09641 42  PHE A CE2 
324  C CZ  . PHE A 45  ? 0.94359 0.45298 0.56273 -0.11325 0.13609  -0.08888 42  PHE A CZ  
325  N N   . ASN A 46  ? 0.89316 0.48649 0.48885 0.02668  0.09991  0.00490  43  ASN A N   
326  C CA  . ASN A 46  ? 0.85662 0.48299 0.44679 0.04660  0.08483  0.01060  43  ASN A CA  
327  C C   . ASN A 46  ? 0.82037 0.50887 0.45279 0.04190  0.05081  -0.00324 43  ASN A C   
328  O O   . ASN A 46  ? 0.78593 0.49806 0.42943 0.05436  0.03500  -0.00231 43  ASN A O   
329  C CB  . ASN A 46  ? 0.94079 0.54660 0.48336 0.08860  0.09071  0.03206  43  ASN A CB  
330  C CG  . ASN A 46  ? 1.14106 0.76380 0.65972 0.10534  0.08548  0.03735  43  ASN A CG  
331  O OD1 . ASN A 46  ? 1.11138 0.70803 0.61342 0.09242  0.10697  0.03913  43  ASN A OD1 
332  N ND2 . ASN A 46  ? 1.03759 0.70905 0.55498 0.13226  0.05768  0.03746  43  ASN A ND2 
333  N N   . PHE A 47  ? 0.76679 0.47819 0.41939 0.02600  0.04358  -0.01499 44  PHE A N   
334  C CA  . PHE A 47  ? 0.73856 0.49117 0.42472 0.01977  0.01709  -0.02793 44  PHE A CA  
335  C C   . PHE A 47  ? 0.78976 0.56256 0.46565 0.03224  0.00391  -0.03295 44  PHE A C   
336  O O   . PHE A 47  ? 0.78196 0.54398 0.43526 0.03775  0.01595  -0.03105 44  PHE A O   
337  C CB  . PHE A 47  ? 0.66263 0.42428 0.37821 -0.00303 0.01723  -0.03915 44  PHE A CB  
338  C CG  . PHE A 47  ? 0.72259 0.47660 0.45021 -0.01771 0.02178  -0.04099 44  PHE A CG  
339  C CD1 . PHE A 47  ? 0.65572 0.41725 0.39270 -0.01554 0.00982  -0.04006 44  PHE A CD1 
340  C CD2 . PHE A 47  ? 0.71927 0.46205 0.44867 -0.03646 0.03918  -0.04638 44  PHE A CD2 
341  C CE1 . PHE A 47  ? 0.70314 0.45654 0.44352 -0.02704 0.01448  -0.04334 44  PHE A CE1 
342  C CE2 . PHE A 47  ? 0.69240 0.43006 0.42832 -0.05188 0.04127  -0.05334 44  PHE A CE2 
343  C CZ  . PHE A 47  ? 0.65651 0.39735 0.39428 -0.04479 0.02851  -0.05130 44  PHE A CZ  
344  N N   . GLN A 48  ? 0.69666 0.49778 0.38703 0.03426  -0.01818 -0.04099 45  GLN A N   
345  C CA  . GLN A 48  ? 0.73621 0.55642 0.41820 0.03913  -0.03312 -0.05374 45  GLN A CA  
346  C C   . GLN A 48  ? 0.65378 0.46941 0.35606 0.02251  -0.03712 -0.06846 45  GLN A C   
347  O O   . GLN A 48  ? 0.68275 0.49135 0.40892 0.01009  -0.03415 -0.06722 45  GLN A O   
348  C CB  . GLN A 48  ? 0.70691 0.56486 0.39665 0.04458  -0.05412 -0.05988 45  GLN A CB  
349  C CG  . GLN A 48  ? 0.67198 0.54377 0.33534 0.07368  -0.05344 -0.04491 45  GLN A CG  
350  C CD  . GLN A 48  ? 0.75367 0.68362 0.43709 0.07926  -0.07595 -0.05297 45  GLN A CD  
351  O OE1 . GLN A 48  ? 0.74628 0.70184 0.46344 0.05432  -0.08988 -0.07187 45  GLN A OE1 
352  N NE2 . GLN A 48  ? 0.74891 0.70072 0.41166 0.11261  -0.07743 -0.03844 45  GLN A NE2 
353  N N   . LEU A 49  ? 0.64303 0.46047 0.32944 0.02653  -0.04346 -0.08247 46  LEU A N   
354  C CA  . LEU A 49  ? 0.65462 0.45771 0.35179 0.01814  -0.04393 -0.09599 46  LEU A CA  
355  C C   . LEU A 49  ? 0.67197 0.47083 0.39521 0.00153  -0.05414 -0.10156 46  LEU A C   
356  O O   . LEU A 49  ? 0.63244 0.41219 0.36769 -0.00184 -0.04928 -0.10101 46  LEU A O   
357  C CB  . LEU A 49  ? 0.68333 0.48238 0.35129 0.02628  -0.04786 -0.11356 46  LEU A CB  
358  C CG  . LEU A 49  ? 0.66933 0.44249 0.33947 0.02344  -0.04559 -0.12935 46  LEU A CG  
359  C CD1 . LEU A 49  ? 0.65266 0.42127 0.33885 0.03115  -0.02893 -0.11812 46  LEU A CD1 
360  C CD2 . LEU A 49  ? 0.70478 0.46975 0.33795 0.03245  -0.04751 -0.14989 46  LEU A CD2 
361  N N   . GLN A 50  ? 0.68648 0.50618 0.41813 -0.00710 -0.06652 -0.10547 47  GLN A N   
362  C CA  . GLN A 50  ? 0.74342 0.55903 0.50003 -0.02713 -0.07050 -0.10923 47  GLN A CA  
363  C C   . GLN A 50  ? 0.73184 0.53781 0.50438 -0.02823 -0.06087 -0.09104 47  GLN A C   
364  O O   . GLN A 50  ? 0.79143 0.58117 0.57595 -0.04097 -0.05871 -0.09004 47  GLN A O   
365  C CB  . GLN A 50  ? 0.67233 0.52993 0.44311 -0.03704 -0.08350 -0.11716 47  GLN A CB  
366  C CG  . GLN A 50  ? 0.78155 0.67112 0.55724 -0.02094 -0.08252 -0.09931 47  GLN A CG  
367  C CD  . GLN A 50  ? 0.86787 0.80892 0.67054 -0.02937 -0.09293 -0.10474 47  GLN A CD  
368  O OE1 . GLN A 50  ? 0.86500 0.81560 0.68987 -0.05629 -0.09764 -0.12107 47  GLN A OE1 
369  N NE2 . GLN A 50  ? 0.89095 0.86506 0.69193 -0.00614 -0.09380 -0.09128 47  GLN A NE2 
370  N N   . ASP A 51  ? 0.60400 0.41385 0.37173 -0.01640 -0.05297 -0.07803 48  ASP A N   
371  C CA  . ASP A 51  ? 0.62515 0.43059 0.40402 -0.01930 -0.04581 -0.06568 48  ASP A CA  
372  C C   . ASP A 51  ? 0.61254 0.40486 0.39273 -0.01658 -0.04134 -0.06511 48  ASP A C   
373  O O   . ASP A 51  ? 0.61349 0.40601 0.40038 -0.01906 -0.03961 -0.05838 48  ASP A O   
374  C CB  . ASP A 51  ? 0.59519 0.40762 0.36677 -0.01202 -0.03795 -0.05583 48  ASP A CB  
375  C CG  . ASP A 51  ? 0.63716 0.46996 0.40806 -0.00489 -0.04234 -0.05272 48  ASP A CG  
376  O OD1 . ASP A 51  ? 0.77207 0.62267 0.56156 -0.01369 -0.04921 -0.05596 48  ASP A OD1 
377  O OD2 . ASP A 51  ? 0.62196 0.45375 0.37324 0.01080  -0.03674 -0.04596 48  ASP A OD2 
378  N N   . LEU A 52  ? 0.51713 0.30359 0.28985 -0.00867 -0.04013 -0.07288 49  LEU A N   
379  C CA  . LEU A 52  ? 0.59549 0.38274 0.37382 0.00071  -0.03616 -0.07249 49  LEU A CA  
380  C C   . LEU A 52  ? 0.55961 0.32075 0.33528 0.00512  -0.03988 -0.07164 49  LEU A C   
381  O O   . LEU A 52  ? 0.62357 0.35750 0.38728 0.00541  -0.04016 -0.08064 49  LEU A O   
382  C CB  . LEU A 52  ? 0.53502 0.33042 0.30708 0.01149  -0.02838 -0.07972 49  LEU A CB  
383  C CG  . LEU A 52  ? 0.59738 0.41382 0.38396 0.02398  -0.02303 -0.08014 49  LEU A CG  
384  C CD1 . LEU A 52  ? 0.53416 0.38224 0.34074 0.01383  -0.02189 -0.07514 49  LEU A CD1 
385  C CD2 . LEU A 52  ? 0.60861 0.43668 0.39001 0.03398  -0.01082 -0.08756 49  LEU A CD2 
386  N N   . ARG A 53  ? 0.54648 0.31136 0.32747 0.00813  -0.04119 -0.06142 50  ARG A N   
387  C CA  . ARG A 53  ? 0.60548 0.33671 0.37471 0.01651  -0.04071 -0.05392 50  ARG A CA  
388  C C   . ARG A 53  ? 0.64417 0.36417 0.40499 0.04301  -0.03804 -0.05540 50  ARG A C   
389  O O   . ARG A 53  ? 0.65169 0.32177 0.39241 0.05187  -0.03262 -0.05262 50  ARG A O   
390  C CB  . ARG A 53  ? 0.56038 0.30544 0.33052 0.01590  -0.04319 -0.04115 50  ARG A CB  
391  C CG  . ARG A 53  ? 0.53472 0.29183 0.31197 -0.00491 -0.04256 -0.04035 50  ARG A CG  
392  C CD  . ARG A 53  ? 0.53202 0.30671 0.30571 -0.00370 -0.04420 -0.03262 50  ARG A CD  
393  N NE  . ARG A 53  ? 0.66101 0.41687 0.41581 0.01018  -0.04425 -0.01978 50  ARG A NE  
394  C CZ  . ARG A 53  ? 0.58716 0.31175 0.32729 0.00428  -0.03599 -0.00833 50  ARG A CZ  
395  N NH1 . ARG A 53  ? 0.57600 0.29648 0.32705 -0.01709 -0.02901 -0.01102 50  ARG A NH1 
396  N NH2 . ARG A 53  ? 0.62944 0.33024 0.34323 0.02171  -0.03318 0.00693  50  ARG A NH2 
397  N N   . ASN A 54  ? 0.60160 0.36506 0.37718 0.05472  -0.03853 -0.05998 51  ASN A N   
398  C CA  . ASN A 54  ? 0.63093 0.40021 0.40476 0.08645  -0.03524 -0.06080 51  ASN A CA  
399  C C   . ASN A 54  ? 0.66820 0.45030 0.44627 0.08876  -0.02719 -0.07479 51  ASN A C   
400  O O   . ASN A 54  ? 0.62591 0.46118 0.42583 0.09707  -0.02389 -0.07776 51  ASN A O   
401  C CB  . ASN A 54  ? 0.63503 0.46417 0.42859 0.10296  -0.04231 -0.05465 51  ASN A CB  
402  C CG  . ASN A 54  ? 0.62971 0.51680 0.45081 0.07831  -0.04495 -0.06171 51  ASN A CG  
403  O OD1 . ASN A 54  ? 0.58866 0.46181 0.40803 0.05130  -0.04181 -0.06453 51  ASN A OD1 
404  N ND2 . ASN A 54  ? 0.58342 0.53626 0.42931 0.08833  -0.04970 -0.06558 51  ASN A ND2 
405  N N   . PRO A 55  ? 0.72375 0.46005 0.47958 0.08297  -0.02264 -0.08510 52  PRO A N   
406  C CA  . PRO A 55  ? 0.70905 0.45571 0.45973 0.08954  -0.01401 -0.09800 52  PRO A CA  
407  C C   . PRO A 55  ? 0.78868 0.55753 0.54682 0.12459  -0.00510 -0.09819 52  PRO A C   
408  O O   . PRO A 55  ? 0.78017 0.51753 0.52549 0.14965  -0.00400 -0.09379 52  PRO A O   
409  C CB  . PRO A 55  ? 0.71325 0.40436 0.43363 0.07790  -0.01486 -0.11174 52  PRO A CB  
410  C CG  . PRO A 55  ? 0.83446 0.47763 0.54619 0.07210  -0.01797 -0.10571 52  PRO A CG  
411  C CD  . PRO A 55  ? 0.75237 0.43217 0.48794 0.06670  -0.02473 -0.08728 52  PRO A CD  
412  N N   . PRO A 56  ? 0.69372 0.51875 0.47268 0.12799  0.00407  -0.10217 53  PRO A N   
413  C CA  . PRO A 56  ? 0.68034 0.54687 0.47673 0.16143  0.01342  -0.10346 53  PRO A CA  
414  C C   . PRO A 56  ? 0.77908 0.60424 0.54589 0.19373  0.02662  -0.11358 53  PRO A C   
415  O O   . PRO A 56  ? 0.77122 0.54407 0.50407 0.18301  0.03032  -0.12495 53  PRO A O   
416  C CB  . PRO A 56  ? 0.67729 0.61282 0.50510 0.14402  0.02446  -0.10703 53  PRO A CB  
417  C CG  . PRO A 56  ? 0.63891 0.54068 0.44346 0.11329  0.02679  -0.10887 53  PRO A CG  
418  C CD  . PRO A 56  ? 0.65988 0.51164 0.44673 0.10064  0.00873  -0.10375 53  PRO A CD  
419  N N   . SER A 57  ? 0.96218 0.81329 0.74039 0.23533  0.03261  -0.11050 54  SER A N   
420  C CA  . SER A 57  ? 0.95850 0.76666 0.70563 0.27422  0.04928  -0.12040 54  SER A CA  
421  C C   . SER A 57  ? 1.02796 0.87560 0.78072 0.27436  0.06823  -0.13395 54  SER A C   
422  O O   . SER A 57  ? 0.95961 0.88324 0.75116 0.25333  0.07143  -0.13155 54  SER A O   
423  C CB  . SER A 57  ? 0.91814 0.74118 0.67198 0.32731  0.05135  -0.10996 54  SER A CB  
424  O OG  . SER A 57  ? 1.16301 0.92375 0.87698 0.36681  0.07002  -0.11946 54  SER A OG  
425  N N   . THR A 58  ? 1.28284 1.07362 0.99296 0.29621  0.08335  -0.14865 55  THR A N   
426  C CA  . THR A 58  ? 1.23607 1.05780 0.94053 0.30246  0.10550  -0.16157 55  THR A CA  
427  C C   . THR A 58  ? 1.20512 1.12628 0.96233 0.33296  0.11999  -0.15529 55  THR A C   
428  O O   . THR A 58  ? 1.29622 1.27533 1.07166 0.32394  0.13905  -0.15958 55  THR A O   
429  C CB  . THR A 58  ? 1.27284 1.00712 0.91414 0.32340  0.11770  -0.18201 55  THR A CB  
430  O OG1 . THR A 58  ? 1.42151 1.10672 1.04929 0.36399  0.11974  -0.17911 55  THR A OG1 
431  C CG2 . THR A 58  ? 1.24950 0.91311 0.84689 0.28373  0.10342  -0.19494 55  THR A CG2 
432  N N   . VAL A 59  ? 1.22069 1.16179 0.99904 0.36955  0.11262  -0.14534 56  VAL A N   
433  C CA  . VAL A 59  ? 1.29246 1.34577 1.12744 0.40540  0.12292  -0.14154 56  VAL A CA  
434  C C   . VAL A 59  ? 1.20156 1.34515 1.09646 0.38265  0.10183  -0.13016 56  VAL A C   
435  O O   . VAL A 59  ? 1.25655 1.50091 1.20178 0.41349  0.10226  -0.12790 56  VAL A O   
436  C CB  . VAL A 59  ? 1.31820 1.33814 1.12992 0.47541  0.12953  -0.13865 56  VAL A CB  
437  C CG1 . VAL A 59  ? 1.27589 1.20808 1.02702 0.49849  0.15426  -0.15541 56  VAL A CG1 
438  C CG2 . VAL A 59  ? 1.24617 1.19522 1.03049 0.48637  0.10761  -0.12315 56  VAL A CG2 
439  N N   . GLN A 60  ? 1.07195 1.18855 0.96286 0.33199  0.08431  -0.12566 57  GLN A N   
440  C CA  . GLN A 60  ? 0.99172 1.17896 0.92822 0.31141  0.06276  -0.11769 57  GLN A CA  
441  C C   . GLN A 60  ? 0.97045 1.28601 0.97574 0.29281  0.07217  -0.12604 57  GLN A C   
442  O O   . GLN A 60  ? 0.99906 1.32760 1.01102 0.26713  0.09606  -0.13433 57  GLN A O   
443  C CB  . GLN A 60  ? 0.90975 1.04034 0.82599 0.25900  0.04840  -0.11376 57  GLN A CB  
444  C CG  . GLN A 60  ? 0.85430 1.03747 0.80309 0.23827  0.02644  -0.10778 57  GLN A CG  
445  C CD  . GLN A 60  ? 0.98311 1.11450 0.90135 0.26519  0.00655  -0.09366 57  GLN A CD  
446  O OE1 . GLN A 60  ? 0.92905 0.95953 0.79814 0.26795  0.00741  -0.08850 57  GLN A OE1 
447  N NE2 . GLN A 60  ? 0.92956 1.13227 0.87533 0.28430  -0.01045 -0.08808 57  GLN A NE2 
448  N N   . ASP A 61  ? 1.12895 1.53766 1.18156 0.30522  0.05468  -0.12459 58  ASP A N   
449  C CA  . ASP A 61  ? 1.04708 1.58421 1.17191 0.27202  0.06092  -0.13792 58  ASP A CA  
450  C C   . ASP A 61  ? 1.06760 1.58015 1.18951 0.21268  0.04592  -0.13860 58  ASP A C   
451  O O   . ASP A 61  ? 1.07655 1.56816 1.18222 0.22063  0.01846  -0.13057 58  ASP A O   
452  C CB  . ASP A 61  ? 1.06146 1.72649 1.24164 0.31389  0.04618  -0.14106 58  ASP A CB  
453  C CG  . ASP A 61  ? 1.08522 1.89505 1.34785 0.27301  0.05303  -0.16098 58  ASP A CG  
454  O OD1 . ASP A 61  ? 1.06427 1.86778 1.33830 0.22113  0.08071  -0.17019 58  ASP A OD1 
455  O OD2 . ASP A 61  ? 1.06114 1.98910 1.37376 0.29307  0.03144  -0.16753 58  ASP A OD2 
456  N N   . PHE A 62  ? 0.93381 1.44272 1.06508 0.15870  0.06663  -0.14645 59  PHE A N   
457  C CA  . PHE A 62  ? 0.88867 1.35180 1.00496 0.10666  0.05709  -0.14593 59  PHE A CA  
458  C C   . PHE A 62  ? 0.94536 1.51003 1.11801 0.07684  0.04381  -0.16090 59  PHE A C   
459  O O   . PHE A 62  ? 0.93430 1.46713 1.09523 0.03775  0.03426  -0.16339 59  PHE A O   
460  C CB  . PHE A 62  ? 0.90264 1.29648 0.98812 0.07081  0.08525  -0.14375 59  PHE A CB  
461  C CG  . PHE A 62  ? 0.91961 1.20711 0.93989 0.09451  0.08618  -0.13207 59  PHE A CG  
462  C CD1 . PHE A 62  ? 0.90991 1.18893 0.91419 0.13129  0.10167  -0.13301 59  PHE A CD1 
463  C CD2 . PHE A 62  ? 0.92527 1.12670 0.90134 0.07909  0.07199  -0.12332 59  PHE A CD2 
464  C CE1 . PHE A 62  ? 0.98724 1.17136 0.93034 0.14792  0.10081  -0.12858 59  PHE A CE1 
465  C CE2 . PHE A 62  ? 0.96134 1.07949 0.88398 0.09589  0.07071  -0.11772 59  PHE A CE2 
466  C CZ  . PHE A 62  ? 0.96212 1.07039 0.86715 0.12798  0.08414  -0.12194 59  PHE A CZ  
467  N N   . ASN A 63  ? 1.08558 1.77465 1.31860 0.09481  0.04382  -0.17327 60  ASN A N   
468  C CA  . ASN A 63  ? 1.04442 1.84677 1.33428 0.06677  0.02550  -0.19314 60  ASN A CA  
469  C C   . ASN A 63  ? 1.05038 1.82913 1.30851 0.09341  -0.01436 -0.18381 60  ASN A C   
470  O O   . ASN A 63  ? 1.02727 1.81798 1.28933 0.05365  -0.02958 -0.19561 60  ASN A O   
471  C CB  . ASN A 63  ? 1.08342 2.04035 1.44886 0.08822  0.03033  -0.20873 60  ASN A CB  
472  C CG  . ASN A 63  ? 1.10150 2.19013 1.53500 0.04379  0.01639  -0.23765 60  ASN A CG  
473  O OD1 . ASN A 63  ? 1.10917 2.16683 1.53967 -0.02188 0.02176  -0.25114 60  ASN A OD1 
474  N ND2 . ASN A 63  ? 1.01819 2.25541 1.51184 0.08032  -0.00135 -0.24922 60  ASN A ND2 
475  N N   . ASP A 64  ? 1.33763 2.08003 1.56147 0.15882  -0.02714 -0.16381 61  ASP A N   
476  C CA  . ASP A 64  ? 1.42648 2.12782 1.60766 0.18907  -0.05895 -0.14869 61  ASP A CA  
477  C C   . ASP A 64  ? 1.42444 1.98964 1.54525 0.15855  -0.05752 -0.13683 61  ASP A C   
478  O O   . ASP A 64  ? 1.47795 2.02841 1.57708 0.15254  -0.07933 -0.13329 61  ASP A O   
479  C CB  . ASP A 64  ? 1.49261 2.17756 1.64792 0.26830  -0.06459 -0.12851 61  ASP A CB  
480  C CG  . ASP A 64  ? 1.59674 2.42863 1.80829 0.31428  -0.07441 -0.13644 61  ASP A CG  
481  O OD1 . ASP A 64  ? 1.56626 2.52440 1.83865 0.28162  -0.08557 -0.15948 61  ASP A OD1 
482  O OD2 . ASP A 64  ? 1.69034 2.51062 1.88455 0.38254  -0.06996 -0.12125 61  ASP A OD2 
483  N N   . TYR A 65  ? 0.81922 1.29512 0.91267 0.14324  -0.03356 -0.13123 62  TYR A N   
484  C CA  . TYR A 65  ? 0.76620 1.12041 0.80373 0.12452  -0.03355 -0.11873 62  TYR A CA  
485  C C   . TYR A 65  ? 0.67010 1.00726 0.70573 0.06985  -0.03475 -0.12649 62  TYR A C   
486  O O   . TYR A 65  ? 0.66096 1.05140 0.73241 0.03148  -0.02272 -0.14352 62  TYR A O   
487  C CB  . TYR A 65  ? 0.68040 0.95980 0.68941 0.13066  -0.01107 -0.11338 62  TYR A CB  
488  C CG  . TYR A 65  ? 0.63155 0.80190 0.58965 0.11575  -0.01090 -0.10350 62  TYR A CG  
489  C CD1 . TYR A 65  ? 0.65279 0.75290 0.57109 0.14320  -0.02067 -0.09100 62  TYR A CD1 
490  C CD2 . TYR A 65  ? 0.66173 0.80122 0.61175 0.07494  0.00162  -0.10682 62  TYR A CD2 
491  C CE1 . TYR A 65  ? 0.66485 0.68074 0.54580 0.12485  -0.02043 -0.08573 62  TYR A CE1 
492  C CE2 . TYR A 65  ? 0.69014 0.74700 0.59923 0.06507  -0.00035 -0.09887 62  TYR A CE2 
493  C CZ  . TYR A 65  ? 0.69166 0.69402 0.57096 0.08754  -0.01241 -0.09023 62  TYR A CZ  
494  O OH  . TYR A 65  ? 0.74983 0.68718 0.59833 0.07267  -0.01418 -0.08613 62  TYR A OH  
495  N N   . GLU A 66  ? 0.68940 0.95050 0.68263 0.06712  -0.04586 -0.11448 63  GLU A N   
496  C CA  . GLU A 66  ? 0.60226 0.82709 0.58261 0.02270  -0.04350 -0.11913 63  GLU A CA  
497  C C   . GLU A 66  ? 0.63492 0.75899 0.57031 0.02585  -0.03804 -0.10319 63  GLU A C   
498  O O   . GLU A 66  ? 0.69109 0.78021 0.60428 0.05724  -0.04542 -0.09072 63  GLU A O   
499  C CB  . GLU A 66  ? 0.58839 0.84101 0.56466 0.02030  -0.06619 -0.12256 63  GLU A CB  
500  C CG  . GLU A 66  ? 0.72165 1.05689 0.73650 -0.01490 -0.06871 -0.14827 63  GLU A CG  
501  C CD  . GLU A 66  ? 0.79693 1.18216 0.80756 -0.00687 -0.09670 -0.15527 63  GLU A CD  
502  O OE1 . GLU A 66  ? 0.79315 1.12335 0.76029 0.01477  -0.10806 -0.13758 63  GLU A OE1 
503  O OE2 . GLU A 66  ? 0.88818 1.37125 0.93848 -0.02334 -0.10635 -0.17948 63  GLU A OE2 
504  N N   . TYR A 67  ? 0.59552 0.67615 0.51756 -0.00507 -0.02470 -0.10427 64  TYR A N   
505  C CA  . TYR A 67  ? 0.55614 0.55965 0.44205 -0.00201 -0.02135 -0.09199 64  TYR A CA  
506  C C   . TYR A 67  ? 0.59264 0.56474 0.45919 -0.01034 -0.03212 -0.08583 64  TYR A C   
507  O O   . TYR A 67  ? 0.63468 0.61450 0.50399 -0.03382 -0.02921 -0.09278 64  TYR A O   
508  C CB  . TYR A 67  ? 0.57578 0.55356 0.45277 -0.02183 -0.00034 -0.09329 64  TYR A CB  
509  C CG  . TYR A 67  ? 0.61922 0.61281 0.50303 -0.01368 0.01608  -0.09651 64  TYR A CG  
510  C CD1 . TYR A 67  ? 0.66509 0.71452 0.58142 -0.02799 0.03142  -0.10700 64  TYR A CD1 
511  C CD2 . TYR A 67  ? 0.61796 0.57301 0.47493 0.00490  0.01843  -0.09153 64  TYR A CD2 
512  C CE1 . TYR A 67  ? 0.77362 0.84009 0.69559 -0.02009 0.05114  -0.10908 64  TYR A CE1 
513  C CE2 . TYR A 67  ? 0.70096 0.66813 0.55694 0.01458  0.03548  -0.09533 64  TYR A CE2 
514  C CZ  . TYR A 67  ? 0.71226 0.73462 0.60048 0.00361  0.05340  -0.10236 64  TYR A CZ  
515  O OH  . TYR A 67  ? 0.67176 0.70951 0.55925 0.01332  0.07469  -0.10526 64  TYR A OH  
516  N N   . SER A 68  ? 0.58745 0.52118 0.43318 0.00669  -0.04063 -0.07441 65  SER A N   
517  C CA  . SER A 68  ? 0.64590 0.55231 0.47365 0.00034  -0.04707 -0.06686 65  SER A CA  
518  C C   . SER A 68  ? 0.61906 0.47945 0.43152 -0.00765 -0.04062 -0.06148 65  SER A C   
519  O O   . SER A 68  ? 0.60536 0.44135 0.41037 0.00174  -0.04108 -0.05867 65  SER A O   
520  C CB  . SER A 68  ? 0.63366 0.53758 0.44977 0.02277  -0.05842 -0.05689 65  SER A CB  
521  O OG  . SER A 68  ? 0.76564 0.72665 0.59613 0.03567  -0.06824 -0.06225 65  SER A OG  
522  N N   . PHE A 69  ? 0.54071 0.39171 0.34755 -0.02339 -0.03513 -0.06174 66  PHE A N   
523  C CA  . PHE A 69  ? 0.54383 0.36741 0.34011 -0.02564 -0.03035 -0.05707 66  PHE A CA  
524  C C   . PHE A 69  ? 0.57054 0.38157 0.35946 -0.02905 -0.03149 -0.05042 66  PHE A C   
525  O O   . PHE A 69  ? 0.57941 0.39447 0.36392 -0.03402 -0.03030 -0.05107 66  PHE A O   
526  C CB  . PHE A 69  ? 0.57732 0.39549 0.36770 -0.03309 -0.01696 -0.05946 66  PHE A CB  
527  C CG  . PHE A 69  ? 0.55059 0.37440 0.34168 -0.03015 -0.00891 -0.06308 66  PHE A CG  
528  C CD1 . PHE A 69  ? 0.54088 0.35427 0.32014 -0.01891 -0.01083 -0.06138 66  PHE A CD1 
529  C CD2 . PHE A 69  ? 0.55005 0.39331 0.35284 -0.04100 0.00232  -0.07028 66  PHE A CD2 
530  C CE1 . PHE A 69  ? 0.64366 0.46032 0.41622 -0.01397 -0.00082 -0.06437 66  PHE A CE1 
531  C CE2 . PHE A 69  ? 0.65266 0.50261 0.45554 -0.03879 0.01494  -0.07231 66  PHE A CE2 
532  C CZ  . PHE A 69  ? 0.61303 0.44664 0.39735 -0.02303 0.01392  -0.06810 66  PHE A CZ  
533  N N   . ASN A 70  ? 0.58894 0.39005 0.37747 -0.02751 -0.03333 -0.04663 67  ASN A N   
534  C CA  . ASN A 70  ? 0.60298 0.40256 0.39084 -0.03097 -0.03064 -0.04072 67  ASN A CA  
535  C C   . ASN A 70  ? 0.63465 0.43384 0.41508 -0.02821 -0.02186 -0.03998 67  ASN A C   
536  O O   . ASN A 70  ? 0.59460 0.39426 0.37115 -0.02149 -0.02007 -0.04003 67  ASN A O   
537  C CB  . ASN A 70  ? 0.55454 0.35595 0.35186 -0.03494 -0.03430 -0.04102 67  ASN A CB  
538  C CG  . ASN A 70  ? 0.60224 0.38427 0.39833 -0.03956 -0.03527 -0.03884 67  ASN A CG  
539  O OD1 . ASN A 70  ? 0.61837 0.39057 0.40445 -0.03551 -0.03302 -0.03110 67  ASN A OD1 
540  N ND2 . ASN A 70  ? 0.57574 0.34807 0.37638 -0.04696 -0.03766 -0.04616 67  ASN A ND2 
541  N N   . PHE A 71  ? 0.56797 0.36075 0.33937 -0.03033 -0.01488 -0.03898 68  PHE A N   
542  C CA  . PHE A 71  ? 0.59211 0.36836 0.34806 -0.02612 -0.00158 -0.03906 68  PHE A CA  
543  C C   . PHE A 71  ? 0.63831 0.41835 0.39248 -0.01515 0.00486  -0.03210 68  PHE A C   
544  O O   . PHE A 71  ? 0.65301 0.42495 0.39733 0.00004  0.01388  -0.02745 68  PHE A O   
545  C CB  . PHE A 71  ? 0.55895 0.32169 0.30212 -0.03856 0.00451  -0.04917 68  PHE A CB  
546  C CG  . PHE A 71  ? 0.61890 0.34637 0.33889 -0.03852 0.02355  -0.05231 68  PHE A CG  
547  C CD1 . PHE A 71  ? 0.66248 0.36643 0.37269 -0.03837 0.03587  -0.05105 68  PHE A CD1 
548  C CD2 . PHE A 71  ? 0.64621 0.35547 0.34738 -0.03740 0.03298  -0.05609 68  PHE A CD2 
549  C CE1 . PHE A 71  ? 0.66825 0.32298 0.34870 -0.03720 0.05895  -0.05177 68  PHE A CE1 
550  C CE2 . PHE A 71  ? 0.69812 0.36041 0.37082 -0.03570 0.05458  -0.06015 68  PHE A CE2 
551  C CZ  . PHE A 71  ? 0.66781 0.29869 0.32935 -0.03577 0.06843  -0.05718 68  PHE A CZ  
552  N N   . GLY A 72  ? 0.69906 0.49201 0.46067 -0.01959 0.00254  -0.02965 69  GLY A N   
553  C CA  . GLY A 72  ? 0.66253 0.46904 0.42803 -0.01027 0.01201  -0.02354 69  GLY A CA  
554  C C   . GLY A 72  ? 0.69757 0.52139 0.47686 -0.02043 0.01105  -0.01872 69  GLY A C   
555  O O   . GLY A 72  ? 0.70616 0.52197 0.48592 -0.03106 0.00262  -0.01868 69  GLY A O   
556  N N   . THR A 73  ? 0.68192 0.52691 0.47055 -0.01532 0.02268  -0.01355 70  THR A N   
557  C CA  . THR A 73  ? 0.72522 0.58291 0.52531 -0.02871 0.02947  -0.00702 70  THR A CA  
558  C C   . THR A 73  ? 0.71676 0.56700 0.49380 -0.02105 0.04688  -0.00247 70  THR A C   
559  O O   . THR A 73  ? 0.70809 0.56589 0.48102 -0.00396 0.05701  -0.00443 70  THR A O   
560  C CB  . THR A 73  ? 0.68821 0.59191 0.52939 -0.03681 0.02995  -0.00768 70  THR A CB  
561  O OG1 . THR A 73  ? 0.90583 0.84461 0.75834 -0.01601 0.03660  -0.00754 70  THR A OG1 
562  C CG2 . THR A 73  ? 0.76510 0.67363 0.62150 -0.04591 0.01221  -0.01609 70  THR A CG2 
563  N N   . LEU A 74  ? 0.74965 0.58166 0.50594 -0.02921 0.05160  0.00419  71  LEU A N   
564  C CA  . LEU A 74  ? 0.85277 0.67769 0.57893 -0.02111 0.06902  0.00814  71  LEU A CA  
565  C C   . LEU A 74  ? 0.85220 0.70746 0.60238 -0.02712 0.09048  0.01859  71  LEU A C   
566  O O   . LEU A 74  ? 0.91399 0.76272 0.66829 -0.04386 0.09647  0.02896  71  LEU A O   
567  C CB  . LEU A 74  ? 0.76686 0.56263 0.45237 -0.02237 0.06275  0.01184  71  LEU A CB  
568  C CG  . LEU A 74  ? 1.01412 0.79813 0.65360 -0.01150 0.07301  0.00879  71  LEU A CG  
569  C CD1 . LEU A 74  ? 1.01709 0.80095 0.65395 -0.00155 0.08147  -0.00563 71  LEU A CD1 
570  C CD2 . LEU A 74  ? 1.05075 0.81978 0.65283 -0.00885 0.05444  0.00294  71  LEU A CD2 
571  N N   . ASN A 75  ? 0.91037 0.79639 0.67528 -0.01315 0.10450  0.01611  72  ASN A N   
572  C CA  . ASN A 75  ? 0.93380 0.86509 0.72946 -0.01869 0.12816  0.02413  72  ASN A CA  
573  C C   . ASN A 75  ? 1.03920 0.96519 0.80154 0.00258  0.15131  0.02567  72  ASN A C   
574  O O   . ASN A 75  ? 0.99590 0.90812 0.73919 0.02641  0.14932  0.01625  72  ASN A O   
575  C CB  . ASN A 75  ? 1.01174 1.00685 0.86621 -0.01756 0.12349  0.01858  72  ASN A CB  
576  C CG  . ASN A 75  ? 1.07330 1.13310 0.96898 -0.02368 0.14848  0.02304  72  ASN A CG  
577  O OD1 . ASN A 75  ? 1.10641 1.16938 1.01395 -0.05310 0.16350  0.02970  72  ASN A OD1 
578  N ND2 . ASN A 75  ? 1.02609 1.13704 0.94307 0.00514  0.15615  0.02024  72  ASN A ND2 
579  N N   . ASN A 76  ? 1.44280 1.06548 1.15934 -0.06296 0.20738  0.17037  73  ASN A N   
580  C CA  . ASN A 76  ? 1.48688 1.10842 1.15762 -0.06309 0.23986  0.17563  73  ASN A CA  
581  C C   . ASN A 76  ? 1.43986 1.05425 1.04947 -0.03511 0.21009  0.16967  73  ASN A C   
582  O O   . ASN A 76  ? 1.45976 1.03299 1.02131 -0.02070 0.17902  0.18043  73  ASN A O   
583  C CB  . ASN A 76  ? 1.49485 1.18003 1.23945 -0.07439 0.27169  0.16131  73  ASN A CB  
584  C CG  . ASN A 76  ? 1.58061 1.27477 1.38511 -0.10589 0.30635  0.16938  73  ASN A CG  
585  O OD1 . ASN A 76  ? 1.61069 1.25711 1.38339 -0.12136 0.31530  0.18555  73  ASN A OD1 
586  N ND2 . ASN A 76  ? 1.55857 1.32214 1.45915 -0.11323 0.31759  0.15513  73  ASN A ND2 
587  N N   . GLU A 77  ? 1.18552 0.83819 0.80223 -0.02785 0.21900  0.15261  74  GLU A N   
588  C CA  . GLU A 77  ? 1.20482 0.85413 0.76967 -0.00672 0.19084  0.14263  74  GLU A CA  
589  C C   . GLU A 77  ? 1.11584 0.81956 0.74792 0.00650  0.16420  0.11985  74  GLU A C   
590  O O   . GLU A 77  ? 1.04903 0.76204 0.65855 0.01874  0.14860  0.10635  74  GLU A O   
591  C CB  . GLU A 77  ? 1.31131 0.94734 0.81675 -0.01058 0.22326  0.13840  74  GLU A CB  
592  C CG  . GLU A 77  ? 1.40573 0.98985 0.82395 -0.01306 0.21973  0.15310  74  GLU A CG  
593  C CD  . GLU A 77  ? 1.49583 1.07526 0.87152 -0.01908 0.24846  0.14123  74  GLU A CD  
594  O OE1 . GLU A 77  ? 1.43572 1.04850 0.86355 -0.02605 0.28559  0.12716  74  GLU A OE1 
595  O OE2 . GLU A 77  ? 1.67975 1.22206 0.97259 -0.01539 0.23221  0.14580  74  GLU A OE2 
596  N N   . TYR A 78  ? 1.02869 0.76350 0.73546 0.00189  0.15948  0.11540  75  TYR A N   
597  C CA  . TYR A 78  ? 0.90024 0.68135 0.66154 0.01319  0.13953  0.09636  75  TYR A CA  
598  C C   . TYR A 78  ? 0.88866 0.66811 0.67069 0.02050  0.10758  0.09420  75  TYR A C   
599  O O   . TYR A 78  ? 0.85401 0.61434 0.64744 0.01007  0.10762  0.10257  75  TYR A O   
600  C CB  . TYR A 78  ? 0.82736 0.65207 0.65706 0.00457  0.16080  0.08979  75  TYR A CB  
601  C CG  . TYR A 78  ? 0.86749 0.70457 0.69386 0.00572  0.19261  0.08385  75  TYR A CG  
602  C CD1 . TYR A 78  ? 0.81755 0.67234 0.64921 0.01962  0.18731  0.06857  75  TYR A CD1 
603  C CD2 . TYR A 78  ? 0.90392 0.73042 0.72198 -0.00788 0.23275  0.09252  75  TYR A CD2 
604  C CE1 . TYR A 78  ? 0.83902 0.69696 0.66598 0.02204  0.21914  0.06024  75  TYR A CE1 
605  C CE2 . TYR A 78  ? 0.89545 0.72943 0.70943 -0.00495 0.26803  0.08411  75  TYR A CE2 
606  C CZ  . TYR A 78  ? 0.85139 0.69944 0.66923 0.01111  0.26021  0.06697  75  TYR A CZ  
607  O OH  . TYR A 78  ? 0.91969 0.76750 0.73237 0.01528  0.29741  0.05600  75  TYR A OH  
608  N N   . ILE A 79  ? 0.74501 0.54136 0.53263 0.03633  0.08482  0.08156  76  ILE A N   
609  C CA  . ILE A 79  ? 0.70211 0.49958 0.51246 0.04495  0.06164  0.07569  76  ILE A CA  
610  C C   . ILE A 79  ? 0.67664 0.50841 0.53610 0.03952  0.06406  0.06474  76  ILE A C   
611  O O   . ILE A 79  ? 0.67981 0.53966 0.55409 0.04488  0.06658  0.05595  76  ILE A O   
612  C CB  . ILE A 79  ? 0.70332 0.50618 0.50264 0.06338  0.04014  0.06777  76  ILE A CB  
613  C CG1 . ILE A 79  ? 0.67708 0.44566 0.42809 0.07206  0.02647  0.08098  76  ILE A CG1 
614  C CG2 . ILE A 79  ? 0.69668 0.51059 0.52888 0.07257  0.02737  0.05678  76  ILE A CG2 
615  C CD1 . ILE A 79  ? 0.75169 0.52811 0.47022 0.07542  0.02001  0.07654  76  ILE A CD1 
616  N N   . THR A 80  ? 0.65682 0.48199 0.53669 0.02836  0.06168  0.06562  77  THR A N   
617  C CA  . THR A 80  ? 0.64128 0.49716 0.56028 0.02248  0.05656  0.05648  77  THR A CA  
618  C C   . THR A 80  ? 0.65025 0.50079 0.56246 0.03339  0.03925  0.04417  77  THR A C   
619  O O   . THR A 80  ? 0.68265 0.50286 0.58298 0.03203  0.03171  0.04107  77  THR A O   
620  C CB  . THR A 80  ? 0.64999 0.50825 0.59851 0.00056  0.06052  0.06043  77  THR A CB  
621  O OG1 . THR A 80  ? 0.72763 0.59253 0.68447 -0.00867 0.08533  0.07175  77  THR A OG1 
622  C CG2 . THR A 80  ? 0.64634 0.53987 0.63368 -0.00465 0.04667  0.05200  77  THR A CG2 
623  N N   . VAL A 81  ? 0.55852 0.43288 0.47659 0.04346  0.03763  0.03739  78  VAL A N   
624  C CA  . VAL A 81  ? 0.56814 0.43769 0.47737 0.05224  0.02906  0.02570  78  VAL A CA  
625  C C   . VAL A 81  ? 0.52906 0.40659 0.44435 0.04314  0.01957  0.02142  78  VAL A C   
626  O O   . VAL A 81  ? 0.57275 0.47657 0.50678 0.04155  0.01970  0.02727  78  VAL A O   
627  C CB  . VAL A 81  ? 0.54765 0.43218 0.45623 0.06498  0.03475  0.02143  78  VAL A CB  
628  C CG1 . VAL A 81  ? 0.55217 0.43026 0.45339 0.07290  0.03447  0.00988  78  VAL A CG1 
629  C CG2 . VAL A 81  ? 0.47856 0.36080 0.38142 0.07092  0.03646  0.02479  78  VAL A CG2 
630  N N   . PRO A 82  ? 0.74096 0.59497 0.63954 0.03768  0.00946  0.01099  79  PRO A N   
631  C CA  . PRO A 82  ? 0.71890 0.57939 0.61212 0.02833  -0.00601 0.00550  79  PRO A CA  
632  C C   . PRO A 82  ? 0.76823 0.64290 0.64760 0.03994  -0.00433 0.00693  79  PRO A C   
633  O O   . PRO A 82  ? 0.71220 0.57945 0.57704 0.05218  0.01012  0.00330  79  PRO A O   
634  C CB  . PRO A 82  ? 0.70075 0.52064 0.56310 0.02273  -0.01218 -0.01099 79  PRO A CB  
635  C CG  . PRO A 82  ? 0.77231 0.56688 0.64041 0.02551  -0.00183 -0.00860 79  PRO A CG  
636  C CD  . PRO A 82  ? 0.72187 0.53777 0.60297 0.04085  0.01062  0.00330  79  PRO A CD  
637  N N   . GLY A 83  ? 0.59803 0.49356 0.48625 0.03584  -0.01957 0.01368  80  GLY A N   
638  C CA  . GLY A 83  ? 0.59503 0.49613 0.46578 0.04748  -0.01811 0.02039  80  GLY A CA  
639  C C   . GLY A 83  ? 0.59723 0.46656 0.41248 0.05109  -0.01300 0.00967  80  GLY A C   
640  O O   . GLY A 83  ? 0.59631 0.46059 0.39465 0.06078  0.00316  0.01391  80  GLY A O   
641  N N   . ARG A 84  ? 0.70056 0.54406 0.48589 0.04181  -0.02259 -0.00576 81  ARG A N   
642  C CA  . ARG A 84  ? 0.73899 0.54728 0.46584 0.04525  -0.01170 -0.01942 81  ARG A CA  
643  C C   . ARG A 84  ? 0.74906 0.55209 0.48531 0.05788  0.02118  -0.02493 81  ARG A C   
644  O O   . ARG A 84  ? 0.78171 0.56829 0.48392 0.06373  0.04138  -0.03051 81  ARG A O   
645  C CB  . ARG A 84  ? 0.74279 0.51836 0.43629 0.03217  -0.02628 -0.03942 81  ARG A CB  
646  C CG  . ARG A 84  ? 0.74458 0.51293 0.47452 0.02682  -0.02360 -0.04659 81  ARG A CG  
647  C CD  . ARG A 84  ? 0.77273 0.49816 0.46627 0.01226  -0.03540 -0.06907 81  ARG A CD  
648  N NE  . ARG A 84  ? 0.79996 0.50398 0.52081 0.01040  -0.02670 -0.07446 81  ARG A NE  
649  C CZ  . ARG A 84  ? 0.84401 0.52263 0.56302 0.02760  -0.00224 -0.08176 81  ARG A CZ  
650  N NH1 . ARG A 84  ? 0.75480 0.43225 0.45433 0.04540  0.01975  -0.08739 81  ARG A NH1 
651  N NH2 . ARG A 84  ? 0.83056 0.48461 0.57171 0.02745  0.00107  -0.08190 81  ARG A NH2 
652  N N   . ILE A 85  ? 0.67592 0.49361 0.45827 0.06168  0.02673  -0.02288 82  ILE A N   
653  C CA  . ILE A 85  ? 0.66796 0.49077 0.47084 0.07432  0.04967  -0.02711 82  ILE A CA  
654  C C   . ILE A 85  ? 0.67381 0.51623 0.48428 0.07816  0.06451  -0.01853 82  ILE A C   
655  O O   . ILE A 85  ? 0.67548 0.52098 0.49509 0.08468  0.08667  -0.02545 82  ILE A O   
656  C CB  . ILE A 85  ? 0.63440 0.46725 0.47603 0.07759  0.04444  -0.02256 82  ILE A CB  
657  C CG1 . ILE A 85  ? 0.67146 0.47672 0.50442 0.07029  0.03156  -0.02736 82  ILE A CG1 
658  C CG2 . ILE A 85  ? 0.61982 0.46066 0.48625 0.09218  0.05905  -0.02834 82  ILE A CG2 
659  C CD1 . ILE A 85  ? 0.60848 0.37954 0.42774 0.07974  0.04125  -0.04404 82  ILE A CD1 
660  N N   . LEU A 86  ? 0.66648 0.52182 0.47924 0.07408  0.05439  -0.00382 83  LEU A N   
661  C CA  . LEU A 86  ? 0.64265 0.50729 0.46212 0.07684  0.06870  0.00565  83  LEU A CA  
662  C C   . LEU A 86  ? 0.69627 0.54279 0.47198 0.07616  0.06638  0.01609  83  LEU A C   
663  O O   . LEU A 86  ? 0.69380 0.53981 0.47183 0.07864  0.07643  0.02833  83  LEU A O   
664  C CB  . LEU A 86  ? 0.57465 0.46178 0.43270 0.07710  0.06337  0.01505  83  LEU A CB  
665  C CG  . LEU A 86  ? 0.53985 0.43991 0.42802 0.07800  0.06447  0.00816  83  LEU A CG  
666  C CD1 . LEU A 86  ? 0.55193 0.46560 0.46110 0.07656  0.06162  0.01606  83  LEU A CD1 
667  C CD2 . LEU A 86  ? 0.52965 0.43551 0.43202 0.08103  0.08071  -0.00172 83  LEU A CD2 
668  N N   . SER A 87  ? 0.80194 0.62817 0.53270 0.07259  0.05164  0.01176  84  SER A N   
669  C CA  . SER A 87  ? 0.89432 0.69727 0.56741 0.07260  0.04321  0.02263  84  SER A CA  
670  C C   . SER A 87  ? 0.92931 0.74962 0.62324 0.07742  0.02043  0.04456  84  SER A C   
671  O O   . SER A 87  ? 0.89150 0.69489 0.55515 0.08365  0.02213  0.06184  84  SER A O   
672  C CB  . SER A 87  ? 0.80073 0.57803 0.43621 0.07455  0.07819  0.02390  84  SER A CB  
673  O OG  . SER A 87  ? 1.08777 0.84841 0.70153 0.07243  0.10046  0.00264  84  SER A OG  
674  N N   . ILE A 88  ? 0.76541 0.61721 0.51275 0.07573  0.00172  0.04511  85  ILE A N   
675  C CA  . ILE A 88  ? 0.74645 0.62220 0.52918 0.08245  -0.01788 0.06321  85  ILE A CA  
676  C C   . ILE A 88  ? 0.76039 0.65932 0.56595 0.07335  -0.05128 0.05921  85  ILE A C   
677  O O   . ILE A 88  ? 0.74211 0.63439 0.53914 0.06051  -0.05527 0.04210  85  ILE A O   
678  C CB  . ILE A 88  ? 0.68549 0.58153 0.52495 0.08858  0.00273  0.06753  85  ILE A CB  
679  C CG1 . ILE A 88  ? 0.65578 0.56984 0.53068 0.07985  0.00811  0.05367  85  ILE A CG1 
680  C CG2 . ILE A 88  ? 0.60250 0.47617 0.42520 0.09240  0.03337  0.06836  85  ILE A CG2 
681  C CD1 . ILE A 88  ? 0.59103 0.52129 0.50879 0.08402  0.02553  0.05614  85  ILE A CD1 
682  N N   . ASN A 89  ? 1.05669 0.98299 0.89787 0.08011  -0.07484 0.07503  86  ASN A N   
683  C CA  . ASN A 89  ? 1.09976 1.05738 0.97638 0.06857  -0.10968 0.07146  86  ASN A CA  
684  C C   . ASN A 89  ? 1.08799 1.07836 1.03831 0.06143  -0.09379 0.06674  86  ASN A C   
685  O O   . ASN A 89  ? 1.15735 1.15380 1.12175 0.04266  -0.10304 0.05389  86  ASN A O   
686  C CB  . ASN A 89  ? 1.15438 1.13197 1.04053 0.07962  -0.14764 0.09038  86  ASN A CB  
687  C CG  . ASN A 89  ? 1.20340 1.20313 1.14455 0.10211  -0.13615 0.11138  86  ASN A CG  
688  O OD1 . ASN A 89  ? 1.10316 1.07191 1.01252 0.11645  -0.11355 0.12194  86  ASN A OD1 
689  N ND2 . ASN A 89  ? 1.23954 1.29090 1.26646 0.10466  -0.14857 0.11643  86  ASN A ND2 
690  N N   . ARG A 90  ? 0.86358 0.86606 0.85092 0.07433  -0.06744 0.07573  87  ARG A N   
691  C CA  . ARG A 90  ? 0.79098 0.81856 0.83604 0.06818  -0.04719 0.07243  87  ARG A CA  
692  C C   . ARG A 90  ? 0.79730 0.79807 0.81271 0.05684  -0.02678 0.05838  87  ARG A C   
693  O O   . ARG A 90  ? 0.80092 0.77081 0.76603 0.05958  -0.02152 0.05196  87  ARG A O   
694  C CB  . ARG A 90  ? 0.72050 0.75536 0.79442 0.08614  -0.02142 0.08210  87  ARG A CB  
695  C CG  . ARG A 90  ? 0.91138 0.96759 1.01985 0.10499  -0.03767 0.09925  87  ARG A CG  
696  C CD  . ARG A 90  ? 0.83062 0.86489 0.93350 0.12420  -0.01053 0.10631  87  ARG A CD  
697  N NE  . ARG A 90  ? 0.80122 0.84588 0.93409 0.14726  -0.02482 0.12570  87  ARG A NE  
698  C CZ  . ARG A 90  ? 0.94083 0.96322 1.03149 0.15753  -0.04948 0.14049  87  ARG A CZ  
699  N NH1 . ARG A 90  ? 1.05454 1.04417 1.07093 0.14486  -0.05723 0.13510  87  ARG A NH1 
700  N NH2 . ARG A 90  ? 1.00813 1.03739 1.12821 0.18227  -0.06437 0.16169  87  ARG A NH2 
701  N N   . ASP A 91  ? 0.65856 0.67059 0.70635 0.04597  -0.01385 0.05561  88  ASP A N   
702  C CA  . ASP A 91  ? 0.64169 0.62507 0.66054 0.03966  0.00339  0.04714  88  ASP A CA  
703  C C   . ASP A 91  ? 0.61023 0.59115 0.62802 0.05092  0.02979  0.04996  88  ASP A C   
704  O O   . ASP A 91  ? 0.61894 0.61791 0.66291 0.06062  0.03795  0.05659  88  ASP A O   
705  C CB  . ASP A 91  ? 0.68494 0.66921 0.72517 0.02013  0.00277  0.04509  88  ASP A CB  
706  C CG  . ASP A 91  ? 0.72212 0.68835 0.74372 0.00557  -0.02095 0.03466  88  ASP A CG  
707  O OD1 . ASP A 91  ? 0.82308 0.77764 0.81009 0.01156  -0.03716 0.02860  88  ASP A OD1 
708  O OD2 . ASP A 91  ? 0.73616 0.69454 0.77319 -0.01310 -0.02043 0.03205  88  ASP A OD2 
709  N N   . VAL A 92  ? 0.59395 0.55122 0.58162 0.05087  0.04011  0.04410  89  VAL A N   
710  C CA  . VAL A 92  ? 0.60184 0.55432 0.58063 0.05835  0.05927  0.04308  89  VAL A CA  
711  C C   . VAL A 92  ? 0.71134 0.65022 0.67660 0.05112  0.06863  0.04416  89  VAL A C   
712  O O   . VAL A 92  ? 0.67657 0.59650 0.62307 0.04741  0.05916  0.04290  89  VAL A O   
713  C CB  . VAL A 92  ? 0.59875 0.53898 0.55372 0.06654  0.05900  0.03578  89  VAL A CB  
714  C CG1 . VAL A 92  ? 0.58517 0.51878 0.52880 0.06864  0.07122  0.03026  89  VAL A CG1 
715  C CG2 . VAL A 92  ? 0.63492 0.57974 0.59480 0.07361  0.05776  0.03940  89  VAL A CG2 
716  N N   . LEU A 93  ? 0.55265 0.49571 0.52303 0.05031  0.08862  0.04709  90  LEU A N   
717  C CA  . LEU A 93  ? 0.61608 0.53909 0.55986 0.04255  0.10076  0.05130  90  LEU A CA  
718  C C   . LEU A 93  ? 0.63236 0.53948 0.53727 0.04900  0.10776  0.04475  90  LEU A C   
719  O O   . LEU A 93  ? 0.62585 0.53995 0.53763 0.05299  0.12391  0.03922  90  LEU A O   
720  C CB  . LEU A 93  ? 0.60257 0.54028 0.57781 0.03248  0.12310  0.05876  90  LEU A CB  
721  C CG  . LEU A 93  ? 0.65203 0.59376 0.65367 0.01643  0.11678  0.06562  90  LEU A CG  
722  C CD1 . LEU A 93  ? 0.52406 0.49693 0.57204 0.01655  0.09488  0.06255  90  LEU A CD1 
723  C CD2 . LEU A 93  ? 0.57044 0.51823 0.59305 0.00257  0.14811  0.07372  90  LEU A CD2 
724  N N   . ILE A 94  ? 0.59502 0.48052 0.46255 0.05061  0.09334  0.04451  91  ILE A N   
725  C CA  . ILE A 94  ? 0.57099 0.44325 0.39915 0.05432  0.09098  0.03689  91  ILE A CA  
726  C C   . ILE A 94  ? 0.65338 0.49517 0.43095 0.04902  0.09638  0.04743  91  ILE A C   
727  O O   . ILE A 94  ? 0.66482 0.48956 0.43109 0.04907  0.08423  0.05896  91  ILE A O   
728  C CB  . ILE A 94  ? 0.61955 0.49729 0.45054 0.06235  0.06545  0.02887  91  ILE A CB  
729  C CG1 . ILE A 94  ? 0.56120 0.45991 0.43385 0.06578  0.06334  0.02378  91  ILE A CG1 
730  C CG2 . ILE A 94  ? 0.60341 0.47850 0.40964 0.06253  0.05930  0.01641  91  ILE A CG2 
731  C CD1 . ILE A 94  ? 0.57414 0.48369 0.46054 0.06599  0.07334  0.01352  91  ILE A CD1 
732  N N   . HIS A 95  ? 0.73675 0.56527 0.47855 0.04503  0.11604  0.04332  92  HIS A N   
733  C CA  . HIS A 95  ? 0.76289 0.55428 0.43900 0.03919  0.12456  0.05439  92  HIS A CA  
734  C C   . HIS A 95  ? 0.81011 0.58140 0.43959 0.04677  0.08784  0.05723  92  HIS A C   
735  O O   . HIS A 95  ? 0.83153 0.62119 0.47512 0.05380  0.06299  0.04329  92  HIS A O   
736  C CB  . HIS A 95  ? 0.79788 0.57553 0.43695 0.03378  0.15699  0.04479  92  HIS A CB  
737  C CG  . HIS A 95  ? 0.88295 0.61869 0.45022 0.02490  0.17819  0.05855  92  HIS A CG  
738  N ND1 . HIS A 95  ? 0.86118 0.55758 0.33690 0.02456  0.16689  0.05673  92  HIS A ND1 
739  C CD2 . HIS A 95  ? 0.86562 0.59015 0.43587 0.01417  0.21031  0.07533  92  HIS A CD2 
740  C CE1 . HIS A 95  ? 0.95183 0.60854 0.36690 0.01549  0.19348  0.07385  92  HIS A CE1 
741  N NE2 . HIS A 95  ? 0.98973 0.66338 0.46485 0.00800  0.22306  0.08530  92  HIS A NE2 
742  N N   . LYS A 96  ? 0.95272 0.68619 0.53052 0.04540  0.08458  0.07697  93  LYS A N   
743  C CA  . LYS A 96  ? 1.02853 0.74171 0.56540 0.05726  0.04501  0.08494  93  LYS A CA  
744  C C   . LYS A 96  ? 1.03579 0.74699 0.52370 0.05895  0.02523  0.07013  93  LYS A C   
745  O O   . LYS A 96  ? 1.06660 0.78534 0.55222 0.07063  -0.01652 0.06867  93  LYS A O   
746  C CB  . LYS A 96  ? 1.11142 0.77208 0.58963 0.05563  0.04886  0.11313  93  LYS A CB  
747  C CG  . LYS A 96  ? 1.23786 0.89330 0.76320 0.05174  0.06096  0.12629  93  LYS A CG  
748  C CD  . LYS A 96  ? 1.46316 1.05629 0.92639 0.04748  0.06846  0.15582  93  LYS A CD  
749  C CE  . LYS A 96  ? 1.46379 1.02542 0.88400 0.06937  0.02455  0.17058  93  LYS A CE  
750  N NZ  . LYS A 96  ? 1.44079 0.94298 0.81662 0.06597  0.03100  0.19946  93  LYS A NZ  
751  N N   . SER A 97  ? 0.89836 0.60006 0.35052 0.04744  0.05381  0.05718  94  SER A N   
752  C CA  . SER A 97  ? 0.99436 0.68809 0.39372 0.04488  0.03528  0.03778  94  SER A CA  
753  C C   . SER A 97  ? 0.98082 0.71964 0.44687 0.04797  0.00968  0.01463  94  SER A C   
754  O O   . SER A 97  ? 1.06057 0.79983 0.49697 0.04513  -0.01975 -0.00177 94  SER A O   
755  C CB  . SER A 97  ? 0.95798 0.62649 0.30803 0.03212  0.07999  0.02469  94  SER A CB  
756  O OG  . SER A 97  ? 1.01125 0.71107 0.43777 0.03035  0.11283  0.01155  94  SER A OG  
757  N N   . ILE A 98  ? 0.81137 0.58589 0.36317 0.05147  0.02031  0.01271  95  ILE A N   
758  C CA  . ILE A 98  ? 0.82278 0.63610 0.43818 0.05289  0.00342  -0.00569 95  ILE A CA  
759  C C   . ILE A 98  ? 0.81087 0.64630 0.46489 0.06614  -0.03136 0.00369  95  ILE A C   
760  O O   . ILE A 98  ? 0.73785 0.57005 0.41176 0.07456  -0.02663 0.02110  95  ILE A O   
761  C CB  . ILE A 98  ? 0.71333 0.54601 0.38886 0.05060  0.03588  -0.01126 95  ILE A CB  
762  C CG1 . ILE A 98  ? 0.70127 0.51339 0.34890 0.04230  0.07107  -0.02208 95  ILE A CG1 
763  C CG2 . ILE A 98  ? 0.63018 0.49574 0.36578 0.05103  0.02291  -0.02551 95  ILE A CG2 
764  C CD1 . ILE A 98  ? 0.74369 0.56427 0.43274 0.04499  0.10566  -0.01254 95  ILE A CD1 
765  N N   . LYS A 99  ? 0.89130 0.74945 0.56045 0.06760  -0.06558 -0.00976 96  LYS A N   
766  C CA  . LYS A 99  ? 0.89617 0.78104 0.61284 0.08361  -0.09747 -0.00292 96  LYS A CA  
767  C C   . LYS A 99  ? 0.75196 0.66661 0.54690 0.08725  -0.07757 -0.00677 96  LYS A C   
768  O O   . LYS A 99  ? 0.78585 0.71986 0.61548 0.07618  -0.05980 -0.02319 96  LYS A O   
769  C CB  . LYS A 99  ? 0.84614 0.75905 0.57500 0.08245  -0.13937 -0.01890 96  LYS A CB  
770  C CG  . LYS A 99  ? 1.24265 1.12329 0.88150 0.07929  -0.16827 -0.01599 96  LYS A CG  
771  C CD  . LYS A 99  ? 1.34974 1.26634 1.01066 0.07575  -0.21719 -0.03501 96  LYS A CD  
772  C CE  . LYS A 99  ? 1.32904 1.20863 0.88526 0.07150  -0.25167 -0.03338 96  LYS A CE  
773  N NZ  . LYS A 99  ? 1.31114 1.23111 0.89291 0.06598  -0.30803 -0.05396 96  LYS A NZ  
774  N N   . LEU A 100 ? 0.75227 0.66320 0.56766 0.10247  -0.07941 0.00843  97  LEU A N   
775  C CA  . LEU A 100 ? 0.68652 0.61870 0.56255 0.10663  -0.06150 0.00363  97  LEU A CA  
776  C C   . LEU A 100 ? 0.62467 0.60133 0.56454 0.11199  -0.07682 -0.01173 97  LEU A C   
777  O O   . LEU A 100 ? 0.65178 0.64247 0.61329 0.12831  -0.10574 -0.00824 97  LEU A O   
778  C CB  . LEU A 100 ? 0.64630 0.55363 0.51900 0.11962  -0.05832 0.02013  97  LEU A CB  
779  C CG  . LEU A 100 ? 0.72339 0.59849 0.56031 0.10839  -0.03359 0.03125  97  LEU A CG  
780  C CD1 . LEU A 100 ? 0.73009 0.57567 0.56393 0.11738  -0.03384 0.04495  97  LEU A CD1 
781  C CD2 . LEU A 100 ? 0.58235 0.47473 0.44398 0.09640  -0.00783 0.02052  97  LEU A CD2 
782  N N   . GLU A 101 ? 0.70904 0.70782 0.68316 0.09866  -0.05634 -0.02744 98  GLU A N   
783  C CA  . GLU A 101 ? 0.68151 0.72436 0.72505 0.09828  -0.05990 -0.04301 98  GLU A CA  
784  C C   . GLU A 101 ? 0.62265 0.66741 0.68880 0.08830  -0.02168 -0.04907 98  GLU A C   
785  O O   . GLU A 101 ? 0.59303 0.60865 0.62187 0.08296  -0.00094 -0.04159 98  GLU A O   
786  C CB  . GLU A 101 ? 0.73389 0.79964 0.78609 0.08463  -0.08469 -0.05863 98  GLU A CB  
787  C CG  . GLU A 101 ? 0.73958 0.78200 0.75233 0.06214  -0.06661 -0.06830 98  GLU A CG  
788  C CD  . GLU A 101 ? 0.86116 0.91706 0.87183 0.04564  -0.09319 -0.08791 98  GLU A CD  
789  O OE1 . GLU A 101 ? 0.86194 0.94638 0.89323 0.05277  -0.13341 -0.09051 98  GLU A OE1 
790  O OE2 . GLU A 101 ? 0.99154 1.02781 0.98042 0.02606  -0.07585 -0.10146 98  GLU A OE2 
791  N N   . ARG A 102 ? 0.60113 0.68115 0.73009 0.08600  -0.01237 -0.06149 99  ARG A N   
792  C CA  . ARG A 102 ? 0.54268 0.61706 0.68228 0.07694  0.02582  -0.06412 99  ARG A CA  
793  C C   . ARG A 102 ? 0.53612 0.59196 0.65107 0.05635  0.04018  -0.06758 99  ARG A C   
794  O O   . ARG A 102 ? 0.52423 0.55340 0.61251 0.05346  0.06496  -0.05950 99  ARG A O   
795  C CB  . ARG A 102 ? 0.46588 0.58021 0.67825 0.07731  0.03996  -0.07640 99  ARG A CB  
796  C CG  . ARG A 102 ? 0.59727 0.69478 0.80311 0.07643  0.08077  -0.07392 99  ARG A CG  
797  C CD  . ARG A 102 ? 0.52701 0.65929 0.79971 0.06693  0.10806  -0.08727 99  ARG A CD  
798  N NE  . ARG A 102 ? 0.56795 0.67059 0.81043 0.06053  0.15034  -0.08250 99  ARG A NE  
799  C CZ  . ARG A 102 ? 0.61235 0.71955 0.87856 0.04146  0.18398  -0.08745 99  ARG A CZ  
800  N NH1 . ARG A 102 ? 0.67673 0.82130 1.00780 0.02379  0.18152  -0.10047 99  ARG A NH1 
801  N NH2 . ARG A 102 ? 0.63382 0.70392 0.85396 0.03810  0.21996  -0.07879 99  ARG A NH2 
802  N N   . LYS A 103 ? 0.58567 0.65167 0.70666 0.04295  0.02281  -0.07992 100 LYS A N   
803  C CA  . LYS A 103 ? 0.55429 0.59543 0.65305 0.02405  0.03857  -0.08658 100 LYS A CA  
804  C C   . LYS A 103 ? 0.62811 0.62823 0.66498 0.03002  0.04678  -0.07352 100 LYS A C   
805  O O   . LYS A 103 ? 0.66805 0.64210 0.68936 0.02114  0.06739  -0.07478 100 LYS A O   
806  C CB  . LYS A 103 ? 0.61123 0.66666 0.72151 0.00709  0.01443  -0.10698 100 LYS A CB  
807  C CG  . LYS A 103 ? 0.76011 0.86438 0.94966 -0.00473 0.00795  -0.12315 100 LYS A CG  
808  C CD  . LYS A 103 ? 0.86528 0.98534 1.06406 -0.02408 -0.02503 -0.14564 100 LYS A CD  
809  C CE  . LYS A 103 ? 0.85580 1.03469 1.15063 -0.03904 -0.03310 -0.16337 100 LYS A CE  
810  N NZ  . LYS A 103 ? 0.95413 1.15246 1.25915 -0.06017 -0.07457 -0.18777 100 LYS A NZ  
811  N N   . VAL A 104 ? 0.60986 0.60320 0.61681 0.04493  0.03296  -0.06071 101 VAL A N   
812  C CA  . VAL A 104 ? 0.54593 0.50906 0.50991 0.04947  0.04523  -0.04772 101 VAL A CA  
813  C C   . VAL A 104 ? 0.48216 0.43702 0.45474 0.05267  0.06858  -0.03750 101 VAL A C   
814  O O   . VAL A 104 ? 0.52157 0.45696 0.47835 0.05239  0.08349  -0.03123 101 VAL A O   
815  C CB  . VAL A 104 ? 0.57919 0.53577 0.51487 0.06093  0.02846  -0.03524 101 VAL A CB  
816  C CG1 . VAL A 104 ? 0.49619 0.43138 0.40662 0.06352  0.04496  -0.02145 101 VAL A CG1 
817  C CG2 . VAL A 104 ? 0.59381 0.54626 0.49910 0.05797  0.00521  -0.04135 101 VAL A CG2 
818  N N   . PHE A 105 ? 0.56344 0.53182 0.55975 0.05714  0.07191  -0.03590 102 PHE A N   
819  C CA  . PHE A 105 ? 0.53276 0.48839 0.52133 0.06072  0.08905  -0.02547 102 PHE A CA  
820  C C   . PHE A 105 ? 0.57225 0.52533 0.57704 0.05208  0.11147  -0.02898 102 PHE A C   
821  O O   . PHE A 105 ? 0.53843 0.46978 0.52250 0.05336  0.12557  -0.01750 102 PHE A O   
822  C CB  . PHE A 105 ? 0.55458 0.51336 0.54026 0.07138  0.08218  -0.02141 102 PHE A CB  
823  C CG  . PHE A 105 ? 0.49456 0.44831 0.46386 0.07778  0.06320  -0.01561 102 PHE A CG  
824  C CD1 . PHE A 105 ? 0.49771 0.43613 0.44396 0.07768  0.06275  -0.00446 102 PHE A CD1 
825  C CD2 . PHE A 105 ? 0.53374 0.49796 0.51323 0.08348  0.04542  -0.01969 102 PHE A CD2 
826  C CE1 . PHE A 105 ? 0.52146 0.45155 0.45366 0.07955  0.05127  0.00198  102 PHE A CE1 
827  C CE2 . PHE A 105 ? 0.53730 0.48670 0.49267 0.08868  0.03080  -0.01041 102 PHE A CE2 
828  C CZ  . PHE A 105 ? 0.56908 0.49959 0.50001 0.08487  0.03693  0.00018  102 PHE A CZ  
829  N N   . ALA A 106 ? 0.64142 0.61556 0.68345 0.04249  0.11439  -0.04321 103 ALA A N   
830  C CA  . ALA A 106 ? 0.68785 0.65988 0.75094 0.03058  0.14165  -0.04647 103 ALA A CA  
831  C C   . ALA A 106 ? 0.70770 0.68153 0.79640 0.01125  0.14512  -0.06015 103 ALA A C   
832  O O   . ALA A 106 ? 0.65150 0.64799 0.76029 0.00631  0.12193  -0.07454 103 ALA A O   
833  C CB  . ALA A 106 ? 0.58013 0.58079 0.68013 0.03349  0.15072  -0.05381 103 ALA A CB  
834  N N   . SER A 107 ? 0.58483 0.52922 0.66722 -0.00033 0.17253  -0.05539 104 SER A N   
835  C CA  . SER A 107 ? 0.56709 0.50734 0.68016 -0.02409 0.18388  -0.07048 104 SER A CA  
836  C C   . SER A 107 ? 0.54831 0.51171 0.71069 -0.03914 0.20858  -0.07672 104 SER A C   
837  O O   . SER A 107 ? 0.56115 0.53683 0.72444 -0.02852 0.22085  -0.06876 104 SER A O   
838  C CB  . SER A 107 ? 0.52731 0.41195 0.60540 -0.02762 0.20295  -0.06032 104 SER A CB  
839  O OG  . SER A 107 ? 0.65926 0.53095 0.76400 -0.05314 0.21415  -0.07790 104 SER A OG  
840  N N   . GLU A 108 ? 0.78491 0.75297 0.98988 -0.06593 0.21862  -0.09335 105 GLU A N   
841  C CA  . GLU A 108 ? 0.77127 0.76753 1.03776 -0.08513 0.24673  -0.10145 105 GLU A CA  
842  C C   . GLU A 108 ? 0.77079 0.72800 1.00086 -0.08202 0.29077  -0.07892 105 GLU A C   
843  O O   . GLU A 108 ? 0.75938 0.65875 0.92431 -0.07443 0.30051  -0.05864 105 GLU A O   
844  C CB  . GLU A 108 ? 0.79547 0.79286 1.11000 -0.12012 0.25248  -0.12253 105 GLU A CB  
845  C CG  . GLU A 108 ? 0.89463 0.95076 1.26619 -0.12923 0.20947  -0.15004 105 GLU A CG  
846  C CD  . GLU A 108 ? 0.94456 1.07519 1.39987 -0.12747 0.20671  -0.15889 105 GLU A CD  
847  O OE1 . GLU A 108 ? 0.92064 1.06406 1.42710 -0.14475 0.24813  -0.15974 105 GLU A OE1 
848  O OE2 . GLU A 108 ? 0.94181 1.11597 1.41274 -0.10767 0.16579  -0.16390 105 GLU A OE2 
849  N N   . ARG A 109 ? 0.78895 0.77837 1.06091 -0.08634 0.31727  -0.08243 106 ARG A N   
850  C CA  . ARG A 109 ? 0.79430 0.74914 1.02207 -0.08198 0.36027  -0.06318 106 ARG A CA  
851  C C   . ARG A 109 ? 0.82363 0.75631 0.97561 -0.05060 0.34286  -0.04652 106 ARG A C   
852  O O   . ARG A 109 ? 0.79171 0.67341 0.87244 -0.04491 0.36401  -0.02537 106 ARG A O   
853  C CB  . ARG A 109 ? 0.73494 0.62407 0.92452 -0.10189 0.39718  -0.04655 106 ARG A CB  
854  C CG  . ARG A 109 ? 0.76984 0.67195 1.03099 -0.13712 0.41905  -0.06321 106 ARG A CG  
855  C CD  . ARG A 109 ? 0.88540 0.84223 1.21121 -0.14200 0.43206  -0.07758 106 ARG A CD  
856  N NE  . ARG A 109 ? 0.89749 0.81456 1.16446 -0.13340 0.46324  -0.05900 106 ARG A NE  
857  C CZ  . ARG A 109 ? 0.93212 0.83918 1.21849 -0.15206 0.49831  -0.05982 106 ARG A CZ  
858  N NH1 . ARG A 109 ? 1.00808 0.94507 1.37644 -0.18037 0.50569  -0.07842 106 ARG A NH1 
859  N NH2 . ARG A 109 ? 1.02232 0.88867 1.24341 -0.14343 0.52611  -0.04288 106 ARG A NH2 
860  N N   . ASN A 110 ? 0.60030 0.56823 0.76475 -0.03166 0.30246  -0.05544 107 ASN A N   
861  C CA  . ASN A 110 ? 0.63016 0.58487 0.73828 -0.00601 0.28589  -0.04495 107 ASN A CA  
862  C C   . ASN A 110 ? 0.62014 0.52166 0.65098 0.00185  0.27615  -0.02283 107 ASN A C   
863  O O   . ASN A 110 ? 0.63880 0.51130 0.60979 0.01331  0.28053  -0.00904 107 ASN A O   
864  C CB  . ASN A 110 ? 0.66196 0.61734 0.76130 -0.00028 0.31861  -0.04625 107 ASN A CB  
865  C CG  . ASN A 110 ? 0.68761 0.70199 0.87865 -0.00425 0.33208  -0.06793 107 ASN A CG  
866  O OD1 . ASN A 110 ? 0.64973 0.70785 0.89108 0.00673  0.29835  -0.08021 107 ASN A OD1 
867  N ND2 . ASN A 110 ? 0.73615 0.74821 0.94385 -0.01928 0.36849  -0.06890 107 ASN A ND2 
868  N N   . VAL A 111 ? 0.62434 0.51341 0.65780 -0.00358 0.26156  -0.02083 108 VAL A N   
869  C CA  . VAL A 111 ? 0.63564 0.48160 0.61355 0.00734  0.25154  -0.00044 108 VAL A CA  
870  C C   . VAL A 111 ? 0.64887 0.51290 0.61642 0.02535  0.21470  -0.00074 108 VAL A C   
871  O O   . VAL A 111 ? 0.59174 0.48144 0.58931 0.02424  0.19511  -0.01443 108 VAL A O   
872  C CB  . VAL A 111 ? 0.68642 0.50418 0.67412 -0.00487 0.25989  0.00027  108 VAL A CB  
873  C CG1 . VAL A 111 ? 0.67404 0.45355 0.61714 0.01284  0.24803  0.02127  108 VAL A CG1 
874  C CG2 . VAL A 111 ? 0.67429 0.46603 0.67065 -0.02636 0.30030  0.00303  108 VAL A CG2 
875  N N   . SER A 112 ? 0.60891 0.45710 0.53063 0.03975  0.20510  0.01438  109 SER A N   
876  C CA  . SER A 112 ? 0.57120 0.43416 0.48608 0.05304  0.17391  0.01548  109 SER A CA  
877  C C   . SER A 112 ? 0.55887 0.41201 0.47724 0.05732  0.16387  0.02273  109 SER A C   
878  O O   . SER A 112 ? 0.59832 0.42392 0.49316 0.06456  0.16612  0.04058  109 SER A O   
879  C CB  . SER A 112 ? 0.60452 0.45337 0.47326 0.06262  0.16522  0.02653  109 SER A CB  
880  O OG  . SER A 112 ? 0.57475 0.44047 0.44642 0.07037  0.13749  0.02462  109 SER A OG  
881  N N   . ILE A 113 ? 0.60960 0.48287 0.55493 0.05463  0.15334  0.00922  110 ILE A N   
882  C CA  . ILE A 113 ? 0.59775 0.45968 0.54558 0.05852  0.15099  0.01136  110 ILE A CA  
883  C C   . ILE A 113 ? 0.58329 0.44396 0.51810 0.07405  0.13819  0.02834  110 ILE A C   
884  O O   . ILE A 113 ? 0.59802 0.43933 0.53153 0.08331  0.14327  0.04102  110 ILE A O   
885  C CB  . ILE A 113 ? 0.54221 0.42268 0.50533 0.05218  0.14115  -0.00710 110 ILE A CB  
886  C CG1 . ILE A 113 ? 0.60716 0.49166 0.59189 0.03480  0.14879  -0.02542 110 ILE A CG1 
887  C CG2 . ILE A 113 ? 0.50986 0.37695 0.46705 0.05839  0.14314  -0.00614 110 ILE A CG2 
888  C CD1 . ILE A 113 ? 0.58949 0.49374 0.58143 0.02839  0.13035  -0.04365 110 ILE A CD1 
889  N N   . PHE A 114 ? 0.56227 0.44402 0.49337 0.07719  0.12060  0.02852  111 PHE A N   
890  C CA  . PHE A 114 ? 0.58972 0.47826 0.51977 0.08713  0.10559  0.04160  111 PHE A CA  
891  C C   . PHE A 114 ? 0.65233 0.52707 0.55720 0.09317  0.09820  0.05719  111 PHE A C   
892  O O   . PHE A 114 ? 0.69180 0.57115 0.60199 0.10299  0.08361  0.07103  111 PHE A O   
893  C CB  . PHE A 114 ? 0.51513 0.42456 0.44977 0.08397  0.09070  0.03520  111 PHE A CB  
894  C CG  . PHE A 114 ? 0.51493 0.43154 0.45992 0.07941  0.09493  0.02410  111 PHE A CG  
895  C CD1 . PHE A 114 ? 0.54855 0.46546 0.50459 0.08214  0.10323  0.02537  111 PHE A CD1 
896  C CD2 . PHE A 114 ? 0.46644 0.38785 0.40781 0.07400  0.09082  0.01248  111 PHE A CD2 
897  C CE1 . PHE A 114 ? 0.48095 0.39654 0.42975 0.07682  0.10810  0.01467  111 PHE A CE1 
898  C CE2 . PHE A 114 ? 0.58381 0.50779 0.52324 0.07045  0.08882  0.00430  111 PHE A CE2 
899  C CZ  . PHE A 114 ? 0.49518 0.41303 0.43100 0.07049  0.09790  0.00511  111 PHE A CZ  
900  N N   . GLY A 115 ? 0.73212 0.59081 0.60937 0.08759  0.10796  0.05525  112 GLY A N   
901  C CA  . GLY A 115 ? 0.64675 0.48042 0.48238 0.09260  0.10471  0.07159  112 GLY A CA  
902  C C   . GLY A 115 ? 0.68538 0.49343 0.51861 0.10210  0.11151  0.09075  112 GLY A C   
903  O O   . GLY A 115 ? 0.70808 0.50413 0.51915 0.11412  0.09376  0.11063  112 GLY A O   
904  N N   . ARG A 116 ? 0.77541 0.57230 0.63163 0.09728  0.13477  0.08472  113 ARG A N   
905  C CA  . ARG A 116 ? 0.81415 0.57763 0.67099 0.10736  0.14498  0.10146  113 ARG A CA  
906  C C   . ARG A 116 ? 0.77539 0.55613 0.66784 0.12459  0.12987  0.10721  113 ARG A C   
907  O O   . ARG A 116 ? 0.85251 0.61618 0.74360 0.14324  0.12135  0.12942  113 ARG A O   
908  C CB  . ARG A 116 ? 0.81585 0.55770 0.68758 0.09285  0.17553  0.08844  113 ARG A CB  
909  C CG  . ARG A 116 ? 0.86779 0.59842 0.72106 0.07412  0.19693  0.08240  113 ARG A CG  
910  C CD  . ARG A 116 ? 0.86595 0.54674 0.71136 0.06527  0.22742  0.09103  113 ARG A CD  
911  N NE  . ARG A 116 ? 0.97674 0.61099 0.77373 0.08032  0.22759  0.12367  113 ARG A NE  
912  C CZ  . ARG A 116 ? 1.00998 0.62355 0.75353 0.07802  0.23401  0.13876  113 ARG A CZ  
913  N NH1 . ARG A 116 ? 1.03196 0.66893 0.77073 0.06250  0.24551  0.12243  113 ARG A NH1 
914  N NH2 . ARG A 116 ? 1.09434 0.65992 0.78503 0.09341  0.22920  0.17133  113 ARG A NH2 
915  N N   . LEU A 117 ? 0.76628 0.58030 0.69158 0.11988  0.12767  0.08874  114 LEU A N   
916  C CA  . LEU A 117 ? 0.73136 0.56311 0.69538 0.13410  0.12354  0.09136  114 LEU A CA  
917  C C   . LEU A 117 ? 0.75550 0.61353 0.73161 0.14745  0.09433  0.10893  114 LEU A C   
918  O O   . LEU A 117 ? 0.79325 0.65674 0.80245 0.16703  0.08938  0.12301  114 LEU A O   
919  C CB  . LEU A 117 ? 0.66262 0.51844 0.64455 0.12292  0.13044  0.06899  114 LEU A CB  
920  C CG  . LEU A 117 ? 0.64003 0.51746 0.65997 0.13336  0.13445  0.06810  114 LEU A CG  
921  C CD1 . LEU A 117 ? 0.64465 0.49506 0.68372 0.14924  0.15600  0.07115  114 LEU A CD1 
922  C CD2 . LEU A 117 ? 0.64753 0.53881 0.66305 0.11900  0.14163  0.04859  114 LEU A CD2 
923  N N   . SER A 118 ? 0.75957 0.63432 0.71325 0.13738  0.07375  0.10688  115 SER A N   
924  C CA  . SER A 118 ? 0.80879 0.71171 0.77572 0.14400  0.04118  0.11819  115 SER A CA  
925  C C   . SER A 118 ? 0.78039 0.66397 0.72895 0.16213  0.02246  0.14390  115 SER A C   
926  O O   . SER A 118 ? 0.84847 0.75971 0.83372 0.17636  -0.00383 0.15736  115 SER A O   
927  C CB  . SER A 118 ? 0.73804 0.65028 0.67495 0.12695  0.02527  0.10658  115 SER A CB  
928  O OG  . SER A 118 ? 0.87910 0.81577 0.82642 0.12853  -0.00938 0.11410  115 SER A OG  
929  N N   . LYS A 119 ? 0.85873 0.69526 0.75236 0.16185  0.03513  0.15256  116 LYS A N   
930  C CA  . LYS A 119 ? 0.98481 0.79050 0.84818 0.18069  0.01905  0.18181  116 LYS A CA  
931  C C   . LYS A 119 ? 0.90068 0.70110 0.81544 0.20533  0.02607  0.19689  116 LYS A C   
932  O O   . LYS A 119 ? 1.00979 0.80256 0.92481 0.22863  0.00042  0.22394  116 LYS A O   
933  C CB  . LYS A 119 ? 0.92247 0.67114 0.71107 0.17179  0.04070  0.18865  116 LYS A CB  
934  C CG  . LYS A 119 ? 1.19275 0.89932 0.92432 0.18889  0.02106  0.22238  116 LYS A CG  
935  C CD  . LYS A 119 ? 1.26316 0.91017 0.91285 0.17583  0.04951  0.22921  116 LYS A CD  
936  C CE  . LYS A 119 ? 1.14571 0.75509 0.73700 0.18715  0.02671  0.25922  116 LYS A CE  
937  N NZ  . LYS A 119 ? 1.30581 0.86573 0.82290 0.16830  0.05738  0.26081  116 LYS A NZ  
938  N N   . LEU A 120 ? 0.79007 0.59223 0.74610 0.20224  0.05873  0.17949  117 LEU A N   
939  C CA  . LEU A 120 ? 0.78085 0.57119 0.78474 0.22590  0.07320  0.18827  117 LEU A CA  
940  C C   . LEU A 120 ? 0.84720 0.69559 0.92846 0.24047  0.06043  0.18577  117 LEU A C   
941  O O   . LEU A 120 ? 0.86455 0.71200 0.99286 0.26442  0.06548  0.19520  117 LEU A O   
942  C CB  . LEU A 120 ? 0.84729 0.60421 0.85079 0.21349  0.11659  0.16679  117 LEU A CB  
943  C CG  . LEU A 120 ? 0.83362 0.53239 0.77993 0.19870  0.13675  0.16952  117 LEU A CG  
944  C CD1 . LEU A 120 ? 0.86169 0.54172 0.81645 0.17918  0.17195  0.14087  117 LEU A CD1 
945  C CD2 . LEU A 120 ? 0.85965 0.51236 0.78726 0.21743  0.13317  0.19834  117 LEU A CD2 
946  N N   . LEU A 121 ? 0.83842 0.73634 0.93472 0.22268  0.04666  0.17043  118 LEU A N   
947  C CA  . LEU A 121 ? 0.81389 0.77096 0.98963 0.23001  0.04090  0.16615  118 LEU A CA  
948  C C   . LEU A 121 ? 0.91457 0.90675 1.12636 0.24922  -0.00440 0.19018  118 LEU A C   
949  O O   . LEU A 121 ? 0.85929 0.84015 1.01647 0.24320  -0.03853 0.20110  118 LEU A O   
950  C CB  . LEU A 121 ? 0.80100 0.78864 0.97397 0.20111  0.04382  0.14343  118 LEU A CB  
951  C CG  . LEU A 121 ? 0.78311 0.74649 0.93067 0.18483  0.08194  0.12025  118 LEU A CG  
952  C CD1 . LEU A 121 ? 0.63894 0.62850 0.78189 0.16081  0.07978  0.10423  118 LEU A CD1 
953  C CD2 . LEU A 121 ? 0.73169 0.68744 0.91875 0.19970  0.11691  0.11408  118 LEU A CD2 
954  N N   . ASP A 122 ? 1.15688 1.19099 1.45780 0.27163  -0.00457 0.19688  119 ASP A N   
955  C CA  . ASP A 122 ? 1.19842 1.27598 1.54660 0.28877  -0.05383 0.21619  119 ASP A CA  
956  C C   . ASP A 122 ? 1.14348 1.29765 1.56072 0.27242  -0.07295 0.20687  119 ASP A C   
957  O O   . ASP A 122 ? 1.27411 1.47759 1.74738 0.28131  -0.11274 0.21514  119 ASP A O   
958  C CB  . ASP A 122 ? 1.17717 1.25040 1.57198 0.31583  -0.04663 0.22048  119 ASP A CB  
959  C CG  . ASP A 122 ? 1.32718 1.32419 1.65313 0.32984  -0.04476 0.23567  119 ASP A CG  
960  O OD1 . ASP A 122 ? 1.42913 1.39307 1.68069 0.32504  -0.07301 0.25202  119 ASP A OD1 
961  O OD2 . ASP A 122 ? 1.37417 1.34224 1.71786 0.34301  -0.01301 0.23057  119 ASP A OD2 
962  N N   . HIS A 123 ? 0.99069 1.14684 1.38894 0.24081  -0.04605 0.18168  120 HIS A N   
963  C CA  . HIS A 123 ? 0.85086 1.06932 1.30973 0.21808  -0.05569 0.16911  120 HIS A CA  
964  C C   . HIS A 123 ? 0.95516 1.15394 1.33903 0.18333  -0.07032 0.15459  120 HIS A C   
965  O O   . HIS A 123 ? 1.02481 1.16763 1.32426 0.17645  -0.05331 0.14816  120 HIS A O   
966  C CB  . HIS A 123 ? 0.86867 1.10775 1.38817 0.21588  -0.00225 0.15461  120 HIS A CB  
967  C CG  . HIS A 123 ? 0.96159 1.14282 1.40844 0.20542  0.04267  0.13858  120 HIS A CG  
968  N ND1 . HIS A 123 ? 0.88460 1.04910 1.27633 0.17441  0.05086  0.12248  120 HIS A ND1 
969  C CD2 . HIS A 123 ? 0.90345 1.03934 1.32531 0.22137  0.07832  0.13536  120 HIS A CD2 
970  C CE1 . HIS A 123 ? 0.85376 0.97162 1.19229 0.17248  0.08546  0.11105  120 HIS A CE1 
971  N NE2 . HIS A 123 ? 0.99017 1.08912 1.34463 0.19853  0.10322  0.11679  120 HIS A NE2 
972  N N   . THR A 124 ? 0.99416 1.23771 1.41455 0.16211  -0.09944 0.14841  121 THR A N   
973  C CA  . THR A 124 ? 1.07084 1.29132 1.42437 0.12982  -0.11252 0.13255  121 THR A CA  
974  C C   . THR A 124 ? 0.96657 1.18163 1.32548 0.10827  -0.06902 0.11535  121 THR A C   
975  O O   . THR A 124 ? 0.93938 1.13003 1.24788 0.08417  -0.07302 0.10234  121 THR A O   
976  C CB  . THR A 124 ? 1.11103 1.37116 1.49181 0.11442  -0.16714 0.13189  121 THR A CB  
977  O OG1 . THR A 124 ? 1.21861 1.44091 1.52105 0.08694  -0.17715 0.11513  121 THR A OG1 
978  C CG2 . THR A 124 ? 0.95704 1.28929 1.45608 0.10314  -0.16680 0.12838  121 THR A CG2 
979  N N   . ASN A 125 ? 0.85454 1.08607 1.26685 0.11816  -0.02825 0.11572  122 ASN A N   
980  C CA  . ASN A 125 ? 0.79959 1.02120 1.20741 0.09871  0.01403  0.10250  122 ASN A CA  
981  C C   . ASN A 125 ? 0.77889 0.93826 1.08874 0.09352  0.02835  0.09371  122 ASN A C   
982  O O   . ASN A 125 ? 0.82560 0.95426 1.09384 0.11069  0.02845  0.09733  122 ASN A O   
983  C CB  . ASN A 125 ? 0.78625 1.03190 1.25923 0.11195  0.05811  0.10348  122 ASN A CB  
984  C CG  . ASN A 125 ? 0.76949 1.07958 1.35031 0.12918  0.04353  0.11469  122 ASN A CG  
985  O OD1 . ASN A 125 ? 0.85963 1.21273 1.48629 0.11818  0.00276  0.11846  122 ASN A OD1 
986  N ND2 . ASN A 125 ? 0.83661 1.15399 1.46163 0.15665  0.07517  0.11862  122 ASN A ND2 
987  N N   . PRO A 126 ? 0.75699 0.89675 1.03342 0.07090  0.04024  0.08349  123 PRO A N   
988  C CA  . PRO A 126 ? 0.68352 0.77287 0.87942 0.06781  0.04792  0.07549  123 PRO A CA  
989  C C   . PRO A 126 ? 0.70589 0.77124 0.87758 0.07984  0.08129  0.07202  123 PRO A C   
990  O O   . PRO A 126 ? 0.75327 0.83283 0.96048 0.08466  0.10863  0.07254  123 PRO A O   
991  C CB  . PRO A 126 ? 0.67898 0.75770 0.86152 0.04402  0.05207  0.06928  123 PRO A CB  
992  C CG  . PRO A 126 ? 0.70092 0.81870 0.95469 0.03414  0.06838  0.07356  123 PRO A CG  
993  C CD  . PRO A 126 ? 0.70296 0.86712 1.02167 0.04740  0.04656  0.08067  123 PRO A CD  
994  N N   . ILE A 127 ? 0.66092 0.69114 0.77526 0.08309  0.07954  0.06646  124 ILE A N   
995  C CA  . ILE A 127 ? 0.65810 0.66321 0.74579 0.08951  0.10591  0.05895  124 ILE A CA  
996  C C   . ILE A 127 ? 0.67164 0.66418 0.73352 0.07639  0.12219  0.05182  124 ILE A C   
997  O O   . ILE A 127 ? 0.66651 0.64841 0.70146 0.06586  0.10788  0.05055  124 ILE A O   
998  C CB  . ILE A 127 ? 0.66972 0.64768 0.71579 0.09336  0.09775  0.05479  124 ILE A CB  
999  C CG1 . ILE A 127 ? 0.71121 0.69187 0.76422 0.10366  0.07911  0.06604  124 ILE A CG1 
1000 C CG2 . ILE A 127 ? 0.57959 0.53438 0.60786 0.09701  0.12092  0.04488  124 ILE A CG2 
1001 C CD1 . ILE A 127 ? 0.66922 0.62044 0.68180 0.10488  0.07958  0.06356  124 ILE A CD1 
1002 N N   . ILE A 128 ? 0.59406 0.58248 0.65887 0.07841  0.15211  0.04782  125 ILE A N   
1003 C CA  . ILE A 128 ? 0.58220 0.55077 0.60749 0.06659  0.16884  0.04357  125 ILE A CA  
1004 C C   . ILE A 128 ? 0.54806 0.48645 0.52741 0.07080  0.18323  0.03017  125 ILE A C   
1005 O O   . ILE A 128 ? 0.50303 0.43872 0.49804 0.08087  0.20442  0.02389  125 ILE A O   
1006 C CB  . ILE A 128 ? 0.59237 0.57909 0.65265 0.05973  0.19630  0.04949  125 ILE A CB  
1007 C CG1 . ILE A 128 ? 0.57541 0.59774 0.69346 0.05224  0.17735  0.05973  125 ILE A CG1 
1008 C CG2 . ILE A 128 ? 0.60201 0.55756 0.60504 0.04601  0.21375  0.04944  125 ILE A CG2 
1009 C CD1 . ILE A 128 ? 0.54023 0.58645 0.70521 0.03969  0.20452  0.06550  125 ILE A CD1 
1010 N N   . ILE A 129 ? 0.62718 0.54199 0.55246 0.06356  0.16994  0.02482  126 ILE A N   
1011 C CA  . ILE A 129 ? 0.62590 0.51419 0.50519 0.06316  0.17360  0.00932  126 ILE A CA  
1012 C C   . ILE A 129 ? 0.70996 0.57300 0.53000 0.05420  0.18271  0.00825  126 ILE A C   
1013 O O   . ILE A 129 ? 0.77611 0.63287 0.57197 0.04912  0.16421  0.01794  126 ILE A O   
1014 C CB  . ILE A 129 ? 0.65483 0.54241 0.52644 0.06298  0.14458  0.00331  126 ILE A CB  
1015 C CG1 . ILE A 129 ? 0.56738 0.47232 0.48395 0.07043  0.13816  0.00851  126 ILE A CG1 
1016 C CG2 . ILE A 129 ? 0.61519 0.48106 0.45111 0.05865  0.14563  -0.01560 126 ILE A CG2 
1017 C CD1 . ILE A 129 ? 0.55961 0.45743 0.49626 0.07852  0.15804  0.00411  126 ILE A CD1 
1018 N N   . GLY A 130 ? 0.80339 0.64488 0.59247 0.05324  0.21187  -0.00332 127 GLY A N   
1019 C CA  . GLY A 130 ? 0.85453 0.66163 0.56594 0.04410  0.22135  -0.00539 127 GLY A CA  
1020 C C   . GLY A 130 ? 0.89343 0.69789 0.60165 0.03804  0.25085  0.01042  127 GLY A C   
1021 O O   . GLY A 130 ? 0.91040 0.74732 0.68901 0.03998  0.26256  0.02058  127 GLY A O   
1022 N N   . GLY A 131 ? 0.84967 0.61522 0.47603 0.02936  0.26131  0.01284  128 GLY A N   
1023 C CA  . GLY A 131 ? 0.86248 0.61847 0.47909 0.01944  0.29260  0.03042  128 GLY A CA  
1024 C C   . GLY A 131 ? 0.89221 0.65838 0.54270 0.01745  0.33324  0.02192  128 GLY A C   
1025 O O   . GLY A 131 ? 0.93683 0.69474 0.57750 0.02330  0.34124  0.00170  128 GLY A O   
1026 N N   . ASP A 132 ? 0.96387 0.74366 0.65079 0.00819  0.35836  0.03656  129 ASP A N   
1027 C CA  . ASP A 132 ? 1.09997 0.89014 0.82018 0.00637  0.40033  0.02963  129 ASP A CA  
1028 C C   . ASP A 132 ? 0.92751 0.77679 0.76747 0.01094  0.41279  0.03437  129 ASP A C   
1029 O O   . ASP A 132 ? 1.05012 0.91812 0.93699 0.01239  0.44528  0.02940  129 ASP A O   
1030 C CB  . ASP A 132 ? 1.09518 0.85209 0.75749 -0.00969 0.42285  0.04090  129 ASP A CB  
1031 C CG  . ASP A 132 ? 1.29777 0.99769 0.83994 -0.01308 0.40161  0.04077  129 ASP A CG  
1032 O OD1 . ASP A 132 ? 1.32202 1.00142 0.81727 -0.00717 0.39863  0.02111  129 ASP A OD1 
1033 O OD2 . ASP A 132 ? 1.46288 1.13868 0.96139 -0.02152 0.38564  0.06056  129 ASP A OD2 
1034 N N   . LYS A 133 ? 0.86047 0.73860 0.74793 0.01411  0.38622  0.04326  130 LYS A N   
1035 C CA  . LYS A 133 ? 0.86318 0.80232 0.86742 0.01968  0.39008  0.04747  130 LYS A CA  
1036 C C   . LYS A 133 ? 0.86783 0.82154 0.91056 0.04064  0.39775  0.03204  130 LYS A C   
1037 O O   . LYS A 133 ? 0.79345 0.71918 0.78948 0.05137  0.38412  0.02003  130 LYS A O   
1038 C CB  . LYS A 133 ? 0.77234 0.73557 0.81242 0.01853  0.35470  0.05900  130 LYS A CB  
1039 C CG  . LYS A 133 ? 0.81958 0.76623 0.83614 -0.00365 0.34150  0.07410  130 LYS A CG  
1040 C CD  . LYS A 133 ? 0.77418 0.73700 0.81880 -0.00430 0.28909  0.07777  130 LYS A CD  
1041 C CE  . LYS A 133 ? 0.97120 0.90862 0.99334 -0.02561 0.27983  0.09069  130 LYS A CE  
1042 N NZ  . LYS A 133 ? 1.09166 1.03797 1.13419 -0.02541 0.23229  0.08961  130 LYS A NZ  
1043 N N   . PRO A 134 ? 0.93164 0.92566 1.05892 0.04581  0.41929  0.03212  131 PRO A N   
1044 C CA  . PRO A 134 ? 0.91552 0.91668 1.07903 0.06711  0.42924  0.02011  131 PRO A CA  
1045 C C   . PRO A 134 ? 0.84460 0.86140 1.04353 0.08682  0.39585  0.02132  131 PRO A C   
1046 O O   . PRO A 134 ? 0.89984 0.89278 1.08267 0.10125  0.39808  0.01013  131 PRO A O   
1047 C CB  . PRO A 134 ? 0.87368 0.92379 1.13083 0.06660  0.45516  0.02492  131 PRO A CB  
1048 C CG  . PRO A 134 ? 0.83837 0.88348 1.07150 0.03977  0.47126  0.03375  131 PRO A CG  
1049 C CD  . PRO A 134 ? 0.96579 0.99716 1.15688 0.03000  0.43606  0.04350  131 PRO A CD  
1050 N N   . GLU A 135 ? 0.78417 0.83821 1.03086 0.08606  0.36737  0.03530  132 GLU A N   
1051 C CA  . GLU A 135 ? 0.75442 0.82462 1.03650 0.10628  0.33464  0.04005  132 GLU A CA  
1052 C C   . GLU A 135 ? 0.72410 0.75059 0.92468 0.10556  0.31584  0.03487  132 GLU A C   
1053 O O   . GLU A 135 ? 0.69120 0.72194 0.90315 0.11620  0.28205  0.03994  132 GLU A O   
1054 C CB  . GLU A 135 ? 0.68454 0.81539 1.05187 0.10428  0.30978  0.05669  132 GLU A CB  
1055 C CG  . GLU A 135 ? 0.77117 0.89093 1.09333 0.07610  0.28794  0.06141  132 GLU A CG  
1056 C CD  . GLU A 135 ? 0.80316 0.95274 1.17238 0.05330  0.30962  0.06754  132 GLU A CD  
1057 O OE1 . GLU A 135 ? 0.76054 0.90037 1.12344 0.04844  0.35501  0.06280  132 GLU A OE1 
1058 O OE2 . GLU A 135 ? 0.88068 1.05498 1.28193 0.03747  0.27661  0.07480  132 GLU A OE2 
1059 N N   . ALA A 136 ? 0.67975 0.66220 0.79396 0.09067  0.32718  0.02505  133 ALA A N   
1060 C CA  . ALA A 136 ? 0.66904 0.61544 0.70838 0.08515  0.29813  0.01931  133 ALA A CA  
1061 C C   . ALA A 136 ? 0.63543 0.54604 0.63980 0.09523  0.30446  0.00175  133 ALA A C   
1062 O O   . ALA A 136 ? 0.78560 0.67466 0.77069 0.09373  0.32727  -0.01051 133 ALA A O   
1063 C CB  . ALA A 136 ? 0.68227 0.60080 0.64887 0.06603  0.29980  0.01977  133 ALA A CB  
1064 N N   . ILE A 137 ? 0.68704 0.59039 0.68385 0.09856  0.27314  0.00096  134 ILE A N   
1065 C CA  . ILE A 137 ? 0.67519 0.54002 0.63621 0.10141  0.27793  -0.01706 134 ILE A CA  
1066 C C   . ILE A 137 ? 0.65629 0.48705 0.53689 0.08495  0.28332  -0.03393 134 ILE A C   
1067 O O   . ILE A 137 ? 0.67317 0.50612 0.51817 0.07290  0.25827  -0.02895 134 ILE A O   
1068 C CB  . ILE A 137 ? 0.63578 0.50041 0.60141 0.10142  0.24398  -0.01295 134 ILE A CB  
1069 C CG1 . ILE A 137 ? 0.64217 0.53540 0.67144 0.11734  0.23304  0.00696  134 ILE A CG1 
1070 C CG2 . ILE A 137 ? 0.63153 0.45508 0.56701 0.09918  0.25184  -0.03275 134 ILE A CG2 
1071 C CD1 . ILE A 137 ? 0.56823 0.45491 0.59182 0.11680  0.20611  0.01316  134 ILE A CD1 
1072 N N   . PRO A 138 ? 0.74388 0.54531 0.59597 0.08140  0.30191  -0.05078 135 PRO A N   
1073 C CA  . PRO A 138 ? 0.77150 0.53942 0.53901 0.06555  0.30221  -0.06604 135 PRO A CA  
1074 C C   . PRO A 138 ? 0.79654 0.54917 0.51660 0.05632  0.27100  -0.07659 135 PRO A C   
1075 O O   . PRO A 138 ? 0.76726 0.52281 0.51672 0.05868  0.25650  -0.08140 135 PRO A O   
1076 C CB  . PRO A 138 ? 0.80254 0.54015 0.55661 0.06589  0.32628  -0.08525 135 PRO A CB  
1077 C CG  . PRO A 138 ? 0.81454 0.57750 0.65083 0.08332  0.34690  -0.07323 135 PRO A CG  
1078 C CD  . PRO A 138 ? 0.72304 0.51864 0.61579 0.09312  0.32371  -0.05546 135 PRO A CD  
1079 N N   . LYS A 139 ? 0.84671 0.58502 0.49714 0.04493  0.25639  -0.07719 136 LYS A N   
1080 C CA  . LYS A 139 ? 0.83404 0.57161 0.45553 0.03459  0.21096  -0.08413 136 LYS A CA  
1081 C C   . LYS A 139 ? 0.86482 0.57766 0.47240 0.02652  0.20855  -0.11357 136 LYS A C   
1082 O O   . LYS A 139 ? 0.89460 0.62286 0.52930 0.02036  0.17819  -0.11889 136 LYS A O   
1083 C CB  . LYS A 139 ? 0.85768 0.57630 0.39898 0.02619  0.19385  -0.07941 136 LYS A CB  
1084 C CG  . LYS A 139 ? 0.95532 0.68279 0.47845 0.01978  0.14088  -0.08271 136 LYS A CG  
1085 C CD  . LYS A 139 ? 0.99401 0.69568 0.42998 0.01558  0.12142  -0.07419 136 LYS A CD  
1086 C CE  . LYS A 139 ? 1.16932 0.88727 0.60008 0.01364  0.06349  -0.07630 136 LYS A CE  
1087 N NZ  . LYS A 139 ? 1.25367 0.94250 0.59505 0.01356  0.03797  -0.06346 136 LYS A NZ  
1088 N N   . SER A 140 ? 0.92470 0.60242 0.50098 0.02477  0.24039  -0.13209 137 SER A N   
1089 C CA  . SER A 140 ? 1.00008 0.64986 0.56758 0.01453  0.23857  -0.16059 137 SER A CA  
1090 C C   . SER A 140 ? 0.95155 0.61007 0.59680 0.02347  0.24883  -0.15718 137 SER A C   
1091 O O   . SER A 140 ? 0.99015 0.63250 0.64048 0.01160  0.23750  -0.17593 137 SER A O   
1092 C CB  . SER A 140 ? 1.03862 0.65644 0.56684 0.01155  0.26403  -0.17466 137 SER A CB  
1093 O OG  . SER A 140 ? 1.07797 0.70814 0.65630 0.02825  0.30027  -0.15762 137 SER A OG  
1094 N N   . VAL A 141 ? 0.84360 0.52658 0.55010 0.04262  0.26806  -0.13258 138 VAL A N   
1095 C CA  . VAL A 141 ? 0.82426 0.51307 0.59640 0.05353  0.27243  -0.12297 138 VAL A CA  
1096 C C   . VAL A 141 ? 0.81004 0.52161 0.60336 0.04990  0.24516  -0.11395 138 VAL A C   
1097 O O   . VAL A 141 ? 0.78208 0.48337 0.59996 0.04511  0.24039  -0.11738 138 VAL A O   
1098 C CB  . VAL A 141 ? 0.78589 0.49860 0.61611 0.07511  0.29168  -0.09872 138 VAL A CB  
1099 C CG1 . VAL A 141 ? 0.70177 0.41765 0.58885 0.08851  0.28942  -0.08379 138 VAL A CG1 
1100 C CG2 . VAL A 141 ? 0.79402 0.48638 0.61311 0.07823  0.32061  -0.10884 138 VAL A CG2 
1101 N N   . PHE A 142 ? 0.71797 0.46641 0.50928 0.04895  0.22117  -0.09723 139 PHE A N   
1102 C CA  . PHE A 142 ? 0.72941 0.50912 0.54854 0.04445  0.18904  -0.08537 139 PHE A CA  
1103 C C   . PHE A 142 ? 0.73534 0.50843 0.53688 0.02473  0.16674  -0.10695 139 PHE A C   
1104 O O   . PHE A 142 ? 0.71161 0.49485 0.54896 0.01891  0.15836  -0.10645 139 PHE A O   
1105 C CB  . PHE A 142 ? 0.65053 0.46180 0.46776 0.04840  0.17081  -0.06611 139 PHE A CB  
1106 C CG  . PHE A 142 ? 0.63357 0.47399 0.48081 0.04772  0.14402  -0.05491 139 PHE A CG  
1107 C CD1 . PHE A 142 ? 0.61127 0.46572 0.49973 0.05721  0.14727  -0.03869 139 PHE A CD1 
1108 C CD2 . PHE A 142 ? 0.70709 0.55969 0.53970 0.03921  0.11555  -0.06086 139 PHE A CD2 
1109 C CE1 . PHE A 142 ? 0.57089 0.44586 0.47776 0.05627  0.12870  -0.03123 139 PHE A CE1 
1110 C CE2 . PHE A 142 ? 0.61416 0.49323 0.47960 0.04105  0.09746  -0.05278 139 PHE A CE2 
1111 C CZ  . PHE A 142 ? 0.51380 0.40148 0.41257 0.04861  0.10712  -0.03927 139 PHE A CZ  
1112 N N   . GLN A 143 ? 0.95664 0.71306 0.70281 0.01295  0.15694  -0.12623 140 GLN A N   
1113 C CA  . GLN A 143 ? 0.99285 0.74890 0.72735 -0.00769 0.12896  -0.14940 140 GLN A CA  
1114 C C   . GLN A 143 ? 0.95429 0.68028 0.70761 -0.02057 0.14652  -0.17084 140 GLN A C   
1115 O O   . GLN A 143 ? 0.99550 0.73475 0.77808 -0.03825 0.12782  -0.18304 140 GLN A O   
1116 C CB  . GLN A 143 ? 1.04905 0.78621 0.70681 -0.01704 0.11169  -0.16552 140 GLN A CB  
1117 C CG  . GLN A 143 ? 1.10000 0.86312 0.73691 -0.00872 0.08352  -0.14438 140 GLN A CG  
1118 C CD  . GLN A 143 ? 1.27987 1.01162 0.82344 -0.01531 0.07165  -0.15460 140 GLN A CD  
1119 O OE1 . GLN A 143 ? 1.20234 0.89000 0.69066 -0.02157 0.09855  -0.17381 140 GLN A OE1 
1120 N NE2 . GLN A 143 ? 1.44541 1.19453 0.96570 -0.01247 0.03234  -0.14139 140 GLN A NE2 
1121 N N   . GLU A 144 ? 0.90798 0.59260 0.65050 -0.01199 0.18449  -0.17566 141 GLU A N   
1122 C CA  . GLU A 144 ? 0.95149 0.59537 0.71010 -0.02222 0.20496  -0.19406 141 GLU A CA  
1123 C C   . GLU A 144 ? 0.87690 0.53722 0.69947 -0.01821 0.20796  -0.17253 141 GLU A C   
1124 O O   . GLU A 144 ? 0.90663 0.55148 0.75049 -0.03785 0.20825  -0.18567 141 GLU A O   
1125 C CB  . GLU A 144 ? 1.03131 0.63038 0.77113 -0.00757 0.24419  -0.19884 141 GLU A CB  
1126 C CG  . GLU A 144 ? 1.11984 0.67678 0.87456 -0.01729 0.25998  -0.21255 141 GLU A CG  
1127 C CD  . GLU A 144 ? 1.25548 0.78612 1.00291 -0.00099 0.28885  -0.21009 141 GLU A CD  
1128 O OE1 . GLU A 144 ? 1.22978 0.77909 0.96599 0.01536  0.29741  -0.19851 141 GLU A OE1 
1129 O OE2 . GLU A 144 ? 1.22956 0.72022 0.98538 -0.00554 0.30494  -0.22018 141 GLU A OE2 
1130 N N   . LEU A 145 ? 0.81790 0.50660 0.66773 0.00466  0.21091  -0.14001 142 LEU A N   
1131 C CA  . LEU A 145 ? 0.82338 0.52526 0.71747 0.00858  0.21135  -0.11798 142 LEU A CA  
1132 C C   . LEU A 145 ? 0.82119 0.55889 0.73478 -0.01121 0.18582  -0.12317 142 LEU A C   
1133 O O   . LEU A 145 ? 0.80512 0.53658 0.74779 -0.02298 0.19365  -0.12166 142 LEU A O   
1134 C CB  . LEU A 145 ? 0.78713 0.51458 0.69739 0.03466  0.21187  -0.08589 142 LEU A CB  
1135 C CG  . LEU A 145 ? 0.79172 0.49658 0.70567 0.05788  0.23693  -0.07683 142 LEU A CG  
1136 C CD1 . LEU A 145 ? 0.66635 0.41145 0.59881 0.07697  0.22775  -0.05113 142 LEU A CD1 
1137 C CD2 . LEU A 145 ? 0.72081 0.38294 0.65412 0.06612  0.25795  -0.06884 142 LEU A CD2 
1138 N N   . GLN A 146 ? 0.69273 0.46682 0.59307 -0.01416 0.15743  -0.12815 143 GLN A N   
1139 C CA  . GLN A 146 ? 0.68939 0.50387 0.61912 -0.02854 0.13156  -0.13401 143 GLN A CA  
1140 C C   . GLN A 146 ? 0.73178 0.53417 0.67886 -0.05754 0.13013  -0.16222 143 GLN A C   
1141 O O   . GLN A 146 ? 0.70226 0.52638 0.69804 -0.07103 0.13094  -0.16285 143 GLN A O   
1142 C CB  . GLN A 146 ? 0.71971 0.56510 0.62640 -0.02366 0.09887  -0.13471 143 GLN A CB  
1143 C CG  . GLN A 146 ? 0.69919 0.55559 0.59283 -0.00033 0.09986  -0.10846 143 GLN A CG  
1144 C CD  . GLN A 146 ? 0.80264 0.69974 0.72831 0.00686  0.08097  -0.09465 143 GLN A CD  
1145 O OE1 . GLN A 146 ? 0.85026 0.76830 0.76813 0.00880  0.05306  -0.09603 143 GLN A OE1 
1146 N NE2 . GLN A 146 ? 0.72008 0.62347 0.67704 0.01246  0.09654  -0.08095 143 GLN A NE2 
1147 N N   . SER A 147 ? 0.73334 0.49913 0.64101 -0.06967 0.13076  -0.18774 144 SER A N   
1148 C CA  . SER A 147 ? 0.75328 0.50405 0.67493 -0.10211 0.12570  -0.21966 144 SER A CA  
1149 C C   . SER A 147 ? 0.76182 0.47175 0.71389 -0.11174 0.16282  -0.21766 144 SER A C   
1150 O O   . SER A 147 ? 0.77937 0.48750 0.76644 -0.14225 0.16204  -0.23777 144 SER A O   
1151 C CB  . SER A 147 ? 0.81169 0.52400 0.66823 -0.11315 0.11694  -0.25056 144 SER A CB  
1152 O OG  . SER A 147 ? 0.86965 0.52161 0.69039 -0.09955 0.15618  -0.24998 144 SER A OG  
1153 N N   . LYS A 148 ? 0.79475 0.47118 0.73644 -0.08703 0.19407  -0.19286 145 LYS A N   
1154 C CA  . LYS A 148 ? 0.80536 0.43498 0.76839 -0.09182 0.22804  -0.18425 145 LYS A CA  
1155 C C   . LYS A 148 ? 0.83487 0.49519 0.83982 -0.09201 0.23300  -0.15827 145 LYS A C   
1156 O O   . LYS A 148 ? 0.86313 0.49288 0.89104 -0.10957 0.25670  -0.15643 145 LYS A O   
1157 C CB  . LYS A 148 ? 0.82053 0.40016 0.75719 -0.06184 0.25591  -0.16730 145 LYS A CB  
1158 C CG  . LYS A 148 ? 0.87410 0.40851 0.76924 -0.06229 0.26572  -0.19619 145 LYS A CG  
1159 C CD  . LYS A 148 ? 0.87719 0.39375 0.76612 -0.02692 0.28652  -0.17044 145 LYS A CD  
1160 C CE  . LYS A 148 ? 1.10151 0.58832 0.95729 -0.02773 0.29571  -0.19228 145 LYS A CE  
1161 N NZ  . LYS A 148 ? 1.10891 0.58847 0.97320 0.00585  0.31594  -0.16883 145 LYS A NZ  
1162 N N   . PHE A 149 ? 0.64829 0.36195 0.65887 -0.07412 0.21467  -0.13900 146 PHE A N   
1163 C CA  . PHE A 149 ? 0.61654 0.35682 0.65729 -0.07318 0.22188  -0.11762 146 PHE A CA  
1164 C C   . PHE A 149 ? 0.67026 0.43176 0.76084 -0.10749 0.22433  -0.13737 146 PHE A C   
1165 O O   . PHE A 149 ? 0.69541 0.48084 0.80362 -0.12786 0.20109  -0.16697 146 PHE A O   
1166 C CB  . PHE A 149 ? 0.55761 0.35068 0.59595 -0.05226 0.19837  -0.10334 146 PHE A CB  
1167 C CG  . PHE A 149 ? 0.54150 0.32152 0.54463 -0.02212 0.19829  -0.08087 146 PHE A CG  
1168 C CD1 . PHE A 149 ? 0.57044 0.30288 0.55748 -0.00920 0.22071  -0.06438 146 PHE A CD1 
1169 C CD2 . PHE A 149 ? 0.50250 0.31837 0.49455 -0.00681 0.17507  -0.07548 146 PHE A CD2 
1170 C CE1 . PHE A 149 ? 0.55553 0.28673 0.52531 0.01812  0.21743  -0.04466 146 PHE A CE1 
1171 C CE2 . PHE A 149 ? 0.48934 0.29884 0.46025 0.01631  0.17561  -0.05659 146 PHE A CE2 
1172 C CZ  . PHE A 149 ? 0.51958 0.29192 0.48401 0.02862  0.19554  -0.04204 146 PHE A CZ  
1173 N N   . PRO A 150 ? 0.79383 0.54796 0.90798 -0.11569 0.25212  -0.12163 147 PRO A N   
1174 C CA  . PRO A 150 ? 0.79915 0.57433 0.97251 -0.15194 0.26272  -0.14057 147 PRO A CA  
1175 C C   . PRO A 150 ? 0.75858 0.61693 0.98253 -0.15601 0.23168  -0.15578 147 PRO A C   
1176 O O   . PRO A 150 ? 0.69817 0.59252 0.91871 -0.13153 0.22206  -0.13965 147 PRO A O   
1177 C CB  . PRO A 150 ? 0.75018 0.49479 0.92268 -0.15312 0.30517  -0.11268 147 PRO A CB  
1178 C CG  . PRO A 150 ? 0.76167 0.50098 0.88293 -0.11437 0.30057  -0.08138 147 PRO A CG  
1179 C CD  . PRO A 150 ? 0.77747 0.50286 0.86274 -0.09371 0.27543  -0.08562 147 PRO A CD  
1180 N N   . ASN A 151 ? 0.77397 0.66086 1.04673 -0.18683 0.21386  -0.18783 148 ASN A N   
1181 C CA  . ASN A 151 ? 0.76117 0.73013 1.09577 -0.19183 0.17970  -0.20397 148 ASN A CA  
1182 C C   . ASN A 151 ? 0.80489 0.81232 1.22744 -0.21847 0.20715  -0.20924 148 ASN A C   
1183 O O   . ASN A 151 ? 0.81131 0.77617 1.23318 -0.23157 0.25515  -0.19620 148 ASN A O   
1184 C CB  . ASN A 151 ? 0.72666 0.70800 1.05695 -0.20749 0.13404  -0.23630 148 ASN A CB  
1185 C CG  . ASN A 151 ? 0.84201 0.77186 1.17107 -0.24495 0.14830  -0.26175 148 ASN A CG  
1186 O OD1 . ASN A 151 ? 0.93977 0.79578 1.20263 -0.23944 0.16647  -0.25889 148 ASN A OD1 
1187 N ND2 . ASN A 151 ? 0.87900 0.84764 1.28731 -0.28353 0.14091  -0.28819 148 ASN A ND2 
1188 N N   . THR A 152 ? 0.77342 0.78681 0.88088 0.10490  0.02328  0.16943  149 THR A N   
1189 C CA  . THR A 152 ? 0.70191 0.71644 0.83708 0.11760  0.03661  0.18681  149 THR A CA  
1190 C C   . THR A 152 ? 0.73383 0.76326 0.86508 0.10057  0.03397  0.18125  149 THR A C   
1191 O O   . THR A 152 ? 0.71097 0.72420 0.84533 0.11325  0.04634  0.17908  149 THR A O   
1192 C CB  . THR A 152 ? 0.70499 0.75461 0.89042 0.12055  0.03644  0.22745  149 THR A CB  
1193 O OG1 . THR A 152 ? 0.74776 0.79297 0.96467 0.13970  0.05651  0.24689  149 THR A OG1 
1194 C CG2 . THR A 152 ? 0.73701 0.84741 0.93966 0.08503  0.01257  0.24864  149 THR A CG2 
1195 N N   . GLY A 153 ? 0.77545 0.83136 0.89398 0.06784  0.01992  0.17769  150 GLY A N   
1196 C CA  . GLY A 153 ? 0.77166 0.83354 0.87602 0.04437  0.02082  0.17132  150 GLY A CA  
1197 C C   . GLY A 153 ? 0.75151 0.76805 0.82843 0.05663  0.03625  0.13875  150 GLY A C   
1198 O O   . GLY A 153 ? 0.72729 0.73655 0.80271 0.05537  0.04335  0.13660  150 GLY A O   
1199 N N   . GLU A 154 ? 0.81184 0.80202 0.87164 0.06797  0.04100  0.11834  151 GLU A N   
1200 C CA  . GLU A 154 ? 0.75158 0.70709 0.79850 0.08041  0.05598  0.09801  151 GLU A CA  
1201 C C   . GLU A 154 ? 0.74524 0.68597 0.80451 0.10531  0.06151  0.10419  151 GLU A C   
1202 O O   . GLU A 154 ? 0.75833 0.68449 0.81702 0.10842  0.07082  0.09730  151 GLU A O   
1203 C CB  . GLU A 154 ? 0.65954 0.60119 0.69528 0.08669  0.05859  0.08651  151 GLU A CB  
1204 C CG  . GLU A 154 ? 0.70729 0.62276 0.74372 0.09955  0.07501  0.07703  151 GLU A CG  
1205 C CD  . GLU A 154 ? 0.79214 0.70365 0.82785 0.10820  0.07636  0.07763  151 GLU A CD  
1206 O OE1 . GLU A 154 ? 0.84922 0.77182 0.87547 0.09772  0.07022  0.07441  151 GLU A OE1 
1207 O OE2 . GLU A 154 ? 0.70687 0.60922 0.75325 0.12275  0.08191  0.08559  151 GLU A OE2 
1208 N N   . LEU A 155 ? 0.67564 0.61547 0.74308 0.12052  0.05896  0.11656  152 LEU A N   
1209 C CA  . LEU A 155 ? 0.74545 0.66475 0.81584 0.13758  0.06933  0.12040  152 LEU A CA  
1210 C C   . LEU A 155 ? 0.71013 0.64461 0.80177 0.13767  0.07361  0.13259  152 LEU A C   
1211 O O   . LEU A 155 ? 0.70381 0.62294 0.79479 0.14577  0.08255  0.12969  152 LEU A O   
1212 C CB  . LEU A 155 ? 0.69192 0.59388 0.75643 0.14883  0.07420  0.12788  152 LEU A CB  
1213 C CG  . LEU A 155 ? 0.84320 0.72829 0.87952 0.14595  0.06854  0.11916  152 LEU A CG  
1214 C CD1 . LEU A 155 ? 0.93281 0.79716 0.95694 0.15098  0.07471  0.12624  152 LEU A CD1 
1215 C CD2 . LEU A 155 ? 0.82920 0.69513 0.84753 0.14453  0.07189  0.11263  152 LEU A CD2 
1216 N N   . ASP A 156 ? 0.67032 0.64009 0.78189 0.12524  0.06552  0.15061  153 ASP A N   
1217 C CA  . ASP A 156 ? 0.66818 0.66227 0.80242 0.12071  0.06649  0.16998  153 ASP A CA  
1218 C C   . ASP A 156 ? 0.64645 0.63526 0.76013 0.10368  0.06478  0.15370  153 ASP A C   
1219 O O   . ASP A 156 ? 0.66633 0.65439 0.78731 0.10857  0.06989  0.15828  153 ASP A O   
1220 C CB  . ASP A 156 ? 0.67695 0.72062 0.84076 0.10409  0.05454  0.20335  153 ASP A CB  
1221 C CG  . ASP A 156 ? 0.65188 0.70214 0.85548 0.12819  0.06530  0.23157  153 ASP A CG  
1222 O OD1 . ASP A 156 ? 0.75808 0.76761 0.95830 0.15488  0.08616  0.22208  153 ASP A OD1 
1223 O OD2 . ASP A 156 ? 0.70984 0.80410 0.94736 0.11725  0.05547  0.26515  153 ASP A OD2 
1224 N N   . ARG A 157 ? 0.50476 0.48536 0.59195 0.08351  0.06164  0.13430  154 ARG A N   
1225 C CA  . ARG A 157 ? 0.56362 0.52626 0.62866 0.06743  0.06881  0.11676  154 ARG A CA  
1226 C C   . ARG A 157 ? 0.52496 0.45487 0.59144 0.09152  0.08080  0.10257  154 ARG A C   
1227 O O   . ARG A 157 ? 0.54513 0.46543 0.60918 0.08860  0.08656  0.09866  154 ARG A O   
1228 C CB  . ARG A 157 ? 0.62800 0.57949 0.66304 0.03972  0.07285  0.09856  154 ARG A CB  
1229 C CG  . ARG A 157 ? 0.71026 0.69462 0.73094 -0.00243 0.06030  0.11241  154 ARG A CG  
1230 C CD  . ARG A 157 ? 0.78415 0.74510 0.76301 -0.03573 0.07153  0.08788  154 ARG A CD  
1231 N NE  . ARG A 157 ? 0.80984 0.76164 0.79408 -0.01728 0.07410  0.07715  154 ARG A NE  
1232 C CZ  . ARG A 157 ? 0.84459 0.82709 0.83437 -0.02709 0.05746  0.08946  154 ARG A CZ  
1233 N NH1 . ARG A 157 ? 0.81866 0.84724 0.81625 -0.05494 0.03720  0.11729  154 ARG A NH1 
1234 N NH2 . ARG A 157 ? 0.77280 0.74440 0.76433 -0.00992 0.06002  0.07875  154 ARG A NH2 
1235 N N   . TYR A 158 ? 0.59881 0.51461 0.66823 0.11084  0.08279  0.09837  155 TYR A N   
1236 C CA  . TYR A 158 ? 0.60348 0.49805 0.67635 0.12637  0.09005  0.09399  155 TYR A CA  
1237 C C   . TYR A 158 ? 0.65081 0.54680 0.73229 0.13484  0.09063  0.10267  155 TYR A C   
1238 O O   . TYR A 158 ? 0.58259 0.47030 0.66740 0.13548  0.09489  0.09978  155 TYR A O   
1239 C CB  . TYR A 158 ? 0.55114 0.43772 0.61993 0.13639  0.08781  0.09572  155 TYR A CB  
1240 C CG  . TYR A 158 ? 0.54991 0.42402 0.62078 0.14345  0.09056  0.10070  155 TYR A CG  
1241 C CD1 . TYR A 158 ? 0.54373 0.41417 0.62815 0.14400  0.09688  0.10265  155 TYR A CD1 
1242 C CD2 . TYR A 158 ? 0.58535 0.45077 0.64552 0.14613  0.08993  0.10672  155 TYR A CD2 
1243 C CE1 . TYR A 158 ? 0.56797 0.43788 0.66048 0.14486  0.09549  0.11631  155 TYR A CE1 
1244 C CE2 . TYR A 158 ? 0.59068 0.44780 0.64545 0.14180  0.09002  0.11366  155 TYR A CE2 
1245 C CZ  . TYR A 158 ? 0.59342 0.45860 0.66700 0.14005  0.08925  0.12136  155 TYR A CZ  
1246 O OH  . TYR A 158 ? 0.65019 0.51763 0.72450 0.13050  0.08553  0.13710  155 TYR A OH  
1247 N N   . ALA A 159 ? 0.53881 0.44434 0.62708 0.14168  0.08962  0.11496  156 ALA A N   
1248 C CA  . ALA A 159 ? 0.59893 0.50174 0.69644 0.15124  0.09732  0.12383  156 ALA A CA  
1249 C C   . ALA A 159 ? 0.60764 0.53051 0.71606 0.14226  0.09387  0.12996  156 ALA A C   
1250 O O   . ALA A 159 ? 0.64197 0.55704 0.75102 0.14561  0.09780  0.12781  156 ALA A O   
1251 C CB  . ALA A 159 ? 0.55750 0.46115 0.66629 0.16259  0.10636  0.13857  156 ALA A CB  
1252 N N   . ASN A 160 ? 0.54325 0.49237 0.65558 0.12573  0.08525  0.13902  157 ASN A N   
1253 C CA  . ASN A 160 ? 0.60601 0.57630 0.71975 0.10769  0.07971  0.14892  157 ASN A CA  
1254 C C   . ASN A 160 ? 0.63829 0.58152 0.72997 0.09865  0.08368  0.12636  157 ASN A C   
1255 O O   . ASN A 160 ? 0.73799 0.68373 0.83152 0.09637  0.08358  0.13003  157 ASN A O   
1256 C CB  . ASN A 160 ? 0.61706 0.62273 0.73016 0.07938  0.06760  0.16683  157 ASN A CB  
1257 C CG  . ASN A 160 ? 0.74507 0.79439 0.89862 0.08587  0.06373  0.20688  157 ASN A CG  
1258 O OD1 . ASN A 160 ? 0.77043 0.85393 0.93860 0.07251  0.05732  0.23357  157 ASN A OD1 
1259 N ND2 . ASN A 160 ? 0.69509 0.74392 0.87005 0.10625  0.06970  0.21530  157 ASN A ND2 
1260 N N   . ALA A 161 ? 0.59945 0.51793 0.67573 0.09531  0.08969  0.10686  158 ALA A N   
1261 C CA  . ALA A 161 ? 0.66996 0.55853 0.73551 0.09048  0.10159  0.08996  158 ALA A CA  
1262 C C   . ALA A 161 ? 0.63527 0.51596 0.71904 0.11110  0.10332  0.09252  158 ALA A C   
1263 O O   . ALA A 161 ? 0.62825 0.49856 0.71221 0.10658  0.10797  0.08944  158 ALA A O   
1264 C CB  . ALA A 161 ? 0.62460 0.49044 0.68170 0.08842  0.11380  0.07535  158 ALA A CB  
1265 N N   . ARG A 162 ? 0.73947 0.62290 0.83292 0.12770  0.10016  0.09830  159 ARG A N   
1266 C CA  . ARG A 162 ? 0.73960 0.61663 0.84188 0.13706  0.10060  0.10257  159 ARG A CA  
1267 C C   . ARG A 162 ? 0.77793 0.66538 0.88328 0.13636  0.09833  0.10847  159 ARG A C   
1268 O O   . ARG A 162 ? 0.77823 0.66168 0.88941 0.13455  0.09827  0.10850  159 ARG A O   
1269 C CB  . ARG A 162 ? 0.68122 0.55378 0.77704 0.14367  0.09939  0.10686  159 ARG A CB  
1270 C CG  . ARG A 162 ? 0.94830 0.81398 1.04237 0.14079  0.09864  0.11320  159 ARG A CG  
1271 C CD  . ARG A 162 ? 0.81134 0.67821 0.91761 0.13752  0.09639  0.12146  159 ARG A CD  
1272 N NE  . ARG A 162 ? 0.81627 0.68880 0.93400 0.12911  0.09270  0.13482  159 ARG A NE  
1273 C CZ  . ARG A 162 ? 0.91888 0.79583 1.06177 0.13066  0.09503  0.13856  159 ARG A CZ  
1274 N NH1 . ARG A 162 ? 0.88308 0.75199 1.03321 0.13749  0.10392  0.12647  159 ARG A NH1 
1275 N NH2 . ARG A 162 ? 0.95420 0.84208 1.11122 0.12057  0.08902  0.15555  159 ARG A NH2 
1276 N N   . VAL A 163 ? 0.62897 0.53342 0.73640 0.13764  0.09706  0.11775  160 VAL A N   
1277 C CA  . VAL A 163 ? 0.64412 0.56464 0.76134 0.13879  0.09716  0.12980  160 VAL A CA  
1278 C C   . VAL A 163 ? 0.64627 0.57357 0.75802 0.12235  0.09033  0.12804  160 VAL A C   
1279 O O   . VAL A 163 ? 0.66027 0.58899 0.77553 0.12240  0.08915  0.12990  160 VAL A O   
1280 C CB  . VAL A 163 ? 0.58647 0.53032 0.72053 0.14539  0.10076  0.15049  160 VAL A CB  
1281 C CG1 . VAL A 163 ? 0.61573 0.58779 0.76768 0.14375  0.09977  0.17138  160 VAL A CG1 
1282 C CG2 . VAL A 163 ? 0.55937 0.48304 0.69464 0.16211  0.11641  0.15062  160 VAL A CG2 
1283 N N   . HIS A 164 ? 0.58879 0.51509 0.68612 0.10486  0.08802  0.12285  161 HIS A N   
1284 C CA  . HIS A 164 ? 0.73631 0.65688 0.81409 0.08081  0.08693  0.11814  161 HIS A CA  
1285 C C   . HIS A 164 ? 0.72075 0.61028 0.80016 0.08702  0.09611  0.10348  161 HIS A C   
1286 O O   . HIS A 164 ? 0.74694 0.63545 0.82187 0.07836  0.09405  0.10508  161 HIS A O   
1287 C CB  . HIS A 164 ? 0.77707 0.69086 0.82725 0.05357  0.08922  0.11113  161 HIS A CB  
1288 C CG  . HIS A 164 ? 0.77663 0.66253 0.79202 0.02376  0.09813  0.09776  161 HIS A CG  
1289 N ND1 . HIS A 164 ? 0.84589 0.74921 0.84030 -0.00514 0.08806  0.11066  161 HIS A ND1 
1290 C CD2 . HIS A 164 ? 0.88319 0.72091 0.87963 0.01661  0.12037  0.07445  161 HIS A CD2 
1291 C CE1 . HIS A 164 ? 0.82827 0.68935 0.78295 -0.03246 0.10336  0.09164  161 HIS A CE1 
1292 N NE2 . HIS A 164 ? 0.99819 0.81562 0.95616 -0.01736 0.12671  0.06866  161 HIS A NE2 
1293 N N   . ALA A 165 ? 0.75362 0.62395 0.84404 0.10096  0.10487  0.09531  162 ALA A N   
1294 C CA  . ALA A 165 ? 0.79583 0.64422 0.90169 0.10705  0.11501  0.09183  162 ALA A CA  
1295 C C   . ALA A 165 ? 0.75418 0.61837 0.87643 0.11469  0.10439  0.10264  162 ALA A C   
1296 O O   . ALA A 165 ? 0.84217 0.69767 0.97457 0.11175  0.10738  0.10414  162 ALA A O   
1297 C CB  . ALA A 165 ? 0.74055 0.57793 0.86295 0.11899  0.12450  0.09203  162 ALA A CB  
1298 N N   . ILE A 166 ? 0.63318 0.51538 0.75605 0.12222  0.09597  0.10950  163 ILE A N   
1299 C CA  . ILE A 166 ? 0.63660 0.52835 0.76648 0.12402  0.09033  0.11693  163 ILE A CA  
1300 C C   . ILE A 166 ? 0.62025 0.52499 0.74689 0.11784  0.08526  0.12012  163 ILE A C   
1301 O O   . ILE A 166 ? 0.61464 0.52172 0.74841 0.11376  0.08092  0.12297  163 ILE A O   
1302 C CB  . ILE A 166 ? 0.66949 0.56306 0.79123 0.12983  0.09252  0.11985  163 ILE A CB  
1303 C CG1 . ILE A 166 ? 0.61640 0.49926 0.73639 0.12934  0.09353  0.12036  163 ILE A CG1 
1304 C CG2 . ILE A 166 ? 0.60847 0.50567 0.72706 0.12584  0.09281  0.12412  163 ILE A CG2 
1305 C CD1 . ILE A 166 ? 0.68440 0.55825 0.78477 0.13115  0.09950  0.11933  163 ILE A CD1 
1306 N N   . LEU A 167 ? 0.61955 0.53852 0.73773 0.11422  0.08367  0.12464  164 LEU A N   
1307 C CA  . LEU A 167 ? 0.65649 0.59562 0.77212 0.10446  0.07643  0.13503  164 LEU A CA  
1308 C C   . LEU A 167 ? 0.64887 0.57150 0.74931 0.08626  0.07479  0.12666  164 LEU A C   
1309 O O   . LEU A 167 ? 0.64072 0.57063 0.73985 0.07900  0.06823  0.13142  164 LEU A O   
1310 C CB  . LEU A 167 ? 0.60286 0.57088 0.71979 0.10017  0.07343  0.15290  164 LEU A CB  
1311 C CG  . LEU A 167 ? 0.54864 0.53174 0.68795 0.12068  0.08231  0.16752  164 LEU A CG  
1312 C CD1 . LEU A 167 ? 0.54851 0.56916 0.70343 0.11594  0.07920  0.19606  164 LEU A CD1 
1313 C CD2 . LEU A 167 ? 0.56879 0.55454 0.71838 0.13062  0.08839  0.17190  164 LEU A CD2 
1314 N N   . ALA A 168 ? 0.73390 0.62931 0.82060 0.07779  0.08458  0.11351  165 ALA A N   
1315 C CA  . ALA A 168 ? 0.74798 0.61188 0.81614 0.05995  0.09420  0.10253  165 ALA A CA  
1316 C C   . ALA A 168 ? 0.72426 0.57343 0.81942 0.07294  0.09934  0.10196  165 ALA A C   
1317 O O   . ALA A 168 ? 0.73099 0.56516 0.81895 0.06147  0.10216  0.10028  165 ALA A O   
1318 C CB  . ALA A 168 ? 0.74455 0.57462 0.79075 0.04779  0.11270  0.08722  165 ALA A CB  
1319 N N   . GLY A 169 ? 0.67877 0.53439 0.80431 0.09246  0.09944  0.10720  166 GLY A N   
1320 C CA  . GLY A 169 ? 0.66136 0.51565 0.81912 0.09928  0.09995  0.11670  166 GLY A CA  
1321 C C   . GLY A 169 ? 0.69069 0.56895 0.85125 0.09471  0.08305  0.12493  166 GLY A C   
1322 O O   . GLY A 169 ? 0.71152 0.58744 0.89204 0.09186  0.08203  0.13242  166 GLY A O   
1323 N N   . TYR A 170 ? 0.61384 0.51562 0.75906 0.09467  0.07239  0.12629  167 TYR A N   
1324 C CA  . TYR A 170 ? 0.68144 0.60507 0.82756 0.09017  0.06044  0.13372  167 TYR A CA  
1325 C C   . TYR A 170 ? 0.70127 0.62362 0.83205 0.07632  0.05582  0.13350  167 TYR A C   
1326 O O   . TYR A 170 ? 0.66650 0.59354 0.80455 0.07015  0.04822  0.13791  167 TYR A O   
1327 C CB  . TYR A 170 ? 0.57089 0.51447 0.71054 0.09724  0.06013  0.13818  167 TYR A CB  
1328 C CG  . TYR A 170 ? 0.60344 0.57193 0.73918 0.09360  0.05384  0.14835  167 TYR A CG  
1329 C CD1 . TYR A 170 ? 0.56962 0.54989 0.71071 0.08874  0.04707  0.15256  167 TYR A CD1 
1330 C CD2 . TYR A 170 ? 0.58949 0.57597 0.71955 0.09253  0.05360  0.15913  167 TYR A CD2 
1331 C CE1 . TYR A 170 ? 0.55304 0.55953 0.69374 0.08658  0.04228  0.16504  167 TYR A CE1 
1332 C CE2 . TYR A 170 ? 0.63281 0.65094 0.76699 0.08890  0.04747  0.17772  167 TYR A CE2 
1333 C CZ  . TYR A 170 ? 0.60574 0.63242 0.74519 0.08783  0.04288  0.17954  167 TYR A CZ  
1334 O OH  . TYR A 170 ? 0.60554 0.66692 0.75204 0.08529  0.03766  0.20097  167 TYR A OH  
1335 N N   . LEU A 171 ? 0.61208 0.52848 0.71743 0.06571  0.05913  0.13007  168 LEU A N   
1336 C CA  . LEU A 171 ? 0.66377 0.57654 0.74131 0.04213  0.05426  0.13149  168 LEU A CA  
1337 C C   . LEU A 171 ? 0.75871 0.62676 0.83062 0.03314  0.06819  0.11905  168 LEU A C   
1338 O O   . LEU A 171 ? 0.79278 0.65595 0.85418 0.01946  0.06297  0.12123  168 LEU A O   
1339 C CB  . LEU A 171 ? 0.65202 0.57187 0.69814 0.02253  0.05349  0.13539  168 LEU A CB  
1340 C CG  . LEU A 171 ? 0.68007 0.65062 0.74041 0.02947  0.04153  0.15887  168 LEU A CG  
1341 C CD1 . LEU A 171 ? 0.63478 0.61622 0.67439 0.00927  0.04050  0.16781  168 LEU A CD1 
1342 C CD2 . LEU A 171 ? 0.59056 0.59689 0.65427 0.02226  0.02668  0.17970  168 LEU A CD2 
1343 N N   . ASP A 172 ? 0.75435 0.58805 0.83632 0.04168  0.08919  0.10833  169 ASP A N   
1344 C CA  . ASP A 172 ? 0.77598 0.56103 0.86196 0.03751  0.11300  0.10037  169 ASP A CA  
1345 C C   . ASP A 172 ? 0.77261 0.57027 0.90530 0.05115  0.10645  0.11491  169 ASP A C   
1346 O O   . ASP A 172 ? 0.78494 0.55729 0.91720 0.04199  0.11520  0.11501  169 ASP A O   
1347 C CB  . ASP A 172 ? 0.81380 0.56333 0.90915 0.04716  0.14151  0.09096  169 ASP A CB  
1348 C CG  . ASP A 172 ? 0.91981 0.64387 0.95980 0.02274  0.15359  0.07367  169 ASP A CG  
1349 O OD1 . ASP A 172 ? 0.90606 0.62786 0.89694 -0.00857 0.14552  0.07012  169 ASP A OD1 
1350 O OD2 . ASP A 172 ? 0.90003 0.60963 0.94386 0.03037  0.16957  0.06649  169 ASP A OD2 
1351 N N   . GLY A 173 ? 0.74933 0.58442 0.91906 0.06806  0.09173  0.12863  170 GLY A N   
1352 C CA  . GLY A 173 ? 0.68141 0.53805 0.89160 0.07160  0.08022  0.14694  170 GLY A CA  
1353 C C   . GLY A 173 ? 0.72034 0.59806 0.91303 0.05841  0.05970  0.14847  170 GLY A C   
1354 O O   . GLY A 173 ? 0.75783 0.63620 0.97246 0.05363  0.05575  0.15882  170 GLY A O   
1355 N N   . MET A 174 ? 0.74901 0.64688 0.90718 0.05282  0.04749  0.14244  171 MET A N   
1356 C CA  . MET A 174 ? 0.76801 0.69077 0.91058 0.04055  0.02894  0.14795  171 MET A CA  
1357 C C   . MET A 174 ? 0.87842 0.76924 0.99706 0.02217  0.03479  0.14281  171 MET A C   
1358 O O   . MET A 174 ? 0.85595 0.75445 0.98288 0.01479  0.02384  0.14997  171 MET A O   
1359 C CB  . MET A 174 ? 0.71806 0.66951 0.83700 0.03949  0.02092  0.15089  171 MET A CB  
1360 C CG  . MET A 174 ? 0.84156 0.82499 0.95054 0.02866  0.00371  0.16284  171 MET A CG  
1361 S SD  . MET A 174 ? 0.77733 0.80437 0.88349 0.03548  0.00067  0.17969  171 MET A SD  
1362 C CE  . MET A 174 ? 0.79644 0.86005 0.89479 0.01977  -0.01858 0.19878  171 MET A CE  
1363 N N   . LYS A 175 ? 0.86581 0.71829 0.95038 0.01082  0.05311  0.12993  172 LYS A N   
1364 C CA  . LYS A 175 ? 0.93797 0.74538 0.98189 -0.01583 0.06570  0.12084  172 LYS A CA  
1365 C C   . LYS A 175 ? 0.95040 0.72046 1.03077 -0.00631 0.08528  0.12147  172 LYS A C   
1366 O O   . LYS A 175 ? 0.98187 0.73527 1.04790 -0.02227 0.08385  0.12267  172 LYS A O   
1367 C CB  . LYS A 175 ? 0.95738 0.72640 0.94949 -0.03729 0.08565  0.10535  172 LYS A CB  
1368 C CG  . LYS A 175 ? 1.16214 0.87368 1.09084 -0.07692 0.10379  0.09219  172 LYS A CG  
1369 C CD  . LYS A 175 ? 1.14775 0.82346 1.01575 -0.10812 0.12273  0.07704  172 LYS A CD  
1370 C CE  . LYS A 175 ? 1.36430 0.97127 1.15329 -0.15809 0.14599  0.06092  172 LYS A CE  
1371 N NZ  . LYS A 175 ? 1.43061 1.00250 1.15168 -0.19815 0.16467  0.04593  172 LYS A NZ  
1372 N N   . ASP A 176 ? 0.89152 0.65321 1.02183 0.01824  0.10247  0.12594  173 ASP A N   
1373 C CA  . ASP A 176 ? 0.94127 0.67560 1.12452 0.03041  0.12428  0.13835  173 ASP A CA  
1374 C C   . ASP A 176 ? 0.94320 0.72358 1.16326 0.03098  0.09466  0.15983  173 ASP A C   
1375 O O   . ASP A 176 ? 0.96033 0.71566 1.19593 0.02580  0.10510  0.16693  173 ASP A O   
1376 C CB  . ASP A 176 ? 0.94733 0.67904 1.18440 0.05527  0.14460  0.14949  173 ASP A CB  
1377 C CG  . ASP A 176 ? 1.11641 0.78981 1.32264 0.05407  0.18343  0.12825  173 ASP A CG  
1378 O OD1 . ASP A 176 ? 1.19430 0.81156 1.34495 0.03142  0.20602  0.10697  173 ASP A OD1 
1379 O OD2 . ASP A 176 ? 1.20523 0.88842 1.43753 0.07116  0.19107  0.13302  173 ASP A OD2 
1380 N N   . ALA A 177 ? 0.81745 0.65793 1.04698 0.03439  0.06234  0.16873  174 ALA A N   
1381 C CA  . ALA A 177 ? 0.77444 0.66026 1.03202 0.02886  0.03418  0.18745  174 ALA A CA  
1382 C C   . ALA A 177 ? 0.76197 0.64337 0.97988 0.01012  0.02187  0.18015  174 ALA A C   
1383 O O   . ALA A 177 ? 0.84942 0.73838 1.09328 0.00382  0.01294  0.19406  174 ALA A O   
1384 C CB  . ALA A 177 ? 0.67325 0.60918 0.93162 0.03052  0.01165  0.19174  174 ALA A CB  
1385 N N   . ARG A 178 ? 0.64967 0.52416 0.80905 -0.00124 0.01964  0.16396  175 ARG A N   
1386 C CA  . ARG A 178 ? 0.75641 0.63141 0.87161 -0.02497 0.00563  0.16204  175 ARG A CA  
1387 C C   . ARG A 178 ? 0.87869 0.69039 0.98147 -0.03814 0.02983  0.15557  175 ARG A C   
1388 O O   . ARG A 178 ? 0.87917 0.69396 0.97873 -0.05134 0.01719  0.16257  175 ARG A O   
1389 C CB  . ARG A 178 ? 0.77135 0.65650 0.83206 -0.03891 0.00002  0.15570  175 ARG A CB  
1390 C CG  . ARG A 178 ? 0.84033 0.72852 0.84897 -0.07074 -0.01474 0.15978  175 ARG A CG  
1391 C CD  . ARG A 178 ? 0.82445 0.68773 0.77031 -0.09892 -0.00499 0.15287  175 ARG A CD  
1392 N NE  . ARG A 178 ? 0.98446 0.87006 0.94107 -0.08402 -0.00194 0.15396  175 ARG A NE  
1393 C CZ  . ARG A 178 ? 1.01968 0.87989 0.93545 -0.10344 0.01195  0.14609  175 ARG A CZ  
1394 N NH1 . ARG A 178 ? 1.02536 0.83086 0.87830 -0.14287 0.02724  0.13385  175 ARG A NH1 
1395 N NH2 . ARG A 178 ? 0.92955 0.81553 0.86280 -0.08747 0.01228  0.14998  175 ARG A NH2 
1396 N N   . GLU A 179 ? 0.89056 0.64331 0.98767 -0.03435 0.06717  0.14270  176 GLU A N   
1397 C CA  . GLU A 179 ? 0.90567 0.58016 0.98421 -0.04786 0.10409  0.13299  176 GLU A CA  
1398 C C   . GLU A 179 ? 0.89876 0.57665 1.05066 -0.03096 0.10758  0.15521  176 GLU A C   
1399 O O   . GLU A 179 ? 0.94276 0.58355 1.07728 -0.04749 0.11662  0.15438  176 GLU A O   
1400 C CB  . GLU A 179 ? 0.90241 0.51227 0.96656 -0.04423 0.15025  0.11528  176 GLU A CB  
1401 C CG  . GLU A 179 ? 0.96609 0.54451 0.93608 -0.08083 0.15648  0.09169  176 GLU A CG  
1402 C CD  . GLU A 179 ? 1.05080 0.59755 1.00962 -0.07565 0.18642  0.07632  176 GLU A CD  
1403 O OE1 . GLU A 179 ? 1.06920 0.62029 1.09628 -0.03963 0.20220  0.08468  176 GLU A OE1 
1404 O OE2 . GLU A 179 ? 1.10018 0.62220 0.98164 -0.11149 0.19208  0.05943  176 GLU A OE2 
1405 N N   . ARG A 180 ? 1.06252 0.78475 1.29188 -0.00368 0.09995  0.17777  177 ARG A N   
1406 C CA  . ARG A 180 ? 1.07307 0.81178 1.38188 0.00804  0.09963  0.20931  177 ARG A CA  
1407 C C   . ARG A 180 ? 1.03774 0.82303 1.34135 -0.00883 0.05859  0.21915  177 ARG A C   
1408 O O   . ARG A 180 ? 1.09981 0.87284 1.43658 -0.01231 0.06309  0.23579  177 ARG A O   
1409 C CB  . ARG A 180 ? 0.97189 0.76006 1.35586 0.02981  0.09312  0.23720  177 ARG A CB  
1410 C CG  . ARG A 180 ? 1.01414 0.76073 1.41396 0.04886  0.13423  0.23316  177 ARG A CG  
1411 C CD  . ARG A 180 ? 1.08670 0.89141 1.53213 0.06190  0.11673  0.25482  177 ARG A CD  
1412 N NE  . ARG A 180 ? 1.26386 1.03603 1.69180 0.07471  0.14462  0.23812  177 ARG A NE  
1413 C CZ  . ARG A 180 ? 1.23445 0.97497 1.71439 0.09434  0.18530  0.25438  177 ARG A CZ  
1414 N NH1 . ARG A 180 ? 0.98392 0.74702 1.52800 0.10062  0.19885  0.27886  177 ARG A NH1 
1415 N NH2 . ARG A 180 ? 1.13128 0.84433 1.58491 0.10255  0.20785  0.23447  177 ARG A NH2 
1416 N N   . TYR A 181 ? 0.77156 0.60948 1.03714 -0.01855 0.02147  0.21094  178 TYR A N   
1417 C CA  . TYR A 181 ? 0.78671 0.66816 1.04172 -0.03536 -0.01490 0.21854  178 TYR A CA  
1418 C C   . TYR A 181 ? 0.83106 0.66788 1.02753 -0.05785 -0.00924 0.20495  178 TYR A C   
1419 O O   . TYR A 181 ? 0.76344 0.60812 0.97116 -0.06925 -0.02350 0.21666  178 TYR A O   
1420 C CB  . TYR A 181 ? 0.61926 0.55922 0.84865 -0.03768 -0.04483 0.21375  178 TYR A CB  
1421 C CG  . TYR A 181 ? 0.66640 0.65461 0.88730 -0.05354 -0.07905 0.22237  178 TYR A CG  
1422 C CD1 . TYR A 181 ? 0.65305 0.66392 0.91972 -0.06054 -0.09424 0.24288  178 TYR A CD1 
1423 C CD2 . TYR A 181 ? 0.59269 0.60862 0.76578 -0.06188 -0.09551 0.21489  178 TYR A CD2 
1424 C CE1 . TYR A 181 ? 0.60515 0.66057 0.86199 -0.07707 -0.12541 0.24966  178 TYR A CE1 
1425 C CE2 . TYR A 181 ? 0.63034 0.69131 0.79841 -0.07486 -0.12347 0.22446  178 TYR A CE2 
1426 C CZ  . TYR A 181 ? 0.61875 0.69729 0.82485 -0.08318 -0.13862 0.23882  178 TYR A CZ  
1427 O OH  . TYR A 181 ? 0.72064 0.84423 0.91961 -0.09812 -0.16635 0.24717  178 TYR A OH  
1428 N N   . GLU A 182 ? 0.85184 0.64141 0.98108 -0.07004 0.01072  0.18178  179 GLU A N   
1429 C CA  . GLU A 182 ? 0.89978 0.64294 0.95718 -0.10275 0.01645  0.16932  179 GLU A CA  
1430 C C   . GLU A 182 ? 0.92144 0.58461 0.99022 -0.10573 0.05684  0.16687  179 GLU A C   
1431 O O   . GLU A 182 ? 1.02457 0.64552 1.03714 -0.13586 0.06133  0.15901  179 GLU A O   
1432 C CB  . GLU A 182 ? 0.89194 0.60987 0.87038 -0.12473 0.02616  0.14987  179 GLU A CB  
1433 C CG  . GLU A 182 ? 0.90350 0.69919 0.86711 -0.12659 -0.01201 0.15907  179 GLU A CG  
1434 C CD  . GLU A 182 ? 0.93449 0.71474 0.83221 -0.15015 -0.00408 0.14925  179 GLU A CD  
1435 O OE1 . GLU A 182 ? 1.04525 0.76270 0.92413 -0.15314 0.03220  0.13088  179 GLU A OE1 
1436 O OE2 . GLU A 182 ? 0.85814 0.69191 0.72629 -0.16724 -0.03304 0.16374  179 GLU A OE2 
1437 N N   . HIS A 183 ? 0.95269 0.59320 1.09415 -0.07605 0.08906  0.17676  180 HIS A N   
1438 C CA  . HIS A 183 ? 1.03014 0.59846 1.20432 -0.07139 0.13371  0.18337  180 HIS A CA  
1439 C C   . HIS A 183 ? 1.01322 0.61530 1.22985 -0.07508 0.10684  0.20853  180 HIS A C   
1440 O O   . HIS A 183 ? 1.00841 0.54562 1.22519 -0.08305 0.13788  0.21029  180 HIS A O   
1441 C CB  . HIS A 183 ? 0.95274 0.50676 1.21194 -0.03511 0.17193  0.19990  180 HIS A CB  
1442 C CG  . HIS A 183 ? 1.06078 0.60571 1.41759 -0.01522 0.19404  0.23636  180 HIS A CG  
1443 N ND1 . HIS A 183 ? 1.17821 0.63442 1.53139 -0.01572 0.24978  0.22966  180 HIS A ND1 
1444 C CD2 . HIS A 183 ? 1.01615 0.63756 1.47550 0.00313  0.16730  0.28140  180 HIS A CD2 
1445 C CE1 . HIS A 183 ? 1.13442 0.63813 1.58047 0.00728  0.24910  0.26229  180 HIS A CE1 
1446 N NE2 . HIS A 183 ? 0.99857 0.60261 1.51000 0.01608  0.19887  0.29546  180 HIS A NE2 
1447 N N   . TYR A 184 ? 0.89871 0.59684 1.14291 -0.07327 0.05158  0.22575  181 TYR A N   
1448 C CA  . TYR A 184 ? 0.88409 0.62460 1.16325 -0.08230 0.01911  0.24944  181 TYR A CA  
1449 C C   . TYR A 184 ? 0.93775 0.69859 1.13196 -0.11364 -0.01727 0.23318  181 TYR A C   
1450 O O   . TYR A 184 ? 0.96025 0.76621 1.17211 -0.12420 -0.05139 0.24975  181 TYR A O   
1451 C CB  . TYR A 184 ? 0.83235 0.66725 1.19057 -0.06894 -0.01831 0.28043  181 TYR A CB  
1452 C CG  . TYR A 184 ? 0.81676 0.65813 1.26423 -0.04293 0.00528  0.30775  181 TYR A CG  
1453 C CD1 . TYR A 184 ? 0.79749 0.62458 1.33128 -0.03194 0.02792  0.34426  181 TYR A CD1 
1454 C CD2 . TYR A 184 ? 0.71332 0.58051 1.16449 -0.03007 0.00429  0.30322  181 TYR A CD2 
1455 C CE1 . TYR A 184 ? 0.72265 0.57305 1.34149 -0.00870 0.04750  0.37396  181 TYR A CE1 
1456 C CE2 . TYR A 184 ? 0.65674 0.53651 1.18847 -0.00989 0.02268  0.33344  181 TYR A CE2 
1457 C CZ  . TYR A 184 ? 0.64652 0.52158 1.26460 0.00045  0.04362  0.37136  181 TYR A CZ  
1458 O OH  . TYR A 184 ? 0.71180 0.62755 1.39980 0.01893  0.05895  0.39240  181 TYR A OH  
1459 N N   . LEU A 185 ? 0.81965 0.55430 0.92806 -0.13055 -0.01171 0.20684  182 LEU A N   
1460 C CA  . LEU A 185 ? 0.79547 0.56502 0.83036 -0.16129 -0.04933 0.20197  182 LEU A CA  
1461 C C   . LEU A 185 ? 0.89345 0.58166 0.83413 -0.20029 -0.02608 0.18315  182 LEU A C   
1462 O O   . LEU A 185 ? 1.00134 0.61915 0.90334 -0.20664 0.01521  0.16305  182 LEU A O   
1463 C CB  . LEU A 185 ? 0.80676 0.63280 0.82355 -0.15503 -0.06919 0.19861  182 LEU A CB  
1464 C CG  . LEU A 185 ? 0.73584 0.64391 0.81895 -0.12947 -0.09686 0.21446  182 LEU A CG  
1465 C CD1 . LEU A 185 ? 0.66495 0.61978 0.71997 -0.12701 -0.11166 0.21191  182 LEU A CD1 
1466 C CD2 . LEU A 185 ? 0.66299 0.61965 0.77418 -0.13742 -0.13018 0.23255  182 LEU A CD2 
1467 N N   . ASN A 186 ? 0.93524 0.63081 0.83496 -0.23007 -0.05089 0.18936  183 ASN A N   
1468 C CA  . ASN A 186 ? 1.01651 0.63539 0.80891 -0.27963 -0.03288 0.17293  183 ASN A CA  
1469 C C   . ASN A 186 ? 1.08829 0.72461 0.80291 -0.30767 -0.04339 0.16629  183 ASN A C   
1470 O O   . ASN A 186 ? 1.26572 0.82003 0.89806 -0.34387 -0.00853 0.14593  183 ASN A O   
1471 C CB  . ASN A 186 ? 1.02800 0.66255 0.79248 -0.30793 -0.06417 0.18545  183 ASN A CB  
1472 C CG  . ASN A 186 ? 1.14822 0.69217 0.79699 -0.36505 -0.04155 0.16889  183 ASN A CG  
1473 O OD1 . ASN A 186 ? 1.23906 0.67594 0.85233 -0.37584 0.01554  0.14553  183 ASN A OD1 
1474 N ND2 . ASN A 186 ? 1.15666 0.74002 0.74220 -0.40530 -0.08320 0.18172  183 ASN A ND2 
1475 N N   . ARG A 187 ? 1.69953 1.43681 1.44028 -0.29391 -0.08610 0.18505  184 ARG A N   
1476 C CA  . ARG A 187 ? 1.70061 1.47046 1.38203 -0.31962 -0.09994 0.19086  184 ARG A CA  
1477 C C   . ARG A 187 ? 1.49636 1.29188 1.22980 -0.28080 -0.08849 0.18697  184 ARG A C   
1478 O O   . ARG A 187 ? 1.47892 1.32644 1.29465 -0.23706 -0.10009 0.19481  184 ARG A O   
1479 C CB  . ARG A 187 ? 1.68197 1.54655 1.35551 -0.33383 -0.15126 0.22208  184 ARG A CB  
1480 C CG  . ARG A 187 ? 1.76778 1.68083 1.39536 -0.36065 -0.16812 0.24242  184 ARG A CG  
1481 C CD  . ARG A 187 ? 1.71511 1.72504 1.34727 -0.37100 -0.21392 0.28138  184 ARG A CD  
1482 N NE  . ARG A 187 ? 1.73048 1.79790 1.36366 -0.38465 -0.22052 0.29529  184 ARG A NE  
1483 C CZ  . ARG A 187 ? 1.69155 1.81779 1.38695 -0.34801 -0.21887 0.30795  184 ARG A CZ  
1484 N NH1 . ARG A 187 ? 1.54178 1.67643 1.28741 -0.30113 -0.21561 0.30965  184 ARG A NH1 
1485 N NH2 . ARG A 187 ? 1.66887 1.84430 1.37838 -0.36085 -0.22034 0.32150  184 ARG A NH2 
# 
