data_9EWP
# 
_entry.id   9EWP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9EWP         pdb_00009ewp 10.2210/pdb9ewp/pdb 
WWPDB D_1292137285 ?            ?                   
# 
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 2024-11-20 
2 'Structure model' 1 1 2024-11-27 
3 'Structure model' 1 2 2024-12-25 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation 
2 3 'Structure model' 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.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
3 3 'Structure model' '_citation.journal_volume'          
4 3 'Structure model' '_citation.page_first'              
5 3 'Structure model' '_citation.page_last'               
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EWP 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        '9EN5 contains the same protein' 
_pdbx_database_related.db_id          9EN5 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexander.stein@mpinat.mpg.de 
_pdbx_contact_author.name_first         Alexander 
_pdbx_contact_author.name_last          Stein 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2696-0611 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Swarnkar, A.' 1 0009-0002-7641-4907 
'Stein, A.'    2 0000-0002-2696-0611 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Embo J.' 
_citation.journal_id_ASTM           EMJODG 
_citation.journal_id_CSD            0897 
_citation.journal_id_ISSN           1460-2075 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            43 
_citation.language                  ? 
_citation.page_first                6705 
_citation.page_last                 6739 
_citation.title                     
'Determinants of chemoselectivity in ubiquitination by the J2 family of ubiquitin-conjugating enzymes.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s44318-024-00301-3 
_citation.pdbx_database_id_PubMed   39533056 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Swarnkar, A.'   1  ? 
primary 'Leidner, F.'    2  ? 
primary 'Rout, A.K.'     3  ? 
primary 'Ainatzi, S.'    4  ? 
primary 'Schmidt, C.C.'  5  ? 
primary 'Becker, S.'     6  ? 
primary 'Urlaub, H.'     7  ? 
primary 'Griesinger, C.' 8  ? 
primary 'Grubmuller, H.' 9  ? 
primary 'Stein, A.'      10 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ubiquitin-conjugating enzyme E2 6' 20347.016 1   2.3.2.23 ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                      62.068    3   ?        ? ? ? 
3 non-polymer syn 'CADMIUM ION'                       112.411   4   ?        ? ? ? 
4 non-polymer syn 'SODIUM ION'                        22.990    2   ?        ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                      35.453    3   ?        ? ? ? 
6 water       nat water                               18.015    241 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'E2 ubiquitin-conjugating enzyme 6,Ubiquitin carrier protein UBC6,Ubiquitin-protein ligase UBC6' 
# 
_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       
;MATKQAHKRLTKEYKLMVENPPPYILARPNEDNILEWHYIITGPADTPYKGGQYHGTLTFPSDYPYKPPAIRMITPNGRF
KPNTRLCLSMSDYHPDTWNPGWSVSTILNGLLSFMTSDEATTGSITTSDHQKKTLARNSISYNTFQNVRFKLIFPEVVQE
NVETLEKRKLDELPETGG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATKQAHKRLTKEYKLMVENPPPYILARPNEDNILEWHYIITGPADTPYKGGQYHGTLTFPSDYPYKPPAIRMITPNGRF
KPNTRLCLSMSDYHPDTWNPGWSVSTILNGLLSFMTSDEATTGSITTSDHQKKTLARNSISYNTFQNVRFKLIFPEVVQE
NVETLEKRKLDELPETGG
;
_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 1,2-ETHANEDIOL EDO 
3 'CADMIUM ION'  CD  
4 'SODIUM ION'   NA  
5 'CHLORIDE ION' CL  
6 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   GLN n 
1 6   ALA n 
1 7   HIS n 
1 8   LYS n 
1 9   ARG n 
1 10  LEU n 
1 11  THR n 
1 12  LYS n 
1 13  GLU n 
1 14  TYR n 
1 15  LYS n 
1 16  LEU n 
1 17  MET n 
1 18  VAL n 
1 19  GLU n 
1 20  ASN n 
1 21  PRO n 
1 22  PRO n 
1 23  PRO n 
1 24  TYR n 
1 25  ILE n 
1 26  LEU n 
1 27  ALA n 
1 28  ARG n 
1 29  PRO n 
1 30  ASN n 
1 31  GLU n 
1 32  ASP n 
1 33  ASN n 
1 34  ILE n 
1 35  LEU n 
1 36  GLU n 
1 37  TRP n 
1 38  HIS n 
1 39  TYR n 
1 40  ILE n 
1 41  ILE n 
1 42  THR n 
1 43  GLY n 
1 44  PRO n 
1 45  ALA n 
1 46  ASP n 
1 47  THR n 
1 48  PRO n 
1 49  TYR n 
1 50  LYS n 
1 51  GLY n 
1 52  GLY n 
1 53  GLN n 
1 54  TYR n 
1 55  HIS n 
1 56  GLY n 
1 57  THR n 
1 58  LEU n 
1 59  THR n 
1 60  PHE n 
1 61  PRO n 
1 62  SER n 
1 63  ASP n 
1 64  TYR n 
1 65  PRO n 
1 66  TYR n 
1 67  LYS n 
1 68  PRO n 
1 69  PRO n 
1 70  ALA n 
1 71  ILE n 
1 72  ARG n 
1 73  MET n 
1 74  ILE n 
1 75  THR n 
1 76  PRO n 
1 77  ASN n 
1 78  GLY n 
1 79  ARG n 
1 80  PHE n 
1 81  LYS n 
1 82  PRO n 
1 83  ASN n 
1 84  THR n 
1 85  ARG n 
1 86  LEU n 
1 87  CYS n 
1 88  LEU n 
1 89  SER n 
1 90  MET n 
1 91  SER n 
1 92  ASP n 
1 93  TYR n 
1 94  HIS n 
1 95  PRO n 
1 96  ASP n 
1 97  THR n 
1 98  TRP n 
1 99  ASN n 
1 100 PRO n 
1 101 GLY n 
1 102 TRP n 
1 103 SER n 
1 104 VAL n 
1 105 SER n 
1 106 THR n 
1 107 ILE n 
1 108 LEU n 
1 109 ASN n 
1 110 GLY n 
1 111 LEU n 
1 112 LEU n 
1 113 SER n 
1 114 PHE n 
1 115 MET n 
1 116 THR n 
1 117 SER n 
1 118 ASP n 
1 119 GLU n 
1 120 ALA n 
1 121 THR n 
1 122 THR n 
1 123 GLY n 
1 124 SER n 
1 125 ILE n 
1 126 THR n 
1 127 THR n 
1 128 SER n 
1 129 ASP n 
1 130 HIS n 
1 131 GLN n 
1 132 LYS n 
1 133 LYS n 
1 134 THR n 
1 135 LEU n 
1 136 ALA n 
1 137 ARG n 
1 138 ASN n 
1 139 SER n 
1 140 ILE n 
1 141 SER n 
1 142 TYR n 
1 143 ASN n 
1 144 THR n 
1 145 PHE n 
1 146 GLN n 
1 147 ASN n 
1 148 VAL n 
1 149 ARG n 
1 150 PHE n 
1 151 LYS n 
1 152 LEU n 
1 153 ILE n 
1 154 PHE n 
1 155 PRO n 
1 156 GLU n 
1 157 VAL n 
1 158 VAL n 
1 159 GLN n 
1 160 GLU n 
1 161 ASN n 
1 162 VAL n 
1 163 GLU n 
1 164 THR n 
1 165 LEU n 
1 166 GLU n 
1 167 LYS n 
1 168 ARG n 
1 169 LYS n 
1 170 LEU n 
1 171 ASP n 
1 172 GLU n 
1 173 LEU n 
1 174 PRO n 
1 175 GLU n 
1 176 THR n 
1 177 GLY n 
1 178 GLY 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                   178 
_entity_src_gen.gene_src_common_name               
;brewer's yeast
;
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'UBC6, GI527_G0001907' 
_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      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4932 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
CD  non-polymer         . 'CADMIUM ION'   ?                 'Cd 2'           112.411 
CL  non-polymer         . 'CHLORIDE ION'  ?                 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
NA  non-polymer         . 'SODIUM ION'    ?                 'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   HIS 7   7   7   HIS HIS A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ASN 33  33  33  ASN ASN A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  TRP 37  37  37  TRP TRP A . n 
A 1 38  HIS 38  38  38  HIS HIS A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  HIS 55  55  55  HIS HIS A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  TYR 66  66  66  TYR TYR A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  ARG 85  85  85  ARG ARG A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  CYS 87  87  87  CYS CYS A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  MET 90  90  90  MET MET A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 TRP 102 102 102 TRP TRP A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 MET 115 115 115 MET MET A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ASP 118 118 118 ASP ASP A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 ASN 138 138 138 ASN ASN A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 TYR 142 142 142 TYR TYR A . n 
A 1 143 ASN 143 143 143 ASN ASN A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 PHE 145 145 145 PHE PHE A . n 
A 1 146 GLN 146 146 146 GLN GLN A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 LEU 173 173 173 LEU GLY A . n 
A 1 174 PRO 174 174 ?   ?   ?   A . n 
A 1 175 GLU 175 175 ?   ?   ?   A . n 
A 1 176 THR 176 176 ?   ?   ?   A . n 
A 1 177 GLY 177 177 ?   ?   ?   A . n 
A 1 178 GLY 178 178 ?   ?   ?   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 EDO 1   201 201 EDO EDO A . 
C 2 EDO 1   202 202 EDO EDO A . 
D 2 EDO 1   203 203 EDO EDO A . 
E 3 CD  1   204 1   CD  CD  A . 
F 3 CD  1   205 2   CD  CD  A . 
G 3 CD  1   206 3   CD  CD  A . 
H 3 CD  1   207 4   CD  CD  A . 
I 4 NA  1   208 1   NA  NA  A . 
J 4 NA  1   209 2   NA  NA  A . 
K 5 CL  1   210 1   CL  CL  A . 
L 5 CL  1   211 2   CL  CL  A . 
M 5 CL  1   212 3   CL  CL  A . 
N 6 HOH 1   301 233 HOH HOH A . 
N 6 HOH 2   302 188 HOH HOH A . 
N 6 HOH 3   303 190 HOH HOH A . 
N 6 HOH 4   304 173 HOH HOH A . 
N 6 HOH 5   305 157 HOH HOH A . 
N 6 HOH 6   306 209 HOH HOH A . 
N 6 HOH 7   307 28  HOH HOH A . 
N 6 HOH 8   308 63  HOH HOH A . 
N 6 HOH 9   309 194 HOH HOH A . 
N 6 HOH 10  310 115 HOH HOH A . 
N 6 HOH 11  311 133 HOH HOH A . 
N 6 HOH 12  312 120 HOH HOH A . 
N 6 HOH 13  313 105 HOH HOH A . 
N 6 HOH 14  314 138 HOH HOH A . 
N 6 HOH 15  315 97  HOH HOH A . 
N 6 HOH 16  316 81  HOH HOH A . 
N 6 HOH 17  317 83  HOH HOH A . 
N 6 HOH 18  318 90  HOH HOH A . 
N 6 HOH 19  319 226 HOH HOH A . 
N 6 HOH 20  320 151 HOH HOH A . 
N 6 HOH 21  321 45  HOH HOH A . 
N 6 HOH 22  322 69  HOH HOH A . 
N 6 HOH 23  323 44  HOH HOH A . 
N 6 HOH 24  324 6   HOH HOH A . 
N 6 HOH 25  325 21  HOH HOH A . 
N 6 HOH 26  326 61  HOH HOH A . 
N 6 HOH 27  327 1   HOH HOH A . 
N 6 HOH 28  328 41  HOH HOH A . 
N 6 HOH 29  329 8   HOH HOH A . 
N 6 HOH 30  330 49  HOH HOH A . 
N 6 HOH 31  331 42  HOH HOH A . 
N 6 HOH 32  332 123 HOH HOH A . 
N 6 HOH 33  333 31  HOH HOH A . 
N 6 HOH 34  334 101 HOH HOH A . 
N 6 HOH 35  335 13  HOH HOH A . 
N 6 HOH 36  336 99  HOH HOH A . 
N 6 HOH 37  337 65  HOH HOH A . 
N 6 HOH 38  338 70  HOH HOH A . 
N 6 HOH 39  339 109 HOH HOH A . 
N 6 HOH 40  340 62  HOH HOH A . 
N 6 HOH 41  341 23  HOH HOH A . 
N 6 HOH 42  342 12  HOH HOH A . 
N 6 HOH 43  343 118 HOH HOH A . 
N 6 HOH 44  344 124 HOH HOH A . 
N 6 HOH 45  345 153 HOH HOH A . 
N 6 HOH 46  346 7   HOH HOH A . 
N 6 HOH 47  347 11  HOH HOH A . 
N 6 HOH 48  348 102 HOH HOH A . 
N 6 HOH 49  349 29  HOH HOH A . 
N 6 HOH 50  350 64  HOH HOH A . 
N 6 HOH 51  351 14  HOH HOH A . 
N 6 HOH 52  352 57  HOH HOH A . 
N 6 HOH 53  353 141 HOH HOH A . 
N 6 HOH 54  354 136 HOH HOH A . 
N 6 HOH 55  355 181 HOH HOH A . 
N 6 HOH 56  356 4   HOH HOH A . 
N 6 HOH 57  357 129 HOH HOH A . 
N 6 HOH 58  358 48  HOH HOH A . 
N 6 HOH 59  359 236 HOH HOH A . 
N 6 HOH 60  360 235 HOH HOH A . 
N 6 HOH 61  361 93  HOH HOH A . 
N 6 HOH 62  362 174 HOH HOH A . 
N 6 HOH 63  363 164 HOH HOH A . 
N 6 HOH 64  364 54  HOH HOH A . 
N 6 HOH 65  365 104 HOH HOH A . 
N 6 HOH 66  366 52  HOH HOH A . 
N 6 HOH 67  367 20  HOH HOH A . 
N 6 HOH 68  368 73  HOH HOH A . 
N 6 HOH 69  369 146 HOH HOH A . 
N 6 HOH 70  370 128 HOH HOH A . 
N 6 HOH 71  371 77  HOH HOH A . 
N 6 HOH 72  372 16  HOH HOH A . 
N 6 HOH 73  373 234 HOH HOH A . 
N 6 HOH 74  374 15  HOH HOH A . 
N 6 HOH 75  375 155 HOH HOH A . 
N 6 HOH 76  376 114 HOH HOH A . 
N 6 HOH 77  377 113 HOH HOH A . 
N 6 HOH 78  378 26  HOH HOH A . 
N 6 HOH 79  379 112 HOH HOH A . 
N 6 HOH 80  380 92  HOH HOH A . 
N 6 HOH 81  381 116 HOH HOH A . 
N 6 HOH 82  382 2   HOH HOH A . 
N 6 HOH 83  383 67  HOH HOH A . 
N 6 HOH 84  384 40  HOH HOH A . 
N 6 HOH 85  385 85  HOH HOH A . 
N 6 HOH 86  386 224 HOH HOH A . 
N 6 HOH 87  387 55  HOH HOH A . 
N 6 HOH 88  388 18  HOH HOH A . 
N 6 HOH 89  389 60  HOH HOH A . 
N 6 HOH 90  390 3   HOH HOH A . 
N 6 HOH 91  391 25  HOH HOH A . 
N 6 HOH 92  392 241 HOH HOH A . 
N 6 HOH 93  393 84  HOH HOH A . 
N 6 HOH 94  394 58  HOH HOH A . 
N 6 HOH 95  395 219 HOH HOH A . 
N 6 HOH 96  396 35  HOH HOH A . 
N 6 HOH 97  397 175 HOH HOH A . 
N 6 HOH 98  398 24  HOH HOH A . 
N 6 HOH 99  399 95  HOH HOH A . 
N 6 HOH 100 400 39  HOH HOH A . 
N 6 HOH 101 401 79  HOH HOH A . 
N 6 HOH 102 402 33  HOH HOH A . 
N 6 HOH 103 403 206 HOH HOH A . 
N 6 HOH 104 404 10  HOH HOH A . 
N 6 HOH 105 405 19  HOH HOH A . 
N 6 HOH 106 406 126 HOH HOH A . 
N 6 HOH 107 407 137 HOH HOH A . 
N 6 HOH 108 408 56  HOH HOH A . 
N 6 HOH 109 409 34  HOH HOH A . 
N 6 HOH 110 410 51  HOH HOH A . 
N 6 HOH 111 411 37  HOH HOH A . 
N 6 HOH 112 412 32  HOH HOH A . 
N 6 HOH 113 413 87  HOH HOH A . 
N 6 HOH 114 414 5   HOH HOH A . 
N 6 HOH 115 415 91  HOH HOH A . 
N 6 HOH 116 416 177 HOH HOH A . 
N 6 HOH 117 417 66  HOH HOH A . 
N 6 HOH 118 418 230 HOH HOH A . 
N 6 HOH 119 419 76  HOH HOH A . 
N 6 HOH 120 420 50  HOH HOH A . 
N 6 HOH 121 421 38  HOH HOH A . 
N 6 HOH 122 422 96  HOH HOH A . 
N 6 HOH 123 423 47  HOH HOH A . 
N 6 HOH 124 424 106 HOH HOH A . 
N 6 HOH 125 425 200 HOH HOH A . 
N 6 HOH 126 426 184 HOH HOH A . 
N 6 HOH 127 427 125 HOH HOH A . 
N 6 HOH 128 428 30  HOH HOH A . 
N 6 HOH 129 429 46  HOH HOH A . 
N 6 HOH 130 430 154 HOH HOH A . 
N 6 HOH 131 431 130 HOH HOH A . 
N 6 HOH 132 432 59  HOH HOH A . 
N 6 HOH 133 433 9   HOH HOH A . 
N 6 HOH 134 434 36  HOH HOH A . 
N 6 HOH 135 435 132 HOH HOH A . 
N 6 HOH 136 436 210 HOH HOH A . 
N 6 HOH 137 437 127 HOH HOH A . 
N 6 HOH 138 438 237 HOH HOH A . 
N 6 HOH 139 439 78  HOH HOH A . 
N 6 HOH 140 440 179 HOH HOH A . 
N 6 HOH 141 441 117 HOH HOH A . 
N 6 HOH 142 442 17  HOH HOH A . 
N 6 HOH 143 443 187 HOH HOH A . 
N 6 HOH 144 444 198 HOH HOH A . 
N 6 HOH 145 445 53  HOH HOH A . 
N 6 HOH 146 446 107 HOH HOH A . 
N 6 HOH 147 447 144 HOH HOH A . 
N 6 HOH 148 448 193 HOH HOH A . 
N 6 HOH 149 449 122 HOH HOH A . 
N 6 HOH 150 450 189 HOH HOH A . 
N 6 HOH 151 451 216 HOH HOH A . 
N 6 HOH 152 452 231 HOH HOH A . 
N 6 HOH 153 453 167 HOH HOH A . 
N 6 HOH 154 454 180 HOH HOH A . 
N 6 HOH 155 455 162 HOH HOH A . 
N 6 HOH 156 456 71  HOH HOH A . 
N 6 HOH 157 457 204 HOH HOH A . 
N 6 HOH 158 458 72  HOH HOH A . 
N 6 HOH 159 459 191 HOH HOH A . 
N 6 HOH 160 460 183 HOH HOH A . 
N 6 HOH 161 461 94  HOH HOH A . 
N 6 HOH 162 462 202 HOH HOH A . 
N 6 HOH 163 463 111 HOH HOH A . 
N 6 HOH 164 464 228 HOH HOH A . 
N 6 HOH 165 465 121 HOH HOH A . 
N 6 HOH 166 466 229 HOH HOH A . 
N 6 HOH 167 467 172 HOH HOH A . 
N 6 HOH 168 468 119 HOH HOH A . 
N 6 HOH 169 469 82  HOH HOH A . 
N 6 HOH 170 470 201 HOH HOH A . 
N 6 HOH 171 471 142 HOH HOH A . 
N 6 HOH 172 472 169 HOH HOH A . 
N 6 HOH 173 473 166 HOH HOH A . 
N 6 HOH 174 474 168 HOH HOH A . 
N 6 HOH 175 475 148 HOH HOH A . 
N 6 HOH 176 476 186 HOH HOH A . 
N 6 HOH 177 477 223 HOH HOH A . 
N 6 HOH 178 478 208 HOH HOH A . 
N 6 HOH 179 479 74  HOH HOH A . 
N 6 HOH 180 480 170 HOH HOH A . 
N 6 HOH 181 481 110 HOH HOH A . 
N 6 HOH 182 482 43  HOH HOH A . 
N 6 HOH 183 483 192 HOH HOH A . 
N 6 HOH 184 484 145 HOH HOH A . 
N 6 HOH 185 485 139 HOH HOH A . 
N 6 HOH 186 486 176 HOH HOH A . 
N 6 HOH 187 487 89  HOH HOH A . 
N 6 HOH 188 488 159 HOH HOH A . 
N 6 HOH 189 489 156 HOH HOH A . 
N 6 HOH 190 490 212 HOH HOH A . 
N 6 HOH 191 491 218 HOH HOH A . 
N 6 HOH 192 492 205 HOH HOH A . 
N 6 HOH 193 493 211 HOH HOH A . 
N 6 HOH 194 494 207 HOH HOH A . 
N 6 HOH 195 495 196 HOH HOH A . 
N 6 HOH 196 496 158 HOH HOH A . 
N 6 HOH 197 497 227 HOH HOH A . 
N 6 HOH 198 498 232 HOH HOH A . 
N 6 HOH 199 499 217 HOH HOH A . 
N 6 HOH 200 500 161 HOH HOH A . 
N 6 HOH 201 501 182 HOH HOH A . 
N 6 HOH 202 502 108 HOH HOH A . 
N 6 HOH 203 503 185 HOH HOH A . 
N 6 HOH 204 504 152 HOH HOH A . 
N 6 HOH 205 505 178 HOH HOH A . 
N 6 HOH 206 506 143 HOH HOH A . 
N 6 HOH 207 507 131 HOH HOH A . 
N 6 HOH 208 508 160 HOH HOH A . 
N 6 HOH 209 509 134 HOH HOH A . 
N 6 HOH 210 510 103 HOH HOH A . 
N 6 HOH 211 511 220 HOH HOH A . 
N 6 HOH 212 512 199 HOH HOH A . 
N 6 HOH 213 513 203 HOH HOH A . 
N 6 HOH 214 514 75  HOH HOH A . 
N 6 HOH 215 515 80  HOH HOH A . 
N 6 HOH 216 516 225 HOH HOH A . 
N 6 HOH 217 517 27  HOH HOH A . 
N 6 HOH 218 518 214 HOH HOH A . 
N 6 HOH 219 519 197 HOH HOH A . 
N 6 HOH 220 520 86  HOH HOH A . 
N 6 HOH 221 521 163 HOH HOH A . 
N 6 HOH 222 522 215 HOH HOH A . 
N 6 HOH 223 523 140 HOH HOH A . 
N 6 HOH 224 524 238 HOH HOH A . 
N 6 HOH 225 525 88  HOH HOH A . 
N 6 HOH 226 526 100 HOH HOH A . 
N 6 HOH 227 527 149 HOH HOH A . 
N 6 HOH 228 528 22  HOH HOH A . 
N 6 HOH 229 529 165 HOH HOH A . 
N 6 HOH 230 530 68  HOH HOH A . 
N 6 HOH 231 531 222 HOH HOH A . 
N 6 HOH 232 532 221 HOH HOH A . 
N 6 HOH 233 533 150 HOH HOH A . 
N 6 HOH 234 534 213 HOH HOH A . 
N 6 HOH 235 535 240 HOH HOH A . 
N 6 HOH 236 536 135 HOH HOH A . 
N 6 HOH 237 537 171 HOH HOH A . 
N 6 HOH 238 538 195 HOH HOH A . 
N 6 HOH 239 539 147 HOH HOH A . 
N 6 HOH 240 540 239 HOH HOH A . 
N 6 HOH 241 541 98  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A LEU 173 ? CB  ? A LEU 173 CB  
2 1 Y 1 A LEU 173 ? CG  ? A LEU 173 CG  
3 1 Y 1 A LEU 173 ? CD1 ? A LEU 173 CD1 
4 1 Y 1 A LEU 173 ? CD2 ? A LEU 173 CD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.1_4122 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? AutoSol ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EWP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     43.139 
_cell.length_a_esd                 ? 
_cell.length_b                     44.169 
_cell.length_b_esd                 ? 
_cell.length_c                     97.578 
_cell.length_c_esd                 ? 
_cell.volume                       185925.755 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9EWP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9EWP 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.28 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.16 
_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              7 
_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    'PEG smear, ethylene glycol, ammonium sulphate, cadmium chloride hydrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-02-19 
_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   1 
_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 X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          15.16 
_reflns.entry_id                                       9EWP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.21 
_reflns.d_resolution_low                               40.24 
_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                                     109888 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.55 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          25.47 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.21 
_reflns_shell.d_res_low                                     1.253 
_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                             5615 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.876 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                               20.95 
_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                                 9EWP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.21 
_refine.ls_d_res_low                             40.24 
_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                     109227 
_refine.ls_number_reflns_R_free                  5474 
_refine.ls_number_reflns_R_work                  103753 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.16 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1356 
_refine.ls_R_factor_R_free                       0.1557 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1346 
_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                          1.33 
_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          SAD 
_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                 19.3534 
_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                            0.2057 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.21 
_refine_hist.d_res_low                        40.24 
_refine_hist.number_atoms_solvent             241 
_refine_hist.number_atoms_total               1651 
_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        1389 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         21 
_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' ? 0.0189 ? 1451 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.6121 ? 1973 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.1020 ? 213  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0165 ? 255  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 5.6424 ? 195  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.21 1.22  . . 158 2958 84.35  . . . . 0.9701 . . . . . . . . . . . 1.0834 
'X-RAY DIFFRACTION' 1.22 1.24  . . 180 3417 97.85  . . . . 0.6896 . . . . . . . . . . . 0.7252 
'X-RAY DIFFRACTION' 1.24 1.25  . . 179 3382 97.80  . . . . 0.4211 . . . . . . . . . . . 0.3265 
'X-RAY DIFFRACTION' 1.25 1.27  . . 183 3506 98.87  . . . . 0.2831 . . . . . . . . . . . 0.2942 
'X-RAY DIFFRACTION' 1.27 1.28  . . 183 3418 99.28  . . . . 0.2344 . . . . . . . . . . . 0.2325 
'X-RAY DIFFRACTION' 1.28 1.30  . . 182 3484 99.27  . . . . 0.2367 . . . . . . . . . . . 0.2657 
'X-RAY DIFFRACTION' 1.30 1.32  . . 182 3410 99.72  . . . . 0.2551 . . . . . . . . . . . 0.2902 
'X-RAY DIFFRACTION' 1.32 1.34  . . 187 3549 99.47  . . . . 0.2907 . . . . . . . . . . . 0.3325 
'X-RAY DIFFRACTION' 1.34 1.36  . . 178 3433 99.75  . . . . 0.2454 . . . . . . . . . . . 0.3305 
'X-RAY DIFFRACTION' 1.36 1.38  . . 187 3510 99.81  . . . . 0.2096 . . . . . . . . . . . 0.2005 
'X-RAY DIFFRACTION' 1.38 1.41  . . 187 3467 99.86  . . . . 0.1789 . . . . . . . . . . . 0.1531 
'X-RAY DIFFRACTION' 1.41 1.43  . . 184 3495 99.70  . . . . 0.1417 . . . . . . . . . . . 0.1671 
'X-RAY DIFFRACTION' 1.43 1.46  . . 185 3470 100.00 . . . . 0.1184 . . . . . . . . . . . 0.1607 
'X-RAY DIFFRACTION' 1.46 1.49  . . 182 3486 100.00 . . . . 0.1065 . . . . . . . . . . . 0.1441 
'X-RAY DIFFRACTION' 1.49 1.52  . . 184 3465 99.95  . . . . 0.1089 . . . . . . . . . . . 0.1364 
'X-RAY DIFFRACTION' 1.52 1.56  . . 182 3490 100.00 . . . . 0.1094 . . . . . . . . . . . 0.1260 
'X-RAY DIFFRACTION' 1.56 1.60  . . 184 3510 99.95  . . . . 0.1158 . . . . . . . . . . . 0.1433 
'X-RAY DIFFRACTION' 1.60 1.64  . . 182 3468 99.95  . . . . 0.1177 . . . . . . . . . . . 0.1728 
'X-RAY DIFFRACTION' 1.64 1.69  . . 184 3497 100.00 . . . . 0.1134 . . . . . . . . . . . 0.1475 
'X-RAY DIFFRACTION' 1.69 1.74  . . 181 3465 100.00 . . . . 0.0993 . . . . . . . . . . . 0.1309 
'X-RAY DIFFRACTION' 1.74 1.81  . . 188 3516 100.00 . . . . 0.1039 . . . . . . . . . . . 0.1241 
'X-RAY DIFFRACTION' 1.81 1.88  . . 186 3479 100.00 . . . . 0.1064 . . . . . . . . . . . 0.1440 
'X-RAY DIFFRACTION' 1.88 1.96  . . 185 3474 100.00 . . . . 0.1057 . . . . . . . . . . . 0.1314 
'X-RAY DIFFRACTION' 1.96 2.07  . . 183 3509 100.00 . . . . 0.1046 . . . . . . . . . . . 0.1182 
'X-RAY DIFFRACTION' 2.07 2.20  . . 186 3474 100.00 . . . . 0.1061 . . . . . . . . . . . 0.1440 
'X-RAY DIFFRACTION' 2.20 2.37  . . 186 3491 100.00 . . . . 0.1063 . . . . . . . . . . . 0.1240 
'X-RAY DIFFRACTION' 2.37 2.60  . . 178 3471 100.00 . . . . 0.1098 . . . . . . . . . . . 0.1164 
'X-RAY DIFFRACTION' 2.60 2.98  . . 187 3497 100.00 . . . . 0.1233 . . . . . . . . . . . 0.1251 
'X-RAY DIFFRACTION' 2.98 3.76  . . 181 3481 100.00 . . . . 0.1304 . . . . . . . . . . . 0.1492 
'X-RAY DIFFRACTION' 3.76 40.24 . . 180 3481 99.51  . . . . 0.1562 . . . . . . . . . . . 0.1766 
# 
_struct.entry_id                     9EWP 
_struct.title                        'Crystal structure of yeast E2 Ubiquitin-conjugating enzyme Ubc6 UBC domain' 
_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        9EWP 
_struct_keywords.text            'Ubiquitin, Endoplasmic Reticulum, non-canonical ubiquitination, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A8H8ULW7_YEASX 
_struct_ref.pdbx_db_accession          A0A8H8ULW7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKQAHKRLTKEYKLMVENPPPYILARPNEDNILEWHYIITGPADTPYKGGQYHGTLTFPSDYPYKPPAIRMITPNGRF
KPNTRLCLSMSDYHPDTWNPGWSVSTILNGLLSFMTSDEATTGSITTSDHQKKTLARNSISYNTFQNVRFKLIFPEVVQE
NVETLEKRKLDE
;
_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              9EWP 
_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                 172 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A8H8ULW7 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  172 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       172 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EWP LEU A 173 ? UNP A0A8H8ULW7 ? ? 'expression tag' 173 1 
1 9EWP PRO A 174 ? UNP A0A8H8ULW7 ? ? 'expression tag' 174 2 
1 9EWP GLU A 175 ? UNP A0A8H8ULW7 ? ? 'expression tag' 175 3 
1 9EWP THR A 176 ? UNP A0A8H8ULW7 ? ? 'expression tag' 176 4 
1 9EWP GLY A 177 ? UNP A0A8H8ULW7 ? ? 'expression tag' 177 5 
1 9EWP GLY A 178 ? UNP A0A8H8ULW7 ? ? 'expression tag' 178 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 THR A 3   ? ASN A 20  ? THR A 3   ASN A 20  1 ? 18 
HELX_P HELX_P2 AA2 SER A 103 ? SER A 117 ? SER A 103 SER A 117 1 ? 15 
HELX_P HELX_P3 AA3 SER A 128 ? GLN A 146 ? SER A 128 GLN A 146 1 ? 19 
HELX_P HELX_P4 AA4 ASN A 147 ? PHE A 154 ? ASN A 147 PHE A 154 1 ? 8  
HELX_P HELX_P5 AA5 PHE A 154 ? LEU A 173 ? PHE A 154 LEU A 173 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A GLU 31  OE1 ? ? ? 1_555 J NA  . NA ? ? A GLU 31  A NA  209 1_555 ? ? ? ? ? ? ? 2.522 ? ? 
metalc2  metalc ? ? A GLU 31  OE2 ? ? ? 1_555 J NA  . NA ? ? A GLU 31  A NA  209 1_555 ? ? ? ? ? ? ? 2.432 ? ? 
metalc3  metalc ? ? A ASP 32  OD1 ? ? ? 1_555 I NA  . NA ? ? A ASP 32  A NA  208 1_555 ? ? ? ? ? ? ? 2.405 ? ? 
metalc4  metalc ? ? A ASP 32  OD2 ? ? ? 1_555 I NA  . NA ? ? A ASP 32  A NA  208 1_555 ? ? ? ? ? ? ? 2.529 ? ? 
metalc5  metalc ? ? A ASP 46  OD2 ? ? ? 1_555 E CD  . CD ? ? A ASP 46  A CD  204 4_556 ? ? ? ? ? ? ? 2.296 ? ? 
metalc6  metalc ? ? A CYS 87  SG  ? ? ? 1_555 E CD  . CD ? ? A CYS 87  A CD  204 1_565 ? ? ? ? ? ? ? 2.482 ? ? 
metalc7  metalc ? ? A CYS 87  SG  ? ? ? 1_555 F CD  . CD ? ? A CYS 87  A CD  205 1_565 ? ? ? ? ? ? ? 2.598 ? ? 
metalc8  metalc ? ? A HIS 94  ND1 ? ? ? 1_555 G CD  . CD ? ? A HIS 94  A CD  206 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc9  metalc ? ? A ASP 96  OD1 ? ? ? 1_555 G CD  . CD ? ? A ASP 96  A CD  206 1_555 ? ? ? ? ? ? ? 2.393 ? ? 
metalc10 metalc ? ? A ASP 96  OD2 ? ? ? 1_555 G CD  . CD ? ? A ASP 96  A CD  206 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc11 metalc ? ? A THR 121 OG1 ? ? ? 1_555 F CD  . CD ? ? A THR 121 A CD  205 1_565 ? ? ? ? ? ? ? 2.338 ? ? 
metalc12 metalc ? ? A HIS 130 NE2 ? ? ? 1_555 H CD  . CD ? ? A HIS 130 A CD  207 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc13 metalc ? ? A GLU 163 OE1 ? ? ? 1_555 E CD  . CD ? ? A GLU 163 A CD  204 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
metalc14 metalc ? ? A GLU 163 OE2 ? ? ? 1_555 F CD  . CD ? ? A GLU 163 A CD  205 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc15 metalc ? ? A GLU 166 OE1 ? ? ? 1_555 E CD  . CD ? ? A GLU 166 A CD  204 1_555 ? ? ? ? ? ? ? 2.263 ? ? 
metalc16 metalc ? ? A GLU 166 OE2 ? ? ? 1_555 F CD  . CD ? ? A GLU 166 A CD  205 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc17 metalc ? ? B EDO .   O1  ? ? ? 1_555 F CD  . CD ? ? A EDO 201 A CD  205 1_565 ? ? ? ? ? ? ? 2.346 ? ? 
metalc18 metalc ? ? E CD  .   CD  ? ? ? 1_555 N HOH . O  ? ? A CD  204 A HOH 324 4_456 ? ? ? ? ? ? ? 2.195 ? ? 
metalc19 metalc ? ? F CD  .   CD  ? ? ? 1_555 N HOH . O  ? ? A CD  205 A HOH 329 1_545 ? ? ? ? ? ? ? 2.340 ? ? 
metalc20 metalc ? ? G CD  .   CD  ? ? ? 1_555 N HOH . O  ? ? A CD  206 A HOH 362 1_555 ? ? ? ? ? ? ? 2.417 ? ? 
metalc21 metalc ? ? I NA  .   NA  ? ? ? 1_555 N HOH . O  ? ? A NA  208 A HOH 318 1_555 ? ? ? ? ? ? ? 2.961 ? ? 
metalc22 metalc ? ? J NA  .   NA  ? ? ? 1_555 N HOH . O  ? ? A NA  209 A HOH 380 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
metalc23 metalc ? ? J NA  .   NA  ? ? ? 1_555 N HOH . O  ? ? A NA  209 A HOH 406 1_555 ? ? ? ? ? ? ? 2.856 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLU 31  ? A GLU 31  ? 1_555 NA ? J NA . ? A NA 209 ? 1_555 OE2 ? A GLU 31  ? A GLU 31  ? 1_555 54.1  ? 
2  OE1 ? A GLU 31  ? A GLU 31  ? 1_555 NA ? J NA . ? A NA 209 ? 1_555 O   ? N HOH .   ? A HOH 380 ? 1_555 71.8  ? 
3  OE2 ? A GLU 31  ? A GLU 31  ? 1_555 NA ? J NA . ? A NA 209 ? 1_555 O   ? N HOH .   ? A HOH 380 ? 1_555 89.7  ? 
4  OE1 ? A GLU 31  ? A GLU 31  ? 1_555 NA ? J NA . ? A NA 209 ? 1_555 O   ? N HOH .   ? A HOH 406 ? 1_555 118.2 ? 
5  OE2 ? A GLU 31  ? A GLU 31  ? 1_555 NA ? J NA . ? A NA 209 ? 1_555 O   ? N HOH .   ? A HOH 406 ? 1_555 64.3  ? 
6  O   ? N HOH .   ? A HOH 380 ? 1_555 NA ? J NA . ? A NA 209 ? 1_555 O   ? N HOH .   ? A HOH 406 ? 1_555 106.2 ? 
7  OD1 ? A ASP 32  ? A ASP 32  ? 1_555 NA ? I NA . ? A NA 208 ? 1_555 OD2 ? A ASP 32  ? A ASP 32  ? 1_555 52.8  ? 
8  OD1 ? A ASP 32  ? A ASP 32  ? 1_555 NA ? I NA . ? A NA 208 ? 1_555 O   ? N HOH .   ? A HOH 318 ? 1_555 57.3  ? 
9  OD2 ? A ASP 32  ? A ASP 32  ? 1_555 NA ? I NA . ? A NA 208 ? 1_555 O   ? N HOH .   ? A HOH 318 ? 1_555 107.4 ? 
10 OD2 ? A ASP 46  ? A ASP 46  ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 SG  ? A CYS 87  ? A CYS 87  ? 1_555 35.1  ? 
11 OD2 ? A ASP 46  ? A ASP 46  ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 OE1 ? A GLU 163 ? A GLU 163 ? 1_555 50.9  ? 
12 SG  ? A CYS 87  ? A CYS 87  ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 OE1 ? A GLU 163 ? A GLU 163 ? 1_555 86.0  ? 
13 OD2 ? A ASP 46  ? A ASP 46  ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 OE1 ? A GLU 166 ? A GLU 166 ? 1_555 51.2  ? 
14 SG  ? A CYS 87  ? A CYS 87  ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 OE1 ? A GLU 166 ? A GLU 166 ? 1_555 86.0  ? 
15 OE1 ? A GLU 163 ? A GLU 163 ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 OE1 ? A GLU 166 ? A GLU 166 ? 1_555 5.6   ? 
16 OD2 ? A ASP 46  ? A ASP 46  ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 O   ? N HOH .   ? A HOH 324 ? 4_456 47.1  ? 
17 SG  ? A CYS 87  ? A CYS 87  ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 O   ? N HOH .   ? A HOH 324 ? 4_456 82.2  ? 
18 OE1 ? A GLU 163 ? A GLU 163 ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 O   ? N HOH .   ? A HOH 324 ? 4_456 3.8   ? 
19 OE1 ? A GLU 166 ? A GLU 166 ? 1_555 CD ? E CD . ? A CD 204 ? 4_556 O   ? N HOH .   ? A HOH 324 ? 4_456 6.3   ? 
20 SG  ? A CYS 87  ? A CYS 87  ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 OG1 ? A THR 121 ? A THR 121 ? 1_555 84.8  ? 
21 SG  ? A CYS 87  ? A CYS 87  ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 OE2 ? A GLU 163 ? A GLU 163 ? 1_555 75.8  ? 
22 OG1 ? A THR 121 ? A THR 121 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 OE2 ? A GLU 163 ? A GLU 163 ? 1_555 19.8  ? 
23 SG  ? A CYS 87  ? A CYS 87  ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 OE2 ? A GLU 166 ? A GLU 166 ? 1_555 76.0  ? 
24 OG1 ? A THR 121 ? A THR 121 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 OE2 ? A GLU 166 ? A GLU 166 ? 1_555 16.4  ? 
25 OE2 ? A GLU 163 ? A GLU 163 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 OE2 ? A GLU 166 ? A GLU 166 ? 1_555 3.7   ? 
26 SG  ? A CYS 87  ? A CYS 87  ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 O1  ? B EDO .   ? A EDO 201 ? 1_555 91.0  ? 
27 OG1 ? A THR 121 ? A THR 121 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 O1  ? B EDO .   ? A EDO 201 ? 1_555 101.7 ? 
28 OE2 ? A GLU 163 ? A GLU 163 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 O1  ? B EDO .   ? A EDO 201 ? 1_555 84.2  ? 
29 OE2 ? A GLU 166 ? A GLU 166 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 O1  ? B EDO .   ? A EDO 201 ? 1_555 87.9  ? 
30 SG  ? A CYS 87  ? A CYS 87  ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 O   ? N HOH .   ? A HOH 329 ? 1_545 78.5  ? 
31 OG1 ? A THR 121 ? A THR 121 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 O   ? N HOH .   ? A HOH 329 ? 1_545 18.4  ? 
32 OE2 ? A GLU 163 ? A GLU 163 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 O   ? N HOH .   ? A HOH 329 ? 1_545 2.7   ? 
33 OE2 ? A GLU 166 ? A GLU 166 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 O   ? N HOH .   ? A HOH 329 ? 1_545 4.2   ? 
34 O1  ? B EDO .   ? A EDO 201 ? 1_555 CD ? F CD . ? A CD 205 ? 1_565 O   ? N HOH .   ? A HOH 329 ? 1_545 84.5  ? 
35 ND1 ? A HIS 94  ? A HIS 94  ? 1_555 CD ? G CD . ? A CD 206 ? 1_555 OD1 ? A ASP 96  ? A ASP 96  ? 1_555 104.8 ? 
36 ND1 ? A HIS 94  ? A HIS 94  ? 1_555 CD ? G CD . ? A CD 206 ? 1_555 OD2 ? A ASP 96  ? A ASP 96  ? 1_555 159.0 ? 
37 OD1 ? A ASP 96  ? A ASP 96  ? 1_555 CD ? G CD . ? A CD 206 ? 1_555 OD2 ? A ASP 96  ? A ASP 96  ? 1_555 54.3  ? 
38 ND1 ? A HIS 94  ? A HIS 94  ? 1_555 CD ? G CD . ? A CD 206 ? 1_555 O   ? N HOH .   ? A HOH 362 ? 1_555 80.8  ? 
39 OD1 ? A ASP 96  ? A ASP 96  ? 1_555 CD ? G CD . ? A CD 206 ? 1_555 O   ? N HOH .   ? A HOH 362 ? 1_555 84.4  ? 
40 OD2 ? A ASP 96  ? A ASP 96  ? 1_555 CD ? G CD . ? A CD 206 ? 1_555 O   ? N HOH .   ? A HOH 362 ? 1_555 94.6  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TYR 
_struct_mon_prot_cis.label_seq_id           64 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TYR 
_struct_mon_prot_cis.auth_seq_id            64 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    65 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     65 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       15.18 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   4 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
# 
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 ILE A 25 ? ASN A 30 ? ILE A 25 ASN A 30 
AA1 2 ASN A 33 ? THR A 42 ? ASN A 33 THR A 42 
AA1 3 GLN A 53 ? THR A 59 ? GLN A 53 THR A 59 
AA1 4 ALA A 70 ? MET A 73 ? ALA A 70 MET A 73 
# 
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 ASN A 30 ? N ASN A 30 O GLU A 36 ? O GLU A 36 
AA1 2 3 N TRP A 37 ? N TRP A 37 O LEU A 58 ? O LEU A 58 
AA1 3 4 N THR A 59 ? N THR A 59 O ALA A 70 ? O ALA A 70 
# 
_pdbx_entry_details.entry_id                   9EWP 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HD2 A HIS 130 ? ? CD A CD  207 ? ? 1.47 
2 1 HO1 A EDO 203 ? ? O  A HOH 304 ? ? 1.53 
3 1 CD2 A HIS 130 ? ? CD A CD  207 ? ? 1.82 
4 1 O   A HOH 498 ? ? O  A HOH 535 ? ? 1.87 
5 1 O   A HOH 438 ? ? O  A HOH 485 ? ? 1.89 
6 1 OD2 A ASP 171 ? ? O  A HOH 301 ? ? 2.03 
7 1 O   A HOH 444 ? ? O  A HOH 524 ? ? 2.03 
8 1 O   A HOH 344 ? ? O  A HOH 486 ? ? 2.09 
9 1 O   A HOH 318 ? ? O  A HOH 392 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 28 ? ? CZ A ARG 28 ? ? NH1 A ARG 28 ? ? 124.29 120.30 3.99  0.50 N 
2 1 NE A ARG 28 ? ? CZ A ARG 28 ? ? NH2 A ARG 28 ? ? 116.56 120.30 -3.74 0.50 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 TYR A 24 ? ? 75.47   -0.28  
2 1 ASN A 33 ? ? -163.14 100.41 
3 1 ASP A 46 ? ? -92.60  47.06  
4 1 ASN A 77 ? ? -148.12 -25.33 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A PRO 174 ? A PRO 174 
3 1 Y 1 A GLU 175 ? A GLU 175 
4 1 Y 1 A THR 176 ? A THR 176 
5 1 Y 1 A GLY 177 ? A GLY 177 
6 1 Y 1 A GLY 178 ? A GLY 178 
# 
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  
CD  CD   CD N N 74  
CL  CL   CL N N 75  
CYS N    N  N N 76  
CYS CA   C  N R 77  
CYS C    C  N N 78  
CYS O    O  N N 79  
CYS CB   C  N N 80  
CYS SG   S  N N 81  
CYS OXT  O  N N 82  
CYS H    H  N N 83  
CYS H2   H  N N 84  
CYS HA   H  N N 85  
CYS HB2  H  N N 86  
CYS HB3  H  N N 87  
CYS HG   H  N N 88  
CYS HXT  H  N N 89  
EDO C1   C  N N 90  
EDO O1   O  N N 91  
EDO C2   C  N N 92  
EDO O2   O  N N 93  
EDO H11  H  N N 94  
EDO H12  H  N N 95  
EDO HO1  H  N N 96  
EDO H21  H  N N 97  
EDO H22  H  N N 98  
EDO HO2  H  N N 99  
GLN N    N  N N 100 
GLN CA   C  N S 101 
GLN C    C  N N 102 
GLN O    O  N N 103 
GLN CB   C  N N 104 
GLN CG   C  N N 105 
GLN CD   C  N N 106 
GLN OE1  O  N N 107 
GLN NE2  N  N N 108 
GLN OXT  O  N N 109 
GLN H    H  N N 110 
GLN H2   H  N N 111 
GLN HA   H  N N 112 
GLN HB2  H  N N 113 
GLN HB3  H  N N 114 
GLN HG2  H  N N 115 
GLN HG3  H  N N 116 
GLN HE21 H  N N 117 
GLN HE22 H  N N 118 
GLN HXT  H  N N 119 
GLU N    N  N N 120 
GLU CA   C  N S 121 
GLU C    C  N N 122 
GLU O    O  N N 123 
GLU CB   C  N N 124 
GLU CG   C  N N 125 
GLU CD   C  N N 126 
GLU OE1  O  N N 127 
GLU OE2  O  N N 128 
GLU OXT  O  N N 129 
GLU H    H  N N 130 
GLU H2   H  N N 131 
GLU HA   H  N N 132 
GLU HB2  H  N N 133 
GLU HB3  H  N N 134 
GLU HG2  H  N N 135 
GLU HG3  H  N N 136 
GLU HE2  H  N N 137 
GLU HXT  H  N N 138 
GLY N    N  N N 139 
GLY CA   C  N N 140 
GLY C    C  N N 141 
GLY O    O  N N 142 
GLY OXT  O  N N 143 
GLY H    H  N N 144 
GLY H2   H  N N 145 
GLY HA2  H  N N 146 
GLY HA3  H  N N 147 
GLY HXT  H  N N 148 
HIS N    N  N N 149 
HIS CA   C  N S 150 
HIS C    C  N N 151 
HIS O    O  N N 152 
HIS CB   C  N N 153 
HIS CG   C  Y N 154 
HIS ND1  N  Y N 155 
HIS CD2  C  Y N 156 
HIS CE1  C  Y N 157 
HIS NE2  N  Y N 158 
HIS OXT  O  N N 159 
HIS H    H  N N 160 
HIS H2   H  N N 161 
HIS HA   H  N N 162 
HIS HB2  H  N N 163 
HIS HB3  H  N N 164 
HIS HD1  H  N N 165 
HIS HD2  H  N N 166 
HIS HE1  H  N N 167 
HIS HE2  H  N N 168 
HIS HXT  H  N N 169 
HOH O    O  N N 170 
HOH H1   H  N N 171 
HOH H2   H  N N 172 
ILE N    N  N N 173 
ILE CA   C  N S 174 
ILE C    C  N N 175 
ILE O    O  N N 176 
ILE CB   C  N S 177 
ILE CG1  C  N N 178 
ILE CG2  C  N N 179 
ILE CD1  C  N N 180 
ILE OXT  O  N N 181 
ILE H    H  N N 182 
ILE H2   H  N N 183 
ILE HA   H  N N 184 
ILE HB   H  N N 185 
ILE HG12 H  N N 186 
ILE HG13 H  N N 187 
ILE HG21 H  N N 188 
ILE HG22 H  N N 189 
ILE HG23 H  N N 190 
ILE HD11 H  N N 191 
ILE HD12 H  N N 192 
ILE HD13 H  N N 193 
ILE HXT  H  N N 194 
LEU N    N  N N 195 
LEU CA   C  N S 196 
LEU C    C  N N 197 
LEU O    O  N N 198 
LEU CB   C  N N 199 
LEU CG   C  N N 200 
LEU CD1  C  N N 201 
LEU CD2  C  N N 202 
LEU OXT  O  N N 203 
LEU H    H  N N 204 
LEU H2   H  N N 205 
LEU HA   H  N N 206 
LEU HB2  H  N N 207 
LEU HB3  H  N N 208 
LEU HG   H  N N 209 
LEU HD11 H  N N 210 
LEU HD12 H  N N 211 
LEU HD13 H  N N 212 
LEU HD21 H  N N 213 
LEU HD22 H  N N 214 
LEU HD23 H  N N 215 
LEU HXT  H  N N 216 
LYS N    N  N N 217 
LYS CA   C  N S 218 
LYS C    C  N N 219 
LYS O    O  N N 220 
LYS CB   C  N N 221 
LYS CG   C  N N 222 
LYS CD   C  N N 223 
LYS CE   C  N N 224 
LYS NZ   N  N N 225 
LYS OXT  O  N N 226 
LYS H    H  N N 227 
LYS H2   H  N N 228 
LYS HA   H  N N 229 
LYS HB2  H  N N 230 
LYS HB3  H  N N 231 
LYS HG2  H  N N 232 
LYS HG3  H  N N 233 
LYS HD2  H  N N 234 
LYS HD3  H  N N 235 
LYS HE2  H  N N 236 
LYS HE3  H  N N 237 
LYS HZ1  H  N N 238 
LYS HZ2  H  N N 239 
LYS HZ3  H  N N 240 
LYS HXT  H  N N 241 
MET N    N  N N 242 
MET CA   C  N S 243 
MET C    C  N N 244 
MET O    O  N N 245 
MET CB   C  N N 246 
MET CG   C  N N 247 
MET SD   S  N N 248 
MET CE   C  N N 249 
MET OXT  O  N N 250 
MET H    H  N N 251 
MET H2   H  N N 252 
MET HA   H  N N 253 
MET HB2  H  N N 254 
MET HB3  H  N N 255 
MET HG2  H  N N 256 
MET HG3  H  N N 257 
MET HE1  H  N N 258 
MET HE2  H  N N 259 
MET HE3  H  N N 260 
MET HXT  H  N N 261 
NA  NA   NA N N 262 
PHE N    N  N N 263 
PHE CA   C  N S 264 
PHE C    C  N N 265 
PHE O    O  N N 266 
PHE CB   C  N N 267 
PHE CG   C  Y N 268 
PHE CD1  C  Y N 269 
PHE CD2  C  Y N 270 
PHE CE1  C  Y N 271 
PHE CE2  C  Y N 272 
PHE CZ   C  Y N 273 
PHE OXT  O  N N 274 
PHE H    H  N N 275 
PHE H2   H  N N 276 
PHE HA   H  N N 277 
PHE HB2  H  N N 278 
PHE HB3  H  N N 279 
PHE HD1  H  N N 280 
PHE HD2  H  N N 281 
PHE HE1  H  N N 282 
PHE HE2  H  N N 283 
PHE HZ   H  N N 284 
PHE HXT  H  N N 285 
PRO N    N  N N 286 
PRO CA   C  N S 287 
PRO C    C  N N 288 
PRO O    O  N N 289 
PRO CB   C  N N 290 
PRO CG   C  N N 291 
PRO CD   C  N N 292 
PRO OXT  O  N N 293 
PRO H    H  N N 294 
PRO HA   H  N N 295 
PRO HB2  H  N N 296 
PRO HB3  H  N N 297 
PRO HG2  H  N N 298 
PRO HG3  H  N N 299 
PRO HD2  H  N N 300 
PRO HD3  H  N N 301 
PRO HXT  H  N N 302 
SER N    N  N N 303 
SER CA   C  N S 304 
SER C    C  N N 305 
SER O    O  N N 306 
SER CB   C  N N 307 
SER OG   O  N N 308 
SER OXT  O  N N 309 
SER H    H  N N 310 
SER H2   H  N N 311 
SER HA   H  N N 312 
SER HB2  H  N N 313 
SER HB3  H  N N 314 
SER HG   H  N N 315 
SER HXT  H  N N 316 
THR N    N  N N 317 
THR CA   C  N S 318 
THR C    C  N N 319 
THR O    O  N N 320 
THR CB   C  N R 321 
THR OG1  O  N N 322 
THR CG2  C  N N 323 
THR OXT  O  N N 324 
THR H    H  N N 325 
THR H2   H  N N 326 
THR HA   H  N N 327 
THR HB   H  N N 328 
THR HG1  H  N N 329 
THR HG21 H  N N 330 
THR HG22 H  N N 331 
THR HG23 H  N N 332 
THR HXT  H  N N 333 
TRP N    N  N N 334 
TRP CA   C  N S 335 
TRP C    C  N N 336 
TRP O    O  N N 337 
TRP CB   C  N N 338 
TRP CG   C  Y N 339 
TRP CD1  C  Y N 340 
TRP CD2  C  Y N 341 
TRP NE1  N  Y N 342 
TRP CE2  C  Y N 343 
TRP CE3  C  Y N 344 
TRP CZ2  C  Y N 345 
TRP CZ3  C  Y N 346 
TRP CH2  C  Y N 347 
TRP OXT  O  N N 348 
TRP H    H  N N 349 
TRP H2   H  N N 350 
TRP HA   H  N N 351 
TRP HB2  H  N N 352 
TRP HB3  H  N N 353 
TRP HD1  H  N N 354 
TRP HE1  H  N N 355 
TRP HE3  H  N N 356 
TRP HZ2  H  N N 357 
TRP HZ3  H  N N 358 
TRP HH2  H  N N 359 
TRP HXT  H  N N 360 
TYR N    N  N N 361 
TYR CA   C  N S 362 
TYR C    C  N N 363 
TYR O    O  N N 364 
TYR CB   C  N N 365 
TYR CG   C  Y N 366 
TYR CD1  C  Y N 367 
TYR CD2  C  Y N 368 
TYR CE1  C  Y N 369 
TYR CE2  C  Y N 370 
TYR CZ   C  Y N 371 
TYR OH   O  N N 372 
TYR OXT  O  N N 373 
TYR H    H  N N 374 
TYR H2   H  N N 375 
TYR HA   H  N N 376 
TYR HB2  H  N N 377 
TYR HB3  H  N N 378 
TYR HD1  H  N N 379 
TYR HD2  H  N N 380 
TYR HE1  H  N N 381 
TYR HE2  H  N N 382 
TYR HH   H  N N 383 
TYR HXT  H  N N 384 
VAL N    N  N N 385 
VAL CA   C  N S 386 
VAL C    C  N N 387 
VAL O    O  N N 388 
VAL CB   C  N N 389 
VAL CG1  C  N N 390 
VAL CG2  C  N N 391 
VAL OXT  O  N N 392 
VAL H    H  N N 393 
VAL H2   H  N N 394 
VAL HA   H  N N 395 
VAL HB   H  N N 396 
VAL HG11 H  N N 397 
VAL HG12 H  N N 398 
VAL HG13 H  N N 399 
VAL HG21 H  N N 400 
VAL HG22 H  N N 401 
VAL HG23 H  N N 402 
VAL HXT  H  N N 403 
# 
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  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
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' 677770  1 
'German Research Foundation (DFG)' Germany          SFB1190 2 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EWP 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.023181 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.022640 
_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]   0.010248 
_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.
;
? 
CD  ? ? 36.69012 11.13669 ? ? 1.60906  22.94611 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL  ? ? 9.50761  7.44341  ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H   ? ? 0.51345  0.48472  ? ? 24.73122 6.32584  ? ? 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.
;
? 
NA  ? ? 9.38062  1.54875  ? ? 3.38349  72.32734 ? ? 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.
;
? 
O1- ? ? 5.12366  3.84317  ? ? 3.49406  27.47979 ? ? 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    . ALA A 1 2   ? 12.73769 29.61207 22.88878 1.000 30.80875 ?  2   ALA A N    1 
ATOM   2    C  CA   . ALA A 1 2   ? 13.93765 30.50881 23.04862 1.000 28.78721 ?  2   ALA A CA   1 
ATOM   3    C  C    . ALA A 1 2   ? 14.17341 31.24156 21.71864 1.000 25.58866 ?  2   ALA A C    1 
ATOM   4    O  O    . ALA A 1 2   ? 13.75358 30.68196 20.73746 1.000 28.20883 ?  2   ALA A O    1 
ATOM   5    C  CB   . ALA A 1 2   ? 15.19820 29.72676 23.36932 1.000 28.30173 ?  2   ALA A CB   1 
ATOM   6    H  HA   . ALA A 1 2   ? 13.77047 31.12044 23.78269 1.000 34.55096 ?  2   ALA A HA   1 
ATOM   7    H  HB1  . ALA A 1 2   ? 15.94727 30.34114 23.41775 1.000 33.96838 ?  2   ALA A HB1  1 
ATOM   8    H  HB2  . ALA A 1 2   ? 15.08307 29.27772 24.22138 1.000 33.96838 ?  2   ALA A HB2  1 
ATOM   9    H  HB3  . ALA A 1 2   ? 15.35115 29.07325 22.66902 1.000 33.96838 ?  2   ALA A HB3  1 
ATOM   10   N  N    . THR A 1 3   ? 14.84307 32.43507 21.63394 1.000 23.30422 ?  3   THR A N    1 
ATOM   11   C  CA   . THR A 1 3   ? 15.17632 32.95093 20.29431 1.000 20.89304 ?  3   THR A CA   1 
ATOM   12   C  C    . THR A 1 3   ? 16.16060 31.96677 19.63148 1.000 18.13787 ?  3   THR A C    1 
ATOM   13   O  O    . THR A 1 3   ? 16.90432 31.19871 20.27206 1.000 17.38348 ?  3   THR A O    1 
ATOM   14   C  CB   . THR A 1 3   ? 15.85430 34.33776 20.33192 1.000 20.30642 ?  3   THR A CB   1 
ATOM   15   O  OG1  . THR A 1 3   ? 17.13550 34.17529 20.94974 1.000 20.19573 ?  3   THR A OG1  1 
ATOM   16   C  CG2  . THR A 1 3   ? 14.97461 35.41737 20.98909 1.000 21.48981 ?  3   THR A CG2  1 
ATOM   17   H  H    . THR A 1 3   ? 15.09204 32.92071 22.29859 1.000 27.97136 ?  3   THR A H    1 
ATOM   18   H  HA   . THR A 1 3   ? 14.35424 33.04696 19.78849 1.000 25.07795 ?  3   THR A HA   1 
ATOM   19   H  HB   . THR A 1 3   ? 15.98450 34.68683 19.43632 1.000 24.37400 ?  3   THR A HB   1 
ATOM   20   H  HG1  . THR A 1 3   ? 17.49881 34.92472 21.05914 1.000 24.24118 ?  3   THR A HG1  1 
ATOM   21   H  HG21 . THR A 1 3   ? 15.44728 36.26420 21.00800 1.000 25.79407 ?  3   THR A HG21 1 
ATOM   22   H  HG22 . THR A 1 3   ? 14.15250 35.52689 20.48606 1.000 25.79407 ?  3   THR A HG22 1 
ATOM   23   H  HG23 . THR A 1 3   ? 14.75549 35.15879 21.89794 1.000 25.79407 ?  3   THR A HG23 1 
ATOM   24   N  N    . LYS A 1 4   ? 16.22072 32.04158 18.33149 1.000 18.39384 ?  4   LYS A N    1 
ATOM   25   C  CA   . LYS A 1 4   ? 17.11262 31.17044 17.59076 1.000 19.30740 ?  4   LYS A CA   1 
ATOM   26   C  C    . LYS A 1 4   ? 18.56437 31.43758 17.96927 1.000 17.74054 ?  4   LYS A C    1 
ATOM   27   O  O    . LYS A 1 4   ? 19.38000 30.51207 18.13575 1.000 18.14282 ?  4   LYS A O    1 
ATOM   28   C  CB   . LYS A 1 4   ? 16.95767 31.35632 16.06055 1.000 21.48959 ?  4   LYS A CB   1 
ATOM   29   C  CG   . LYS A 1 4   ? 15.59514 30.97995 15.59333 1.000 25.44296 ?  4   LYS A CG   1 
ATOM   30   C  CD   . LYS A 1 4   ? 15.35225 31.50851 14.14368 1.000 28.05120 ?  4   LYS A CD   1 
ATOM   31   C  CE   . LYS A 1 4   ? 13.92322 31.26599 13.66067 1.000 29.67753 ?  4   LYS A CE   1 
ATOM   32   N  NZ   . LYS A 1 4   ? 13.73028 31.72839 12.26635 1.000 30.01606 ?  4   LYS A NZ   1 
ATOM   33   H  H    . LYS A 1 4   ? 15.76122 32.58297 17.84634 1.000 22.07891 ?  4   LYS A H    1 
ATOM   34   H  HA   . LYS A 1 4   ? 16.87052 30.25669 17.80835 1.000 23.17519 ?  4   LYS A HA   1 
ATOM   35   H  HB2  . LYS A 1 4   ? 17.11065 32.28719 15.83478 1.000 25.79382 ?  4   LYS A HB2  1 
ATOM   36   H  HB3  . LYS A 1 4   ? 17.60242 30.79383 15.60359 1.000 25.79382 ?  4   LYS A HB3  1 
ATOM   37   H  HG2  . LYS A 1 4   ? 15.50754 30.01392 15.58939 1.000 30.53786 ?  4   LYS A HG2  1 
ATOM   38   H  HG3  . LYS A 1 4   ? 14.92983 31.37101 16.18099 1.000 30.53786 ?  4   LYS A HG3  1 
ATOM   39   H  HD2  . LYS A 1 4   ? 15.51783 32.46405 14.12287 1.000 33.66774 ?  4   LYS A HD2  1 
ATOM   40   H  HD3  . LYS A 1 4   ? 15.95572 31.05391 13.53535 1.000 33.66774 ?  4   LYS A HD3  1 
ATOM   41   H  HE2  . LYS A 1 4   ? 13.73014 30.31605 13.69558 1.000 35.61934 ?  4   LYS A HE2  1 
ATOM   42   H  HE3  . LYS A 1 4   ? 13.30588 31.75117 14.23022 1.000 35.61934 ?  4   LYS A HE3  1 
ATOM   43   H  HZ1  . LYS A 1 4   ? 12.89534 31.56586 12.00453 1.000 36.02557 ?  4   LYS A HZ1  1 
ATOM   44   H  HZ2  . LYS A 1 4   ? 13.88507 32.60311 12.21156 1.000 36.02557 ?  4   LYS A HZ2  1 
ATOM   45   H  HZ3  . LYS A 1 4   ? 14.29153 31.30120 11.72357 1.000 36.02557 ?  4   LYS A HZ3  1 
ATOM   46   N  N    . GLN A 1 5   ? 18.90742 32.70530 18.19106 1.000 17.24425 ?  5   GLN A N    1 
ATOM   47   C  CA   . GLN A 1 5   ? 20.24526 33.04920 18.63031 1.000 17.40411 ?  5   GLN A CA   1 
ATOM   48   C  C    . GLN A 1 5   ? 20.56233 32.42876 19.97443 1.000 16.70505 ?  5   GLN A C    1 
ATOM   49   O  O    . GLN A 1 5   ? 21.64186 31.86207 20.16207 1.000 17.52451 ?  5   GLN A O    1 
ATOM   50   C  CB   . GLN A 1 5   ? 20.36426 34.57890 18.68706 1.000 17.38615 ?  5   GLN A CB   1 
ATOM   51   C  CG   . GLN A 1 5   ? 21.72322 35.05302 19.12718 1.000 18.12607 ?  5   GLN A CG   1 
ATOM   52   C  CD   . GLN A 1 5   ? 21.75792 36.53519 19.37559 1.000 18.71921 ?  5   GLN A CD   1 
ATOM   53   O  OE1  . GLN A 1 5   ? 20.71522 37.17306 19.52954 1.000 20.79643 ?  5   GLN A OE1  1 
ATOM   54   N  NE2  . GLN A 1 5   ? 22.94878 37.11662 19.37237 1.000 18.10404 ?  5   GLN A NE2  1 
ATOM   55   H  H    . GLN A 1 5   ? 18.38226 33.37931 18.09350 1.000 20.69940 ?  5   GLN A H    1 
ATOM   56   H  HA   . GLN A 1 5   ? 20.89507 32.70622 17.99706 1.000 20.89124 ?  5   GLN A HA   1 
ATOM   57   H  HB2  . GLN A 1 5   ? 20.19426 34.93987 17.80292 1.000 20.86968 ?  5   GLN A HB2  1 
ATOM   58   H  HB3  . GLN A 1 5   ? 19.71051 34.92135 19.31654 1.000 20.86968 ?  5   GLN A HB3  1 
ATOM   59   H  HG2  . GLN A 1 5   ? 21.96509 34.60307 19.95177 1.000 21.75758 ?  5   GLN A HG2  1 
ATOM   60   H  HG3  . GLN A 1 5   ? 22.37096 34.84780 18.43493 1.000 21.75758 ?  5   GLN A HG3  1 
ATOM   61   H  HE21 . GLN A 1 5   ? 23.65591 36.64761 19.23236 1.000 21.73115 ?  5   GLN A HE21 1 
ATOM   62   H  HE22 . GLN A 1 5   ? 23.01446 37.96294 19.51030 1.000 21.73115 ?  5   GLN A HE22 1 
ATOM   63   N  N    . ALA A 1 6   ? 19.65806 32.56677 20.91863 1.000 16.42904 ?  6   ALA A N    1 
ATOM   64   C  CA   . ALA A 1 6   ? 19.92139 31.99406 22.23513 1.000 16.26298 ?  6   ALA A CA   1 
ATOM   65   C  C    . ALA A 1 6   ? 20.04592 30.47644 22.17647 1.000 16.47044 ?  6   ALA A C    1 
ATOM   66   O  O    . ALA A 1 6   ? 20.88300 29.88210 22.86809 1.000 16.40857 ?  6   ALA A O    1 
ATOM   67   C  CB   . ALA A 1 6   ? 18.82164 32.40678 23.22781 1.000 17.70953 ?  6   ALA A CB   1 
ATOM   68   H  H    . ALA A 1 6   ? 18.90478 32.97308 20.83452 1.000 19.72115 ?  6   ALA A H    1 
ATOM   69   H  HA   . ALA A 1 6   ? 20.76513 32.34854 22.55660 1.000 19.52188 ?  6   ALA A HA   1 
ATOM   70   H  HB1  . ALA A 1 6   ? 18.98498 31.97136 24.07906 1.000 21.25774 ?  6   ALA A HB1  1 
ATOM   71   H  HB2  . ALA A 1 6   ? 18.84246 33.37009 23.33963 1.000 21.25774 ?  6   ALA A HB2  1 
ATOM   72   H  HB3  . ALA A 1 6   ? 17.95999 32.13314 22.87625 1.000 21.25774 ?  6   ALA A HB3  1 
ATOM   73   N  N    . HIS A 1 7   ? 19.15591 29.84644 21.39632 1.000 16.40223 ?  7   HIS A N    1 
ATOM   74   C  CA   . HIS A 1 7   ? 19.17009 28.41546 21.29483 1.000 15.74437 ?  7   HIS A CA   1 
ATOM   75   C  C    . HIS A 1 7   ? 20.48913 27.93193 20.70975 1.000 15.52599 ?  7   HIS A C    1 
ATOM   76   O  O    . HIS A 1 7   ? 21.09652 26.98259 21.22172 1.000 16.17953 ?  7   HIS A O    1 
ATOM   77   C  CB   . HIS A 1 7   ? 17.98221 27.99022 20.44976 1.000 16.98320 ?  7   HIS A CB   1 
ATOM   78   C  CG   . HIS A 1 7   ? 17.94354 26.52746 20.23234 1.000 19.38335 ?  7   HIS A CG   1 
ATOM   79   N  ND1  . HIS A 1 7   ? 18.59846 25.89422 19.19859 1.000 20.65161 ?  7   HIS A ND1  1 
ATOM   80   C  CD2  . HIS A 1 7   ? 17.29827 25.56398 20.91399 1.000 21.45347 ?  7   HIS A CD2  1 
ATOM   81   C  CE1  . HIS A 1 7   ? 18.37432 24.59798 19.26871 1.000 21.54712 ?  7   HIS A CE1  1 
ATOM   82   N  NE2  . HIS A 1 7   ? 17.58537 24.36733 20.30088 1.000 22.36407 ?  7   HIS A NE2  1 
ATOM   83   H  H    . HIS A 1 7   ? 18.54796 30.23479 20.92814 1.000 19.68897 ?  7   HIS A H    1 
ATOM   84   H  HA   . HIS A 1 7   ? 19.08428 28.00613 22.17004 1.000 18.89955 ?  7   HIS A HA   1 
ATOM   85   H  HB2  . HIS A 1 7   ? 17.16312 28.25080 20.89930 1.000 20.38615 ?  7   HIS A HB2  1 
ATOM   86   H  HB3  . HIS A 1 7   ? 18.03745 28.42325 19.58354 1.000 20.38615 ?  7   HIS A HB3  1 
ATOM   87   H  HD2  . HIS A 1 7   ? 16.75814 25.68485 21.66135 1.000 25.75047 ?  7   HIS A HD2  1 
ATOM   88   H  HE1  . HIS A 1 7   ? 18.71431 23.95487 18.68930 1.000 25.86284 ?  7   HIS A HE1  1 
ATOM   89   H  HE2  . HIS A 1 7   ? 17.29809 23.59569 20.54918 1.000 26.84318 ?  7   HIS A HE2  1 
ATOM   90   N  N    . LYS A 1 8   ? 20.96442 28.57023 19.64433 1.000 15.49608 ?  8   LYS A N    1 
ATOM   91   C  CA   . LYS A 1 8   ? 22.23545 28.18060 19.06487 1.000 16.08963 ?  8   LYS A CA   1 
ATOM   92   C  C    . LYS A 1 8   ? 23.37955 28.34590 20.05438 1.000 15.38844 ?  8   LYS A C    1 
ATOM   93   O  O    . LYS A 1 8   ? 24.25451 27.47660 20.19784 1.000 15.69152 ?  8   LYS A O    1 
ATOM   94   C  CB   . LYS A 1 8   ? 22.46362 28.96753 17.77529 1.000 17.92782 ?  8   LYS A CB   1 
ATOM   95   C  CG   . LYS A 1 8   ? 23.79126 28.66902 17.08793 1.000 19.25334 ?  8   LYS A CG   1 
ATOM   96   C  CD   . LYS A 1 8   ? 23.86291 29.46167 15.76898 1.000 20.68484 ?  8   LYS A CD   1 
ATOM   97   C  CE   . LYS A 1 8   ? 25.21688 29.27581 15.06029 1.000 23.85883 ?  8   LYS A CE   1 
ATOM   98   N  NZ   . LYS A 1 8   ? 25.59240 27.95520 14.75327 1.000 27.87801 ?  8   LYS A NZ   1 
ATOM   99   H  H    . LYS A 1 8   ? 20.57261 29.22371 19.24552 1.000 18.60160 ?  8   LYS A H    1 
ATOM   100  H  HA   . LYS A 1 8   ? 22.21150 27.23868 18.83441 1.000 19.31386 ?  8   LYS A HA   1 
ATOM   101  H  HB2  . LYS A 1 8   ? 21.75369 28.75167 17.15054 1.000 21.51969 ?  8   LYS A HB2  1 
ATOM   102  H  HB3  . LYS A 1 8   ? 22.44616 29.91490 17.98289 1.000 21.51969 ?  8   LYS A HB3  1 
ATOM   103  H  HG2  . LYS A 1 8   ? 24.52739 28.93961 17.65872 1.000 23.11031 ?  8   LYS A HG2  1 
ATOM   104  H  HG3  . LYS A 1 8   ? 23.85566 27.72157 16.89024 1.000 23.11031 ?  8   LYS A HG3  1 
ATOM   105  H  HD2  . LYS A 1 8   ? 23.16338 29.15309 15.17204 1.000 24.82811 ?  8   LYS A HD2  1 
ATOM   106  H  HD3  . LYS A 1 8   ? 23.74610 30.40613 15.95673 1.000 24.82811 ?  8   LYS A HD3  1 
ATOM   107  H  HE2  . LYS A 1 8   ? 25.18784 29.76377 14.22246 1.000 28.63689 ?  8   LYS A HE2  1 
ATOM   108  H  HE3  . LYS A 1 8   ? 25.90932 29.64098 15.63307 1.000 28.63689 ?  8   LYS A HE3  1 
ATOM   109  H  HZ1  . LYS A 1 8   ? 26.38857 27.94977 14.35555 1.000 33.45992 ?  8   LYS A HZ1  1 
ATOM   110  H  HZ2  . LYS A 1 8   ? 25.63848 27.47078 15.49846 1.000 33.45992 ?  8   LYS A HZ2  1 
ATOM   111  H  HZ3  . LYS A 1 8   ? 24.99389 27.58785 14.20651 1.000 33.45992 ?  8   LYS A HZ3  1 
ATOM   112  N  N    . ARG A 1 9   ? 23.39648 29.48216 20.74225 1.000 15.27736 ?  9   ARG A N    1 
ATOM   113  C  CA   . ARG A 1 9   ? 24.46958 29.74784 21.69995 1.000 15.46248 ?  9   ARG A CA   1 
ATOM   114  C  C    . ARG A 1 9   ? 24.50182 28.73646 22.83068 1.000 15.37930 ?  9   ARG A C    1 
ATOM   115  O  O    . ARG A 1 9   ? 25.58062 28.22322 23.19350 1.000 15.68805 ?  9   ARG A O    1 
ATOM   116  C  CB   . ARG A 1 9   ? 24.36503 31.17317 22.23578 1.000 15.30532 ?  9   ARG A CB   1 
ATOM   117  C  CG   . ARG A 1 9   ? 25.40268 31.51167 23.33247 1.000 16.45828 ?  9   ARG A CG   1 
ATOM   118  C  CD   . ARG A 1 9   ? 26.84542 31.39790 22.87710 1.000 16.77776 ?  9   ARG A CD   1 
ATOM   119  N  NE   . ARG A 1 9   ? 27.76609 31.73404 23.93563 1.000 16.36303 ?  9   ARG A NE   1 
ATOM   120  C  CZ   . ARG A 1 9   ? 27.96691 32.94648 24.41020 1.000 17.18453 ?  9   ARG A CZ   1 
ATOM   121  N  NH1  . ARG A 1 9   ? 27.45530 34.00777 23.81014 1.000 18.67207 ?  9   ARG A NH1  1 
ATOM   122  N  NH2  . ARG A 1 9   ? 28.76868 33.08632 25.46270 1.000 18.60041 ?  9   ARG A NH2  1 
ATOM   123  H  H    . ARG A 1 9   ? 22.80971 30.10744 20.67650 1.000 18.33913 ?  9   ARG A H    1 
ATOM   124  H  HA   . ARG A 1 9   ? 25.31318 29.66820 21.22782 1.000 18.56127 ?  9   ARG A HA   1 
ATOM   125  H  HB2  . ARG A 1 9   ? 24.49980 31.79201 21.50108 1.000 18.37269 ?  9   ARG A HB2  1 
ATOM   126  H  HB3  . ARG A 1 9   ? 23.48177 31.29789 22.61682 1.000 18.37269 ?  9   ARG A HB3  1 
ATOM   127  H  HG2  . ARG A 1 9   ? 25.25852 32.42482 23.62617 1.000 19.75624 ?  9   ARG A HG2  1 
ATOM   128  H  HG3  . ARG A 1 9   ? 25.28030 30.90081 24.07595 1.000 19.75624 ?  9   ARG A HG3  1 
ATOM   129  H  HD2  . ARG A 1 9   ? 27.02240 30.48594 22.59797 1.000 20.13961 ?  9   ARG A HD2  1 
ATOM   130  H  HD3  . ARG A 1 9   ? 26.99690 32.00663 22.13724 1.000 20.13961 ?  9   ARG A HD3  1 
ATOM   131  H  HE   . ARG A 1 9   ? 28.21978 31.09212 24.28449 1.000 19.64194 ?  9   ARG A HE   1 
ATOM   132  H  HH11 . ARG A 1 9   ? 26.98264 33.91294 23.09797 1.000 22.41278 ?  9   ARG A HH11 1 
ATOM   133  H  HH12 . ARG A 1 9   ? 27.59520 34.79290 24.13201 1.000 22.41278 ?  9   ARG A HH12 1 
ATOM   134  H  HH21 . ARG A 1 9   ? 29.14022 32.39536 25.81503 1.000 22.32679 ?  9   ARG A HH21 1 
ATOM   135  H  HH22 . ARG A 1 9   ? 28.91539 33.86766 25.79070 1.000 22.32679 ?  9   ARG A HH22 1 
ATOM   136  N  N    . LEU A 1 10  ? 23.34345 28.49797 23.43931 1.000 15.02437 ?  10  LEU A N    1 
ATOM   137  C  CA   . LEU A 1 10  ? 23.31740 27.59958 24.59624 1.000 15.52951 ?  10  LEU A CA   1 
ATOM   138  C  C    . LEU A 1 10  ? 23.58937 26.15118 24.21437 1.000 15.81225 ?  10  LEU A C    1 
ATOM   139  O  O    . LEU A 1 10  ? 24.22714 25.40370 24.98371 1.000 16.00426 ?  10  LEU A O    1 
ATOM   140  C  CB   . LEU A 1 10  ? 22.02439 27.79506 25.35558 1.000 15.71666 ?  10  LEU A CB   1 
ATOM   141  C  CG   . LEU A 1 10  ? 21.87799 29.13969 26.05043 1.000 15.19197 ?  10  LEU A CG   1 
ATOM   142  C  CD1  . LEU A 1 10  ? 20.51117 29.40761 26.50696 1.000 16.72065 ?  10  LEU A CD1  1 
ATOM   143  C  CD2  . LEU A 1 10  ? 22.89316 29.25011 27.19520 1.000 16.20912 ?  10  LEU A CD2  1 
ATOM   144  H  H    . LEU A 1 10  ? 22.58320 28.83025 23.21301 1.000 18.03555 ?  10  LEU A H    1 
ATOM   145  H  HA   . LEU A 1 10  ? 24.03187 27.83062 25.21030 1.000 18.64171 ?  10  LEU A HA   1 
ATOM   146  H  HB2  . LEU A 1 10  ? 21.28731 27.70903 24.73091 1.000 18.86630 ?  10  LEU A HB2  1 
ATOM   147  H  HB3  . LEU A 1 10  ? 21.96354 27.10762 26.03721 1.000 18.86630 ?  10  LEU A HB3  1 
ATOM   148  H  HG   . LEU A 1 10  ? 22.06695 29.83513 25.40115 1.000 18.23667 ?  10  LEU A HG   1 
ATOM   149  H  HD11 . LEU A 1 10  ? 20.48898 30.27156 26.94741 1.000 20.07109 ?  10  LEU A HD11 1 
ATOM   150  H  HD12 . LEU A 1 10  ? 19.91722 29.41192 25.74009 1.000 20.07109 ?  10  LEU A HD12 1 
ATOM   151  H  HD13 . LEU A 1 10  ? 20.24386 28.71251 27.12848 1.000 20.07109 ?  10  LEU A HD13 1 
ATOM   152  H  HD21 . LEU A 1 10  ? 22.66418 30.01374 27.74778 1.000 19.45724 ?  10  LEU A HD21 1 
ATOM   153  H  HD22 . LEU A 1 10  ? 22.86206 28.43773 27.72433 1.000 19.45724 ?  10  LEU A HD22 1 
ATOM   154  H  HD23 . LEU A 1 10  ? 23.78019 29.36706 26.82051 1.000 19.45724 ?  10  LEU A HD23 1 
ATOM   155  N  N    A THR A 1 11  ? 23.14106 25.75251 23.02528 0.649 15.45539 ?  11  THR A N    1 
ATOM   156  N  N    B THR A 1 11  ? 23.14809 25.73823 23.02878 0.351 16.05213 ?  11  THR A N    1 
ATOM   157  C  CA   A THR A 1 11  ? 23.50791 24.43158 22.50065 0.649 16.07167 ?  11  THR A CA   1 
ATOM   158  C  CA   B THR A 1 11  ? 23.52455 24.39913 22.59642 0.351 16.66467 ?  11  THR A CA   1 
ATOM   159  C  C    A THR A 1 11  ? 25.03288 24.31962 22.39924 0.649 16.09287 ?  11  THR A C    1 
ATOM   160  C  C    B THR A 1 11  ? 25.04620 24.30623 22.42386 0.351 16.42397 ?  11  THR A C    1 
ATOM   161  O  O    A THR A 1 11  ? 25.64199 23.31255 22.79417 0.649 16.25839 ?  11  THR A O    1 
ATOM   162  O  O    B THR A 1 11  ? 25.66514 23.29993 22.79945 0.351 16.52886 ?  11  THR A O    1 
ATOM   163  C  CB   A THR A 1 11  ? 22.82211 24.25024 21.11717 0.649 17.67758 ?  11  THR A CB   1 
ATOM   164  C  CB   B THR A 1 11  ? 22.80296 23.98345 21.31618 0.351 18.24715 ?  11  THR A CB   1 
ATOM   165  O  OG1  A THR A 1 11  ? 21.41182 24.19884 21.31307 0.649 20.10813 ?  11  THR A OG1  1 
ATOM   166  O  OG1  B THR A 1 11  ? 23.10333 24.87124 20.28724 0.351 17.99115 ?  11  THR A OG1  1 
ATOM   167  C  CG2  A THR A 1 11  ? 23.25056 22.90944 20.40896 0.649 17.99712 ?  11  THR A CG2  1 
ATOM   168  C  CG2  B THR A 1 11  ? 21.32466 24.07463 21.40092 0.351 19.44465 ?  11  THR A CG2  1 
ATOM   169  H  H    A THR A 1 11  ? 22.63264 26.21596 22.50922 0.649 18.55277 ?  11  THR A H    1 
ATOM   170  H  H    B THR A 1 11  ? 22.65663 26.18958 22.48623 0.351 19.26886 ?  11  THR A H    1 
ATOM   171  H  HA   A THR A 1 11  ? 23.19935 23.72205 23.08569 0.649 19.29230 ?  11  THR A HA   1 
ATOM   172  H  HA   B THR A 1 11  ? 23.24114 23.76944 23.27766 0.351 20.00390 ?  11  THR A HA   1 
ATOM   173  H  HB   A THR A 1 11  ? 23.08309 24.99016 20.54682 0.649 21.21940 ?  11  THR A HB   1 
ATOM   174  H  HB   B THR A 1 11  ? 23.08423 23.06865 21.15827 0.351 21.90288 ?  11  THR A HB   1 
ATOM   175  H  HG1  A THR A 1 11  ? 21.14775 24.90349 21.68634 0.649 24.13606 ?  11  THR A HG1  1 
ATOM   176  H  HG1  B THR A 1 11  ? 22.95508 25.65983 20.53575 0.351 21.59569 ?  11  THR A HG1  1 
ATOM   177  H  HG21 A THR A 1 11  ? 22.46672 22.44458 20.07669 0.649 21.60285 ?  11  THR A HG21 1 
ATOM   178  H  HG21 B THR A 1 11  ? 20.91814 23.36048 20.88553 0.351 23.33988 ?  11  THR A HG21 1 
ATOM   179  H  HG22 A THR A 1 11  ? 23.84170 23.10176 19.66433 0.649 21.60285 ?  11  THR A HG22 1 
ATOM   180  H  HG22 B THR A 1 11  ? 21.03994 23.99741 22.32497 0.351 23.33988 ?  11  THR A HG22 1 
ATOM   181  H  HG23 A THR A 1 11  ? 23.71389 22.33507 21.03851 0.649 21.60285 ?  11  THR A HG23 1 
ATOM   182  H  HG23 B THR A 1 11  ? 21.02414 24.92717 21.04912 0.351 23.33988 ?  11  THR A HG23 1 
ATOM   183  N  N    . LYS A 1 12  ? 25.68026 25.34709 21.87177 1.000 16.08854 ?  12  LYS A N    1 
ATOM   184  C  CA   . LYS A 1 12  ? 27.13598 25.30815 21.74734 1.000 16.12196 ?  12  LYS A CA   1 
ATOM   185  C  C    . LYS A 1 12  ? 27.79621 25.30605 23.12250 1.000 16.21245 ?  12  LYS A C    1 
ATOM   186  O  O    . LYS A 1 12  ? 28.79643 24.59709 23.34310 1.000 16.69705 ?  12  LYS A O    1 
ATOM   187  C  CB   . LYS A 1 12  ? 27.58670 26.52570 20.94479 1.000 17.83589 ?  12  LYS A CB   1 
ATOM   188  C  CG   . LYS A 1 12  ? 29.11136 26.70045 20.84395 1.000 22.13131 ?  12  LYS A CG   1 
ATOM   189  C  CD   . LYS A 1 12  ? 29.76625 25.45138 20.24440 1.000 27.85781 ?  12  LYS A CD   1 
ATOM   190  C  CE   . LYS A 1 12  ? 31.26714 25.53345 19.85187 1.000 32.89565 ?  12  LYS A CE   1 
ATOM   191  N  NZ   . LYS A 1 12  ? 31.53427 26.80445 19.15099 1.000 36.57758 ?  12  LYS A NZ   1 
ATOM   192  H  H    A LYS A 1 12  ? 25.31164 26.06800 21.58194 0.649 19.31255 ?  12  LYS A H    1 
ATOM   193  H  H    B LYS A 1 12  ? 25.30321 26.06002 21.57317 0.351 19.31255 ?  12  LYS A H    1 
ATOM   194  H  HA   . LYS A 1 12  ? 27.40909 24.50205 21.28202 1.000 19.35266 ?  12  LYS A HA   1 
ATOM   195  H  HB2  . LYS A 1 12  ? 27.24162 26.44457 20.04188 1.000 21.40937 ?  12  LYS A HB2  1 
ATOM   196  H  HB3  . LYS A 1 12  ? 27.22860 27.32248 21.36646 1.000 21.40937 ?  12  LYS A HB3  1 
ATOM   197  H  HG2  . LYS A 1 12  ? 29.31318 27.45775 20.27240 1.000 26.56388 ?  12  LYS A HG2  1 
ATOM   198  H  HG3  . LYS A 1 12  ? 29.47970 26.84567 21.72947 1.000 26.56388 ?  12  LYS A HG3  1 
ATOM   199  H  HD2  . LYS A 1 12  ? 29.68851 24.73521 20.89398 1.000 33.43567 ?  12  LYS A HD2  1 
ATOM   200  H  HD3  . LYS A 1 12  ? 29.28086 25.22091 19.43681 1.000 33.43567 ?  12  LYS A HD3  1 
ATOM   201  H  HE2  . LYS A 1 12  ? 31.81668 25.49626 20.65032 1.000 39.48109 ?  12  LYS A HE2  1 
ATOM   202  H  HE3  . LYS A 1 12  ? 31.49132 24.79813 19.26029 1.000 39.48109 ?  12  LYS A HE3  1 
ATOM   203  H  HZ1  . LYS A 1 12  ? 30.99713 26.88180 18.44557 1.000 43.89940 ?  12  LYS A HZ1  1 
ATOM   204  H  HZ2  . LYS A 1 12  ? 31.39117 27.49050 19.69959 1.000 43.89940 ?  12  LYS A HZ2  1 
ATOM   205  H  HZ3  . LYS A 1 12  ? 32.37979 26.82752 18.87411 1.000 43.89940 ?  12  LYS A HZ3  1 
ATOM   206  N  N    . GLU A 1 13  ? 27.26573 26.07872 24.06351 1.000 16.38203 ?  13  GLU A N    1 
ATOM   207  C  CA   . GLU A 1 13  ? 27.83509 26.06237 25.41276 1.000 15.96609 ?  13  GLU A CA   1 
ATOM   208  C  C    . GLU A 1 13  ? 27.80681 24.65743 26.00809 1.000 16.52932 ?  13  GLU A C    1 
ATOM   209  O  O    . GLU A 1 13  ? 28.75098 24.26921 26.70394 1.000 18.17570 ?  13  GLU A O    1 
ATOM   210  C  CB   . GLU A 1 13  ? 27.08722 27.06230 26.29385 1.000 15.89593 ?  13  GLU A CB   1 
ATOM   211  C  CG   . GLU A 1 13  ? 27.34914 28.50466 25.94128 1.000 16.79603 ?  13  GLU A CG   1 
ATOM   212  C  CD   . GLU A 1 13  ? 28.72733 29.01496 26.26516 1.000 16.88897 ?  13  GLU A CD   1 
ATOM   213  O  OE1  . GLU A 1 13  ? 29.37200 28.44305 27.14616 1.000 17.07600 ?  13  GLU A OE1  1 
ATOM   214  O  OE2  . GLU A 1 13  ? 29.14468 30.02663 25.66346 1.000 18.63974 -1 13  GLU A OE2  1 
ATOM   215  H  H    . GLU A 1 13  ? 26.59609 26.60721 23.95448 1.000 19.66474 ?  13  GLU A H    1 
ATOM   216  H  HA   . GLU A 1 13  ? 28.76439 26.33803 25.37645 1.000 19.16561 ?  13  GLU A HA   1 
ATOM   217  H  HB2  . GLU A 1 13  ? 26.13440 26.90458 26.20352 1.000 19.08142 ?  13  GLU A HB2  1 
ATOM   218  H  HB3  . GLU A 1 13  ? 27.35961 26.92941 27.21529 1.000 19.08142 ?  13  GLU A HB3  1 
ATOM   219  H  HG2  . GLU A 1 13  ? 27.21944 28.61340 24.98616 1.000 20.16154 ?  13  GLU A HG2  1 
ATOM   220  H  HG3  . GLU A 1 13  ? 26.71664 29.05689 26.42696 1.000 20.16154 ?  13  GLU A HG3  1 
ATOM   221  N  N    . TYR A 1 14  ? 26.71130 23.89794 25.80928 1.000 15.76170 ?  14  TYR A N    1 
ATOM   222  C  CA   . TYR A 1 14  ? 26.67674 22.55230 26.35765 1.000 15.54476 ?  14  TYR A CA   1 
ATOM   223  C  C    . TYR A 1 14  ? 27.71832 21.65923 25.68700 1.000 15.00582 ?  14  TYR A C    1 
ATOM   224  O  O    . TYR A 1 14  ? 28.44136 20.92095 26.34487 1.000 16.50902 ?  14  TYR A O    1 
ATOM   225  C  CB   . TYR A 1 14  ? 25.27963 21.93613 26.23673 1.000 16.58905 ?  14  TYR A CB   1 
ATOM   226  C  CG   . TYR A 1 14  ? 25.28664 20.53657 26.77518 1.000 16.86830 ?  14  TYR A CG   1 
ATOM   227  C  CD1  . TYR A 1 14  ? 25.52098 20.28811 28.12636 1.000 17.85300 ?  14  TYR A CD1  1 
ATOM   228  C  CD2  . TYR A 1 14  ? 25.09318 19.47787 25.92889 1.000 17.06593 ?  14  TYR A CD2  1 
ATOM   229  C  CE1  . TYR A 1 14  ? 25.59630 18.99225 28.59910 1.000 18.41751 ?  14  TYR A CE1  1 
ATOM   230  C  CE2  . TYR A 1 14  ? 25.19379 18.16241 26.39201 1.000 18.10972 ?  14  TYR A CE2  1 
ATOM   231  C  CZ   . TYR A 1 14  ? 25.42687 17.90857 27.72147 1.000 17.78892 ?  14  TYR A CZ   1 
ATOM   232  O  OH   . TYR A 1 14  ? 25.52701 16.61773 28.22149 1.000 19.51178 ?  14  TYR A OH   1 
ATOM   233  H  H    . TYR A 1 14  ? 26.00845 24.13880 25.37617 1.000 18.92034 ?  14  TYR A H    1 
ATOM   234  H  HA   . TYR A 1 14  ? 26.88089 22.60859 27.30425 1.000 18.66002 ?  14  TYR A HA   1 
ATOM   235  H  HB2  . TYR A 1 14  ? 24.64542 22.46336 26.74732 1.000 19.91317 ?  14  TYR A HB2  1 
ATOM   236  H  HB3  . TYR A 1 14  ? 25.01440 21.90995 25.30406 1.000 19.91317 ?  14  TYR A HB3  1 
ATOM   237  H  HD1  . TYR A 1 14  ? 25.62752 21.00053 28.71457 1.000 21.42991 ?  14  TYR A HD1  1 
ATOM   238  H  HD2  . TYR A 1 14  ? 24.89231 19.63567 25.03466 1.000 20.48542 ?  14  TYR A HD2  1 
ATOM   239  H  HE1  . TYR A 1 14  ? 25.75971 18.83681 29.50133 1.000 22.10731 ?  14  TYR A HE1  1 
ATOM   240  H  HE2  . TYR A 1 14  ? 25.10226 17.45458 25.79577 1.000 21.73797 ?  14  TYR A HE2  1 
ATOM   241  H  HH   . TYR A 1 14  ? 25.42910 16.06067 27.60045 1.000 23.42044 ?  14  TYR A HH   1 
ATOM   242  N  N    . LYS A 1 15  ? 27.85610 21.79608 24.36743 1.000 15.80838 ?  15  LYS A N    1 
ATOM   243  C  CA   . LYS A 1 15  ? 28.85592 21.03821 23.66348 1.000 16.99504 ?  15  LYS A CA   1 
ATOM   244  C  C    . LYS A 1 15  ? 30.25376 21.32636 24.20314 1.000 17.52044 ?  15  LYS A C    1 
ATOM   245  O  O    . LYS A 1 15  ? 31.07210 20.40725 24.38301 1.000 17.74368 ?  15  LYS A O    1 
ATOM   246  C  CB   . LYS A 1 15  ? 28.75938 21.32953 22.15969 1.000 19.12775 ?  15  LYS A CB   1 
ATOM   247  C  CG   . LYS A 1 15  ? 29.80319 20.60116 21.30682 1.000 23.22449 ?  15  LYS A CG   1 
ATOM   248  C  CD   . LYS A 1 15  ? 29.57300 20.91687 19.80345 1.000 27.77049 ?  15  LYS A CD   1 
ATOM   249  C  CE   . LYS A 1 15  ? 30.58418 20.31822 18.82928 1.000 31.48432 ?  15  LYS A CE   1 
ATOM   250  N  NZ   . LYS A 1 15  ? 30.84120 18.89516 19.11240 1.000 34.21814 ?  15  LYS A NZ   1 
ATOM   251  H  H    . LYS A 1 15  ? 27.38379 22.31737 23.87269 1.000 18.97635 ?  15  LYS A H    1 
ATOM   252  H  HA   . LYS A 1 15  ? 28.69120 20.09085 23.79104 1.000 20.40035 ?  15  LYS A HA   1 
ATOM   253  H  HB2  . LYS A 1 15  ? 27.88261 21.05652 21.84723 1.000 22.95961 ?  15  LYS A HB2  1 
ATOM   254  H  HB3  . LYS A 1 15  ? 28.87941 22.28197 22.02063 1.000 22.95961 ?  15  LYS A HB3  1 
ATOM   255  H  HG2  . LYS A 1 15  ? 30.69287 20.89777 21.55458 1.000 27.87569 ?  15  LYS A HG2  1 
ATOM   256  H  HG3  . LYS A 1 15  ? 29.72375 19.64358 21.43959 1.000 27.87569 ?  15  LYS A HG3  1 
ATOM   257  H  HD2  . LYS A 1 15  ? 28.69966 20.57764 19.55223 1.000 33.33089 ?  15  LYS A HD2  1 
ATOM   258  H  HD3  . LYS A 1 15  ? 29.60086 21.87953 19.68764 1.000 33.33089 ?  15  LYS A HD3  1 
ATOM   259  H  HE2  . LYS A 1 15  ? 30.23928 20.39059 17.92556 1.000 37.78749 ?  15  LYS A HE2  1 
ATOM   260  H  HE3  . LYS A 1 15  ? 31.42334 20.79903 18.90361 1.000 37.78749 ?  15  LYS A HE3  1 
ATOM   261  H  HZ1  . LYS A 1 15  ? 30.08296 18.43228 19.05843 1.000 41.06808 ?  15  LYS A HZ1  1 
ATOM   262  H  HZ2  . LYS A 1 15  ? 31.42212 18.56763 18.52303 1.000 41.06808 ?  15  LYS A HZ2  1 
ATOM   263  H  HZ3  . LYS A 1 15  ? 31.17780 18.80366 19.93120 1.000 41.06808 ?  15  LYS A HZ3  1 
ATOM   264  N  N    . LEU A 1 16  ? 30.55636 22.60787 24.44098 1.000 17.78610 ?  16  LEU A N    1 
ATOM   265  C  CA   . LEU A 1 16  ? 31.85099 22.95263 24.98526 1.000 17.82841 ?  16  LEU A CA   1 
ATOM   266  C  C    . LEU A 1 16  ? 32.08440 22.32377 26.34774 1.000 18.51739 ?  16  LEU A C    1 
ATOM   267  O  O    . LEU A 1 16  ? 33.20687 21.92655 26.68444 1.000 20.04111 ?  16  LEU A O    1 
ATOM   268  C  CB   . LEU A 1 16  ? 31.95362 24.49069 25.12850 1.000 19.86491 ?  16  LEU A CB   1 
ATOM   269  C  CG   . LEU A 1 16  ? 32.01678 25.29962 23.85996 1.000 21.21053 ?  16  LEU A CG   1 
ATOM   270  C  CD1  . LEU A 1 16  ? 31.87791 26.77888 24.11070 1.000 22.03628 ?  16  LEU A CD1  1 
ATOM   271  C  CD2  . LEU A 1 16  ? 33.30789 25.03236 23.15092 1.000 23.87543 ?  16  LEU A CD2  1 
ATOM   272  H  H    . LEU A 1 16  ? 30.03411 23.27552 24.29573 1.000 21.34962 ?  16  LEU A H    1 
ATOM   273  H  HA   . LEU A 1 16  ? 32.52978 22.62610 24.37409 1.000 21.40040 ?  16  LEU A HA   1 
ATOM   274  H  HB2  . LEU A 1 16  ? 31.17446 24.79626 25.61884 1.000 23.84420 ?  16  LEU A HB2  1 
ATOM   275  H  HB3  . LEU A 1 16  ? 32.75999 24.68945 25.62967 1.000 23.84420 ?  16  LEU A HB3  1 
ATOM   276  H  HG   . LEU A 1 16  ? 31.26978 25.03224 23.30192 1.000 25.45894 ?  16  LEU A HG   1 
ATOM   277  H  HD11 . LEU A 1 16  ? 31.91009 27.24743 23.26198 1.000 26.44983 ?  16  LEU A HD11 1 
ATOM   278  H  HD12 . LEU A 1 16  ? 31.02904 26.94654 24.54913 1.000 26.44983 ?  16  LEU A HD12 1 
ATOM   279  H  HD13 . LEU A 1 16  ? 32.60727 27.07275 24.67864 1.000 26.44983 ?  16  LEU A HD13 1 
ATOM   280  H  HD21 . LEU A 1 16  ? 33.38871 25.64261 22.40129 1.000 28.65681 ?  16  LEU A HD21 1 
ATOM   281  H  HD22 . LEU A 1 16  ? 34.04223 25.16941 23.76968 1.000 28.65681 ?  16  LEU A HD22 1 
ATOM   282  H  HD23 . LEU A 1 16  ? 33.30980 24.11591 22.83309 1.000 28.65681 ?  16  LEU A HD23 1 
ATOM   283  N  N    . MET A 1 17  ? 31.04223 22.24703 27.16166 1.000 18.46336 ?  17  MET A N    1 
ATOM   284  C  CA   . MET A 1 17  ? 31.18437 21.63134 28.48243 1.000 19.47950 ?  17  MET A CA   1 
ATOM   285  C  C    . MET A 1 17  ? 31.36490 20.12352 28.40890 1.000 17.64447 ?  17  MET A C    1 
ATOM   286  O  O    . MET A 1 17  ? 32.05698 19.52106 29.23894 1.000 19.54201 ?  17  MET A O    1 
ATOM   287  C  CB   . MET A 1 17  ? 29.98301 21.96519 29.32942 1.000 22.23307 ?  17  MET A CB   1 
ATOM   288  C  CG   . MET A 1 17  ? 29.96757 23.45388 29.55597 1.000 27.63305 ?  17  MET A CG   1 
ATOM   289  S  SD   . MET A 1 17  ? 28.75910 24.06802 30.66164 1.000 32.31841 ?  17  MET A SD   1 
ATOM   290  C  CE   . MET A 1 17  ? 29.67131 23.54566 32.00958 1.000 31.83077 ?  17  MET A CE   1 
ATOM   291  H  H    . MET A 1 17  ? 30.25278 22.53707 26.98211 1.000 22.16234 ?  17  MET A H    1 
ATOM   292  H  HA   . MET A 1 17  ? 31.97647 22.00761 28.89703 1.000 23.38170 ?  17  MET A HA   1 
ATOM   293  H  HB2  . MET A 1 17  ? 29.16915 21.70323 28.87126 1.000 26.68598 ?  17  MET A HB2  1 
ATOM   294  H  HB3  . MET A 1 17  ? 30.04243 21.51234 30.18516 1.000 26.68598 ?  17  MET A HB3  1 
ATOM   295  H  HG2  . MET A 1 17  ? 30.83273 23.71330 29.90967 1.000 33.16597 ?  17  MET A HG2  1 
ATOM   296  H  HG3  . MET A 1 17  ? 29.81526 23.88663 28.70132 1.000 33.16597 ?  17  MET A HG3  1 
ATOM   297  H  HE1  . MET A 1 17  ? 29.20200 23.79032 32.82247 1.000 38.20322 ?  17  MET A HE1  1 
ATOM   298  H  HE2  . MET A 1 17  ? 29.77655 22.58240 31.96555 1.000 38.20322 ?  17  MET A HE2  1 
ATOM   299  H  HE3  . MET A 1 17  ? 30.54096 23.97476 31.98781 1.000 38.20322 ?  17  MET A HE3  1 
ATOM   300  N  N    . VAL A 1 18  ? 30.74189 19.47080 27.43589 1.000 17.27898 ?  18  VAL A N    1 
ATOM   301  C  CA   . VAL A 1 18  ? 30.98395 18.04384 27.22616 1.000 18.13441 ?  18  VAL A CA   1 
ATOM   302  C  C    . VAL A 1 18  ? 32.43789 17.81340 26.87040 1.000 19.53008 ?  18  VAL A C    1 
ATOM   303  O  O    . VAL A 1 18  ? 33.07794 16.84752 27.32834 1.000 20.69233 ?  18  VAL A O    1 
ATOM   304  C  CB   . VAL A 1 18  ? 30.03684 17.49226 26.15619 1.000 19.14121 ?  18  VAL A CB   1 
ATOM   305  C  CG1  . VAL A 1 18  ? 30.42754 16.06796 25.74332 1.000 19.60821 ?  18  VAL A CG1  1 
ATOM   306  C  CG2  . VAL A 1 18  ? 28.62925 17.57185 26.68838 1.000 19.54811 ?  18  VAL A CG2  1 
ATOM   307  H  H    . VAL A 1 18  ? 30.18042 19.82303 26.88792 1.000 20.74108 ?  18  VAL A H    1 
ATOM   308  H  HA   . VAL A 1 18  ? 30.79795 17.56897 28.05127 1.000 21.76759 ?  18  VAL A HA   1 
ATOM   309  H  HB   . VAL A 1 18  ? 30.09529 18.02114 25.34517 1.000 22.97575 ?  18  VAL A HB   1 
ATOM   310  H  HG11 . VAL A 1 18  ? 29.68818 15.66463 25.26209 1.000 23.53615 ?  18  VAL A HG11 1 
ATOM   311  H  HG12 . VAL A 1 18  ? 31.21092 16.10824 25.17272 1.000 23.53615 ?  18  VAL A HG12 1 
ATOM   312  H  HG13 . VAL A 1 18  ? 30.62487 15.55111 26.54007 1.000 23.53615 ?  18  VAL A HG13 1 
ATOM   313  H  HG21 . VAL A 1 18  ? 28.02415 17.17699 26.04120 1.000 23.46404 ?  18  VAL A HG21 1 
ATOM   314  H  HG22 . VAL A 1 18  ? 28.58050 17.08570 27.52635 1.000 23.46404 ?  18  VAL A HG22 1 
ATOM   315  H  HG23 . VAL A 1 18  ? 28.39817 18.50288 26.83217 1.000 23.46404 ?  18  VAL A HG23 1 
ATOM   316  N  N    . GLU A 1 19  ? 32.95892 18.65731 25.98019 1.000 20.18203 ?  19  GLU A N    1 
ATOM   317  C  CA   . GLU A 1 19  ? 34.31489 18.50117 25.47438 1.000 22.77731 ?  19  GLU A CA   1 
ATOM   318  C  C    . GLU A 1 19  ? 35.35555 18.79026 26.54227 1.000 22.48727 ?  19  GLU A C    1 
ATOM   319  O  O    . GLU A 1 19  ? 36.42816 18.17262 26.55545 1.000 24.45903 ?  19  GLU A O    1 
ATOM   320  C  CB   . GLU A 1 19  ? 34.52403 19.43384 24.27461 1.000 27.33821 ?  19  GLU A CB   1 
ATOM   321  C  CG   . GLU A 1 19  ? 33.84548 18.95866 23.01416 1.000 33.31219 ?  19  GLU A CG   1 
ATOM   322  C  CD   . GLU A 1 19  ? 33.84245 19.95485 21.80095 1.000 38.68666 ?  19  GLU A CD   1 
ATOM   323  O  OE1  . GLU A 1 19  ? 34.14602 21.17757 21.92569 1.000 40.35157 ?  19  GLU A OE1  1 
ATOM   324  O  OE2  . GLU A 1 19  ? 33.50179 19.46361 20.71500 1.000 41.09323 -1 19  GLU A OE2  1 
ATOM   325  H  H    . GLU A 1 19  ? 32.54262 19.33417 25.65132 1.000 24.22474 ?  19  GLU A H    1 
ATOM   326  H  HA   . GLU A 1 19  ? 34.43191 17.58216 25.18693 1.000 27.33908 ?  19  GLU A HA   1 
ATOM   327  H  HB2  . GLU A 1 19  ? 34.16580 20.30847 24.49278 1.000 32.81215 ?  19  GLU A HB2  1 
ATOM   328  H  HB3  . GLU A 1 19  ? 35.47451 19.50054 24.09284 1.000 32.81215 ?  19  GLU A HB3  1 
ATOM   329  H  HG2  . GLU A 1 19  ? 34.29308 18.15105 22.71695 1.000 39.98094 ?  19  GLU A HG2  1 
ATOM   330  H  HG3  . GLU A 1 19  ? 32.91857 18.76577 23.22515 1.000 39.98094 ?  19  GLU A HG3  1 
ATOM   331  N  N    . ASN A 1 20  ? 35.10236 19.77323 27.40120 1.000 21.05078 ?  20  ASN A N    1 
ATOM   332  C  CA   . ASN A 1 20  ? 36.04371 20.14221 28.44668 1.000 22.86475 ?  20  ASN A CA   1 
ATOM   333  C  C    . ASN A 1 20  ? 35.25524 20.39711 29.71094 1.000 22.01450 ?  20  ASN A C    1 
ATOM   334  O  O    . ASN A 1 20  ? 34.93082 21.53188 30.06083 1.000 22.01072 ?  20  ASN A O    1 
ATOM   335  C  CB   . ASN A 1 20  ? 36.83800 21.37671 28.04923 1.000 26.77116 ?  20  ASN A CB   1 
ATOM   336  C  CG   . ASN A 1 20  ? 37.88022 21.06691 27.02814 1.000 31.23114 ?  20  ASN A CG   1 
ATOM   337  O  OD1  . ASN A 1 20  ? 37.77755 21.47915 25.89546 1.000 33.75414 ?  20  ASN A OD1  1 
ATOM   338  N  ND2  . ASN A 1 20  ? 38.89671 20.31020 27.43567 1.000 32.48742 ?  20  ASN A ND2  1 
ATOM   339  H  H    . ASN A 1 20  ? 34.38315 20.24472 27.39615 1.000 25.26723 ?  20  ASN A H    1 
ATOM   340  H  HA   . ASN A 1 20  ? 36.66560 19.41413 28.60178 1.000 27.44400 ?  20  ASN A HA   1 
ATOM   341  H  HB2  . ASN A 1 20  ? 36.23436 22.03748 27.67520 1.000 32.13170 ?  20  ASN A HB2  1 
ATOM   342  H  HB3  . ASN A 1 20  ? 37.28012 21.73757 28.83359 1.000 32.13170 ?  20  ASN A HB3  1 
ATOM   343  H  HD21 . ASN A 1 20  ? 38.92518 20.02955 28.24809 1.000 38.99121 ?  20  ASN A HD21 1 
ATOM   344  H  HD22 . ASN A 1 20  ? 39.52495 20.10196 26.88653 1.000 38.99121 ?  20  ASN A HD22 1 
ATOM   345  N  N    . PRO A 1 21  ? 34.95397 19.35106 30.45450 1.000 22.28196 ?  21  PRO A N    1 
ATOM   346  C  CA   . PRO A 1 21  ? 34.12305 19.50276 31.62375 1.000 23.48679 ?  21  PRO A CA   1 
ATOM   347  C  C    . PRO A 1 21  ? 34.86855 20.24412 32.71485 1.000 24.08425 ?  21  PRO A C    1 
ATOM   348  O  O    . PRO A 1 21  ? 36.01843 19.92140 33.02384 1.000 25.38522 ?  21  PRO A O    1 
ATOM   349  C  CB   . PRO A 1 21  ? 33.83617 18.03930 32.02984 1.000 25.15067 ?  21  PRO A CB   1 
ATOM   350  C  CG   . PRO A 1 21  ? 34.81123 17.29647 31.34697 1.000 26.62381 ?  21  PRO A CG   1 
ATOM   351  C  CD   . PRO A 1 21  ? 35.11927 17.94292 30.09705 1.000 24.04365 ?  21  PRO A CD   1 
ATOM   352  H  HA   . PRO A 1 21  ? 33.29317 19.96155 31.41950 1.000 28.19045 ?  21  PRO A HA   1 
ATOM   353  H  HB2  . PRO A 1 21  ? 33.92590 17.93587 32.99013 1.000 30.18711 ?  21  PRO A HB2  1 
ATOM   354  H  HB3  . PRO A 1 21  ? 32.94276 17.78468 31.75078 1.000 30.18711 ?  21  PRO A HB3  1 
ATOM   355  H  HG2  . PRO A 1 21  ? 35.60805 17.24625 31.89784 1.000 31.95487 ?  21  PRO A HG2  1 
ATOM   356  H  HG3  . PRO A 1 21  ? 34.46568 16.40536 31.18140 1.000 31.95487 ?  21  PRO A HG3  1 
ATOM   357  H  HD2  . PRO A 1 21  ? 36.02866 17.75442 29.81709 1.000 28.85869 ?  21  PRO A HD2  1 
ATOM   358  H  HD3  . PRO A 1 21  ? 34.49670 17.68017 29.40115 1.000 28.85869 ?  21  PRO A HD3  1 
ATOM   359  N  N    . PRO A 1 22  ? 34.24325 21.25652 33.30090 1.000 23.75920 ?  22  PRO A N    1 
ATOM   360  C  CA   . PRO A 1 22  ? 34.89425 22.03420 34.30127 1.000 24.35863 ?  22  PRO A CA   1 
ATOM   361  C  C    . PRO A 1 22  ? 34.99541 21.23904 35.58337 1.000 23.78551 ?  22  PRO A C    1 
ATOM   362  O  O    . PRO A 1 22  ? 34.04036 20.55811 35.97558 1.000 22.52126 ?  22  PRO A O    1 
ATOM   363  C  CB   . PRO A 1 22  ? 33.94447 23.23425 34.45688 1.000 24.58572 ?  22  PRO A CB   1 
ATOM   364  C  CG   . PRO A 1 22  ? 32.69579 22.80187 34.03975 1.000 24.92032 ?  22  PRO A CG   1 
ATOM   365  C  CD   . PRO A 1 22  ? 32.91569 21.79705 32.97880 1.000 24.03841 ?  22  PRO A CD   1 
ATOM   366  H  HA   . PRO A 1 22  ? 35.77252 22.33808 34.02341 1.000 29.23665 ?  22  PRO A HA   1 
ATOM   367  H  HB2  . PRO A 1 22  ? 33.91826 23.50873 35.38686 1.000 29.50917 ?  22  PRO A HB2  1 
ATOM   368  H  HB3  . PRO A 1 22  ? 34.25500 23.96763 33.90314 1.000 29.50917 ?  22  PRO A HB3  1 
ATOM   369  H  HG2  . PRO A 1 22  ? 32.22520 22.40549 34.78964 1.000 29.91068 ?  22  PRO A HG2  1 
ATOM   370  H  HG3  . PRO A 1 22  ? 32.19304 23.55574 33.69359 1.000 29.91068 ?  22  PRO A HG3  1 
ATOM   371  H  HD2  . PRO A 1 22  ? 32.24071 21.10141 33.01603 1.000 28.85239 ?  22  PRO A HD2  1 
ATOM   372  H  HD3  . PRO A 1 22  ? 32.91506 22.21337 32.10268 1.000 28.85239 ?  22  PRO A HD3  1 
ATOM   373  N  N    . PRO A 1 23  ? 36.12217 21.32251 36.27743 1.000 25.17740 ?  23  PRO A N    1 
ATOM   374  C  CA   . PRO A 1 23  ? 36.23052 20.66467 37.56356 1.000 24.32118 ?  23  PRO A CA   1 
ATOM   375  C  C    . PRO A 1 23  ? 35.10750 21.09892 38.49281 1.000 21.97720 ?  23  PRO A C    1 
ATOM   376  O  O    . PRO A 1 23  ? 34.73637 22.27064 38.57490 1.000 22.20905 ?  23  PRO A O    1 
ATOM   377  C  CB   . PRO A 1 23  ? 37.58650 21.16091 38.08160 1.000 26.72162 ?  23  PRO A CB   1 
ATOM   378  C  CG   . PRO A 1 23  ? 38.33470 21.36864 36.88109 1.000 27.63091 ?  23  PRO A CG   1 
ATOM   379  C  CD   . PRO A 1 23  ? 37.41130 21.92388 35.91719 1.000 27.10194 ?  23  PRO A CD   1 
ATOM   380  H  HA   . PRO A 1 23  ? 36.23196 19.69972 37.46474 1.000 29.19172 ?  23  PRO A HA   1 
ATOM   381  H  HB2  . PRO A 1 23  ? 37.47686 21.98704 38.57799 1.000 32.07225 ?  23  PRO A HB2  1 
ATOM   382  H  HB3  . PRO A 1 23  ? 38.00001 20.48794 38.64465 1.000 32.07225 ?  23  PRO A HB3  1 
ATOM   383  H  HG2  . PRO A 1 23  ? 39.06146 21.98742 37.05385 1.000 33.16340 ?  23  PRO A HG2  1 
ATOM   384  H  HG3  . PRO A 1 23  ? 38.68783 20.52143 36.56733 1.000 33.16340 ?  23  PRO A HG3  1 
ATOM   385  H  HD2  . PRO A 1 23  ? 37.37304 22.88992 35.99592 1.000 32.52863 ?  23  PRO A HD2  1 
ATOM   386  H  HD3  . PRO A 1 23  ? 37.66599 21.67437 35.01509 1.000 32.52863 ?  23  PRO A HD3  1 
ATOM   387  N  N    . TYR A 1 24  ? 34.58595 20.14229 39.19735 1.000 18.03550 ?  24  TYR A N    1 
ATOM   388  C  CA   . TYR A 1 24  ? 33.60585 20.26978 40.25977 1.000 16.85808 ?  24  TYR A CA   1 
ATOM   389  C  C    . TYR A 1 24  ? 32.19652 20.54604 39.78883 1.000 16.16403 ?  24  TYR A C    1 
ATOM   390  O  O    . TYR A 1 24  ? 31.32077 20.62281 40.61277 1.000 18.56657 ?  24  TYR A O    1 
ATOM   391  C  CB   . TYR A 1 24  ? 33.95942 21.33579 41.30853 1.000 17.91568 ?  24  TYR A CB   1 
ATOM   392  C  CG   . TYR A 1 24  ? 35.27456 21.07471 41.96184 1.000 19.45494 ?  24  TYR A CG   1 
ATOM   393  C  CD1  . TYR A 1 24  ? 35.41405 20.05357 42.93653 1.000 20.62537 ?  24  TYR A CD1  1 
ATOM   394  C  CD2  . TYR A 1 24  ? 36.36018 21.83553 41.66303 1.000 21.61939 ?  24  TYR A CD2  1 
ATOM   395  C  CE1  . TYR A 1 24  ? 36.59155 19.81008 43.51953 1.000 22.52743 ?  24  TYR A CE1  1 
ATOM   396  C  CE2  . TYR A 1 24  ? 37.56369 21.58289 42.26606 1.000 23.67648 ?  24  TYR A CE2  1 
ATOM   397  C  CZ   . TYR A 1 24  ? 37.66718 20.60412 43.22380 1.000 23.73754 ?  24  TYR A CZ   1 
ATOM   398  O  OH   . TYR A 1 24  ? 38.92916 20.36736 43.73142 1.000 27.04747 ?  24  TYR A OH   1 
ATOM   399  H  H    . TYR A 1 24  ? 34.80052 19.31884 39.07284 1.000 21.64890 ?  24  TYR A H    1 
ATOM   400  H  HA   . TYR A 1 24  ? 33.60391 19.40264 40.69448 1.000 20.23600 ?  24  TYR A HA   1 
ATOM   401  H  HB2  . TYR A 1 24  ? 34.00362 22.20325 40.87673 1.000 21.50512 ?  24  TYR A HB2  1 
ATOM   402  H  HB3  . TYR A 1 24  ? 33.27618 21.34234 41.99704 1.000 21.50512 ?  24  TYR A HB3  1 
ATOM   403  H  HD1  . TYR A 1 24  ? 34.67286 19.54452 43.17403 1.000 24.75675 ?  24  TYR A HD1  1 
ATOM   404  H  HD2  . TYR A 1 24  ? 36.28580 22.52906 41.04791 1.000 25.94957 ?  24  TYR A HD2  1 
ATOM   405  H  HE1  . TYR A 1 24  ? 36.67981 19.10671 44.12150 1.000 27.03922 ?  24  TYR A HE1  1 
ATOM   406  H  HE2  . TYR A 1 24  ? 38.31437 22.07651 42.02581 1.000 28.41808 ?  24  TYR A HE2  1 
ATOM   407  H  HH   . TYR A 1 24  ? 39.46553 20.94987 43.45108 1.000 32.46327 ?  24  TYR A HH   1 
ATOM   408  N  N    . ILE A 1 25  ? 31.95407 20.65647 38.47874 1.000 15.73787 ?  25  ILE A N    1 
ATOM   409  C  CA   . ILE A 1 25  ? 30.67553 21.20275 38.00376 1.000 17.18445 ?  25  ILE A CA   1 
ATOM   410  C  C    . ILE A 1 25  ? 30.13910 20.37112 36.84085 1.000 17.41764 ?  25  ILE A C    1 
ATOM   411  O  O    . ILE A 1 25  ? 30.82880 20.20220 35.84193 1.000 19.12463 ?  25  ILE A O    1 
ATOM   412  C  CB   . ILE A 1 25  ? 30.77234 22.66917 37.57418 1.000 18.70663 ?  25  ILE A CB   1 
ATOM   413  C  CG1  . ILE A 1 25  ? 31.32355 23.53040 38.70656 1.000 18.64473 ?  25  ILE A CG1  1 
ATOM   414  C  CG2  . ILE A 1 25  ? 29.36539 23.13834 37.13727 1.000 22.41550 ?  25  ILE A CG2  1 
ATOM   415  C  CD1  . ILE A 1 25  ? 31.72525 24.91058 38.30964 1.000 22.01737 ?  25  ILE A CD1  1 
ATOM   416  H  H    . ILE A 1 25  ? 32.50287 20.42662 37.85778 1.000 18.89175 ?  25  ILE A H    1 
ATOM   417  H  HA   . ILE A 1 25  ? 30.04701 21.12276 38.73824 1.000 20.62764 ?  25  ILE A HA   1 
ATOM   418  H  HB   . ILE A 1 25  ? 31.38894 22.75684 36.83053 1.000 22.45426 ?  25  ILE A HB   1 
ATOM   419  H  HG12 . ILE A 1 25  ? 30.64093 23.61164 39.39091 1.000 22.37998 ?  25  ILE A HG12 1 
ATOM   420  H  HG13 . ILE A 1 25  ? 32.10853 23.09258 39.07129 1.000 22.37998 ?  25  ILE A HG13 1 
ATOM   421  H  HG21 . ILE A 1 25  ? 29.34521 24.10806 37.12602 1.000 26.90490 ?  25  ILE A HG21 1 
ATOM   422  H  HG22 . ILE A 1 25  ? 29.17878 22.79329 36.25013 1.000 26.90490 ?  25  ILE A HG22 1 
ATOM   423  H  HG23 . ILE A 1 25  ? 28.71006 22.80115 37.76794 1.000 26.90490 ?  25  ILE A HG23 1 
ATOM   424  H  HD11 . ILE A 1 25  ? 32.25476 25.30245 39.02164 1.000 26.42714 ?  25  ILE A HD11 1 
ATOM   425  H  HD12 . ILE A 1 25  ? 32.24912 24.86491 37.49454 1.000 26.42714 ?  25  ILE A HD12 1 
ATOM   426  H  HD13 . ILE A 1 25  ? 30.92707 25.44122 38.16055 1.000 26.42714 ?  25  ILE A HD13 1 
ATOM   427  N  N    . LEU A 1 26  ? 28.92798 19.86112 36.99042 1.000 16.80497 ?  26  LEU A N    1 
ATOM   428  C  CA   . LEU A 1 26  ? 28.16529 19.20938 35.93577 1.000 18.10090 ?  26  LEU A CA   1 
ATOM   429  C  C    . LEU A 1 26  ? 26.99630 20.13906 35.62375 1.000 16.89983 ?  26  LEU A C    1 
ATOM   430  O  O    . LEU A 1 26  ? 26.34933 20.59064 36.53459 1.000 18.76168 ?  26  LEU A O    1 
ATOM   431  C  CB   . LEU A 1 26  ? 27.65498 17.84819 36.47869 1.000 19.36679 ?  26  LEU A CB   1 
ATOM   432  C  CG   . LEU A 1 26  ? 26.77701 16.99702 35.53844 1.000 22.33139 ?  26  LEU A CG   1 
ATOM   433  C  CD1  . LEU A 1 26  ? 27.65099 16.31533 34.55292 1.000 24.45520 ?  26  LEU A CD1  1 
ATOM   434  C  CD2  . LEU A 1 26  ? 26.04679 15.86720 36.25474 1.000 24.23831 ?  26  LEU A CD2  1 
ATOM   435  H  H    . LEU A 1 26  ? 28.50097 19.88087 37.73666 1.000 20.17227 ?  26  LEU A H    1 
ATOM   436  H  HA   . LEU A 1 26  ? 28.67711 19.05216 35.12694 1.000 21.72738 ?  26  LEU A HA   1 
ATOM   437  H  HB2  . LEU A 1 26  ? 28.42901 17.30950 36.70583 1.000 23.24645 ?  26  LEU A HB2  1 
ATOM   438  H  HB3  . LEU A 1 26  ? 27.12808 18.02381 37.27395 1.000 23.24645 ?  26  LEU A HB3  1 
ATOM   439  H  HG   . LEU A 1 26  ? 26.13182 17.60302 35.14172 1.000 26.80397 ?  26  LEU A HG   1 
ATOM   440  H  HD11 . LEU A 1 26  ? 27.09816 15.80713 33.93891 1.000 29.35254 ?  26  LEU A HD11 1 
ATOM   441  H  HD12 . LEU A 1 26  ? 28.15850 16.98318 34.06577 1.000 29.35254 ?  26  LEU A HD12 1 
ATOM   442  H  HD13 . LEU A 1 26  ? 28.25459 15.72024 35.02455 1.000 29.35254 ?  26  LEU A HD13 1 
ATOM   443  H  HD21 . LEU A 1 26  ? 25.54543 15.35224 35.60332 1.000 29.09227 ?  26  LEU A HD21 1 
ATOM   444  H  HD22 . LEU A 1 26  ? 26.69832 15.29915 36.69489 1.000 29.09227 ?  26  LEU A HD22 1 
ATOM   445  H  HD23 . LEU A 1 26  ? 25.44269 16.24788 36.91129 1.000 29.09227 ?  26  LEU A HD23 1 
ATOM   446  N  N    . ALA A 1 27  ? 26.70375 20.40542 34.36726 1.000 15.60450 ?  27  ALA A N    1 
ATOM   447  C  CA   . ALA A 1 27  ? 25.59070 21.27772 34.03693 1.000 16.38652 ?  27  ALA A CA   1 
ATOM   448  C  C    . ALA A 1 27  ? 25.02740 20.94839 32.67268 1.000 15.85552 ?  27  ALA A C    1 
ATOM   449  O  O    . ALA A 1 27  ? 25.76928 20.54556 31.76749 1.000 18.01744 ?  27  ALA A O    1 
ATOM   450  C  CB   . ALA A 1 27  ? 25.96638 22.76071 34.04673 1.000 16.79015 ?  27  ALA A CB   1 
ATOM   451  H  H    . ALA A 1 27  ? 27.13138 20.09583 33.68838 1.000 18.73170 ?  27  ALA A H    1 
ATOM   452  H  HA   . ALA A 1 27  ? 24.90919 21.11278 34.70717 1.000 19.67013 ?  27  ALA A HA   1 
ATOM   453  H  HB1  . ALA A 1 27  ? 25.18388 23.28623 33.81775 1.000 20.15448 ?  27  ALA A HB1  1 
ATOM   454  H  HB2  . ALA A 1 27  ? 26.27880 23.00149 34.93291 1.000 20.15448 ?  27  ALA A HB2  1 
ATOM   455  H  HB3  . ALA A 1 27  ? 26.66909 22.91278 33.39561 1.000 20.15448 ?  27  ALA A HB3  1 
ATOM   456  N  N    . ARG A 1 28  ? 23.72446 21.16524 32.51338 1.000 15.45407 ?  28  ARG A N    1 
ATOM   457  C  CA   . ARG A 1 28  ? 23.09036 20.91649 31.22383 1.000 16.13632 ?  28  ARG A CA   1 
ATOM   458  C  C    . ARG A 1 28  ? 21.75734 21.63185 31.17514 1.000 15.33724 ?  28  ARG A C    1 
ATOM   459  O  O    . ARG A 1 28  ? 21.17975 21.97108 32.21171 1.000 16.00133 ?  28  ARG A O    1 
ATOM   460  C  CB   . ARG A 1 28  ? 22.89718 19.40721 30.97533 1.000 17.62723 ?  28  ARG A CB   1 
ATOM   461  C  CG   . ARG A 1 28  ? 22.05493 18.74288 31.92897 1.000 19.56621 ?  28  ARG A CG   1 
ATOM   462  C  CD   . ARG A 1 28  ? 22.04537 17.30940 31.43173 1.000 22.93412 ?  28  ARG A CD   1 
ATOM   463  N  NE   . ARG A 1 28  ? 21.41456 16.31761 32.24190 1.000 24.30513 ?  28  ARG A NE   1 
ATOM   464  C  CZ   . ARG A 1 28  ? 21.90331 15.27895 32.91502 1.000 21.85590 ?  28  ARG A CZ   1 
ATOM   465  N  NH1  . ARG A 1 28  ? 23.18476 14.97224 32.98069 1.000 23.50471 ?  28  ARG A NH1  1 
ATOM   466  N  NH2  . ARG A 1 28  ? 21.05258 14.47319 33.41594 1.000 21.64391 ?  28  ARG A NH2  1 
ATOM   467  H  H    . ARG A 1 28  ? 23.19564 21.45182 33.12805 1.000 18.55118 ?  28  ARG A H    1 
ATOM   468  H  HA   . ARG A 1 28  ? 23.65219 21.28115 30.52221 1.000 19.36989 ?  28  ARG A HA   1 
ATOM   469  H  HB2  . ARG A 1 28  ? 22.49679 19.28826 30.09987 1.000 21.15898 ?  28  ARG A HB2  1 
ATOM   470  H  HB3  . ARG A 1 28  ? 23.76606 18.97694 31.00400 1.000 21.15898 ?  28  ARG A HB3  1 
ATOM   471  H  HG2  . ARG A 1 28  ? 22.42792 18.79015 32.82314 1.000 23.48575 ?  28  ARG A HG2  1 
ATOM   472  H  HG3  . ARG A 1 28  ? 21.15730 19.11048 31.92408 1.000 23.48575 ?  28  ARG A HG3  1 
ATOM   473  H  HD2  . ARG A 1 28  ? 21.58959 17.29721 30.57557 1.000 27.52725 ?  28  ARG A HD2  1 
ATOM   474  H  HD3  . ARG A 1 28  ? 22.96746 17.02955 31.32072 1.000 27.52725 ?  28  ARG A HD3  1 
ATOM   475  H  HE   . ARG A 1 28  ? 20.56180 16.40802 32.30691 1.000 29.17246 ?  28  ARG A HE   1 
ATOM   476  H  HH11 . ARG A 1 28  ? 23.76465 15.45783 32.57139 1.000 28.21196 ?  28  ARG A HH11 1 
ATOM   477  H  HH12 . ARG A 1 28  ? 23.44020 14.28672 33.43281 1.000 28.21196 ?  28  ARG A HH12 1 
ATOM   478  H  HH21 . ARG A 1 28  ? 20.21111 14.61578 33.31014 1.000 25.97899 ?  28  ARG A HH21 1 
ATOM   479  H  HH22 . ARG A 1 28  ? 21.31993 13.78680 33.85979 1.000 25.97899 ?  28  ARG A HH22 1 
ATOM   480  N  N    . PRO A 1 29  ? 21.23049 21.84827 29.96705 1.000 16.09721 ?  29  PRO A N    1 
ATOM   481  C  CA   . PRO A 1 29  ? 19.89545 22.40320 29.83270 1.000 15.14360 ?  29  PRO A CA   1 
ATOM   482  C  C    . PRO A 1 29  ? 18.81047 21.41939 30.18811 1.000 15.26534 ?  29  PRO A C    1 
ATOM   483  O  O    . PRO A 1 29  ? 18.96201 20.20517 30.01668 1.000 16.40937 ?  29  PRO A O    1 
ATOM   484  C  CB   . PRO A 1 29  ? 19.78819 22.75284 28.34717 1.000 16.88107 ?  29  PRO A CB   1 
ATOM   485  C  CG   . PRO A 1 29  ? 21.10954 22.57952 27.74821 1.000 16.82185 ?  29  PRO A CG   1 
ATOM   486  C  CD   . PRO A 1 29  ? 21.87966 21.64999 28.67117 1.000 16.01058 ?  29  PRO A CD   1 
ATOM   487  H  HA   . PRO A 1 29  ? 19.82603 23.19555 30.38791 1.000 18.17863 ?  29  PRO A HA   1 
ATOM   488  H  HB2  . PRO A 1 29  ? 19.14734 22.15888 27.92597 1.000 20.26359 ?  29  PRO A HB2  1 
ATOM   489  H  HB3  . PRO A 1 29  ? 19.49618 23.67347 28.25726 1.000 20.26359 ?  29  PRO A HB3  1 
ATOM   490  H  HG2  . PRO A 1 29  ? 21.01758 22.18615 26.86634 1.000 20.19252 ?  29  PRO A HG2  1 
ATOM   491  H  HG3  . PRO A 1 29  ? 21.55229 23.44012 27.68307 1.000 20.19252 ?  29  PRO A HG3  1 
ATOM   492  H  HD2  . PRO A 1 29  ? 21.79623 20.72825 28.38076 1.000 19.21900 ?  29  PRO A HD2  1 
ATOM   493  H  HD3  . PRO A 1 29  ? 22.81558 21.90157 28.71188 1.000 19.21900 ?  29  PRO A HD3  1 
ATOM   494  N  N    . ASN A 1 30  ? 17.65774 21.91866 30.58647 1.000 15.50633 ?  30  ASN A N    1 
ATOM   495  C  CA   . ASN A 1 30  ? 16.42931 21.13311 30.60592 1.000 16.20430 ?  30  ASN A CA   1 
ATOM   496  C  C    . ASN A 1 30  ? 16.09359 20.74761 29.19016 1.000 17.46317 ?  30  ASN A C    1 
ATOM   497  O  O    . ASN A 1 30  ? 16.10989 21.61085 28.28832 1.000 17.68399 ?  30  ASN A O    1 
ATOM   498  C  CB   . ASN A 1 30  ? 15.35280 22.05403 31.18900 1.000 17.65739 ?  30  ASN A CB   1 
ATOM   499  C  CG   . ASN A 1 30  ? 14.06069 21.39810 31.42856 1.000 19.13008 ?  30  ASN A CG   1 
ATOM   500  O  OD1  . ASN A 1 30  ? 13.66874 20.50941 30.68264 1.000 20.44965 ?  30  ASN A OD1  1 
ATOM   501  N  ND2  . ASN A 1 30  ? 13.36083 21.84406 32.44120 1.000 20.13693 ?  30  ASN A ND2  1 
ATOM   502  H  H    . ASN A 1 30  ? 17.55082 22.72767 30.85790 1.000 18.61390 ?  30  ASN A H    1 
ATOM   503  H  HA   . ASN A 1 30  ? 16.49525 20.32156 31.13312 1.000 19.45146 ?  30  ASN A HA   1 
ATOM   504  H  HB2  . ASN A 1 30  ? 15.66790 22.40029 32.03854 1.000 21.19517 ?  30  ASN A HB2  1 
ATOM   505  H  HB3  . ASN A 1 30  ? 15.20049 22.78433 30.56903 1.000 21.19517 ?  30  ASN A HB3  1 
ATOM   506  H  HD21 . ASN A 1 30  ? 12.59705 21.49344 32.62369 1.000 24.17062 ?  30  ASN A HD21 1 
ATOM   507  H  HD22 . ASN A 1 30  ? 13.66490 22.48761 32.92388 1.000 24.17062 ?  30  ASN A HD22 1 
ATOM   508  N  N    . GLU A 1 31  ? 15.85321 19.45352 28.97065 1.000 18.91982 ?  31  GLU A N    1 
ATOM   509  C  CA   . GLU A 1 31  ? 15.55461 18.99394 27.61821 1.000 20.58433 ?  31  GLU A CA   1 
ATOM   510  C  C    . GLU A 1 31  ? 14.29992 19.61412 27.07093 1.000 22.23538 ?  31  GLU A C    1 
ATOM   511  O  O    . GLU A 1 31  ? 14.04429 19.47615 25.86372 1.000 25.98802 ?  31  GLU A O    1 
ATOM   512  C  CB   . GLU A 1 31  ? 15.43156 17.48261 27.65650 1.000 22.74449 ?  31  GLU A CB   1 
ATOM   513  C  CG   . GLU A 1 31  ? 16.76412 16.79489 27.91612 1.000 25.40668 ?  31  GLU A CG   1 
ATOM   514  C  CD   . GLU A 1 31  ? 16.59532 15.32090 28.31404 1.000 29.47499 ?  31  GLU A CD   1 
ATOM   515  O  OE1  . GLU A 1 31  ? 15.93251 14.64202 27.50789 1.000 31.94649 ?  31  GLU A OE1  1 
ATOM   516  O  OE2  . GLU A 1 31  ? 17.17357 14.89948 29.37146 1.000 30.49411 -1 31  GLU A OE2  1 
ATOM   517  H  H    . GLU A 1 31  ? 15.85723 18.83918 29.57246 1.000 22.71009 ?  31  GLU A H    1 
ATOM   518  H  HA   . GLU A 1 31  ? 16.27221 19.23801 27.01290 1.000 24.70750 ?  31  GLU A HA   1 
ATOM   519  H  HB2  . GLU A 1 31  ? 14.82017 17.23280 28.36692 1.000 27.29969 ?  31  GLU A HB2  1 
ATOM   520  H  HB3  . GLU A 1 31  ? 15.09303 17.17095 26.80259 1.000 27.29969 ?  31  GLU A HB3  1 
ATOM   521  H  HG2  . GLU A 1 31  ? 17.30161 16.82955 27.10940 1.000 30.49432 ?  31  GLU A HG2  1 
ATOM   522  H  HG3  . GLU A 1 31  ? 17.22142 17.25175 28.63934 1.000 30.49432 ?  31  GLU A HG3  1 
ATOM   523  N  N    . ASP A 1 32  ? 13.45694 20.18936 27.92284 1.000 20.56870 ?  32  ASP A N    1 
ATOM   524  C  CA   . ASP A 1 32  ? 12.24723 20.83492 27.43532 1.000 23.96862 ?  32  ASP A CA   1 
ATOM   525  C  C    . ASP A 1 32  ? 12.35279 22.35267 27.38908 1.000 21.90483 ?  32  ASP A C    1 
ATOM   526  O  O    . ASP A 1 32  ? 11.38559 23.01261 26.97251 1.000 23.20807 ?  32  ASP A O    1 
ATOM   527  C  CB   . ASP A 1 32  ? 11.07341 20.49497 28.33226 1.000 29.72387 ?  32  ASP A CB   1 
ATOM   528  C  CG   . ASP A 1 32  ? 10.72473 19.03893 28.29182 1.000 36.93022 ?  32  ASP A CG   1 
ATOM   529  O  OD1  . ASP A 1 32  ? 10.88208 18.42242 27.22759 1.000 39.26332 ?  32  ASP A OD1  1 
ATOM   530  O  OD2  . ASP A 1 32  ? 10.29531 18.55406 29.33886 1.000 39.90750 -1 32  ASP A OD2  1 
ATOM   531  H  H    . ASP A 1 32  ? 13.56430 20.21725 28.77565 1.000 24.68875 ?  32  ASP A H    1 
ATOM   532  H  HA   . ASP A 1 32  ? 12.08126 20.49967 26.54035 1.000 28.76865 ?  32  ASP A HA   1 
ATOM   533  H  HB2  . ASP A 1 32  ? 11.29635 20.72591 29.24761 1.000 35.67495 ?  32  ASP A HB2  1 
ATOM   534  H  HB3  . ASP A 1 32  ? 10.29669 20.99876 28.04276 1.000 35.67495 ?  32  ASP A HB3  1 
ATOM   535  N  N    . ASN A 1 33  ? 13.46669 22.93493 27.78646 1.000 19.04515 ?  33  ASN A N    1 
ATOM   536  C  CA   . ASN A 1 33  ? 13.59499 24.39488 27.82546 1.000 18.37101 ?  33  ASN A CA   1 
ATOM   537  C  C    . ASN A 1 33  ? 15.07288 24.72862 27.90952 1.000 17.34880 ?  33  ASN A C    1 
ATOM   538  O  O    . ASN A 1 33  ? 15.64339 24.73202 28.99881 1.000 17.67855 ?  33  ASN A O    1 
ATOM   539  C  CB   . ASN A 1 33  ? 12.82131 24.95528 28.99720 1.000 19.28343 ?  33  ASN A CB   1 
ATOM   540  C  CG   . ASN A 1 33  ? 13.00320 26.46234 29.12489 1.000 21.09237 ?  33  ASN A CG   1 
ATOM   541  O  OD1  . ASN A 1 33  ? 13.58973 27.11857 28.22608 1.000 20.80642 ?  33  ASN A OD1  1 
ATOM   542  N  ND2  . ASN A 1 33  ? 12.49589 27.01385 30.22048 1.000 23.27992 ?  33  ASN A ND2  1 
ATOM   543  H  H    . ASN A 1 33  ? 14.17149 22.51340 28.04173 1.000 22.86048 ?  33  ASN A H    1 
ATOM   544  H  HA   . ASN A 1 33  ? 13.25078 24.78048 27.00464 1.000 22.05152 ?  33  ASN A HA   1 
ATOM   545  H  HB2  . ASN A 1 33  ? 11.87675 24.77225 28.87388 1.000 23.14642 ?  33  ASN A HB2  1 
ATOM   546  H  HB3  . ASN A 1 33  ? 13.13550 24.54052 29.81583 1.000 23.14642 ?  33  ASN A HB3  1 
ATOM   547  H  HD21 . ASN A 1 33  ? 12.56764 27.86130 30.34807 1.000 27.94221 ?  33  ASN A HD21 1 
ATOM   548  H  HD22 . ASN A 1 33  ? 12.09544 26.52373 30.80274 1.000 27.94221 ?  33  ASN A HD22 1 
ATOM   549  N  N    . ILE A 1 34  ? 15.65780 25.09394 26.77298 1.000 17.81798 ?  34  ILE A N    1 
ATOM   550  C  CA   . ILE A 1 34  ? 17.08298 25.36524 26.70394 1.000 17.17795 ?  34  ILE A CA   1 
ATOM   551  C  C    . ILE A 1 34  ? 17.51338 26.53408 27.58419 1.000 16.89570 ?  34  ILE A C    1 
ATOM   552  O  O    . ILE A 1 34  ? 18.69756 26.61932 27.92728 1.000 16.33957 ?  34  ILE A O    1 
ATOM   553  C  CB   . ILE A 1 34  ? 17.43335 25.58891 25.21362 1.000 19.04231 ?  34  ILE A CB   1 
ATOM   554  C  CG1  . ILE A 1 34  ? 18.91904 25.66900 24.92824 1.000 22.81195 ?  34  ILE A CG1  1 
ATOM   555  C  CG2  . ILE A 1 34  ? 16.98921 26.90338 24.69998 1.000 19.49186 ?  34  ILE A CG2  1 
ATOM   556  C  CD1  . ILE A 1 34  ? 19.64817 24.61147 25.28165 1.000 23.75208 ?  34  ILE A CD1  1 
ATOM   557  H  H    . ILE A 1 34  ? 15.24662 25.19189 26.02402 1.000 21.38788 ?  34  ILE A H    1 
ATOM   558  H  HA   . ILE A 1 34  ? 17.58034 24.60613 27.04641 1.000 20.61984 ?  34  ILE A HA   1 
ATOM   559  H  HB   . ILE A 1 34  ? 16.99794 24.82379 24.80628 1.000 22.85707 ?  34  ILE A HB   1 
ATOM   560  H  HG12 . ILE A 1 34  ? 19.03654 25.78936 23.97294 1.000 27.38064 ?  34  ILE A HG12 1 
ATOM   561  H  HG13 . ILE A 1 34  ? 19.27697 26.43386 25.40550 1.000 27.38064 ?  34  ILE A HG13 1 
ATOM   562  H  HG21 . ILE A 1 34  ? 17.28888 27.00164 23.78268 1.000 23.39654 ?  34  ILE A HG21 1 
ATOM   563  H  HG22 . ILE A 1 34  ? 16.02092 26.94654 24.73806 1.000 23.39654 ?  34  ILE A HG22 1 
ATOM   564  H  HG23 . ILE A 1 34  ? 17.37342 27.60369 25.25030 1.000 23.39654 ?  34  ILE A HG23 1 
ATOM   565  H  HD11 . ILE A 1 34  ? 20.58216 24.79524 25.09507 1.000 28.50880 ?  34  ILE A HD11 1 
ATOM   566  H  HD12 . ILE A 1 34  ? 19.52649 24.44657 26.22975 1.000 28.50880 ?  34  ILE A HD12 1 
ATOM   567  H  HD13 . ILE A 1 34  ? 19.35439 23.84058 24.77144 1.000 28.50880 ?  34  ILE A HD13 1 
ATOM   568  N  N    . LEU A 1 35  ? 16.57905 27.44712 27.92833 1.000 16.33193 ?  35  LEU A N    1 
ATOM   569  C  CA   . LEU A 1 35  ? 16.91323 28.56315 28.80764 1.000 16.20091 ?  35  LEU A CA   1 
ATOM   570  C  C    . LEU A 1 35  ? 17.06917 28.16625 30.25208 1.000 16.15908 ?  35  LEU A C    1 
ATOM   571  O  O    . LEU A 1 35  ? 17.69776 28.91298 31.01962 1.000 17.49905 ?  35  LEU A O    1 
ATOM   572  C  CB   . LEU A 1 35  ? 15.83275 29.62623 28.73634 1.000 16.54696 ?  35  LEU A CB   1 
ATOM   573  C  CG   . LEU A 1 35  ? 15.70089 30.26492 27.33117 1.000 17.31999 ?  35  LEU A CG   1 
ATOM   574  C  CD1  . LEU A 1 35  ? 14.53053 31.23279 27.36277 1.000 18.03353 ?  35  LEU A CD1  1 
ATOM   575  C  CD2  . LEU A 1 35  ? 16.94461 30.95214 26.83724 1.000 17.49183 ?  35  LEU A CD2  1 
ATOM   576  H  H    . LEU A 1 35  ? 15.76045 27.43420 27.66502 1.000 19.60462 ?  35  LEU A H    1 
ATOM   577  H  HA   . LEU A 1 35  ? 17.75643 28.92691 28.49523 1.000 19.44740 ?  35  LEU A HA   1 
ATOM   578  H  HB2  . LEU A 1 35  ? 14.98028 29.22292 28.96337 1.000 19.86266 ?  35  LEU A HB2  1 
ATOM   579  H  HB3  . LEU A 1 35  ? 16.04456 30.33172 29.36747 1.000 19.86266 ?  35  LEU A HB3  1 
ATOM   580  H  HG   . LEU A 1 35  ? 15.55117 29.55206 26.69061 1.000 20.79030 ?  35  LEU A HG   1 
ATOM   581  H  HD11 . LEU A 1 35  ? 14.43651 31.64328 26.48896 1.000 21.64654 ?  35  LEU A HD11 1 
ATOM   582  H  HD12 . LEU A 1 35  ? 13.72301 30.74462 27.58752 1.000 21.64654 ?  35  LEU A HD12 1 
ATOM   583  H  HD13 . LEU A 1 35  ? 14.70213 31.91410 28.03156 1.000 21.64654 ?  35  LEU A HD13 1 
ATOM   584  H  HD21 . LEU A 1 35  ? 16.74326 31.41084 26.00660 1.000 20.99650 ?  35  LEU A HD21 1 
ATOM   585  H  HD22 . LEU A 1 35  ? 17.23874 31.59116 27.50510 1.000 20.99650 ?  35  LEU A HD22 1 
ATOM   586  H  HD23 . LEU A 1 35  ? 17.63510 30.28721 26.68894 1.000 20.99650 ?  35  LEU A HD23 1 
ATOM   587  N  N    . GLU A 1 36  ? 16.56282 27.02268 30.68203 1.000 15.95796 ?  36  GLU A N    1 
ATOM   588  C  CA   . GLU A 1 36  ? 16.64776 26.60588 32.07980 1.000 16.46757 ?  36  GLU A CA   1 
ATOM   589  C  C    . GLU A 1 36  ? 17.72946 25.55804 32.21612 1.000 15.26794 ?  36  GLU A C    1 
ATOM   590  O  O    . GLU A 1 36  ? 17.54295 24.40401 31.81646 1.000 17.55892 ?  36  GLU A O    1 
ATOM   591  C  CB   . GLU A 1 36  ? 15.32082 26.08972 32.58178 1.000 17.88650 ?  36  GLU A CB   1 
ATOM   592  C  CG   . GLU A 1 36  ? 15.45131 25.62842 34.05985 1.000 19.42860 ?  36  GLU A CG   1 
ATOM   593  C  CD   . GLU A 1 36  ? 14.21616 25.02519 34.57827 1.000 21.84443 ?  36  GLU A CD   1 
ATOM   594  O  OE1  . GLU A 1 36  ? 13.17786 25.67854 34.68927 1.000 26.43393 ?  36  GLU A OE1  1 
ATOM   595  O  OE2  . GLU A 1 36  ? 14.14936 23.74854 34.56670 1.000 20.85200 -1 36  GLU A OE2  1 
ATOM   596  H  H    . GLU A 1 36  ? 16.15675 26.45758 30.17669 1.000 19.15586 ?  36  GLU A H    1 
ATOM   597  H  HA   . GLU A 1 36  ? 16.89661 27.37279 32.61907 1.000 19.76739 ?  36  GLU A HA   1 
ATOM   598  H  HB2  . GLU A 1 36  ? 14.65726 26.79558 32.53323 1.000 21.47010 ?  36  GLU A HB2  1 
ATOM   599  H  HB3  . GLU A 1 36  ? 15.04060 25.33333 32.04302 1.000 21.47010 ?  36  GLU A HB3  1 
ATOM   600  H  HG2  . GLU A 1 36  ? 16.15777 24.96676 34.12325 1.000 23.32063 ?  36  GLU A HG2  1 
ATOM   601  H  HG3  . GLU A 1 36  ? 15.66518 26.39612 34.61284 1.000 23.32063 ?  36  GLU A HG3  1 
ATOM   602  N  N    . TRP A 1 37  ? 18.85088 25.90330 32.78220 1.000 15.04677 ?  37  TRP A N    1 
ATOM   603  C  CA   . TRP A 1 37  ? 19.93272 24.98485 33.05694 1.000 14.71742 ?  37  TRP A CA   1 
ATOM   604  C  C    . TRP A 1 37  ? 19.94700 24.56777 34.50616 1.000 14.88378 ?  37  TRP A C    1 
ATOM   605  O  O    . TRP A 1 37  ? 19.57343 25.30741 35.41527 1.000 15.68571 ?  37  TRP A O    1 
ATOM   606  C  CB   . TRP A 1 37  ? 21.28955 25.55251 32.68948 1.000 14.88190 ?  37  TRP A CB   1 
ATOM   607  C  CG   . TRP A 1 37  ? 21.57793 25.67769 31.24024 1.000 14.85097 ?  37  TRP A CG   1 
ATOM   608  C  CD1  . TRP A 1 37  ? 20.77363 26.23599 30.24191 1.000 15.72672 ?  37  TRP A CD1  1 
ATOM   609  C  CD2  . TRP A 1 37  ? 22.78910 25.26772 30.58393 1.000 14.46166 ?  37  TRP A CD2  1 
ATOM   610  N  NE1  . TRP A 1 37  ? 21.44009 26.17586 29.04296 1.000 16.18493 ?  37  TRP A NE1  1 
ATOM   611  C  CE2  . TRP A 1 37  ? 22.67172 25.60471 29.22033 1.000 14.75757 ?  37  TRP A CE2  1 
ATOM   612  C  CE3  . TRP A 1 37  ? 23.95400 24.62745 31.00714 1.000 15.02271 ?  37  TRP A CE3  1 
ATOM   613  C  CZ2  . TRP A 1 37  ? 23.69354 25.34367 28.30097 1.000 16.34795 ?  37  TRP A CZ2  1 
ATOM   614  C  CZ3  . TRP A 1 37  ? 24.93468 24.32712 30.06794 1.000 15.74276 ?  37  TRP A CZ3  1 
ATOM   615  C  CH2  . TRP A 1 37  ? 24.78492 24.69893 28.72983 1.000 15.88360 ?  37  TRP A CH2  1 
ATOM   616  H  H    . TRP A 1 37  ? 19.02556 26.70716 33.03300 1.000 18.06243 ?  37  TRP A H    1 
ATOM   617  H  HA   . TRP A 1 37  ? 19.78388 24.19767 32.51004 1.000 17.66721 ?  37  TRP A HA   1 
ATOM   618  H  HB2  . TRP A 1 37  ? 21.35892 26.44125 33.07188 1.000 17.86459 ?  37  TRP A HB2  1 
ATOM   619  H  HB3  . TRP A 1 37  ? 21.97114 24.97476 33.06703 1.000 17.86459 ?  37  TRP A HB3  1 
ATOM   620  H  HD1  . TRP A 1 37  ? 19.92362 26.59109 30.36955 1.000 18.87836 ?  37  TRP A HD1  1 
ATOM   621  H  HE1  . TRP A 1 37  ? 21.12964 26.45571 28.29136 1.000 19.42821 ?  37  TRP A HE1  1 
ATOM   622  H  HE3  . TRP A 1 37  ? 24.07279 24.40517 31.90234 1.000 18.03356 ?  37  TRP A HE3  1 
ATOM   623  H  HZ2  . TRP A 1 37  ? 23.61619 25.61160 27.41376 1.000 19.62384 ?  37  TRP A HZ2  1 
ATOM   624  H  HZ3  . TRP A 1 37  ? 25.70089 23.87239 30.33447 1.000 18.89762 ?  37  TRP A HZ3  1 
ATOM   625  H  HH2  . TRP A 1 37  ? 25.45918 24.49370 28.12307 1.000 19.06663 ?  37  TRP A HH2  1 
ATOM   626  N  N    . HIS A 1 38  ? 20.40947 23.32233 34.70164 1.000 14.84007 ?  38  HIS A N    1 
ATOM   627  C  CA   . HIS A 1 38  ? 20.63353 22.73336 36.00158 1.000 14.33333 ?  38  HIS A CA   1 
ATOM   628  C  C    . HIS A 1 38  ? 22.09234 22.38907 36.14024 1.000 13.94638 ?  38  HIS A C    1 
ATOM   629  O  O    . HIS A 1 38  ? 22.69839 21.86918 35.20353 1.000 15.67543 ?  38  HIS A O    1 
ATOM   630  C  CB   . HIS A 1 38  ? 19.76548 21.48580 36.18320 1.000 15.58604 ?  38  HIS A CB   1 
ATOM   631  C  CG   . HIS A 1 38  ? 18.30901 21.80945 36.24497 1.000 15.82007 ?  38  HIS A CG   1 
ATOM   632  N  ND1  . HIS A 1 38  ? 17.56787 21.72237 37.42269 1.000 15.06576 ?  38  HIS A ND1  1 
ATOM   633  C  CD2  . HIS A 1 38  ? 17.48466 22.27553 35.27539 1.000 15.91122 ?  38  HIS A CD2  1 
ATOM   634  C  CE1  . HIS A 1 38  ? 16.33718 22.17153 37.14325 1.000 16.19506 ?  38  HIS A CE1  1 
ATOM   635  N  NE2  . HIS A 1 38  ? 16.26341 22.49262 35.85028 1.000 16.24854 ?  38  HIS A NE2  1 
ATOM   636  H  H    . HIS A 1 38  ? 20.60519 22.78659 34.05799 1.000 17.81438 ?  38  HIS A H    1 
ATOM   637  H  HA   . HIS A 1 38  ? 20.40530 23.36163 36.70449 1.000 17.20630 ?  38  HIS A HA   1 
ATOM   638  H  HB2  . HIS A 1 38  ? 19.91002 20.88714 35.43379 1.000 18.70955 ?  38  HIS A HB2  1 
ATOM   639  H  HB3  . HIS A 1 38  ? 20.01219 21.04577 37.01170 1.000 18.70955 ?  38  HIS A HB3  1 
ATOM   640  H  HD2  . HIS A 1 38  ? 17.70825 22.42072 34.38442 1.000 19.09977 ?  38  HIS A HD2  1 
ATOM   641  H  HE1  . HIS A 1 38  ? 15.64161 22.24778 37.75584 1.000 19.44037 ?  38  HIS A HE1  1 
ATOM   642  H  HE2  . HIS A 1 38  ? 15.56395 22.78716 35.44580 1.000 19.50455 ?  38  HIS A HE2  1 
ATOM   643  N  N    . TYR A 1 39  ? 22.64030 22.63261 37.33388 1.000 14.38541 ?  39  TYR A N    1 
ATOM   644  C  CA   . TYR A 1 39  ? 24.02548 22.27328 37.62377 1.000 13.91917 ?  39  TYR A CA   1 
ATOM   645  C  C    . TYR A 1 39  ? 24.07949 21.45858 38.91100 1.000 13.89100 ?  39  TYR A C    1 
ATOM   646  O  O    . TYR A 1 39  ? 23.16757 21.54478 39.75734 1.000 14.05547 ?  39  TYR A O    1 
ATOM   647  C  CB   . TYR A 1 39  ? 24.91512 23.54491 37.73367 1.000 14.00385 ?  39  TYR A CB   1 
ATOM   648  C  CG   . TYR A 1 39  ? 24.58379 24.45827 38.87899 1.000 13.43638 ?  39  TYR A CG   1 
ATOM   649  C  CD1  . TYR A 1 39  ? 25.00161 24.12697 40.15844 1.000 13.97352 ?  39  TYR A CD1  1 
ATOM   650  C  CD2  . TYR A 1 39  ? 23.83332 25.62401 38.73838 1.000 13.96575 ?  39  TYR A CD2  1 
ATOM   651  C  CE1  . TYR A 1 39  ? 24.66371 24.91781 41.29158 1.000 13.95501 ?  39  TYR A CE1  1 
ATOM   652  C  CE2  . TYR A 1 39  ? 23.48865 26.40137 39.84859 1.000 13.97958 ?  39  TYR A CE2  1 
ATOM   653  C  CZ   . TYR A 1 39  ? 23.91457 26.03346 41.07921 1.000 13.93275 ?  39  TYR A CZ   1 
ATOM   654  O  OH   . TYR A 1 39  ? 23.54288 26.76937 42.16371 1.000 14.76642 ?  39  TYR A OH   1 
ATOM   655  H  H    . TYR A 1 39  ? 22.22738 23.00511 37.98989 1.000 17.26879 ?  39  TYR A H    1 
ATOM   656  H  HA   . TYR A 1 39  ? 24.38317 21.71681 36.91434 1.000 16.70931 ?  39  TYR A HA   1 
ATOM   657  H  HB2  . TYR A 1 39  ? 25.83745 23.26519 37.84304 1.000 16.81093 ?  39  TYR A HB2  1 
ATOM   658  H  HB3  . TYR A 1 39  ? 24.81876 24.05797 36.91612 1.000 16.81093 ?  39  TYR A HB3  1 
ATOM   659  H  HD1  . TYR A 1 39  ? 25.51903 23.36380 40.27987 1.000 16.77453 ?  39  TYR A HD1  1 
ATOM   660  H  HD2  . TYR A 1 39  ? 23.55677 25.88976 37.89115 1.000 16.76520 ?  39  TYR A HD2  1 
ATOM   661  H  HE1  . TYR A 1 39  ? 24.94450 24.68096 42.14596 1.000 16.75231 ?  39  TYR A HE1  1 
ATOM   662  H  HE2  . TYR A 1 39  ? 22.97020 27.16605 39.74188 1.000 16.78180 ?  39  TYR A HE2  1 
ATOM   663  H  HH   . TYR A 1 39  ? 23.08016 27.42670 41.91996 1.000 17.72601 ?  39  TYR A HH   1 
ATOM   664  N  N    . ILE A 1 40  ? 25.19499 20.73028 39.04134 1.000 14.12143 ?  40  ILE A N    1 
ATOM   665  C  CA   . ILE A 1 40  ? 25.56070 20.08882 40.27924 1.000 14.37200 ?  40  ILE A CA   1 
ATOM   666  C  C    . ILE A 1 40  ? 26.99394 20.49960 40.57637 1.000 14.94443 ?  40  ILE A C    1 
ATOM   667  O  O    . ILE A 1 40  ? 27.88489 20.22721 39.75637 1.000 15.89377 ?  40  ILE A O    1 
ATOM   668  C  CB   . ILE A 1 40  ? 25.46340 18.55588 40.24144 1.000 14.61536 ?  40  ILE A CB   1 
ATOM   669  C  CG1  . ILE A 1 40  ? 24.07855 18.05767 39.84496 1.000 15.62414 ?  40  ILE A CG1  1 
ATOM   670  C  CG2  . ILE A 1 40  ? 25.89798 18.01504 41.60521 1.000 15.62737 ?  40  ILE A CG2  1 
ATOM   671  C  CD1  . ILE A 1 40  ? 23.95928 16.58379 39.64630 1.000 16.08043 ?  40  ILE A CD1  1 
ATOM   672  H  H    . ILE A 1 40  ? 25.75846 20.59897 38.40506 1.000 16.95202 ?  40  ILE A H    1 
ATOM   673  H  HA   . ILE A 1 40  ? 24.96204 20.39997 40.97615 1.000 17.25270 ?  40  ILE A HA   1 
ATOM   674  H  HB   . ILE A 1 40  ? 26.05540 18.22399 39.54841 1.000 17.54473 ?  40  ILE A HB   1 
ATOM   675  H  HG12 . ILE A 1 40  ? 23.45319 18.30634 40.54352 1.000 18.75527 ?  40  ILE A HG12 1 
ATOM   676  H  HG13 . ILE A 1 40  ? 23.82893 18.48270 39.00953 1.000 18.75527 ?  40  ILE A HG13 1 
ATOM   677  H  HG21 . ILE A 1 40  ? 25.63857 17.08279 41.67249 1.000 18.75914 ?  40  ILE A HG21 1 
ATOM   678  H  HG22 . ILE A 1 40  ? 26.86121 18.09695 41.68507 1.000 18.75914 ?  40  ILE A HG22 1 
ATOM   679  H  HG23 . ILE A 1 40  ? 25.46323 18.53050 42.30249 1.000 18.75914 ?  40  ILE A HG23 1 
ATOM   680  H  HD11 . ILE A 1 40  ? 23.11594 16.39153 39.20730 1.000 19.30281 ?  40  ILE A HD11 1 
ATOM   681  H  HD12 . ILE A 1 40  ? 24.69647 16.27882 39.09454 1.000 19.30281 ?  40  ILE A HD12 1 
ATOM   682  H  HD13 . ILE A 1 40  ? 23.98967 16.14511 40.51090 1.000 19.30281 ?  40  ILE A HD13 1 
ATOM   683  N  N    . ILE A 1 41  ? 27.21481 21.17400 41.71774 1.000 15.06192 ?  41  ILE A N    1 
ATOM   684  C  CA   . ILE A 1 41  ? 28.55167 21.44574 42.22784 1.000 15.16531 ?  41  ILE A CA   1 
ATOM   685  C  C    . ILE A 1 41  ? 28.92927 20.36792 43.22901 1.000 14.44848 ?  41  ILE A C    1 
ATOM   686  O  O    . ILE A 1 41  ? 28.15288 20.04301 44.12336 1.000 15.35541 ?  41  ILE A O    1 
ATOM   687  C  CB   . ILE A 1 41  ? 28.60573 22.84874 42.89541 1.000 16.47556 ?  41  ILE A CB   1 
ATOM   688  C  CG1  . ILE A 1 41  ? 28.66173 23.93104 41.84758 1.000 17.05274 ?  41  ILE A CG1  1 
ATOM   689  C  CG2  . ILE A 1 41  ? 29.79827 22.94471 43.90888 1.000 16.91717 ?  41  ILE A CG2  1 
ATOM   690  C  CD1  . ILE A 1 41  ? 28.43267 25.37681 42.41005 1.000 17.88822 ?  41  ILE A CD1  1 
ATOM   691  H  H    . ILE A 1 41  ? 26.58855 21.48658 42.21744 1.000 18.08060 ?  41  ILE A H    1 
ATOM   692  H  HA   . ILE A 1 41  ? 29.18421 21.41813 41.49297 1.000 18.20467 ?  41  ILE A HA   1 
ATOM   693  H  HB   . ILE A 1 41  ? 27.78994 22.97798 43.40403 1.000 19.77698 ?  41  ILE A HB   1 
ATOM   694  H  HG12 . ILE A 1 41  ? 29.53627 23.91284 41.42835 1.000 20.46959 ?  41  ILE A HG12 1 
ATOM   695  H  HG13 . ILE A 1 41  ? 27.97318 23.75937 41.18627 1.000 20.46959 ?  41  ILE A HG13 1 
ATOM   696  H  HG21 . ILE A 1 41  ? 29.95552 23.87737 44.12411 1.000 20.30691 ?  41  ILE A HG21 1 
ATOM   697  H  HG22 . ILE A 1 41  ? 29.56927 22.45364 44.71343 1.000 20.30691 ?  41  ILE A HG22 1 
ATOM   698  H  HG23 . ILE A 1 41  ? 30.59059 22.56112 43.50147 1.000 20.30691 ?  41  ILE A HG23 1 
ATOM   699  H  HD11 . ILE A 1 41  ? 28.35712 25.99628 41.66745 1.000 21.47217 ?  41  ILE A HD11 1 
ATOM   700  H  HD12 . ILE A 1 41  ? 27.61590 25.38640 42.93321 1.000 21.47217 ?  41  ILE A HD12 1 
ATOM   701  H  HD13 . ILE A 1 41  ? 29.18659 25.62122 42.96930 1.000 21.47217 ?  41  ILE A HD13 1 
ATOM   702  N  N    . THR A 1 42  ? 30.10793 19.81535 43.04817 1.000 15.22893 ?  42  THR A N    1 
ATOM   703  C  CA   . THR A 1 42  ? 30.70696 18.91878 44.03789 1.000 15.62205 ?  42  THR A CA   1 
ATOM   704  C  C    . THR A 1 42  ? 31.57065 19.79231 44.96381 1.000 14.79750 ?  42  THR A C    1 
ATOM   705  O  O    . THR A 1 42  ? 32.39078 20.57457 44.48588 1.000 15.79440 ?  42  THR A O    1 
ATOM   706  C  CB   . THR A 1 42  ? 31.57684 17.86144 43.33845 1.000 17.85944 ?  42  THR A CB   1 
ATOM   707  O  OG1  . THR A 1 42  ? 30.75754 17.04615 42.50503 1.000 18.82084 ?  42  THR A OG1  1 
ATOM   708  C  CG2  . THR A 1 42  ? 32.34591 16.97293 44.31704 1.000 18.21229 ?  42  THR A CG2  1 
ATOM   709  H  H    . THR A 1 42  ? 30.59688 19.93987 42.35174 1.000 18.28102 ?  42  THR A H    1 
ATOM   710  H  HA   . THR A 1 42  ? 30.03102 18.44979 44.55176 1.000 18.75276 ?  42  THR A HA   1 
ATOM   711  H  HB   . THR A 1 42  ? 32.24150 18.32853 42.80840 1.000 21.43763 ?  42  THR A HB   1 
ATOM   712  H  HG1  . THR A 1 42  ? 30.39160 17.51672 41.91321 1.000 22.59131 ?  42  THR A HG1  1 
ATOM   713  H  HG21 . THR A 1 42  ? 32.78937 16.25649 43.83646 1.000 21.86104 ?  42  THR A HG21 1 
ATOM   714  H  HG22 . THR A 1 42  ? 33.01330 17.49708 44.78688 1.000 21.86104 ?  42  THR A HG22 1 
ATOM   715  H  HG23 . THR A 1 42  ? 31.73559 16.58694 44.96467 1.000 21.86104 ?  42  THR A HG23 1 
ATOM   716  N  N    . GLY A 1 43  ? 31.31563 19.72311 46.26634 1.000 15.35767 ?  43  GLY A N    1 
ATOM   717  C  CA   . GLY A 1 43  ? 32.02637 20.54431 47.19653 1.000 16.30560 ?  43  GLY A CA   1 
ATOM   718  C  C    . GLY A 1 43  ? 33.51243 20.26356 47.11913 1.000 15.67265 ?  43  GLY A C    1 
ATOM   719  O  O    . GLY A 1 43  ? 33.92544 19.10425 47.26201 1.000 16.63178 ?  43  GLY A O    1 
ATOM   720  H  H    . GLY A 1 43  ? 30.73136 19.20253 46.62300 1.000 18.43551 ?  43  GLY A H    1 
ATOM   721  H  HA2  . GLY A 1 43  ? 31.87243 21.48025 46.99352 1.000 19.57302 ?  43  GLY A HA2  1 
ATOM   722  H  HA3  . GLY A 1 43  ? 31.71871 20.36199 48.09820 1.000 19.57302 ?  43  GLY A HA3  1 
ATOM   723  N  N    . PRO A 1 44  ? 34.37068 21.27877 46.97772 1.000 16.38529 ?  44  PRO A N    1 
ATOM   724  C  CA   . PRO A 1 44  ? 35.81112 21.02793 46.98178 1.000 15.93660 ?  44  PRO A CA   1 
ATOM   725  C  C    . PRO A 1 44  ? 36.27786 20.49367 48.32733 1.000 15.29006 ?  44  PRO A C    1 
ATOM   726  O  O    . PRO A 1 44  ? 35.76042 20.82294 49.38504 1.000 15.63714 ?  44  PRO A O    1 
ATOM   727  C  CB   . PRO A 1 44  ? 36.41023 22.37820 46.57732 1.000 16.38269 ?  44  PRO A CB   1 
ATOM   728  C  CG   . PRO A 1 44  ? 35.32602 23.02314 45.78628 1.000 16.88094 ?  44  PRO A CG   1 
ATOM   729  C  CD   . PRO A 1 44  ? 34.06220 22.65066 46.51223 1.000 17.40721 ?  44  PRO A CD   1 
ATOM   730  H  HA   . PRO A 1 44  ? 36.07239 20.38379 46.30524 1.000 19.13022 ?  44  PRO A HA   1 
ATOM   731  H  HB2  . PRO A 1 44  ? 36.62708 22.89870 47.36660 1.000 19.66553 ?  44  PRO A HB2  1 
ATOM   732  H  HB3  . PRO A 1 44  ? 37.20614 22.24419 46.03930 1.000 19.66553 ?  44  PRO A HB3  1 
ATOM   733  H  HG2  . PRO A 1 44  ? 35.45029 23.98506 45.77303 1.000 20.26343 ?  44  PRO A HG2  1 
ATOM   734  H  HG3  . PRO A 1 44  ? 35.32319 22.67648 44.88034 1.000 20.26343 ?  44  PRO A HG3  1 
ATOM   735  H  HD2  . PRO A 1 44  ? 33.89908 23.24627 47.26025 1.000 20.89495 ?  44  PRO A HD2  1 
ATOM   736  H  HD3  . PRO A 1 44  ? 33.29958 22.65429 45.91282 1.000 20.89495 ?  44  PRO A HD3  1 
ATOM   737  N  N    . ALA A 1 45  ? 37.34643 19.72346 48.29662 1.000 15.17668 ?  45  ALA A N    1 
ATOM   738  C  CA   . ALA A 1 45  ? 37.75914 18.96106 49.47068 1.000 16.04676 ?  45  ALA A CA   1 
ATOM   739  C  C    . ALA A 1 45  ? 38.26946 19.83544 50.59588 1.000 15.53914 ?  45  ALA A C    1 
ATOM   740  O  O    . ALA A 1 45  ? 38.06138 19.48091 51.75587 1.000 16.27479 ?  45  ALA A O    1 
ATOM   741  C  CB   . ALA A 1 45  ? 38.82378 17.91831 49.13706 1.000 17.39529 ?  45  ALA A CB   1 
ATOM   742  H  H    . ALA A 1 45  ? 37.85547 19.61949 47.61129 1.000 18.21832 ?  45  ALA A H    1 
ATOM   743  H  HA   . ALA A 1 45  ? 36.96059 18.49929 49.77067 1.000 19.26242 ?  45  ALA A HA   1 
ATOM   744  H  HB1  . ALA A 1 45  ? 39.06865 17.44628 49.94831 1.000 20.88065 ?  45  ALA A HB1  1 
ATOM   745  H  HB2  . ALA A 1 45  ? 38.46255 17.29474 48.48776 1.000 20.88065 ?  45  ALA A HB2  1 
ATOM   746  H  HB3  . ALA A 1 45  ? 39.60061 18.36699 48.76813 1.000 20.88065 ?  45  ALA A HB3  1 
ATOM   747  N  N    . ASP A 1 46  ? 38.98126 20.92876 50.32294 1.000 14.80916 ?  46  ASP A N    1 
ATOM   748  C  CA   . ASP A 1 46  ? 39.56002 21.75133 51.36933 1.000 14.80525 ?  46  ASP A CA   1 
ATOM   749  C  C    . ASP A 1 46  ? 38.63838 22.88500 51.77454 1.000 14.47879 ?  46  ASP A C    1 
ATOM   750  O  O    . ASP A 1 46  ? 39.06686 24.03104 51.93120 1.000 15.64405 ?  46  ASP A O    1 
ATOM   751  C  CB   . ASP A 1 46  ? 40.92309 22.28075 50.96258 1.000 14.76028 ?  46  ASP A CB   1 
ATOM   752  C  CG   . ASP A 1 46  ? 41.82453 22.54734 52.14306 1.000 14.38412 ?  46  ASP A CG   1 
ATOM   753  O  OD1  . ASP A 1 46  ? 41.59123 22.04996 53.27286 1.000 15.16411 ?  46  ASP A OD1  1 
ATOM   754  O  OD2  . ASP A 1 46  ? 42.89009 23.22873 51.91135 1.000 12.95487 -1 46  ASP A OD2  1 
ATOM   755  H  H    . ASP A 1 46  ? 39.14175 21.21371 49.52754 1.000 17.77729 ?  46  ASP A H    1 
ATOM   756  H  HA   . ASP A 1 46  ? 39.69373 21.18123 52.14265 1.000 17.77261 ?  46  ASP A HA   1 
ATOM   757  H  HB2  . ASP A 1 46  ? 41.35918 21.62658 50.39444 1.000 17.71864 ?  46  ASP A HB2  1 
ATOM   758  H  HB3  . ASP A 1 46  ? 40.80695 23.11423 50.48017 1.000 17.71864 ?  46  ASP A HB3  1 
ATOM   759  N  N    . THR A 1 47  ? 37.37393 22.54619 51.98877 1.000 14.82293 ?  47  THR A N    1 
ATOM   760  C  CA   . THR A 1 47  ? 36.29767 23.45422 52.34457 1.000 15.09195 ?  47  THR A CA   1 
ATOM   761  C  C    . THR A 1 47  ? 35.34895 22.69827 53.26693 1.000 14.99773 ?  47  THR A C    1 
ATOM   762  O  O    . THR A 1 47  ? 35.31903 21.45359 53.24890 1.000 15.38375 ?  47  THR A O    1 
ATOM   763  C  CB   . THR A 1 47  ? 35.50428 23.96472 51.12035 1.000 15.32882 ?  47  THR A CB   1 
ATOM   764  O  OG1  . THR A 1 47  ? 34.60350 22.97698 50.65380 1.000 15.55288 ?  47  THR A OG1  1 
ATOM   765  C  CG2  . THR A 1 47  ? 36.39448 24.47053 49.96695 1.000 16.33032 ?  47  THR A CG2  1 
ATOM   766  H  H    . THR A 1 47  ? 37.09472 21.73495 51.92932 1.000 17.79382 ?  47  THR A H    1 
ATOM   767  H  HA   . THR A 1 47  ? 36.68127 24.22086 52.79845 1.000 18.11665 ?  47  THR A HA   1 
ATOM   768  H  HB   . THR A 1 47  ? 34.99925 24.73717 51.41895 1.000 18.40089 ?  47  THR A HB   1 
ATOM   769  H  HG1  . THR A 1 47  ? 35.02529 22.28521 50.43210 1.000 18.66976 ?  47  THR A HG1  1 
ATOM   770  H  HG21 . THR A 1 47  ? 35.84167 24.79996 49.24115 1.000 19.60269 ?  47  THR A HG21 1 
ATOM   771  H  HG22 . THR A 1 47  ? 36.96533 25.18985 50.27936 1.000 19.60269 ?  47  THR A HG22 1 
ATOM   772  H  HG23 . THR A 1 47  ? 36.95089 23.74819 49.63600 1.000 19.60269 ?  47  THR A HG23 1 
ATOM   773  N  N    . PRO A 1 48  ? 34.43505 23.41422 53.92824 1.000 15.59518 ?  48  PRO A N    1 
ATOM   774  C  CA   . PRO A 1 48  ? 33.41833 22.71843 54.72459 1.000 16.59678 ?  48  PRO A CA   1 
ATOM   775  C  C    . PRO A 1 48  ? 32.37927 22.03787 53.86404 1.000 15.30456 ?  48  PRO A C    1 
ATOM   776  O  O    . PRO A 1 48  ? 31.54550 21.28063 54.39496 1.000 16.46985 ?  48  PRO A O    1 
ATOM   777  C  CB   . PRO A 1 48  ? 32.78421 23.81352 55.58361 1.000 18.42963 ?  48  PRO A CB   1 
ATOM   778  C  CG   . PRO A 1 48  ? 33.03339 25.07241 54.87843 1.000 19.15386 ?  48  PRO A CG   1 
ATOM   779  C  CD   . PRO A 1 48  ? 34.39489 24.87059 54.16787 1.000 16.70916 ?  48  PRO A CD   1 
ATOM   780  H  HA   . PRO A 1 48  ? 33.84092 22.07973 55.31988 1.000 19.92243 ?  48  PRO A HA   1 
ATOM   781  H  HB2  . PRO A 1 48  ? 31.83190 23.65039 55.66961 1.000 22.12185 ?  48  PRO A HB2  1 
ATOM   782  H  HB3  . PRO A 1 48  ? 33.19975 23.82241 56.46005 1.000 22.12185 ?  48  PRO A HB3  1 
ATOM   783  H  HG2  . PRO A 1 48  ? 32.32694 25.23602 54.23418 1.000 22.99094 ?  48  PRO A HG2  1 
ATOM   784  H  HG3  . PRO A 1 48  ? 33.07894 25.80395 55.51377 1.000 22.99094 ?  48  PRO A HG3  1 
ATOM   785  H  HD2  . PRO A 1 48  ? 34.42409 25.35982 53.33079 1.000 20.05730 ?  48  PRO A HD2  1 
ATOM   786  H  HD3  . PRO A 1 48  ? 35.12789 25.14742 54.73968 1.000 20.05730 ?  48  PRO A HD3  1 
ATOM   787  N  N    . TYR A 1 49  ? 32.41444 22.28362 52.56615 1.000 15.14418 ?  49  TYR A N    1 
ATOM   788  C  CA   . TYR A 1 49  ? 31.52533 21.65595 51.62089 1.000 14.20819 ?  49  TYR A CA   1 
ATOM   789  C  C    . TYR A 1 49  ? 32.02904 20.30516 51.13009 1.000 14.49002 ?  49  TYR A C    1 
ATOM   790  O  O    . TYR A 1 49  ? 31.36982 19.68739 50.26852 1.000 14.79925 ?  49  TYR A O    1 
ATOM   791  C  CB   . TYR A 1 49  ? 31.26185 22.61960 50.41520 1.000 14.26999 ?  49  TYR A CB   1 
ATOM   792  C  CG   . TYR A 1 49  ? 30.98774 24.00597 50.85234 1.000 14.54081 ?  49  TYR A CG   1 
ATOM   793  C  CD1  . TYR A 1 49  ? 29.80866 24.29585 51.50484 1.000 14.96424 ?  49  TYR A CD1  1 
ATOM   794  C  CD2  . TYR A 1 49  ? 31.90811 25.02695 50.72027 1.000 14.82957 ?  49  TYR A CD2  1 
ATOM   795  C  CE1  . TYR A 1 49  ? 29.53693 25.55571 51.97412 1.000 15.22698 ?  49  TYR A CE1  1 
ATOM   796  C  CE2  . TYR A 1 49  ? 31.66157 26.33590 51.20767 1.000 15.07069 ?  49  TYR A CE2  1 
ATOM   797  C  CZ   . TYR A 1 49  ? 30.48527 26.55912 51.86026 1.000 15.21624 ?  49  TYR A CZ   1 
ATOM   798  O  OH   . TYR A 1 49  ? 30.20731 27.79524 52.37787 1.000 16.21111 ?  49  TYR A OH   1 
ATOM   799  H  H    . TYR A 1 49  ? 32.96681 22.83139 52.19951 1.000 18.17932 ?  49  TYR A H    1 
ATOM   800  H  HA   . TYR A 1 49  ? 30.67164 21.49492 52.05238 1.000 17.05613 ?  49  TYR A HA   1 
ATOM   801  H  HB2  . TYR A 1 49  ? 32.04469 22.63269 49.84259 1.000 17.13029 ?  49  TYR A HB2  1 
ATOM   802  H  HB3  . TYR A 1 49  ? 30.49213 22.30206 49.91762 1.000 17.13029 ?  49  TYR A HB3  1 
ATOM   803  H  HD1  . TYR A 1 49  ? 29.18178 23.62038 51.63000 1.000 17.96339 ?  49  TYR A HD1  1 
ATOM   804  H  HD2  . TYR A 1 49  ? 32.71727 24.85023 50.29727 1.000 17.80178 ?  49  TYR A HD2  1 
ATOM   805  H  HE1  . TYR A 1 49  ? 28.71477 25.73661 52.36937 1.000 18.27868 ?  49  TYR A HE1  1 
ATOM   806  H  HE2  . TYR A 1 49  ? 32.28115 27.01875 51.08631 1.000 18.09113 ?  49  TYR A HE2  1 
ATOM   807  H  HH   . TYR A 1 49  ? 30.85912 28.31090 52.25608 1.000 19.45963 ?  49  TYR A HH   1 
ATOM   808  N  N    . LYS A 1 50  ? 33.15666 19.81784 51.59481 1.000 14.84780 ?  50  LYS A N    1 
ATOM   809  C  CA   . LYS A 1 50  ? 33.69116 18.54770 51.14642 1.000 15.54485 ?  50  LYS A CA   1 
ATOM   810  C  C    . LYS A 1 50  ? 32.63617 17.44166 51.21286 1.000 16.96491 ?  50  LYS A C    1 
ATOM   811  O  O    . LYS A 1 50  ? 31.92659 17.29191 52.22562 1.000 17.74518 ?  50  LYS A O    1 
ATOM   812  C  CB   . LYS A 1 50  ? 34.86658 18.15220 52.04743 1.000 15.67451 ?  50  LYS A CB   1 
ATOM   813  C  CG   . LYS A 1 50  ? 35.45492 16.76454 51.70643 1.000 16.74846 ?  50  LYS A CG   1 
ATOM   814  C  CD   . LYS A 1 50  ? 36.63542 16.41419 52.59374 1.000 18.24300 ?  50  LYS A CD   1 
ATOM   815  C  CE   . LYS A 1 50  ? 37.20195 15.06505 52.35928 1.000 20.65242 ?  50  LYS A CE   1 
ATOM   816  N  NZ   . LYS A 1 50  ? 36.27294 13.82389 52.61580 1.000 22.61281 ?  50  LYS A NZ   1 
ATOM   817  H  H    . LYS A 1 50  ? 33.64584 20.20897 52.18415 1.000 17.82366 ?  50  LYS A H    1 
ATOM   818  H  HA   . LYS A 1 50  ? 33.98577 18.63811 50.22667 1.000 18.66013 ?  50  LYS A HA   1 
ATOM   819  H  HB2  . LYS A 1 50  ? 35.57348 18.80888 51.94762 1.000 18.81571 ?  50  LYS A HB2  1 
ATOM   820  H  HB3  . LYS A 1 50  ? 34.56251 18.12943 52.96826 1.000 18.81571 ?  50  LYS A HB3  1 
ATOM   821  H  HG2  . LYS A 1 50  ? 34.77098 16.08813 51.83135 1.000 20.10445 ?  50  LYS A HG2  1 
ATOM   822  H  HG3  . LYS A 1 50  ? 35.75796 16.76372 50.78499 1.000 20.10445 ?  50  LYS A HG3  1 
ATOM   823  H  HD2  . LYS A 1 50  ? 37.34279 17.05916 52.43708 1.000 21.89790 ?  50  LYS A HD2  1 
ATOM   824  H  HD3  . LYS A 1 50  ? 36.34938 16.45387 53.51975 1.000 21.89790 ?  50  LYS A HD3  1 
ATOM   825  H  HE2  . LYS A 1 50  ? 37.47935 15.01714 51.43103 1.000 24.78921 ?  50  LYS A HE2  1 
ATOM   826  H  HE3  . LYS A 1 50  ? 37.97107 14.96119 52.94116 1.000 24.78921 ?  50  LYS A HE3  1 
ATOM   827  H  HZ1  . LYS A 1 50  ? 36.71953 13.07101 52.45507 1.000 27.14168 ?  50  LYS A HZ1  1 
ATOM   828  H  HZ2  . LYS A 1 50  ? 35.99609 13.82053 53.46163 1.000 27.14168 ?  50  LYS A HZ2  1 
ATOM   829  H  HZ3  . LYS A 1 50  ? 35.56334 13.85885 52.07976 1.000 27.14168 ?  50  LYS A HZ3  1 
ATOM   830  N  N    . GLY A 1 51  ? 32.53379 16.64282 50.14385 1.000 18.62871 ?  51  GLY A N    1 
ATOM   831  C  CA   . GLY A 1 51  ? 31.57710 15.57210 50.03764 1.000 18.94492 ?  51  GLY A CA   1 
ATOM   832  C  C    . GLY A 1 51  ? 30.19107 16.02451 49.69652 1.000 17.92599 ?  51  GLY A C    1 
ATOM   833  O  O    . GLY A 1 51  ? 29.33173 15.16387 49.43451 1.000 20.29301 ?  51  GLY A O    1 
ATOM   834  H  H    . GLY A 1 51  ? 33.03316 16.71530 49.44745 1.000 22.36075 ?  51  GLY A H    1 
ATOM   835  H  HA2  . GLY A 1 51  ? 31.86984 14.95706 49.34704 1.000 22.74021 ?  51  GLY A HA2  1 
ATOM   836  H  HA3  . GLY A 1 51  ? 31.53834 15.10076 50.88454 1.000 22.74021 ?  51  GLY A HA3  1 
ATOM   837  N  N    . GLY A 1 52  ? 29.92674 17.32512 49.63277 1.000 17.03844 ?  52  GLY A N    1 
ATOM   838  C  CA   . GLY A 1 52  ? 28.60208 17.77220 49.33637 1.000 16.01078 ?  52  GLY A CA   1 
ATOM   839  C  C    . GLY A 1 52  ? 28.27436 17.76276 47.84940 1.000 14.85780 ?  52  GLY A C    1 
ATOM   840  O  O    . GLY A 1 52  ? 29.15025 17.88380 47.00281 1.000 16.55462 ?  52  GLY A O    1 
ATOM   841  H  H    . GLY A 1 52  ? 30.50109 17.95281 49.75816 1.000 20.45243 ?  52  GLY A H    1 
ATOM   842  H  HA2  . GLY A 1 52  ? 27.96544 17.19649 49.78820 1.000 19.21924 ?  52  GLY A HA2  1 
ATOM   843  H  HA3  . GLY A 1 52  ? 28.49412 18.67942 49.66226 1.000 19.21924 ?  52  GLY A HA3  1 
ATOM   844  N  N    . GLN A 1 53  ? 26.97247 17.69434 47.58677 1.000 14.17224 ?  53  GLN A N    1 
ATOM   845  C  CA   . GLN A 1 53  ? 26.44632 17.65881 46.21478 1.000 13.95884 ?  53  GLN A CA   1 
ATOM   846  C  C    . GLN A 1 53  ? 25.36726 18.73101 46.13845 1.000 14.19870 ?  53  GLN A C    1 
ATOM   847  O  O    . GLN A 1 53  ? 24.30394 18.56882 46.75814 1.000 14.67543 ?  53  GLN A O    1 
ATOM   848  C  CB   . GLN A 1 53  ? 25.88374 16.28069 45.93473 1.000 14.11951 ?  53  GLN A CB   1 
ATOM   849  C  CG   . GLN A 1 53  ? 25.32825 16.11712 44.53549 1.000 15.18081 ?  53  GLN A CG   1 
ATOM   850  C  CD   . GLN A 1 53  ? 24.60118 14.79971 44.44131 1.000 15.39218 ?  53  GLN A CD   1 
ATOM   851  O  OE1  . GLN A 1 53  ? 23.48822 14.62712 44.98495 1.000 15.41146 ?  53  GLN A OE1  1 
ATOM   852  N  NE2  . GLN A 1 53  ? 25.21638 13.81237 43.76399 1.000 16.50430 ?  53  GLN A NE2  1 
ATOM   853  H  H    . GLN A 1 53  ? 26.36194 17.66678 48.19183 1.000 17.01299 ?  53  GLN A H    1 
ATOM   854  H  HA   . GLN A 1 53  ? 27.12836 17.85804 45.55445 1.000 16.75691 ?  53  GLN A HA   1 
ATOM   855  H  HB2  . GLN A 1 53  ? 26.59066 15.62662 46.05032 1.000 16.94971 ?  53  GLN A HB2  1 
ATOM   856  H  HB3  . GLN A 1 53  ? 25.16388 16.10532 46.56079 1.000 16.94971 ?  53  GLN A HB3  1 
ATOM   857  H  HG2  . GLN A 1 53  ? 24.70526 16.83504 44.34216 1.000 18.22327 ?  53  GLN A HG2  1 
ATOM   858  H  HG3  . GLN A 1 53  ? 26.05262 16.12374 43.89041 1.000 18.22327 ?  53  GLN A HG3  1 
ATOM   859  H  HE21 . GLN A 1 53  ? 25.98797 13.94976 43.40993 1.000 19.81146 ?  53  GLN A HE21 1 
ATOM   860  H  HE22 . GLN A 1 53  ? 24.83781 13.04419 43.68534 1.000 19.81146 ?  53  GLN A HE22 1 
ATOM   861  N  N    . TYR A 1 54  ? 25.63068 19.76652 45.35922 1.000 14.13158 ?  54  TYR A N    1 
ATOM   862  C  CA   . TYR A 1 54  ? 24.77663 20.96355 45.40590 1.000 13.89473 ?  54  TYR A CA   1 
ATOM   863  C  C    . TYR A 1 54  ? 24.13147 21.24742 44.05922 1.000 13.32011 ?  54  TYR A C    1 
ATOM   864  O  O    . TYR A 1 54  ? 24.80198 21.68114 43.10527 1.000 14.30632 ?  54  TYR A O    1 
ATOM   865  C  CB   . TYR A 1 54  ? 25.57707 22.17050 45.86416 1.000 15.17817 ?  54  TYR A CB   1 
ATOM   866  C  CG   . TYR A 1 54  ? 26.22252 21.92316 47.21344 1.000 14.22832 ?  54  TYR A CG   1 
ATOM   867  C  CD1  . TYR A 1 54  ? 25.51298 21.98181 48.37350 1.000 14.22616 ?  54  TYR A CD1  1 
ATOM   868  C  CD2  . TYR A 1 54  ? 27.57021 21.56123 47.28382 1.000 15.03838 ?  54  TYR A CD2  1 
ATOM   869  C  CE1  . TYR A 1 54  ? 26.17260 21.70284 49.62014 1.000 15.10679 ?  54  TYR A CE1  1 
ATOM   870  C  CE2  . TYR A 1 54  ? 28.20790 21.28885 48.46885 1.000 14.72779 ?  54  TYR A CE2  1 
ATOM   871  C  CZ   . TYR A 1 54  ? 27.49883 21.40201 49.65118 1.000 14.72415 ?  54  TYR A CZ   1 
ATOM   872  O  OH   . TYR A 1 54  ? 28.07873 21.11452 50.84805 1.000 14.90372 ?  54  TYR A OH   1 
ATOM   873  H  H    . TYR A 1 54  ? 26.28467 19.80727 44.80223 1.000 16.96419 ?  54  TYR A H    1 
ATOM   874  H  HA   . TYR A 1 54  ? 24.05464 20.77532 46.02574 1.000 16.67998 ?  54  TYR A HA   1 
ATOM   875  H  HB2  . TYR A 1 54  ? 26.27720 22.35560 45.21882 1.000 18.22010 ?  54  TYR A HB2  1 
ATOM   876  H  HB3  . TYR A 1 54  ? 24.98709 22.93646 45.94244 1.000 18.22010 ?  54  TYR A HB3  1 
ATOM   877  H  HD1  . TYR A 1 54  ? 24.60915 22.20048 48.35985 1.000 17.07770 ?  54  TYR A HD1  1 
ATOM   878  H  HD2  . TYR A 1 54  ? 28.05661 21.50224 46.49336 1.000 18.05236 ?  54  TYR A HD2  1 
ATOM   879  H  HE1  . TYR A 1 54  ? 25.68768 21.72833 50.41330 1.000 18.13445 ?  54  TYR A HE1  1 
ATOM   880  H  HE2  . TYR A 1 54  ? 29.10184 21.03249 48.47650 1.000 17.67965 ?  54  TYR A HE2  1 
ATOM   881  H  HH   . TYR A 1 54  ? 28.89582 20.95248 50.73985 1.000 17.89076 ?  54  TYR A HH   1 
ATOM   882  N  N    . HIS A 1 55  ? 22.83553 21.00272 43.97814 1.000 13.56585 ?  55  HIS A N    1 
ATOM   883  C  CA   . HIS A 1 55  ? 22.05457 21.24826 42.76550 1.000 13.47140 ?  55  HIS A CA   1 
ATOM   884  C  C    . HIS A 1 55  ? 21.53245 22.65876 42.76869 1.000 13.61895 ?  55  HIS A C    1 
ATOM   885  O  O    . HIS A 1 55  ? 21.04205 23.14885 43.79322 1.000 13.96263 ?  55  HIS A O    1 
ATOM   886  C  CB   . HIS A 1 55  ? 20.87396 20.26206 42.80721 1.000 14.00736 ?  55  HIS A CB   1 
ATOM   887  C  CG   . HIS A 1 55  ? 19.82931 20.44320 41.76580 1.000 14.01537 ?  55  HIS A CG   1 
ATOM   888  N  ND1  . HIS A 1 55  ? 18.50633 20.12721 42.01503 1.000 14.95031 ?  55  HIS A ND1  1 
ATOM   889  C  CD2  . HIS A 1 55  ? 19.88132 20.87134 40.46395 1.000 14.70200 ?  55  HIS A CD2  1 
ATOM   890  C  CE1  . HIS A 1 55  ? 17.80403 20.29562 40.89071 1.000 14.78551 ?  55  HIS A CE1  1 
ATOM   891  N  NE2  . HIS A 1 55  ? 18.60548 20.78589 39.95578 1.000 15.24329 ?  55  HIS A NE2  1 
ATOM   892  H  H    . HIS A 1 55  ? 22.36730 20.68562 44.62606 1.000 16.28532 ?  55  HIS A H    1 
ATOM   893  H  HA   . HIS A 1 55  ? 22.58175 21.13445 41.95925 1.000 16.17199 ?  55  HIS A HA   1 
ATOM   894  H  HB2  . HIS A 1 55  ? 21.22643 19.36420 42.70470 1.000 16.81513 ?  55  HIS A HB2  1 
ATOM   895  H  HB3  . HIS A 1 55  ? 20.43663 20.35046 43.66851 1.000 16.81513 ?  55  HIS A HB3  1 
ATOM   896  H  HD2  . HIS A 1 55  ? 20.63778 21.16470 40.00941 1.000 17.64870 ?  55  HIS A HD2  1 
ATOM   897  H  HE1  . HIS A 1 55  ? 16.90118 20.10081 40.78208 1.000 17.74892 ?  55  HIS A HE1  1 
ATOM   898  H  HE2  . HIS A 1 55  ? 18.36707 21.01339 39.16143 1.000 18.29825 ?  55  HIS A HE2  1 
ATOM   899  N  N    . GLY A 1 56  ? 21.58785 23.28895 41.61636 1.000 13.60681 ?  56  GLY A N    1 
ATOM   900  C  CA   . GLY A 1 56  ? 20.91871 24.55937 41.42040 1.000 13.93917 ?  56  GLY A CA   1 
ATOM   901  C  C    . GLY A 1 56  ? 20.61187 24.80371 39.95117 1.000 13.88446 ?  56  GLY A C    1 
ATOM   902  O  O    . GLY A 1 56  ? 20.73457 23.89647 39.10138 1.000 14.11545 ?  56  GLY A O    1 
ATOM   903  H  H    . GLY A 1 56  ? 22.00939 23.00215 40.92379 1.000 16.33448 ?  56  GLY A H    1 
ATOM   904  H  HA2  . GLY A 1 56  ? 20.08510 24.56785 41.91632 1.000 16.73330 ?  56  GLY A HA2  1 
ATOM   905  H  HA3  . GLY A 1 56  ? 21.48489 25.27827 41.74214 1.000 16.73330 ?  56  GLY A HA3  1 
ATOM   906  N  N    . THR A 1 57  ? 20.18860 26.03383 39.64728 1.000 14.51842 ?  57  THR A N    1 
ATOM   907  C  CA   . THR A 1 57  ? 19.75667 26.38533 38.30440 1.000 14.00926 ?  57  THR A CA   1 
ATOM   908  C  C    . THR A 1 57  ? 20.41422 27.68941 37.84845 1.000 14.29406 ?  57  THR A C    1 
ATOM   909  O  O    . THR A 1 57  ? 20.75080 28.60952 38.62233 1.000 14.27715 ?  57  THR A O    1 
ATOM   910  C  CB   . THR A 1 57  ? 18.23860 26.53616 38.22750 1.000 15.58063 ?  57  THR A CB   1 
ATOM   911  O  OG1  . THR A 1 57  ? 17.83814 27.49764 39.20794 1.000 15.79851 ?  57  THR A OG1  1 
ATOM   912  C  CG2  . THR A 1 57  ? 17.56839 25.21639 38.38131 1.000 16.86283 ?  57  THR A CG2  1 
ATOM   913  H  H    . THR A 1 57  ? 20.14457 26.68231 40.21043 1.000 17.42840 ?  57  THR A H    1 
ATOM   914  H  HA   . THR A 1 57  ? 20.03615 25.68300 37.69651 1.000 16.81741 ?  57  THR A HA   1 
ATOM   915  H  HB   . THR A 1 57  ? 17.95057 26.86029 37.35982 1.000 18.70306 ?  57  THR A HB   1 
ATOM   916  H  HG1  . THR A 1 57  ? 17.00506 27.60253 39.18395 1.000 18.96451 ?  57  THR A HG1  1 
ATOM   917  H  HG21 . THR A 1 57  ? 16.60594 25.32486 38.32817 1.000 20.24170 ?  57  THR A HG21 1 
ATOM   918  H  HG22 . THR A 1 57  ? 17.85660 24.61396 37.67780 1.000 20.24170 ?  57  THR A HG22 1 
ATOM   919  H  HG23 . THR A 1 57  ? 17.79440 24.82769 39.24080 1.000 20.24170 ?  57  THR A HG23 1 
ATOM   920  N  N    . LEU A 1 58  ? 20.56089 27.77642 36.52533 1.000 14.70188 ?  58  LEU A N    1 
ATOM   921  C  CA   . LEU A 1 58  ? 20.81440 29.02238 35.80150 1.000 15.31429 ?  58  LEU A CA   1 
ATOM   922  C  C    . LEU A 1 58  ? 19.63696 29.23276 34.86003 1.000 15.17794 ?  58  LEU A C    1 
ATOM   923  O  O    . LEU A 1 58  ? 19.37506 28.38535 34.02434 1.000 17.58099 ?  58  LEU A O    1 
ATOM   924  C  CB   . LEU A 1 58  ? 22.04301 29.03662 34.90577 1.000 18.24814 ?  58  LEU A CB   1 
ATOM   925  C  CG   . LEU A 1 58  ? 23.32845 28.54861 35.45754 1.000 20.33873 ?  58  LEU A CG   1 
ATOM   926  C  CD1  . LEU A 1 58  ? 24.37011 28.53281 34.35176 1.000 20.54740 ?  58  LEU A CD1  1 
ATOM   927  C  CD2  . LEU A 1 58  ? 23.78608 29.44060 36.57183 1.000 22.18292 ?  58  LEU A CD2  1 
ATOM   928  H  H    . LEU A 1 58  ? 20.51547 27.09546 36.00205 1.000 17.64856 ?  58  LEU A H    1 
ATOM   929  H  HA   . LEU A 1 58  ? 20.92746 29.70342 36.48289 1.000 18.38345 ?  58  LEU A HA   1 
ATOM   930  H  HB2  . LEU A 1 58  ? 21.84728 28.48455 34.13259 1.000 21.90407 ?  58  LEU A HB2  1 
ATOM   931  H  HB3  . LEU A 1 58  ? 22.19216 29.95426 34.62901 1.000 21.90407 ?  58  LEU A HB3  1 
ATOM   932  H  HG   . LEU A 1 58  ? 23.21655 27.65189 35.81007 1.000 24.41278 ?  58  LEU A HG   1 
ATOM   933  H  HD11 . LEU A 1 58  ? 25.21079 28.21240 34.71439 1.000 24.66318 ?  58  LEU A HD11 1 
ATOM   934  H  HD12 . LEU A 1 58  ? 24.06933 27.94285 33.64297 1.000 24.66318 ?  58  LEU A HD12 1 
ATOM   935  H  HD13 . LEU A 1 58  ? 24.47980 29.43333 34.00834 1.000 24.66318 ?  58  LEU A HD13 1 
ATOM   936  H  HD21 . LEU A 1 58  ? 24.63308 29.11207 36.91177 1.000 26.62580 ?  58  LEU A HD21 1 
ATOM   937  H  HD22 . LEU A 1 58  ? 23.89391 30.34218 36.23063 1.000 26.62580 ?  58  LEU A HD22 1 
ATOM   938  H  HD23 . LEU A 1 58  ? 23.12050 29.43134 37.27740 1.000 26.62580 ?  58  LEU A HD23 1 
ATOM   939  N  N    . THR A 1 59  ? 18.88606 30.31980 35.04070 1.000 15.33972 ?  59  THR A N    1 
ATOM   940  C  CA   . THR A 1 59  ? 17.73122 30.55982 34.19484 1.000 15.35807 ?  59  THR A CA   1 
ATOM   941  C  C    . THR A 1 59  ? 18.09496 31.74900 33.31898 1.000 15.99751 ?  59  THR A C    1 
ATOM   942  O  O    . THR A 1 59  ? 18.13618 32.91339 33.77612 1.000 15.37844 ?  59  THR A O    1 
ATOM   943  C  CB   . THR A 1 59  ? 16.47465 30.81743 34.97335 1.000 16.20589 ?  59  THR A CB   1 
ATOM   944  O  OG1  . THR A 1 59  ? 16.29872 29.73380 35.84497 1.000 17.11717 ?  59  THR A OG1  1 
ATOM   945  C  CG2  . THR A 1 59  ? 15.25809 30.88489 34.06759 1.000 17.82851 ?  59  THR A CG2  1 
ATOM   946  H  H    . THR A 1 59  ? 19.02902 30.92001 35.63980 1.000 18.41396 ?  59  THR A H    1 
ATOM   947  H  HA   . THR A 1 59  ? 17.55430 29.77480 33.65323 1.000 18.43598 ?  59  THR A HA   1 
ATOM   948  H  HB   . THR A 1 59  ? 16.54584 31.66352 35.44234 1.000 19.45336 ?  59  THR A HB   1 
ATOM   949  H  HG1  . THR A 1 59  ? 15.61885 29.85681 36.32271 1.000 20.54691 ?  59  THR A HG1  1 
ATOM   950  H  HG21 . THR A 1 59  ? 14.45392 30.99101 34.59952 1.000 21.40051 ?  59  THR A HG21 1 
ATOM   951  H  HG22 . THR A 1 59  ? 15.33671 31.63856 33.46204 1.000 21.40051 ?  59  THR A HG22 1 
ATOM   952  H  HG23 . THR A 1 59  ? 15.18611 30.06932 33.54744 1.000 21.40051 ?  59  THR A HG23 1 
ATOM   953  N  N    . PHE A 1 60  ? 18.36625 31.44985 32.03282 1.000 16.08956 ?  60  PHE A N    1 
ATOM   954  C  CA   . PHE A 1 60  ? 18.69116 32.49739 31.06583 1.000 15.59799 ?  60  PHE A CA   1 
ATOM   955  C  C    . PHE A 1 60  ? 17.41901 33.21121 30.61664 1.000 15.76447 ?  60  PHE A C    1 
ATOM   956  O  O    . PHE A 1 60  ? 16.38028 32.56915 30.41661 1.000 16.61757 ?  60  PHE A O    1 
ATOM   957  C  CB   . PHE A 1 60  ? 19.43123 31.89130 29.90231 1.000 15.84384 ?  60  PHE A CB   1 
ATOM   958  C  CG   . PHE A 1 60  ? 20.76471 31.33038 30.26068 1.000 16.03310 ?  60  PHE A CG   1 
ATOM   959  C  CD1  . PHE A 1 60  ? 21.87714 32.11620 30.31942 1.000 16.99964 ?  60  PHE A CD1  1 
ATOM   960  C  CD2  . PHE A 1 60  ? 20.92843 29.98751 30.61290 1.000 16.12079 ?  60  PHE A CD2  1 
ATOM   961  C  CE1  . PHE A 1 60  ? 23.10063 31.66318 30.63243 1.000 17.40661 ?  60  PHE A CE1  1 
ATOM   962  C  CE2  . PHE A 1 60  ? 22.19627 29.49540 30.99728 1.000 16.71634 ?  60  PHE A CE2  1 
ATOM   963  C  CZ   . PHE A 1 60  ? 23.26398 30.35308 31.01214 1.000 17.75941 ?  60  PHE A CZ   1 
ATOM   964  H  H    . PHE A 1 60  ? 18.36691 30.65454 31.70559 1.000 19.31377 ?  60  PHE A H    1 
ATOM   965  H  HA   . PHE A 1 60  ? 19.26455 33.17219 31.46178 1.000 18.72389 ?  60  PHE A HA   1 
ATOM   966  H  HB2  . PHE A 1 60  ? 18.89653 31.17022 29.53483 1.000 19.01891 ?  60  PHE A HB2  1 
ATOM   967  H  HB3  . PHE A 1 60  ? 19.57009 32.57702 29.23044 1.000 19.01891 ?  60  PHE A HB3  1 
ATOM   968  H  HD1  . PHE A 1 60  ? 21.78212 33.02194 30.13096 1.000 20.40587 ?  60  PHE A HD1  1 
ATOM   969  H  HD2  . PHE A 1 60  ? 20.19711 29.41330 30.59414 1.000 19.35126 ?  60  PHE A HD2  1 
ATOM   970  H  HE1  . PHE A 1 60  ? 23.83440 32.23318 30.59255 1.000 20.89423 ?  60  PHE A HE1  1 
ATOM   971  H  HE2  . PHE A 1 60  ? 22.30389 28.60313 31.23639 1.000 20.06591 ?  60  PHE A HE2  1 
ATOM   972  H  HZ   . PHE A 1 60  ? 24.10082 30.04810 31.27969 1.000 21.31759 ?  60  PHE A HZ   1 
ATOM   973  N  N    . PRO A 1 61  ? 17.47085 34.53127 30.47596 1.000 15.56554 ?  61  PRO A N    1 
ATOM   974  C  CA   . PRO A 1 61  ? 16.29432 35.31526 30.12703 1.000 16.06492 ?  61  PRO A CA   1 
ATOM   975  C  C    . PRO A 1 61  ? 16.05944 35.23656 28.62610 1.000 16.44765 ?  61  PRO A C    1 
ATOM   976  O  O    . PRO A 1 61  ? 16.90021 34.79925 27.83402 1.000 15.47445 ?  61  PRO A O    1 
ATOM   977  C  CB   . PRO A 1 61  ? 16.68831 36.73614 30.56464 1.000 17.36812 ?  61  PRO A CB   1 
ATOM   978  C  CG   . PRO A 1 61  ? 18.14833 36.78130 30.38300 1.000 17.40848 ?  61  PRO A CG   1 
ATOM   979  C  CD   . PRO A 1 61  ? 18.62296 35.39985 30.77855 1.000 16.90503 ?  61  PRO A CD   1 
ATOM   980  H  HA   . PRO A 1 61  ? 15.50071 35.03905 30.61159 1.000 19.28421 ?  61  PRO A HA   1 
ATOM   981  H  HB2  . PRO A 1 61  ? 16.24574 37.39202 30.00351 1.000 20.84804 ?  61  PRO A HB2  1 
ATOM   982  H  HB3  . PRO A 1 61  ? 16.44702 36.87733 31.49348 1.000 20.84804 ?  61  PRO A HB3  1 
ATOM   983  H  HG2  . PRO A 1 61  ? 18.36241 36.97111 29.45616 1.000 20.89648 ?  61  PRO A HG2  1 
ATOM   984  H  HG3  . PRO A 1 61  ? 18.53416 37.46025 30.95838 1.000 20.89648 ?  61  PRO A HG3  1 
ATOM   985  H  HD2  . PRO A 1 61  ? 19.39621 35.13939 30.25400 1.000 20.29233 ?  61  PRO A HD2  1 
ATOM   986  H  HD3  . PRO A 1 61  ? 18.83753 35.36834 31.72399 1.000 20.29233 ?  61  PRO A HD3  1 
ATOM   987  N  N    . SER A 1 62  ? 14.86531 35.67975 28.23170 1.000 17.75389 ?  62  SER A N    1 
ATOM   988  C  CA   . SER A 1 62  ? 14.46687 35.61604 26.83396 1.000 19.41694 ?  62  SER A CA   1 
ATOM   989  C  C    . SER A 1 62  ? 15.36551 36.42586 25.90662 1.000 17.80161 ?  62  SER A C    1 
ATOM   990  O  O    . SER A 1 62  ? 15.46651 36.10148 24.70814 1.000 19.13424 ?  62  SER A O    1 
ATOM   991  C  CB   . SER A 1 62  ? 13.02685 36.21002 26.75729 1.000 23.67795 ?  62  SER A CB   1 
ATOM   992  O  OG   . SER A 1 62  ? 13.04059 37.62729 27.10806 1.000 27.05141 ?  62  SER A OG   1 
ATOM   993  H  H    . SER A 1 62  ? 14.27247 36.01976 28.75375 1.000 21.31097 ?  62  SER A H    1 
ATOM   994  H  HA   . SER A 1 62  ? 14.49984 34.69593 26.52865 1.000 23.30663 ?  62  SER A HA   1 
ATOM   995  H  HB2  . SER A 1 62  ? 12.69003 36.11009 25.85315 1.000 28.41984 ?  62  SER A HB2  1 
ATOM   996  H  HB3  . SER A 1 62  ? 12.45394 35.73469 27.37918 1.000 28.41984 ?  62  SER A HB3  1 
ATOM   997  H  HG   . SER A 1 62  ? 12.26297 37.94180 27.06363 1.000 32.46799 ?  62  SER A HG   1 
ATOM   998  N  N    . ASP A 1 63  ? 16.04272 37.43784 26.45352 1.000 16.11540 ?  63  ASP A N    1 
ATOM   999  C  CA   . ASP A 1 63  ? 16.94155 38.30991 25.72556 1.000 15.70068 ?  63  ASP A CA   1 
ATOM   1000 C  C    . ASP A 1 63  ? 18.40121 37.89959 25.84941 1.000 15.35175 ?  63  ASP A C    1 
ATOM   1001 O  O    . ASP A 1 63  ? 19.27542 38.62879 25.37425 1.000 15.74442 ?  63  ASP A O    1 
ATOM   1002 C  CB   . ASP A 1 63  ? 16.69640 39.79433 26.06578 1.000 16.65353 ?  63  ASP A CB   1 
ATOM   1003 C  CG   . ASP A 1 63  ? 16.72082 40.15901 27.54082 1.000 18.32285 ?  63  ASP A CG   1 
ATOM   1004 O  OD1  . ASP A 1 63  ? 16.42971 39.29273 28.39776 1.000 18.78355 ?  63  ASP A OD1  1 
ATOM   1005 O  OD2  . ASP A 1 63  ? 16.91387 41.35161 27.84361 1.000 18.51725 -1 63  ASP A OD2  1 
ATOM   1006 H  H    . ASP A 1 63  ? 15.98985 37.64276 27.28707 1.000 19.34479 ?  63  ASP A H    1 
ATOM   1007 H  HA   . ASP A 1 63  ? 16.73146 38.24255 24.78098 1.000 18.84711 ?  63  ASP A HA   1 
ATOM   1008 H  HB2  . ASP A 1 63  ? 17.38408 40.32203 25.63043 1.000 19.99054 ?  63  ASP A HB2  1 
ATOM   1009 H  HB3  . ASP A 1 63  ? 15.82261 40.04239 25.72541 1.000 19.99054 ?  63  ASP A HB3  1 
ATOM   1010 N  N    . TYR A 1 64  ? 18.67075 36.70372 26.41612 1.000 15.66834 ?  64  TYR A N    1 
ATOM   1011 C  CA   . TYR A 1 64  ? 20.00600 36.13065 26.30528 1.000 15.67138 ?  64  TYR A CA   1 
ATOM   1012 C  C    . TYR A 1 64  ? 20.39659 36.09842 24.82911 1.000 16.07558 ?  64  TYR A C    1 
ATOM   1013 O  O    . TYR A 1 64  ? 19.57603 35.72776 24.01063 1.000 16.50730 ?  64  TYR A O    1 
ATOM   1014 C  CB   . TYR A 1 64  ? 20.00501 34.71619 26.93808 1.000 15.75027 ?  64  TYR A CB   1 
ATOM   1015 C  CG   . TYR A 1 64  ? 21.39538 34.09890 26.96532 1.000 14.42307 ?  64  TYR A CG   1 
ATOM   1016 C  CD1  . TYR A 1 64  ? 22.33100 34.51745 27.90041 1.000 15.69106 ?  64  TYR A CD1  1 
ATOM   1017 C  CD2  . TYR A 1 64  ? 21.78849 33.17479 26.02865 1.000 15.20606 ?  64  TYR A CD2  1 
ATOM   1018 C  CE1  . TYR A 1 64  ? 23.62598 34.02666 27.88109 1.000 15.50373 ?  64  TYR A CE1  1 
ATOM   1019 C  CE2  . TYR A 1 64  ? 23.06670 32.64971 25.99786 1.000 16.08252 ?  64  TYR A CE2  1 
ATOM   1020 C  CZ   . TYR A 1 64  ? 23.98521 33.08356 26.92942 1.000 16.27087 ?  64  TYR A CZ   1 
ATOM   1021 O  OH   . TYR A 1 64  ? 25.24229 32.57861 26.77841 1.000 17.18282 ?  64  TYR A OH   1 
ATOM   1022 H  H    . TYR A 1 64  ? 18.10651 36.22606 26.85553 1.000 18.80831 ?  64  TYR A H    1 
ATOM   1023 H  HA   . TYR A 1 64  ? 20.66914 36.65820 26.77733 1.000 18.81196 ?  64  TYR A HA   1 
ATOM   1024 H  HB2  . TYR A 1 64  ? 19.68240 34.77637 27.85088 1.000 18.90663 ?  64  TYR A HB2  1 
ATOM   1025 H  HB3  . TYR A 1 64  ? 19.42615 34.13604 26.41920 1.000 18.90663 ?  64  TYR A HB3  1 
ATOM   1026 H  HD1  . TYR A 1 64  ? 22.08507 35.13642 28.54947 1.000 18.83557 ?  64  TYR A HD1  1 
ATOM   1027 H  HD2  . TYR A 1 64  ? 21.17237 32.89201 25.39199 1.000 18.25358 ?  64  TYR A HD2  1 
ATOM   1028 H  HE1  . TYR A 1 64  ? 24.25011 34.32720 28.50160 1.000 18.61077 ?  64  TYR A HE1  1 
ATOM   1029 H  HE2  . TYR A 1 64  ? 23.30268 32.01522 25.36018 1.000 19.30532 ?  64  TYR A HE2  1 
ATOM   1030 H  HH   . TYR A 1 64  ? 25.76622 32.94430 27.32372 1.000 20.62569 ?  64  TYR A HH   1 
ATOM   1031 N  N    . PRO A 1 65  ? 21.65677 36.44617 24.44800 1.000 15.56648 ?  65  PRO A N    1 
ATOM   1032 C  CA   . PRO A 1 65  ? 22.87129 36.59032 25.26475 1.000 15.53464 ?  65  PRO A CA   1 
ATOM   1033 C  C    . PRO A 1 65  ? 23.15225 37.99930 25.74404 1.000 15.91218 ?  65  PRO A C    1 
ATOM   1034 O  O    . PRO A 1 65  ? 24.26027 38.29646 26.20698 1.000 16.88266 ?  65  PRO A O    1 
ATOM   1035 C  CB   . PRO A 1 65  ? 23.98049 36.15068 24.30010 1.000 16.87039 ?  65  PRO A CB   1 
ATOM   1036 C  CG   . PRO A 1 65  ? 23.47150 36.61762 22.95505 1.000 16.57332 ?  65  PRO A CG   1 
ATOM   1037 C  CD   . PRO A 1 65  ? 22.04099 36.32193 23.02103 1.000 16.52241 ?  65  PRO A CD   1 
ATOM   1038 H  HA   . PRO A 1 65  ? 22.81100 36.00422 26.03530 1.000 18.64787 ?  65  PRO A HA   1 
ATOM   1039 H  HB2  . PRO A 1 65  ? 24.81851 36.58152 24.53033 1.000 20.25077 ?  65  PRO A HB2  1 
ATOM   1040 H  HB3  . PRO A 1 65  ? 24.08569 35.18668 24.32341 1.000 20.25077 ?  65  PRO A HB3  1 
ATOM   1041 H  HG2  . PRO A 1 65  ? 23.63134 37.56792 22.84423 1.000 19.89428 ?  65  PRO A HG2  1 
ATOM   1042 H  HG3  . PRO A 1 65  ? 23.90212 36.12319 22.24021 1.000 19.89428 ?  65  PRO A HG3  1 
ATOM   1043 H  HD2  . PRO A 1 65  ? 21.54338 36.95878 22.48465 1.000 19.83319 ?  65  PRO A HD2  1 
ATOM   1044 H  HD3  . PRO A 1 65  ? 21.87172 35.41990 22.70704 1.000 19.83319 ?  65  PRO A HD3  1 
ATOM   1045 N  N    . TYR A 1 66  ? 22.16297 38.88740 25.73876 1.000 15.40605 ?  66  TYR A N    1 
ATOM   1046 C  CA   . TYR A 1 66  ? 22.40013 40.30007 26.08156 1.000 15.35121 ?  66  TYR A CA   1 
ATOM   1047 C  C    . TYR A 1 66  ? 22.02741 40.63838 27.49900 1.000 16.17118 ?  66  TYR A C    1 
ATOM   1048 O  O    . TYR A 1 66  ? 22.20357 41.79192 27.91691 1.000 18.84266 ?  66  TYR A O    1 
ATOM   1049 C  CB   . TYR A 1 66  ? 21.63571 41.20875 25.09035 1.000 15.72437 ?  66  TYR A CB   1 
ATOM   1050 C  CG   . TYR A 1 66  ? 22.05464 40.95914 23.65863 1.000 15.40407 ?  66  TYR A CG   1 
ATOM   1051 C  CD1  . TYR A 1 66  ? 23.20434 41.49334 23.13629 1.000 16.31566 ?  66  TYR A CD1  1 
ATOM   1052 C  CD2  . TYR A 1 66  ? 21.33151 40.10018 22.85005 1.000 15.46687 ?  66  TYR A CD2  1 
ATOM   1053 C  CE1  . TYR A 1 66  ? 23.60738 41.24762 21.83179 1.000 16.34826 ?  66  TYR A CE1  1 
ATOM   1054 C  CE2  . TYR A 1 66  ? 21.68954 39.80830 21.55470 1.000 16.10747 ?  66  TYR A CE2  1 
ATOM   1055 C  CZ   . TYR A 1 66  ? 22.84125 40.40839 21.04113 1.000 15.74854 ?  66  TYR A CZ   1 
ATOM   1056 O  OH   . TYR A 1 66  ? 23.14873 40.09153 19.76006 1.000 17.19338 ?  66  TYR A OH   1 
ATOM   1057 H  H    . TYR A 1 66  ? 21.34638 38.70317 25.54168 1.000 18.49356 ?  66  TYR A H    1 
ATOM   1058 H  HA   . TYR A 1 66  ? 23.34661 40.49137 25.98952 1.000 18.42775 ?  66  TYR A HA   1 
ATOM   1059 H  HB2  . TYR A 1 66  ? 20.68475 41.03225 25.16402 1.000 18.87554 ?  66  TYR A HB2  1 
ATOM   1060 H  HB3  . TYR A 1 66  ? 21.81823 42.13739 25.30301 1.000 18.87554 ?  66  TYR A HB3  1 
ATOM   1061 H  HD1  . TYR A 1 66  ? 23.73154 42.03861 23.67448 1.000 19.58510 ?  66  TYR A HD1  1 
ATOM   1062 H  HD2  . TYR A 1 66  ? 20.56726 39.70139 23.19904 1.000 18.56655 ?  66  TYR A HD2  1 
ATOM   1063 H  HE1  . TYR A 1 66  ? 24.37974 41.64032 21.49393 1.000 19.62422 ?  66  TYR A HE1  1 
ATOM   1064 H  HE2  . TYR A 1 66  ? 21.17981 39.22851 21.03613 1.000 19.33527 ?  66  TYR A HE2  1 
ATOM   1065 H  HH   . TYR A 1 66  ? 23.85088 40.48899 19.52640 1.000 20.63836 ?  66  TYR A HH   1 
ATOM   1066 N  N    . LYS A 1 67  ? 21.62384 39.66321 28.28434 1.000 16.32649 ?  67  LYS A N    1 
ATOM   1067 C  CA   . LYS A 1 67  ? 21.20845 39.84533 29.67025 1.000 16.62546 ?  67  LYS A CA   1 
ATOM   1068 C  C    . LYS A 1 67  ? 21.66215 38.59275 30.41714 1.000 15.98114 ?  67  LYS A C    1 
ATOM   1069 O  O    . LYS A 1 67  ? 21.63382 37.49333 29.85320 1.000 16.87892 ?  67  LYS A O    1 
ATOM   1070 C  CB   . LYS A 1 67  ? 19.68116 39.99763 29.64139 1.000 18.96313 ?  67  LYS A CB   1 
ATOM   1071 C  CG   . LYS A 1 67  ? 18.92873 40.32602 30.90203 1.000 21.18282 ?  67  LYS A CG   1 
ATOM   1072 C  CD   . LYS A 1 67  ? 19.12168 41.78010 31.39363 1.000 21.56233 ?  67  LYS A CD   1 
ATOM   1073 C  CE   . LYS A 1 67  ? 18.61372 42.82090 30.50408 1.000 22.49213 ?  67  LYS A CE   1 
ATOM   1074 N  NZ   . LYS A 1 67  ? 17.12128 42.77454 30.12360 1.000 21.76630 ?  67  LYS A NZ   1 
ATOM   1075 H  H    . LYS A 1 67  ? 21.57697 38.84270 28.03103 1.000 19.59809 ?  67  LYS A H    1 
ATOM   1076 H  HA   . LYS A 1 67  ? 21.60301 40.60317 30.12948 1.000 19.95686 ?  67  LYS A HA   1 
ATOM   1077 H  HB2  . LYS A 1 67  ? 19.47608 40.70846 29.01404 1.000 22.76206 ?  67  LYS A HB2  1 
ATOM   1078 H  HB3  . LYS A 1 67  ? 19.31562 39.15775 29.32222 1.000 22.76206 ?  67  LYS A HB3  1 
ATOM   1079 H  HG2  . LYS A 1 67  ? 17.98120 40.19339 30.74235 1.000 25.42569 ?  67  LYS A HG2  1 
ATOM   1080 H  HG3  . LYS A 1 67  ? 19.23209 39.73459 31.60848 1.000 25.42569 ?  67  LYS A HG3  1 
ATOM   1081 H  HD2  . LYS A 1 67  ? 18.66277 41.87884 32.24248 1.000 25.88110 ?  67  LYS A HD2  1 
ATOM   1082 H  HD3  . LYS A 1 67  ? 20.07142 41.93976 31.50939 1.000 25.88110 ?  67  LYS A HD3  1 
ATOM   1083 H  HE2  . LYS A 1 67  ? 18.76486 43.67772 30.93293 1.000 26.99686 ?  67  LYS A HE2  1 
ATOM   1084 H  HE3  . LYS A 1 67  ? 19.11384 42.77238 29.67437 1.000 26.99686 ?  67  LYS A HE3  1 
ATOM   1085 H  HZ1  . LYS A 1 67  ? 16.92284 43.45570 29.58625 1.000 26.12586 ?  67  LYS A HZ1  1 
ATOM   1086 H  HZ2  . LYS A 1 67  ? 16.93792 42.01193 29.70300 1.000 26.12586 ?  67  LYS A HZ2  1 
ATOM   1087 H  HZ3  . LYS A 1 67  ? 16.61859 42.82852 30.85606 1.000 26.12586 ?  67  LYS A HZ3  1 
ATOM   1088 N  N    . PRO A 1 68  ? 22.02536 38.70304 31.69405 1.000 15.83782 ?  68  PRO A N    1 
ATOM   1089 C  CA   . PRO A 1 68  ? 22.54493 37.54465 32.43213 1.000 15.09102 ?  68  PRO A CA   1 
ATOM   1090 C  C    . PRO A 1 68  ? 21.48223 36.61402 32.96795 1.000 14.74197 ?  68  PRO A C    1 
ATOM   1091 O  O    . PRO A 1 68  ? 20.32798 37.00866 33.14063 1.000 15.41497 ?  68  PRO A O    1 
ATOM   1092 C  CB   . PRO A 1 68  ? 23.22093 38.18052 33.65563 1.000 15.21019 ?  68  PRO A CB   1 
ATOM   1093 C  CG   . PRO A 1 68  ? 23.19775 39.65258 33.38761 1.000 15.76329 ?  68  PRO A CG   1 
ATOM   1094 C  CD   . PRO A 1 68  ? 22.10116 39.93794 32.48318 1.000 16.44848 ?  68  PRO A CD   1 
ATOM   1095 H  HA   . PRO A 1 68  ? 23.14913 37.07203 31.83843 1.000 18.11552 ?  68  PRO A HA   1 
ATOM   1096 H  HB2  . PRO A 1 68  ? 22.72060 37.96571 34.45839 1.000 18.25853 ?  68  PRO A HB2  1 
ATOM   1097 H  HB3  . PRO A 1 68  ? 24.13164 37.85633 33.73562 1.000 18.25853 ?  68  PRO A HB3  1 
ATOM   1098 H  HG2  . PRO A 1 68  ? 23.07092 40.12468 34.22542 1.000 18.92225 ?  68  PRO A HG2  1 
ATOM   1099 H  HG3  . PRO A 1 68  ? 24.04011 39.91387 32.98379 1.000 18.92225 ?  68  PRO A HG3  1 
ATOM   1100 H  HD2  . PRO A 1 68  ? 21.27692 40.09292 32.97053 1.000 19.74448 ?  68  PRO A HD2  1 
ATOM   1101 H  HD3  . PRO A 1 68  ? 22.30198 40.70152 31.91969 1.000 19.74448 ?  68  PRO A HD3  1 
ATOM   1102 N  N    . PRO A 1 69  ? 21.87033 35.39170 33.31354 1.000 15.42397 ?  69  PRO A N    1 
ATOM   1103 C  CA   . PRO A 1 69  ? 20.96054 34.45166 33.98107 1.000 14.75806 ?  69  PRO A CA   1 
ATOM   1104 C  C    . PRO A 1 69  ? 20.70955 34.77877 35.43607 1.000 14.67984 ?  69  PRO A C    1 
ATOM   1105 O  O    . PRO A 1 69  ? 21.51706 35.42924 36.10989 1.000 15.31140 ?  69  PRO A O    1 
ATOM   1106 C  CB   . PRO A 1 69  ? 21.68539 33.08626 33.89270 1.000 15.44158 ?  69  PRO A CB   1 
ATOM   1107 C  CG   . PRO A 1 69  ? 23.19626 33.50227 33.91990 1.000 16.29735 ?  69  PRO A CG   1 
ATOM   1108 C  CD   . PRO A 1 69  ? 23.22285 34.79110 33.12355 1.000 16.39607 ?  69  PRO A CD   1 
ATOM   1109 H  HA   . PRO A 1 69  ? 20.12370 34.43560 33.49083 1.000 17.71597 ?  69  PRO A HA   1 
ATOM   1110 H  HB2  . PRO A 1 69  ? 21.45556 32.52921 34.65282 1.000 18.53620 ?  69  PRO A HB2  1 
ATOM   1111 H  HB3  . PRO A 1 69  ? 21.45580 32.63197 33.06699 1.000 18.53620 ?  69  PRO A HB3  1 
ATOM   1112 H  HG2  . PRO A 1 69  ? 23.48930 33.64662 34.83324 1.000 19.56312 ?  69  PRO A HG2  1 
ATOM   1113 H  HG3  . PRO A 1 69  ? 23.74140 32.81812 33.50079 1.000 19.56312 ?  69  PRO A HG3  1 
ATOM   1114 H  HD2  . PRO A 1 69  ? 23.90851 35.38609 33.46525 1.000 19.68159 ?  69  PRO A HD2  1 
ATOM   1115 H  HD3  . PRO A 1 69  ? 23.38214 34.60579 32.18483 1.000 19.68159 ?  69  PRO A HD3  1 
ATOM   1116 N  N    . ALA A 1 70  ? 19.56100 34.31241 35.89237 1.000 14.17694 ?  70  ALA A N    1 
ATOM   1117 C  CA   . ALA A 1 70  ? 19.27793 34.20882 37.32177 1.000 14.84516 ?  70  ALA A CA   1 
ATOM   1118 C  C    . ALA A 1 70  ? 19.90638 32.93398 37.87762 1.000 14.64102 ?  70  ALA A C    1 
ATOM   1119 O  O    . ALA A 1 70  ? 19.69448 31.85938 37.28270 1.000 15.29052 ?  70  ALA A O    1 
ATOM   1120 C  CB   . ALA A 1 70  ? 17.76758 34.14890 37.53272 1.000 16.05254 ?  70  ALA A CB   1 
ATOM   1121 H  H    . ALA A 1 70  ? 18.91565 34.04385 35.39139 1.000 17.01863 ?  70  ALA A H    1 
ATOM   1122 H  HA   . ALA A 1 70  ? 19.64464 34.97586 37.78875 1.000 17.82050 ?  70  ALA A HA   1 
ATOM   1123 H  HB1  . ALA A 1 70  ? 17.58361 34.08875 38.48321 1.000 19.26935 ?  70  ALA A HB1  1 
ATOM   1124 H  HB2  . ALA A 1 70  ? 17.36566 34.95296 37.16824 1.000 19.26935 ?  70  ALA A HB2  1 
ATOM   1125 H  HB3  . ALA A 1 70  ? 17.41590 33.36778 37.07766 1.000 19.26935 ?  70  ALA A HB3  1 
ATOM   1126 N  N    . ILE A 1 71  ? 20.65752 33.02475 38.96750 1.000 14.34124 ?  71  ILE A N    1 
ATOM   1127 C  CA   . ILE A 1 71  ? 21.42601 31.94317 39.55007 1.000 14.70776 ?  71  ILE A CA   1 
ATOM   1128 C  C    . ILE A 1 71  ? 20.83710 31.60901 40.89266 1.000 13.66465 ?  71  ILE A C    1 
ATOM   1129 O  O    . ILE A 1 71  ? 20.72757 32.47755 41.74886 1.000 14.19116 ?  71  ILE A O    1 
ATOM   1130 C  CB   . ILE A 1 71  ? 22.90199 32.32996 39.63722 1.000 15.02963 ?  71  ILE A CB   1 
ATOM   1131 C  CG1  . ILE A 1 71  ? 23.38080 32.74107 38.23003 1.000 16.47799 ?  71  ILE A CG1  1 
ATOM   1132 C  CG2  . ILE A 1 71  ? 23.66358 31.12811 40.24179 1.000 15.39801 ?  71  ILE A CG2  1 
ATOM   1133 C  CD1  . ILE A 1 71  ? 24.83856 32.97137 38.16519 1.000 17.55443 ?  71  ILE A CD1  1 
ATOM   1134 H  H    . ILE A 1 71  ? 20.74091 33.75452 39.41481 1.000 17.21579 ?  71  ILE A H    1 
ATOM   1135 H  HA   . ILE A 1 71  ? 21.34873 31.14228 39.00832 1.000 17.65561 ?  71  ILE A HA   1 
ATOM   1136 H  HB   . ILE A 1 71  ? 23.06151 33.09319 40.21423 1.000 18.04185 ?  71  ILE A HB   1 
ATOM   1137 H  HG12 . ILE A 1 71  ? 23.16051 32.03459 37.60293 1.000 19.77990 ?  71  ILE A HG12 1 
ATOM   1138 H  HG13 . ILE A 1 71  ? 22.93543 33.56357 37.97304 1.000 19.77990 ?  71  ILE A HG13 1 
ATOM   1139 H  HG21 . ILE A 1 71  ? 24.61577 31.31094 40.21330 1.000 18.48391 ?  71  ILE A HG21 1 
ATOM   1140 H  HG22 . ILE A 1 71  ? 23.37811 31.00307 41.16036 1.000 18.48391 ?  71  ILE A HG22 1 
ATOM   1141 H  HG23 . ILE A 1 71  ? 23.46358 30.33379 39.72222 1.000 18.48391 ?  71  ILE A HG23 1 
ATOM   1142 H  HD11 . ILE A 1 71  ? 25.05798 33.36658 37.30696 1.000 21.07162 ?  71  ILE A HD11 1 
ATOM   1143 H  HD12 . ILE A 1 71  ? 25.09545 33.57271 38.88164 1.000 21.07162 ?  71  ILE A HD12 1 
ATOM   1144 H  HD13 . ILE A 1 71  ? 25.29714 32.12251 38.26540 1.000 21.07162 ?  71  ILE A HD13 1 
ATOM   1145 N  N    . ARG A 1 72  ? 20.42877 30.34633 41.09138 1.000 13.44060 ?  72  ARG A N    1 
ATOM   1146 C  CA   . ARG A 1 72  ? 19.84740 29.89143 42.34143 1.000 14.40927 ?  72  ARG A CA   1 
ATOM   1147 C  C    . ARG A 1 72  ? 20.50140 28.56830 42.72904 1.000 13.82614 ?  72  ARG A C    1 
ATOM   1148 O  O    . ARG A 1 72  ? 20.97322 27.82247 41.84058 1.000 14.59622 ?  72  ARG A O    1 
ATOM   1149 C  CB   . ARG A 1 72  ? 18.33244 29.67856 42.20115 1.000 14.76154 ?  72  ARG A CB   1 
ATOM   1150 C  CG   . ARG A 1 72  ? 17.54651 30.87854 41.77751 1.000 13.90966 ?  72  ARG A CG   1 
ATOM   1151 C  CD   . ARG A 1 72  ? 16.09167 30.64296 41.65078 1.000 15.49372 ?  72  ARG A CD   1 
ATOM   1152 N  NE   . ARG A 1 72  ? 15.32566 31.83892 41.34350 1.000 15.17443 ?  72  ARG A NE   1 
ATOM   1153 C  CZ   . ARG A 1 72  ? 15.02336 32.25865 40.12990 1.000 15.67262 ?  72  ARG A CZ   1 
ATOM   1154 N  NH1  . ARG A 1 72  ? 15.51926 31.69838 39.05781 1.000 17.23717 ?  72  ARG A NH1  1 
ATOM   1155 N  NH2  . ARG A 1 72  ? 14.25024 33.33931 39.98539 1.000 15.98327 ?  72  ARG A NH2  1 
ATOM   1156 H  H    . ARG A 1 72  ? 20.48384 29.72778 40.49643 1.000 16.13502 ?  72  ARG A H    1 
ATOM   1157 H  HA   . ARG A 1 72  ? 20.00575 30.54468 43.04078 1.000 17.29742 ?  72  ARG A HA   1 
ATOM   1158 H  HB2  . ARG A 1 72  ? 18.18233 28.98702 41.53771 1.000 17.72015 ?  72  ARG A HB2  1 
ATOM   1159 H  HB3  . ARG A 1 72  ? 17.98400 29.39483 43.06080 1.000 17.72015 ?  72  ARG A HB3  1 
ATOM   1160 H  HG2  . ARG A 1 72  ? 17.67295 31.58014 42.43530 1.000 16.69790 ?  72  ARG A HG2  1 
ATOM   1161 H  HG3  . ARG A 1 72  ? 17.87162 31.17255 40.91220 1.000 16.69790 ?  72  ARG A HG3  1 
ATOM   1162 H  HD2  . ARG A 1 72  ? 15.94028 30.00433 40.93655 1.000 18.59877 ?  72  ARG A HD2  1 
ATOM   1163 H  HD3  . ARG A 1 72  ? 15.75914 30.28739 42.48977 1.000 18.59877 ?  72  ARG A HD3  1 
ATOM   1164 H  HE   . ARG A 1 72  ? 15.04696 32.31109 42.00606 1.000 18.21562 ?  72  ARG A HE   1 
ATOM   1165 H  HH11 . ARG A 1 72  ? 16.06087 31.03437 39.13098 1.000 20.69090 ?  72  ARG A HH11 1 
ATOM   1166 H  HH12 . ARG A 1 72  ? 15.30386 31.99383 38.27941 1.000 20.69090 ?  72  ARG A HH12 1 
ATOM   1167 H  HH21 . ARG A 1 72  ? 13.95552 33.75308 40.67931 1.000 19.18622 ?  72  ARG A HH21 1 
ATOM   1168 H  HH22 . ARG A 1 72  ? 14.04750 33.62086 39.19848 1.000 19.18622 ?  72  ARG A HH22 1 
ATOM   1169 N  N    . MET A 1 73  ? 20.54929 28.27596 44.01193 1.000 13.44749 ?  73  MET A N    1 
ATOM   1170 C  CA   . MET A 1 73  ? 20.94121 26.97988 44.54121 1.000 14.43817 ?  73  MET A CA   1 
ATOM   1171 C  C    . MET A 1 73  ? 19.77008 26.33687 45.22458 1.000 13.76001 ?  73  MET A C    1 
ATOM   1172 O  O    . MET A 1 73  ? 19.14660 26.98822 46.05571 1.000 14.47867 ?  73  MET A O    1 
ATOM   1173 C  CB   . MET A 1 73  ? 22.11220 27.10478 45.52512 1.000 14.07474 ?  73  MET A CB   1 
ATOM   1174 C  CG   . MET A 1 73  ? 22.76017 25.72863 45.80757 1.000 14.58832 ?  73  MET A CG   1 
ATOM   1175 S  SD   . MET A 1 73  ? 24.34298 25.82175 46.65869 1.000 14.81067 ?  73  MET A SD   1 
ATOM   1176 C  CE   . MET A 1 73  ? 25.41520 25.99263 45.18247 1.000 16.34401 ?  73  MET A CE   1 
ATOM   1177 H  H    . MET A 1 73  ? 20.34949 28.83894 44.63058 1.000 16.14329 ?  73  MET A H    1 
ATOM   1178 H  HA   . MET A 1 73  ? 21.22819 26.42093 43.80222 1.000 17.33210 ?  73  MET A HA   1 
ATOM   1179 H  HB2  . MET A 1 73  ? 22.78770 27.68967 45.14761 1.000 16.89599 ?  73  MET A HB2  1 
ATOM   1180 H  HB3  . MET A 1 73  ? 21.78915 27.46915 46.36403 1.000 16.89599 ?  73  MET A HB3  1 
ATOM   1181 H  HG2  . MET A 1 73  ? 22.15766 25.20953 46.36292 1.000 17.51228 ?  73  MET A HG2  1 
ATOM   1182 H  HG3  . MET A 1 73  ? 22.90667 25.27485 44.96287 1.000 17.51228 ?  73  MET A HG3  1 
ATOM   1183 H  HE1  . MET A 1 73  ? 26.33637 26.08894 45.47068 1.000 19.61911 ?  73  MET A HE1  1 
ATOM   1184 H  HE2  . MET A 1 73  ? 25.32224 25.19996 44.63118 1.000 19.61911 ?  73  MET A HE2  1 
ATOM   1185 H  HE3  . MET A 1 73  ? 25.14132 26.77734 44.68236 1.000 19.61911 ?  73  MET A HE3  1 
ATOM   1186 N  N    . ILE A 1 74  ? 19.48049 25.10295 44.88090 1.000 13.59677 ?  74  ILE A N    1 
ATOM   1187 C  CA   . ILE A 1 74  ? 18.31254 24.38810 45.43418 1.000 14.67551 ?  74  ILE A CA   1 
ATOM   1188 C  C    . ILE A 1 74  ? 18.67153 23.61243 46.70581 1.000 14.06849 ?  74  ILE A C    1 
ATOM   1189 O  O    . ILE A 1 74  ? 17.99787 23.68914 47.73379 1.000 15.17025 ?  74  ILE A O    1 
ATOM   1190 C  CB   . ILE A 1 74  ? 17.66049 23.49445 44.35518 1.000 15.35280 ?  74  ILE A CB   1 
ATOM   1191 C  CG1  . ILE A 1 74  ? 17.09450 24.30700 43.20919 1.000 15.71137 ?  74  ILE A CG1  1 
ATOM   1192 C  CG2  . ILE A 1 74  ? 16.62658 22.56115 44.99248 1.000 16.08945 ?  74  ILE A CG2  1 
ATOM   1193 C  CD1  . ILE A 1 74  ? 16.80045 23.48941 41.96721 1.000 16.79869 ?  74  ILE A CD1  1 
ATOM   1194 H  H    . ILE A 1 74  ? 19.93987 24.63664 44.32312 1.000 16.32243 ?  74  ILE A H    1 
ATOM   1195 H  HA   . ILE A 1 74  ? 17.64808 25.04746 45.68837 1.000 17.61692 ?  74  ILE A HA   1 
ATOM   1196 H  HB   . ILE A 1 74  ? 18.35287 22.94005 43.96255 1.000 18.42967 ?  74  ILE A HB   1 
ATOM   1197 H  HG12 . ILE A 1 74  ? 16.26376 24.71635 43.49763 1.000 18.85995 ?  74  ILE A HG12 1 
ATOM   1198 H  HG13 . ILE A 1 74  ? 17.73585 24.99318 42.96686 1.000 18.85995 ?  74  ILE A HG13 1 
ATOM   1199 H  HG21 . ILE A 1 74  ? 16.06819 22.18472 44.29434 1.000 19.31364 ?  74  ILE A HG21 1 
ATOM   1200 H  HG22 . ILE A 1 74  ? 17.09006 21.85142 45.46404 1.000 19.31364 ?  74  ILE A HG22 1 
ATOM   1201 H  HG23 . ILE A 1 74  ? 16.08199 23.07005 45.61325 1.000 19.31364 ?  74  ILE A HG23 1 
ATOM   1202 H  HD11 . ILE A 1 74  ? 16.56182 24.08938 41.24334 1.000 20.16474 ?  74  ILE A HD11 1 
ATOM   1203 H  HD12 . ILE A 1 74  ? 17.59176 22.98163 41.72872 1.000 20.16474 ?  74  ILE A HD12 1 
ATOM   1204 H  HD13 . ILE A 1 74  ? 16.06397 22.88618 42.15327 1.000 20.16474 ?  74  ILE A HD13 1 
ATOM   1205 N  N    . THR A 1 75  ? 19.75650 22.84203 46.65975 1.000 13.74233 ?  75  THR A N    1 
ATOM   1206 C  CA   . THR A 1 75  ? 20.11699 21.97721 47.78884 1.000 13.45984 ?  75  THR A CA   1 
ATOM   1207 C  C    . THR A 1 75  ? 20.50305 22.86098 48.99118 1.000 13.56287 ?  75  THR A C    1 
ATOM   1208 O  O    . THR A 1 75  ? 21.36922 23.74686 48.87015 1.000 14.74481 ?  75  THR A O    1 
ATOM   1209 C  CB   . THR A 1 75  ? 21.33688 21.13462 47.42663 1.000 14.03927 ?  75  THR A CB   1 
ATOM   1210 O  OG1  . THR A 1 75  ? 21.14318 20.46468 46.18603 1.000 14.29591 ?  75  THR A OG1  1 
ATOM   1211 C  CG2  . THR A 1 75  ? 21.70150 20.16316 48.54183 1.000 14.89974 ?  75  THR A CG2  1 
ATOM   1212 H  H    . THR A 1 75  ? 20.29862 22.79932 45.99351 1.000 16.49709 ?  75  THR A H    1 
ATOM   1213 H  HA   . THR A 1 75  ? 19.36804 21.40178 48.00985 1.000 16.15812 ?  75  THR A HA   1 
ATOM   1214 H  HB   . THR A 1 75  ? 22.09954 21.72419 47.31866 1.000 16.85343 ?  75  THR A HB   1 
ATOM   1215 H  HG1  . THR A 1 75  ? 20.48331 19.94758 46.23873 1.000 17.16139 ?  75  THR A HG1  1 
ATOM   1216 H  HG21 . THR A 1 75  ? 22.38602 19.54802 48.23534 1.000 17.88599 ?  75  THR A HG21 1 
ATOM   1217 H  HG22 . THR A 1 75  ? 22.03764 20.65090 49.30996 1.000 17.88599 ?  75  THR A HG22 1 
ATOM   1218 H  HG23 . THR A 1 75  ? 20.91906 19.65582 48.80886 1.000 17.88599 ?  75  THR A HG23 1 
ATOM   1219 N  N    . PRO A 1 76  ? 19.95375 22.62761 50.18228 1.000 14.31189 ?  76  PRO A N    1 
ATOM   1220 C  CA   . PRO A 1 76  ? 20.41240 23.31221 51.39767 1.000 14.56655 ?  76  PRO A CA   1 
ATOM   1221 C  C    . PRO A 1 76  ? 21.89457 23.13272 51.57138 1.000 15.05316 ?  76  PRO A C    1 
ATOM   1222 O  O    . PRO A 1 76  ? 22.42558 22.02959 51.41769 1.000 15.38162 ?  76  PRO A O    1 
ATOM   1223 C  CB   . PRO A 1 76  ? 19.58127 22.64468 52.52048 1.000 16.68907 ?  76  PRO A CB   1 
ATOM   1224 C  CG   . PRO A 1 76  ? 18.28193 22.28175 51.76784 1.000 16.57362 ?  76  PRO A CG   1 
ATOM   1225 C  CD   . PRO A 1 76  ? 18.76637 21.79721 50.42957 1.000 15.12068 ?  76  PRO A CD   1 
ATOM   1226 H  HA   . PRO A 1 76  ? 20.20165 24.25891 51.38226 1.000 17.48617 ?  76  PRO A HA   1 
ATOM   1227 H  HB2  . PRO A 1 76  ? 20.03248 21.85605 52.86016 1.000 20.03319 ?  76  PRO A HB2  1 
ATOM   1228 H  HB3  . PRO A 1 76  ? 19.41552 23.26943 53.24375 1.000 20.03319 ?  76  PRO A HB3  1 
ATOM   1229 H  HG2  . PRO A 1 76  ? 17.80349 21.58365 52.24182 1.000 19.89464 ?  76  PRO A HG2  1 
ATOM   1230 H  HG3  . PRO A 1 76  ? 17.71824 23.06560 51.67439 1.000 19.89464 ?  76  PRO A HG3  1 
ATOM   1231 H  HD2  . PRO A 1 76  ? 19.00357 20.85742 50.46736 1.000 18.15112 ?  76  PRO A HD2  1 
ATOM   1232 H  HD3  . PRO A 1 76  ? 18.09434 21.94250 49.74535 1.000 18.15112 ?  76  PRO A HD3  1 
ATOM   1233 N  N    . ASN A 1 77  ? 22.57706 24.22020 51.94156 1.000 14.45383 ?  77  ASN A N    1 
ATOM   1234 C  CA   . ASN A 1 77  ? 24.02921 24.26752 51.80000 1.000 13.92658 ?  77  ASN A CA   1 
ATOM   1235 C  C    . ASN A 1 77  ? 24.73112 25.10866 52.86998 1.000 14.37117 ?  77  ASN A C    1 
ATOM   1236 O  O    . ASN A 1 77  ? 25.90205 24.86886 53.13790 1.000 14.99037 ?  77  ASN A O    1 
ATOM   1237 C  CB   . ASN A 1 77  ? 24.40664 24.70299 50.38610 1.000 14.84818 ?  77  ASN A CB   1 
ATOM   1238 C  CG   . ASN A 1 77  ? 23.90556 26.08466 50.10050 1.000 14.67394 ?  77  ASN A CG   1 
ATOM   1239 O  OD1  . ASN A 1 77  ? 24.60199 27.08886 50.41281 1.000 14.73543 ?  77  ASN A OD1  1 
ATOM   1240 N  ND2  . ASN A 1 77  ? 22.70524 26.20584 49.57068 1.000 14.52932 ?  77  ASN A ND2  1 
ATOM   1241 H  H    . ASN A 1 77  ? 22.22479 24.93164 52.27227 1.000 17.35090 ?  77  ASN A H    1 
ATOM   1242 H  HA   . ASN A 1 77  ? 24.36778 23.36952 51.94097 1.000 16.71820 ?  77  ASN A HA   1 
ATOM   1243 H  HB2  . ASN A 1 77  ? 25.37229 24.70082 50.29428 1.000 17.82411 ?  77  ASN A HB2  1 
ATOM   1244 H  HB3  . ASN A 1 77  ? 24.01094 24.09330 49.74376 1.000 17.82411 ?  77  ASN A HB3  1 
ATOM   1245 H  HD21 . ASN A 1 77  ? 22.38951 26.98628 49.39509 1.000 17.44148 ?  77  ASN A HD21 1 
ATOM   1246 H  HD22 . ASN A 1 77  ? 22.23754 25.50450 49.40046 1.000 17.44148 ?  77  ASN A HD22 1 
ATOM   1247 N  N    . GLY A 1 78  ? 24.04784 26.09217 53.47262 1.000 14.60952 ?  78  GLY A N    1 
ATOM   1248 C  CA   . GLY A 1 78  ? 24.63741 26.89280 54.54072 1.000 14.32957 ?  78  GLY A CA   1 
ATOM   1249 C  C    . GLY A 1 78  ? 25.39990 28.11998 54.08631 1.000 14.13911 ?  78  GLY A C    1 
ATOM   1250 O  O    . GLY A 1 78  ? 25.86860 28.89634 54.94101 1.000 16.40723 ?  78  GLY A O    1 
ATOM   1251 H  H    . GLY A 1 78  ? 23.23972 26.31109 53.27611 1.000 17.53773 ?  78  GLY A H    1 
ATOM   1252 H  HA2  . GLY A 1 78  ? 23.92761 27.19004 55.13124 1.000 17.20178 ?  78  GLY A HA2  1 
ATOM   1253 H  HA3  . GLY A 1 78  ? 25.25193 26.33410 55.04185 1.000 17.20178 ?  78  GLY A HA3  1 
ATOM   1254 N  N    . ARG A 1 79  ? 25.48578 28.34990 52.79632 1.000 14.18419 ?  79  ARG A N    1 
ATOM   1255 C  CA   . ARG A 1 79  ? 26.15163 29.48666 52.20398 1.000 13.84876 ?  79  ARG A CA   1 
ATOM   1256 C  C    . ARG A 1 79  ? 25.21661 30.42127 51.47049 1.000 14.15295 ?  79  ARG A C    1 
ATOM   1257 O  O    . ARG A 1 79  ? 25.32590 31.65958 51.59040 1.000 15.20829 ?  79  ARG A O    1 
ATOM   1258 C  CB   . ARG A 1 79  ? 27.22396 28.98063 51.25854 1.000 15.06143 ?  79  ARG A CB   1 
ATOM   1259 C  CG   . ARG A 1 79  ? 28.02255 30.09473 50.57848 1.000 15.53405 ?  79  ARG A CG   1 
ATOM   1260 C  CD   . ARG A 1 79  ? 28.81151 30.96357 51.50522 1.000 15.43752 ?  79  ARG A CD   1 
ATOM   1261 N  NE   . ARG A 1 79  ? 29.74407 31.81228 50.76105 1.000 15.50619 ?  79  ARG A NE   1 
ATOM   1262 C  CZ   . ARG A 1 79  ? 29.71784 33.14538 50.66821 1.000 15.35864 ?  79  ARG A CZ   1 
ATOM   1263 N  NH1  . ARG A 1 79  ? 28.92797 33.89077 51.42073 1.000 16.85452 ?  79  ARG A NH1  1 
ATOM   1264 N  NH2  . ARG A 1 79  ? 30.49461 33.73716 49.78745 1.000 16.08314 ?  79  ARG A NH2  1 
ATOM   1265 H  H    . ARG A 1 79  ? 25.14412 27.82812 52.20419 1.000 17.02734 ?  79  ARG A H    1 
ATOM   1266 H  HA   . ARG A 1 79  ? 26.57874 30.01433 52.89682 1.000 16.62481 ?  79  ARG A HA   1 
ATOM   1267 H  HB2  . ARG A 1 79  ? 27.84799 28.43258 51.75966 1.000 18.08001 ?  79  ARG A HB2  1 
ATOM   1268 H  HB3  . ARG A 1 79  ? 26.80224 28.45187 50.56323 1.000 18.08001 ?  79  ARG A HB3  1 
ATOM   1269 H  HG2  . ARG A 1 79  ? 28.64830 29.68992 49.95762 1.000 18.64717 ?  79  ARG A HG2  1 
ATOM   1270 H  HG3  . ARG A 1 79  ? 27.40414 30.66836 50.09951 1.000 18.64717 ?  79  ARG A HG3  1 
ATOM   1271 H  HD2  . ARG A 1 79  ? 28.20767 31.53506 52.00490 1.000 18.53132 ?  79  ARG A HD2  1 
ATOM   1272 H  HD3  . ARG A 1 79  ? 29.32159 30.40695 52.11422 1.000 18.53132 ?  79  ARG A HD3  1 
ATOM   1273 H  HE   . ARG A 1 79  ? 30.37609 31.41014 50.33864 1.000 18.61373 ?  79  ARG A HE   1 
ATOM   1274 H  HH11 . ARG A 1 79  ? 28.40638 33.52016 51.99536 1.000 20.23173 ?  79  ARG A HH11 1 
ATOM   1275 H  HH12 . ARG A 1 79  ? 28.93545 34.74655 51.33591 1.000 20.23173 ?  79  ARG A HH12 1 
ATOM   1276 H  HH21 . ARG A 1 79  ? 31.00847 33.26716 49.28282 1.000 19.30607 ?  79  ARG A HH21 1 
ATOM   1277 H  HH22 . ARG A 1 79  ? 30.48873 34.59417 49.71607 1.000 19.30607 ?  79  ARG A HH22 1 
ATOM   1278 N  N    . PHE A 1 80  ? 24.25109 29.86137 50.75227 1.000 14.39839 ?  80  PHE A N    1 
ATOM   1279 C  CA   . PHE A 1 80  ? 23.25568 30.60296 50.00581 1.000 14.35978 ?  80  PHE A CA   1 
ATOM   1280 C  C    . PHE A 1 80  ? 21.85891 30.15469 50.46617 1.000 14.18819 ?  80  PHE A C    1 
ATOM   1281 O  O    . PHE A 1 80  ? 21.60820 28.94806 50.63573 1.000 14.75585 ?  80  PHE A O    1 
ATOM   1282 C  CB   . PHE A 1 80  ? 23.40211 30.27940 48.51349 1.000 15.36425 ?  80  PHE A CB   1 
ATOM   1283 C  CG   . PHE A 1 80  ? 24.75212 30.53599 47.92741 1.000 14.72416 ?  80  PHE A CG   1 
ATOM   1284 C  CD1  . PHE A 1 80  ? 25.26464 31.81633 47.96129 1.000 15.21410 ?  80  PHE A CD1  1 
ATOM   1285 C  CD2  . PHE A 1 80  ? 25.48231 29.59723 47.24834 1.000 15.49643 ?  80  PHE A CD2  1 
ATOM   1286 C  CE1  . PHE A 1 80  ? 26.42281 32.13646 47.35106 1.000 15.06503 ?  80  PHE A CE1  1 
ATOM   1287 C  CE2  . PHE A 1 80  ? 26.62128 29.89655 46.67685 1.000 15.94521 ?  80  PHE A CE2  1 
ATOM   1288 C  CZ   . PHE A 1 80  ? 27.11216 31.21386 46.70962 1.000 15.92863 ?  80  PHE A CZ   1 
ATOM   1289 H  H    . PHE A 1 80  ? 24.15076 29.01020 50.68125 1.000 17.28437 ?  80  PHE A H    1 
ATOM   1290 H  HA   . PHE A 1 80  ? 23.35087 31.55693 50.15345 1.000 17.23804 ?  80  PHE A HA   1 
ATOM   1291 H  HB2  . PHE A 1 80  ? 23.20625 29.33811 48.38503 1.000 18.44340 ?  80  PHE A HB2  1 
ATOM   1292 H  HB3  . PHE A 1 80  ? 22.76612 30.82091 48.02035 1.000 18.44340 ?  80  PHE A HB3  1 
ATOM   1293 H  HD1  . PHE A 1 80  ? 24.79736 32.47776 48.41852 1.000 18.26322 ?  80  PHE A HD1  1 
ATOM   1294 H  HD2  . PHE A 1 80  ? 25.16126 28.72624 47.19188 1.000 18.60202 ?  80  PHE A HD2  1 
ATOM   1295 H  HE1  . PHE A 1 80  ? 26.73681 33.01128 47.38258 1.000 18.08434 ?  80  PHE A HE1  1 
ATOM   1296 H  HE2  . PHE A 1 80  ? 27.10965 29.23279 46.24578 1.000 19.14055 ?  80  PHE A HE2  1 
ATOM   1297 H  HZ   . PHE A 1 80  ? 27.91078 31.43086 46.28534 1.000 19.12066 ?  80  PHE A HZ   1 
ATOM   1298 N  N    . LYS A 1 81  ? 20.93648 31.09596 50.60757 1.000 14.17795 ?  81  LYS A N    1 
ATOM   1299 C  CA   . LYS A 1 81  ? 19.57260 30.75380 50.91136 1.000 14.73377 ?  81  LYS A CA   1 
ATOM   1300 C  C    . LYS A 1 81  ? 18.98744 29.96058 49.75005 1.000 15.00352 ?  81  LYS A C    1 
ATOM   1301 O  O    . LYS A 1 81  ? 19.17091 30.36495 48.58935 1.000 15.69710 ?  81  LYS A O    1 
ATOM   1302 C  CB   . LYS A 1 81  ? 18.74430 32.05088 51.06425 1.000 15.99899 ?  81  LYS A CB   1 
ATOM   1303 C  CG   . LYS A 1 81  ? 17.25624 31.76134 51.42175 1.000 16.99215 ?  81  LYS A CG   1 
ATOM   1304 C  CD   . LYS A 1 81  ? 16.55833 32.92486 52.02557 1.000 17.88301 ?  81  LYS A CD   1 
ATOM   1305 C  CE   . LYS A 1 81  ? 16.45799 34.07220 51.10229 1.000 18.45124 ?  81  LYS A CE   1 
ATOM   1306 N  NZ   . LYS A 1 81  ? 15.75857 35.30452 51.66152 1.000 19.16032 ?  81  LYS A NZ   1 
ATOM   1307 H  H    . LYS A 1 81  ? 21.08209 31.94008 50.53102 1.000 17.01984 ?  81  LYS A H    1 
ATOM   1308 H  HA   . LYS A 1 81  ? 19.53571 30.23116 51.72769 1.000 17.68682 ?  81  LYS A HA   1 
ATOM   1309 H  HB2  . LYS A 1 81  ? 19.12664 32.59011 51.77415 1.000 19.20508 ?  81  LYS A HB2  1 
ATOM   1310 H  HB3  . LYS A 1 81  ? 18.76459 32.54121 50.22755 1.000 19.20508 ?  81  LYS A HB3  1 
ATOM   1311 H  HG2  . LYS A 1 81  ? 16.78054 31.51701 50.61248 1.000 20.39688 ?  81  LYS A HG2  1 
ATOM   1312 H  HG3  . LYS A 1 81  ? 17.22270 31.03127 52.05953 1.000 20.39688 ?  81  LYS A HG3  1 
ATOM   1313 H  HD2  . LYS A 1 81  ? 15.65867 32.66045 52.27375 1.000 21.46591 ?  81  LYS A HD2  1 
ATOM   1314 H  HD3  . LYS A 1 81  ? 17.04765 33.21459 52.81140 1.000 21.46591 ?  81  LYS A HD3  1 
ATOM   1315 H  HE2  . LYS A 1 81  ? 17.35516 34.34029 50.84911 1.000 22.14778 ?  81  LYS A HE2  1 
ATOM   1316 H  HE3  . LYS A 1 81  ? 15.96198 33.79076 50.31764 1.000 22.14778 ?  81  LYS A HE3  1 
ATOM   1317 H  HZ1  . LYS A 1 81  ? 15.73598 35.94719 51.04625 1.000 22.99869 ?  81  LYS A HZ1  1 
ATOM   1318 H  HZ2  . LYS A 1 81  ? 14.92485 35.10073 51.89707 1.000 22.99869 ?  81  LYS A HZ2  1 
ATOM   1319 H  HZ3  . LYS A 1 81  ? 16.19560 35.60438 52.37650 1.000 22.99869 ?  81  LYS A HZ3  1 
ATOM   1320 N  N    . PRO A 1 82  ? 18.32929 28.83488 49.98688 1.000 14.91725 ?  82  PRO A N    1 
ATOM   1321 C  CA   . PRO A 1 82  ? 17.84080 28.03524 48.84289 1.000 15.06428 ?  82  PRO A CA   1 
ATOM   1322 C  C    . PRO A 1 82  ? 16.83379 28.78674 48.00177 1.000 14.62894 ?  82  PRO A C    1 
ATOM   1323 O  O    . PRO A 1 82  ? 16.06928 29.63595 48.49009 1.000 15.24107 ?  82  PRO A O    1 
ATOM   1324 C  CB   . PRO A 1 82  ? 17.25250 26.77633 49.49834 1.000 15.79925 ?  82  PRO A CB   1 
ATOM   1325 C  CG   . PRO A 1 82  ? 17.88849 26.65497 50.77533 1.000 16.41417 ?  82  PRO A CG   1 
ATOM   1326 C  CD   . PRO A 1 82  ? 18.23920 28.07386 51.27662 1.000 15.62026 ?  82  PRO A CD   1 
ATOM   1327 H  HA   . PRO A 1 82  ? 18.58025 27.77420 48.27195 1.000 18.08344 ?  82  PRO A HA   1 
ATOM   1328 H  HB2  . PRO A 1 82  ? 16.29378 26.88153 49.60175 1.000 18.96540 ?  82  PRO A HB2  1 
ATOM   1329 H  HB3  . PRO A 1 82  ? 17.44363 26.00253 48.94554 1.000 18.96540 ?  82  PRO A HB3  1 
ATOM   1330 H  HG2  . PRO A 1 82  ? 17.27905 26.22247 51.39373 1.000 19.70331 ?  82  PRO A HG2  1 
ATOM   1331 H  HG3  . PRO A 1 82  ? 18.69514 26.12490 50.67918 1.000 19.70331 ?  82  PRO A HG3  1 
ATOM   1332 H  HD2  . PRO A 1 82  ? 17.53889 28.42876 51.84628 1.000 18.75061 ?  82  PRO A HD2  1 
ATOM   1333 H  HD3  . PRO A 1 82  ? 19.08640 28.08065 51.74897 1.000 18.75061 ?  82  PRO A HD3  1 
ATOM   1334 N  N    . ASN A 1 83  ? 16.79948 28.45021 46.72828 1.000 14.76291 ?  83  ASN A N    1 
ATOM   1335 C  CA   . ASN A 1 83  ? 15.76258 28.90773 45.82367 1.000 14.11397 ?  83  ASN A CA   1 
ATOM   1336 C  C    . ASN A 1 83  ? 15.69129 30.40634 45.68053 1.000 14.79799 ?  83  ASN A C    1 
ATOM   1337 O  O    . ASN A 1 83  ? 14.61582 30.94470 45.40749 1.000 15.72785 ?  83  ASN A O    1 
ATOM   1338 C  CB   . ASN A 1 83  ? 14.39489 28.32733 46.23149 1.000 15.86285 ?  83  ASN A CB   1 
ATOM   1339 C  CG   . ASN A 1 83  ? 14.40865 26.82063 46.14632 1.000 17.45120 ?  83  ASN A CG   1 
ATOM   1340 O  OD1  . ASN A 1 83  ? 14.74988 26.27538 45.07383 1.000 19.39164 ?  83  ASN A OD1  1 
ATOM   1341 N  ND2  . ASN A 1 83  ? 14.03400 26.15322 47.22047 1.000 19.18760 ?  83  ASN A ND2  1 
ATOM   1342 H  H    . ASN A 1 83  ? 17.38254 27.94255 46.35155 1.000 17.72180 ?  83  ASN A H    1 
ATOM   1343 H  HA   . ASN A 1 83  ? 15.99057 28.58236 44.93877 1.000 16.94307 ?  83  ASN A HA   1 
ATOM   1344 H  HB2  . ASN A 1 83  ? 14.19380 28.58305 47.14531 1.000 19.04173 ?  83  ASN A HB2  1 
ATOM   1345 H  HB3  . ASN A 1 83  ? 13.70882 28.66405 45.63414 1.000 19.04173 ?  83  ASN A HB3  1 
ATOM   1346 H  HD21 . ASN A 1 83  ? 14.02808 25.29328 47.21209 1.000 23.03142 ?  83  ASN A HD21 1 
ATOM   1347 H  HD22 . ASN A 1 83  ? 13.79564 26.57797 47.92925 1.000 23.03142 ?  83  ASN A HD22 1 
ATOM   1348 N  N    . THR A 1 84  ? 16.82384 31.06823 45.77322 1.000 14.22314 ?  84  THR A N    1 
ATOM   1349 C  CA   . THR A 1 84  ? 16.87822 32.53049 45.81744 1.000 13.91623 ?  84  THR A CA   1 
ATOM   1350 C  C    . THR A 1 84  ? 17.90966 33.03612 44.81623 1.000 13.76223 ?  84  THR A C    1 
ATOM   1351 O  O    . THR A 1 84  ? 19.01747 32.51083 44.73948 1.000 14.65081 ?  84  THR A O    1 
ATOM   1352 C  CB   . THR A 1 84  ? 17.34483 32.94073 47.21592 1.000 15.54175 ?  84  THR A CB   1 
ATOM   1353 O  OG1  . THR A 1 84  ? 16.38569 32.47748 48.19056 1.000 15.50980 ?  84  THR A OG1  1 
ATOM   1354 C  CG2  . THR A 1 84  ? 17.49121 34.47577 47.36855 1.000 15.32611 ?  84  THR A CG2  1 
ATOM   1355 H  H    . THR A 1 84  ? 17.59661 30.69298 45.81347 1.000 17.07407 ?  84  THR A H    1 
ATOM   1356 H  HA   . THR A 1 84  ? 16.01476 32.91017 45.59119 1.000 16.70577 ?  84  THR A HA   1 
ATOM   1357 H  HB   . THR A 1 84  ? 18.21809 32.54707 47.36874 1.000 18.65640 ?  84  THR A HB   1 
ATOM   1358 H  HG1  . THR A 1 84  ? 16.33456 31.63936 48.16747 1.000 18.61806 ?  84  THR A HG1  1 
ATOM   1359 H  HG21 . THR A 1 84  ? 17.62692 34.70498 48.30126 1.000 18.39763 ?  84  THR A HG21 1 
ATOM   1360 H  HG22 . THR A 1 84  ? 18.25100 34.78942 46.85354 1.000 18.39763 ?  84  THR A HG22 1 
ATOM   1361 H  HG23 . THR A 1 84  ? 16.68972 34.91887 47.04889 1.000 18.39763 ?  84  THR A HG23 1 
ATOM   1362 N  N    . ARG A 1 85  ? 17.54466 34.06390 44.04055 1.000 13.88239 ?  85  ARG A N    1 
ATOM   1363 C  CA   . ARG A 1 85  ? 18.51241 34.66608 43.13299 1.000 13.65258 ?  85  ARG A CA   1 
ATOM   1364 C  C    . ARG A 1 85  ? 19.73404 35.19471 43.88154 1.000 13.26829 ?  85  ARG A C    1 
ATOM   1365 O  O    . ARG A 1 85  ? 19.62452 35.93624 44.85413 1.000 14.46248 ?  85  ARG A O    1 
ATOM   1366 C  CB   . ARG A 1 85  ? 17.88081 35.81388 42.37379 1.000 15.62337 ?  85  ARG A CB   1 
ATOM   1367 C  CG   . ARG A 1 85  ? 16.79988 35.32566 41.38078 1.000 16.68275 ?  85  ARG A CG   1 
ATOM   1368 C  CD   . ARG A 1 85  ? 15.99467 36.50961 40.79240 1.000 17.82846 ?  85  ARG A CD   1 
ATOM   1369 N  NE   . ARG A 1 85  ? 16.86040 37.57390 40.33283 1.000 19.13097 ?  85  ARG A NE   1 
ATOM   1370 C  CZ   . ARG A 1 85  ? 16.99514 38.79122 40.83019 1.000 19.00064 ?  85  ARG A CZ   1 
ATOM   1371 N  NH1  . ARG A 1 85  ? 16.15171 39.26442 41.73310 1.000 21.69040 ?  85  ARG A NH1  1 
ATOM   1372 N  NH2  . ARG A 1 85  ? 18.00575 39.54915 40.39862 1.000 19.58894 ?  85  ARG A NH2  1 
ATOM   1373 H  H    . ARG A 1 85  ? 16.76134 34.41852 44.02500 1.000 16.66517 ?  85  ARG A H    1 
ATOM   1374 H  HA   . ARG A 1 85  ? 18.79910 33.97985 42.51025 1.000 16.38939 ?  85  ARG A HA   1 
ATOM   1375 H  HB2  . ARG A 1 85  ? 17.46226 36.42089 43.00408 1.000 18.75435 ?  85  ARG A HB2  1 
ATOM   1376 H  HB3  . ARG A 1 85  ? 18.56728 36.27935 41.87081 1.000 18.75435 ?  85  ARG A HB3  1 
ATOM   1377 H  HG2  . ARG A 1 85  ? 17.22594 34.85291 40.64875 1.000 20.02561 ?  85  ARG A HG2  1 
ATOM   1378 H  HG3  . ARG A 1 85  ? 16.18264 34.73625 41.84178 1.000 20.02561 ?  85  ARG A HG3  1 
ATOM   1379 H  HD2  . ARG A 1 85  ? 15.47128 36.19684 40.03799 1.000 21.40045 ?  85  ARG A HD2  1 
ATOM   1380 H  HD3  . ARG A 1 85  ? 15.40852 36.86909 41.47658 1.000 21.40045 ?  85  ARG A HD3  1 
ATOM   1381 H  HE   . ARG A 1 85  ? 17.34939 37.39136 39.64934 1.000 22.96347 ?  85  ARG A HE   1 
ATOM   1382 H  HH11 . ARG A 1 85  ? 15.49874 38.77724 42.00857 1.000 26.03479 ?  85  ARG A HH11 1 
ATOM   1383 H  HH12 . ARG A 1 85  ? 16.25646 40.05918 42.04452 1.000 26.03479 ?  85  ARG A HH12 1 
ATOM   1384 H  HH21 . ARG A 1 85  ? 18.55199 39.24262 39.80933 1.000 23.51303 ?  85  ARG A HH21 1 
ATOM   1385 H  HH22 . ARG A 1 85  ? 18.11058 40.34397 40.70987 1.000 23.51303 ?  85  ARG A HH22 1 
ATOM   1386 N  N    . LEU A 1 86  ? 20.91107 34.81878 43.41567 1.000 13.49208 ?  86  LEU A N    1 
ATOM   1387 C  CA   . LEU A 1 86  ? 22.15892 35.15981 44.08054 1.000 13.09866 ?  86  LEU A CA   1 
ATOM   1388 C  C    . LEU A 1 86  ? 22.84805 36.30361 43.34998 1.000 13.64591 ?  86  LEU A C    1 
ATOM   1389 O  O    . LEU A 1 86  ? 23.01204 36.30649 42.12068 1.000 14.42866 ?  86  LEU A O    1 
ATOM   1390 C  CB   . LEU A 1 86  ? 23.06721 33.91586 44.10194 1.000 14.90936 ?  86  LEU A CB   1 
ATOM   1391 C  CG   . LEU A 1 86  ? 22.48252 32.63634 44.74374 1.000 14.43181 ?  86  LEU A CG   1 
ATOM   1392 C  CD1  . LEU A 1 86  ? 23.47995 31.47910 44.63712 1.000 14.73808 ?  86  LEU A CD1  1 
ATOM   1393 C  CD2  . LEU A 1 86  ? 22.06969 32.96567 46.18434 1.000 15.48607 ?  86  LEU A CD2  1 
ATOM   1394 H  H    . LEU A 1 86  ? 21.01741 34.35461 42.69954 1.000 16.19680 ?  86  LEU A H    1 
ATOM   1395 H  HA   . LEU A 1 86  ? 21.98827 35.45883 44.98739 1.000 15.72469 ?  86  LEU A HA   1 
ATOM   1396 H  HB2  . LEU A 1 86  ? 23.29397 33.69516 43.18501 1.000 17.89754 ?  86  LEU A HB2  1 
ATOM   1397 H  HB3  . LEU A 1 86  ? 23.87031 34.14028 44.59750 1.000 17.89754 ?  86  LEU A HB3  1 
ATOM   1398 H  HG   . LEU A 1 86  ? 21.68937 32.33024 44.27670 1.000 17.32447 ?  86  LEU A HG   1 
ATOM   1399 H  HD11 . LEU A 1 86  ? 23.09405 30.69055 45.04964 1.000 17.69200 ?  86  LEU A HD11 1 
ATOM   1400 H  HD12 . LEU A 1 86  ? 23.66392 31.30602 43.70058 1.000 17.69200 ?  86  LEU A HD12 1 
ATOM   1401 H  HD13 . LEU A 1 86  ? 24.29891 31.72484 45.09517 1.000 17.69200 ?  86  LEU A HD13 1 
ATOM   1402 H  HD21 . LEU A 1 86  ? 21.73967 32.15920 46.61048 1.000 18.58958 ?  86  LEU A HD21 1 
ATOM   1403 H  HD22 . LEU A 1 86  ? 22.84221 33.30152 46.66529 1.000 18.58958 ?  86  LEU A HD22 1 
ATOM   1404 H  HD23 . LEU A 1 86  ? 21.37229 33.63962 46.16677 1.000 18.58958 ?  86  LEU A HD23 1 
ATOM   1405 N  N    . CYS A 1 87  ? 23.31460 37.29401 44.13399 1.000 13.71063 ?  87  CYS A N    1 
ATOM   1406 C  CA   . CYS A 1 87  ? 23.95651 38.47213 43.58265 1.000 13.27698 ?  87  CYS A CA   1 
ATOM   1407 C  C    . CYS A 1 87  ? 25.44537 38.19600 43.40682 1.000 13.45726 ?  87  CYS A C    1 
ATOM   1408 O  O    . CYS A 1 87  ? 26.21186 38.20333 44.36230 1.000 15.23883 ?  87  CYS A O    1 
ATOM   1409 C  CB   . CYS A 1 87  ? 23.67034 39.69121 44.49737 1.000 13.67937 ?  87  CYS A CB   1 
ATOM   1410 S  SG   . CYS A 1 87  ? 24.62376 41.14612 44.01045 1.000 14.32449 ?  87  CYS A SG   1 
ATOM   1411 H  H    . CYS A 1 87  ? 23.26429 37.29397 44.99251 1.000 16.45906 ?  87  CYS A H    1 
ATOM   1412 H  HA   . CYS A 1 87  ? 23.60684 38.65987 42.69756 1.000 15.93868 ?  87  CYS A HA   1 
ATOM   1413 H  HB2  . CYS A 1 87  ? 22.72792 39.91457 44.44390 1.000 16.42155 ?  87  CYS A HB2  1 
ATOM   1414 H  HB3  . CYS A 1 87  ? 23.90656 39.46578 45.41076 1.000 16.42155 ?  87  CYS A HB3  1 
ATOM   1415 H  HG   . CYS A 1 87  ? 24.67476 41.90765 44.93644 1.000 17.19569 ?  87  CYS A HG   1 
ATOM   1416 N  N    . LEU A 1 88  ? 25.81572 37.88810 42.17419 1.000 14.42848 ?  88  LEU A N    1 
ATOM   1417 C  CA   . LEU A 1 88  ? 27.16390 37.53584 41.77432 1.000 14.29722 ?  88  LEU A CA   1 
ATOM   1418 C  C    . LEU A 1 88  ? 27.60135 38.47652 40.65077 1.000 14.40445 ?  88  LEU A C    1 
ATOM   1419 O  O    . LEU A 1 88  ? 26.76445 39.03612 39.93273 1.000 15.12776 ?  88  LEU A O    1 
ATOM   1420 C  CB   . LEU A 1 88  ? 27.23955 36.06428 41.30320 1.000 14.94572 ?  88  LEU A CB   1 
ATOM   1421 C  CG   . LEU A 1 88  ? 26.76104 35.04823 42.33570 1.000 16.17298 ?  88  LEU A CG   1 
ATOM   1422 C  CD1  . LEU A 1 88  ? 26.47745 33.66685 41.72650 1.000 17.15951 ?  88  LEU A CD1  1 
ATOM   1423 C  CD2  . LEU A 1 88  ? 27.76392 34.90223 43.48746 1.000 17.94097 ?  88  LEU A CD2  1 
ATOM   1424 H  H    . LEU A 1 88  ? 25.26799 37.87600 41.51128 1.000 17.32048 ?  88  LEU A H    1 
ATOM   1425 H  HA   . LEU A 1 88  ? 27.77538 37.63584 42.52064 1.000 17.16297 ?  88  LEU A HA   1 
ATOM   1426 H  HB2  . LEU A 1 88  ? 26.68587 35.96404 40.51307 1.000 17.94117 ?  88  LEU A HB2  1 
ATOM   1427 H  HB3  . LEU A 1 88  ? 28.16249 35.85515 41.09027 1.000 17.94117 ?  88  LEU A HB3  1 
ATOM   1428 H  HG   . LEU A 1 88  ? 25.92410 35.39072 42.68660 1.000 19.41388 ?  88  LEU A HG   1 
ATOM   1429 H  HD11 . LEU A 1 88  ? 26.20472 33.06026 42.43260 1.000 20.59771 ?  88  LEU A HD11 1 
ATOM   1430 H  HD12 . LEU A 1 88  ? 25.76814 33.75073 41.07019 1.000 20.59771 ?  88  LEU A HD12 1 
ATOM   1431 H  HD13 . LEU A 1 88  ? 27.28457 33.33762 41.30100 1.000 20.59771 ?  88  LEU A HD13 1 
ATOM   1432 H  HD21 . LEU A 1 88  ? 27.43529 34.23455 44.10963 1.000 21.53547 ?  88  LEU A HD21 1 
ATOM   1433 H  HD22 . LEU A 1 88  ? 28.62073 34.62509 43.12692 1.000 21.53547 ?  88  LEU A HD22 1 
ATOM   1434 H  HD23 . LEU A 1 88  ? 27.85508 35.75689 43.93707 1.000 21.53547 ?  88  LEU A HD23 1 
ATOM   1435 N  N    . SER A 1 89  ? 28.92250 38.62979 40.47944 1.000 14.50346 ?  89  SER A N    1 
ATOM   1436 C  CA   . SER A 1 89  ? 29.40043 39.52468 39.44203 1.000 16.24610 ?  89  SER A CA   1 
ATOM   1437 C  C    . SER A 1 89  ? 28.87632 39.14974 38.05999 1.000 15.04546 ?  89  SER A C    1 
ATOM   1438 O  O    . SER A 1 89  ? 28.63817 40.04821 37.20215 1.000 16.36820 ?  89  SER A O    1 
ATOM   1439 C  CB   . SER A 1 89  ? 30.91087 39.51178 39.43331 1.000 19.52237 ?  89  SER A CB   1 
ATOM   1440 O  OG   . SER A 1 89  ? 31.38142 40.05403 40.62596 1.000 23.26097 ?  89  SER A OG   1 
ATOM   1441 H  H    . SER A 1 89  ? 29.53430 38.23710 40.93888 1.000 17.41045 ?  89  SER A H    1 
ATOM   1442 H  HA   . SER A 1 89  ? 29.08589 40.42070 39.63983 1.000 19.50162 ?  89  SER A HA   1 
ATOM   1443 H  HB2  . SER A 1 89  ? 31.22468 38.59781 39.34909 1.000 23.43315 ?  89  SER A HB2  1 
ATOM   1444 H  HB3  . SER A 1 89  ? 31.23321 40.04317 38.68858 1.000 23.43315 ?  89  SER A HB3  1 
ATOM   1445 H  HG   . SER A 1 89  ? 31.11476 40.84653 40.70619 1.000 27.91947 ?  89  SER A HG   1 
ATOM   1446 N  N    . MET A 1 90  ? 28.70081 37.84385 37.80059 1.000 15.21153 ?  90  MET A N    1 
ATOM   1447 C  CA   . MET A 1 90  ? 28.18489 37.36256 36.51588 1.000 15.16074 ?  90  MET A CA   1 
ATOM   1448 C  C    . MET A 1 90  ? 26.79777 36.81180 36.89208 1.000 15.40610 ?  90  MET A C    1 
ATOM   1449 O  O    . MET A 1 90  ? 26.67381 35.62776 37.24130 1.000 16.33381 ?  90  MET A O    1 
ATOM   1450 C  CB   . MET A 1 90  ? 29.12162 36.25407 35.95063 1.000 16.26077 ?  90  MET A CB   1 
ATOM   1451 C  CG   . MET A 1 90  ? 30.46633 36.76442 35.68709 1.000 15.84231 ?  90  MET A CG   1 
ATOM   1452 S  SD   . MET A 1 90  ? 31.57046 35.51915 34.98480 1.000 18.42143 ?  90  MET A SD   1 
ATOM   1453 C  CE   . MET A 1 90  ? 32.01646 34.61670 36.43558 1.000 17.69815 ?  90  MET A CE   1 
ATOM   1454 H  H    . MET A 1 90  ? 28.87646 37.21571 38.36111 1.000 18.26013 ?  90  MET A H    1 
ATOM   1455 H  HA   . MET A 1 90  ? 28.12653 38.05822 35.84242 1.000 18.19919 ?  90  MET A HA   1 
ATOM   1456 H  HB2  . MET A 1 90  ? 29.19024 35.53361 36.59649 1.000 19.51923 ?  90  MET A HB2  1 
ATOM   1457 H  HB3  . MET A 1 90  ? 28.75413 35.91911 35.11777 1.000 19.51923 ?  90  MET A HB3  1 
ATOM   1458 H  HG2  . MET A 1 90  ? 30.40630 37.49970 35.05727 1.000 19.01707 ?  90  MET A HG2  1 
ATOM   1459 H  HG3  . MET A 1 90  ? 30.85523 37.07248 36.52061 1.000 19.01707 ?  90  MET A HG3  1 
ATOM   1460 H  HE1  . MET A 1 90  ? 32.56103 33.85598 36.17935 1.000 21.24408 ?  90  MET A HE1  1 
ATOM   1461 H  HE2  . MET A 1 90  ? 32.51850 35.19849 37.02751 1.000 21.24408 ?  90  MET A HE2  1 
ATOM   1462 H  HE3  . MET A 1 90  ? 31.20915 34.31145 36.87826 1.000 21.24408 ?  90  MET A HE3  1 
ATOM   1463 N  N    . SER A 1 91  ? 25.77477 37.65299 36.90749 1.000 15.20633 ?  91  SER A N    1 
ATOM   1464 C  CA   . SER A 1 91  ? 24.43150 37.28768 37.30511 1.000 15.04986 ?  91  SER A CA   1 
ATOM   1465 C  C    . SER A 1 91  ? 23.48349 38.41865 36.94003 1.000 15.06583 ?  91  SER A C    1 
ATOM   1466 O  O    . SER A 1 91  ? 23.90281 39.53351 36.60860 1.000 15.47483 ?  91  SER A O    1 
ATOM   1467 C  CB   . SER A 1 91  ? 24.26065 37.01604 38.78316 1.000 15.45271 ?  91  SER A CB   1 
ATOM   1468 O  OG   . SER A 1 91  ? 24.22692 38.26476 39.51239 1.000 15.57746 ?  91  SER A OG   1 
ATOM   1469 H  H    . SER A 1 91  ? 25.83928 38.48000 36.68057 1.000 18.25389 ?  91  SER A H    1 
ATOM   1470 H  HA   . SER A 1 91  ? 24.22779 36.47880 36.81002 1.000 18.06613 ?  91  SER A HA   1 
ATOM   1471 H  HB2  . SER A 1 91  ? 23.42785 36.53977 38.92636 1.000 18.54955 ?  91  SER A HB2  1 
ATOM   1472 H  HB3  . SER A 1 91  ? 25.00663 36.48205 39.09824 1.000 18.54955 ?  91  SER A HB3  1 
ATOM   1473 H  HG   . SER A 1 91  ? 24.94493 38.68490 39.39603 1.000 18.69926 ?  91  SER A HG   1 
ATOM   1474 N  N    . ASP A 1 92  ? 22.19475 38.12221 37.04481 1.000 14.80986 ?  92  ASP A N    1 
ATOM   1475 C  CA   . ASP A 1 92  ? 21.15498 39.10349 36.69745 1.000 14.90379 ?  92  ASP A CA   1 
ATOM   1476 C  C    . ASP A 1 92  ? 21.05110 40.29007 37.62683 1.000 14.13802 ?  92  ASP A C    1 
ATOM   1477 O  O    . ASP A 1 92  ? 20.33530 41.23829 37.27441 1.000 15.51776 ?  92  ASP A O    1 
ATOM   1478 C  CB   . ASP A 1 92  ? 19.79792 38.39068 36.51516 1.000 15.26084 ?  92  ASP A CB   1 
ATOM   1479 C  CG   . ASP A 1 92  ? 19.22317 37.82033 37.78293 1.000 16.31999 ?  92  ASP A CG   1 
ATOM   1480 O  OD1  . ASP A 1 92  ? 19.85628 37.86821 38.80144 1.000 16.45604 ?  92  ASP A OD1  1 
ATOM   1481 O  OD2  . ASP A 1 92  ? 18.07687 37.33256 37.68460 1.000 19.76635 -1 92  ASP A OD2  1 
ATOM   1482 H  H    . ASP A 1 92  ? 21.88909 37.36440 37.31295 1.000 17.77813 ?  92  ASP A H    1 
ATOM   1483 H  HA   . ASP A 1 92  ? 21.39144 39.49323 35.84124 1.000 17.89085 ?  92  ASP A HA   1 
ATOM   1484 H  HB2  . ASP A 1 92  ? 19.15728 39.02855 36.16359 1.000 18.31931 ?  92  ASP A HB2  1 
ATOM   1485 H  HB3  . ASP A 1 92  ? 19.91388 37.65810 35.89004 1.000 18.31931 ?  92  ASP A HB3  1 
ATOM   1486 N  N    . TYR A 1 93  ? 21.78666 40.32779 38.72503 1.000 14.34566 ?  93  TYR A N    1 
ATOM   1487 C  CA   . TYR A 1 93  ? 21.90611 41.54598 39.50498 1.000 13.92690 ?  93  TYR A CA   1 
ATOM   1488 C  C    . TYR A 1 93  ? 22.80405 42.56530 38.84959 1.000 13.83754 ?  93  TYR A C    1 
ATOM   1489 O  O    . TYR A 1 93  ? 22.75619 43.76274 39.22746 1.000 15.63419 ?  93  TYR A O    1 
ATOM   1490 C  CB   . TYR A 1 93  ? 22.41145 41.24215 40.91371 1.000 13.88548 ?  93  TYR A CB   1 
ATOM   1491 C  CG   . TYR A 1 93  ? 21.44154 40.50984 41.77371 1.000 13.78184 ?  93  TYR A CG   1 
ATOM   1492 C  CD1  . TYR A 1 93  ? 21.33028 39.11702 41.73958 1.000 14.34997 ?  93  TYR A CD1  1 
ATOM   1493 C  CD2  . TYR A 1 93  ? 20.68913 41.20914 42.73236 1.000 14.36037 ?  93  TYR A CD2  1 
ATOM   1494 C  CE1  . TYR A 1 93  ? 20.49661 38.43096 42.62026 1.000 14.85445 ?  93  TYR A CE1  1 
ATOM   1495 C  CE2  . TYR A 1 93  ? 19.84298 40.52071 43.59853 1.000 14.22443 ?  93  TYR A CE2  1 
ATOM   1496 C  CZ   . TYR A 1 93  ? 19.75149 39.15343 43.53949 1.000 14.35868 ?  93  TYR A CZ   1 
ATOM   1497 O  OH   . TYR A 1 93  ? 18.95637 38.52313 44.44970 1.000 15.12233 ?  93  TYR A OH   1 
ATOM   1498 H  H    . TYR A 1 93  ? 22.22778 39.66071 39.04128 1.000 17.22109 ?  93  TYR A H    1 
ATOM   1499 H  HA   . TYR A 1 93  ? 21.02134 41.93453 39.58929 1.000 16.71859 ?  93  TYR A HA   1 
ATOM   1500 H  HB2  . TYR A 1 93  ? 23.21081 40.69709 40.84423 1.000 16.66888 ?  93  TYR A HB2  1 
ATOM   1501 H  HB3  . TYR A 1 93  ? 22.61899 42.08069 41.35493 1.000 16.66888 ?  93  TYR A HB3  1 
ATOM   1502 H  HD1  . TYR A 1 93  ? 21.82414 38.63707 41.11456 1.000 17.22627 ?  93  TYR A HD1  1 
ATOM   1503 H  HD2  . TYR A 1 93  ? 20.75631 42.13499 42.78878 1.000 17.23875 ?  93  TYR A HD2  1 
ATOM   1504 H  HE1  . TYR A 1 93  ? 20.44086 37.50307 42.59193 1.000 17.83165 ?  93  TYR A HE1  1 
ATOM   1505 H  HE2  . TYR A 1 93  ? 19.33679 40.99117 44.22090 1.000 17.07562 ?  93  TYR A HE2  1 
ATOM   1506 H  HH   . TYR A 1 93  ? 19.02857 37.69040 44.36635 1.000 18.15309 ?  93  TYR A HH   1 
ATOM   1507 N  N    . HIS A 1 94  ? 23.62480 42.16667 37.89446 1.000 14.58225 ?  94  HIS A N    1 
ATOM   1508 C  CA   . HIS A 1 94  ? 24.59062 43.05344 37.23248 1.000 15.03362 ?  94  HIS A CA   1 
ATOM   1509 C  C    . HIS A 1 94  ? 24.47407 43.02586 35.72109 1.000 14.52980 ?  94  HIS A C    1 
ATOM   1510 O  O    . HIS A 1 94  ? 25.41011 42.65796 35.00554 1.000 15.64429 ?  94  HIS A O    1 
ATOM   1511 C  CB   . HIS A 1 94  ? 26.01572 42.77343 37.71763 1.000 15.44486 ?  94  HIS A CB   1 
ATOM   1512 C  CG   . HIS A 1 94  ? 26.13792 43.08336 39.20100 1.000 15.58496 ?  94  HIS A CG   1 
ATOM   1513 N  ND1  . HIS A 1 94  ? 26.11913 44.36340 39.73461 1.000 16.72895 ?  94  HIS A ND1  1 
ATOM   1514 C  CD2  . HIS A 1 94  ? 26.08652 42.23115 40.27395 1.000 15.43353 ?  94  HIS A CD2  1 
ATOM   1515 C  CE1  . HIS A 1 94  ? 26.10062 44.28077 41.05867 1.000 16.00203 ?  94  HIS A CE1  1 
ATOM   1516 N  NE2  . HIS A 1 94  ? 26.04853 43.00720 41.39587 1.000 16.89467 ?  94  HIS A NE2  1 
ATOM   1517 H  H    . HIS A 1 94  ? 23.64880 41.36054 37.59583 1.000 17.50500 ?  94  HIS A H    1 
ATOM   1518 H  HA   . HIS A 1 94  ? 24.36233 43.96233 37.48291 1.000 18.04664 ?  94  HIS A HA   1 
ATOM   1519 H  HB2  . HIS A 1 94  ? 26.22913 41.83769 37.57713 1.000 18.54014 ?  94  HIS A HB2  1 
ATOM   1520 H  HB3  . HIS A 1 94  ? 26.64084 43.33300 37.23079 1.000 18.54014 ?  94  HIS A HB3  1 
ATOM   1521 H  HD2  . HIS A 1 94  ? 26.07898 41.30170 40.24303 1.000 18.52654 ?  94  HIS A HD2  1 
ATOM   1522 H  HE1  . HIS A 1 94  ? 26.12093 44.99927 41.64880 1.000 19.20874 ?  94  HIS A HE1  1 
ATOM   1523 H  HE2  . HIS A 1 94  ? 25.99820 42.71028 42.20142 1.000 20.27991 ?  94  HIS A HE2  1 
ATOM   1524 N  N    . PRO A 1 95  ? 23.32827 43.45396 35.20822 1.000 14.65477 ?  95  PRO A N    1 
ATOM   1525 C  CA   . PRO A 1 95  ? 23.17324 43.54457 33.76004 1.000 16.10230 ?  95  PRO A CA   1 
ATOM   1526 C  C    . PRO A 1 95  ? 24.06731 44.62880 33.13821 1.000 16.37297 ?  95  PRO A C    1 
ATOM   1527 O  O    . PRO A 1 95  ? 24.37963 44.61896 31.94853 1.000 17.89610 ?  95  PRO A O    1 
ATOM   1528 C  CB   . PRO A 1 95  ? 21.68144 43.84115 33.59132 1.000 16.92391 ?  95  PRO A CB   1 
ATOM   1529 C  CG   . PRO A 1 95  ? 21.30392 44.59264 34.81340 1.000 17.08972 ?  95  PRO A CG   1 
ATOM   1530 C  CD   . PRO A 1 95  ? 22.13467 43.92852 35.93924 1.000 16.38278 ?  95  PRO A CD   1 
ATOM   1531 H  HA   . PRO A 1 95  ? 23.36186 42.69615 33.32933 1.000 19.32906 ?  95  PRO A HA   1 
ATOM   1532 H  HB2  . PRO A 1 95  ? 21.53846 44.37689 32.79543 1.000 20.31499 ?  95  PRO A HB2  1 
ATOM   1533 H  HB3  . PRO A 1 95  ? 21.18425 43.01082 33.52605 1.000 20.31499 ?  95  PRO A HB3  1 
ATOM   1534 H  HG2  . PRO A 1 95  ? 21.53540 45.52938 34.71421 1.000 20.51397 ?  95  PRO A HG2  1 
ATOM   1535 H  HG3  . PRO A 1 95  ? 20.35278 44.50186 34.98073 1.000 20.51397 ?  95  PRO A HG3  1 
ATOM   1536 H  HD2  . PRO A 1 95  ? 22.37669 44.57374 36.62189 1.000 19.66564 ?  95  PRO A HD2  1 
ATOM   1537 H  HD3  . PRO A 1 95  ? 21.65234 43.18787 36.33887 1.000 19.66564 ?  95  PRO A HD3  1 
ATOM   1538 N  N    . ASP A 1 96  ? 24.47039 45.59994 33.99342 1.000 16.11169 ?  96  ASP A N    1 
ATOM   1539 C  CA   . ASP A 1 96  ? 25.29002 46.74448 33.61781 1.000 16.97278 ?  96  ASP A CA   1 
ATOM   1540 C  C    . ASP A 1 96  ? 26.67557 46.33625 33.16783 1.000 17.29434 ?  96  ASP A C    1 
ATOM   1541 O  O    . ASP A 1 96  ? 27.20675 46.89362 32.18064 1.000 18.83770 ?  96  ASP A O    1 
ATOM   1542 C  CB   . ASP A 1 96  ? 25.38420 47.74573 34.76889 1.000 17.30888 ?  96  ASP A CB   1 
ATOM   1543 C  CG   . ASP A 1 96  ? 25.77429 47.17199 36.14398 1.000 17.86723 ?  96  ASP A CG   1 
ATOM   1544 O  OD1  . ASP A 1 96  ? 25.68955 45.96760 36.43254 1.000 17.74741 ?  96  ASP A OD1  1 
ATOM   1545 O  OD2  . ASP A 1 96  ? 26.10531 47.98593 37.04310 1.000 18.85540 -1 96  ASP A OD2  1 
ATOM   1546 H  H    . ASP A 1 96  ? 24.26734 45.60793 34.82906 1.000 19.34034 ?  96  ASP A H    1 
ATOM   1547 H  HA   . ASP A 1 96  ? 24.85175 47.18170 32.87104 1.000 20.37363 ?  96  ASP A HA   1 
ATOM   1548 H  HB2  . ASP A 1 96  ? 26.05238 48.40983 34.53779 1.000 20.77696 ?  96  ASP A HB2  1 
ATOM   1549 H  HB3  . ASP A 1 96  ? 24.51769 48.16914 34.87273 1.000 20.77696 ?  96  ASP A HB3  1 
ATOM   1550 N  N    . THR A 1 97  ? 27.25623 45.33448 33.79433 1.000 16.94025 ?  97  THR A N    1 
ATOM   1551 C  CA   . THR A 1 97  ? 28.60345 44.90509 33.45606 1.000 17.33388 ?  97  THR A CA   1 
ATOM   1552 C  C    . THR A 1 97  ? 28.63621 43.51100 32.85004 1.000 16.91511 ?  97  THR A C    1 
ATOM   1553 O  O    . THR A 1 97  ? 29.71557 42.91086 32.73051 1.000 18.62178 ?  97  THR A O    1 
ATOM   1554 C  CB   . THR A 1 97  ? 29.49480 44.99968 34.70064 1.000 17.71113 ?  97  THR A CB   1 
ATOM   1555 O  OG1  . THR A 1 97  ? 28.81234 44.43641 35.82949 1.000 17.76504 ?  97  THR A OG1  1 
ATOM   1556 C  CG2  . THR A 1 97  ? 29.81561 46.47628 35.04330 1.000 17.89243 ?  97  THR A CG2  1 
ATOM   1557 H  H    . THR A 1 97  ? 26.88955 44.88061 34.42612 1.000 20.33461 ?  97  THR A H    1 
ATOM   1558 H  HA   . THR A 1 97  ? 28.96940 45.50045 32.78336 1.000 20.80696 ?  97  THR A HA   1 
ATOM   1559 H  HB   . THR A 1 97  ? 30.32041 44.52239 34.52329 1.000 21.25966 ?  97  THR A HB   1 
ATOM   1560 H  HG1  . THR A 1 97  ? 28.14302 44.90527 36.02385 1.000 21.32435 ?  97  THR A HG1  1 
ATOM   1561 H  HG21 . THR A 1 97  ? 30.38822 46.51856 35.82511 1.000 21.47721 ?  97  THR A HG21 1 
ATOM   1562 H  HG22 . THR A 1 97  ? 30.26950 46.89887 34.29744 1.000 21.47721 ?  97  THR A HG22 1 
ATOM   1563 H  HG23 . THR A 1 97  ? 28.99520 46.95992 35.22746 1.000 21.47721 ?  97  THR A HG23 1 
ATOM   1564 N  N    . TRP A 1 98  ? 27.49762 43.03493 32.39507 1.000 17.57657 ?  98  TRP A N    1 
ATOM   1565 C  CA   . TRP A 1 98  ? 27.39338 41.74341 31.74897 1.000 16.71524 ?  98  TRP A CA   1 
ATOM   1566 C  C    . TRP A 1 98  ? 28.21042 41.70911 30.48066 1.000 16.63952 ?  98  TRP A C    1 
ATOM   1567 O  O    . TRP A 1 98  ? 28.19996 42.64850 29.68726 1.000 17.92608 ?  98  TRP A O    1 
ATOM   1568 C  CB   . TRP A 1 98  ? 25.92976 41.57275 31.42754 1.000 16.67175 ?  98  TRP A CB   1 
ATOM   1569 C  CG   . TRP A 1 98  ? 25.64797 40.38384 30.54072 1.000 17.49753 ?  98  TRP A CG   1 
ATOM   1570 C  CD1  . TRP A 1 98  ? 25.21993 40.45861 29.22440 1.000 17.20175 ?  98  TRP A CD1  1 
ATOM   1571 C  CD2  . TRP A 1 98  ? 25.78609 38.98982 30.84354 1.000 16.44070 ?  98  TRP A CD2  1 
ATOM   1572 N  NE1  . TRP A 1 98  ? 25.07078 39.21969 28.72083 1.000 17.02347 ?  98  TRP A NE1  1 
ATOM   1573 C  CE2  . TRP A 1 98  ? 25.44052 38.29155 29.66020 1.000 16.10168 ?  98  TRP A CE2  1 
ATOM   1574 C  CE3  . TRP A 1 98  ? 26.21494 38.23949 31.94593 1.000 16.85685 ?  98  TRP A CE3  1 
ATOM   1575 C  CZ2  . TRP A 1 98  ? 25.47300 36.90163 29.56369 1.000 17.52739 ?  98  TRP A CZ2  1 
ATOM   1576 C  CZ3  . TRP A 1 98  ? 26.19320 36.83265 31.85379 1.000 16.83889 ?  98  TRP A CZ3  1 
ATOM   1577 C  CH2  . TRP A 1 98  ? 25.84145 36.18861 30.66053 1.000 16.86472 ?  98  TRP A CH2  1 
ATOM   1578 H  H    . TRP A 1 98  ? 26.74658 43.45049 32.44833 1.000 21.09819 ?  98  TRP A H    1 
ATOM   1579 H  HA   . TRP A 1 98  ? 27.72212 41.02432 32.31088 1.000 20.06459 ?  98  TRP A HA   1 
ATOM   1580 H  HB2  . TRP A 1 98  ? 25.43901 41.45008 32.25520 1.000 20.01240 ?  98  TRP A HB2  1 
ATOM   1581 H  HB3  . TRP A 1 98  ? 25.61438 42.36752 30.96953 1.000 20.01240 ?  98  TRP A HB3  1 
ATOM   1582 H  HD1  . TRP A 1 98  ? 25.05971 41.24749 28.75868 1.000 20.64840 ?  98  TRP A HD1  1 
ATOM   1583 H  HE1  . TRP A 1 98  ? 24.78665 39.03757 27.92982 1.000 20.43447 ?  98  TRP A HE1  1 
ATOM   1584 H  HE3  . TRP A 1 98  ? 26.50773 38.66020 32.72194 1.000 20.23452 ?  98  TRP A HE3  1 
ATOM   1585 H  HZ2  . TRP A 1 98  ? 25.24839 36.47316 28.76942 1.000 21.03917 ?  98  TRP A HZ2  1 
ATOM   1586 H  HZ3  . TRP A 1 98  ? 26.41648 36.32293 32.59892 1.000 20.21297 ?  98  TRP A HZ3  1 
ATOM   1587 H  HH2  . TRP A 1 98  ? 25.86033 35.25976 30.61827 1.000 20.24397 ?  98  TRP A HH2  1 
ATOM   1588 N  N    . ASN A 1 99  ? 28.90105 40.59529 30.28418 1.000 16.74181 ?  99  ASN A N    1 
ATOM   1589 C  CA   . ASN A 1 99  ? 29.62855 40.35284 29.03825 1.000 17.44942 ?  99  ASN A CA   1 
ATOM   1590 C  C    . ASN A 1 99  ? 29.02007 39.16417 28.31586 1.000 17.18863 ?  99  ASN A C    1 
ATOM   1591 O  O    . ASN A 1 99  ? 29.11332 38.03095 28.82041 1.000 17.00621 ?  99  ASN A O    1 
ATOM   1592 C  CB   . ASN A 1 99  ? 31.08440 40.03209 29.37297 1.000 18.60856 ?  99  ASN A CB   1 
ATOM   1593 C  CG   . ASN A 1 99  ? 31.97365 39.97635 28.15862 1.000 19.62136 ?  99  ASN A CG   1 
ATOM   1594 O  OD1  . ASN A 1 99  ? 31.54318 39.63675 27.09780 1.000 20.18996 ?  99  ASN A OD1  1 
ATOM   1595 N  ND2  . ASN A 1 99  ? 33.21893 40.33660 28.31686 1.000 24.24992 ?  99  ASN A ND2  1 
ATOM   1596 H  H    . ASN A 1 99  ? 28.96667 39.95836 30.85829 1.000 20.09647 ?  99  ASN A H    1 
ATOM   1597 H  HA   . ASN A 1 99  ? 29.57130 41.13391 28.46592 1.000 20.94561 ?  99  ASN A HA   1 
ATOM   1598 H  HB2  . ASN A 1 99  ? 31.42986 40.71916 29.96416 1.000 22.33658 ?  99  ASN A HB2  1 
ATOM   1599 H  HB3  . ASN A 1 99  ? 31.12323 39.16742 29.81085 1.000 22.33658 ?  99  ASN A HB3  1 
ATOM   1600 H  HD21 . ASN A 1 99  ? 33.75983 40.31927 27.64848 1.000 29.10621 ?  99  ASN A HD21 1 
ATOM   1601 H  HD22 . ASN A 1 99  ? 33.49807 40.59117 29.08944 1.000 29.10621 ?  99  ASN A HD22 1 
ATOM   1602 N  N    . PRO A 1 100 ? 28.35795 39.35775 27.18686 1.000 16.40161 ?  100 PRO A N    1 
ATOM   1603 C  CA   . PRO A 1 100 ? 27.75487 38.22808 26.47147 1.000 16.35691 ?  100 PRO A CA   1 
ATOM   1604 C  C    . PRO A 1 100 ? 28.68950 37.10177 26.18244 1.000 16.93220 ?  100 PRO A C    1 
ATOM   1605 O  O    . PRO A 1 100 ? 28.24027 35.95110 26.02286 1.000 17.24057 ?  100 PRO A O    1 
ATOM   1606 C  CB   . PRO A 1 100 ? 27.27862 38.85903 25.15757 1.000 16.71230 ?  100 PRO A CB   1 
ATOM   1607 C  CG   . PRO A 1 100 ? 26.93939 40.31436 25.56864 1.000 17.60136 ?  100 PRO A CG   1 
ATOM   1608 C  CD   . PRO A 1 100 ? 28.07655 40.66283 26.53352 1.000 17.64484 ?  100 PRO A CD   1 
ATOM   1609 H  HA   . PRO A 1 100 ? 27.00342 37.90315 26.99169 1.000 19.63460 ?  100 PRO A HA   1 
ATOM   1610 H  HB2  . PRO A 1 100 ? 27.98661 38.83431 24.49497 1.000 20.06106 ?  100 PRO A HB2  1 
ATOM   1611 H  HB3  . PRO A 1 100 ? 26.49557 38.39385 24.82391 1.000 20.06106 ?  100 PRO A HB3  1 
ATOM   1612 H  HG2  . PRO A 1 100 ? 26.94098 40.89627 24.79258 1.000 21.12793 ?  100 PRO A HG2  1 
ATOM   1613 H  HG3  . PRO A 1 100 ? 26.07591 40.35102 26.00903 1.000 21.12793 ?  100 PRO A HG3  1 
ATOM   1614 H  HD2  . PRO A 1 100 ? 28.85437 40.98599 26.05242 1.000 21.18011 ?  100 PRO A HD2  1 
ATOM   1615 H  HD3  . PRO A 1 100 ? 27.79084 41.32318 27.18406 1.000 21.18011 ?  100 PRO A HD3  1 
ATOM   1616 N  N    . GLY A 1 101 ? 29.97666 37.37617 26.07221 1.000 17.07238 ?  101 GLY A N    1 
ATOM   1617 C  CA   . GLY A 1 101 ? 30.97557 36.37963 25.75601 1.000 18.36481 ?  101 GLY A CA   1 
ATOM   1618 C  C    . GLY A 1 101 ? 31.32307 35.42431 26.87169 1.000 18.00328 ?  101 GLY A C    1 
ATOM   1619 O  O    . GLY A 1 101 ? 32.03392 34.44634 26.62864 1.000 19.01930 ?  101 GLY A O    1 
ATOM   1620 H  H    . GLY A 1 101 ? 30.30853 38.16217 26.18019 1.000 20.49315 ?  101 GLY A H    1 
ATOM   1621 H  HA2  . GLY A 1 101 ? 30.65650 35.85116 25.00781 1.000 22.04408 ?  101 GLY A HA2  1 
ATOM   1622 H  HA3  . GLY A 1 101 ? 31.79197 36.83440 25.49606 1.000 22.04408 ?  101 GLY A HA3  1 
ATOM   1623 N  N    . TRP A 1 102 ? 30.90316 35.69493 28.09650 1.000 17.06008 ?  102 TRP A N    1 
ATOM   1624 C  CA   . TRP A 1 102 ? 31.21603 34.74394 29.15068 1.000 17.44751 ?  102 TRP A CA   1 
ATOM   1625 C  C    . TRP A 1 102 ? 30.60055 33.36715 28.84735 1.000 17.30421 ?  102 TRP A C    1 
ATOM   1626 O  O    . TRP A 1 102 ? 29.42360 33.27260 28.53506 1.000 17.64261 ?  102 TRP A O    1 
ATOM   1627 C  CB   . TRP A 1 102 ? 30.72515 35.28078 30.48267 1.000 17.50263 ?  102 TRP A CB   1 
ATOM   1628 C  CG   . TRP A 1 102 ? 31.46962 36.40108 31.06910 1.000 17.11751 ?  102 TRP A CG   1 
ATOM   1629 C  CD1  . TRP A 1 102 ? 32.80920 36.62109 30.94412 1.000 18.88766 ?  102 TRP A CD1  1 
ATOM   1630 C  CD2  . TRP A 1 102 ? 30.95232 37.45397 31.89159 1.000 17.13161 ?  102 TRP A CD2  1 
ATOM   1631 N  NE1  . TRP A 1 102 ? 33.17666 37.72957 31.69482 1.000 19.62057 ?  102 TRP A NE1  1 
ATOM   1632 C  CE2  . TRP A 1 102 ? 32.04432 38.27231 32.26655 1.000 18.04121 ?  102 TRP A CE2  1 
ATOM   1633 C  CE3  . TRP A 1 102 ? 29.68114 37.77300 32.34334 1.000 17.69437 ?  102 TRP A CE3  1 
ATOM   1634 C  CZ2  . TRP A 1 102 ? 31.87475 39.42182 33.06531 1.000 18.91985 ?  102 TRP A CZ2  1 
ATOM   1635 C  CZ3  . TRP A 1 102 ? 29.50888 38.92335 33.11871 1.000 17.74929 ?  102 TRP A CZ3  1 
ATOM   1636 C  CH2  . TRP A 1 102 ? 30.60080 39.74451 33.44527 1.000 18.41266 ?  102 TRP A CH2  1 
ATOM   1637 H  H    . TRP A 1 102 ? 30.45578 36.39002 28.33382 1.000 20.47840 ?  102 TRP A H    1 
ATOM   1638 H  HA   . TRP A 1 102 ? 32.17690 34.62409 29.20779 1.000 20.94331 ?  102 TRP A HA   1 
ATOM   1639 H  HB2  . TRP A 1 102 ? 29.81068 35.58193 30.36453 1.000 21.00946 ?  102 TRP A HB2  1 
ATOM   1640 H  HB3  . TRP A 1 102 ? 30.75511 34.55563 31.12622 1.000 21.00946 ?  102 TRP A HB3  1 
ATOM   1641 H  HD1  . TRP A 1 102 ? 33.39007 36.10564 30.43244 1.000 22.67149 ?  102 TRP A HD1  1 
ATOM   1642 H  HE1  . TRP A 1 102 ? 33.97763 38.02850 31.78808 1.000 23.55099 ?  102 TRP A HE1  1 
ATOM   1643 H  HE3  . TRP A 1 102 ? 28.95511 37.23080 32.13408 1.000 21.23955 ?  102 TRP A HE3  1 
ATOM   1644 H  HZ2  . TRP A 1 102 ? 32.60160 39.94107 33.32411 1.000 22.71013 ?  102 TRP A HZ2  1 
ATOM   1645 H  HZ3  . TRP A 1 102 ? 28.65922 39.14822 33.42270 1.000 21.30545 ?  102 TRP A HZ3  1 
ATOM   1646 H  HH2  . TRP A 1 102 ? 30.45448 40.52443 33.93027 1.000 22.10150 ?  102 TRP A HH2  1 
ATOM   1647 N  N    . SER A 1 103 ? 31.39340 32.31085 29.01208 1.000 16.39900 ?  103 SER A N    1 
ATOM   1648 C  CA   . SER A 1 103 ? 30.88578 30.97748 28.79269 1.000 16.00229 ?  103 SER A CA   1 
ATOM   1649 C  C    . SER A 1 103 ? 30.09951 30.51208 30.01146 1.000 16.02877 ?  103 SER A C    1 
ATOM   1650 O  O    . SER A 1 103 ? 30.21112 31.08188 31.10326 1.000 16.26915 ?  103 SER A O    1 
ATOM   1651 C  CB   . SER A 1 103 ? 32.04616 30.04178 28.56877 1.000 17.45769 ?  103 SER A CB   1 
ATOM   1652 O  OG   . SER A 1 103 ? 32.76003 29.83836 29.74392 1.000 17.27945 ?  103 SER A OG   1 
ATOM   1653 H  H    . SER A 1 103 ? 32.21951 32.34793 29.24822 1.000 19.68510 ?  103 SER A H    1 
ATOM   1654 H  HA   . SER A 1 103 ? 30.30006 30.96173 28.01965 1.000 19.20906 ?  103 SER A HA   1 
ATOM   1655 H  HB2  . SER A 1 103 ? 31.70660 29.18892 28.25533 1.000 20.95553 ?  103 SER A HB2  1 
ATOM   1656 H  HB3  . SER A 1 103 ? 32.63783 30.42781 27.90409 1.000 20.95553 ?  103 SER A HB3  1 
ATOM   1657 H  HG   . SER A 1 103 ? 33.39643 29.30789 29.60532 1.000 20.74164 ?  103 SER A HG   1 
ATOM   1658 N  N    . VAL A 1 104 ? 29.29593 29.46256 29.81522 1.000 16.10352 ?  104 VAL A N    1 
ATOM   1659 C  CA   . VAL A 1 104 ? 28.56051 28.89894 30.94357 1.000 15.58915 ?  104 VAL A CA   1 
ATOM   1660 C  C    . VAL A 1 104 ? 29.51949 28.32251 31.97588 1.000 15.77735 ?  104 VAL A C    1 
ATOM   1661 O  O    . VAL A 1 104 ? 29.32816 28.49359 33.17248 1.000 16.40979 ?  104 VAL A O    1 
ATOM   1662 C  CB   . VAL A 1 104 ? 27.51293 27.87012 30.45061 1.000 18.06540 ?  104 VAL A CB   1 
ATOM   1663 C  CG1  . VAL A 1 104 ? 26.83792 27.20151 31.66503 1.000 19.51795 ?  104 VAL A CG1  1 
ATOM   1664 C  CG2  . VAL A 1 104 ? 26.46091 28.51900 29.58481 1.000 20.08553 ?  104 VAL A CG2  1 
ATOM   1665 H  H    . VAL A 1 104 ? 29.16447 29.07160 29.06059 1.000 19.33052 ?  104 VAL A H    1 
ATOM   1666 H  HA   . VAL A 1 104 ? 28.07046 29.61197 31.38214 1.000 18.71329 ?  104 VAL A HA   1 
ATOM   1667 H  HB   . VAL A 1 104 ? 27.96852 27.20251 29.91429 1.000 21.68478 ?  104 VAL A HB   1 
ATOM   1668 H  HG11 . VAL A 1 104 ? 26.04575 26.72869 31.36535 1.000 23.42785 ?  104 VAL A HG11 1 
ATOM   1669 H  HG12 . VAL A 1 104 ? 27.46167 26.57858 32.06973 1.000 23.42785 ?  104 VAL A HG12 1 
ATOM   1670 H  HG13 . VAL A 1 104 ? 26.59158 27.88646 32.30617 1.000 23.42785 ?  104 VAL A HG13 1 
ATOM   1671 H  HG21 . VAL A 1 104 ? 25.83087 27.84189 29.29246 1.000 24.10894 ?  104 VAL A HG21 1 
ATOM   1672 H  HG22 . VAL A 1 104 ? 26.00043 29.19778 30.10261 1.000 24.10894 ?  104 VAL A HG22 1 
ATOM   1673 H  HG23 . VAL A 1 104 ? 26.89100 28.92469 28.81583 1.000 24.10894 ?  104 VAL A HG23 1 
ATOM   1674 N  N    . SER A 1 105 ? 30.63601 27.74198 31.52456 1.000 16.02965 ?  105 SER A N    1 
ATOM   1675 C  CA   . SER A 1 105 ? 31.65782 27.26556 32.45999 1.000 16.65993 ?  105 SER A CA   1 
ATOM   1676 C  C    . SER A 1 105 ? 32.20126 28.41271 33.27648 1.000 15.80213 ?  105 SER A C    1 
ATOM   1677 O  O    . SER A 1 105 ? 32.38900 28.28557 34.50098 1.000 16.28945 ?  105 SER A O    1 
ATOM   1678 C  CB   . SER A 1 105 ? 32.81799 26.58450 31.67321 1.000 19.31875 ?  105 SER A CB   1 
ATOM   1679 O  OG   . SER A 1 105 ? 32.34895 25.38221 31.25368 1.000 23.69202 ?  105 SER A OG   1 
ATOM   1680 H  H    . SER A 1 105 ? 30.82336 27.61390 30.69505 1.000 19.24188 ?  105 SER A H    1 
ATOM   1681 H  HA   . SER A 1 105 ? 31.26329 26.61054 33.05680 1.000 19.99821 ?  105 SER A HA   1 
ATOM   1682 H  HB2  . SER A 1 105 ? 33.06664 27.12905 30.90997 1.000 23.18880 ?  105 SER A HB2  1 
ATOM   1683 H  HB3  . SER A 1 105 ? 33.58434 26.45800 32.25425 1.000 23.18880 ?  105 SER A HB3  1 
ATOM   1684 H  HG   . SER A 1 105 ? 32.93856 24.98361 30.80751 1.000 28.43672 ?  105 SER A HG   1 
ATOM   1685 N  N    . THR A 1 106 ? 32.45711 29.56239 32.64509 1.000 15.63154 ?  106 THR A N    1 
ATOM   1686 C  CA   . THR A 1 106 ? 32.98335 30.69976 33.36591 1.000 15.79228 ?  106 THR A CA   1 
ATOM   1687 C  C    . THR A 1 106 ? 31.98246 31.18493 34.40181 1.000 15.22222 ?  106 THR A C    1 
ATOM   1688 O  O    . THR A 1 106 ? 32.35863 31.46312 35.54782 1.000 15.35065 ?  106 THR A O    1 
ATOM   1689 C  CB   . THR A 1 106 ? 33.35747 31.77535 32.36751 1.000 16.70073 ?  106 THR A CB   1 
ATOM   1690 O  OG1  . THR A 1 106 ? 34.54419 31.30755 31.68167 1.000 18.04739 ?  106 THR A OG1  1 
ATOM   1691 C  CG2  . THR A 1 106 ? 33.62984 33.13041 33.02679 1.000 17.26946 ?  106 THR A CG2  1 
ATOM   1692 H  H    . THR A 1 106 ? 32.33249 29.69968 31.80531 1.000 18.76415 ?  106 THR A H    1 
ATOM   1693 H  HA   . THR A 1 106 ? 33.78861 30.45851 33.84990 1.000 18.95704 ?  106 THR A HA   1 
ATOM   1694 H  HB   . THR A 1 106 ? 32.62378 31.93259 31.75278 1.000 20.04718 ?  106 THR A HB   1 
ATOM   1695 H  HG1  . THR A 1 106 ? 34.77684 31.86462 31.09758 1.000 21.66317 ?  106 THR A HG1  1 
ATOM   1696 H  HG21 . THR A 1 106 ? 34.05183 33.72965 32.39140 1.000 20.72966 ?  106 THR A HG21 1 
ATOM   1697 H  HG22 . THR A 1 106 ? 32.79701 33.52635 33.32766 1.000 20.72966 ?  106 THR A HG22 1 
ATOM   1698 H  HG23 . THR A 1 106 ? 34.21770 33.01593 33.78982 1.000 20.72966 ?  106 THR A HG23 1 
ATOM   1699 N  N    . ILE A 1 107 ? 30.70506 31.28345 34.03561 1.000 14.69319 ?  107 ILE A N    1 
ATOM   1700 C  CA   . ILE A 1 107 ? 29.67862 31.74889 34.95894 1.000 14.93558 ?  107 ILE A CA   1 
ATOM   1701 C  C    . ILE A 1 107 ? 29.57747 30.80608 36.16579 1.000 14.42056 ?  107 ILE A C    1 
ATOM   1702 O  O    . ILE A 1 107 ? 29.50987 31.22467 37.31622 1.000 15.24900 ?  107 ILE A O    1 
ATOM   1703 C  CB   . ILE A 1 107 ? 28.34944 31.89048 34.21638 1.000 15.56642 ?  107 ILE A CB   1 
ATOM   1704 C  CG1  . ILE A 1 107 ? 28.44106 32.95401 33.10966 1.000 15.66761 ?  107 ILE A CG1  1 
ATOM   1705 C  CG2  . ILE A 1 107 ? 27.21978 32.15415 35.17554 1.000 15.93693 ?  107 ILE A CG2  1 
ATOM   1706 C  CD1  . ILE A 1 107 ? 27.27619 32.94194 32.10666 1.000 17.55324 ?  107 ILE A CD1  1 
ATOM   1707 H  H    . ILE A 1 107 ? 30.40664 31.08555 33.25371 1.000 17.63813 ?  107 ILE A H    1 
ATOM   1708 H  HA   . ILE A 1 107 ? 29.92503 32.62211 35.30197 1.000 17.92900 ?  107 ILE A HA   1 
ATOM   1709 H  HB   . ILE A 1 107 ? 28.15847 31.04665 33.77776 1.000 18.68600 ?  107 ILE A HB   1 
ATOM   1710 H  HG12 . ILE A 1 107 ? 28.45900 33.83024 33.52535 1.000 18.80744 ?  107 ILE A HG12 1 
ATOM   1711 H  HG13 . ILE A 1 107 ? 29.25876 32.80760 32.60883 1.000 18.80744 ?  107 ILE A HG13 1 
ATOM   1712 H  HG21 . ILE A 1 107 ? 26.45629 32.48917 34.67981 1.000 19.13062 ?  107 ILE A HG21 1 
ATOM   1713 H  HG22 . ILE A 1 107 ? 26.98592 31.32609 35.62334 1.000 19.13062 ?  107 ILE A HG22 1 
ATOM   1714 H  HG23 . ILE A 1 107 ? 27.50609 32.81316 35.82718 1.000 19.13062 ?  107 ILE A HG23 1 
ATOM   1715 H  HD11 . ILE A 1 107 ? 27.47096 33.56474 31.38896 1.000 21.07019 ?  107 ILE A HD11 1 
ATOM   1716 H  HD12 . ILE A 1 107 ? 27.17665 32.04578 31.74904 1.000 21.07019 ?  107 ILE A HD12 1 
ATOM   1717 H  HD13 . ILE A 1 107 ? 26.46305 33.20786 32.56382 1.000 21.07019 ?  107 ILE A HD13 1 
ATOM   1718 N  N    . LEU A 1 108 ? 29.55074 29.50260 35.90595 1.000 14.77187 ?  108 LEU A N    1 
ATOM   1719 C  CA   . LEU A 1 108 ? 29.46881 28.49345 36.96631 1.000 14.77910 ?  108 LEU A CA   1 
ATOM   1720 C  C    . LEU A 1 108 ? 30.72181 28.48579 37.83197 1.000 15.03866 ?  108 LEU A C    1 
ATOM   1721 O  O    . LEU A 1 108 ? 30.63048 28.34850 39.06026 1.000 15.35831 ?  108 LEU A O    1 
ATOM   1722 C  CB   . LEU A 1 108 ? 29.15332 27.13631 36.37566 1.000 16.34296 ?  108 LEU A CB   1 
ATOM   1723 C  CG   . LEU A 1 108 ? 27.72694 26.97348 35.85885 1.000 18.40049 ?  108 LEU A CG   1 
ATOM   1724 C  CD1  . LEU A 1 108 ? 27.62049 25.68189 35.00950 1.000 19.41234 ?  108 LEU A CD1  1 
ATOM   1725 C  CD2  . LEU A 1 108 ? 26.70151 27.01884 37.01697 1.000 20.74832 ?  108 LEU A CD2  1 
ATOM   1726 H  H    . LEU A 1 108 ? 29.57900 29.16665 35.11478 1.000 17.73254 ?  108 LEU A H    1 
ATOM   1727 H  HA   . LEU A 1 108 ? 28.73205 28.71105 37.55854 1.000 17.74123 ?  108 LEU A HA   1 
ATOM   1728 H  HB2  . LEU A 1 108 ? 29.75323 26.98002 35.62962 1.000 19.61786 ?  108 LEU A HB2  1 
ATOM   1729 H  HB3  . LEU A 1 108 ? 29.29363 26.46403 37.06068 1.000 19.61786 ?  108 LEU A HB3  1 
ATOM   1730 H  HG   . LEU A 1 108 ? 27.49940 27.71742 35.27948 1.000 22.08689 ?  108 LEU A HG   1 
ATOM   1731 H  HD11 . LEU A 1 108 ? 26.71681 25.60351 34.66583 1.000 23.30111 ?  108 LEU A HD11 1 
ATOM   1732 H  HD12 . LEU A 1 108 ? 28.25067 25.73477 34.27399 1.000 23.30111 ?  108 LEU A HD12 1 
ATOM   1733 H  HD13 . LEU A 1 108 ? 27.82892 24.91768 35.56937 1.000 23.30111 ?  108 LEU A HD13 1 
ATOM   1734 H  HD21 . LEU A 1 108 ? 25.83061 26.75898 36.67801 1.000 24.90428 ?  108 LEU A HD21 1 
ATOM   1735 H  HD22 . LEU A 1 108 ? 26.98289 26.40369 37.71219 1.000 24.90428 ?  108 LEU A HD22 1 
ATOM   1736 H  HD23 . LEU A 1 108 ? 26.66327 27.92161 37.36973 1.000 24.90428 ?  108 LEU A HD23 1 
ATOM   1737 N  N    . ASN A 1 109 ? 31.89693 28.61736 37.21779 1.000 15.85624 ?  109 ASN A N    1 
ATOM   1738 C  CA   . ASN A 1 109 ? 33.10363 28.74832 38.01824 1.000 17.28404 ?  109 ASN A CA   1 
ATOM   1739 C  C    . ASN A 1 109 ? 33.05065 29.97928 38.90120 1.000 16.38915 ?  109 ASN A C    1 
ATOM   1740 O  O    . ASN A 1 109 ? 33.58321 29.95137 40.01618 1.000 16.79861 ?  109 ASN A O    1 
ATOM   1741 C  CB   . ASN A 1 109 ? 34.29635 28.80316 37.08421 1.000 18.79667 ?  109 ASN A CB   1 
ATOM   1742 C  CG   . ASN A 1 109 ? 34.79900 27.46955 36.61671 1.000 24.69933 ?  109 ASN A CG   1 
ATOM   1743 O  OD1  . ASN A 1 109 ? 34.51313 26.45669 37.23753 1.000 27.40331 ?  109 ASN A OD1  1 
ATOM   1744 N  ND2  . ASN A 1 109 ? 35.49831 27.46103 35.48941 1.000 26.03286 ?  109 ASN A ND2  1 
ATOM   1745 H  H    . ASN A 1 109 ? 32.01581 28.63296 36.36619 1.000 19.03379 ?  109 ASN A H    1 
ATOM   1746 H  HA   . ASN A 1 109 ? 33.20197 27.98041 38.60266 1.000 20.74715 ?  109 ASN A HA   1 
ATOM   1747 H  HB2  . ASN A 1 109 ? 34.04667 29.31140 36.29664 1.000 22.56231 ?  109 ASN A HB2  1 
ATOM   1748 H  HB3  . ASN A 1 109 ? 35.02751 29.24343 37.54514 1.000 22.56231 ?  109 ASN A HB3  1 
ATOM   1749 H  HD21 . ASN A 1 109 ? 35.64223 28.19625 35.06710 1.000 31.24573 ?  109 ASN A HD21 1 
ATOM   1750 H  HD22 . ASN A 1 109 ? 35.80773 26.72029 35.18092 1.000 31.24573 ?  109 ASN A HD22 1 
ATOM   1751 N  N    . GLY A 1 110 ? 32.40011 31.05302 38.45346 1.000 16.37929 ?  110 GLY A N    1 
ATOM   1752 C  CA   . GLY A 1 110 ? 32.31974 32.21570 39.32666 1.000 16.49908 ?  110 GLY A CA   1 
ATOM   1753 C  C    . GLY A 1 110 ? 31.41542 31.95845 40.50872 1.000 15.57893 ?  110 GLY A C    1 
ATOM   1754 O  O    . GLY A 1 110 ? 31.68173 32.43781 41.61766 1.000 15.76002 ?  110 GLY A O    1 
ATOM   1755 H  H    . GLY A 1 110 ? 32.01683 31.12837 37.68729 1.000 19.66146 ?  110 GLY A H    1 
ATOM   1756 H  HA2  . GLY A 1 110 ? 33.20508 32.43572 39.65630 1.000 19.80520 ?  110 GLY A HA2  1 
ATOM   1757 H  HA3  . GLY A 1 110 ? 31.97115 32.97179 38.82896 1.000 19.80520 ?  110 GLY A HA3  1 
ATOM   1758 N  N    . LEU A 1 111 ? 30.34177 31.20023 40.28412 1.000 15.47100 ?  111 LEU A N    1 
ATOM   1759 C  CA   . LEU A 1 111 ? 29.49974 30.78854 41.39460 1.000 14.89402 ?  111 LEU A CA   1 
ATOM   1760 C  C    . LEU A 1 111 ? 30.27884 29.97190 42.41465 1.000 14.45562 ?  111 LEU A C    1 
ATOM   1761 O  O    . LEU A 1 111 ? 30.19497 30.21819 43.61158 1.000 15.19164 ?  111 LEU A O    1 
ATOM   1762 C  CB   . LEU A 1 111 ? 28.32985 29.96835 40.84582 1.000 14.74698 ?  111 LEU A CB   1 
ATOM   1763 C  CG   . LEU A 1 111 ? 27.46786 29.23729 41.89381 1.000 14.85212 ?  111 LEU A CG   1 
ATOM   1764 C  CD1  . LEU A 1 111 ? 26.80642 30.17962 42.90056 1.000 16.02406 ?  111 LEU A CD1  1 
ATOM   1765 C  CD2  . LEU A 1 111 ? 26.43687 28.33196 41.14592 1.000 15.99582 ?  111 LEU A CD2  1 
ATOM   1766 H  H    . LEU A 1 111 ? 30.08751 30.91849 39.51238 1.000 18.57150 ?  111 LEU A H    1 
ATOM   1767 H  HA   . LEU A 1 111 ? 29.15996 31.57700 41.84601 1.000 17.87913 ?  111 LEU A HA   1 
ATOM   1768 H  HB2  . LEU A 1 111 ? 27.74292 30.56725 40.35823 1.000 17.70267 ?  111 LEU A HB2  1 
ATOM   1769 H  HB3  . LEU A 1 111 ? 28.68756 29.29417 40.24714 1.000 17.70267 ?  111 LEU A HB3  1 
ATOM   1770 H  HG   . LEU A 1 111 ? 28.03921 28.67829 42.44333 1.000 17.82885 ?  111 LEU A HG   1 
ATOM   1771 H  HD11 . LEU A 1 111 ? 26.30993 29.65337 43.54668 1.000 19.23517 ?  111 LEU A HD11 1 
ATOM   1772 H  HD12 . LEU A 1 111 ? 27.49456 30.69357 43.35135 1.000 19.23517 ?  111 LEU A HD12 1 
ATOM   1773 H  HD13 . LEU A 1 111 ? 26.20503 30.77565 42.42730 1.000 19.23517 ?  111 LEU A HD13 1 
ATOM   1774 H  HD21 . LEU A 1 111 ? 25.88739 27.87235 41.79992 1.000 19.20129 ?  111 LEU A HD21 1 
ATOM   1775 H  HD22 . LEU A 1 111 ? 25.88044 28.88876 40.57911 1.000 19.20129 ?  111 LEU A HD22 1 
ATOM   1776 H  HD23 . LEU A 1 111 ? 26.91772 27.68589 40.60528 1.000 19.20129 ?  111 LEU A HD23 1 
ATOM   1777 N  N    . LEU A 1 112 ? 31.03624 28.96975 41.95348 1.000 14.40832 ?  112 LEU A N    1 
ATOM   1778 C  CA   . LEU A 1 112 ? 31.78477 28.12388 42.85239 1.000 13.67139 ?  112 LEU A CA   1 
ATOM   1779 C  C    . LEU A 1 112 ? 32.86163 28.90953 43.57875 1.000 13.63453 ?  112 LEU A C    1 
ATOM   1780 O  O    . LEU A 1 112 ? 33.05305 28.76436 44.79404 1.000 15.32175 ?  112 LEU A O    1 
ATOM   1781 C  CB   . LEU A 1 112 ? 32.38990 26.97034 42.05022 1.000 15.16894 ?  112 LEU A CB   1 
ATOM   1782 C  CG   . LEU A 1 112 ? 33.33253 26.08016 42.80962 1.000 17.41813 ?  112 LEU A CG   1 
ATOM   1783 C  CD1  . LEU A 1 112 ? 32.68851 25.45515 44.01849 1.000 19.58624 ?  112 LEU A CD1  1 
ATOM   1784 C  CD2  . LEU A 1 112 ? 33.85343 24.93020 41.94923 1.000 20.01526 ?  112 LEU A CD2  1 
ATOM   1785 H  H    . LEU A 1 112 ? 31.12657 28.76744 41.12252 1.000 17.29629 ?  112 LEU A H    1 
ATOM   1786 H  HA   . LEU A 1 112 ? 31.19425 27.75538 43.52795 1.000 16.41197 ?  112 LEU A HA   1 
ATOM   1787 H  HB2  . LEU A 1 112 ? 31.66574 26.41367 41.72372 1.000 18.20904 ?  112 LEU A HB2  1 
ATOM   1788 H  HB3  . LEU A 1 112 ? 32.88327 27.34453 41.30358 1.000 18.20904 ?  112 LEU A HB3  1 
ATOM   1789 H  HG   . LEU A 1 112 ? 34.06253 26.65699 43.08397 1.000 20.90806 ?  112 LEU A HG   1 
ATOM   1790 H  HD11 . LEU A 1 112 ? 33.30810 24.82284 44.41498 1.000 23.50979 ?  112 LEU A HD11 1 
ATOM   1791 H  HD12 . LEU A 1 112 ? 32.47321 26.15236 44.65758 1.000 23.50979 ?  112 LEU A HD12 1 
ATOM   1792 H  HD13 . LEU A 1 112 ? 31.87895 24.99694 43.74360 1.000 23.50979 ?  112 LEU A HD13 1 
ATOM   1793 H  HD21 . LEU A 1 112 ? 34.47277 24.39885 42.47362 1.000 24.02462 ?  112 LEU A HD21 1 
ATOM   1794 H  HD22 . LEU A 1 112 ? 33.10428 24.38241 41.66709 1.000 24.02462 ?  112 LEU A HD22 1 
ATOM   1795 H  HD23 . LEU A 1 112 ? 34.30625 25.29623 41.17342 1.000 24.02462 ?  112 LEU A HD23 1 
ATOM   1796 N  N    . SER A 1 113 ? 33.55239 29.78966 42.86370 1.000 14.87476 ?  113 SER A N    1 
ATOM   1797 C  CA   . SER A 1 113 ? 34.60091 30.58574 43.48186 1.000 15.37720 ?  113 SER A CA   1 
ATOM   1798 C  C    . SER A 1 113 ? 34.02454 31.49709 44.54339 1.000 15.51727 ?  113 SER A C    1 
ATOM   1799 O  O    . SER A 1 113 ? 34.61157 31.67300 45.62132 1.000 16.38726 ?  113 SER A O    1 
ATOM   1800 C  CB   . SER A 1 113 ? 35.30820 31.42401 42.39762 1.000 17.18245 ?  113 SER A CB   1 
ATOM   1801 O  OG   . SER A 1 113 ? 36.30185 32.26407 42.93043 1.000 19.44043 ?  113 SER A OG   1 
ATOM   1802 H  H    . SER A 1 113 ? 33.43443 29.94359 42.02585 1.000 17.85602 ?  113 SER A H    1 
ATOM   1803 H  HA   . SER A 1 113 ? 35.25057 29.99811 43.89843 1.000 18.45894 ?  113 SER A HA   1 
ATOM   1804 H  HB2  . SER A 1 113 ? 35.72233 30.82032 41.76126 1.000 20.62524 ?  113 SER A HB2  1 
ATOM   1805 H  HB3  . SER A 1 113 ? 34.64566 31.97372 41.95066 1.000 20.62524 ?  113 SER A HB3  1 
ATOM   1806 H  HG   . SER A 1 113 ? 35.95743 32.81398 43.46388 1.000 23.33482 ?  113 SER A HG   1 
ATOM   1807 N  N    . PHE A 1 114 ? 32.86366 32.08420 44.27906 1.000 14.74770 ?  114 PHE A N    1 
ATOM   1808 C  CA   . PHE A 1 114 ? 32.22461 32.91670 45.28395 1.000 14.41475 ?  114 PHE A CA   1 
ATOM   1809 C  C    . PHE A 1 114 ? 31.80476 32.05589 46.47124 1.000 14.87181 ?  114 PHE A C    1 
ATOM   1810 O  O    . PHE A 1 114 ? 31.95853 32.44628 47.63035 1.000 14.78979 ?  114 PHE A O    1 
ATOM   1811 C  CB   . PHE A 1 114 ? 31.01044 33.63930 44.69036 1.000 14.59646 ?  114 PHE A CB   1 
ATOM   1812 C  CG   . PHE A 1 114 ? 30.50481 34.69780 45.58824 1.000 15.51912 ?  114 PHE A CG   1 
ATOM   1813 C  CD1  . PHE A 1 114 ? 31.03400 35.96126 45.54919 1.000 16.12953 ?  114 PHE A CD1  1 
ATOM   1814 C  CD2  . PHE A 1 114 ? 29.51347 34.41908 46.49118 1.000 17.09660 ?  114 PHE A CD2  1 
ATOM   1815 C  CE1  . PHE A 1 114 ? 30.54950 36.96276 46.41691 1.000 17.22540 ?  114 PHE A CE1  1 
ATOM   1816 C  CE2  . PHE A 1 114 ? 29.06894 35.36583 47.36725 1.000 18.54831 ?  114 PHE A CE2  1 
ATOM   1817 C  CZ   . PHE A 1 114 ? 29.58029 36.61167 47.31675 1.000 18.25657 ?  114 PHE A CZ   1 
ATOM   1818 H  H    . PHE A 1 114 ? 32.43295 32.01723 43.53771 1.000 17.70354 ?  114 PHE A H    1 
ATOM   1819 H  HA   . PHE A 1 114 ? 32.84652 33.59802 45.58381 1.000 17.30400 ?  114 PHE A HA   1 
ATOM   1820 H  HB2  . PHE A 1 114 ? 31.26377 34.05011 43.84896 1.000 17.52206 ?  114 PHE A HB2  1 
ATOM   1821 H  HB3  . PHE A 1 114 ? 30.29733 32.99802 44.54502 1.000 17.52206 ?  114 PHE A HB3  1 
ATOM   1822 H  HD1  . PHE A 1 114 ? 31.71544 36.15943 44.94814 1.000 19.36174 ?  114 PHE A HD1  1 
ATOM   1823 H  HD2  . PHE A 1 114 ? 29.13649 33.56906 46.50743 1.000 20.52222 ?  114 PHE A HD2  1 
ATOM   1824 H  HE1  . PHE A 1 114 ? 30.87775 37.83206 46.37858 1.000 20.67678 ?  114 PHE A HE1  1 
ATOM   1825 H  HE2  . PHE A 1 114 ? 28.41708 35.15274 47.99540 1.000 22.26428 ?  114 PHE A HE2  1 
ATOM   1826 H  HZ   . PHE A 1 114 ? 29.26462 37.25272 47.91199 1.000 21.91419 ?  114 PHE A HZ   1 
ATOM   1827 N  N    . MET A 1 115 ? 31.21054 30.89255 46.20049 1.000 14.92333 ?  115 MET A N    1 
ATOM   1828 C  CA   . MET A 1 115 ? 30.68512 30.02504 47.26502 1.000 14.31551 ?  115 MET A CA   1 
ATOM   1829 C  C    . MET A 1 115 ? 31.75864 29.68131 48.30347 1.000 14.25827 ?  115 MET A C    1 
ATOM   1830 O  O    . MET A 1 115 ? 31.45899 29.64754 49.49639 1.000 14.33876 ?  115 MET A O    1 
ATOM   1831 C  CB   . MET A 1 115 ? 30.03490 28.76100 46.64989 1.000 14.54006 ?  115 MET A CB   1 
ATOM   1832 C  CG   . MET A 1 115 ? 29.61059 27.74314 47.63458 1.000 15.50049 ?  115 MET A CG   1 
ATOM   1833 S  SD   . MET A 1 115 ? 29.00667 26.27707 46.79899 1.000 16.31718 ?  115 MET A SD   1 
ATOM   1834 C  CE   . MET A 1 115 ? 28.08945 25.52294 48.19238 1.000 16.85217 ?  115 MET A CE   1 
ATOM   1835 H  H    . MET A 1 115 ? 31.09647 30.57776 45.40835 1.000 17.91430 ?  115 MET A H    1 
ATOM   1836 H  HA   . MET A 1 115 ? 29.98048 30.50016 47.73261 1.000 17.18492 ?  115 MET A HA   1 
ATOM   1837 H  HB2  . MET A 1 115 ? 29.24790 29.03094 46.15122 1.000 17.45438 ?  115 MET A HB2  1 
ATOM   1838 H  HB3  . MET A 1 115 ? 30.67697 28.34248 46.05535 1.000 17.45438 ?  115 MET A HB3  1 
ATOM   1839 H  HG2  . MET A 1 115 ? 30.36565 27.49402 48.19022 1.000 18.60689 ?  115 MET A HG2  1 
ATOM   1840 H  HG3  . MET A 1 115 ? 28.89723 28.10159 48.18551 1.000 18.60689 ?  115 MET A HG3  1 
ATOM   1841 H  HE1  . MET A 1 115 ? 27.68814 24.69199 47.89341 1.000 20.22891 ?  115 MET A HE1  1 
ATOM   1842 H  HE2  . MET A 1 115 ? 28.70713 25.34903 48.91979 1.000 20.22891 ?  115 MET A HE2  1 
ATOM   1843 H  HE3  . MET A 1 115 ? 27.39840 26.13752 48.48503 1.000 20.22891 ?  115 MET A HE3  1 
ATOM   1844 N  N    . THR A 1 116 ? 32.99846 29.43405 47.87767 1.000 14.92859 ?  116 THR A N    1 
ATOM   1845 C  CA   . THR A 1 116 ? 34.03121 29.00220 48.79369 1.000 15.07235 ?  116 THR A CA   1 
ATOM   1846 C  C    . THR A 1 116 ? 34.75155 30.16673 49.47527 1.000 16.12322 ?  116 THR A C    1 
ATOM   1847 O  O    . THR A 1 116 ? 35.51885 29.94918 50.44218 1.000 17.47044 ?  116 THR A O    1 
ATOM   1848 C  CB   . THR A 1 116 ? 35.01947 28.05663 48.08653 1.000 15.78893 ?  116 THR A CB   1 
ATOM   1849 O  OG1  . THR A 1 116 ? 35.72190 28.77805 47.08751 1.000 18.17550 ?  116 THR A OG1  1 
ATOM   1850 C  CG2  . THR A 1 116 ? 34.33037 26.82194 47.57063 1.000 15.71080 ?  116 THR A CG2  1 
ATOM   1851 H  H    . THR A 1 116 ? 33.25761 29.51166 47.06133 1.000 17.92061 ?  116 THR A H    1 
ATOM   1852 H  HA   . THR A 1 116 ? 33.62902 28.47919 49.50475 1.000 18.09312 ?  116 THR A HA   1 
ATOM   1853 H  HB   . THR A 1 116 ? 35.68010 27.71996 48.71193 1.000 18.95302 ?  116 THR A HB   1 
ATOM   1854 H  HG1  . THR A 1 116 ? 35.18115 29.09498 46.52826 1.000 21.81690 ?  116 THR A HG1  1 
ATOM   1855 H  HG21 . THR A 1 116 ? 34.97795 26.22734 47.16076 1.000 18.85926 ?  116 THR A HG21 1 
ATOM   1856 H  HG22 . THR A 1 116 ? 33.89342 26.35629 48.30079 1.000 18.85926 ?  116 THR A HG22 1 
ATOM   1857 H  HG23 . THR A 1 116 ? 33.66407 27.06575 46.90919 1.000 18.85926 ?  116 THR A HG23 1 
ATOM   1858 N  N    . SER A 1 117 ? 34.46688 31.38276 49.08796 1.000 15.99471 ?  117 SER A N    1 
ATOM   1859 C  CA   . SER A 1 117 ? 34.79633 32.56961 49.88674 1.000 15.27683 ?  117 SER A CA   1 
ATOM   1860 C  C    . SER A 1 117 ? 33.71464 32.74583 50.93631 1.000 15.79110 ?  117 SER A C    1 
ATOM   1861 O  O    . SER A 1 117 ? 32.72720 32.01280 50.96934 1.000 16.66910 ?  117 SER A O    1 
ATOM   1862 C  CB   . SER A 1 117 ? 34.83449 33.81262 48.94886 1.000 15.99167 ?  117 SER A CB   1 
ATOM   1863 O  OG   . SER A 1 117 ? 33.56405 34.39862 48.76512 1.000 16.71884 ?  117 SER A OG   1 
ATOM   1864 H  H    . SER A 1 117 ? 34.07169 31.57006 48.34746 1.000 19.19995 ?  117 SER A H    1 
ATOM   1865 H  HA   . SER A 1 117 ? 35.65922 32.47963 50.32058 1.000 18.33850 ?  117 SER A HA   1 
ATOM   1866 H  HB2  . SER A 1 117 ? 35.42545 34.47511 49.33970 1.000 19.19631 ?  117 SER A HB2  1 
ATOM   1867 H  HB3  . SER A 1 117 ? 35.17350 33.53500 48.08347 1.000 19.19631 ?  117 SER A HB3  1 
ATOM   1868 H  HG   . SER A 1 117 ? 33.03586 33.83947 48.42751 1.000 20.06892 ?  117 SER A HG   1 
ATOM   1869 N  N    . ASP A 1 118 ? 33.91248 33.73639 51.81385 1.000 15.71505 ?  118 ASP A N    1 
ATOM   1870 C  CA   . ASP A 1 118 ? 32.90987 34.15083 52.78997 1.000 16.24830 ?  118 ASP A CA   1 
ATOM   1871 C  C    . ASP A 1 118 ? 32.34926 35.54076 52.48752 1.000 15.62148 ?  118 ASP A C    1 
ATOM   1872 O  O    . ASP A 1 118 ? 31.72798 36.15592 53.35178 1.000 17.82029 ?  118 ASP A O    1 
ATOM   1873 C  CB   . ASP A 1 118 ? 33.50902 34.12950 54.20760 1.000 18.52512 ?  118 ASP A CB   1 
ATOM   1874 C  CG   . ASP A 1 118 ? 33.98442 32.76313 54.57113 1.000 20.48856 ?  118 ASP A CG   1 
ATOM   1875 O  OD1  . ASP A 1 118 ? 33.12584 31.83890 54.46028 1.000 24.11092 ?  118 ASP A OD1  1 
ATOM   1876 O  OD2  . ASP A 1 118 ? 35.14429 32.50891 54.84674 1.000 18.71807 -1 118 ASP A OD2  1 
ATOM   1877 H  H    . ASP A 1 118 ? 34.64003 34.19253 51.86087 1.000 18.86437 ?  118 ASP A H    1 
ATOM   1878 H  HA   . ASP A 1 118 ? 32.17514 33.51831 52.75856 1.000 19.50426 ?  118 ASP A HA   1 
ATOM   1879 H  HB2  . ASP A 1 118 ? 34.26379 34.73747 54.24753 1.000 22.23645 ?  118 ASP A HB2  1 
ATOM   1880 H  HB3  . ASP A 1 118 ? 32.83179 34.39890 54.84766 1.000 22.23645 ?  118 ASP A HB3  1 
ATOM   1881 N  N    . GLU A 1 119 ? 32.54683 36.05868 51.27498 1.000 15.54969 ?  119 GLU A N    1 
ATOM   1882 C  CA   . GLU A 1 119 ? 32.04989 37.38327 50.94073 1.000 15.52597 ?  119 GLU A CA   1 
ATOM   1883 C  C    . GLU A 1 119 ? 30.51291 37.38521 51.01954 1.000 15.55948 ?  119 GLU A C    1 
ATOM   1884 O  O    . GLU A 1 119 ? 29.84405 36.45464 50.55567 1.000 16.41395 ?  119 GLU A O    1 
ATOM   1885 C  CB   . GLU A 1 119 ? 32.54821 37.70589 49.52544 1.000 16.93771 ?  119 GLU A CB   1 
ATOM   1886 C  CG   . GLU A 1 119 ? 32.25704 39.16475 49.07149 1.000 18.99682 ?  119 GLU A CG   1 
ATOM   1887 C  CD   . GLU A 1 119 ? 33.11245 39.53901 47.86851 1.000 20.75508 ?  119 GLU A CD   1 
ATOM   1888 O  OE1  . GLU A 1 119 ? 34.35859 39.33442 47.97056 1.000 21.62363 ?  119 GLU A OE1  1 
ATOM   1889 O  OE2  . GLU A 1 119 ? 32.59876 40.10778 46.92844 1.000 23.79795 -1 119 GLU A OE2  1 
ATOM   1890 H  H    . GLU A 1 119 ? 32.96325 35.66312 50.63488 1.000 18.66592 ?  119 GLU A H    1 
ATOM   1891 H  HA   . GLU A 1 119 ? 32.36651 38.06859 51.54981 1.000 18.63746 ?  119 GLU A HA   1 
ATOM   1892 H  HB2  . GLU A 1 119 ? 33.50868 37.57346 49.49603 1.000 20.33155 ?  119 GLU A HB2  1 
ATOM   1893 H  HB3  . GLU A 1 119 ? 32.11159 37.10859 48.89815 1.000 20.33155 ?  119 GLU A HB3  1 
ATOM   1894 H  HG2  . GLU A 1 119 ? 31.32307 39.24561 48.82238 1.000 22.80249 ?  119 GLU A HG2  1 
ATOM   1895 H  HG3  . GLU A 1 119 ? 32.46111 39.77589 49.79659 1.000 22.80249 ?  119 GLU A HG3  1 
ATOM   1896 N  N    . ALA A 1 120 ? 29.96179 38.47705 51.55888 1.000 15.74174 ?  120 ALA A N    1 
ATOM   1897 C  CA   . ALA A 1 120 ? 28.53067 38.62332 51.68656 1.000 15.40940 ?  120 ALA A CA   1 
ATOM   1898 C  C    . ALA A 1 120 ? 27.92544 39.24485 50.44334 1.000 15.52162 ?  120 ALA A C    1 
ATOM   1899 O  O    . ALA A 1 120 ? 28.49946 40.12796 49.84301 1.000 16.50526 ?  120 ALA A O    1 
ATOM   1900 C  CB   . ALA A 1 120 ? 28.21643 39.44107 52.91516 1.000 17.85199 ?  120 ALA A CB   1 
ATOM   1901 H  H    . ALA A 1 120 ? 30.40970 39.14752 51.85797 1.000 18.89639 ?  120 ALA A H    1 
ATOM   1902 H  HA   . ALA A 1 120 ? 28.11463 37.75255 51.78436 1.000 18.49758 ?  120 ALA A HA   1 
ATOM   1903 H  HB1  . ALA A 1 120 ? 27.25478 39.54530 52.98769 1.000 21.42868 ?  120 ALA A HB1  1 
ATOM   1904 H  HB2  . ALA A 1 120 ? 28.55915 38.98067 53.69713 1.000 21.42868 ?  120 ALA A HB2  1 
ATOM   1905 H  HB3  . ALA A 1 120 ? 28.63806 40.31068 52.83206 1.000 21.42868 ?  120 ALA A HB3  1 
ATOM   1906 N  N    . THR A 1 121 ? 26.72116 38.83303 50.10460 1.000 14.35560 ?  121 THR A N    1 
ATOM   1907 C  CA   . THR A 1 121 ? 26.00791 39.37909 48.96780 1.000 14.66576 ?  121 THR A CA   1 
ATOM   1908 C  C    . THR A 1 121 ? 24.53647 39.04834 49.14827 1.000 14.70061 ?  121 THR A C    1 
ATOM   1909 O  O    . THR A 1 121 ? 24.19250 38.10790 49.87767 1.000 15.37270 ?  121 THR A O    1 
ATOM   1910 C  CB   . THR A 1 121 ? 26.55496 38.79158 47.64904 1.000 14.56332 ?  121 THR A CB   1 
ATOM   1911 O  OG1  . THR A 1 121 ? 26.07965 39.58660 46.57237 1.000 15.30176 ?  121 THR A OG1  1 
ATOM   1912 C  CG2  . THR A 1 121 ? 26.13765 37.37872 47.44170 1.000 15.43915 ?  121 THR A CG2  1 
ATOM   1913 H  H    . THR A 1 121 ? 26.28385 38.22411 50.52599 1.000 17.23303 ?  121 THR A H    1 
ATOM   1914 H  HA   . THR A 1 121 ? 26.10299 40.34370 48.93059 1.000 17.60521 ?  121 THR A HA   1 
ATOM   1915 H  HB   . THR A 1 121 ? 27.52448 38.79407 47.67937 1.000 17.48229 ?  121 THR A HB   1 
ATOM   1916 H  HG1  . THR A 1 121 ? 26.34090 39.26592 45.84127 1.000 18.36841 ?  121 THR A HG1  1 
ATOM   1917 H  HG21 . THR A 1 121 ? 26.67107 36.97489 46.73936 1.000 18.53328 ?  121 THR A HG21 1 
ATOM   1918 H  HG22 . THR A 1 121 ? 26.26024 36.87304 48.26033 1.000 18.53328 ?  121 THR A HG22 1 
ATOM   1919 H  HG23 . THR A 1 121 ? 25.20244 37.34303 47.18670 1.000 18.53328 ?  121 THR A HG23 1 
ATOM   1920 N  N    . THR A 1 122 ? 23.66473 39.72133 48.42226 1.000 14.36099 ?  122 THR A N    1 
ATOM   1921 C  CA   . THR A 1 122 ? 22.27333 39.33415 48.45994 1.000 14.60723 ?  122 THR A CA   1 
ATOM   1922 C  C    . THR A 1 122 ? 22.11211 37.85900 48.10913 1.000 13.98580 ?  122 THR A C    1 
ATOM   1923 O  O    . THR A 1 122 ? 22.55892 37.41167 47.03233 1.000 14.75182 ?  122 THR A O    1 
ATOM   1924 C  CB   . THR A 1 122 ? 21.48984 40.22767 47.49965 1.000 14.48479 ?  122 THR A CB   1 
ATOM   1925 O  OG1  . THR A 1 122 ? 21.74551 41.59009 47.86391 1.000 15.40790 ?  122 THR A OG1  1 
ATOM   1926 C  CG2  . THR A 1 122 ? 20.01095 39.95484 47.56791 1.000 15.92596 ?  122 THR A CG2  1 
ATOM   1927 H  H    . THR A 1 122 ? 23.84975 40.38900 47.91275 1.000 17.23949 ?  122 THR A H    1 
ATOM   1928 H  HA   . THR A 1 122 ? 21.91274 39.45070 49.35285 1.000 17.53497 ?  122 THR A HA   1 
ATOM   1929 H  HB   . THR A 1 122 ? 21.76522 40.05586 46.58557 1.000 17.38805 ?  122 THR A HB   1 
ATOM   1930 H  HG1  . THR A 1 122 ? 21.42337 41.74981 48.62306 1.000 18.49578 ?  122 THR A HG1  1 
ATOM   1931 H  HG21 . THR A 1 122 ? 19.52997 40.59428 47.01957 1.000 19.11746 ?  122 THR A HG21 1 
ATOM   1932 H  HG22 . THR A 1 122 ? 19.82352 39.05953 47.24514 1.000 19.11746 ?  122 THR A HG22 1 
ATOM   1933 H  HG23 . THR A 1 122 ? 19.70161 40.03034 48.48416 1.000 19.11746 ?  122 THR A HG23 1 
ATOM   1934 N  N    A GLY A 1 123 ? 21.40275 37.12766 48.96489 0.498 14.26341 ?  123 GLY A N    1 
ATOM   1935 N  N    B GLY A 1 123 ? 21.40295 37.12770 48.96538 0.502 14.25768 ?  123 GLY A N    1 
ATOM   1936 C  CA   A GLY A 1 123 ? 21.21642 35.69609 48.81634 0.498 15.24724 ?  123 GLY A CA   1 
ATOM   1937 C  CA   B GLY A 1 123 ? 21.21570 35.69613 48.81750 0.502 15.23421 ?  123 GLY A CA   1 
ATOM   1938 C  C    A GLY A 1 123 ? 22.15914 34.84442 49.62860 0.498 15.91161 ?  123 GLY A C    1 
ATOM   1939 C  C    B GLY A 1 123 ? 22.15927 34.84435 49.62854 0.502 15.89440 ?  123 GLY A C    1 
ATOM   1940 O  O    A GLY A 1 123 ? 21.87801 33.64146 49.80581 0.498 16.88339 ?  123 GLY A O    1 
ATOM   1941 O  O    B GLY A 1 123 ? 21.87881 33.64106 49.80501 0.502 16.87204 ?  123 GLY A O    1 
ATOM   1942 H  H    A GLY A 1 123 ? 21.01029 37.45206 49.65796 0.498 17.12239 ?  123 GLY A H    1 
ATOM   1943 H  H    B GLY A 1 123 ? 21.01104 37.45234 49.65864 0.502 17.11552 ?  123 GLY A H    1 
ATOM   1944 H  HA2  A GLY A 1 123 ? 20.31128 35.47156 49.08319 0.498 18.30299 ?  123 GLY A HA2  1 
ATOM   1945 H  HA2  B GLY A 1 123 ? 20.31087 35.47208 49.08582 0.502 18.28736 ?  123 GLY A HA2  1 
ATOM   1946 H  HA3  A GLY A 1 123 ? 21.33752 35.46256 47.88269 0.498 18.30299 ?  123 GLY A HA3  1 
ATOM   1947 H  HA3  B GLY A 1 123 ? 21.33525 35.46226 47.88373 0.502 18.28736 ?  123 GLY A HA3  1 
ATOM   1948 N  N    . SER A 1 124 ? 23.24373 35.40281 50.15537 1.000 16.87080 ?  124 SER A N    1 
ATOM   1949 C  CA   . SER A 1 124 ? 24.09900 34.62361 51.04994 1.000 17.61243 ?  124 SER A CA   1 
ATOM   1950 C  C    . SER A 1 124 ? 23.56938 34.63440 52.47590 1.000 18.04557 ?  124 SER A C    1 
ATOM   1951 O  O    . SER A 1 124 ? 22.71986 35.45344 52.85756 1.000 17.36343 ?  124 SER A O    1 
ATOM   1952 C  CB   . SER A 1 124 ? 25.53550 35.11246 51.00360 1.000 18.50731 ?  124 SER A CB   1 
ATOM   1953 O  OG   . SER A 1 124 ? 25.71807 36.40020 51.67918 1.000 18.60776 ?  124 SER A OG   1 
ATOM   1954 H  H    A SER A 1 124 ? 23.50176 36.21114 50.01530 0.498 20.25126 ?  124 SER A H    1 
ATOM   1955 H  H    B SER A 1 124 ? 23.50170 36.21117 50.01536 0.502 20.25126 ?  124 SER A H    1 
ATOM   1956 H  HA   . SER A 1 124 ? 24.09842 33.70103 50.75035 1.000 21.14122 ?  124 SER A HA   1 
ATOM   1957 H  HB2  . SER A 1 124 ? 26.09929 34.45374 51.43849 1.000 22.21507 ?  124 SER A HB2  1 
ATOM   1958 H  HB3  . SER A 1 124 ? 25.79729 35.21192 50.07490 1.000 22.21507 ?  124 SER A HB3  1 
ATOM   1959 H  HG   . SER A 1 124 ? 25.50325 36.33307 52.48846 1.000 22.33561 ?  124 SER A HG   1 
ATOM   1960 N  N    . ILE A 1 125 ? 23.97549 33.61387 53.23883 1.000 17.17605 ?  125 ILE A N    1 
ATOM   1961 C  CA   . ILE A 1 125 ? 23.52637 33.44353 54.60709 1.000 16.93739 ?  125 ILE A CA   1 
ATOM   1962 C  C    . ILE A 1 125 ? 24.73510 33.13514 55.48041 1.000 17.79313 ?  125 ILE A C    1 
ATOM   1963 O  O    . ILE A 1 125 ? 25.79031 32.68783 55.04113 1.000 19.81679 ?  125 ILE A O    1 
ATOM   1964 C  CB   . ILE A 1 125 ? 22.46092 32.33517 54.72681 1.000 16.37034 ?  125 ILE A CB   1 
ATOM   1965 C  CG1  . ILE A 1 125 ? 22.93872 30.99818 54.21468 1.000 17.42492 ?  125 ILE A CG1  1 
ATOM   1966 C  CG2  . ILE A 1 125 ? 21.15303 32.72980 54.04345 1.000 17.29762 ?  125 ILE A CG2  1 
ATOM   1967 C  CD1  . ILE A 1 125 ? 21.99616 29.80717 54.48946 1.000 18.69646 ?  125 ILE A CD1  1 
ATOM   1968 H  H    . ILE A 1 125 ? 24.51939 33.00259 52.97404 1.000 20.61757 ?  125 ILE A H    1 
ATOM   1969 H  HA   . ILE A 1 125 ? 23.13474 34.27084 54.92818 1.000 20.33117 ?  125 ILE A HA   1 
ATOM   1970 H  HB   . ILE A 1 125 ? 22.29753 32.23635 55.67783 1.000 19.65071 ?  125 ILE A HB   1 
ATOM   1971 H  HG12 . ILE A 1 125 ? 23.05085 31.06187 53.25329 1.000 20.91621 ?  125 ILE A HG12 1 
ATOM   1972 H  HG13 . ILE A 1 125 ? 23.78920 30.79638 54.63523 1.000 20.91621 ?  125 ILE A HG13 1 
ATOM   1973 H  HG21 . ILE A 1 125 ? 20.48949 32.04225 54.21045 1.000 20.76345 ?  125 ILE A HG21 1 
ATOM   1974 H  HG22 . ILE A 1 125 ? 20.85019 33.57686 54.40633 1.000 20.76345 ?  125 ILE A HG22 1 
ATOM   1975 H  HG23 . ILE A 1 125 ? 21.30822 32.81506 53.08975 1.000 20.76345 ?  125 ILE A HG23 1 
ATOM   1976 H  HD11 . ILE A 1 125 ? 22.42486 28.98979 54.19112 1.000 22.44205 ?  125 ILE A HD11 1 
ATOM   1977 H  HD12 . ILE A 1 125 ? 21.81792 29.75866 55.44171 1.000 22.44205 ?  125 ILE A HD12 1 
ATOM   1978 H  HD13 . ILE A 1 125 ? 21.16715 29.94202 54.00422 1.000 22.44205 ?  125 ILE A HD13 1 
ATOM   1979 N  N    . THR A 1 126 ? 24.52844 33.28480 56.78529 1.000 19.80452 ?  126 THR A N    1 
ATOM   1980 C  CA   . THR A 1 126 ? 25.58361 33.05755 57.77499 1.000 22.06097 ?  126 THR A CA   1 
ATOM   1981 C  C    . THR A 1 126 ? 25.25497 31.81166 58.58539 1.000 20.75603 ?  126 THR A C    1 
ATOM   1982 O  O    . THR A 1 126 ? 24.17214 31.72163 59.17312 1.000 22.04175 ?  126 THR A O    1 
ATOM   1983 C  CB   . THR A 1 126 ? 25.72735 34.27948 58.70391 1.000 26.58690 ?  126 THR A CB   1 
ATOM   1984 O  OG1  . THR A 1 126 ? 26.23718 35.34567 57.88710 1.000 28.69684 ?  126 THR A OG1  1 
ATOM   1985 C  CG2  . THR A 1 126 ? 26.67865 34.01662 59.83152 1.000 28.51655 ?  126 THR A CG2  1 
ATOM   1986 H  H    . THR A 1 126 ? 23.77582 33.52048 57.12826 1.000 23.77172 ?  126 THR A H    1 
ATOM   1987 H  HA   . THR A 1 126 ? 26.42594 32.90752 57.31797 1.000 26.47947 ?  126 THR A HA   1 
ATOM   1988 H  HB   . THR A 1 126 ? 24.87662 34.50524 59.11158 1.000 31.91058 ?  126 THR A HB   1 
ATOM   1989 H  HG1  . THR A 1 126 ? 25.67795 35.54491 57.29282 1.000 34.44251 ?  126 THR A HG1  1 
ATOM   1990 H  HG21 . THR A 1 126 ? 26.92273 34.85137 60.26108 1.000 34.22617 ?  126 THR A HG21 1 
ATOM   1991 H  HG22 . THR A 1 126 ? 26.26330 33.43485 60.48720 1.000 34.22617 ?  126 THR A HG22 1 
ATOM   1992 H  HG23 . THR A 1 126 ? 27.48176 33.58906 59.49520 1.000 34.22617 ?  126 THR A HG23 1 
ATOM   1993 N  N    . THR A 1 127 ? 26.13102 30.79627 58.50064 1.000 18.83933 ?  127 THR A N    1 
ATOM   1994 C  CA   . THR A 1 127 ? 26.04453 29.58969 59.30954 1.000 19.04481 ?  127 THR A CA   1 
ATOM   1995 C  C    . THR A 1 127 ? 27.41573 29.24233 59.84900 1.000 18.61727 ?  127 THR A C    1 
ATOM   1996 O  O    . THR A 1 127 ? 28.44820 29.73749 59.39267 1.000 19.78379 ?  127 THR A O    1 
ATOM   1997 C  CB   . THR A 1 127 ? 25.50295 28.41185 58.49659 1.000 18.66588 ?  127 THR A CB   1 
ATOM   1998 O  OG1  . THR A 1 127 ? 26.41150 28.12277 57.42196 1.000 18.19492 ?  127 THR A OG1  1 
ATOM   1999 C  CG2  . THR A 1 127 ? 24.15474 28.71476 57.95376 1.000 20.30078 ?  127 THR A CG2  1 
ATOM   2000 H  H    . THR A 1 127 ? 26.80153 30.79235 57.96211 1.000 22.61350 ?  127 THR A H    1 
ATOM   2001 H  HA   . THR A 1 127 ? 25.44922 29.75541 60.05722 1.000 22.86007 ?  127 THR A HA   1 
ATOM   2002 H  HB   . THR A 1 127 ? 25.41872 27.63233 59.06768 1.000 22.40536 ?  127 THR A HB   1 
ATOM   2003 H  HG1  . THR A 1 127 ? 26.50225 28.79943 56.93259 1.000 21.84020 ?  127 THR A HG1  1 
ATOM   2004 H  HG21 . THR A 1 127 ? 23.79569 27.93461 57.50283 1.000 24.36724 ?  127 THR A HG21 1 
ATOM   2005 H  HG22 . THR A 1 127 ? 23.55564 28.96543 58.67428 1.000 24.36724 ?  127 THR A HG22 1 
ATOM   2006 H  HG23 . THR A 1 127 ? 24.20907 29.44732 57.32028 1.000 24.36724 ?  127 THR A HG23 1 
ATOM   2007 N  N    . SER A 1 128 ? 27.41029 28.31331 60.79591 1.000 19.19318 ?  128 SER A N    1 
ATOM   2008 C  CA   . SER A 1 128 ? 28.67744 27.83551 61.32269 1.000 19.49508 ?  128 SER A CA   1 
ATOM   2009 C  C    . SER A 1 128 ? 29.30814 26.77478 60.39266 1.000 19.03148 ?  128 SER A C    1 
ATOM   2010 O  O    . SER A 1 128 ? 28.66287 26.18235 59.51581 1.000 18.76980 ?  128 SER A O    1 
ATOM   2011 C  CB   . SER A 1 128 ? 28.46729 27.19092 62.67407 1.000 20.17570 ?  128 SER A CB   1 
ATOM   2012 O  OG   . SER A 1 128 ? 27.71224 25.98484 62.50853 1.000 20.95755 ?  128 SER A OG   1 
ATOM   2013 H  H    . SER A 1 128 ? 26.70728 27.95558 61.13857 1.000 23.03812 ?  128 SER A H    1 
ATOM   2014 H  HA   . SER A 1 128 ? 29.27513 28.59590 61.39657 1.000 23.40040 ?  128 SER A HA   1 
ATOM   2015 H  HB2  . SER A 1 128 ? 29.32829 26.98060 63.06820 1.000 24.21714 ?  128 SER A HB2  1 
ATOM   2016 H  HB3  . SER A 1 128 ? 27.97903 27.80041 63.24942 1.000 24.21714 ?  128 SER A HB3  1 
ATOM   2017 H  HG   . SER A 1 128 ? 27.58385 25.62154 63.25494 1.000 25.15536 ?  128 SER A HG   1 
ATOM   2018 N  N    . ASP A 1 129 ? 30.58532 26.48895 60.64697 1.000 19.88911 ?  129 ASP A N    1 
ATOM   2019 C  CA   . ASP A 1 129 ? 31.26825 25.40395 59.95343 1.000 22.09075 ?  129 ASP A CA   1 
ATOM   2020 C  C    . ASP A 1 129 ? 30.55997 24.07435 60.18746 1.000 19.86725 ?  129 ASP A C    1 
ATOM   2021 O  O    . ASP A 1 129 ? 30.38057 23.26640 59.26694 1.000 19.17312 ?  129 ASP A O    1 
ATOM   2022 C  CB   . ASP A 1 129 ? 32.70574 25.38775 60.46201 1.000 25.87048 ?  129 ASP A CB   1 
ATOM   2023 C  CG   . ASP A 1 129 ? 33.53598 24.31053 59.87125 1.000 29.32009 ?  129 ASP A CG   1 
ATOM   2024 O  OD1  . ASP A 1 129 ? 33.90704 24.52231 58.72186 1.000 31.37122 ?  129 ASP A OD1  1 
ATOM   2025 O  OD2  . ASP A 1 129 ? 33.93738 23.37728 60.62403 1.000 32.23204 -1 129 ASP A OD2  1 
ATOM   2026 H  H    . ASP A 1 129 ? 31.07641 26.90781 61.21530 1.000 23.87323 ?  129 ASP A H    1 
ATOM   2027 H  HA   . ASP A 1 129 ? 31.27316 25.54032 58.99308 1.000 26.51520 ?  129 ASP A HA   1 
ATOM   2028 H  HB2  . ASP A 1 129 ? 33.12342 26.23585 60.24482 1.000 31.05088 ?  129 ASP A HB2  1 
ATOM   2029 H  HB3  . ASP A 1 129 ? 32.69542 25.25960 61.42345 1.000 31.05088 ?  129 ASP A HB3  1 
ATOM   2030 N  N    . HIS A 1 130 ? 30.12169 23.83321 61.39735 1.000 20.11381 ?  130 HIS A N    1 
ATOM   2031 C  CA   . HIS A 1 130 ? 29.43237 22.61371 61.71356 1.000 21.00351 ?  130 HIS A CA   1 
ATOM   2032 C  C    . HIS A 1 130 ? 28.14860 22.48390 60.92157 1.000 19.54672 ?  130 HIS A C    1 
ATOM   2033 O  O    . HIS A 1 130 ? 27.83285 21.39954 60.42675 1.000 19.50193 ?  130 HIS A O    1 
ATOM   2034 C  CB   . HIS A 1 130 ? 29.06082 22.60497 63.20819 1.000 26.60035 ?  130 HIS A CB   1 
ATOM   2035 C  CG   . HIS A 1 130 ? 28.43432 21.34107 63.57893 1.000 32.73725 ?  130 HIS A CG   1 
ATOM   2036 N  ND1  . HIS A 1 130 ? 27.15513 21.26377 64.05841 1.000 36.48264 ?  130 HIS A ND1  1 
ATOM   2037 C  CD2  . HIS A 1 130 ? 28.91219 20.08485 63.53897 1.000 35.25414 ?  130 HIS A CD2  1 
ATOM   2038 C  CE1  . HIS A 1 130 ? 26.89305 19.99974 64.33351 1.000 37.14423 ?  130 HIS A CE1  1 
ATOM   2039 N  NE2  . HIS A 1 130 ? 27.96904 19.27610 64.08291 1.000 36.95356 ?  130 HIS A NE2  1 
ATOM   2040 H  H    . HIS A 1 130 ? 30.21185 24.36802 62.06477 1.000 24.14287 ?  130 HIS A H    1 
ATOM   2041 H  HA   . HIS A 1 130 ? 30.02212 21.87213 61.50581 1.000 25.21051 ?  130 HIS A HA   1 
ATOM   2042 H  HB2  . HIS A 1 130 ? 29.86299 22.71975 63.74134 1.000 31.92672 ?  130 HIS A HB2  1 
ATOM   2043 H  HB3  . HIS A 1 130 ? 28.43584 23.32414 63.39009 1.000 31.92672 ?  130 HIS A HB3  1 
ATOM   2044 H  HD1  . HIS A 1 130 ? 26.61500 21.92484 64.16256 1.000 43.78547 ?  130 HIS A HD1  1 
ATOM   2045 H  HD2  . HIS A 1 130 ? 29.73695 19.81961 63.20087 1.000 42.31127 ?  130 HIS A HD2  1 
ATOM   2046 H  HE1  . HIS A 1 130 ? 26.08296 19.67216 64.65186 1.000 44.57938 ?  130 HIS A HE1  1 
ATOM   2047 N  N    . GLN A 1 131 ? 27.39076 23.56240 60.80527 1.000 19.20161 ?  131 GLN A N    1 
ATOM   2048 C  CA   . GLN A 1 131 ? 26.15988 23.49040 60.03240 1.000 19.00016 ?  131 GLN A CA   1 
ATOM   2049 C  C    . GLN A 1 131 ? 26.45891 23.19882 58.56423 1.000 16.76293 ?  131 GLN A C    1 
ATOM   2050 O  O    . GLN A 1 131 ? 25.76323 22.39895 57.92781 1.000 17.34182 ?  131 GLN A O    1 
ATOM   2051 C  CB   . GLN A 1 131 ? 25.41508 24.81053 60.19025 1.000 20.89610 ?  131 GLN A CB   1 
ATOM   2052 C  CG   . GLN A 1 131 ? 24.87711 25.01420 61.59700 1.000 24.82398 ?  131 GLN A CG   1 
ATOM   2053 C  CD   . GLN A 1 131 ? 24.24480 26.40752 61.80416 1.000 26.71685 ?  131 GLN A CD   1 
ATOM   2054 O  OE1  . GLN A 1 131 ? 24.84392 27.44424 61.60705 1.000 25.57589 ?  131 GLN A OE1  1 
ATOM   2055 N  NE2  . GLN A 1 131 ? 23.06723 26.39422 62.40882 1.000 30.47505 ?  131 GLN A NE2  1 
ATOM   2056 H  H    . GLN A 1 131 ? 27.56032 24.32987 61.15432 1.000 23.04823 ?  131 GLN A H    1 
ATOM   2057 H  HA   . GLN A 1 131 ? 25.59475 22.77391 60.36130 1.000 22.80649 ?  131 GLN A HA   1 
ATOM   2058 H  HB2  . GLN A 1 131 ? 26.02122 25.54120 59.99120 1.000 25.08163 ?  131 GLN A HB2  1 
ATOM   2059 H  HB3  . GLN A 1 131 ? 24.66450 24.82542 59.57600 1.000 25.08163 ?  131 GLN A HB3  1 
ATOM   2060 H  HG2  . GLN A 1 131 ? 24.19537 24.34714 61.77353 1.000 29.79508 ?  131 GLN A HG2  1 
ATOM   2061 H  HG3  . GLN A 1 131 ? 25.60587 24.91937 62.23010 1.000 29.79508 ?  131 GLN A HG3  1 
ATOM   2062 H  HE21 . GLN A 1 131 ? 22.71670 25.64722 62.65117 1.000 36.57637 ?  131 GLN A HE21 1 
ATOM   2063 H  HE22 . GLN A 1 131 ? 22.65275 27.13257 62.55929 1.000 36.57637 ?  131 GLN A HE22 1 
ATOM   2064 N  N    . LYS A 1 132 ? 27.48782 23.84976 58.01370 1.000 16.74700 ?  132 LYS A N    1 
ATOM   2065 C  CA   . LYS A 1 132 ? 27.85090 23.56720 56.61696 1.000 15.74857 ?  132 LYS A CA   1 
ATOM   2066 C  C    . LYS A 1 132 ? 28.23456 22.11096 56.44156 1.000 15.91956 ?  132 LYS A C    1 
ATOM   2067 O  O    . LYS A 1 132 ? 27.85967 21.49719 55.44627 1.000 16.02173 ?  132 LYS A O    1 
ATOM   2068 C  CB   . LYS A 1 132 ? 29.01529 24.42195 56.16290 1.000 16.17781 ?  132 LYS A CB   1 
ATOM   2069 C  CG   . LYS A 1 132 ? 28.64538 25.87901 55.99707 1.000 16.95134 ?  132 LYS A CG   1 
ATOM   2070 C  CD   . LYS A 1 132 ? 29.86482 26.78440 55.63350 1.000 17.77623 ?  132 LYS A CD   1 
ATOM   2071 C  CE   . LYS A 1 132 ? 29.48855 28.25429 55.48875 1.000 17.95651 ?  132 LYS A CE   1 
ATOM   2072 N  NZ   . LYS A 1 132 ? 29.18129 28.84323 56.80187 1.000 18.81255 ?  132 LYS A NZ   1 
ATOM   2073 H  H    . LYS A 1 132 ? 27.97516 24.43766 58.40927 1.000 20.10270 ?  132 LYS A H    1 
ATOM   2074 H  HA   . LYS A 1 132 ? 27.07877 23.78077 56.07005 1.000 18.90458 ?  132 LYS A HA   1 
ATOM   2075 H  HB2  . LYS A 1 132 ? 29.72389 24.36566 56.82292 1.000 19.41968 ?  132 LYS A HB2  1 
ATOM   2076 H  HB3  . LYS A 1 132 ? 29.33235 24.09373 55.30695 1.000 19.41968 ?  132 LYS A HB3  1 
ATOM   2077 H  HG2  . LYS A 1 132 ? 27.99206 25.95902 55.28456 1.000 20.34791 ?  132 LYS A HG2  1 
ATOM   2078 H  HG3  . LYS A 1 132 ? 28.26982 26.20540 56.82973 1.000 20.34791 ?  132 LYS A HG3  1 
ATOM   2079 H  HD2  . LYS A 1 132 ? 30.53113 26.71389 56.33490 1.000 21.33777 ?  132 LYS A HD2  1 
ATOM   2080 H  HD3  . LYS A 1 132 ? 30.23890 26.48689 54.78943 1.000 21.33777 ?  132 LYS A HD3  1 
ATOM   2081 H  HE2  . LYS A 1 132 ? 30.23031 28.74197 55.09776 1.000 21.55411 ?  132 LYS A HE2  1 
ATOM   2082 H  HE3  . LYS A 1 132 ? 28.70427 28.33418 54.92357 1.000 21.55411 ?  132 LYS A HE3  1 
ATOM   2083 H  HZ1  . LYS A 1 132 ? 28.49577 28.41515 57.17459 1.000 22.58136 ?  132 LYS A HZ1  1 
ATOM   2084 H  HZ2  . LYS A 1 132 ? 29.88869 28.77766 57.33795 1.000 22.58136 ?  132 LYS A HZ2  1 
ATOM   2085 H  HZ3  . LYS A 1 132 ? 28.96871 29.70236 56.70794 1.000 22.58136 ?  132 LYS A HZ3  1 
ATOM   2086 N  N    . LYS A 1 133 ? 29.00899 21.54032 57.37798 1.000 16.09877 ?  133 LYS A N    1 
ATOM   2087 C  CA   . LYS A 1 133 ? 29.39402 20.15263 57.25332 1.000 16.27691 ?  133 LYS A CA   1 
ATOM   2088 C  C    . LYS A 1 133 ? 28.18908 19.21485 57.37181 1.000 16.36465 ?  133 LYS A C    1 
ATOM   2089 O  O    . LYS A 1 133 ? 28.14613 18.18177 56.68842 1.000 17.41545 ?  133 LYS A O    1 
ATOM   2090 C  CB   . LYS A 1 133 ? 30.49578 19.78624 58.28650 1.000 18.47041 ?  133 LYS A CB   1 
ATOM   2091 C  CG   . LYS A 1 133 ? 31.78597 20.50123 58.00554 1.000 20.85319 ?  133 LYS A CG   1 
ATOM   2092 C  CD   . LYS A 1 133 ? 32.81589 20.31809 59.14021 1.000 23.46835 ?  133 LYS A CD   1 
ATOM   2093 C  CE   . LYS A 1 133 ? 34.17826 20.74535 58.67983 1.000 26.37121 ?  133 LYS A CE   1 
ATOM   2094 N  NZ   . LYS A 1 133 ? 35.10587 21.00713 59.80780 1.000 29.40386 ?  133 LYS A NZ   1 
ATOM   2095 H  H    . LYS A 1 133 ? 29.31280 21.93778 58.07750 1.000 19.32483 ?  133 LYS A H    1 
ATOM   2096 H  HA   . LYS A 1 133 ? 29.77666 20.02592 56.37104 1.000 19.53860 ?  133 LYS A HA   1 
ATOM   2097 H  HB2  . LYS A 1 133 ? 30.19642 20.03665 59.17452 1.000 22.17079 ?  133 LYS A HB2  1 
ATOM   2098 H  HB3  . LYS A 1 133 ? 30.66290 18.83146 58.24969 1.000 22.17079 ?  133 LYS A HB3  1 
ATOM   2099 H  HG2  . LYS A 1 133 ? 32.17262 20.15066 57.18792 1.000 25.03014 ?  133 LYS A HG2  1 
ATOM   2100 H  HG3  . LYS A 1 133 ? 31.60949 21.45012 57.90881 1.000 25.03014 ?  133 LYS A HG3  1 
ATOM   2101 H  HD2  . LYS A 1 133 ? 32.56153 20.86180 59.90216 1.000 28.16833 ?  133 LYS A HD2  1 
ATOM   2102 H  HD3  . LYS A 1 133 ? 32.85459 19.38365 59.39757 1.000 28.16833 ?  133 LYS A HD3  1 
ATOM   2103 H  HE2  . LYS A 1 133 ? 34.56231 20.04295 58.13206 1.000 31.65176 ?  133 LYS A HE2  1 
ATOM   2104 H  HE3  . LYS A 1 133 ? 34.09630 21.56193 58.16275 1.000 31.65176 ?  133 LYS A HE3  1 
ATOM   2105 H  HZ1  . LYS A 1 133 ? 35.89763 21.26839 59.49644 1.000 35.29094 ?  133 LYS A HZ1  1 
ATOM   2106 H  HZ2  . LYS A 1 133 ? 34.77586 21.64695 60.33109 1.000 35.29094 ?  133 LYS A HZ2  1 
ATOM   2107 H  HZ3  . LYS A 1 133 ? 35.21504 20.26718 60.29015 1.000 35.29094 ?  133 LYS A HZ3  1 
ATOM   2108 N  N    . THR A 1 134 ? 27.24182 19.53290 58.25195 1.000 17.22205 ?  134 THR A N    1 
ATOM   2109 C  CA   . THR A 1 134 ? 26.05106 18.72578 58.37379 1.000 17.28176 ?  134 THR A CA   1 
ATOM   2110 C  C    . THR A 1 134 ? 25.26745 18.74189 57.07619 1.000 16.71465 ?  134 THR A C    1 
ATOM   2111 O  O    . THR A 1 134 ? 24.84422 17.69493 56.56823 1.000 16.46282 ?  134 THR A O    1 
ATOM   2112 C  CB   . THR A 1 134 ? 25.20917 19.23978 59.52134 1.000 19.31089 ?  134 THR A CB   1 
ATOM   2113 O  OG1  . THR A 1 134 ? 25.92184 19.07008 60.73877 1.000 21.46804 ?  134 THR A OG1  1 
ATOM   2114 C  CG2  . THR A 1 134 ? 23.92446 18.49165 59.58618 1.000 21.24341 ?  134 THR A CG2  1 
ATOM   2115 H  H    . THR A 1 134 ? 27.27117 20.20822 58.78363 1.000 20.67277 ?  134 THR A H    1 
ATOM   2116 H  HA   . THR A 1 134 ? 26.29285 17.80698 58.56936 1.000 20.74441 ?  134 THR A HA   1 
ATOM   2117 H  HB   . THR A 1 134 ? 25.01057 20.18064 59.39393 1.000 23.17938 ?  134 THR A HB   1 
ATOM   2118 H  HG1  . THR A 1 134 ? 26.64679 19.49334 60.70870 1.000 25.76796 ?  134 THR A HG1  1 
ATOM   2119 H  HG21 . THR A 1 134 ? 23.52984 18.58579 60.46727 1.000 25.49840 ?  134 THR A HG21 1 
ATOM   2120 H  HG22 . THR A 1 134 ? 23.30498 18.83825 58.92512 1.000 25.49840 ?  134 THR A HG22 1 
ATOM   2121 H  HG23 . THR A 1 134 ? 24.07932 17.55052 59.40953 1.000 25.49840 ?  134 THR A HG23 1 
ATOM   2122 N  N    . LEU A 1 135 ? 25.10842 19.91322 56.48078 1.000 16.24219 ?  135 LEU A N    1 
ATOM   2123 C  CA   . LEU A 1 135 ? 24.37398 20.04885 55.23524 1.000 15.31344 ?  135 LEU A CA   1 
ATOM   2124 C  C    . LEU A 1 135 ? 25.12143 19.33147 54.11297 1.000 15.25846 ?  135 LEU A C    1 
ATOM   2125 O  O    . LEU A 1 135 ? 24.48423 18.77251 53.20465 1.000 15.75262 ?  135 LEU A O    1 
ATOM   2126 C  CB   . LEU A 1 135 ? 24.13634 21.53865 54.94562 1.000 15.41785 ?  135 LEU A CB   1 
ATOM   2127 C  CG   . LEU A 1 135 ? 23.15835 22.19686 55.92014 1.000 16.59464 ?  135 LEU A CG   1 
ATOM   2128 C  CD1  . LEU A 1 135 ? 23.21360 23.72866 55.80396 1.000 18.33352 ?  135 LEU A CD1  1 
ATOM   2129 C  CD2  . LEU A 1 135 ? 21.75073 21.81561 55.61067 1.000 19.33083 ?  135 LEU A CD2  1 
ATOM   2130 H  H    . LEU A 1 135 ? 25.42009 20.65644 56.78094 1.000 19.49693 ?  135 LEU A H    1 
ATOM   2131 H  HA   . LEU A 1 135 ? 23.49633 19.64064 55.29859 1.000 18.38244 ?  135 LEU A HA   1 
ATOM   2132 H  HB2  . LEU A 1 135 ? 24.98260 22.00848 55.00896 1.000 18.50773 ?  135 LEU A HB2  1 
ATOM   2133 H  HB3  . LEU A 1 135 ? 23.77273 21.62926 54.05093 1.000 18.50773 ?  135 LEU A HB3  1 
ATOM   2134 H  HG   . LEU A 1 135 ? 23.41013 21.90313 56.80966 1.000 19.91987 ?  135 LEU A HG   1 
ATOM   2135 H  HD11 . LEU A 1 135 ? 22.61784 24.11709 56.46357 1.000 22.00653 ?  135 LEU A HD11 1 
ATOM   2136 H  HD12 . LEU A 1 135 ? 24.12317 24.02495 55.96458 1.000 22.00653 ?  135 LEU A HD12 1 
ATOM   2137 H  HD13 . LEU A 1 135 ? 22.93385 23.98802 54.91212 1.000 22.00653 ?  135 LEU A HD13 1 
ATOM   2138 H  HD21 . LEU A 1 135 ? 21.15704 22.27255 56.22682 1.000 23.20330 ?  135 LEU A HD21 1 
ATOM   2139 H  HD22 . LEU A 1 135 ? 21.54599 22.07655 54.69914 1.000 23.20330 ?  135 LEU A HD22 1 
ATOM   2140 H  HD23 . LEU A 1 135 ? 21.65462 20.85544 55.70938 1.000 23.20330 ?  135 LEU A HD23 1 
ATOM   2141 N  N    . ALA A 1 136 ? 26.44683 19.39875 54.11651 1.000 14.92617 ?  136 ALA A N    1 
ATOM   2142 C  CA   . ALA A 1 136 ? 27.16521 18.67729 53.07248 1.000 15.35424 ?  136 ALA A CA   1 
ATOM   2143 C  C    . ALA A 1 136 ? 26.91766 17.20126 53.18776 1.000 16.13947 ?  136 ALA A C    1 
ATOM   2144 O  O    . ALA A 1 136 ? 26.67067 16.51360 52.19732 1.000 16.85190 ?  136 ALA A O    1 
ATOM   2145 C  CB   . ALA A 1 136 ? 28.66485 18.97380 53.19844 1.000 16.02021 ?  136 ALA A CB   1 
ATOM   2146 H  H    . ALA A 1 136 ? 26.92978 19.83159 54.68131 1.000 17.91771 ?  136 ALA A H    1 
ATOM   2147 H  HA   . ALA A 1 136 ? 26.85875 18.97386 52.20126 1.000 18.43139 ?  136 ALA A HA   1 
ATOM   2148 H  HB1  . ALA A 1 136 ? 29.14028 18.50057 52.49778 1.000 19.23055 ?  136 ALA A HB1  1 
ATOM   2149 H  HB2  . ALA A 1 136 ? 28.80663 19.92905 53.10738 1.000 19.23055 ?  136 ALA A HB2  1 
ATOM   2150 H  HB3  . ALA A 1 136 ? 28.97392 18.67493 54.06795 1.000 19.23055 ?  136 ALA A HB3  1 
ATOM   2151 N  N    . ARG A 1 137 ? 27.02917 16.67763 54.39076 1.000 16.88151 ?  137 ARG A N    1 
ATOM   2152 C  CA   . ARG A 1 137 ? 26.80933 15.25887 54.57656 1.000 18.28571 ?  137 ARG A CA   1 
ATOM   2153 C  C    . ARG A 1 137 ? 25.41690 14.85577 54.11764 1.000 17.75492 ?  137 ARG A C    1 
ATOM   2154 O  O    . ARG A 1 137 ? 25.24147 13.78809 53.48835 1.000 20.04408 ?  137 ARG A O    1 
ATOM   2155 C  CB   . ARG A 1 137 ? 27.05614 14.92911 56.04705 1.000 20.89508 ?  137 ARG A CB   1 
ATOM   2156 C  CG   . ARG A 1 137 ? 26.69461 13.46717 56.35588 1.000 27.75679 ?  137 ARG A CG   1 
ATOM   2157 C  CD   . ARG A 1 137 ? 26.98455 13.09278 57.81523 1.000 35.70473 ?  137 ARG A CD   1 
ATOM   2158 N  NE   . ARG A 1 137 ? 25.94911 13.55075 58.73593 1.000 42.13552 ?  137 ARG A NE   1 
ATOM   2159 C  CZ   . ARG A 1 137 ? 26.13777 14.44713 59.70516 1.000 46.60115 ?  137 ARG A CZ   1 
ATOM   2160 N  NH1  . ARG A 1 137 ? 27.30414 15.06270 59.85985 1.000 48.09341 ?  137 ARG A NH1  1 
ATOM   2161 N  NH2  . ARG A 1 137 ? 25.13881 14.72394 60.55047 1.000 47.91414 ?  137 ARG A NH2  1 
ATOM   2162 H  H    . ARG A 1 137 ? 27.22766 17.11288 55.10543 1.000 20.26411 ?  137 ARG A H    1 
ATOM   2163 H  HA   . ARG A 1 137 ? 27.43088 14.73968 54.04268 1.000 21.94915 ?  137 ARG A HA   1 
ATOM   2164 H  HB2  . ARG A 1 137 ? 27.99417 15.06387 56.25405 1.000 25.08040 ?  137 ARG A HB2  1 
ATOM   2165 H  HB3  . ARG A 1 137 ? 26.50777 15.50505 56.60246 1.000 25.08040 ?  137 ARG A HB3  1 
ATOM   2166 H  HG2  . ARG A 1 137 ? 25.74818 13.33176 56.19203 1.000 33.31445 ?  137 ARG A HG2  1 
ATOM   2167 H  HG3  . ARG A 1 137 ? 27.21714 12.88249 55.78492 1.000 33.31445 ?  137 ARG A HG3  1 
ATOM   2168 H  HD2  . ARG A 1 137 ? 27.04342 12.12728 57.88770 1.000 42.85198 ?  137 ARG A HD2  1 
ATOM   2169 H  HD3  . ARG A 1 137 ? 27.82409 13.49746 58.08411 1.000 42.85198 ?  137 ARG A HD3  1 
ATOM   2170 H  HE   . ARG A 1 137 ? 25.16074 13.21880 58.64713 1.000 50.56893 ?  137 ARG A HE   1 
ATOM   2171 H  HH11 . ARG A 1 137 ? 27.95724 14.88621 59.32890 1.000 57.71840 ?  137 ARG A HH11 1 
ATOM   2172 H  HH12 . ARG A 1 137 ? 27.40643 15.63786 60.49098 1.000 57.71840 ?  137 ARG A HH12 1 
ATOM   2173 H  HH21 . ARG A 1 137 ? 24.38160 14.32490 60.46670 1.000 57.50327 ?  137 ARG A HH21 1 
ATOM   2174 H  HH22 . ARG A 1 137 ? 25.25372 15.30094 61.17774 1.000 57.50327 ?  137 ARG A HH22 1 
ATOM   2175 N  N    . ASN A 1 138 ? 24.41116 15.68195 54.41527 1.000 17.08308 ?  138 ASN A N    1 
ATOM   2176 C  CA   . ASN A 1 138 ? 23.04703 15.29755 54.09945 1.000 17.11416 ?  138 ASN A CA   1 
ATOM   2177 C  C    . ASN A 1 138 ? 22.61990 15.66029 52.68934 1.000 16.68569 ?  138 ASN A C    1 
ATOM   2178 O  O    . ASN A 1 138 ? 21.47354 15.32499 52.30709 1.000 17.10327 ?  138 ASN A O    1 
ATOM   2179 C  CB   . ASN A 1 138 ? 22.11851 15.94189 55.15312 1.000 19.38242 ?  138 ASN A CB   1 
ATOM   2180 C  CG   . ASN A 1 138 ? 22.34189 15.34671 56.53114 1.000 22.24481 ?  138 ASN A CG   1 
ATOM   2181 O  OD1  . ASN A 1 138 ? 22.79462 14.18239 56.66878 1.000 25.15251 ?  138 ASN A OD1  1 
ATOM   2182 N  ND2  . ASN A 1 138 ? 21.98000 16.08394 57.52162 1.000 24.40644 ?  138 ASN A ND2  1 
ATOM   2183 H  H    . ASN A 1 138 ? 24.49842 16.45052 54.79116 1.000 20.50599 ?  138 ASN A H    1 
ATOM   2184 H  HA   . ASN A 1 138 ? 22.95085 14.33375 54.15174 1.000 20.54330 ?  138 ASN A HA   1 
ATOM   2185 H  HB2  . ASN A 1 138 ? 22.29791 16.89404 55.19933 1.000 23.26521 ?  138 ASN A HB2  1 
ATOM   2186 H  HB3  . ASN A 1 138 ? 21.19405 15.79031 54.90154 1.000 23.26521 ?  138 ASN A HB3  1 
ATOM   2187 H  HD21 . ASN A 1 138 ? 22.08127 15.80135 58.32753 1.000 29.29402 ?  138 ASN A HD21 1 
ATOM   2188 H  HD22 . ASN A 1 138 ? 21.63685 16.85927 57.37774 1.000 29.29402 ?  138 ASN A HD22 1 
ATOM   2189 N  N    . SER A 1 139 ? 23.45898 16.36042 51.92866 1.000 16.32163 ?  139 SER A N    1 
ATOM   2190 C  CA   . SER A 1 139 ? 23.03697 16.84500 50.61578 1.000 15.14038 ?  139 SER A CA   1 
ATOM   2191 C  C    . SER A 1 139 ? 22.70007 15.73407 49.63691 1.000 15.84733 ?  139 SER A C    1 
ATOM   2192 O  O    . SER A 1 139 ? 21.75464 15.86979 48.86587 1.000 15.49622 ?  139 SER A O    1 
ATOM   2193 C  CB   . SER A 1 139 ? 24.12832 17.73030 50.04258 1.000 16.39989 ?  139 SER A CB   1 
ATOM   2194 O  OG   . SER A 1 139 ? 25.36561 17.02163 49.84832 1.000 16.35641 ?  139 SER A OG   1 
ATOM   2195 H  H    . SER A 1 139 ? 24.26561 16.56598 52.14472 1.000 19.59226 ?  139 SER A H    1 
ATOM   2196 H  HA   . SER A 1 139 ? 22.22259 17.35762 50.73785 1.000 18.17476 ?  139 SER A HA   1 
ATOM   2197 H  HB2  . SER A 1 139 ? 23.83028 18.07293 49.18545 1.000 19.68617 ?  139 SER A HB2  1 
ATOM   2198 H  HB3  . SER A 1 139 ? 24.28552 18.46440 50.65682 1.000 19.68617 ?  139 SER A HB3  1 
ATOM   2199 H  HG   . SER A 1 139 ? 25.65439 16.74041 50.58529 1.000 19.63400 ?  139 SER A HG   1 
ATOM   2200 N  N    . ILE A 1 140 ? 23.43776 14.60624 49.67408 1.000 15.76057 ?  140 ILE A N    1 
ATOM   2201 C  CA   . ILE A 1 140 ? 23.16157 13.53156 48.71254 1.000 16.50526 ?  140 ILE A CA   1 
ATOM   2202 C  C    . ILE A 1 140 ? 21.78551 12.95688 48.99803 1.000 16.64971 ?  140 ILE A C    1 
ATOM   2203 O  O    . ILE A 1 140 ? 20.95545 12.80627 48.11061 1.000 17.28633 ?  140 ILE A O    1 
ATOM   2204 C  CB   . ILE A 1 140 ? 24.31081 12.50437 48.74893 1.000 17.08416 ?  140 ILE A CB   1 
ATOM   2205 C  CG1  . ILE A 1 140 ? 25.56988 13.15870 48.08345 1.000 18.01639 ?  140 ILE A CG1  1 
ATOM   2206 C  CG2  . ILE A 1 140 ? 23.90150 11.21205 48.03254 1.000 18.20687 ?  140 ILE A CG2  1 
ATOM   2207 C  CD1  . ILE A 1 140 ? 26.77851 12.27414 48.02299 1.000 20.87262 ?  140 ILE A CD1  1 
ATOM   2208 H  H    . ILE A 1 140 ? 24.07797 14.44885 50.22630 1.000 18.91899 ?  140 ILE A H    1 
ATOM   2209 H  HA   . ILE A 1 140 ? 23.13391 13.86746 47.80297 1.000 19.81261 ?  140 ILE A HA   1 
ATOM   2210 H  HB   . ILE A 1 140 ? 24.51853 12.26588 49.66592 1.000 20.50729 ?  140 ILE A HB   1 
ATOM   2211 H  HG12 . ILE A 1 140 ? 25.34361 13.40629 47.17328 1.000 21.62597 ?  140 ILE A HG12 1 
ATOM   2212 H  HG13 . ILE A 1 140 ? 25.81151 13.94867 48.59184 1.000 21.62597 ?  140 ILE A HG13 1 
ATOM   2213 H  HG21 . ILE A 1 140 ? 24.68185 10.64419 47.93519 1.000 21.85455 ?  140 ILE A HG21 1 
ATOM   2214 H  HG22 . ILE A 1 140 ? 23.22615 10.75845 48.56080 1.000 21.85455 ?  140 ILE A HG22 1 
ATOM   2215 H  HG23 . ILE A 1 140 ? 23.54358 11.43499 47.15899 1.000 21.85455 ?  140 ILE A HG23 1 
ATOM   2216 H  HD11 . ILE A 1 140 ? 27.54708 12.80677 47.76513 1.000 25.05345 ?  140 ILE A HD11 1 
ATOM   2217 H  HD12 . ILE A 1 140 ? 26.92655 11.88151 48.89753 1.000 25.05345 ?  140 ILE A HD12 1 
ATOM   2218 H  HD13 . ILE A 1 140 ? 26.62578 11.57507 47.36811 1.000 25.05345 ?  140 ILE A HD13 1 
ATOM   2219 N  N    . SER A 1 141 ? 21.47293 12.71594 50.26596 1.000 16.60567 ?  141 SER A N    1 
ATOM   2220 C  CA   . SER A 1 141 ? 20.14321 12.27359 50.63057 1.000 17.01019 ?  141 SER A CA   1 
ATOM   2221 C  C    . SER A 1 141 ? 19.06078 13.28374 50.20448 1.000 16.45803 ?  141 SER A C    1 
ATOM   2222 O  O    . SER A 1 141 ? 17.98602 12.89484 49.69566 1.000 16.98258 ?  141 SER A O    1 
ATOM   2223 C  CB   . SER A 1 141 ? 20.15369 12.01192 52.12549 1.000 20.25916 ?  141 SER A CB   1 
ATOM   2224 O  OG   . SER A 1 141 ? 18.89411 11.57077 52.53300 1.000 23.62434 ?  141 SER A OG   1 
ATOM   2225 H  H    . SER A 1 141 ? 22.01340 12.80171 50.92939 1.000 19.93310 ?  141 SER A H    1 
ATOM   2226 H  HA   . SER A 1 141 ? 19.91175 11.45213 50.16956 1.000 20.41853 ?  141 SER A HA   1 
ATOM   2227 H  HB2  . SER A 1 141 ? 20.81302 11.32956 52.32691 1.000 24.31730 ?  141 SER A HB2  1 
ATOM   2228 H  HB3  . SER A 1 141 ? 20.37257 12.83306 52.59316 1.000 24.31730 ?  141 SER A HB3  1 
ATOM   2229 H  HG   . SER A 1 141 ? 18.68969 10.86679 52.12285 1.000 28.35551 ?  141 SER A HG   1 
ATOM   2230 N  N    . TYR A 1 142 ? 19.26975 14.57681 50.51015 1.000 16.19826 ?  142 TYR A N    1 
ATOM   2231 C  CA   . TYR A 1 142 ? 18.32294 15.59519 50.10753 1.000 16.07366 ?  142 TYR A CA   1 
ATOM   2232 C  C    . TYR A 1 142 ? 18.04558 15.47827 48.61409 1.000 15.61928 ?  142 TYR A C    1 
ATOM   2233 O  O    . TYR A 1 142 ? 16.89689 15.48407 48.19283 1.000 16.14616 ?  142 TYR A O    1 
ATOM   2234 C  CB   . TYR A 1 142 ? 18.83052 17.01345 50.45496 1.000 16.94531 ?  142 TYR A CB   1 
ATOM   2235 C  CG   . TYR A 1 142 ? 17.81721 18.04407 50.09325 1.000 16.73221 ?  142 TYR A CG   1 
ATOM   2236 C  CD1  . TYR A 1 142 ? 17.80823 18.58833 48.81268 1.000 16.55121 ?  142 TYR A CD1  1 
ATOM   2237 C  CD2  . TYR A 1 142 ? 16.86211 18.45225 50.99049 1.000 18.31374 ?  142 TYR A CD2  1 
ATOM   2238 C  CE1  . TYR A 1 142 ? 16.84375 19.50139 48.43585 1.000 17.72940 ?  142 TYR A CE1  1 
ATOM   2239 C  CE2  . TYR A 1 142 ? 15.91272 19.36441 50.63096 1.000 18.78188 ?  142 TYR A CE2  1 
ATOM   2240 C  CZ   . TYR A 1 142 ? 15.88450 19.86368 49.36709 1.000 18.88117 ?  142 TYR A CZ   1 
ATOM   2241 O  OH   . TYR A 1 142 ? 14.88978 20.75852 49.00595 1.000 20.56908 ?  142 TYR A OH   1 
ATOM   2242 H  H    . TYR A 1 142 ? 19.94885 14.87452 50.94580 1.000 19.44422 ?  142 TYR A H    1 
ATOM   2243 H  HA   . TYR A 1 142 ? 17.49979 15.46700 50.60441 1.000 19.29469 ?  142 TYR A HA   1 
ATOM   2244 H  HB2  . TYR A 1 142 ? 19.00155 17.07065 51.40805 1.000 20.34067 ?  142 TYR A HB2  1 
ATOM   2245 H  HB3  . TYR A 1 142 ? 19.64490 17.19507 49.96028 1.000 20.34067 ?  142 TYR A HB3  1 
ATOM   2246 H  HD1  . TYR A 1 142 ? 18.46143 18.33332 48.20178 1.000 19.86775 ?  142 TYR A HD1  1 
ATOM   2247 H  HD2  . TYR A 1 142 ? 16.86189 18.10353 51.85264 1.000 21.98279 ?  142 TYR A HD2  1 
ATOM   2248 H  HE1  . TYR A 1 142 ? 16.83822 19.86368 47.57934 1.000 21.28158 ?  142 TYR A HE1  1 
ATOM   2249 H  HE2  . TYR A 1 142 ? 15.28199 19.64575 51.25380 1.000 22.54456 ?  142 TYR A HE2  1 
ATOM   2250 H  HH   . TYR A 1 142 ? 14.97091 20.96689 48.19626 1.000 24.68920 ?  142 TYR A HH   1 
ATOM   2251 N  N    . ASN A 1 143 ? 19.09926 15.39509 47.79091 1.000 15.37762 ?  143 ASN A N    1 
ATOM   2252 C  CA   . ASN A 1 143 ? 18.85919 15.39175 46.33827 1.000 15.01547 ?  143 ASN A CA   1 
ATOM   2253 C  C    . ASN A 1 143 ? 18.18071 14.11977 45.85553 1.000 15.16770 ?  143 ASN A C    1 
ATOM   2254 O  O    . ASN A 1 143 ? 17.41783 14.16247 44.89082 1.000 16.52756 ?  143 ASN A O    1 
ATOM   2255 C  CB   . ASN A 1 143 ? 20.15930 15.62695 45.60736 1.000 14.45893 ?  143 ASN A CB   1 
ATOM   2256 C  CG   . ASN A 1 143 ? 20.72502 16.99457 45.82750 1.000 15.24373 ?  143 ASN A CG   1 
ATOM   2257 O  OD1  . ASN A 1 143 ? 19.99358 17.95909 46.08235 1.000 15.13788 ?  143 ASN A OD1  1 
ATOM   2258 N  ND2  . ASN A 1 143 ? 21.99114 17.05596 45.81247 1.000 14.85932 ?  143 ASN A ND2  1 
ATOM   2259 H  H    . ASN A 1 143 ? 19.92261 15.34214 48.03358 1.000 18.45945 ?  143 ASN A H    1 
ATOM   2260 H  HA   . ASN A 1 143 ? 18.25679 16.12134 46.12448 1.000 18.02487 ?  143 ASN A HA   1 
ATOM   2261 H  HB2  . ASN A 1 143 ? 20.81398 14.98116 45.91598 1.000 17.35702 ?  143 ASN A HB2  1 
ATOM   2262 H  HB3  . ASN A 1 143 ? 20.00834 15.51732 44.65547 1.000 17.35702 ?  143 ASN A HB3  1 
ATOM   2263 H  HD21 . ASN A 1 143 ? 22.38652 17.81023 45.93222 1.000 17.83748 ?  143 ASN A HD21 1 
ATOM   2264 H  HD22 . ASN A 1 143 ? 22.45468 16.34333 45.68254 1.000 17.83748 ?  143 ASN A HD22 1 
ATOM   2265 N  N    . THR A 1 144 ? 18.42986 13.01468 46.54957 1.000 15.66785 ?  144 THR A N    1 
ATOM   2266 C  CA   . THR A 1 144 ? 17.93830 11.69620 46.14523 1.000 16.23950 ?  144 THR A CA   1 
ATOM   2267 C  C    . THR A 1 144 ? 16.47552 11.54133 46.48903 1.000 17.92130 ?  144 THR A C    1 
ATOM   2268 O  O    . THR A 1 144 ? 15.75263 10.81828 45.79103 1.000 19.48633 ?  144 THR A O    1 
ATOM   2269 C  CB   . THR A 1 144 ? 18.77215 10.60217 46.83727 1.000 17.72511 ?  144 THR A CB   1 
ATOM   2270 O  OG1  . THR A 1 144 ? 20.14097 10.80549 46.52202 1.000 16.92512 ?  144 THR A OG1  1 
ATOM   2271 C  CG2  . THR A 1 144 ? 18.37858 9.17273  46.51082 1.000 18.09795 ?  144 THR A CG2  1 
ATOM   2272 H  H    . THR A 1 144 ? 18.89110 12.99648 47.27519 1.000 18.80772 ?  144 THR A H    1 
ATOM   2273 H  HA   . THR A 1 144 ? 18.03894 11.59036 45.18629 1.000 19.49370 ?  144 THR A HA   1 
ATOM   2274 H  HB   . THR A 1 144 ? 18.60573 10.68334 47.78943 1.000 21.27643 ?  144 THR A HB   1 
ATOM   2275 H  HG1  . THR A 1 144 ? 20.39937 11.54426 46.82705 1.000 20.31644 ?  144 THR A HG1  1 
ATOM   2276 H  HG21 . THR A 1 144 ? 18.99510 8.55422  46.93302 1.000 21.72385 ?  144 THR A HG21 1 
ATOM   2277 H  HG22 . THR A 1 144 ? 17.48187 8.99340  46.83430 1.000 21.72385 ?  144 THR A HG22 1 
ATOM   2278 H  HG23 . THR A 1 144 ? 18.40077 9.03344  45.55113 1.000 21.72385 ?  144 THR A HG23 1 
ATOM   2279 N  N    . PHE A 1 145 ? 16.04019 12.09716 47.60931 1.000 18.61589 ?  145 PHE A N    1 
ATOM   2280 C  CA   . PHE A 1 145 ? 14.72301 11.83833 48.15358 1.000 19.79811 ?  145 PHE A CA   1 
ATOM   2281 C  C    . PHE A 1 145 ? 13.80970 13.03307 48.22105 1.000 20.68926 ?  145 PHE A C    1 
ATOM   2282 O  O    . PHE A 1 145 ? 12.60751 12.84152 48.21956 1.000 24.70188 ?  145 PHE A O    1 
ATOM   2283 C  CB   . PHE A 1 145 ? 14.81482 11.26005 49.56849 1.000 20.75131 ?  145 PHE A CB   1 
ATOM   2284 C  CG   . PHE A 1 145 ? 15.62705 10.00770 49.63581 1.000 20.82898 ?  145 PHE A CG   1 
ATOM   2285 C  CD1  . PHE A 1 145 ? 15.17895 8.84450  48.99713 1.000 20.98975 ?  145 PHE A CD1  1 
ATOM   2286 C  CD2  . PHE A 1 145 ? 16.82512 9.95482  50.32024 1.000 20.63421 ?  145 PHE A CD2  1 
ATOM   2287 C  CE1  . PHE A 1 145 ? 15.91960 7.62780  49.08758 1.000 21.60402 ?  145 PHE A CE1  1 
ATOM   2288 C  CE2  . PHE A 1 145 ? 17.58292 8.77791  50.37829 1.000 21.10918 ?  145 PHE A CE2  1 
ATOM   2289 C  CZ   . PHE A 1 145 ? 17.12228 7.62375  49.76640 1.000 21.66119 ?  145 PHE A CZ   1 
ATOM   2290 H  H    . PHE A 1 145 ? 16.50478 12.64327 48.08420 1.000 22.34537 ?  145 PHE A H    1 
ATOM   2291 H  HA   . PHE A 1 145 ? 14.31088 11.18130 47.57104 1.000 23.76403 ?  145 PHE A HA   1 
ATOM   2292 H  HB2  . PHE A 1 145 ? 15.22829 11.91656 50.15068 1.000 24.90787 ?  145 PHE A HB2  1 
ATOM   2293 H  HB3  . PHE A 1 145 ? 13.92065 11.05409 49.88303 1.000 24.90787 ?  145 PHE A HB3  1 
ATOM   2294 H  HD1  . PHE A 1 145 ? 14.38844 8.86521  48.50768 1.000 25.19400 ?  145 PHE A HD1  1 
ATOM   2295 H  HD2  . PHE A 1 145 ? 17.13592 10.71746 50.75231 1.000 24.76735 ?  145 PHE A HD2  1 
ATOM   2296 H  HE1  . PHE A 1 145 ? 15.59693 6.84890  48.69503 1.000 25.93113 ?  145 PHE A HE1  1 
ATOM   2297 H  HE2  . PHE A 1 145 ? 18.39668 8.77154  50.82845 1.000 25.33731 ?  145 PHE A HE2  1 
ATOM   2298 H  HZ   . PHE A 1 145 ? 17.62506 6.84276  49.81290 1.000 25.99973 ?  145 PHE A HZ   1 
ATOM   2299 N  N    . GLN A 1 146 ? 14.30869 14.22260 48.46038 1.000 18.96758 ?  146 GLN A N    1 
ATOM   2300 C  CA   . GLN A 1 146 ? 13.45631 15.36375 48.66740 1.000 21.11298 ?  146 GLN A CA   1 
ATOM   2301 C  C    . GLN A 1 146 ? 13.47082 16.38420 47.55519 1.000 21.93227 ?  146 GLN A C    1 
ATOM   2302 O  O    . GLN A 1 146 ? 12.91188 17.42066 47.71893 1.000 27.17128 ?  146 GLN A O    1 
ATOM   2303 C  CB   . GLN A 1 146 ? 13.94247 16.08795 49.91845 1.000 23.84680 ?  146 GLN A CB   1 
ATOM   2304 C  CG   . GLN A 1 146 ? 13.83412 15.25749 51.20421 1.000 29.46868 ?  146 GLN A CG   1 
ATOM   2305 C  CD   . GLN A 1 146 ? 14.43310 15.98715 52.38554 1.000 34.86895 ?  146 GLN A CD   1 
ATOM   2306 O  OE1  . GLN A 1 146 ? 15.48931 15.58803 52.93281 1.000 37.67222 ?  146 GLN A OE1  1 
ATOM   2307 N  NE2  . GLN A 1 146 ? 13.84869 17.15486 52.70028 1.000 36.25636 ?  146 GLN A NE2  1 
ATOM   2308 H  H    . GLN A 1 146 ? 15.14975 14.39559 48.50823 1.000 22.76739 ?  146 GLN A H    1 
ATOM   2309 H  HA   . GLN A 1 146 ? 12.54749 15.03646 48.75583 1.000 25.34188 ?  146 GLN A HA   1 
ATOM   2310 H  HB2  . GLN A 1 146 ? 14.87551 16.32411 49.79777 1.000 28.62246 ?  146 GLN A HB2  1 
ATOM   2311 H  HB3  . GLN A 1 146 ? 13.41029 16.88982 50.03969 1.000 28.62246 ?  146 GLN A HB3  1 
ATOM   2312 H  HG2  . GLN A 1 146 ? 12.89947 15.08203 51.39540 1.000 35.36871 ?  146 GLN A HG2  1 
ATOM   2313 H  HG3  . GLN A 1 146 ? 14.31156 14.42122 51.08758 1.000 35.36871 ?  146 GLN A HG3  1 
ATOM   2314 H  HE21 . GLN A 1 146 ? 13.18038 17.43916 52.23969 1.000 43.51394 ?  146 GLN A HE21 1 
ATOM   2315 H  HE22 . GLN A 1 146 ? 14.14282 17.61822 53.36239 1.000 43.51394 ?  146 GLN A HE22 1 
ATOM   2316 N  N    . ASN A 1 147 ? 14.13990 16.15525 46.47852 1.000 20.60129 ?  147 ASN A N    1 
ATOM   2317 C  CA   . ASN A 1 147 ? 14.37355 17.18665 45.45911 1.000 19.48237 ?  147 ASN A CA   1 
ATOM   2318 C  C    . ASN A 1 147 ? 13.74025 16.65946 44.18122 1.000 19.41529 ?  147 ASN A C    1 
ATOM   2319 O  O    . ASN A 1 147 ? 14.36638 15.96683 43.39758 1.000 18.55150 ?  147 ASN A O    1 
ATOM   2320 C  CB   . ASN A 1 147 ? 15.85011 17.43676 45.39309 1.000 17.60588 ?  147 ASN A CB   1 
ATOM   2321 C  CG   . ASN A 1 147 ? 16.23299 18.51740 44.45202 1.000 16.84644 ?  147 ASN A CG   1 
ATOM   2322 O  OD1  . ASN A 1 147 ? 15.43327 18.92366 43.61876 1.000 16.96439 ?  147 ASN A OD1  1 
ATOM   2323 N  ND2  . ASN A 1 147 ? 17.48722 18.96842 44.53519 1.000 16.93609 ?  147 ASN A ND2  1 
ATOM   2324 H  H    . ASN A 1 147 ? 14.49039 15.39390 46.28589 1.000 24.72785 ?  147 ASN A H    1 
ATOM   2325 H  HA   . ASN A 1 147 ? 13.94115 18.03496 45.64435 1.000 23.38514 ?  147 ASN A HA   1 
ATOM   2326 H  HB2  . ASN A 1 147 ? 16.16365 17.68881 46.27573 1.000 21.13335 ?  147 ASN A HB2  1 
ATOM   2327 H  HB3  . ASN A 1 147 ? 16.29179 16.62299 45.10397 1.000 21.13335 ?  147 ASN A HB3  1 
ATOM   2328 H  HD21 . ASN A 1 147 ? 17.75475 19.59453 44.00982 1.000 20.32962 ?  147 ASN A HD21 1 
ATOM   2329 H  HD22 . ASN A 1 147 ? 18.02738 18.63276 45.11412 1.000 20.32962 ?  147 ASN A HD22 1 
ATOM   2330 N  N    . VAL A 1 148 ? 12.49749 17.04647 43.94694 1.000 20.28116 ?  148 VAL A N    1 
ATOM   2331 C  CA   . VAL A 1 148 ? 11.75156 16.59810 42.79222 1.000 22.99051 ?  148 VAL A CA   1 
ATOM   2332 C  C    . VAL A 1 148 ? 12.45198 16.97436 41.48326 1.000 21.59250 ?  148 VAL A C    1 
ATOM   2333 O  O    . VAL A 1 148 ? 12.50848 16.18570 40.53509 1.000 21.74157 ?  148 VAL A O    1 
ATOM   2334 C  CB   . VAL A 1 148 ? 10.35097 17.24653 42.89233 1.000 28.07452 ?  148 VAL A CB   1 
ATOM   2335 C  CG1  . VAL A 1 148 ? 9.60305  17.01912 41.68849 1.000 30.61077 ?  148 VAL A CG1  1 
ATOM   2336 C  CG2  . VAL A 1 148 ? 9.57959  16.78697 44.11022 1.000 29.78190 ?  148 VAL A CG2  1 
ATOM   2337 H  H    . VAL A 1 148 ? 12.05435 17.58108 44.45431 1.000 24.34369 ?  148 VAL A H    1 
ATOM   2338 H  HA   . VAL A 1 148 ? 11.68793 15.63019 42.79082 1.000 27.59492 ?  148 VAL A HA   1 
ATOM   2339 H  HB   . VAL A 1 148 ? 10.47968 18.20199 42.99927 1.000 33.69572 ?  148 VAL A HB   1 
ATOM   2340 H  HG11 . VAL A 1 148 ? 8.66781  17.21438 41.85611 1.000 36.73923 ?  148 VAL A HG11 1 
ATOM   2341 H  HG12 . VAL A 1 148 ? 9.94268  17.60136 40.99096 1.000 36.73923 ?  148 VAL A HG12 1 
ATOM   2342 H  HG13 . VAL A 1 148 ? 9.70502  16.09151 41.42383 1.000 36.73923 ?  148 VAL A HG13 1 
ATOM   2343 H  HG21 . VAL A 1 148 ? 9.10971  17.54529 44.49110 1.000 35.74458 ?  148 VAL A HG21 1 
ATOM   2344 H  HG22 . VAL A 1 148 ? 8.94426  16.10457 43.84267 1.000 35.74458 ?  148 VAL A HG22 1 
ATOM   2345 H  HG23 . VAL A 1 148 ? 10.20181 16.42332 44.75945 1.000 35.74458 ?  148 VAL A HG23 1 
ATOM   2346 N  N    . ARG A 1 149 ? 12.95282 18.21277 41.38608 1.000 19.53339 ?  149 ARG A N    1 
ATOM   2347 C  CA   . ARG A 1 149 ? 13.61122 18.63895 40.15316 1.000 17.87833 ?  149 ARG A CA   1 
ATOM   2348 C  C    . ARG A 1 149 ? 14.88730 17.86798 39.89362 1.000 17.49846 ?  149 ARG A C    1 
ATOM   2349 O  O    . ARG A 1 149 ? 15.16948 17.54409 38.74439 1.000 18.14798 ?  149 ARG A O    1 
ATOM   2350 C  CB   . ARG A 1 149 ? 13.87387 20.13319 40.20067 1.000 18.34854 ?  149 ARG A CB   1 
ATOM   2351 C  CG   . ARG A 1 149 ? 12.60572 20.92042 40.09708 1.000 19.46824 ?  149 ARG A CG   1 
ATOM   2352 C  CD   . ARG A 1 149 ? 12.77899 22.39852 40.37663 1.000 21.68649 ?  149 ARG A CD   1 
ATOM   2353 N  NE   . ARG A 1 149 ? 12.97908 22.64336 41.80634 1.000 23.10197 ?  149 ARG A NE   1 
ATOM   2354 C  CZ   . ARG A 1 149 ? 13.28635 23.82036 42.31305 1.000 23.54671 ?  149 ARG A CZ   1 
ATOM   2355 N  NH1  . ARG A 1 149 ? 13.47190 24.89159 41.52761 1.000 24.43699 ?  149 ARG A NH1  1 
ATOM   2356 N  NH2  . ARG A 1 149 ? 13.40809 23.93519 43.63134 1.000 23.59949 ?  149 ARG A NH2  1 
ATOM   2357 H  H    . ARG A 1 149 ? 12.92373 18.80846 42.00568 1.000 23.44637 ?  149 ARG A H    1 
ATOM   2358 H  HA   . ARG A 1 149 ? 13.01683 18.46092 39.40757 1.000 21.46030 ?  149 ARG A HA   1 
ATOM   2359 H  HB2  . ARG A 1 149 ? 14.30331 20.35591 41.04143 1.000 22.02455 ?  149 ARG A HB2  1 
ATOM   2360 H  HB3  . ARG A 1 149 ? 14.44801 20.38078 39.45907 1.000 22.02455 ?  149 ARG A HB3  1 
ATOM   2361 H  HG2  . ARG A 1 149 ? 12.25416 20.82953 39.19761 1.000 23.36819 ?  149 ARG A HG2  1 
ATOM   2362 H  HG3  . ARG A 1 149 ? 11.96804 20.57149 40.73935 1.000 23.36819 ?  149 ARG A HG3  1 
ATOM   2363 H  HD2  . ARG A 1 149 ? 13.55469 22.72901 39.89708 1.000 26.03009 ?  149 ARG A HD2  1 
ATOM   2364 H  HD3  . ARG A 1 149 ? 11.98438 22.87629 40.09162 1.000 26.03009 ?  149 ARG A HD3  1 
ATOM   2365 H  HE   . ARG A 1 149 ? 12.89092 21.98033 42.34690 1.000 27.72866 ?  149 ARG A HE   1 
ATOM   2366 H  HH11 . ARG A 1 149 ? 13.39080 24.81855 40.67456 1.000 29.33069 ?  149 ARG A HH11 1 
ATOM   2367 H  HH12 . ARG A 1 149 ? 13.67196 25.65151 41.87703 1.000 29.33069 ?  149 ARG A HH12 1 
ATOM   2368 H  HH21 . ARG A 1 149 ? 13.28686 23.24927 44.13573 1.000 28.32568 ?  149 ARG A HH21 1 
ATOM   2369 H  HH22 . ARG A 1 149 ? 13.60811 24.69543 43.98010 1.000 28.32568 ?  149 ARG A HH22 1 
ATOM   2370 N  N    . PHE A 1 150 ? 15.63651 17.50355 40.93760 1.000 17.23532 ?  150 PHE A N    1 
ATOM   2371 C  CA   . PHE A 1 150 ? 16.83769 16.70010 40.72091 1.000 17.40740 ?  150 PHE A CA   1 
ATOM   2372 C  C    . PHE A 1 150 ? 16.48827 15.34644 40.13570 1.000 18.00537 ?  150 PHE A C    1 
ATOM   2373 O  O    . PHE A 1 150 ? 17.20100 14.83754 39.25761 1.000 18.37247 ?  150 PHE A O    1 
ATOM   2374 C  CB   . PHE A 1 150 ? 17.57832 16.57227 42.04355 1.000 16.82432 ?  150 PHE A CB   1 
ATOM   2375 C  CG   . PHE A 1 150 ? 18.90582 15.90986 41.98104 1.000 15.01518 ?  150 PHE A CG   1 
ATOM   2376 C  CD1  . PHE A 1 150 ? 19.03463 14.49792 42.05308 1.000 15.48071 ?  150 PHE A CD1  1 
ATOM   2377 C  CD2  . PHE A 1 150 ? 20.07585 16.65397 41.93865 1.000 15.53748 ?  150 PHE A CD2  1 
ATOM   2378 C  CE1  . PHE A 1 150 ? 20.28203 13.91730 42.05798 1.000 15.72726 ?  150 PHE A CE1  1 
ATOM   2379 C  CE2  . PHE A 1 150 ? 21.28533 16.08888 41.92441 1.000 15.73709 ?  150 PHE A CE2  1 
ATOM   2380 C  CZ   . PHE A 1 150 ? 21.39265 14.72541 42.00417 1.000 15.70262 ?  150 PHE A CZ   1 
ATOM   2381 H  H    . PHE A 1 150 ? 15.47493 17.70340 41.75830 1.000 20.68869 ?  150 PHE A H    1 
ATOM   2382 H  HA   . PHE A 1 150 ? 17.42703 17.13560 40.08536 1.000 20.89518 ?  150 PHE A HA   1 
ATOM   2383 H  HB2  . PHE A 1 150 ? 17.71865 17.46326 42.40041 1.000 20.19549 ?  150 PHE A HB2  1 
ATOM   2384 H  HB3  . PHE A 1 150 ? 17.02748 16.05445 42.65128 1.000 20.19549 ?  150 PHE A HB3  1 
ATOM   2385 H  HD1  . PHE A 1 150 ? 18.27425 13.96426 42.09706 1.000 18.58315 ?  150 PHE A HD1  1 
ATOM   2386 H  HD2  . PHE A 1 150 ? 20.01539 17.58181 41.91943 1.000 18.65128 ?  150 PHE A HD2  1 
ATOM   2387 H  HE1  . PHE A 1 150 ? 20.37234 12.99252 42.09709 1.000 18.87901 ?  150 PHE A HE1  1 
ATOM   2388 H  HE2  . PHE A 1 150 ? 22.04862 16.61638 41.86088 1.000 18.89081 ?  150 PHE A HE2  1 
ATOM   2389 H  HZ   . PHE A 1 150 ? 22.23752 14.33714 42.02235 1.000 18.84945 ?  150 PHE A HZ   1 
ATOM   2390 N  N    . LYS A 1 151 ? 15.41439 14.74478 40.61222 1.000 18.88275 ?  151 LYS A N    1 
ATOM   2391 C  CA   . LYS A 1 151 ? 15.05070 13.42931 40.11402 1.000 20.82195 ?  151 LYS A CA   1 
ATOM   2392 C  C    . LYS A 1 151 ? 14.62898 13.51957 38.65049 1.000 21.96094 ?  151 LYS A C    1 
ATOM   2393 O  O    . LYS A 1 151 ? 14.88841 12.61155 37.85611 1.000 23.51074 ?  151 LYS A O    1 
ATOM   2394 C  CB   . LYS A 1 151 ? 13.99512 12.81355 41.04733 1.000 24.83624 ?  151 LYS A CB   1 
ATOM   2395 C  CG   . LYS A 1 151 ? 14.47309 12.68610 42.57033 1.000 30.85288 ?  151 LYS A CG   1 
ATOM   2396 C  CD   . LYS A 1 151 ? 13.49828 11.82615 43.46101 1.000 35.92879 ?  151 LYS A CD   1 
ATOM   2397 C  CE   . LYS A 1 151 ? 12.87777 12.67029 44.54191 1.000 38.48027 ?  151 LYS A CE   1 
ATOM   2398 N  NZ   . LYS A 1 151 ? 11.88871 11.85899 45.17444 1.000 39.96923 ?  151 LYS A NZ   1 
ATOM   2399 H  H    . LYS A 1 151 ? 14.88863 15.06721 41.21157 1.000 22.66560 ?  151 LYS A H    1 
ATOM   2400 H  HA   . LYS A 1 151 ? 15.80251 12.81666 40.13258 1.000 24.99265 ?  151 LYS A HA   1 
ATOM   2401 H  HB2  . LYS A 1 151 ? 13.20210 13.37192 41.03195 1.000 29.80979 ?  151 LYS A HB2  1 
ATOM   2402 H  HB3  . LYS A 1 151 ? 13.77988 11.92278 40.72935 1.000 29.80979 ?  151 LYS A HB3  1 
ATOM   2403 H  HG2  . LYS A 1 151 ? 15.34570 12.26302 42.59145 1.000 37.02976 ?  151 LYS A HG2  1 
ATOM   2404 H  HG3  . LYS A 1 151 ? 14.52514 13.57346 42.95863 1.000 37.02976 ?  151 LYS A HG3  1 
ATOM   2405 H  HD2  . LYS A 1 151 ? 12.78863 11.46386 42.90780 1.000 43.12085 ?  151 LYS A HD2  1 
ATOM   2406 H  HD3  . LYS A 1 151 ? 13.99348 11.10485 43.87984 1.000 43.12085 ?  151 LYS A HD3  1 
ATOM   2407 H  HE2  . LYS A 1 151 ? 13.54678 12.93454 45.19267 1.000 46.18263 ?  151 LYS A HE2  1 
ATOM   2408 H  HE3  . LYS A 1 151 ? 12.45785 13.45674 44.15974 1.000 46.18263 ?  151 LYS A HE3  1 
ATOM   2409 H  HZ1  . LYS A 1 151 ? 11.50238 12.31090 45.83673 1.000 47.96938 ?  151 LYS A HZ1  1 
ATOM   2410 H  HZ2  . LYS A 1 151 ? 11.26589 11.62269 44.58423 1.000 47.96938 ?  151 LYS A HZ2  1 
ATOM   2411 H  HZ3  . LYS A 1 151 ? 12.26496 11.12424 45.50712 1.000 47.96938 ?  151 LYS A HZ3  1 
ATOM   2412 N  N    . LEU A 1 152 ? 13.97505 14.61879 38.26329 1.000 21.03161 ?  152 LEU A N    1 
ATOM   2413 C  CA   . LEU A 1 152 ? 13.54692 14.78329 36.89058 1.000 22.20993 ?  152 LEU A CA   1 
ATOM   2414 C  C    . LEU A 1 152 ? 14.68772 15.08092 35.93867 1.000 21.11311 ?  152 LEU A C    1 
ATOM   2415 O  O    . LEU A 1 152 ? 14.70442 14.58783 34.79630 1.000 22.31459 ?  152 LEU A O    1 
ATOM   2416 C  CB   . LEU A 1 152 ? 12.52902 15.91986 36.85598 1.000 25.99293 ?  152 LEU A CB   1 
ATOM   2417 C  CG   . LEU A 1 152 ? 11.19233 15.58130 37.51696 1.000 30.32677 ?  152 LEU A CG   1 
ATOM   2418 C  CD1  . LEU A 1 152 ? 10.30511 16.89115 37.63586 1.000 31.49272 ?  152 LEU A CD1  1 
ATOM   2419 C  CD2  . LEU A 1 152 ? 10.45715 14.50732 36.75553 1.000 32.17153 ?  152 LEU A CD2  1 
ATOM   2420 H  H    . LEU A 1 152 ? 13.77184 15.27604 38.77937 1.000 25.24424 ?  152 LEU A H    1 
ATOM   2421 H  HA   . LEU A 1 152 ? 13.14836 13.95327 36.58541 1.000 26.65822 ?  152 LEU A HA   1 
ATOM   2422 H  HB2  . LEU A 1 152 ? 12.90288 16.68484 37.32065 1.000 31.19782 ?  152 LEU A HB2  1 
ATOM   2423 H  HB3  . LEU A 1 152 ? 12.35119 16.14843 35.93022 1.000 31.19782 ?  152 LEU A HB3  1 
ATOM   2424 H  HG   . LEU A 1 152 ? 11.36053 15.23506 38.40731 1.000 36.39843 ?  152 LEU A HG   1 
ATOM   2425 H  HD11 . LEU A 1 152 ? 9.46474  16.66553 38.06454 1.000 37.79757 ?  152 LEU A HD11 1 
ATOM   2426 H  HD12 . LEU A 1 152 ? 10.78155 17.54813 38.16716 1.000 37.79757 ?  152 LEU A HD12 1 
ATOM   2427 H  HD13 . LEU A 1 152 ? 10.13924 17.24199 36.74687 1.000 37.79757 ?  152 LEU A HD13 1 
ATOM   2428 H  HD21 . LEU A 1 152 ? 9.61075  14.33140 37.19548 1.000 38.61214 ?  152 LEU A HD21 1 
ATOM   2429 H  HD22 . LEU A 1 152 ? 10.30108 14.81379 35.84854 1.000 38.61214 ?  152 LEU A HD22 1 
ATOM   2430 H  HD23 . LEU A 1 152 ? 10.99770 13.70198 36.74414 1.000 38.61214 ?  152 LEU A HD23 1 
ATOM   2431 N  N    . ILE A 1 153 ? 15.65291 15.85406 36.37462 1.000 18.92600 ?  153 ILE A N    1 
ATOM   2432 C  CA   . ILE A 1 153 ? 16.73776 16.32383 35.50096 1.000 17.99612 ?  153 ILE A CA   1 
ATOM   2433 C  C    . ILE A 1 153 ? 17.92301 15.37226 35.47835 1.000 17.10284 ?  153 ILE A C    1 
ATOM   2434 O  O    . ILE A 1 153 ? 18.54047 15.17793 34.42890 1.000 19.32952 ?  153 ILE A O    1 
ATOM   2435 C  CB   . ILE A 1 153 ? 17.16035 17.76497 35.88154 1.000 18.01803 ?  153 ILE A CB   1 
ATOM   2436 C  CG1  . ILE A 1 153 ? 16.00458 18.77058 35.71066 1.000 19.13650 ?  153 ILE A CG1  1 
ATOM   2437 C  CG2  . ILE A 1 153 ? 18.40418 18.16408 35.06220 1.000 19.10419 ?  153 ILE A CG2  1 
ATOM   2438 C  CD1  . ILE A 1 153 ? 15.58506 18.98815 34.34302 1.000 20.80287 ?  153 ILE A CD1  1 
ATOM   2439 H  H    . ILE A 1 153 ? 15.71744 16.13447 37.18506 1.000 22.71750 ?  153 ILE A H    1 
ATOM   2440 H  HA   . ILE A 1 153 ? 16.38722 16.35220 34.59696 1.000 21.60164 ?  153 ILE A HA   1 
ATOM   2441 H  HB   . ILE A 1 153 ? 17.38783 17.78243 36.82433 1.000 21.62794 ?  153 ILE A HB   1 
ATOM   2442 H  HG12 . ILE A 1 153 ? 15.23576 18.44212 36.20252 1.000 22.97010 ?  153 ILE A HG12 1 
ATOM   2443 H  HG13 . ILE A 1 153 ? 16.28639 19.62689 36.06872 1.000 22.97010 ?  153 ILE A HG13 1 
ATOM   2444 H  HG21 . ILE A 1 153 ? 18.49441 19.12979 35.07523 1.000 22.93133 ?  153 ILE A HG21 1 
ATOM   2445 H  HG22 . ILE A 1 153 ? 19.18849 17.75321 35.45837 1.000 22.93133 ?  153 ILE A HG22 1 
ATOM   2446 H  HG23 . ILE A 1 153 ? 18.29388 17.85446 34.14958 1.000 22.93133 ?  153 ILE A HG23 1 
ATOM   2447 H  HD11 . ILE A 1 153 ? 14.86566 19.63874 34.33307 1.000 24.96975 ?  153 ILE A HD11 1 
ATOM   2448 H  HD12 . ILE A 1 153 ? 16.33865 19.32043 33.83059 1.000 24.96975 ?  153 ILE A HD12 1 
ATOM   2449 H  HD13 . ILE A 1 153 ? 15.27618 18.14772 33.96995 1.000 24.96975 ?  153 ILE A HD13 1 
ATOM   2450 N  N    . PHE A 1 154 ? 18.24148 14.77900 36.63415 1.000 16.68104 ?  154 PHE A N    1 
ATOM   2451 C  CA   . PHE A 1 154 ? 19.43274 13.97673 36.84031 1.000 16.68180 ?  154 PHE A CA   1 
ATOM   2452 C  C    . PHE A 1 154 ? 19.10771 12.55271 37.31756 1.000 16.69091 ?  154 PHE A C    1 
ATOM   2453 O  O    . PHE A 1 154 ? 19.67849 12.07432 38.30747 1.000 16.83633 ?  154 PHE A O    1 
ATOM   2454 C  CB   . PHE A 1 154 ? 20.37848 14.62769 37.83369 1.000 15.66864 ?  154 PHE A CB   1 
ATOM   2455 C  CG   . PHE A 1 154 ? 20.88550 15.95068 37.39147 1.000 15.22590 ?  154 PHE A CG   1 
ATOM   2456 C  CD1  . PHE A 1 154 ? 21.79029 16.08399 36.35953 1.000 16.77828 ?  154 PHE A CD1  1 
ATOM   2457 C  CD2  . PHE A 1 154 ? 20.53093 17.11531 38.07665 1.000 15.90576 ?  154 PHE A CD2  1 
ATOM   2458 C  CE1  . PHE A 1 154 ? 22.31176 17.33342 36.03111 1.000 17.29396 ?  154 PHE A CE1  1 
ATOM   2459 C  CE2  . PHE A 1 154 ? 21.01164 18.35044 37.72163 1.000 16.97736 ?  154 PHE A CE2  1 
ATOM   2460 C  CZ   . PHE A 1 154 ? 21.90905 18.47828 36.69822 1.000 16.82488 ?  154 PHE A CZ   1 
ATOM   2461 H  H    . PHE A 1 154 ? 17.75602 14.83345 37.34194 1.000 20.02355 ?  154 PHE A H    1 
ATOM   2462 H  HA   . PHE A 1 154 ? 19.86899 13.90791 35.97669 1.000 20.02446 ?  154 PHE A HA   1 
ATOM   2463 H  HB2  . PHE A 1 154 ? 19.91039 14.75489 38.67369 1.000 18.80867 ?  154 PHE A HB2  1 
ATOM   2464 H  HB3  . PHE A 1 154 ? 21.14318 14.04551 37.96487 1.000 18.80867 ?  154 PHE A HB3  1 
ATOM   2465 H  HD1  . PHE A 1 154 ? 22.05475 15.33325 35.87854 1.000 20.14024 ?  154 PHE A HD1  1 
ATOM   2466 H  HD2  . PHE A 1 154 ? 19.94854 17.05120 38.79888 1.000 19.09321 ?  154 PHE A HD2  1 
ATOM   2467 H  HE1  . PHE A 1 154 ? 22.94239 17.39994 35.35083 1.000 20.75906 ?  154 PHE A HE1  1 
ATOM   2468 H  HE2  . PHE A 1 154 ? 20.72474 19.10658 38.18080 1.000 20.37914 ?  154 PHE A HE2  1 
ATOM   2469 H  HZ   . PHE A 1 154 ? 22.24063 19.31277 36.45621 1.000 20.19616 ?  154 PHE A HZ   1 
ATOM   2470 N  N    . PRO A 1 155 ? 18.22466 11.82952 36.65365 1.000 16.95229 ?  155 PRO A N    1 
ATOM   2471 C  CA   . PRO A 1 155 ? 17.88864 10.48491 37.16419 1.000 17.81775 ?  155 PRO A CA   1 
ATOM   2472 C  C    . PRO A 1 155 ? 19.07613 9.51548  37.22415 1.000 17.46967 ?  155 PRO A C    1 
ATOM   2473 O  O    . PRO A 1 155 ? 19.12390 8.62827  38.10306 1.000 18.54481 ?  155 PRO A O    1 
ATOM   2474 C  CB   . PRO A 1 155 ? 16.81315 10.01071 36.19875 1.000 19.11007 ?  155 PRO A CB   1 
ATOM   2475 C  CG   . PRO A 1 155 ? 17.05223 10.79193 34.92735 1.000 18.70803 ?  155 PRO A CG   1 
ATOM   2476 C  CD   . PRO A 1 155 ? 17.54895 12.14959 35.40556 1.000 17.80445 ?  155 PRO A CD   1 
ATOM   2477 H  HA   . PRO A 1 155 ? 17.51208 10.56192 38.05479 1.000 21.38761 ?  155 PRO A HA   1 
ATOM   2478 H  HB2  . PRO A 1 155 ? 16.90691 9.05790  36.04299 1.000 22.93839 ?  155 PRO A HB2  1 
ATOM   2479 H  HB3  . PRO A 1 155 ? 15.93502 10.20242 36.56350 1.000 22.93839 ?  155 PRO A HB3  1 
ATOM   2480 H  HG2  . PRO A 1 155 ? 17.72137 10.34718 34.38390 1.000 22.45594 ?  155 PRO A HG2  1 
ATOM   2481 H  HG3  . PRO A 1 155 ? 16.22450 10.87890 34.42915 1.000 22.45594 ?  155 PRO A HG3  1 
ATOM   2482 H  HD2  . PRO A 1 155 ? 18.16723 12.53702 34.76640 1.000 21.37164 ?  155 PRO A HD2  1 
ATOM   2483 H  HD3  . PRO A 1 155 ? 16.80715 12.75553 35.55877 1.000 21.37164 ?  155 PRO A HD3  1 
ATOM   2484 N  N    . GLU A 1 156 ? 20.05115 9.68886  36.34297 1.000 16.68332 ?  156 GLU A N    1 
ATOM   2485 C  CA   . GLU A 1 156 ? 21.25736 8.86093  36.39195 1.000 16.83616 ?  156 GLU A CA   1 
ATOM   2486 C  C    . GLU A 1 156 ? 22.08010 9.16933  37.61803 1.000 16.56369 ?  156 GLU A C    1 
ATOM   2487 O  O    . GLU A 1 156 ? 22.73868 8.26491  38.16870 1.000 17.62274 ?  156 GLU A O    1 
ATOM   2488 C  CB   . GLU A 1 156 ? 22.05948 9.02291  35.10396 1.000 17.85900 ?  156 GLU A CB   1 
ATOM   2489 C  CG   . GLU A 1 156 ? 22.94967 10.24522 34.99422 1.000 18.97846 ?  156 GLU A CG   1 
ATOM   2490 C  CD   . GLU A 1 156 ? 22.28491 11.58628 34.71052 1.000 20.64488 ?  156 GLU A CD   1 
ATOM   2491 O  OE1  . GLU A 1 156 ? 21.05098 11.71721 34.68115 1.000 21.58094 ?  156 GLU A OE1  1 
ATOM   2492 O  OE2  . GLU A 1 156 ? 23.05035 12.57024 34.56336 1.000 22.42328 -1 156 GLU A OE2  1 
ATOM   2493 H  H    . GLU A 1 156 ? 20.04437 10.27182 35.71074 1.000 20.02628 ?  156 GLU A H    1 
ATOM   2494 H  HA   . GLU A 1 156 ? 21.00923 7.92467  36.44437 1.000 20.20969 ?  156 GLU A HA   1 
ATOM   2495 H  HB2  . GLU A 1 156 ? 22.63365 8.24677  35.00992 1.000 21.43711 ?  156 GLU A HB2  1 
ATOM   2496 H  HB3  . GLU A 1 156 ? 21.43274 9.06345  34.36473 1.000 21.43711 ?  156 GLU A HB3  1 
ATOM   2497 H  HG2  . GLU A 1 156 ? 23.42438 10.34250 35.83451 1.000 22.78045 ?  156 GLU A HG2  1 
ATOM   2498 H  HG3  . GLU A 1 156 ? 23.57970 10.08923 34.27338 1.000 22.78045 ?  156 GLU A HG3  1 
ATOM   2499 N  N    . VAL A 1 157 ? 22.03097 10.43153 38.10328 1.000 15.73735 ?  157 VAL A N    1 
ATOM   2500 C  CA   . VAL A 1 157 ? 22.78072 10.75240 39.31132 1.000 15.50594 ?  157 VAL A CA   1 
ATOM   2501 C  C    . VAL A 1 157 ? 22.03954 10.24629 40.54874 1.000 16.03636 ?  157 VAL A C    1 
ATOM   2502 O  O    . VAL A 1 157 ? 22.66633 9.83477  41.52731 1.000 16.74012 ?  157 VAL A O    1 
ATOM   2503 C  CB   . VAL A 1 157 ? 23.13733 12.24902 39.40957 1.000 15.44145 ?  157 VAL A CB   1 
ATOM   2504 C  CG1  . VAL A 1 157 ? 24.00107 12.51452 40.63809 1.000 16.39686 ?  157 VAL A CG1  1 
ATOM   2505 C  CG2  . VAL A 1 157 ? 23.75519 12.75979 38.11659 1.000 16.67816 ?  157 VAL A CG2  1 
ATOM   2506 H  H    . VAL A 1 157 ? 21.58746 11.08274 37.75858 1.000 18.89112 ?  157 VAL A H    1 
ATOM   2507 H  HA   . VAL A 1 157 ? 23.63254 10.29145 39.25814 1.000 18.61343 ?  157 VAL A HA   1 
ATOM   2508 H  HB   . VAL A 1 157 ? 22.32367 12.76341 39.52896 1.000 18.53604 ?  157 VAL A HB   1 
ATOM   2509 H  HG11 . VAL A 1 157 ? 24.34271 13.42129 40.59395 1.000 19.68253 ?  157 VAL A HG11 1 
ATOM   2510 H  HG12 . VAL A 1 157 ? 23.45929 12.40360 41.43500 1.000 19.68253 ?  157 VAL A HG12 1 
ATOM   2511 H  HG13 . VAL A 1 157 ? 24.73778 11.88362 40.64851 1.000 19.68253 ?  157 VAL A HG13 1 
ATOM   2512 H  HG21 . VAL A 1 157 ? 24.02974 13.68184 38.24045 1.000 20.02009 ?  157 VAL A HG21 1 
ATOM   2513 H  HG22 . VAL A 1 157 ? 24.52498 12.21216 37.89653 1.000 20.02009 ?  157 VAL A HG22 1 
ATOM   2514 H  HG23 . VAL A 1 157 ? 23.09562 12.70345 37.40758 1.000 20.02009 ?  157 VAL A HG23 1 
ATOM   2515 N  N    . VAL A 1 158 ? 20.70344 10.25841 40.52767 1.000 16.06252 ?  158 VAL A N    1 
ATOM   2516 C  CA   . VAL A 1 158 ? 19.94361 9.61662  41.59481 1.000 15.93477 ?  158 VAL A CA   1 
ATOM   2517 C  C    . VAL A 1 158 ? 20.40935 8.18209  41.77379 1.000 16.80085 ?  158 VAL A C    1 
ATOM   2518 O  O    . VAL A 1 158 ? 20.60208 7.72902  42.89338 1.000 16.31329 ?  158 VAL A O    1 
ATOM   2519 C  CB   . VAL A 1 158 ? 18.44099 9.69816  41.35883 1.000 16.34234 ?  158 VAL A CB   1 
ATOM   2520 C  CG1  . VAL A 1 158 ? 17.60682 8.85249  42.32420 1.000 16.97194 ?  158 VAL A CG1  1 
ATOM   2521 C  CG2  . VAL A 1 158 ? 17.98196 11.16176 41.35685 1.000 18.83210 ?  158 VAL A CG2  1 
ATOM   2522 H  H    . VAL A 1 158 ? 20.22368 10.62598 39.91586 1.000 19.28132 ?  158 VAL A H    1 
ATOM   2523 H  HA   . VAL A 1 158 ? 20.11946 10.10339 42.41521 1.000 19.12803 ?  158 VAL A HA   1 
ATOM   2524 H  HB   . VAL A 1 158 ? 18.27521 9.31118  40.48495 1.000 19.61711 ?  158 VAL A HB   1 
ATOM   2525 H  HG11 . VAL A 1 158 ? 16.67398 9.10465  42.23977 1.000 20.37263 ?  158 VAL A HG11 1 
ATOM   2526 H  HG12 . VAL A 1 158 ? 17.71776 7.91534  42.09984 1.000 20.37263 ?  158 VAL A HG12 1 
ATOM   2527 H  HG13 . VAL A 1 158 ? 17.91241 9.01406  43.23052 1.000 20.37263 ?  158 VAL A HG13 1 
ATOM   2528 H  HG21 . VAL A 1 158 ? 17.01713 11.19001 41.26087 1.000 22.60483 ?  158 VAL A HG21 1 
ATOM   2529 H  HG22 . VAL A 1 158 ? 18.24334 11.57584 42.19418 1.000 22.60483 ?  158 VAL A HG22 1 
ATOM   2530 H  HG23 . VAL A 1 158 ? 18.40190 11.62343 40.61428 1.000 22.60483 ?  158 VAL A HG23 1 
ATOM   2531 N  N    . GLN A 1 159 ? 20.59115 7.42283  40.69080 1.000 16.70342 ?  159 GLN A N    1 
ATOM   2532 C  CA   . GLN A 1 159 ? 21.01224 6.02436  40.81300 1.000 17.01172 ?  159 GLN A CA   1 
ATOM   2533 C  C    . GLN A 1 159 ? 22.40242 5.93256  41.39809 1.000 16.53819 ?  159 GLN A C    1 
ATOM   2534 O  O    . GLN A 1 159 ? 22.64958 5.08017  42.25573 1.000 17.09060 ?  159 GLN A O    1 
ATOM   2535 C  CB   . GLN A 1 159 ? 20.90728 5.35160  39.43977 1.000 19.43555 ?  159 GLN A CB   1 
ATOM   2536 C  CG   . GLN A 1 159 ? 19.46633 5.22313  38.94603 1.000 22.95828 ?  159 GLN A CG   1 
ATOM   2537 C  CD   . GLN A 1 159 ? 19.30292 4.45867  37.62742 1.000 27.27803 ?  159 GLN A CD   1 
ATOM   2538 O  OE1  . GLN A 1 159 ? 20.26361 3.97153  37.02023 1.000 28.85080 ?  159 GLN A OE1  1 
ATOM   2539 N  NE2  . GLN A 1 159 ? 18.03927 4.37722  37.15356 1.000 28.80666 ?  159 GLN A NE2  1 
ATOM   2540 H  H    . GLN A 1 159 ? 20.47887 7.68930  39.88087 1.000 20.05041 ?  159 GLN A H    1 
ATOM   2541 H  HA   . GLN A 1 159 ? 20.42478 5.54238  41.41589 1.000 20.42036 ?  159 GLN A HA   1 
ATOM   2542 H  HB2  . GLN A 1 159 ? 21.39965 5.87981  38.79210 1.000 23.32896 ?  159 GLN A HB2  1 
ATOM   2543 H  HB3  . GLN A 1 159 ? 21.28489 4.45992  39.49649 1.000 23.32896 ?  159 GLN A HB3  1 
ATOM   2544 H  HG2  . GLN A 1 159 ? 18.95039 4.75396  39.62026 1.000 27.55624 ?  159 GLN A HG2  1 
ATOM   2545 H  HG3  . GLN A 1 159 ? 19.10588 6.11374  38.81265 1.000 27.55624 ?  159 GLN A HG3  1 
ATOM   2546 H  HE21 . GLN A 1 159 ? 17.39274 4.74153  37.58816 1.000 34.57429 ?  159 GLN A HE21 1 
ATOM   2547 H  HE22 . GLN A 1 159 ? 17.88202 3.96111  36.41754 1.000 34.57429 ?  159 GLN A HE22 1 
ATOM   2548 N  N    . GLU A 1 160 ? 23.32794 6.80716  41.00645 1.000 16.67574 ?  160 GLU A N    1 
ATOM   2549 C  CA   . GLU A 1 160 ? 24.63295 6.81704  41.61323 1.000 17.70832 ?  160 GLU A CA   1 
ATOM   2550 C  C    . GLU A 1 160 ? 24.51350 7.09736  43.08117 1.000 16.22972 ?  160 GLU A C    1 
ATOM   2551 O  O    . GLU A 1 160 ? 25.21401 6.48008  43.89587 1.000 17.39859 ?  160 GLU A O    1 
ATOM   2552 C  CB   . GLU A 1 160 ? 25.50988 7.90500  40.97130 1.000 20.33220 ?  160 GLU A CB   1 
ATOM   2553 C  CG   . GLU A 1 160 ? 25.94395 7.59372  39.59040 1.000 22.69541 ?  160 GLU A CG   1 
ATOM   2554 C  CD   . GLU A 1 160 ? 26.83856 8.64831  39.00416 1.000 24.81445 ?  160 GLU A CD   1 
ATOM   2555 O  OE1  . GLU A 1 160 ? 26.98547 9.76028  39.59477 1.000 27.17743 ?  160 GLU A OE1  1 
ATOM   2556 O  OE2  . GLU A 1 160 ? 27.35403 8.35782  37.92324 1.000 24.59644 -1 160 GLU A OE2  1 
ATOM   2557 H  H    . GLU A 1 160 ? 23.21612 7.39918  40.39276 1.000 20.01719 ?  160 GLU A H    1 
ATOM   2558 H  HA   . GLU A 1 160 ? 25.05239 5.95408  41.47086 1.000 21.25628 ?  160 GLU A HA   1 
ATOM   2559 H  HB2  . GLU A 1 160 ? 25.00577 8.73321  40.94226 1.000 24.40495 ?  160 GLU A HB2  1 
ATOM   2560 H  HB3  . GLU A 1 160 ? 26.30693 8.02054  41.51191 1.000 24.40495 ?  160 GLU A HB3  1 
ATOM   2561 H  HG2  . GLU A 1 160 ? 26.43287 6.75596  39.59508 1.000 27.24079 ?  160 GLU A HG2  1 
ATOM   2562 H  HG3  . GLU A 1 160 ? 25.16057 7.51750  39.02348 1.000 27.24079 ?  160 GLU A HG3  1 
ATOM   2563 N  N    . ASN A 1 161 ? 23.68396 8.06765  43.44741 1.000 15.37883 ?  161 ASN A N    1 
ATOM   2564 C  CA   . ASN A 1 161 ? 23.49340 8.42554  44.85556 1.000 14.67176 ?  161 ASN A CA   1 
ATOM   2565 C  C    . ASN A 1 161 ? 23.00353 7.25360  45.66268 1.000 14.91552 ?  161 ASN A C    1 
ATOM   2566 O  O    . ASN A 1 161 ? 23.36038 7.13550  46.82831 1.000 16.16327 ?  161 ASN A O    1 
ATOM   2567 C  CB   . ASN A 1 161 ? 22.48082 9.58485  44.96699 1.000 15.23893 ?  161 ASN A CB   1 
ATOM   2568 C  CG   . ASN A 1 161 ? 23.03257 10.91562 44.54851 1.000 15.78841 ?  161 ASN A CG   1 
ATOM   2569 O  OD1  . ASN A 1 161 ? 24.21564 11.08844 44.22553 1.000 16.23267 ?  161 ASN A OD1  1 
ATOM   2570 N  ND2  . ASN A 1 161 ? 22.15440 11.92166 44.60004 1.000 15.98323 ?  161 ASN A ND2  1 
ATOM   2571 H  H    . ASN A 1 161 ? 23.21528 8.53913  42.90183 1.000 18.46090 ?  161 ASN A H    1 
ATOM   2572 H  HA   . ASN A 1 161 ? 24.34688 8.71234  45.21642 1.000 17.61241 ?  161 ASN A HA   1 
ATOM   2573 H  HB2  . ASN A 1 161 ? 21.71926 9.38928  44.39895 1.000 18.29302 ?  161 ASN A HB2  1 
ATOM   2574 H  HB3  . ASN A 1 161 ? 22.19478 9.66123  45.89071 1.000 18.29302 ?  161 ASN A HB3  1 
ATOM   2575 H  HD21 . ASN A 1 161 ? 22.39644 12.71565 44.37512 1.000 19.18618 ?  161 ASN A HD21 1 
ATOM   2576 H  HD22 . ASN A 1 161 ? 21.34724 11.77508 44.85813 1.000 19.18618 ?  161 ASN A HD22 1 
ATOM   2577 N  N    . VAL A 1 162 ? 22.11531 6.45403  45.09270 1.000 14.48613 ?  162 VAL A N    1 
ATOM   2578 C  CA   . VAL A 1 162 ? 21.59362 5.30937  45.81191 1.000 14.04388 ?  162 VAL A CA   1 
ATOM   2579 C  C    . VAL A 1 162 ? 22.75205 4.37057  46.20674 1.000 14.57930 ?  162 VAL A C    1 
ATOM   2580 O  O    . VAL A 1 162 ? 22.82142 3.86605  47.33150 1.000 15.78432 ?  162 VAL A O    1 
ATOM   2581 C  CB   . VAL A 1 162 ? 20.49821 4.59431  45.00232 1.000 15.07468 ?  162 VAL A CB   1 
ATOM   2582 C  CG1  . VAL A 1 162 ? 20.20963 3.15677  45.58845 1.000 15.48379 ?  162 VAL A CG1  1 
ATOM   2583 C  CG2  . VAL A 1 162 ? 19.23409 5.43852  44.94808 1.000 16.28524 ?  162 VAL A CG2  1 
ATOM   2584 H  H    . VAL A 1 162 ? 21.80213 6.55246  44.29782 1.000 17.38966 ?  162 VAL A H    1 
ATOM   2585 H  HA   . VAL A 1 162 ? 21.17102 5.61872  46.62837 1.000 16.85895 ?  162 VAL A HA   1 
ATOM   2586 H  HB   . VAL A 1 162 ? 20.81065 4.47582  44.09169 1.000 18.09592 ?  162 VAL A HB   1 
ATOM   2587 H  HG11 . VAL A 1 162 ? 19.36489 2.83573  45.23596 1.000 18.58686 ?  162 VAL A HG11 1 
ATOM   2588 H  HG12 . VAL A 1 162 ? 20.92654 2.55868  45.32534 1.000 18.58686 ?  162 VAL A HG12 1 
ATOM   2589 H  HG13 . VAL A 1 162 ? 20.16431 3.21337  46.55574 1.000 18.58686 ?  162 VAL A HG13 1 
ATOM   2590 H  HG21 . VAL A 1 162 ? 18.57149 4.98061  44.40756 1.000 19.54860 ?  162 VAL A HG21 1 
ATOM   2591 H  HG22 . VAL A 1 162 ? 18.89776 5.56181  45.84952 1.000 19.54860 ?  162 VAL A HG22 1 
ATOM   2592 H  HG23 . VAL A 1 162 ? 19.44566 6.29896  44.55340 1.000 19.54860 ?  162 VAL A HG23 1 
ATOM   2593 N  N    . GLU A 1 163 ? 23.68177 4.10623  45.28587 1.000 15.27908 ?  163 GLU A N    1 
ATOM   2594 C  CA   . GLU A 1 163 ? 24.84647 3.28812  45.58836 1.000 15.47328 ?  163 GLU A CA   1 
ATOM   2595 C  C    . GLU A 1 163 ? 25.71205 3.96488  46.63764 1.000 15.76135 ?  163 GLU A C    1 
ATOM   2596 O  O    . GLU A 1 163 ? 26.25878 3.31897  47.54096 1.000 16.27616 ?  163 GLU A O    1 
ATOM   2597 C  CB   . GLU A 1 163 ? 25.61776 2.99305  44.29786 1.000 15.46217 ?  163 GLU A CB   1 
ATOM   2598 C  CG   . GLU A 1 163 ? 26.72984 1.97455  44.55885 1.000 16.10894 ?  163 GLU A CG   1 
ATOM   2599 C  CD   . GLU A 1 163 ? 26.28472 0.53300  44.79265 1.000 15.59169 ?  163 GLU A CD   1 
ATOM   2600 O  OE1  . GLU A 1 163 ? 25.30972 0.13944  44.06447 1.000 15.90121 ?  163 GLU A OE1  1 
ATOM   2601 O  OE2  . GLU A 1 163 ? 26.94098 -0.17582 45.59626 1.000 16.39135 -1 163 GLU A OE2  1 
ATOM   2602 H  H    . GLU A 1 163 ? 23.65842 4.39178  44.47499 1.000 18.34120 ?  163 GLU A H    1 
ATOM   2603 H  HA   . GLU A 1 163 ? 24.57116 2.43215  45.95225 1.000 18.57423 ?  163 GLU A HA   1 
ATOM   2604 H  HB2  . GLU A 1 163 ? 25.01198 2.62719  43.63447 1.000 18.56091 ?  163 GLU A HB2  1 
ATOM   2605 H  HB3  . GLU A 1 163 ? 26.01880 3.81133  43.96546 1.000 18.56091 ?  163 GLU A HB3  1 
ATOM   2606 H  HG2  . GLU A 1 163 ? 27.32133 1.96889  43.79009 1.000 19.33704 ?  163 GLU A HG2  1 
ATOM   2607 H  HG3  . GLU A 1 163 ? 27.21658 2.25422  45.34990 1.000 19.33704 ?  163 GLU A HG3  1 
ATOM   2608 N  N    . THR A 1 164 ? 25.89544 5.28765  46.52716 1.000 16.00437 ?  164 THR A N    1 
ATOM   2609 C  CA   . THR A 1 164 ? 26.73499 5.97574  47.51166 1.000 16.78533 ?  164 THR A CA   1 
ATOM   2610 C  C    . THR A 1 164 ? 26.14984 5.85796  48.91673 1.000 17.69267 ?  164 THR A C    1 
ATOM   2611 O  O    . THR A 1 164 ? 26.85136 5.55007  49.89064 1.000 18.57367 ?  164 THR A O    1 
ATOM   2612 C  CB   . THR A 1 164 ? 26.81152 7.45736  47.14544 1.000 18.58117 ?  164 THR A CB   1 
ATOM   2613 O  OG1  . THR A 1 164 ? 27.52580 7.55987  45.93610 1.000 20.16364 ?  164 THR A OG1  1 
ATOM   2614 C  CG2  . THR A 1 164 ? 27.54146 8.28173  48.21995 1.000 19.37333 ?  164 THR A CG2  1 
ATOM   2615 H  H    . THR A 1 164 ? 25.55788 5.78894  45.91531 1.000 19.21155 ?  164 THR A H    1 
ATOM   2616 H  HA   . THR A 1 164 ? 27.61978 5.57832  47.50145 1.000 20.14870 ?  164 THR A HA   1 
ATOM   2617 H  HB   . THR A 1 164 ? 25.91518 7.81963  47.06650 1.000 22.30371 ?  164 THR A HB   1 
ATOM   2618 H  HG1  . THR A 1 164 ? 27.12025 7.14734  45.32704 1.000 24.20267 ?  164 THR A HG1  1 
ATOM   2619 H  HG21 . THR A 1 164 ? 27.81236 9.13818  47.85387 1.000 23.25429 ?  164 THR A HG21 1 
ATOM   2620 H  HG22 . THR A 1 164 ? 26.95422 8.43443  48.97675 1.000 23.25429 ?  164 THR A HG22 1 
ATOM   2621 H  HG23 . THR A 1 164 ? 28.33001 7.80589  48.52436 1.000 23.25429 ?  164 THR A HG23 1 
ATOM   2622 N  N    . LEU A 1 165 ? 24.83456 6.02740  49.03046 1.000 16.86131 ?  165 LEU A N    1 
ATOM   2623 C  CA   . LEU A 1 165 ? 24.21023 5.91090  50.32390 1.000 17.58704 ?  165 LEU A CA   1 
ATOM   2624 C  C    . LEU A 1 165 ? 24.16599 4.49226  50.81705 1.000 16.98500 ?  165 LEU A C    1 
ATOM   2625 O  O    . LEU A 1 165 ? 24.26876 4.26089  52.03723 1.000 18.40973 ?  165 LEU A O    1 
ATOM   2626 C  CB   . LEU A 1 165 ? 22.80537 6.45446  50.23921 1.000 18.87666 ?  165 LEU A CB   1 
ATOM   2627 C  CG   . LEU A 1 165 ? 22.75053 8.00612  49.96972 1.000 21.05942 ?  165 LEU A CG   1 
ATOM   2628 C  CD1  . LEU A 1 165 ? 21.31248 8.36505  49.67054 1.000 22.69043 ?  165 LEU A CD1  1 
ATOM   2629 C  CD2  . LEU A 1 165 ? 23.34874 8.83452  51.07650 1.000 23.15954 ?  165 LEU A CD2  1 
ATOM   2630 H  H    . LEU A 1 165 ? 24.29916 6.20679  48.38180 1.000 20.23988 ?  165 LEU A H    1 
ATOM   2631 H  HA   . LEU A 1 165 ? 24.72529 6.42779  50.96299 1.000 21.11075 ?  165 LEU A HA   1 
ATOM   2632 H  HB2  . LEU A 1 165 ? 22.34099 6.00895  49.51342 1.000 22.65829 ?  165 LEU A HB2  1 
ATOM   2633 H  HB3  . LEU A 1 165 ? 22.35196 6.28124  51.07904 1.000 22.65829 ?  165 LEU A HB3  1 
ATOM   2634 H  HG   . LEU A 1 165 ? 23.30769 8.22883  49.20757 1.000 25.27760 ?  165 LEU A HG   1 
ATOM   2635 H  HD11 . LEU A 1 165 ? 21.25346 9.31846  49.50196 1.000 27.23482 ?  165 LEU A HD11 1 
ATOM   2636 H  HD12 . LEU A 1 165 ? 21.02019 7.87206  48.88796 1.000 27.23482 ?  165 LEU A HD12 1 
ATOM   2637 H  HD13 . LEU A 1 165 ? 20.76275 8.12951  50.43423 1.000 27.23482 ?  165 LEU A HD13 1 
ATOM   2638 H  HD21 . LEU A 1 165 ? 23.19392 9.77323  50.88739 1.000 27.79775 ?  165 LEU A HD21 1 
ATOM   2639 H  HD22 . LEU A 1 165 ? 22.92689 8.59221  51.91569 1.000 27.79775 ?  165 LEU A HD22 1 
ATOM   2640 H  HD23 . LEU A 1 165 ? 24.30164 8.65915  51.12253 1.000 27.79775 ?  165 LEU A HD23 1 
ATOM   2641 N  N    . GLU A 1 166 ? 24.05343 3.52554  49.91559 1.000 16.96173 ?  166 GLU A N    1 
ATOM   2642 C  CA   . GLU A 1 166 ? 24.12739 2.11622  50.28809 1.000 16.54344 ?  166 GLU A CA   1 
ATOM   2643 C  C    . GLU A 1 166 ? 25.45142 1.80661  50.91957 1.000 18.09719 ?  166 GLU A C    1 
ATOM   2644 O  O    . GLU A 1 166 ? 25.50531 1.16082  51.96532 1.000 18.60389 ?  166 GLU A O    1 
ATOM   2645 C  CB   . GLU A 1 166 ? 23.94442 1.30350  49.01093 1.000 16.54320 ?  166 GLU A CB   1 
ATOM   2646 C  CG   . GLU A 1 166 ? 24.35051 -0.15276 49.07489 1.000 16.27830 ?  166 GLU A CG   1 
ATOM   2647 C  CD   . GLU A 1 166 ? 24.41479 -0.80902 47.71885 1.000 14.60614 ?  166 GLU A CD   1 
ATOM   2648 O  OE1  . GLU A 1 166 ? 23.85548 -0.18000 46.80257 1.000 15.57210 ?  166 GLU A OE1  1 
ATOM   2649 O  OE2  . GLU A 1 166 ? 24.96029 -1.91903 47.58901 1.000 14.73506 -1 166 GLU A OE2  1 
ATOM   2650 H  H    . GLU A 1 166 ? 23.93269 3.65697  49.07431 1.000 20.36038 ?  166 GLU A H    1 
ATOM   2651 H  HA   . GLU A 1 166 ? 23.43520 1.89009  50.92890 1.000 19.85843 ?  166 GLU A HA   1 
ATOM   2652 H  HB2  . GLU A 1 166 ? 23.00484 1.32667  48.77105 1.000 19.85815 ?  166 GLU A HB2  1 
ATOM   2653 H  HB3  . GLU A 1 166 ? 24.47550 1.71662  48.31222 1.000 19.85815 ?  166 GLU A HB3  1 
ATOM   2654 H  HG2  . GLU A 1 166 ? 25.22975 -0.21691 49.47952 1.000 19.54026 ?  166 GLU A HG2  1 
ATOM   2655 H  HG3  . GLU A 1 166 ? 23.70272 -0.63698 49.61043 1.000 19.54026 ?  166 GLU A HG3  1 
ATOM   2656 N  N    . LYS A 1 167 ? 26.54617 2.27900  50.32008 1.000 20.35314 ?  167 LYS A N    1 
ATOM   2657 C  CA   . LYS A 1 167 ? 27.88197 2.00284  50.83541 1.000 23.27240 ?  167 LYS A CA   1 
ATOM   2658 C  C    . LYS A 1 167 ? 28.09141 2.68871  52.16857 1.000 24.97227 ?  167 LYS A C    1 
ATOM   2659 O  O    . LYS A 1 167 ? 28.69669 2.13697  53.08173 1.000 25.67763 ?  167 LYS A O    1 
ATOM   2660 C  CB   . LYS A 1 167 ? 28.93816 2.38182  49.80909 1.000 25.37001 ?  167 LYS A CB   1 
ATOM   2661 C  CG   . LYS A 1 167 ? 29.00141 1.45267  48.60966 1.000 28.17906 ?  167 LYS A CG   1 
ATOM   2662 C  CD   . LYS A 1 167 ? 30.20511 1.75995  47.69275 1.000 31.15047 ?  167 LYS A CD   1 
ATOM   2663 C  CE   . LYS A 1 167 ? 29.99900 1.38869  46.22465 1.000 32.55569 ?  167 LYS A CE   1 
ATOM   2664 N  NZ   . LYS A 1 167 ? 29.87094 -0.02719 46.18061 1.000 32.30381 ?  167 LYS A NZ   1 
ATOM   2665 H  H    . LYS A 1 167 ? 26.54094 2.76421  49.61005 1.000 24.43007 ?  167 LYS A H    1 
ATOM   2666 H  HA   . LYS A 1 167 ? 27.98432 1.04980  50.98421 1.000 27.93318 ?  167 LYS A HA   1 
ATOM   2667 H  HB2  . LYS A 1 167 ? 28.74540 3.27389  49.48054 1.000 30.45031 ?  167 LYS A HB2  1 
ATOM   2668 H  HB3  . LYS A 1 167 ? 29.80762 2.36725  50.23889 1.000 30.45031 ?  167 LYS A HB3  1 
ATOM   2669 H  HG2  . LYS A 1 167 ? 29.08496 0.53752  48.92017 1.000 33.82117 ?  167 LYS A HG2  1 
ATOM   2670 H  HG3  . LYS A 1 167 ? 28.19074 1.55280  48.08651 1.000 33.82117 ?  167 LYS A HG3  1 
ATOM   2671 H  HD2  . LYS A 1 167 ? 30.38698 2.71202  47.72985 1.000 37.38686 ?  167 LYS A HD2  1 
ATOM   2672 H  HD3  . LYS A 1 167 ? 30.97346 1.26265  48.01403 1.000 37.38686 ?  167 LYS A HD3  1 
ATOM   2673 H  HE2  . LYS A 1 167 ? 29.19077 1.79981  45.88019 1.000 39.07313 ?  167 LYS A HE2  1 
ATOM   2674 H  HE3  . LYS A 1 167 ? 30.76307 1.66339  45.69395 1.000 39.07313 ?  167 LYS A HE3  1 
ATOM   2675 H  HZ1  . LYS A 1 167 ? 29.15880 -0.28314 46.64906 1.000 38.77087 ?  167 LYS A HZ1  1 
ATOM   2676 H  HZ2  . LYS A 1 167 ? 29.77519 -0.29812 45.33827 1.000 38.77087 ?  167 LYS A HZ2  1 
ATOM   2677 H  HZ3  . LYS A 1 167 ? 30.59661 -0.40936 46.52622 1.000 38.77087 ?  167 LYS A HZ3  1 
ATOM   2678 N  N    . ARG A 1 168 ? 27.58358 3.90211  52.32843 1.000 26.40254 ?  168 ARG A N    1 
ATOM   2679 C  CA   . ARG A 1 168 ? 27.74349 4.58110  53.61981 1.000 29.70752 ?  168 ARG A CA   1 
ATOM   2680 C  C    . ARG A 1 168 ? 27.01064 3.85625  54.71840 1.000 31.63487 ?  168 ARG A C    1 
ATOM   2681 O  O    . ARG A 1 168 ? 27.47065 3.80516  55.87512 1.000 31.89958 ?  168 ARG A O    1 
ATOM   2682 C  CB   . ARG A 1 168 ? 27.13704 5.99339  53.59636 1.000 32.50161 ?  168 ARG A CB   1 
ATOM   2683 C  CG   . ARG A 1 168 ? 27.81424 6.96953  52.78144 1.000 35.47677 ?  168 ARG A CG   1 
ATOM   2684 C  CD   . ARG A 1 168 ? 27.25913 8.36509  53.16594 1.000 36.37416 ?  168 ARG A CD   1 
ATOM   2685 N  NE   . ARG A 1 168 ? 27.91054 9.30831  52.31535 1.000 36.87292 ?  168 ARG A NE   1 
ATOM   2686 C  CZ   . ARG A 1 168 ? 27.54725 10.57507 52.25182 1.000 37.11908 ?  168 ARG A CZ   1 
ATOM   2687 N  NH1  . ARG A 1 168 ? 26.58717 11.04474 53.03305 1.000 37.14865 ?  168 ARG A NH1  1 
ATOM   2688 N  NH2  . ARG A 1 168 ? 28.14735 11.36635 51.38319 1.000 38.69729 ?  168 ARG A NH2  1 
ATOM   2689 H  H    . ARG A 1 168 ? 27.15488 4.34609  51.72951 1.000 31.68935 ?  168 ARG A H    1 
ATOM   2690 H  HA   . ARG A 1 168 ? 28.69897 4.61936  53.78257 1.000 35.65533 ?  168 ARG A HA   1 
ATOM   2691 H  HB2  . ARG A 1 168 ? 26.22858 5.92561  53.26318 1.000 39.00824 ?  168 ARG A HB2  1 
ATOM   2692 H  HB3  . ARG A 1 168 ? 27.13281 6.33451  54.50439 1.000 39.00824 ?  168 ARG A HB3  1 
ATOM   2693 H  HG2  . ARG A 1 168 ? 28.76892 6.94544  52.95147 1.000 42.57843 ?  168 ARG A HG2  1 
ATOM   2694 H  HG3  . ARG A 1 168 ? 27.64026 6.80219  51.84195 1.000 42.57843 ?  168 ARG A HG3  1 
ATOM   2695 H  HD2  . ARG A 1 168 ? 26.30091 8.40194  53.01980 1.000 43.65529 ?  168 ARG A HD2  1 
ATOM   2696 H  HD3  . ARG A 1 168 ? 27.46142 8.56796  54.09267 1.000 43.65529 ?  168 ARG A HD3  1 
ATOM   2697 H  HE   . ARG A 1 168 ? 28.56481 9.04064  51.82557 1.000 44.25380 ?  168 ARG A HE   1 
ATOM   2698 H  HH11 . ARG A 1 168 ? 26.19221 10.52231 53.59043 1.000 44.58468 ?  168 ARG A HH11 1 
ATOM   2699 H  HH12 . ARG A 1 168 ? 26.35845 11.87226 52.98315 1.000 44.58468 ?  168 ARG A HH12 1 
ATOM   2700 H  HH21 . ARG A 1 168 ? 28.76353 11.05386 50.87107 1.000 46.44305 ?  168 ARG A HH21 1 
ATOM   2701 H  HH22 . ARG A 1 168 ? 27.92232 12.19463 51.32911 1.000 46.44305 ?  168 ARG A HH22 1 
ATOM   2702 N  N    . LYS A 1 169 ? 25.82316 3.37321  54.41536 1.000 33.10126 ?  169 LYS A N    1 
ATOM   2703 C  CA   . LYS A 1 169 ? 25.06702 2.69061  55.45177 1.000 36.01472 ?  169 LYS A CA   1 
ATOM   2704 C  C    . LYS A 1 169 ? 25.68018 1.33908  55.74144 1.000 36.52249 ?  169 LYS A C    1 
ATOM   2705 O  O    . LYS A 1 169 ? 25.99953 1.01571  56.88784 1.000 36.46422 ?  169 LYS A O    1 
ATOM   2706 C  CB   . LYS A 1 169 ? 23.60888 2.55695  55.01545 1.000 39.00517 ?  169 LYS A CB   1 
ATOM   2707 C  CG   . LYS A 1 169 ? 22.65108 2.08979  56.10936 1.000 42.03955 ?  169 LYS A CG   1 
ATOM   2708 C  CD   . LYS A 1 169 ? 22.95786 2.64049  57.53616 1.000 45.13955 ?  169 LYS A CD   1 
ATOM   2709 C  CE   . LYS A 1 169 ? 22.05349 3.84123  57.92878 1.000 47.60472 ?  169 LYS A CE   1 
ATOM   2710 N  NZ   . LYS A 1 169 ? 22.37731 4.41910  59.29102 1.000 48.95494 ?  169 LYS A NZ   1 
ATOM   2711 H  H    . LYS A 1 169 ? 25.44236 3.42340  53.64589 1.000 39.72781 ?  169 LYS A H    1 
ATOM   2712 H  HA   . LYS A 1 169 ? 25.08313 3.21011  56.27077 1.000 43.22397 ?  169 LYS A HA   1 
ATOM   2713 H  HB2  . LYS A 1 169 ? 23.29943 3.42323  54.70773 1.000 46.81251 ?  169 LYS A HB2  1 
ATOM   2714 H  HB3  . LYS A 1 169 ? 23.56223 1.91198  54.29244 1.000 46.81251 ?  169 LYS A HB3  1 
ATOM   2715 H  HG2  . LYS A 1 169 ? 21.75412 2.37548  55.87537 1.000 50.45376 ?  169 LYS A HG2  1 
ATOM   2716 H  HG3  . LYS A 1 169 ? 22.68875 1.12176  56.15831 1.000 50.45376 ?  169 LYS A HG3  1 
ATOM   2717 H  HD2  . LYS A 1 169 ? 22.81464 1.93383  58.18502 1.000 54.17377 ?  169 LYS A HD2  1 
ATOM   2718 H  HD3  . LYS A 1 169 ? 23.88046 2.93828  57.56816 1.000 54.17377 ?  169 LYS A HD3  1 
ATOM   2719 H  HE2  . LYS A 1 169 ? 22.16631 4.54666  57.27263 1.000 57.13197 ?  169 LYS A HE2  1 
ATOM   2720 H  HE3  . LYS A 1 169 ? 21.12949 3.54642  57.94340 1.000 57.13197 ?  169 LYS A HE3  1 
ATOM   2721 H  HZ1  . LYS A 1 169 ? 21.83280 5.09993  59.47013 1.000 58.75223 ?  169 LYS A HZ1  1 
ATOM   2722 H  HZ2  . LYS A 1 169 ? 22.27610 3.79563  59.91804 1.000 58.75223 ?  169 LYS A HZ2  1 
ATOM   2723 H  HZ3  . LYS A 1 169 ? 23.21825 4.71011  59.30615 1.000 58.75223 ?  169 LYS A HZ3  1 
ATOM   2724 N  N    . LEU A 1 170 ? 25.91139 0.55298  54.70613 1.000 36.53252 ?  170 LEU A N    1 
ATOM   2725 C  CA   . LEU A 1 170 ? 26.36394 -0.82179 54.94109 1.000 38.91131 ?  170 LEU A CA   1 
ATOM   2726 C  C    . LEU A 1 170 ? 27.78282 -0.86633 55.51821 1.000 43.53825 ?  170 LEU A C    1 
ATOM   2727 O  O    . LEU A 1 170 ? 28.05012 -1.67466 56.42561 1.000 43.10385 ?  170 LEU A O    1 
ATOM   2728 C  CB   . LEU A 1 170 ? 26.20410 -1.65250 53.65064 1.000 37.13355 ?  170 LEU A CB   1 
ATOM   2729 C  CG   . LEU A 1 170 ? 24.78870 -1.87200 53.10194 1.000 35.41270 ?  170 LEU A CG   1 
ATOM   2730 C  CD1  . LEU A 1 170 ? 24.63897 -2.79400 51.77022 1.000 33.77229 ?  170 LEU A CD1  1 
ATOM   2731 C  CD2  . LEU A 1 170 ? 23.86314 -2.46002 54.20398 1.000 35.84929 ?  170 LEU A CD2  1 
ATOM   2732 H  H    . LEU A 1 170 ? 25.81967 0.77525  53.88043 1.000 43.84532 ?  170 LEU A H    1 
ATOM   2733 H  HA   . LEU A 1 170 ? 25.79859 -1.23957 55.60947 1.000 46.69988 ?  170 LEU A HA   1 
ATOM   2734 H  HB2  . LEU A 1 170 ? 26.70760 -1.20805 52.95074 1.000 44.56656 ?  170 LEU A HB2  1 
ATOM   2735 H  HB3  . LEU A 1 170 ? 26.57619 -2.53224 53.81945 1.000 44.56656 ?  170 LEU A HB3  1 
ATOM   2736 H  HG   . LEU A 1 170 ? 24.51703 -0.98365 52.82278 1.000 42.50154 ?  170 LEU A HG   1 
ATOM   2737 H  HD11 . LEU A 1 170 ? 23.70115 -2.85037 51.52895 1.000 40.53305 ?  170 LEU A HD11 1 
ATOM   2738 H  HD12 . LEU A 1 170 ? 25.14274 -2.38862 51.04719 1.000 40.53305 ?  170 LEU A HD12 1 
ATOM   2739 H  HD13 . LEU A 1 170 ? 24.98582 -3.68000 51.95890 1.000 40.53305 ?  170 LEU A HD13 1 
ATOM   2740 H  HD21 . LEU A 1 170 ? 23.02079 -2.72336 53.80151 1.000 43.02545 ?  170 LEU A HD21 1 
ATOM   2741 H  HD22 . LEU A 1 170 ? 24.29581 -3.23215 54.60086 1.000 43.02545 ?  170 LEU A HD22 1 
ATOM   2742 H  HD23 . LEU A 1 170 ? 23.70881 -1.78289 54.88116 1.000 43.02545 ?  170 LEU A HD23 1 
ATOM   2743 N  N    . ASP A 1 171 ? 28.70746 -0.01080 55.03342 1.000 47.75426 ?  171 ASP A N    1 
ATOM   2744 C  CA   . ASP A 1 171 ? 30.10927 -0.10506 55.46398 1.000 52.51426 ?  171 ASP A CA   1 
ATOM   2745 C  C    . ASP A 1 171 ? 30.32305 0.44723  56.87810 1.000 55.55114 ?  171 ASP A C    1 
ATOM   2746 O  O    . ASP A 1 171 ? 31.31264 0.10175  57.53986 1.000 56.46209 ?  171 ASP A O    1 
ATOM   2747 C  CB   . ASP A 1 171 ? 31.11234 0.63708  54.54872 1.000 53.86523 ?  171 ASP A CB   1 
ATOM   2748 C  CG   . ASP A 1 171 ? 31.31431 0.00625  53.13301 1.000 55.20443 ?  171 ASP A CG   1 
ATOM   2749 O  OD1  . ASP A 1 171 ? 30.97691 -1.17013 52.83956 1.000 55.08739 ?  171 ASP A OD1  1 
ATOM   2750 O  OD2  . ASP A 1 171 ? 31.97350 0.72596  52.35416 1.000 56.30154 -1 171 ASP A OD2  1 
ATOM   2751 H  H    . ASP A 1 171 ? 28.54725 0.61669  54.46757 1.000 57.31141 ?  171 ASP A H    1 
ATOM   2752 H  HA   . ASP A 1 171 ? 30.32163 -1.04993 55.40912 1.000 63.02342 ?  171 ASP A HA   1 
ATOM   2753 H  HB2  . ASP A 1 171 ? 30.79533 1.54455  54.41869 1.000 64.64458 ?  171 ASP A HB2  1 
ATOM   2754 H  HB3  . ASP A 1 171 ? 31.97759 0.64754  54.98706 1.000 64.64458 ?  171 ASP A HB3  1 
ATOM   2755 N  N    . GLU A 1 172 ? 29.44888 1.32299  57.34279 1.000 57.50157 ?  172 GLU A N    1 
ATOM   2756 C  CA   . GLU A 1 172 ? 29.52317 1.82980  58.70442 1.000 60.04671 ?  172 GLU A CA   1 
ATOM   2757 C  C    . GLU A 1 172 ? 28.53343 1.15998  59.65201 1.000 61.69947 ?  172 GLU A C    1 
ATOM   2758 O  O    . GLU A 1 172 ? 28.46866 1.55029  60.82762 1.000 62.83251 ?  172 GLU A O    1 
ATOM   2759 C  CB   . GLU A 1 172 ? 29.32850 3.34351  58.68562 1.000 61.11318 ?  172 GLU A CB   1 
ATOM   2760 C  CG   . GLU A 1 172 ? 27.90242 3.80266  58.82815 1.000 62.20078 ?  172 GLU A CG   1 
ATOM   2761 C  CD   . GLU A 1 172 ? 27.76515 5.31532  58.69255 1.000 63.15624 ?  172 GLU A CD   1 
ATOM   2762 O  OE1  . GLU A 1 172 ? 28.19885 5.90019  57.65514 1.000 62.67399 ?  172 GLU A OE1  1 
ATOM   2763 O  OE2  . GLU A 1 172 ? 27.25531 5.90624  59.67990 1.000 64.36086 -1 172 GLU A OE2  1 
ATOM   2764 H  H    . GLU A 1 172 ? 28.79547 1.64341  56.88454 1.000 69.00819 ?  172 GLU A H    1 
ATOM   2765 H  HA   . GLU A 1 172 ? 30.40458 1.65148  59.06802 1.000 72.06235 ?  172 GLU A HA   1 
ATOM   2766 H  HB2  . GLU A 1 172 ? 29.83242 3.72703  59.42038 1.000 73.34212 ?  172 GLU A HB2  1 
ATOM   2767 H  HB3  . GLU A 1 172 ? 29.66117 3.68540  57.84103 1.000 73.34212 ?  172 GLU A HB3  1 
ATOM   2768 H  HG2  . GLU A 1 172 ? 27.36418 3.38748  58.13618 1.000 74.64724 ?  172 GLU A HG2  1 
ATOM   2769 H  HG3  . GLU A 1 172 ? 27.57215 3.54686  59.70359 1.000 74.64724 ?  172 GLU A HG3  1 
ATOM   2770 N  N    . LEU A 1 173 ? 27.77865 0.15585  59.17801 1.000 61.52001 ?  173 LEU A N    1 
ATOM   2771 C  CA   . LEU A 1 173 ? 26.84687 -0.62453 59.99448 1.000 60.86797 ?  173 LEU A CA   1 
ATOM   2772 C  C    . LEU A 1 173 ? 26.33610 -1.85546 59.26248 1.000 60.47808 ?  173 LEU A C    1 
ATOM   2773 O  O    . LEU A 1 173 ? 25.24900 -1.84597 58.67970 1.000 60.33869 ?  173 LEU A O    1 
ATOM   2774 H  H    . LEU A 1 173 ? 27.79139 -0.09891 58.35671 1.000 73.83031 ?  173 LEU A H    1 
ATOM   2775 H  HA   . LEU A 1 173 ? 27.29367 -0.91312 60.80565 1.000 73.04786 ?  173 LEU A HA   1 
HETATM 2776 C  C1   . EDO B 2 .   ? 28.81636 40.38896 43.91900 0.950 20.32434 ?  201 EDO A C1   1 
HETATM 2777 O  O1   . EDO B 2 .   ? 28.11173 41.59360 44.32761 0.950 17.64588 ?  201 EDO A O1   1 
HETATM 2778 C  C2   . EDO B 2 .   ? 30.20041 40.42213 44.55109 0.950 22.45676 ?  201 EDO A C2   1 
HETATM 2779 O  O2   . EDO B 2 .   ? 30.07662 40.48389 45.97732 0.950 21.67941 ?  201 EDO A O2   1 
HETATM 2780 H  H11  . EDO B 2 .   ? 28.27126 39.50164 44.24762 0.950 24.39551 ?  201 EDO A H11  1 
HETATM 2781 H  H12  . EDO B 2 .   ? 28.89801 40.34884 42.83080 0.950 24.39551 ?  201 EDO A H12  1 
HETATM 2782 H  HO1  . EDO B 2 .   ? 27.34244 41.72627 43.75693 0.950 21.18135 ?  201 EDO A HO1  1 
HETATM 2783 H  H21  . EDO B 2 .   ? 30.75917 39.52820 44.26621 0.950 26.95441 ?  201 EDO A H21  1 
HETATM 2784 H  H22  . EDO B 2 .   ? 30.75207 41.29228 44.18920 0.950 26.95441 ?  201 EDO A H22  1 
HETATM 2785 H  HO2  . EDO B 2 .   ? 30.95702 40.51056 46.37641 0.950 26.02159 ?  201 EDO A HO2  1 
HETATM 2786 C  C1   . EDO C 2 .   ? 13.06582 30.28410 51.66452 0.859 23.36691 ?  202 EDO A C1   1 
HETATM 2787 O  O1   . EDO C 2 .   ? 12.70066 30.21142 53.08479 0.859 22.82158 ?  202 EDO A O1   1 
HETATM 2788 C  C2   . EDO C 2 .   ? 14.33044 29.46281 51.36393 0.859 23.74571 ?  202 EDO A C2   1 
HETATM 2789 O  O2   . EDO C 2 .   ? 14.07581 28.11635 51.78703 0.859 23.75790 ?  202 EDO A O2   1 
HETATM 2790 H  H11  . EDO C 2 .   ? 12.23843 29.90847 51.05889 0.859 28.04660 ?  202 EDO A H11  1 
HETATM 2791 H  H12  . EDO C 2 .   ? 13.23768 31.32653 51.38837 0.859 28.04660 ?  202 EDO A H12  1 
HETATM 2792 H  HO1  . EDO C 2 .   ? 11.90575 30.73954 53.24065 0.859 27.39220 ?  202 EDO A HO1  1 
HETATM 2793 H  H21  . EDO C 2 .   ? 14.55724 29.48996 50.29609 0.859 28.50115 ?  202 EDO A H21  1 
HETATM 2794 H  H22  . EDO C 2 .   ? 15.18821 29.87457 51.89980 0.859 28.50115 ?  202 EDO A H22  1 
HETATM 2795 H  HO2  . EDO C 2 .   ? 14.86519 27.57754 51.63993 0.859 28.51578 ?  202 EDO A HO2  1 
HETATM 2796 C  C1   . EDO D 2 .   ? 33.53877 -5.81978 54.88090 0.821 28.35931 ?  203 EDO A C1   1 
HETATM 2797 O  O1   . EDO D 2 .   ? 33.56856 -4.96513 53.72397 0.821 30.45391 ?  203 EDO A O1   1 
HETATM 2798 C  C2   . EDO D 2 .   ? 34.91500 -6.43839 54.99497 0.821 25.65776 ?  203 EDO A C2   1 
HETATM 2799 O  O2   . EDO D 2 .   ? 36.03722 -5.47885 54.89594 0.821 21.81823 ?  203 EDO A O2   1 
HETATM 2800 H  H11  . EDO D 2 .   ? 33.30054 -5.24427 55.77784 0.821 34.03748 ?  203 EDO A H11  1 
HETATM 2801 H  H12  . EDO D 2 .   ? 32.77747 -6.59433 54.76705 0.821 34.03748 ?  203 EDO A H12  1 
HETATM 2802 H  HO1  . EDO D 2 .   ? 32.72459 -4.49972 53.64524 0.821 36.55099 ?  203 EDO A HO1  1 
HETATM 2803 H  H21  . EDO D 2 .   ? 34.98423 -6.95418 55.95499 0.821 30.79561 ?  203 EDO A H21  1 
HETATM 2804 H  H22  . EDO D 2 .   ? 35.02609 -7.18378 54.20470 0.821 30.79561 ?  203 EDO A H22  1 
HETATM 2805 H  HO2  . EDO D 2 .   ? 36.87563 -5.95423 54.97447 0.821 26.18818 ?  203 EDO A HO2  1 
HETATM 2806 CD CD   . CD  E 3 .   ? 23.41139 -0.98048 44.73262 1.000 14.68795 ?  204 CD  A CD   1 
HETATM 2807 CD CD   . CD  F 3 .   ? 26.33903 -2.37339 45.85026 0.981 14.62183 ?  205 CD  A CD   1 
HETATM 2808 CD CD   . CD  G 3 .   ? 26.23814 46.39357 38.72229 0.983 16.80087 ?  206 CD  A CD   1 
HETATM 2809 CD CD   . CD  H 3 .   ? 30.25128 19.25196 64.45169 0.237 36.60695 ?  207 CD  A CD   1 
HETATM 2810 NA NA   . NA  I 4 .   ? 10.69614 16.28036 28.30551 0.823 39.95905 ?  208 NA  A NA   1 
HETATM 2811 NA NA   . NA  J 4 .   ? 15.84883 12.86108 29.29177 0.516 31.80515 ?  209 NA  A NA   1 
HETATM 2812 CL CL   . CL  K 5 .   ? 26.73577 47.82409 40.71599 0.941 18.77523 ?  210 CL  A CL   1 
HETATM 2813 CL CL   . CL  L 5 .   ? 28.48612 45.97777 38.10153 0.629 22.37148 ?  211 CL  A CL   1 
HETATM 2814 CL CL   . CL  M 5 .   ? 10.16476 40.71650 33.30992 1.000 48.91024 ?  212 CL  A CL   1 
HETATM 2815 O  O    . HOH N 6 .   ? 33.15813 2.33411  51.98619 1.000 44.65870 ?  301 HOH A O    1 
HETATM 2816 O  O    . HOH N 6 .   ? 16.76647 34.21088 24.11547 0.590 25.05783 ?  302 HOH A O    1 
HETATM 2817 O  O    . HOH N 6 .   ? 36.07857 22.26460 22.81669 0.779 32.07568 ?  303 HOH A O    1 
HETATM 2818 O  O    . HOH N 6 .   ? 31.71512 -3.70827 52.80343 1.000 25.93789 ?  304 HOH A O    1 
HETATM 2819 O  O    . HOH N 6 .   ? 33.55949 26.82699 58.02147 1.000 30.06172 ?  305 HOH A O    1 
HETATM 2820 O  O    . HOH N 6 .   ? 33.30006 29.61053 55.51446 1.000 39.85853 ?  306 HOH A O    1 
HETATM 2821 O  O    . HOH N 6 .   ? 22.70313 3.42762  37.04041 0.902 20.28564 ?  307 HOH A O    1 
HETATM 2822 O  O    . HOH N 6 .   ? 13.91463 14.53602 26.03006 1.000 24.78580 ?  308 HOH A O    1 
HETATM 2823 O  O    . HOH N 6 .   ? 30.97982 42.48564 41.17095 0.708 30.34620 ?  309 HOH A O    1 
HETATM 2824 O  O    . HOH N 6 .   ? 14.82974 33.28909 24.03878 0.604 22.02240 ?  310 HOH A O    1 
HETATM 2825 O  O    . HOH N 6 .   ? 34.33327 24.02152 29.91701 1.000 30.77681 ?  311 HOH A O    1 
HETATM 2826 O  O    . HOH N 6 .   ? 24.33183 14.54560 27.27083 0.825 23.83599 ?  312 HOH A O    1 
HETATM 2827 O  O    . HOH N 6 .   ? 35.95747 24.35044 37.57623 1.000 32.52780 ?  313 HOH A O    1 
HETATM 2828 O  O    . HOH N 6 .   ? 32.29607 14.94908 28.88735 1.000 37.00008 ?  314 HOH A O    1 
HETATM 2829 O  O    . HOH N 6 .   ? 17.46478 36.39597 22.65369 0.721 23.13776 ?  315 HOH A O    1 
HETATM 2830 O  O    . HOH N 6 .   ? 26.62364 6.38424  36.38341 1.000 24.77022 ?  316 HOH A O    1 
HETATM 2831 O  O    . HOH N 6 .   ? 16.68810 37.21384 35.47903 0.827 25.98541 ?  317 HOH A O    1 
HETATM 2832 O  O    . HOH N 6 .   ? 12.26384 16.69610 25.82811 1.000 33.25351 ?  318 HOH A O    1 
HETATM 2833 O  O    . HOH N 6 .   ? 33.84124 40.90119 44.76022 1.000 38.09029 ?  319 HOH A O    1 
HETATM 2834 O  O    . HOH N 6 .   ? 12.69264 20.86488 50.44051 1.000 38.78664 ?  320 HOH A O    1 
HETATM 2835 O  O    . HOH N 6 .   ? 31.59455 30.39226 24.78481 1.000 24.47074 ?  321 HOH A O    1 
HETATM 2836 O  O    . HOH N 6 .   ? 28.13187 33.38894 54.07221 1.000 29.08973 ?  322 HOH A O    1 
HETATM 2837 O  O    . HOH N 6 .   ? 14.201   31.415   54.878   0.935 27.54958 ?  323 HOH A O    1 
HETATM 2838 O  O    . HOH N 6 .   ? 43.957   21.930   54.421   1.000 16.12658 ?  324 HOH A O    1 
HETATM 2839 O  O    . HOH N 6 .   ? 23.39102 12.34291 52.28258 1.000 21.37956 ?  325 HOH A O    1 
HETATM 2840 O  O    . HOH N 6 .   ? 15.34923 27.33667 40.09646 1.000 25.17364 ?  326 HOH A O    1 
HETATM 2841 O  O    . HOH N 6 .   ? 26.98974 22.37075 52.90965 1.000 14.84388 ?  327 HOH A O    1 
HETATM 2842 O  O    . HOH N 6 .   ? 14.95248 40.04426 30.46430 1.000 27.52157 ?  328 HOH A O    1 
HETATM 2843 O  O    . HOH N 6 .   ? 28.156   41.715   47.323   1.000 15.53888 ?  329 HOH A O    1 
HETATM 2844 O  O    . HOH N 6 .   ? 30.65024 26.58574 28.53714 1.000 26.26229 ?  330 HOH A O    1 
HETATM 2845 O  O    . HOH N 6 .   ? 39.55907 22.21784 54.98089 1.000 24.81151 ?  331 HOH A O    1 
HETATM 2846 O  O    . HOH N 6 .   ? 20.42715 25.88629 17.26629 1.000 33.19519 ?  332 HOH A O    1 
HETATM 2847 O  O    . HOH N 6 .   ? 30.09096 42.26671 36.73363 0.857 20.65770 ?  333 HOH A O    1 
HETATM 2848 O  O    . HOH N 6 .   ? 25.72227 12.56861 34.36885 1.000 28.04011 ?  334 HOH A O    1 
HETATM 2849 O  O    . HOH N 6 .   ? 32.19927 29.58853 52.35890 1.000 18.86974 ?  335 HOH A O    1 
HETATM 2850 O  O    . HOH N 6 .   ? 32.39203 43.06283 32.77674 0.966 28.26653 ?  336 HOH A O    1 
HETATM 2851 O  O    . HOH N 6 .   ? 32.25393 33.08392 24.32883 0.931 25.69151 ?  337 HOH A O    1 
HETATM 2852 O  O    . HOH N 6 .   ? 35.19167 28.88874 29.11330 0.845 25.76587 ?  338 HOH A O    1 
HETATM 2853 O  O    . HOH N 6 .   ? 29.37613 36.12325 54.66363 1.000 39.62210 ?  339 HOH A O    1 
HETATM 2854 O  O    . HOH N 6 .   ? 27.09504 35.98904 53.95708 1.000 28.41126 ?  340 HOH A O    1 
HETATM 2855 O  O    . HOH N 6 .   ? 13.71662 32.36152 30.79822 1.000 22.38412 ?  341 HOH A O    1 
HETATM 2856 O  O    . HOH N 6 .   ? 26.95690 34.27497 27.99363 1.000 18.23801 ?  342 HOH A O    1 
HETATM 2857 O  O    . HOH N 6 .   ? 15.39987 27.22396 53.96656 1.000 35.94928 ?  343 HOH A O    1 
HETATM 2858 O  O    . HOH N 6 .   ? 38.74262 32.03465 41.79426 1.000 33.55596 ?  344 HOH A O    1 
HETATM 2859 O  O    . HOH N 6 .   ? 29.96744 -1.70979 50.38454 1.000 36.09502 ?  345 HOH A O    1 
HETATM 2860 O  O    . HOH N 6 .   ? 19.69527 30.16899 45.93854 1.000 14.85627 ?  346 HOH A O    1 
HETATM 2861 O  O    . HOH N 6 .   ? 36.53685 31.09706 52.98362 1.000 19.29372 ?  347 HOH A O    1 
HETATM 2862 O  O    . HOH N 6 .   ? 27.31051 13.93842 51.06652 1.000 28.64205 ?  348 HOH A O    1 
HETATM 2863 O  O    . HOH N 6 .   ? 15.35475 23.48227 48.37706 1.000 22.01669 ?  349 HOH A O    1 
HETATM 2864 O  O    . HOH N 6 .   ? 30.40039 16.78426 56.04968 1.000 25.53177 ?  350 HOH A O    1 
HETATM 2865 O  O    . HOH N 6 .   ? 32.02207 18.59418 54.62259 1.000 19.63372 ?  351 HOH A O    1 
HETATM 2866 O  O    . HOH N 6 .   ? 29.422   43.679   43.149   1.000 26.35139 ?  352 HOH A O    1 
HETATM 2867 O  O    . HOH N 6 .   ? 21.94027 23.68209 18.12115 0.816 30.19460 ?  353 HOH A O    1 
HETATM 2868 O  O    . HOH N 6 .   ? 30.28833 15.57444 53.57937 1.000 34.24338 ?  354 HOH A O    1 
HETATM 2869 O  O    . HOH N 6 .   ? 17.14340 21.68000 20.56445 0.681 28.74621 ?  355 HOH A O    1 
HETATM 2870 O  O    . HOH N 6 .   ? 17.70692 30.04090 38.20186 1.000 15.18766 ?  356 HOH A O    1 
HETATM 2871 O  O    . HOH N 6 .   ? 31.19595 18.37382 33.83498 0.630 24.31943 ?  357 HOH A O    1 
HETATM 2872 O  O    . HOH N 6 .   ? 38.30570 19.65279 54.47988 1.000 26.00515 ?  358 HOH A O    1 
HETATM 2873 O  O    . HOH N 6 .   ? 30.11624 12.54869 49.67540 1.000 45.54976 ?  359 HOH A O    1 
HETATM 2874 O  O    . HOH N 6 .   ? 13.76043 20.72049 46.50758 1.000 47.37504 ?  360 HOH A O    1 
HETATM 2875 O  O    . HOH N 6 .   ? 13.83545 28.56562 36.15497 0.970 28.27386 ?  361 HOH A O    1 
HETATM 2876 O  O    . HOH N 6 .   ? 23.84936 46.27482 39.06851 1.000 16.78109 ?  362 HOH A O    1 
HETATM 2877 O  O    . HOH N 6 .   ? 34.409   16.470   47.881   1.000 36.05077 ?  363 HOH A O    1 
HETATM 2878 O  O    . HOH N 6 .   ? 18.26324 16.29773 31.93356 1.000 23.90731 ?  364 HOH A O    1 
HETATM 2879 O  O    . HOH N 6 .   ? 21.48576 42.34068 50.49687 1.000 28.86155 ?  365 HOH A O    1 
HETATM 2880 O  O    . HOH N 6 .   ? 26.94777 49.61439 31.86997 1.000 25.07609 ?  366 HOH A O    1 
HETATM 2881 O  O    . HOH N 6 .   ? 38.227   26.647   52.066   1.000 17.47898 ?  367 HOH A O    1 
HETATM 2882 O  O    . HOH N 6 .   ? 25.12509 15.44876 30.68401 0.981 25.94837 ?  368 HOH A O    1 
HETATM 2883 O  O    . HOH N 6 .   ? 27.50341 28.53282 12.85403 1.000 35.98283 ?  369 HOH A O    1 
HETATM 2884 O  O    . HOH N 6 .   ? 13.31753 28.06748 25.65256 1.000 37.26689 ?  370 HOH A O    1 
HETATM 2885 O  O    . HOH N 6 .   ? 35.51400 22.97965 25.41727 1.000 28.50546 ?  371 HOH A O    1 
HETATM 2886 O  O    . HOH N 6 .   ? 34.35038 32.70436 29.30827 1.000 21.61262 ?  372 HOH A O    1 
HETATM 2887 O  O    . HOH N 6 .   ? 38.29369 19.63991 31.48364 1.000 48.31329 ?  373 HOH A O    1 
HETATM 2888 O  O    . HOH N 6 .   ? 23.00028 2.39774  41.68798 0.954 19.58566 ?  374 HOH A O    1 
HETATM 2889 O  O    . HOH N 6 .   ? 18.59022 42.74756 26.14010 1.000 18.87808 ?  375 HOH A O    1 
HETATM 2890 O  O    . HOH N 6 .   ? 33.00819 17.99684 36.20091 0.944 27.95784 ?  376 HOH A O    1 
HETATM 2891 O  O    . HOH N 6 .   ? 26.73339 25.19435 64.97957 1.000 37.64637 ?  377 HOH A O    1 
HETATM 2892 O  O    . HOH N 6 .   ? 29.57546 17.88695 40.13877 1.000 18.41547 ?  378 HOH A O    1 
HETATM 2893 O  O    . HOH N 6 .   ? 20.10953 4.06159  34.24824 1.000 27.82354 ?  379 HOH A O    1 
HETATM 2894 O  O    . HOH N 6 .   ? 17.10123 12.12337 27.64159 1.000 27.52856 ?  380 HOH A O    1 
HETATM 2895 O  O    . HOH N 6 .   ? 16.48386 12.93639 52.79176 1.000 35.15892 ?  381 HOH A O    1 
HETATM 2896 O  O    . HOH N 6 .   ? 21.88844 19.41405 52.43088 1.000 15.66396 ?  382 HOH A O    1 
HETATM 2897 O  O    . HOH N 6 .   ? 31.66568 28.73539 58.05909 1.000 28.07840 ?  383 HOH A O    1 
HETATM 2898 O  O    . HOH N 6 .   ? 26.71274 9.86164  44.42037 1.000 24.16544 ?  384 HOH A O    1 
HETATM 2899 O  O    . HOH N 6 .   ? 19.50793 11.52554 32.36247 1.000 28.23034 ?  385 HOH A O    1 
HETATM 2900 O  O    . HOH N 6 .   ? 24.71980 29.77085 63.15729 1.000 43.39486 ?  386 HOH A O    1 
HETATM 2901 O  O    . HOH N 6 .   ? 23.62549 6.12045  36.60367 0.799 20.47904 ?  387 HOH A O    1 
HETATM 2902 O  O    . HOH N 6 .   ? 26.80692 40.15034 35.08585 0.965 17.10217 ?  388 HOH A O    1 
HETATM 2903 O  O    . HOH N 6 .   ? 15.93200 17.60840 31.07651 1.000 26.31278 ?  389 HOH A O    1 
HETATM 2904 O  O    . HOH N 6 .   ? 21.02833 35.66775 40.07997 0.993 15.14383 ?  390 HOH A O    1 
HETATM 2905 O  O    . HOH N 6 .   ? 25.07981 25.46210 18.38454 1.000 19.40075 ?  391 HOH A O    1 
HETATM 2906 O  O    . HOH N 6 .   ? 11.44509 18.21499 24.48393 1.000 46.48397 ?  392 HOH A O    1 
HETATM 2907 O  O    . HOH N 6 .   ? 26.90265 26.93923 17.02166 1.000 27.67701 ?  393 HOH A O    1 
HETATM 2908 O  O    . HOH N 6 .   ? 16.22277 34.97246 33.83411 1.000 25.46588 ?  394 HOH A O    1 
HETATM 2909 O  O    . HOH N 6 .   ? 37.14555 31.73042 32.66846 1.000 45.14337 ?  395 HOH A O    1 
HETATM 2910 O  O    . HOH N 6 .   ? 18.84915 28.15342 16.69283 1.000 24.15558 ?  396 HOH A O    1 
HETATM 2911 O  O    . HOH N 6 .   ? 15.86343 22.88014 21.95939 1.000 35.32763 ?  397 HOH A O    1 
HETATM 2912 O  O    . HOH N 6 .   ? 30.67066 37.32808 42.26260 1.000 20.01889 ?  398 HOH A O    1 
HETATM 2913 O  O    . HOH N 6 .   ? 18.33640 38.96264 33.54474 0.904 24.34667 ?  399 HOH A O    1 
HETATM 2914 O  O    . HOH N 6 .   ? 13.01534 20.36689 43.47354 1.000 23.02685 ?  400 HOH A O    1 
HETATM 2915 O  O    . HOH N 6 .   ? 16.09740 42.03198 42.27479 1.000 24.32052 ?  401 HOH A O    1 
HETATM 2916 O  O    . HOH N 6 .   ? 19.19276 41.42999 34.70232 1.000 23.54016 ?  402 HOH A O    1 
HETATM 2917 O  O    . HOH N 6 .   ? 19.04581 9.02371  53.74839 0.856 36.51316 ?  403 HOH A O    1 
HETATM 2918 O  O    . HOH N 6 .   ? 28.47776 33.58461 38.48534 1.000 16.66017 ?  404 HOH A O    1 
HETATM 2919 O  O    . HOH N 6 .   ? 16.27960 45.45791 29.78746 1.000 19.95556 ?  405 HOH A O    1 
HETATM 2920 O  O    . HOH N 6 .   ? 17.57802 13.12836 31.54869 1.000 38.43818 ?  406 HOH A O    1 
HETATM 2921 O  O    . HOH N 6 .   ? 15.55135 42.58172 32.47834 1.000 37.49200 ?  407 HOH A O    1 
HETATM 2922 O  O    . HOH N 6 .   ? 11.476   27.833   54.031   1.000 27.60109 ?  408 HOH A O    1 
HETATM 2923 O  O    . HOH N 6 .   ? 20.74586 3.35044  49.20244 1.000 22.96960 ?  409 HOH A O    1 
HETATM 2924 O  O    . HOH N 6 .   ? 34.94105 32.31954 36.36928 0.980 23.82026 ?  410 HOH A O    1 
HETATM 2925 O  O    . HOH N 6 .   ? 22.44485 43.05472 30.45634 0.799 20.08586 ?  411 HOH A O    1 
HETATM 2926 O  O    . HOH N 6 .   ? 33.88600 13.33074 51.13957 1.000 25.11151 ?  412 HOH A O    1 
HETATM 2927 O  O    . HOH N 6 .   ? 24.02746 32.24414 18.64837 1.000 28.29698 ?  413 HOH A O    1 
HETATM 2928 O  O    . HOH N 6 .   ? 21.44436 26.80420 52.50927 1.000 14.87935 ?  414 HOH A O    1 
HETATM 2929 O  O    . HOH N 6 .   ? 16.53432 7.63337  38.76532 0.693 24.73308 ?  415 HOH A O    1 
HETATM 2930 O  O    . HOH N 6 .   ? 28.28936 31.52902 56.41861 1.000 32.32115 ?  416 HOH A O    1 
HETATM 2931 O  O    . HOH N 6 .   ? 38.61478 18.54377 45.90881 1.000 25.78332 ?  417 HOH A O    1 
HETATM 2932 O  O    . HOH N 6 .   ? 12.93376 22.89102 37.00967 1.000 30.85299 ?  418 HOH A O    1 
HETATM 2933 O  O    . HOH N 6 .   ? 36.01827 19.86390 55.52339 1.000 29.94514 ?  419 HOH A O    1 
HETATM 2934 O  O    . HOH N 6 .   ? 32.02840 35.25251 41.23389 1.000 24.55974 ?  420 HOH A O    1 
HETATM 2935 O  O    . HOH N 6 .   ? 23.41032 38.33299 52.63261 0.975 21.03494 ?  421 HOH A O    1 
HETATM 2936 O  O    . HOH N 6 .   ? 20.71108 18.57259 56.83654 1.000 29.05665 ?  422 HOH A O    1 
HETATM 2937 O  O    . HOH N 6 .   ? 19.93583 35.70306 52.17367 0.895 21.77659 ?  423 HOH A O    1 
HETATM 2938 O  O    . HOH N 6 .   ? 23.34639 6.19926  53.95771 1.000 30.24804 ?  424 HOH A O    1 
HETATM 2939 O  O    . HOH N 6 .   ? 20.821   38.367   51.515   1.000 26.29554 ?  425 HOH A O    1 
HETATM 2940 O  O    . HOH N 6 .   ? 34.13120 39.15944 40.76741 1.000 42.20345 ?  426 HOH A O    1 
HETATM 2941 O  O    . HOH N 6 .   ? 27.53911 10.96276 42.17209 1.000 35.11612 ?  427 HOH A O    1 
HETATM 2942 O  O    . HOH N 6 .   ? 39.52599 22.46884 47.92501 1.000 23.91694 ?  428 HOH A O    1 
HETATM 2943 O  O    . HOH N 6 .   ? 14.27773 33.06503 36.81646 1.000 27.88052 ?  429 HOH A O    1 
HETATM 2944 O  O    . HOH N 6 .   ? 14.39572 28.03985 19.70335 1.000 37.70884 ?  430 HOH A O    1 
HETATM 2945 O  O    . HOH N 6 .   ? 13.08914 23.00874 46.37055 1.000 34.62575 ?  431 HOH A O    1 
HETATM 2946 O  O    . HOH N 6 .   ? 27.55113 14.06419 42.03282 1.000 26.88252 ?  432 HOH A O    1 
HETATM 2947 O  O    . HOH N 6 .   ? 30.04989 35.69149 39.24541 1.000 17.64380 ?  433 HOH A O    1 
HETATM 2948 O  O    . HOH N 6 .   ? 35.52658 27.47027 51.99358 0.982 21.78318 ?  434 HOH A O    1 
HETATM 2949 O  O    . HOH N 6 .   ? 13.24143 25.16175 38.62475 1.000 35.29346 ?  435 HOH A O    1 
HETATM 2950 O  O    . HOH N 6 .   ? 36.94977 25.07991 34.60753 1.000 43.20436 ?  436 HOH A O    1 
HETATM 2951 O  O    . HOH N 6 .   ? 35.66314 17.42251 39.22297 1.000 33.02449 ?  437 HOH A O    1 
HETATM 2952 O  O    . HOH N 6 .   ? 24.37440 36.79326 56.15705 1.000 48.78351 ?  438 HOH A O    1 
HETATM 2953 O  O    . HOH N 6 .   ? 14.14734 33.71941 17.12907 1.000 31.75005 ?  439 HOH A O    1 
HETATM 2954 O  O    . HOH N 6 .   ? 36.56737 27.72389 44.49128 1.000 35.98527 ?  440 HOH A O    1 
HETATM 2955 O  O    . HOH N 6 .   ? 36.14886 23.24390 57.33682 1.000 35.70140 ?  441 HOH A O    1 
HETATM 2956 O  O    . HOH N 6 .   ? 17.32731 34.97395 17.19693 1.000 20.81556 ?  442 HOH A O    1 
HETATM 2957 O  O    . HOH N 6 .   ? 13.04013 11.17461 36.07861 1.000 41.49328 ?  443 HOH A O    1 
HETATM 2958 O  O    . HOH N 6 .   ? 21.95312 34.41412 57.64838 1.000 28.81829 ?  444 HOH A O    1 
HETATM 2959 O  O    . HOH N 6 .   ? 14.08790 24.88766 24.28530 1.000 28.57168 ?  445 HOH A O    1 
HETATM 2960 O  O    . HOH N 6 .   ? 16.77823 21.85337 25.42229 0.888 28.53420 ?  446 HOH A O    1 
HETATM 2961 O  O    . HOH N 6 .   ? 18.42394 42.47605 40.45146 1.000 31.89827 ?  447 HOH A O    1 
HETATM 2962 O  O    . HOH N 6 .   ? 28.83344 15.48601 44.12126 1.000 40.70824 ?  448 HOH A O    1 
HETATM 2963 O  O    . HOH N 6 .   ? 20.32676 45.07253 40.30046 1.000 34.57605 ?  449 HOH A O    1 
HETATM 2964 O  O    . HOH N 6 .   ? 13.40575 35.19064 37.80349 0.932 34.18509 ?  450 HOH A O    1 
HETATM 2965 O  O    . HOH N 6 .   ? 13.11399 17.64709 31.32504 1.000 42.60668 ?  451 HOH A O    1 
HETATM 2966 O  O    . HOH N 6 .   ? 13.571   38.201   42.851   1.000 33.45363 ?  452 HOH A O    1 
HETATM 2967 O  O    . HOH N 6 .   ? 12.86842 34.98439 23.67427 0.845 32.94451 ?  453 HOH A O    1 
HETATM 2968 O  O    . HOH N 6 .   ? 31.57180 -1.32716 48.30364 1.000 36.67092 ?  454 HOH A O    1 
HETATM 2969 O  O    . HOH N 6 .   ? 31.99815 28.56324 62.32352 1.000 39.55049 ?  455 HOH A O    1 
HETATM 2970 O  O    . HOH N 6 .   ? 12.46090 29.92524 31.03470 0.992 29.34952 ?  456 HOH A O    1 
HETATM 2971 O  O    . HOH N 6 .   ? 21.22286 31.47301 58.44034 0.914 35.60968 ?  457 HOH A O    1 
HETATM 2972 O  O    . HOH N 6 .   ? 13.04023 36.52794 30.53822 1.000 30.62352 ?  458 HOH A O    1 
HETATM 2973 O  O    . HOH N 6 .   ? 35.64099 39.53644 31.93764 1.000 41.82162 ?  459 HOH A O    1 
HETATM 2974 O  O    . HOH N 6 .   ? 10.36910 13.99086 40.71345 1.000 38.10151 ?  460 HOH A O    1 
HETATM 2975 O  O    . HOH N 6 .   ? 34.01654 41.69667 30.96136 0.859 27.28940 ?  461 HOH A O    1 
HETATM 2976 O  O    . HOH N 6 .   ? 28.15605 5.88541  43.19804 1.000 31.92164 ?  462 HOH A O    1 
HETATM 2977 O  O    . HOH N 6 .   ? 33.04631 25.83160 28.28427 1.000 31.69300 ?  463 HOH A O    1 
HETATM 2978 O  O    . HOH N 6 .   ? 10.95027 25.15789 32.15823 1.000 34.33689 ?  464 HOH A O    1 
HETATM 2979 O  O    . HOH N 6 .   ? 11.44573 9.93622  48.52667 1.000 37.22006 ?  465 HOH A O    1 
HETATM 2980 O  O    . HOH N 6 .   ? 29.97091 5.90659  49.71054 1.000 35.45774 ?  466 HOH A O    1 
HETATM 2981 O  O    . HOH N 6 .   ? 21.99185 15.31619 60.57936 0.987 39.50988 ?  467 HOH A O    1 
HETATM 2982 O  O    . HOH N 6 .   ? 36.16107 41.63372 46.73041 1.000 32.67023 ?  468 HOH A O    1 
HETATM 2983 O  O    . HOH N 6 .   ? 18.32956 16.41493 54.12448 1.000 31.93102 ?  469 HOH A O    1 
HETATM 2984 O  O    . HOH N 6 .   ? 17.640   37.305   49.937   1.000 32.99262 ?  470 HOH A O    1 
HETATM 2985 O  O    . HOH N 6 .   ? 29.68811 14.46247 46.28116 1.000 34.79719 ?  471 HOH A O    1 
HETATM 2986 O  O    . HOH N 6 .   ? 11.21137 30.29964 25.76441 1.000 36.76836 ?  472 HOH A O    1 
HETATM 2987 O  O    . HOH N 6 .   ? 25.63455 17.19970 32.33339 0.959 34.72911 ?  473 HOH A O    1 
HETATM 2988 O  O    . HOH N 6 .   ? 14.89055 22.07952 23.80187 0.944 39.88866 ?  474 HOH A O    1 
HETATM 2989 O  O    . HOH N 6 .   ? 22.70021 22.52683 59.49026 1.000 35.27397 ?  475 HOH A O    1 
HETATM 2990 O  O    . HOH N 6 .   ? 36.04047 28.21302 31.86273 1.000 40.80755 ?  476 HOH A O    1 
HETATM 2991 O  O    . HOH N 6 .   ? 24.53352 10.01630 55.64392 1.000 44.91514 ?  477 HOH A O    1 
HETATM 2992 O  O    . HOH N 6 .   ? 30.55245 -4.00318 55.74824 1.000 39.14332 ?  478 HOH A O    1 
HETATM 2993 O  O    . HOH N 6 .   ? 31.74767 17.15396 38.47569 1.000 31.11200 ?  479 HOH A O    1 
HETATM 2994 O  O    . HOH N 6 .   ? 34.50616 37.23138 35.06237 1.000 40.52234 ?  480 HOH A O    1 
HETATM 2995 O  O    . HOH N 6 .   ? 12.39226 32.86878 24.51639 1.000 36.99147 ?  481 HOH A O    1 
HETATM 2996 O  O    . HOH N 6 .   ? 38.28418 27.22566 49.21742 1.000 24.07279 ?  482 HOH A O    1 
HETATM 2997 O  O    . HOH N 6 .   ? 12.00411 30.35508 39.89938 1.000 50.23183 ?  483 HOH A O    1 
HETATM 2998 O  O    . HOH N 6 .   ? 30.82010 34.48217 22.23892 0.988 32.24864 ?  484 HOH A O    1 
HETATM 2999 O  O    . HOH N 6 .   ? 25.14798 38.05669 54.98991 1.000 37.51914 ?  485 HOH A O    1 
HETATM 3000 O  O    . HOH N 6 .   ? 39.60530 30.37853 42.74000 1.000 38.19329 ?  486 HOH A O    1 
HETATM 3001 O  O    . HOH N 6 .   ? 11.97836 33.26057 28.79528 1.000 31.23228 ?  487 HOH A O    1 
HETATM 3002 O  O    . HOH N 6 .   ? 28.51881 49.82998 34.24541 1.000 29.56568 ?  488 HOH A O    1 
HETATM 3003 O  O    . HOH N 6 .   ? 23.46418 24.36318 16.49347 0.990 30.11860 ?  489 HOH A O    1 
HETATM 3004 O  O    . HOH N 6 .   ? 35.33883 16.88269 36.20669 1.000 52.47963 ?  490 HOH A O    1 
HETATM 3005 O  O    . HOH N 6 .   ? 26.61374 31.03924 19.14686 1.000 42.77210 ?  491 HOH A O    1 
HETATM 3006 O  O    . HOH N 6 .   ? 32.717   -1.072   43.693   0.980 41.11394 ?  492 HOH A O    1 
HETATM 3007 O  O    . HOH N 6 .   ? 36.81559 16.90921 45.58500 1.000 42.42747 ?  493 HOH A O    1 
HETATM 3008 O  O    . HOH N 6 .   ? 35.72466 33.16525 38.77544 1.000 38.99906 ?  494 HOH A O    1 
HETATM 3009 O  O    . HOH N 6 .   ? 30.89990 15.09212 58.21817 1.000 41.09016 ?  495 HOH A O    1 
HETATM 3010 O  O    . HOH N 6 .   ? 22.420   5.603    34.076   0.897 24.52316 ?  496 HOH A O    1 
HETATM 3011 O  O    . HOH N 6 .   ? 10.70473 30.25406 28.56328 1.000 46.74703 ?  497 HOH A O    1 
HETATM 3012 O  O    . HOH N 6 .   ? 13.65381 34.60286 32.68096 1.000 36.17754 ?  498 HOH A O    1 
HETATM 3013 O  O    . HOH N 6 .   ? 21.54099 25.01848 58.87658 1.000 45.52970 ?  499 HOH A O    1 
HETATM 3014 O  O    . HOH N 6 .   ? 34.842   -5.941   58.782   1.000 37.21554 ?  500 HOH A O    1 
HETATM 3015 O  O    . HOH N 6 .   ? 37.28520 25.58411 45.02711 1.000 35.61928 ?  501 HOH A O    1 
HETATM 3016 O  O    . HOH N 6 .   ? 35.22237 31.55279 26.88498 1.000 32.61561 ?  502 HOH A O    1 
HETATM 3017 O  O    . HOH N 6 .   ? 17.90010 43.91804 34.05237 0.823 36.67655 ?  503 HOH A O    1 
HETATM 3018 O  O    . HOH N 6 .   ? 34.55762 27.31202 26.95863 1.000 36.25508 ?  504 HOH A O    1 
HETATM 3019 O  O    . HOH N 6 .   ? 25.452   43.288   25.755   1.000 32.12204 ?  505 HOH A O    1 
HETATM 3020 O  O    . HOH N 6 .   ? 22.65908 10.49708 54.38086 1.000 35.16599 ?  506 HOH A O    1 
HETATM 3021 O  O    . HOH N 6 .   ? 33.592   14.287   46.808   1.000 39.29741 ?  507 HOH A O    1 
HETATM 3022 O  O    . HOH N 6 .   ? 31.60811 30.09072 21.81494 1.000 42.88728 ?  508 HOH A O    1 
HETATM 3023 O  O    . HOH N 6 .   ? 35.51420 35.07999 29.36338 0.964 36.62845 ?  509 HOH A O    1 
HETATM 3024 O  O    . HOH N 6 .   ? 27.95854 15.41584 39.76835 1.000 32.91379 ?  510 HOH A O    1 
HETATM 3025 O  O    . HOH N 6 .   ? 18.42003 44.61015 38.99155 0.986 50.25336 ?  511 HOH A O    1 
HETATM 3026 O  O    . HOH N 6 .   ? 19.778   40.685   51.517   1.000 30.15382 ?  512 HOH A O    1 
HETATM 3027 O  O    . HOH N 6 .   ? 29.374   46.146   41.836   0.856 33.65234 ?  513 HOH A O    1 
HETATM 3028 O  O    . HOH N 6 .   ? 20.77104 0.90434  50.65554 1.000 29.92741 ?  514 HOH A O    1 
HETATM 3029 O  O    . HOH N 6 .   ? 21.31905 26.92161 56.65281 0.957 26.56517 ?  515 HOH A O    1 
HETATM 3030 O  O    . HOH N 6 .   ? 36.28045 25.48337 26.04840 1.000 44.49767 ?  516 HOH A O    1 
HETATM 3031 O  O    . HOH N 6 .   ? 19.86058 18.83739 54.19170 1.000 23.05590 ?  517 HOH A O    1 
HETATM 3032 O  O    . HOH N 6 .   ? 18.135   3.991    41.648   0.875 35.43944 ?  518 HOH A O    1 
HETATM 3033 O  O    . HOH N 6 .   ? 39.473   34.729   41.313   1.000 46.67992 ?  519 HOH A O    1 
HETATM 3034 O  O    . HOH N 6 .   ? 33.98675 29.39735 25.60034 1.000 28.75778 ?  520 HOH A O    1 
HETATM 3035 O  O    . HOH N 6 .   ? 34.64292 35.26674 40.14829 1.000 34.26939 ?  521 HOH A O    1 
HETATM 3036 O  O    . HOH N 6 .   ? 36.70381 24.69447 21.65352 0.811 42.53152 ?  522 HOH A O    1 
HETATM 3037 O  O    . HOH N 6 .   ? 32.58116 41.95118 35.89207 0.917 40.37338 ?  523 HOH A O    1 
HETATM 3038 O  O    . HOH N 6 .   ? 20.23331 33.33727 57.76141 1.000 52.62197 ?  524 HOH A O    1 
HETATM 3039 O  O    . HOH N 6 .   ? 18.45428 29.54415 54.36903 1.000 27.10665 ?  525 HOH A O    1 
HETATM 3040 O  O    . HOH N 6 .   ? 34.32170 18.00256 55.93196 1.000 27.50032 ?  526 HOH A O    1 
HETATM 3041 O  O    . HOH N 6 .   ? 15.80363 39.33563 32.95229 0.989 33.05740 ?  527 HOH A O    1 
HETATM 3042 O  O    . HOH N 6 .   ? 19.63347 27.07482 54.45394 1.000 21.68723 ?  528 HOH A O    1 
HETATM 3043 O  O    . HOH N 6 .   ? 33.85059 39.25906 36.77165 1.000 41.77941 ?  529 HOH A O    1 
HETATM 3044 O  O    . HOH N 6 .   ? 40.98974 17.21915 46.47337 1.000 28.07730 ?  530 HOH A O    1 
HETATM 3045 O  O    . HOH N 6 .   ? 38.77823 25.20927 47.35250 1.000 25.60313 ?  531 HOH A O    1 
HETATM 3046 O  O    . HOH N 6 .   ? 34.21182 16.58127 58.38064 1.000 43.38178 ?  532 HOH A O    1 
HETATM 3047 O  O    . HOH N 6 .   ? 20.49563 28.83446 58.39544 0.867 32.71258 ?  533 HOH A O    1 
HETATM 3048 O  O    . HOH N 6 .   ? 20.13904 6.52122  53.23518 0.863 36.79347 ?  534 HOH A O    1 
HETATM 3049 O  O    . HOH N 6 .   ? 12.23441 33.41176 32.95205 1.000 44.98832 ?  535 HOH A O    1 
HETATM 3050 O  O    . HOH N 6 .   ? 20.79302 20.69414 58.83157 0.990 32.46297 ?  536 HOH A O    1 
HETATM 3051 O  O    . HOH N 6 .   ? 11.932   27.738   14.705   0.938 36.68554 ?  537 HOH A O    1 
HETATM 3052 O  O    . HOH N 6 .   ? 34.77715 28.20279 63.03095 1.000 49.55761 ?  538 HOH A O    1 
HETATM 3053 O  O    . HOH N 6 .   ? 17.63246 25.27083 54.24952 0.983 30.14657 ?  539 HOH A O    1 
HETATM 3054 O  O    . HOH N 6 .   ? 38.87886 25.60310 42.99024 1.000 50.10929 ?  540 HOH A O    1 
HETATM 3055 O  O    . HOH N 6 .   ? 17.97243 20.68461 55.11043 1.000 31.45354 ?  541 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   . ALA A 2   ? 0.50148 0.34240 0.32671 -0.02151 0.04262  0.08948  2   ALA A N   
2    C  CA  . ALA A 2   ? 0.45521 0.31864 0.31993 0.02819  0.04770  0.09458  2   ALA A CA  
3    C  C   . ALA A 2   ? 0.41045 0.26802 0.29378 0.05594  0.04988  0.08721  2   ALA A C   
4    O  O   . ALA A 2   ? 0.41439 0.32994 0.32748 0.04384  0.04686  0.11216  2   ALA A O   
5    C  CB  . ALA A 2   ? 0.44475 0.32148 0.30911 0.05719  0.03847  0.10734  2   ALA A CB  
10   N  N   . THR A 3   ? 0.40308 0.22997 0.25241 0.09038  0.04574  0.05839  3   THR A N   
11   C  CA  . THR A 3   ? 0.36953 0.20293 0.22138 0.05623  0.00773  0.02842  3   THR A CA  
12   C  C   . THR A 3   ? 0.31847 0.17025 0.20043 0.00720  -0.00779 0.01914  3   THR A C   
13   O  O   . THR A 3   ? 0.32887 0.14582 0.18580 0.00642  -0.02353 0.00887  3   THR A O   
14   C  CB  . THR A 3   ? 0.37780 0.17743 0.21633 0.05811  -0.02119 0.00113  3   THR A CB  
15   O  OG1 . THR A 3   ? 0.39730 0.15117 0.21888 0.04011  -0.05236 -0.01585 3   THR A OG1 
16   C  CG2 . THR A 3   ? 0.39444 0.19263 0.22945 0.06038  -0.00290 0.01554  3   THR A CG2 
24   N  N   . LYS A 4   ? 0.32260 0.18789 0.18840 -0.00092 -0.00653 0.02578  4   LYS A N   
25   C  CA  . LYS A 4   ? 0.35005 0.20863 0.17492 -0.00643 -0.01237 -0.01086 4   LYS A CA  
26   C  C   . LYS A 4   ? 0.34214 0.16406 0.16786 -0.01359 -0.02417 -0.00189 4   LYS A C   
27   O  O   . LYS A 4   ? 0.35983 0.15139 0.17813 -0.01719 -0.01752 0.00548  4   LYS A O   
28   C  CB  . LYS A 4   ? 0.38707 0.25492 0.17452 -0.00375 -0.02171 -0.03686 4   LYS A CB  
29   C  CG  . LYS A 4   ? 0.44133 0.34466 0.18073 0.01595  -0.02880 -0.01061 4   LYS A CG  
30   C  CD  . LYS A 4   ? 0.47562 0.40270 0.18750 0.05098  -0.04190 -0.00993 4   LYS A CD  
31   C  CE  . LYS A 4   ? 0.50468 0.42414 0.19879 0.09846  -0.03854 -0.00961 4   LYS A CE  
32   N  NZ  . LYS A 4   ? 0.51076 0.42663 0.20307 0.13098  -0.02114 -0.01224 4   LYS A NZ  
46   N  N   . GLN A 5   ? 0.33445 0.14604 0.17472 0.01633  -0.02288 -0.00122 5   GLN A N   
47   C  CA  . GLN A 5   ? 0.34411 0.12821 0.18896 -0.00605 -0.01525 0.00767  5   GLN A CA  
48   C  C   . GLN A 5   ? 0.33024 0.11270 0.19178 -0.00583 -0.01519 0.00474  5   GLN A C   
49   O  O   . GLN A 5   ? 0.33658 0.12712 0.20216 -0.00944 -0.02520 0.01280  5   GLN A O   
50   C  CB  . GLN A 5   ? 0.35936 0.11180 0.18944 -0.01044 -0.02690 0.00244  5   GLN A CB  
51   C  CG  . GLN A 5   ? 0.35837 0.12122 0.20912 0.00295  -0.01788 0.01240  5   GLN A CG  
52   C  CD  . GLN A 5   ? 0.36501 0.12147 0.22476 0.00977  -0.01192 0.01448  5   GLN A CD  
53   O  OE1 . GLN A 5   ? 0.39552 0.12937 0.26528 0.00986  0.00502  -0.01665 5   GLN A OE1 
54   N  NE2 . GLN A 5   ? 0.35518 0.11842 0.21428 -0.00615 -0.00032 0.01388  5   GLN A NE2 
63   N  N   . ALA A 6   ? 0.33558 0.11093 0.17772 0.00649  -0.01950 0.02207  6   ALA A N   
64   C  CA  . ALA A 6   ? 0.32410 0.11968 0.17414 -0.00442 -0.02134 -0.00196 6   ALA A CA  
65   C  C   . ALA A 6   ? 0.30913 0.13208 0.18459 -0.01031 -0.02259 0.01140  6   ALA A C   
66   O  O   . ALA A 6   ? 0.32635 0.12321 0.17389 0.01479  -0.02006 0.00432  6   ALA A O   
67   C  CB  . ALA A 6   ? 0.35828 0.13802 0.17658 0.01708  -0.02300 -0.01275 6   ALA A CB  
73   N  N   . HIS A 7   ? 0.30981 0.12148 0.19191 -0.00863 -0.02678 -0.00492 7   HIS A N   
74   C  CA  . HIS A 7   ? 0.31087 0.09918 0.18817 0.00469  -0.01970 0.00122  7   HIS A CA  
75   C  C   . HIS A 7   ? 0.30387 0.10923 0.17681 -0.00163 -0.02089 0.00346  7   HIS A C   
76   O  O   . HIS A 7   ? 0.32655 0.11810 0.17010 0.00363  -0.01033 -0.00160 7   HIS A O   
77   C  CB  . HIS A 7   ? 0.30525 0.12609 0.21394 0.00410  -0.01416 -0.00999 7   HIS A CB  
78   C  CG  . HIS A 7   ? 0.34355 0.16766 0.22528 -0.00294 -0.02043 -0.02639 7   HIS A CG  
79   N  ND1 . HIS A 7   ? 0.37174 0.16392 0.24901 -0.00727 -0.01537 -0.04711 7   HIS A ND1 
80   C  CD2 . HIS A 7   ? 0.38597 0.19152 0.23765 -0.01685 -0.03484 -0.02575 7   HIS A CD2 
81   C  CE1 . HIS A 7   ? 0.38508 0.17684 0.25678 0.01036  -0.03596 -0.06494 7   HIS A CE1 
82   N  NE2 . HIS A 7   ? 0.40272 0.19289 0.25412 -0.01763 -0.04797 -0.03045 7   HIS A NE2 
90   N  N   . LYS A 8   ? 0.30061 0.11312 0.17504 -0.00317 -0.00322 -0.00437 8   LYS A N   
91   C  CA  . LYS A 8   ? 0.31167 0.11805 0.18161 -0.01334 -0.00494 0.00479  8   LYS A CA  
92   C  C   . LYS A 8   ? 0.30913 0.10165 0.17392 0.00499  -0.01584 0.00766  8   LYS A C   
93   O  O   . LYS A 8   ? 0.32314 0.10014 0.17293 0.00995  -0.01618 0.00264  8   LYS A O   
94   C  CB  . LYS A 8   ? 0.33447 0.15270 0.19401 0.00031  0.00635  0.00183  8   LYS A CB  
95   C  CG  . LYS A 8   ? 0.36349 0.17038 0.19767 0.00258  0.02536  0.01911  8   LYS A CG  
96   C  CD  . LYS A 8   ? 0.42386 0.14609 0.21598 0.00052  0.04836  0.03953  8   LYS A CD  
97   C  CE  . LYS A 8   ? 0.48093 0.18878 0.23682 -0.00180 0.06910  0.05536  8   LYS A CE  
98   N  NZ  . LYS A 8   ? 0.51910 0.28664 0.25350 0.05004  0.07027  0.03516  8   LYS A NZ  
112  N  N   . ARG A 9   ? 0.29586 0.11293 0.17168 -0.00374 -0.00152 0.00317  9   ARG A N   
113  C  CA  . ARG A 9   ? 0.28930 0.11840 0.17981 -0.01473 0.00096  0.00193  9   ARG A CA  
114  C  C   . ARG A 9   ? 0.30032 0.10536 0.17866 -0.00513 -0.00093 0.00100  9   ARG A C   
115  O  O   . ARG A 9   ? 0.29443 0.12545 0.17619 -0.00461 -0.00622 -0.00656 9   ARG A O   
116  C  CB  . ARG A 9   ? 0.30202 0.09818 0.18134 0.00844  -0.00542 -0.01031 9   ARG A CB  
117  C  CG  . ARG A 9   ? 0.31414 0.12389 0.18732 0.00931  -0.01043 -0.01972 9   ARG A CG  
118  C  CD  . ARG A 9   ? 0.31039 0.13650 0.19060 -0.00172 -0.00213 -0.00613 9   ARG A CD  
119  N  NE  . ARG A 9   ? 0.29307 0.12125 0.20740 0.00944  0.00247  -0.01720 9   ARG A NE  
120  C  CZ  . ARG A 9   ? 0.31541 0.12194 0.21558 0.01373  -0.01381 -0.02059 9   ARG A CZ  
121  N  NH1 . ARG A 9   ? 0.33955 0.13578 0.23413 -0.01501 -0.02399 -0.01021 9   ARG A NH1 
122  N  NH2 . ARG A 9   ? 0.33178 0.14919 0.22576 -0.01159 -0.02900 -0.03282 9   ARG A NH2 
136  N  N   . LEU A 10  ? 0.29804 0.10101 0.17181 -0.00396 -0.00106 -0.00681 10  LEU A N   
137  C  CA  . LEU A 10  ? 0.30787 0.11121 0.17097 -0.00829 -0.00197 -0.00056 10  LEU A CA  
138  C  C   . LEU A 10  ? 0.30929 0.11874 0.17277 -0.00282 0.00243  0.00223  10  LEU A C   
139  O  O   . LEU A 10  ? 0.30733 0.12633 0.17443 0.01292  -0.01156 0.01345  10  LEU A O   
140  C  CB  . LEU A 10  ? 0.31150 0.12632 0.15934 -0.00630 -0.00002 -0.00290 10  LEU A CB  
141  C  CG  . LEU A 10  ? 0.30465 0.11027 0.16230 -0.00640 0.00508  -0.00356 10  LEU A CG  
142  C  CD1 . LEU A 10  ? 0.33376 0.11868 0.18287 0.01510  0.01281  0.01015  10  LEU A CD1 
143  C  CD2 . LEU A 10  ? 0.31382 0.12737 0.17468 -0.01097 0.00024  -0.00738 10  LEU A CD2 
155  N  N   A THR A 11  ? 0.30141 0.10875 0.17708 -0.00765 -0.01588 -0.00396 11  THR A N   
156  N  N   B THR A 11  ? 0.30166 0.13445 0.17380 -0.00227 -0.01244 0.00277  11  THR A N   
157  C  CA  A THR A 11  ? 0.29447 0.12102 0.19516 -0.00232 -0.00489 -0.01502 11  THR A CA  
158  C  CA  B THR A 11  ? 0.29662 0.15451 0.18205 0.00584  -0.01103 0.00157  11  THR A CA  
159  C  C   A THR A 11  ? 0.29414 0.12654 0.19077 -0.00462 -0.01399 -0.00960 11  THR A C   
160  C  C   B THR A 11  ? 0.29425 0.14729 0.18250 -0.00065 -0.01422 0.00068  11  THR A C   
161  O  O   A THR A 11  ? 0.29686 0.12874 0.19215 0.00792  -0.01408 -0.01294 11  THR A O   
162  O  O   B THR A 11  ? 0.29492 0.15025 0.18285 0.00413  -0.01447 -0.00139 11  THR A O   
163  C  CB  A THR A 11  ? 0.29810 0.15264 0.22093 -0.03491 -0.00110 -0.05276 11  THR A CB  
164  C  CB  B THR A 11  ? 0.30163 0.19857 0.19310 0.00303  -0.01567 -0.01046 11  THR A CB  
165  O  OG1 A THR A 11  ? 0.33771 0.18171 0.24460 -0.01045 -0.01899 -0.06050 11  THR A OG1 
166  O  OG1 B THR A 11  ? 0.30640 0.18828 0.18891 0.03188  -0.02843 0.01012  11  THR A OG1 
167  C  CG2 A THR A 11  ? 0.30790 0.15451 0.22140 -0.03771 0.00420  -0.04170 11  THR A CG2 
168  C  CG2 B THR A 11  ? 0.31352 0.22164 0.20365 0.00472  -0.01902 -0.02027 11  THR A CG2 
183  N  N   . LYS A 12  ? 0.29345 0.13882 0.17902 0.00107  -0.01073 0.00129  12  LYS A N   
184  C  CA  . LYS A 12  ? 0.31124 0.11924 0.18208 -0.00405 -0.00663 -0.00266 12  LYS A CA  
185  C  C   . LYS A 12  ? 0.30135 0.13762 0.17703 0.00365  -0.01444 -0.00951 12  LYS A C   
186  O  O   . LYS A 12  ? 0.29707 0.14708 0.19026 -0.00039 -0.01113 0.00486  12  LYS A O   
187  C  CB  . LYS A 12  ? 0.33006 0.13615 0.21147 -0.00479 -0.00395 0.00293  12  LYS A CB  
188  C  CG  . LYS A 12  ? 0.36382 0.22872 0.24835 -0.03158 -0.00255 0.01911  12  LYS A CG  
189  C  CD  . LYS A 12  ? 0.42113 0.34982 0.28751 -0.05691 -0.00494 0.04735  12  LYS A CD  
190  C  CE  . LYS A 12  ? 0.49052 0.44419 0.31518 -0.07324 -0.00888 0.07847  12  LYS A CE  
191  N  NZ  . LYS A 12  ? 0.54378 0.50917 0.33683 -0.07759 -0.00977 0.08517  12  LYS A NZ  
206  N  N   . GLU A 13  ? 0.30953 0.13846 0.17445 -0.00046 -0.00639 -0.00671 13  GLU A N   
207  C  CA  . GLU A 13  ? 0.31196 0.11366 0.18102 -0.02355 -0.01836 0.00463  13  GLU A CA  
208  C  C   . GLU A 13  ? 0.31114 0.12514 0.19176 -0.00199 -0.02550 -0.00727 13  GLU A C   
209  O  O   . GLU A 13  ? 0.32873 0.15670 0.20516 -0.00947 -0.03899 -0.00341 13  GLU A O   
210  C  CB  . GLU A 13  ? 0.29965 0.12324 0.18108 -0.00128 -0.01992 -0.01073 13  GLU A CB  
211  C  CG  . GLU A 13  ? 0.30598 0.14458 0.18761 0.02024  -0.01523 -0.01262 13  GLU A CG  
212  C  CD  . GLU A 13  ? 0.29866 0.14739 0.19565 -0.00381 -0.00436 -0.00239 13  GLU A CD  
213  O  OE1 . GLU A 13  ? 0.30175 0.14266 0.20440 0.00153  -0.00871 -0.01989 13  GLU A OE1 
214  O  OE2 . GLU A 13  ? 0.32218 0.17616 0.20989 -0.00985 -0.01950 -0.00775 13  GLU A OE2 
221  N  N   . TYR A 14  ? 0.29369 0.11987 0.18531 0.02175  -0.01334 -0.00326 14  TYR A N   
222  C  CA  . TYR A 14  ? 0.28229 0.11841 0.18992 0.02580  -0.01735 0.01252  14  TYR A CA  
223  C  C   . TYR A 14  ? 0.28529 0.09729 0.18757 0.01075  -0.01139 0.00844  14  TYR A C   
224  O  O   . TYR A 14  ? 0.30390 0.13116 0.19220 0.03293  -0.01109 0.00703  14  TYR A O   
225  C  CB  . TYR A 14  ? 0.28387 0.15791 0.18852 0.01825  -0.01838 0.00687  14  TYR A CB  
226  C  CG  . TYR A 14  ? 0.29850 0.15239 0.19002 0.00837  -0.01057 0.01674  14  TYR A CG  
227  C  CD1 . TYR A 14  ? 0.30101 0.17566 0.20167 0.00324  -0.01038 0.01288  14  TYR A CD1 
228  C  CD2 . TYR A 14  ? 0.30903 0.13958 0.19982 -0.01697 -0.01251 0.02076  14  TYR A CD2 
229  C  CE1 . TYR A 14  ? 0.30250 0.18606 0.21121 0.01429  -0.01320 0.01917  14  TYR A CE1 
230  C  CE2 . TYR A 14  ? 0.30312 0.17716 0.20781 -0.01798 -0.01322 0.03391  14  TYR A CE2 
231  C  CZ  . TYR A 14  ? 0.29548 0.16637 0.21405 0.00570  -0.01040 0.04324  14  TYR A CZ  
232  O  OH  . TYR A 14  ? 0.34090 0.16660 0.23385 -0.01673 -0.01110 0.05120  14  TYR A OH  
242  N  N   . LYS A 15  ? 0.28404 0.12118 0.19543 0.00031  -0.01626 -0.00448 15  LYS A N   
243  C  CA  . LYS A 15  ? 0.29419 0.14086 0.21069 0.00147  0.00213  0.01239  15  LYS A CA  
244  C  C   . LYS A 15  ? 0.31229 0.13752 0.21589 0.01008  -0.00486 0.00000  15  LYS A C   
245  O  O   . LYS A 15  ? 0.29926 0.15277 0.22214 -0.00019 0.00287  -0.00250 15  LYS A O   
246  C  CB  . LYS A 15  ? 0.31104 0.19643 0.21930 -0.00532 0.00737  -0.00489 15  LYS A CB  
247  C  CG  . LYS A 15  ? 0.36765 0.27315 0.24162 0.02088  0.02388  -0.00991 15  LYS A CG  
248  C  CD  . LYS A 15  ? 0.43386 0.35359 0.26770 0.06431  0.03317  -0.01316 15  LYS A CD  
249  C  CE  . LYS A 15  ? 0.48691 0.41123 0.29812 0.08232  0.03753  -0.01222 15  LYS A CE  
250  N  NZ  . LYS A 15  ? 0.52397 0.45313 0.32303 0.06090  0.03452  -0.00891 15  LYS A NZ  
264  N  N   . LEU A 16  ? 0.30686 0.13833 0.23059 -0.01169 -0.01466 -0.00002 16  LEU A N   
265  C  CA  . LEU A 16  ? 0.29753 0.13244 0.24743 -0.02852 -0.01241 0.00910  16  LEU A CA  
266  C  C   . LEU A 16  ? 0.29727 0.15426 0.25204 -0.01532 -0.03629 0.00341  16  LEU A C   
267  O  O   . LEU A 16  ? 0.32299 0.18258 0.25590 -0.01762 -0.03542 -0.00959 16  LEU A O   
268  C  CB  . LEU A 16  ? 0.31980 0.17709 0.25789 -0.03571 -0.01670 0.02458  16  LEU A CB  
269  C  CG  . LEU A 16  ? 0.34440 0.18616 0.27535 -0.03607 -0.00720 0.03689  16  LEU A CG  
270  C  CD1 . LEU A 16  ? 0.36761 0.18478 0.28489 -0.04617 -0.00701 0.02243  16  LEU A CD1 
271  C  CD2 . LEU A 16  ? 0.37003 0.25282 0.28430 -0.03190 0.00300  0.04650  16  LEU A CD2 
283  N  N   . MET A 17  ? 0.29541 0.14977 0.25635 -0.01855 -0.03828 0.01589  17  MET A N   
284  C  CA  . MET A 17  ? 0.31961 0.15100 0.26952 0.02070  -0.02476 0.00300  17  MET A CA  
285  C  C   . MET A 17  ? 0.30729 0.12198 0.24114 0.00830  -0.01844 0.00824  17  MET A C   
286  O  O   . MET A 17  ? 0.34443 0.15904 0.23903 0.02575  -0.02439 0.00487  17  MET A O   
287  C  CB  . MET A 17  ? 0.37303 0.14135 0.33038 0.05180  -0.00065 -0.02734 17  MET A CB  
288  C  CG  . MET A 17  ? 0.42470 0.22062 0.40460 0.03832  0.00141  -0.07114 17  MET A CG  
289  S  SD  . MET A 17  ? 0.44382 0.29238 0.49175 0.02448  0.01306  -0.11057 17  MET A SD  
290  C  CE  . MET A 17  ? 0.45672 0.27096 0.48175 -0.02034 -0.01452 -0.15466 17  MET A CE  
300  N  N   . VAL A 18  ? 0.30940 0.11707 0.23005 -0.01107 -0.02233 -0.00207 18  VAL A N   
301  C  CA  . VAL A 18  ? 0.31014 0.14221 0.23668 -0.00364 -0.01216 0.00211  18  VAL A CA  
302  C  C   . VAL A 18  ? 0.31073 0.17525 0.25608 0.02938  -0.00781 -0.01356 18  VAL A C   
303  O  O   . VAL A 18  ? 0.33939 0.17371 0.27312 0.05145  -0.01074 -0.01540 18  VAL A O   
304  C  CB  . VAL A 18  ? 0.32874 0.15507 0.24347 0.00184  -0.02443 -0.00111 18  VAL A CB  
305  C  CG1 . VAL A 18  ? 0.34013 0.15285 0.25204 0.00879  -0.02394 -0.01168 18  VAL A CG1 
306  C  CG2 . VAL A 18  ? 0.31551 0.18030 0.24693 -0.01319 -0.04424 0.00273  18  VAL A CG2 
316  N  N   . GLU A 19  ? 0.30287 0.20352 0.26043 0.02650  0.00026  -0.02191 19  GLU A N   
317  C  CA  . GLU A 19  ? 0.32104 0.26697 0.27743 0.04390  0.00001  -0.03216 19  GLU A CA  
318  C  C   . GLU A 19  ? 0.29792 0.27460 0.28190 0.04414  0.00180  -0.01014 19  GLU A C   
319  O  O   . GLU A 19  ? 0.33114 0.30098 0.29721 0.05156  -0.00130 -0.02803 19  GLU A O   
320  C  CB  . GLU A 19  ? 0.37327 0.37466 0.29080 0.02948  0.00737  -0.05109 19  GLU A CB  
321  C  CG  . GLU A 19  ? 0.46381 0.48730 0.31460 0.01957  0.00776  -0.04943 19  GLU A CG  
322  C  CD  . GLU A 19  ? 0.54689 0.58415 0.33888 -0.00314 0.01692  -0.04790 19  GLU A CD  
323  O  OE1 . GLU A 19  ? 0.57781 0.60068 0.35469 -0.02995 0.03235  -0.03847 19  GLU A OE1 
324  O  OE2 . GLU A 19  ? 0.58109 0.63674 0.34352 0.00542  0.00724  -0.05654 19  GLU A OE2 
331  N  N   . ASN A 20  ? 0.27213 0.25778 0.26993 0.02721  0.01296  0.00478  20  ASN A N   
332  C  CA  . ASN A 20  ? 0.29830 0.29474 0.27572 0.01754  0.01552  0.01967  20  ASN A CA  
333  C  C   . ASN A 20  ? 0.29332 0.28066 0.26247 0.02060  -0.00087 0.01797  20  ASN A C   
334  O  O   . ASN A 20  ? 0.29635 0.28297 0.25699 0.01265  -0.00486 0.00835  20  ASN A O   
335  C  CB  . ASN A 20  ? 0.36225 0.36844 0.28649 -0.00818 0.03011  0.02750  20  ASN A CB  
336  C  CG  . ASN A 20  ? 0.43893 0.44405 0.30366 -0.02030 0.01946  0.03278  20  ASN A CG  
337  O  OD1 . ASN A 20  ? 0.48374 0.48699 0.31178 -0.03807 0.01880  0.03905  20  ASN A OD1 
338  N  ND2 . ASN A 20  ? 0.45192 0.47124 0.31121 -0.02570 0.02580  0.02790  20  ASN A ND2 
345  N  N   . PRO A 21  ? 0.31738 0.26187 0.26736 0.01285  -0.00438 0.01904  21  PRO A N   
346  C  CA  . PRO A 21  ? 0.33176 0.29267 0.26795 0.00793  -0.00532 0.03352  21  PRO A CA  
347  C  C   . PRO A 21  ? 0.33070 0.32372 0.26067 0.00599  -0.00632 0.03467  21  PRO A C   
348  O  O   . PRO A 21  ? 0.33876 0.36229 0.26348 -0.00066 -0.01550 0.02372  21  PRO A O   
349  C  CB  . PRO A 21  ? 0.36611 0.30766 0.28184 0.01374  0.01101  0.03920  21  PRO A CB  
350  C  CG  . PRO A 21  ? 0.39911 0.32068 0.29179 0.01713  0.01583  0.04059  21  PRO A CG  
351  C  CD  . PRO A 21  ? 0.35417 0.28380 0.27558 0.02264  0.00985  0.02934  21  PRO A CD  
359  N  N   . PRO A 22  ? 0.33144 0.32692 0.24438 -0.00064 -0.00230 0.02028  22  PRO A N   
360  C  CA  . PRO A 22  ? 0.33307 0.34535 0.24710 -0.01361 -0.00109 0.01290  22  PRO A CA  
361  C  C   . PRO A 22  ? 0.31174 0.36212 0.22988 -0.01423 0.00079  0.01460  22  PRO A C   
362  O  O   . PRO A 22  ? 0.31409 0.32488 0.21673 -0.02902 -0.01747 0.01184  22  PRO A O   
363  C  CB  . PRO A 22  ? 0.35209 0.32573 0.25633 0.00126  0.00125  0.01179  22  PRO A CB  
364  C  CG  . PRO A 22  ? 0.36702 0.32762 0.25222 0.02205  -0.00989 0.03585  22  PRO A CG  
365  C  CD  . PRO A 22  ? 0.34494 0.32097 0.24745 0.01798  -0.00324 0.03934  22  PRO A CD  
373  N  N   . PRO A 23  ? 0.32667 0.39908 0.23087 -0.01886 0.01516  0.03000  23  PRO A N   
374  C  CA  . PRO A 23  ? 0.31153 0.38520 0.22737 -0.01377 0.00601  0.03159  23  PRO A CA  
375  C  C   . PRO A 23  ? 0.29562 0.31926 0.22015 -0.00158 -0.00487 0.00229  23  PRO A C   
376  O  O   . PRO A 23  ? 0.31658 0.30089 0.22638 -0.01027 -0.02008 0.01157  23  PRO A O   
377  C  CB  . PRO A 23  ? 0.33561 0.44291 0.23677 -0.01453 -0.00088 0.03986  23  PRO A CB  
378  C  CG  . PRO A 23  ? 0.33804 0.46432 0.24749 -0.02717 0.00873  0.03526  23  PRO A CG  
379  C  CD  . PRO A 23  ? 0.33467 0.45297 0.24212 -0.02689 0.00934  0.03481  23  PRO A CD  
387  N  N   . TYR A 24  ? 0.26750 0.22008 0.19769 -0.00290 -0.02272 -0.01197 24  TYR A N   
388  C  CA  . TYR A 24  ? 0.26625 0.18619 0.18808 0.01459  -0.00662 -0.00604 24  TYR A CA  
389  C  C   . TYR A 24  ? 0.27140 0.15508 0.18768 0.01759  0.00126  -0.00255 24  TYR A C   
390  O  O   . TYR A 24  ? 0.29280 0.22257 0.19007 -0.00194 0.00845  0.00301  24  TYR A O   
391  C  CB  . TYR A 24  ? 0.27902 0.20705 0.19464 0.00266  -0.00927 -0.01328 24  TYR A CB  
392  C  CG  . TYR A 24  ? 0.28464 0.24797 0.20659 0.00057  -0.01032 -0.02507 24  TYR A CG  
393  C  CD1 . TYR A 24  ? 0.28416 0.28892 0.21059 0.03099  -0.02490 -0.02293 24  TYR A CD1 
394  C  CD2 . TYR A 24  ? 0.28543 0.30845 0.22755 0.00473  -0.01878 -0.02782 24  TYR A CD2 
395  C  CE1 . TYR A 24  ? 0.29564 0.33646 0.22384 0.03403  -0.02911 -0.02876 24  TYR A CE1 
396  C  CE2 . TYR A 24  ? 0.30200 0.35376 0.24384 -0.02418 -0.02824 -0.02103 24  TYR A CE2 
397  C  CZ  . TYR A 24  ? 0.29261 0.36995 0.23936 0.00046  -0.04335 -0.02922 24  TYR A CZ  
398  O  OH  . TYR A 24  ? 0.32078 0.44008 0.26683 -0.01108 -0.03611 -0.02190 24  TYR A OH  
408  N  N   . ILE A 25  ? 0.27297 0.14368 0.18131 0.02947  0.00209  -0.00805 25  ILE A N   
409  C  CA  . ILE A 25  ? 0.28678 0.16419 0.20196 0.02100  -0.01061 -0.00516 25  ILE A CA  
410  C  C   . ILE A 25  ? 0.28516 0.18950 0.18713 0.01789  -0.00604 -0.01415 25  ILE A C   
411  O  O   . ILE A 25  ? 0.30286 0.22548 0.19831 -0.01289 0.01762  -0.01669 25  ILE A O   
412  C  CB  . ILE A 25  ? 0.31512 0.16031 0.23533 0.01768  -0.04931 0.00327  25  ILE A CB  
413  C  CG1 . ILE A 25  ? 0.32402 0.13307 0.25132 0.00965  -0.04954 -0.02049 25  ILE A CG1 
414  C  CG2 . ILE A 25  ? 0.36550 0.22011 0.26607 0.02923  -0.06802 -0.00235 25  ILE A CG2 
415  C  CD1 . ILE A 25  ? 0.39501 0.16464 0.27691 0.03096  -0.06724 -0.00285 25  ILE A CD1 
427  N  N   . LEU A 26  ? 0.28354 0.17762 0.17735 0.02625  0.00238  -0.02494 26  LEU A N   
428  C  CA  . LEU A 26  ? 0.30107 0.20547 0.18121 0.01748  -0.00201 -0.02905 26  LEU A CA  
429  C  C   . LEU A 26  ? 0.29063 0.18416 0.16732 0.00372  -0.00186 -0.02560 26  LEU A C   
430  O  O   . LEU A 26  ? 0.30238 0.24950 0.16098 0.04011  -0.00126 -0.02790 26  LEU A O   
431  C  CB  . LEU A 26  ? 0.34371 0.19273 0.19941 0.01359  -0.01468 -0.03660 26  LEU A CB  
432  C  CG  . LEU A 26  ? 0.40366 0.22274 0.22208 -0.01763 -0.00306 -0.02702 26  LEU A CG  
433  C  CD1 . LEU A 26  ? 0.42720 0.26772 0.23427 -0.00538 0.00444  -0.01687 26  LEU A CD1 
434  C  CD2 . LEU A 26  ? 0.44881 0.23453 0.23760 -0.04541 -0.00691 -0.02465 26  LEU A CD2 
446  N  N   . ALA A 27  ? 0.29865 0.13281 0.16143 0.00439  -0.00073 -0.02961 27  ALA A N   
447  C  CA  . ALA A 27  ? 0.32084 0.13549 0.16628 -0.01094 -0.00450 -0.01546 27  ALA A CA  
448  C  C   . ALA A 27  ? 0.29186 0.14555 0.16502 0.01392  0.00015  -0.00798 27  ALA A C   
449  O  O   . ALA A 27  ? 0.29712 0.21030 0.17716 0.03843  -0.01483 -0.02800 27  ALA A O   
450  C  CB  . ALA A 27  ? 0.34998 0.11887 0.16909 -0.01181 -0.01010 -0.01897 27  ALA A CB  
456  N  N   . ARG A 28  ? 0.28810 0.13668 0.16241 0.01499  0.00699  -0.01130 28  ARG A N   
457  C  CA  . ARG A 28  ? 0.30973 0.13015 0.17323 0.01407  -0.01224 -0.00931 28  ARG A CA  
458  C  C   . ARG A 28  ? 0.29751 0.12772 0.15752 -0.00262 0.00129  -0.00528 28  ARG A C   
459  O  O   . ARG A 28  ? 0.29672 0.15186 0.15941 0.01546  -0.00540 -0.01194 28  ARG A O   
460  C  CB  . ARG A 28  ? 0.35565 0.12229 0.19182 0.03337  -0.01322 -0.00665 28  ARG A CB  
461  C  CG  . ARG A 28  ? 0.40989 0.11997 0.21357 -0.01548 -0.01846 -0.01072 28  ARG A CG  
462  C  CD  . ARG A 28  ? 0.46970 0.16596 0.23573 0.00898  -0.00497 0.01101  28  ARG A CD  
463  N  NE  . ARG A 28  ? 0.47668 0.22627 0.22054 0.05498  0.04211  0.02866  28  ARG A NE  
464  C  CZ  . ARG A 28  ? 0.45972 0.16126 0.20944 0.04623  0.03303  -0.00560 28  ARG A CZ  
465  N  NH1 . ARG A 28  ? 0.49933 0.17349 0.22025 -0.01676 0.04400  -0.01154 28  ARG A NH1 
466  N  NH2 . ARG A 28  ? 0.46839 0.14442 0.20956 0.03324  0.00985  -0.01776 28  ARG A NH2 
480  N  N   . PRO A 29  ? 0.30461 0.14824 0.15877 0.00134  0.00624  -0.00589 29  PRO A N   
481  C  CA  . PRO A 29  ? 0.28815 0.12542 0.16182 0.01560  -0.00276 -0.01218 29  PRO A CA  
482  C  C   . PRO A 29  ? 0.29437 0.11239 0.17324 0.01327  0.01521  -0.01879 29  PRO A C   
483  O  O   . PRO A 29  ? 0.30837 0.12777 0.18734 0.01934  0.01725  -0.02173 29  PRO A O   
484  C  CB  . PRO A 29  ? 0.32638 0.15528 0.15975 0.02146  -0.00566 -0.00879 29  PRO A CB  
485  C  CG  . PRO A 29  ? 0.33468 0.14263 0.16185 -0.00035 -0.00127 -0.00047 29  PRO A CG  
486  C  CD  . PRO A 29  ? 0.31872 0.14327 0.14634 0.00042  0.00284  -0.01729 29  PRO A CD  
494  N  N   . ASN A 30  ? 0.28635 0.11029 0.19252 0.00787  0.01393  -0.01840 30  ASN A N   
495  C  CA  . ASN A 30  ? 0.28306 0.13647 0.19616 -0.00460 0.01354  -0.02249 30  ASN A CA  
496  C  C   . ASN A 30  ? 0.29834 0.15283 0.21235 -0.01776 0.00752  -0.03172 30  ASN A C   
497  O  O   . ASN A 30  ? 0.30357 0.16429 0.20406 -0.02850 -0.00698 -0.01271 30  ASN A O   
498  C  CB  . ASN A 30  ? 0.29573 0.16357 0.21161 0.01702  0.01518  -0.00520 30  ASN A CB  
499  C  CG  . ASN A 30  ? 0.31690 0.19297 0.21698 0.00890  0.02421  -0.02581 30  ASN A CG  
500  O  OD1 . ASN A 30  ? 0.33297 0.20713 0.23689 -0.03826 0.03554  -0.04037 30  ASN A OD1 
501  N  ND2 . ASN A 30  ? 0.34433 0.19857 0.22221 0.01506  0.02258  -0.01912 30  ASN A ND2 
508  N  N   . GLU A 31  ? 0.31797 0.16171 0.23919 -0.02124 0.00972  -0.06150 31  GLU A N   
509  C  CA  . GLU A 31  ? 0.32334 0.17805 0.28072 -0.02650 0.01837  -0.06336 31  GLU A CA  
510  C  C   . GLU A 31  ? 0.34328 0.21868 0.28288 -0.02975 0.00491  -0.04245 31  GLU A C   
511  O  O   . GLU A 31  ? 0.36639 0.33803 0.28301 -0.02348 0.00469  -0.05523 31  GLU A O   
512  C  CB  . GLU A 31  ? 0.35113 0.18458 0.32848 -0.02197 0.02115  -0.06231 31  GLU A CB  
513  C  CG  . GLU A 31  ? 0.39020 0.20573 0.36941 -0.00595 0.01372  -0.06703 31  GLU A CG  
514  C  CD  . GLU A 31  ? 0.42527 0.29011 0.40454 -0.00030 0.00216  -0.04964 31  GLU A CD  
515  O  OE1 . GLU A 31  ? 0.46552 0.31928 0.42902 0.01021  -0.01177 -0.05765 31  GLU A OE1 
516  O  OE2 . GLU A 31  ? 0.44134 0.30299 0.41431 -0.02171 0.01009  -0.04144 31  GLU A OE2 
523  N  N   . ASP A 32  ? 0.32304 0.16078 0.29769 -0.00720 -0.00248 -0.01519 32  ASP A N   
524  C  CA  . ASP A 32  ? 0.35963 0.22691 0.32416 -0.02436 -0.00291 -0.01357 32  ASP A CA  
525  C  C   . ASP A 32  ? 0.32984 0.20143 0.30102 -0.01550 -0.01728 -0.02088 32  ASP A C   
526  O  O   . ASP A 32  ? 0.33980 0.22700 0.31500 -0.02491 -0.03723 -0.02944 32  ASP A O   
527  C  CB  . ASP A 32  ? 0.44122 0.31555 0.37260 -0.05124 0.01688  -0.00087 32  ASP A CB  
528  C  CG  . ASP A 32  ? 0.54460 0.44888 0.40970 -0.05650 0.03534  0.00809  32  ASP A CG  
529  O  OD1 . ASP A 32  ? 0.57747 0.48236 0.43200 -0.05467 0.03774  0.00184  32  ASP A OD1 
530  O  OD2 . ASP A 32  ? 0.59245 0.49172 0.43213 -0.06103 0.03377  0.01831  32  ASP A OD2 
535  N  N   . ASN A 33  ? 0.30426 0.15524 0.26412 -0.01663 -0.01405 -0.02799 33  ASN A N   
536  C  CA  . ASN A 33  ? 0.30898 0.14208 0.24696 -0.00121 -0.00770 -0.02460 33  ASN A CA  
537  C  C   . ASN A 33  ? 0.29647 0.14426 0.21844 -0.00128 0.00154  -0.02143 33  ASN A C   
538  O  O   . ASN A 33  ? 0.31607 0.14966 0.20598 -0.00573 -0.01069 -0.01838 33  ASN A O   
539  C  CB  . ASN A 33  ? 0.31409 0.15039 0.26821 0.02230  0.00895  -0.02069 33  ASN A CB  
540  C  CG  . ASN A 33  ? 0.33023 0.18754 0.28365 0.03422  0.01261  -0.01871 33  ASN A CG  
541  O  OD1 . ASN A 33  ? 0.33306 0.16818 0.28931 0.00708  0.00463  -0.02675 33  ASN A OD1 
542  N  ND2 . ASN A 33  ? 0.37987 0.20757 0.29709 0.01805  0.02865  -0.01935 33  ASN A ND2 
549  N  N   . ILE A 34  ? 0.32330 0.15202 0.20168 -0.00394 0.00088  0.00304  34  ILE A N   
550  C  CA  . ILE A 34  ? 0.32276 0.13401 0.19592 0.01122  -0.00750 0.00178  34  ILE A CA  
551  C  C   . ILE A 34  ? 0.32104 0.13365 0.18726 0.00432  -0.00802 -0.00956 34  ILE A C   
552  O  O   . ILE A 34  ? 0.31637 0.12318 0.18129 0.00362  -0.01406 -0.01994 34  ILE A O   
553  C  CB  . ILE A 34  ? 0.34459 0.16995 0.20898 0.00366  -0.00099 -0.01197 34  ILE A CB  
554  C  CG1 . ILE A 34  ? 0.36339 0.26191 0.24145 -0.01107 -0.00695 -0.00349 34  ILE A CG1 
555  C  CG2 . ILE A 34  ? 0.37597 0.16793 0.19670 0.00871  0.00711  -0.00081 34  ILE A CG2 
556  C  CD1 . ILE A 34  ? 0.38068 0.26768 0.25412 -0.01193 -0.01258 0.02980  34  ILE A CD1 
568  N  N   . LEU A 35  ? 0.31239 0.11928 0.18887 0.00673  -0.00851 0.00310  35  LEU A N   
569  C  CA  . LEU A 35  ? 0.31598 0.11349 0.18610 -0.00096 -0.00489 -0.00556 35  LEU A CA  
570  C  C   . LEU A 35  ? 0.32298 0.10909 0.18190 -0.01032 0.00117  -0.00868 35  LEU A C   
571  O  O   . LEU A 35  ? 0.37588 0.10702 0.18198 -0.00542 -0.00350 -0.01168 35  LEU A O   
572  C  CB  . LEU A 35  ? 0.30665 0.12903 0.19302 -0.00220 -0.00660 0.00809  35  LEU A CB  
573  C  CG  . LEU A 35  ? 0.31092 0.15242 0.19475 0.02104  -0.00817 -0.00321 35  LEU A CG  
574  C  CD1 . LEU A 35  ? 0.32317 0.15761 0.20441 0.01178  -0.01050 -0.02054 35  LEU A CD1 
575  C  CD2 . LEU A 35  ? 0.32548 0.15003 0.18910 0.03066  -0.00232 0.00162  35  LEU A CD2 
587  N  N   . GLU A 36  ? 0.30804 0.11466 0.18363 0.00207  0.00340  0.00861  36  GLU A N   
588  C  CA  . GLU A 36  ? 0.30592 0.12022 0.19955 -0.00163 -0.01494 0.00366  36  GLU A CA  
589  C  C   . GLU A 36  ? 0.28418 0.10489 0.19104 -0.00207 -0.00934 -0.00506 36  GLU A C   
590  O  O   . GLU A 36  ? 0.31161 0.12385 0.23170 0.00875  -0.03719 -0.03207 36  GLU A O   
591  C  CB  . GLU A 36  ? 0.32609 0.13691 0.21660 0.02999  -0.00918 0.02218  36  GLU A CB  
592  C  CG  . GLU A 36  ? 0.33931 0.15880 0.24009 0.03242  0.01226  0.02540  36  GLU A CG  
593  C  CD  . GLU A 36  ? 0.34786 0.20748 0.27465 0.08026  0.02490  0.05760  36  GLU A CD  
594  O  OE1 . GLU A 36  ? 0.43573 0.24067 0.32797 0.07909  0.07248  0.06489  36  GLU A OE1 
595  O  OE2 . GLU A 36  ? 0.32460 0.20956 0.25812 0.03100  -0.00115 0.01861  36  GLU A OE2 
602  N  N   . TRP A 37  ? 0.29164 0.09846 0.18161 -0.00852 -0.00239 -0.00713 37  TRP A N   
603  C  CA  . TRP A 37  ? 0.29555 0.10322 0.16042 -0.00741 -0.00845 -0.00741 37  TRP A CA  
604  C  C   . TRP A 37  ? 0.29049 0.11989 0.15514 -0.00079 0.00014  -0.00907 37  TRP A C   
605  O  O   . TRP A 37  ? 0.31707 0.12419 0.15472 -0.00331 0.00598  -0.00589 37  TRP A O   
606  C  CB  . TRP A 37  ? 0.29373 0.10999 0.16172 -0.00811 -0.00595 -0.01646 37  TRP A CB  
607  C  CG  . TRP A 37  ? 0.27496 0.12671 0.16259 -0.00071 0.00169  -0.01103 37  TRP A CG  
608  C  CD1 . TRP A 37  ? 0.29166 0.13513 0.17076 0.00605  0.01535  -0.00523 37  TRP A CD1 
609  C  CD2 . TRP A 37  ? 0.28102 0.10614 0.16232 -0.00122 0.01132  -0.00990 37  TRP A CD2 
610  N  NE1 . TRP A 37  ? 0.30417 0.14193 0.16885 0.00805  0.01915  0.00338  37  TRP A NE1 
611  C  CE2 . TRP A 37  ? 0.29694 0.10028 0.16350 0.01868  0.01470  -0.00375 37  TRP A CE2 
612  C  CE3 . TRP A 37  ? 0.28347 0.12677 0.16055 -0.00226 -0.00131 -0.00686 37  TRP A CE3 
613  C  CZ2 . TRP A 37  ? 0.30693 0.13969 0.17453 0.00877  0.01180  -0.00348 37  TRP A CZ2 
614  C  CZ3 . TRP A 37  ? 0.29027 0.14405 0.16384 0.00380  0.00965  -0.01000 37  TRP A CZ3 
615  C  CH2 . TRP A 37  ? 0.28834 0.14460 0.17056 -0.01093 0.02408  -0.01239 37  TRP A CH2 
626  N  N   . HIS A 38  ? 0.30333 0.09896 0.16157 0.00015  0.00508  -0.01684 38  HIS A N   
627  C  CA  . HIS A 38  ? 0.28973 0.09624 0.15863 0.00393  0.00831  0.00585  38  HIS A CA  
628  C  C   . HIS A 38  ? 0.27852 0.10034 0.15104 -0.00014 0.00055  -0.00611 38  HIS A C   
629  O  O   . HIS A 38  ? 0.28991 0.14804 0.15765 0.01123  0.00899  -0.02579 38  HIS A O   
630  C  CB  . HIS A 38  ? 0.29984 0.12526 0.16709 0.00846  -0.00140 0.01926  38  HIS A CB  
631  C  CG  . HIS A 38  ? 0.30107 0.12290 0.17712 0.00813  -0.00164 0.00680  38  HIS A CG  
632  N  ND1 . HIS A 38  ? 0.29114 0.09655 0.18474 -0.00938 -0.00529 0.00115  38  HIS A ND1 
633  C  CD2 . HIS A 38  ? 0.30140 0.12049 0.18266 -0.02504 -0.00151 -0.00315 38  HIS A CD2 
634  C  CE1 . HIS A 38  ? 0.29628 0.13120 0.18787 -0.00472 0.01136  0.00412  38  HIS A CE1 
635  N  NE2 . HIS A 38  ? 0.29577 0.12978 0.19181 -0.02786 -0.00251 0.00643  38  HIS A NE2 
643  N  N   . TYR A 39  ? 0.29354 0.09927 0.15377 -0.00946 -0.00221 -0.00504 39  TYR A N   
644  C  CA  . TYR A 39  ? 0.26962 0.10729 0.15195 -0.00047 -0.00356 -0.00686 39  TYR A CA  
645  C  C   . TYR A 39  ? 0.27046 0.10408 0.15325 -0.01602 0.00766  -0.01008 39  TYR A C   
646  O  O   . TYR A 39  ? 0.27193 0.11384 0.14827 0.00165  0.00005  -0.01166 39  TYR A O   
647  C  CB  . TYR A 39  ? 0.26976 0.09697 0.16535 -0.00681 -0.00651 -0.00665 39  TYR A CB  
648  C  CG  . TYR A 39  ? 0.26338 0.09088 0.15626 -0.02278 0.00660  0.00155  39  TYR A CG  
649  C  CD1 . TYR A 39  ? 0.26288 0.11259 0.15546 -0.00714 0.01696  -0.00799 39  TYR A CD1 
650  C  CD2 . TYR A 39  ? 0.26980 0.10245 0.15839 -0.01266 0.00783  -0.00327 39  TYR A CD2 
651  C  CE1 . TYR A 39  ? 0.26311 0.10918 0.15793 -0.01450 0.00703  0.00173  39  TYR A CE1 
652  C  CE2 . TYR A 39  ? 0.26308 0.10542 0.16266 -0.00311 0.00628  -0.01223 39  TYR A CE2 
653  C  CZ  . TYR A 39  ? 0.27109 0.09760 0.16069 0.00044  -0.00046 -0.00855 39  TYR A CZ  
654  O  OH  . TYR A 39  ? 0.27970 0.11913 0.16222 0.02116  0.00451  -0.01118 39  TYR A OH  
664  N  N   . ILE A 40  ? 0.26291 0.11689 0.15675 0.00242  0.00993  -0.01426 40  ILE A N   
665  C  CA  . ILE A 40  ? 0.27336 0.10672 0.16599 -0.00530 -0.00057 -0.00306 40  ILE A CA  
666  C  C   . ILE A 40  ? 0.27297 0.12985 0.16500 -0.00843 -0.00643 -0.01138 40  ILE A C   
667  O  O   . ILE A 40  ? 0.28318 0.14887 0.17184 0.00672  -0.00731 -0.02164 40  ILE A O   
668  C  CB  . ILE A 40  ? 0.28129 0.09562 0.17841 -0.01430 -0.00298 0.00160  40  ILE A CB  
669  C  CG1 . ILE A 40  ? 0.30122 0.09542 0.19701 -0.01220 -0.01889 0.00671  40  ILE A CG1 
670  C  CG2 . ILE A 40  ? 0.29694 0.11377 0.18306 0.01605  -0.00785 0.00973  40  ILE A CG2 
671  C  CD1 . ILE A 40  ? 0.30885 0.09132 0.21082 -0.00574 -0.01684 0.00523  40  ILE A CD1 
683  N  N   . ILE A 41  ? 0.27865 0.13034 0.16329 -0.00169 0.00071  0.00784  41  ILE A N   
684  C  CA  . ILE A 41  ? 0.26912 0.13460 0.17250 -0.01034 -0.00046 -0.00893 41  ILE A CA  
685  C  C   . ILE A 41  ? 0.25719 0.11982 0.17197 -0.02228 -0.00498 -0.00622 41  ILE A C   
686  O  O   . ILE A 41  ? 0.26520 0.14835 0.16989 -0.00520 0.00882  -0.00395 41  ILE A O   
687  C  CB  . ILE A 41  ? 0.28458 0.15258 0.18884 -0.00664 0.00776  -0.02630 41  ILE A CB  
688  C  CG1 . ILE A 41  ? 0.29917 0.13085 0.21790 -0.00525 -0.00554 -0.01557 41  ILE A CG1 
689  C  CG2 . ILE A 41  ? 0.29266 0.15776 0.19236 -0.01230 -0.00524 -0.02699 41  ILE A CG2 
690  C  CD1 . ILE A 41  ? 0.29098 0.15151 0.23717 0.02013  -0.00754 0.00611  41  ILE A CD1 
702  N  N   . THR A 42  ? 0.25284 0.14895 0.17684 0.01911  0.00004  -0.00266 42  THR A N   
703  C  CA  . THR A 42  ? 0.27530 0.13358 0.18469 0.02291  -0.00915 -0.01176 42  THR A CA  
704  C  C   . THR A 42  ? 0.27481 0.11512 0.17231 -0.01157 -0.00258 -0.00420 42  THR A C   
705  O  O   . THR A 42  ? 0.27815 0.14451 0.17746 -0.01559 0.00175  0.00332  42  THR A O   
706  C  CB  . THR A 42  ? 0.30799 0.16740 0.20319 0.05038  -0.02840 -0.01274 42  THR A CB  
707  O  OG1 . THR A 42  ? 0.34137 0.15728 0.21646 0.04071  -0.04502 -0.01669 42  THR A OG1 
708  C  CG2 . THR A 42  ? 0.31124 0.16711 0.21363 0.04182  -0.03815 -0.00874 42  THR A CG2 
716  N  N   . GLY A 43  ? 0.28007 0.13101 0.17244 -0.01270 0.00097  -0.00378 43  GLY A N   
717  C  CA  . GLY A 43  ? 0.27736 0.16105 0.18113 0.00130  -0.00427 -0.00852 43  GLY A CA  
718  C  C   . GLY A 43  ? 0.26809 0.13537 0.19203 0.00732  -0.02227 -0.00166 43  GLY A C   
719  O  O   . GLY A 43  ? 0.28943 0.13781 0.20470 0.00696  -0.02645 -0.01208 43  GLY A O   
723  N  N   . PRO A 44  ? 0.28920 0.14202 0.19135 0.01217  -0.01725 -0.00078 44  PRO A N   
724  C  CA  . PRO A 44  ? 0.27982 0.14159 0.18411 -0.00783 -0.01916 -0.00848 44  PRO A CA  
725  C  C   . PRO A 44  ? 0.27361 0.11946 0.18788 -0.00456 -0.01583 0.00207  44  PRO A C   
726  O  O   . PRO A 44  ? 0.28250 0.12211 0.18953 0.00519  -0.00723 -0.00523 44  PRO A O   
727  C  CB  . PRO A 44  ? 0.28863 0.14121 0.19262 -0.02756 -0.02200 0.02502  44  PRO A CB  
728  C  CG  . PRO A 44  ? 0.29312 0.14710 0.20118 -0.00221 -0.01802 0.02821  44  PRO A CG  
729  C  CD  . PRO A 44  ? 0.30878 0.15550 0.19712 0.02280  -0.00531 0.01919  44  PRO A CD  
737  N  N   . ALA A 45  ? 0.25224 0.13229 0.19212 -0.01018 -0.01654 -0.01143 45  ALA A N   
738  C  CA  . ALA A 45  ? 0.26189 0.14503 0.20278 -0.00917 -0.02196 -0.01772 45  ALA A CA  
739  C  C   . ALA A 45  ? 0.26340 0.12712 0.19989 -0.02398 -0.01252 -0.00520 45  ALA A C   
740  O  O   . ALA A 45  ? 0.28237 0.14385 0.19214 -0.00317 -0.01799 -0.00116 45  ALA A O   
741  C  CB  . ALA A 45  ? 0.28807 0.15521 0.21767 0.02652  -0.03219 -0.01680 45  ALA A CB  
747  N  N   . ASP A 46  ? 0.27037 0.09518 0.19712 -0.00443 -0.00797 -0.00507 46  ASP A N   
748  C  CA  . ASP A 46  ? 0.26786 0.10489 0.18979 -0.00414 -0.00228 -0.01119 46  ASP A CA  
749  C  C   . ASP A 46  ? 0.26076 0.09451 0.19486 -0.01404 -0.00649 -0.00797 46  ASP A C   
750  O  O   . ASP A 46  ? 0.27880 0.10954 0.20607 0.00442  -0.01620 -0.00274 46  ASP A O   
751  C  CB  . ASP A 46  ? 0.26671 0.11178 0.18233 0.00369  -0.00507 -0.02265 46  ASP A CB  
752  C  CG  . ASP A 46  ? 0.23388 0.12151 0.19114 -0.00606 0.00104  -0.00885 46  ASP A CG  
753  O  OD1 . ASP A 46  ? 0.24618 0.13189 0.19810 -0.00378 0.00404  0.00176  46  ASP A OD1 
754  O  OD2 . ASP A 46  ? 0.20250 0.10228 0.18744 0.01052  -0.04239 0.00652  46  ASP A OD2 
759  N  N   . THR A 47  ? 0.26207 0.10541 0.19573 0.00540  -0.00669 -0.00852 47  THR A N   
760  C  CA  . THR A 47  ? 0.25222 0.13274 0.18847 -0.00004 -0.00929 -0.01273 47  THR A CA  
761  C  C   . THR A 47  ? 0.26274 0.11834 0.18877 0.03132  -0.00782 -0.01945 47  THR A C   
762  O  O   . THR A 47  ? 0.28585 0.11998 0.17868 0.00272  -0.01034 -0.01401 47  THR A O   
763  C  CB  . THR A 47  ? 0.25815 0.13522 0.18905 -0.01383 -0.01835 -0.01997 47  THR A CB  
764  O  OG1 . THR A 47  ? 0.27374 0.12498 0.19222 -0.00720 0.00326  -0.00906 47  THR A OG1 
765  C  CG2 . THR A 47  ? 0.27157 0.15272 0.19619 -0.01363 -0.02458 -0.00329 47  THR A CG2 
773  N  N   . PRO A 48  ? 0.26675 0.12905 0.19675 -0.00025 -0.00908 -0.02482 48  PRO A N   
774  C  CA  . PRO A 48  ? 0.28651 0.14765 0.19643 0.00174  -0.00040 -0.02439 48  PRO A CA  
775  C  C   . PRO A 48  ? 0.27056 0.12411 0.18683 0.00143  -0.00421 -0.00857 48  PRO A C   
776  O  O   . PRO A 48  ? 0.27176 0.16400 0.19002 -0.00235 0.00345  0.00797  48  PRO A O   
777  C  CB  . PRO A 48  ? 0.31101 0.18016 0.20907 0.00748  -0.00111 -0.03536 48  PRO A CB  
778  C  CG  . PRO A 48  ? 0.34531 0.16482 0.21764 0.03002  0.01509  -0.02801 48  PRO A CG  
779  C  CD  . PRO A 48  ? 0.30560 0.12705 0.20222 -0.00713 -0.00274 -0.01567 48  PRO A CD  
787  N  N   . TYR A 49  ? 0.27894 0.11600 0.18046 0.00094  -0.01479 -0.00715 49  TYR A N   
788  C  CA  . TYR A 49  ? 0.26643 0.08764 0.18578 -0.00212 -0.00702 -0.01021 49  TYR A CA  
789  C  C   . TYR A 49  ? 0.26574 0.09468 0.19014 -0.01383 -0.00497 -0.00948 49  TYR A C   
790  O  O   . TYR A 49  ? 0.27026 0.11347 0.17857 -0.00289 -0.01155 -0.00730 49  TYR A O   
791  C  CB  . TYR A 49  ? 0.25266 0.10758 0.18196 0.00267  -0.02421 0.00111  49  TYR A CB  
792  C  CG  . TYR A 49  ? 0.26797 0.10280 0.18172 0.00622  -0.02751 0.00989  49  TYR A CG  
793  C  CD1 . TYR A 49  ? 0.27213 0.11819 0.17825 -0.00156 -0.01583 0.01830  49  TYR A CD1 
794  C  CD2 . TYR A 49  ? 0.26230 0.11456 0.18660 0.00014  -0.02448 0.01474  49  TYR A CD2 
795  C  CE1 . TYR A 49  ? 0.27375 0.11935 0.18546 0.00921  0.00296  0.01546  49  TYR A CE1 
796  C  CE2 . TYR A 49  ? 0.27066 0.11153 0.19043 -0.00101 -0.00528 0.01042  49  TYR A CE2 
797  C  CZ  . TYR A 49  ? 0.28512 0.10369 0.18934 0.01512  0.00264  -0.01929 49  TYR A CZ  
798  O  OH  . TYR A 49  ? 0.30443 0.10879 0.20273 -0.00034 0.01151  -0.00502 49  TYR A OH  
808  N  N   . LYS A 50  ? 0.26029 0.10734 0.19652 0.01273  -0.00602 0.00292  50  LYS A N   
809  C  CA  . LYS A 50  ? 0.26606 0.10014 0.22443 -0.00015 -0.01034 -0.00972 50  LYS A CA  
810  C  C   . LYS A 50  ? 0.28435 0.11704 0.24320 0.01518  -0.01584 -0.02742 50  LYS A C   
811  O  O   . LYS A 50  ? 0.29538 0.12457 0.25429 -0.00050 -0.01703 0.00489  50  LYS A O   
812  C  CB  . LYS A 50  ? 0.25470 0.10350 0.23736 0.02246  0.00566  0.00034  50  LYS A CB  
813  C  CG  . LYS A 50  ? 0.28400 0.09260 0.25977 0.02941  -0.00588 0.01747  50  LYS A CG  
814  C  CD  . LYS A 50  ? 0.27779 0.12906 0.28631 0.03828  -0.01463 0.00268  50  LYS A CD  
815  C  CE  . LYS A 50  ? 0.30057 0.17587 0.30826 0.06496  -0.03290 -0.00117 50  LYS A CE  
816  N  NZ  . LYS A 50  ? 0.31309 0.22526 0.32083 0.06590  -0.01877 -0.02905 50  LYS A NZ  
830  N  N   . GLY A 51  ? 0.29487 0.15111 0.26182 0.01172  -0.02089 -0.04396 51  GLY A N   
831  C  CA  . GLY A 51  ? 0.29635 0.15135 0.27212 -0.00464 -0.03739 -0.04992 51  GLY A CA  
832  C  C   . GLY A 51  ? 0.28614 0.12254 0.27243 0.00963  -0.03789 -0.03400 51  GLY A C   
833  O  O   . GLY A 51  ? 0.30146 0.15712 0.31247 0.00061  -0.05901 -0.04772 51  GLY A O   
837  N  N   . GLY A 52  ? 0.29500 0.11651 0.23587 0.02242  -0.02515 -0.02696 52  GLY A N   
838  C  CA  . GLY A 52  ? 0.28534 0.11943 0.20357 0.02245  -0.01844 -0.03227 52  GLY A CA  
839  C  C   . GLY A 52  ? 0.27873 0.10176 0.18403 -0.01122 -0.00538 -0.01704 52  GLY A C   
840  O  O   . GLY A 52  ? 0.28408 0.15075 0.19417 -0.02965 -0.00323 -0.01321 52  GLY A O   
844  N  N   . GLN A 53  ? 0.27240 0.09965 0.16643 0.00099  -0.00073 0.00104  53  GLN A N   
845  C  CA  . GLN A 53  ? 0.25844 0.10849 0.16344 -0.00500 -0.00468 -0.00911 53  GLN A CA  
846  C  C   . GLN A 53  ? 0.28194 0.10499 0.15256 -0.00584 -0.00781 -0.00423 53  GLN A C   
847  O  O   . GLN A 53  ? 0.27571 0.10564 0.17624 -0.01938 0.00024  0.00022  53  GLN A O   
848  C  CB  . GLN A 53  ? 0.26688 0.08748 0.18212 -0.02254 -0.01301 -0.00627 53  GLN A CB  
849  C  CG  . GLN A 53  ? 0.29531 0.10074 0.18075 -0.00676 -0.01719 0.00342  53  GLN A CG  
850  C  CD  . GLN A 53  ? 0.29169 0.10631 0.18682 0.00058  -0.01812 -0.00591 53  GLN A CD  
851  O  OE1 . GLN A 53  ? 0.28050 0.10465 0.20041 -0.00178 -0.02482 0.00519  53  GLN A OE1 
852  N  NE2 . GLN A 53  ? 0.31769 0.10563 0.20377 -0.01043 0.00869  -0.00279 53  GLN A NE2 
861  N  N   . TYR A 54  ? 0.28183 0.10865 0.14645 0.01352  0.00600  -0.00453 54  TYR A N   
862  C  CA  . TYR A 54  ? 0.26597 0.09952 0.16245 -0.01381 0.00125  -0.00023 54  TYR A CA  
863  C  C   . TYR A 54  ? 0.26153 0.08667 0.15790 0.01385  0.00510  -0.00669 54  TYR A C   
864  O  O   . TYR A 54  ? 0.27906 0.09878 0.16574 -0.00512 0.01031  -0.00953 54  TYR A O   
865  C  CB  . TYR A 54  ? 0.28790 0.12234 0.16646 -0.00160 -0.01064 -0.00696 54  TYR A CB  
866  C  CG  . TYR A 54  ? 0.28295 0.09759 0.16007 0.00384  -0.00792 -0.00713 54  TYR A CG  
867  C  CD1 . TYR A 54  ? 0.28008 0.09358 0.16687 0.02398  -0.00418 -0.00953 54  TYR A CD1 
868  C  CD2 . TYR A 54  ? 0.28478 0.12325 0.16336 -0.01807 -0.00986 -0.00170 54  TYR A CD2 
869  C  CE1 . TYR A 54  ? 0.28792 0.11863 0.16744 0.00731  -0.00469 -0.01503 54  TYR A CE1 
870  C  CE2 . TYR A 54  ? 0.27095 0.11921 0.16943 -0.01031 -0.00956 0.00590  54  TYR A CE2 
871  C  CZ  . TYR A 54  ? 0.28108 0.10790 0.17047 -0.00214 -0.01089 -0.00165 54  TYR A CZ  
872  O  OH  . TYR A 54  ? 0.26024 0.12470 0.18134 0.00831  -0.00509 0.00384  54  TYR A OH  
882  N  N   . HIS A 55  ? 0.25827 0.10348 0.15369 -0.00373 -0.00458 0.00338  55  HIS A N   
883  C  CA  . HIS A 55  ? 0.26399 0.09043 0.15744 -0.01808 -0.00117 0.00190  55  HIS A CA  
884  C  C   . HIS A 55  ? 0.26840 0.08598 0.16308 -0.02028 0.01369  0.01002  55  HIS A C   
885  O  O   . HIS A 55  ? 0.26314 0.10570 0.16167 0.00428  0.01195  0.00754  55  HIS A O   
886  C  CB  . HIS A 55  ? 0.27152 0.08675 0.17394 -0.00951 0.00049  -0.01522 55  HIS A CB  
887  C  CG  . HIS A 55  ? 0.25946 0.09395 0.17910 -0.00974 -0.00201 -0.00965 55  HIS A CG  
888  N  ND1 . HIS A 55  ? 0.25977 0.12334 0.18494 -0.00337 0.00462  0.00551  55  HIS A ND1 
889  C  CD2 . HIS A 55  ? 0.27306 0.10187 0.18368 -0.00563 0.02423  0.00695  55  HIS A CD2 
890  C  CE1 . HIS A 55  ? 0.24177 0.13948 0.18053 -0.01046 -0.01141 0.00868  55  HIS A CE1 
891  N  NE2 . HIS A 55  ? 0.27562 0.12329 0.18027 0.00355  0.00106  -0.00820 55  HIS A NE2 
899  N  N   . GLY A 56  ? 0.27014 0.08067 0.16619 0.00039  0.02424  0.00266  56  GLY A N   
900  C  CA  . GLY A 56  ? 0.27536 0.08750 0.16676 -0.00634 -0.00646 -0.00472 56  GLY A CA  
901  C  C   . GLY A 56  ? 0.27088 0.09090 0.16577 0.00087  0.00562  -0.01018 56  GLY A C   
902  O  O   . GLY A 56  ? 0.28152 0.08248 0.17233 0.00651  0.00144  -0.01042 56  GLY A O   
906  N  N   . THR A 57  ? 0.29232 0.08958 0.16973 0.00975  0.00511  -0.01417 57  THR A N   
907  C  CA  . THR A 57  ? 0.28114 0.08198 0.16917 0.02363  0.00114  0.00644  57  THR A CA  
908  C  C   . THR A 57  ? 0.29324 0.08664 0.16323 0.02496  -0.00080 -0.01833 57  THR A C   
909  O  O   . THR A 57  ? 0.29861 0.08856 0.15530 0.00152  -0.00278 -0.00911 57  THR A O   
910  C  CB  . THR A 57  ? 0.30170 0.10825 0.18205 -0.01454 -0.01497 0.00884  57  THR A CB  
911  O  OG1 . THR A 57  ? 0.29740 0.11164 0.19124 0.00407  -0.00492 -0.00714 57  THR A OG1 
912  C  CG2 . THR A 57  ? 0.32266 0.10894 0.20911 -0.01556 -0.00487 0.00585  57  THR A CG2 
920  N  N   . LEU A 58  ? 0.30566 0.09588 0.15706 0.01333  -0.00041 -0.00574 58  LEU A N   
921  C  CA  . LEU A 58  ? 0.30480 0.10881 0.16826 -0.01800 0.00236  0.00525  58  LEU A CA  
922  C  C   . LEU A 58  ? 0.32160 0.09012 0.16497 -0.02615 -0.01814 -0.00270 58  LEU A C   
923  O  O   . LEU A 58  ? 0.37201 0.10749 0.18851 0.00393  -0.05308 -0.01992 58  LEU A O   
924  C  CB  . LEU A 58  ? 0.34537 0.15347 0.19450 -0.01125 0.01188  -0.04030 58  LEU A CB  
925  C  CG  . LEU A 58  ? 0.34885 0.20973 0.21420 0.01157  0.02288  -0.02603 58  LEU A CG  
926  C  CD1 . LEU A 58  ? 0.34556 0.21252 0.22262 0.01583  0.03333  -0.00230 58  LEU A CD1 
927  C  CD2 . LEU A 58  ? 0.35098 0.25717 0.23470 -0.00030 0.02261  -0.04001 58  LEU A CD2 
939  N  N   . THR A 59  ? 0.30719 0.10136 0.17429 0.00200  -0.01206 0.00392  59  THR A N   
940  C  CA  . THR A 59  ? 0.30072 0.10222 0.18059 -0.00890 -0.01606 0.01122  59  THR A CA  
941  C  C   . THR A 59  ? 0.29951 0.13048 0.17784 -0.01025 -0.01866 0.01672  59  THR A C   
942  O  O   . THR A 59  ? 0.30885 0.10541 0.17005 -0.01167 -0.00907 0.00298  59  THR A O   
943  C  CB  . THR A 59  ? 0.29255 0.12978 0.19342 -0.00784 -0.00603 0.01710  59  THR A CB  
944  O  OG1 . THR A 59  ? 0.30800 0.13491 0.20746 -0.01438 -0.00087 0.00604  59  THR A OG1 
945  C  CG2 . THR A 59  ? 0.29741 0.17881 0.20118 -0.02223 0.00532  0.00888  59  THR A CG2 
953  N  N   . PHE A 60  ? 0.30968 0.13467 0.16698 -0.00181 -0.00865 0.01540  60  PHE A N   
954  C  CA  . PHE A 60  ? 0.31281 0.10860 0.17125 0.00351  -0.01195 0.00633  60  PHE A CA  
955  C  C   . PHE A 60  ? 0.30972 0.10588 0.18339 0.00676  -0.01329 0.01232  60  PHE A C   
956  O  O   . PHE A 60  ? 0.30630 0.12305 0.20205 0.00033  -0.01363 0.01931  60  PHE A O   
957  C  CB  . PHE A 60  ? 0.32140 0.11361 0.16698 0.00009  -0.00934 0.01901  60  PHE A CB  
958  C  CG  . PHE A 60  ? 0.31248 0.13041 0.16630 0.01535  -0.01150 0.01171  60  PHE A CG  
959  C  CD1 . PHE A 60  ? 0.32373 0.14130 0.18088 -0.00927 0.00473  0.01423  60  PHE A CD1 
960  C  CD2 . PHE A 60  ? 0.32098 0.12360 0.16793 0.02050  -0.01534 0.00518  60  PHE A CD2 
961  C  CE1 . PHE A 60  ? 0.32016 0.16289 0.17832 -0.01350 0.02042  0.01978  60  PHE A CE1 
962  C  CE2 . PHE A 60  ? 0.33149 0.12776 0.17590 0.02357  0.00386  0.01790  60  PHE A CE2 
963  C  CZ  . PHE A 60  ? 0.31536 0.18374 0.17568 -0.00267 0.02372  0.02788  60  PHE A CZ  
973  N  N   . PRO A 61  ? 0.30973 0.09853 0.18316 0.00960  -0.02152 0.00702  61  PRO A N   
974  C  CA  . PRO A 61  ? 0.30960 0.11464 0.18615 0.01536  -0.00917 0.00466  61  PRO A CA  
975  C  C   . PRO A 61  ? 0.30578 0.12706 0.19210 -0.00507 -0.01517 0.02762  61  PRO A C   
976  O  O   . PRO A 61  ? 0.29788 0.10475 0.18533 -0.01920 -0.01731 0.00753  61  PRO A O   
977  C  CB  . PRO A 61  ? 0.34290 0.11678 0.20023 0.01334  -0.01064 0.00843  61  PRO A CB  
978  C  CG  . PRO A 61  ? 0.34435 0.12337 0.19372 -0.00609 -0.01983 0.01176  61  PRO A CG  
979  C  CD  . PRO A 61  ? 0.33047 0.11918 0.19267 -0.00785 -0.01593 0.01375  61  PRO A CD  
987  N  N   . SER A 62  ? 0.31359 0.15040 0.21057 -0.01473 -0.02322 0.02544  62  SER A N   
988  C  CA  . SER A 62  ? 0.33785 0.17976 0.22015 -0.01161 -0.04246 0.04277  62  SER A CA  
989  C  C   . SER A 62  ? 0.33235 0.15016 0.19388 -0.00256 -0.03664 0.03060  62  SER A C   
990  O  O   . SER A 62  ? 0.37803 0.15281 0.19618 -0.03395 -0.04843 0.02264  62  SER A O   
991  C  CB  . SER A 62  ? 0.37753 0.26204 0.26008 -0.00222 -0.04360 0.04567  62  SER A CB  
992  O  OG  . SER A 62  ? 0.41544 0.32915 0.28325 0.04837  -0.03101 0.04842  62  SER A OG  
998  N  N   . ASP A 63  ? 0.29689 0.13352 0.18190 -0.00254 -0.00309 0.01838  63  ASP A N   
999  C  CA  . ASP A 63  ? 0.30328 0.12063 0.17264 -0.00045 -0.00825 0.01048  63  ASP A CA  
1000 C  C   . ASP A 63  ? 0.29569 0.11376 0.17384 0.00592  -0.00522 0.01093  63  ASP A C   
1001 O  O   . ASP A 63  ? 0.30547 0.11893 0.17381 -0.00112 -0.00332 0.01527  63  ASP A O   
1002 C  CB  . ASP A 63  ? 0.31933 0.12448 0.18896 0.01083  -0.01068 -0.00327 63  ASP A CB  
1003 C  CG  . ASP A 63  ? 0.36315 0.12305 0.20999 0.02381  -0.01248 -0.00387 63  ASP A CG  
1004 O  OD1 . ASP A 63  ? 0.38862 0.11328 0.21180 0.00670  -0.01736 0.00392  63  ASP A OD1 
1005 O  OD2 . ASP A 63  ? 0.35357 0.13613 0.21387 0.02508  -0.01176 -0.00967 63  ASP A OD2 
1010 N  N   . TYR A 64  ? 0.29777 0.12504 0.17252 0.00462  -0.01528 0.02060  64  TYR A N   
1011 C  CA  . TYR A 64  ? 0.31085 0.11304 0.17154 -0.00433 -0.01257 0.01359  64  TYR A CA  
1012 C  C   . TYR A 64  ? 0.31253 0.12451 0.17375 0.00215  -0.00888 -0.00388 64  TYR A C   
1013 O  O   . TYR A 64  ? 0.31747 0.13720 0.17253 -0.01210 -0.00886 -0.00900 64  TYR A O   
1014 C  CB  . TYR A 64  ? 0.32320 0.11586 0.15938 0.00706  -0.00231 0.01293  64  TYR A CB  
1015 C  CG  . TYR A 64  ? 0.28661 0.10343 0.15797 0.00853  -0.00052 0.00412  64  TYR A CG  
1016 C  CD1 . TYR A 64  ? 0.30456 0.12250 0.16913 -0.01290 -0.00095 0.01102  64  TYR A CD1 
1017 C  CD2 . TYR A 64  ? 0.28669 0.12473 0.16634 -0.00835 0.00572  0.00075  64  TYR A CD2 
1018 C  CE1 . TYR A 64  ? 0.28973 0.12411 0.17523 0.00547  0.00176  0.02001  64  TYR A CE1 
1019 C  CE2 . TYR A 64  ? 0.28250 0.15351 0.17505 -0.01003 0.00842  0.00400  64  TYR A CE2 
1020 C  CZ  . TYR A 64  ? 0.28431 0.14629 0.18762 -0.00602 -0.00065 0.01305  64  TYR A CZ  
1021 O  OH  . TYR A 64  ? 0.30419 0.14655 0.20212 -0.00316 -0.00474 0.00737  64  TYR A OH  
1031 N  N   . PRO A 65  ? 0.31028 0.11975 0.16142 -0.01282 0.00589  -0.00519 65  PRO A N   
1032 C  CA  . PRO A 65  ? 0.30267 0.12255 0.16502 -0.01870 0.00193  0.00244  65  PRO A CA  
1033 C  C   . PRO A 65  ? 0.31129 0.12797 0.16533 -0.00409 0.00092  -0.00030 65  PRO A C   
1034 O  O   . PRO A 65  ? 0.33544 0.13679 0.16924 -0.00668 -0.00353 -0.00580 65  PRO A O   
1035 C  CB  . PRO A 65  ? 0.32125 0.14793 0.17181 0.00659  0.00597  0.00578  65  PRO A CB  
1036 C  CG  . PRO A 65  ? 0.32764 0.14091 0.16116 -0.01337 0.01786  0.01180  65  PRO A CG  
1037 C  CD  . PRO A 65  ? 0.32615 0.14114 0.16049 -0.00961 -0.00514 0.00796  65  PRO A CD  
1045 N  N   . TYR A 66  ? 0.30782 0.10994 0.16759 -0.01133 -0.00409 0.01256  66  TYR A N   
1046 C  CA  . TYR A 66  ? 0.30397 0.11708 0.16223 -0.02390 -0.01147 0.01982  66  TYR A CA  
1047 C  C   . TYR A 66  ? 0.33812 0.11075 0.16556 -0.00406 -0.00908 0.01614  66  TYR A C   
1048 O  O   . TYR A 66  ? 0.39821 0.13769 0.18003 -0.02142 0.01024  0.00482  66  TYR A O   
1049 C  CB  . TYR A 66  ? 0.30496 0.12336 0.16913 0.01307  -0.00655 0.00896  66  TYR A CB  
1050 C  CG  . TYR A 66  ? 0.29644 0.12031 0.16854 0.00425  -0.01573 0.02074  66  TYR A CG  
1051 C  CD1 . TYR A 66  ? 0.30947 0.13606 0.17439 -0.00265 -0.03166 0.01911  66  TYR A CD1 
1052 C  CD2 . TYR A 66  ? 0.29006 0.13326 0.16435 -0.00932 -0.00808 0.01894  66  TYR A CD2 
1053 C  CE1 . TYR A 66  ? 0.31197 0.13315 0.17604 -0.02103 -0.02435 0.01444  66  TYR A CE1 
1054 C  CE2 . TYR A 66  ? 0.31425 0.12617 0.17159 -0.02664 -0.00932 0.02715  66  TYR A CE2 
1055 C  CZ  . TYR A 66  ? 0.31841 0.10745 0.17251 -0.01807 -0.01015 0.01428  66  TYR A CZ  
1056 O  OH  . TYR A 66  ? 0.35747 0.12558 0.17022 -0.02892 0.00493  0.00751  66  TYR A OH  
1066 N  N   . LYS A 67  ? 0.33383 0.12149 0.16501 -0.00970 -0.00800 0.01697  67  LYS A N   
1067 C  CA  . LYS A 67  ? 0.33152 0.12239 0.17779 -0.00636 0.00818  0.00957  67  LYS A CA  
1068 C  C   . LYS A 67  ? 0.33613 0.10676 0.16432 -0.00229 0.01174  -0.00731 67  LYS A C   
1069 O  O   . LYS A 67  ? 0.35949 0.12100 0.16084 -0.00402 0.00443  -0.01127 67  LYS A O   
1070 C  CB  . LYS A 67  ? 0.36584 0.15003 0.20464 -0.00193 0.01833  0.00790  67  LYS A CB  
1071 C  CG  . LYS A 67  ? 0.39494 0.18551 0.22441 0.01286  -0.00296 -0.01310 67  LYS A CG  
1072 C  CD  . LYS A 67  ? 0.38443 0.19005 0.24480 0.00708  -0.00375 -0.02387 67  LYS A CD  
1073 C  CE  . LYS A 67  ? 0.39005 0.20632 0.25823 0.01063  -0.01077 -0.02452 67  LYS A CE  
1074 N  NZ  . LYS A 67  ? 0.36954 0.19295 0.26454 -0.00710 -0.01141 -0.02367 67  LYS A NZ  
1088 N  N   . PRO A 68  ? 0.33583 0.10741 0.15852 -0.00748 0.00671  -0.00046 68  PRO A N   
1089 C  CA  . PRO A 68  ? 0.31707 0.09866 0.15766 -0.00429 0.01120  -0.00133 68  PRO A CA  
1090 C  C   . PRO A 68  ? 0.30225 0.09726 0.16062 -0.00660 0.00489  0.00766  68  PRO A C   
1091 O  O   . PRO A 68  ? 0.31052 0.10991 0.16527 -0.00114 -0.00681 -0.00291 68  PRO A O   
1092 C  CB  . PRO A 68  ? 0.31749 0.10019 0.16024 -0.00701 0.01350  0.00435  68  PRO A CB  
1093 C  CG  . PRO A 68  ? 0.33518 0.09959 0.16417 -0.00286 0.00454  0.00134  68  PRO A CG  
1094 C  CD  . PRO A 68  ? 0.34422 0.11143 0.16931 0.01251  0.00418  -0.00019 68  PRO A CD  
1102 N  N   . PRO A 69  ? 0.31124 0.09728 0.17753 -0.00811 -0.00127 0.01476  69  PRO A N   
1103 C  CA  . PRO A 69  ? 0.29998 0.08963 0.17113 -0.00655 -0.00749 0.02838  69  PRO A CA  
1104 C  C   . PRO A 69  ? 0.29187 0.09560 0.17030 -0.00598 -0.00902 0.01491  69  PRO A C   
1105 O  O   . PRO A 69  ? 0.30644 0.09391 0.18142 -0.01394 -0.00449 -0.00142 69  PRO A O   
1106 C  CB  . PRO A 69  ? 0.30685 0.09251 0.18735 -0.02518 -0.00534 0.01098  69  PRO A CB  
1107 C  CG  . PRO A 69  ? 0.31878 0.11186 0.18859 -0.00682 -0.00983 0.02294  69  PRO A CG  
1108 C  CD  . PRO A 69  ? 0.32413 0.11074 0.18810 -0.01161 -0.00783 0.00785  69  PRO A CD  
1116 N  N   . ALA A 70  ? 0.27727 0.10230 0.15909 0.00497  -0.01731 0.01304  70  ALA A N   
1117 C  CA  . ALA A 70  ? 0.29290 0.10953 0.16162 -0.00640 -0.00797 0.00431  70  ALA A CA  
1118 C  C   . ALA A 70  ? 0.28965 0.11245 0.15419 -0.01764 -0.00643 -0.00137 70  ALA A C   
1119 O  O   . ALA A 70  ? 0.30964 0.10675 0.16457 -0.00157 -0.02202 0.00238  70  ALA A O   
1120 C  CB  . ALA A 70  ? 0.30394 0.13884 0.16714 -0.00656 0.00103  -0.01382 70  ALA A CB  
1126 N  N   . ILE A 71  ? 0.29276 0.09181 0.16033 -0.01041 0.00109  -0.02060 71  ILE A N   
1127 C  CA  . ILE A 71  ? 0.28793 0.11059 0.16031 0.00200  0.00283  0.00720  71  ILE A CA  
1128 C  C   . ILE A 71  ? 0.27333 0.09399 0.15188 0.00267  0.00107  -0.00612 71  ILE A C   
1129 O  O   . ILE A 71  ? 0.28867 0.09859 0.15194 0.00492  -0.00012 0.00091  71  ILE A O   
1130 C  CB  . ILE A 71  ? 0.28911 0.11113 0.17082 -0.01757 0.01173  0.00790  71  ILE A CB  
1131 C  CG1 . ILE A 71  ? 0.26802 0.17993 0.17814 -0.00893 0.01679  0.01600  71  ILE A CG1 
1132 C  CG2 . ILE A 71  ? 0.29031 0.12551 0.16923 0.00500  0.02250  0.00820  71  ILE A CG2 
1133 C  CD1 . ILE A 71  ? 0.30299 0.16883 0.19517 -0.02792 0.02036  0.01568  71  ILE A CD1 
1145 N  N   . ARG A 72  ? 0.28049 0.08058 0.14961 0.00366  -0.00254 0.00140  72  ARG A N   
1146 C  CA  . ARG A 72  ? 0.28305 0.10587 0.15857 -0.00641 0.00607  0.00868  72  ARG A CA  
1147 C  C   . ARG A 72  ? 0.26855 0.10212 0.15466 -0.00564 0.00432  -0.00419 72  ARG A C   
1148 O  O   . ARG A 72  ? 0.29093 0.10813 0.15554 0.00346  0.00342  -0.01517 72  ARG A O   
1149 C  CB  . ARG A 72  ? 0.28504 0.11902 0.15681 -0.00484 0.00134  0.00618  72  ARG A CB  
1150 C  CG  . ARG A 72  ? 0.25570 0.10940 0.16341 0.00955  -0.01016 0.01090  72  ARG A CG  
1151 C  CD  . ARG A 72  ? 0.28066 0.13218 0.17586 0.02063  -0.01743 0.01417  72  ARG A CD  
1152 N  NE  . ARG A 72  ? 0.25901 0.13249 0.18506 0.00860  -0.01691 0.00129  72  ARG A NE  
1153 C  CZ  . ARG A 72  ? 0.28648 0.12325 0.18576 -0.00346 -0.01890 -0.00925 72  ARG A CZ  
1154 N  NH1 . ARG A 72  ? 0.31256 0.16538 0.17700 -0.01524 -0.01047 -0.01163 72  ARG A NH1 
1155 N  NH2 . ARG A 72  ? 0.28730 0.12629 0.19370 0.00397  -0.01462 0.00282  72  ARG A NH2 
1169 N  N   . MET A 73  ? 0.26124 0.09541 0.15429 0.00708  0.01972  -0.00896 73  MET A N   
1170 C  CA  . MET A 73  ? 0.27592 0.11445 0.15822 0.00088  0.02342  -0.01114 73  MET A CA  
1171 C  C   . MET A 73  ? 0.27001 0.09484 0.15797 0.00669  0.01042  -0.00846 73  MET A C   
1172 O  O   . MET A 73  ? 0.27041 0.09978 0.17993 0.00777  0.01006  -0.01085 73  MET A O   
1173 C  CB  . MET A 73  ? 0.27446 0.10947 0.15084 -0.01251 0.01389  -0.00292 73  MET A CB  
1174 C  CG  . MET A 73  ? 0.28000 0.11552 0.15877 0.00293  -0.00443 0.01583  73  MET A CG  
1175 S  SD  . MET A 73  ? 0.29492 0.10215 0.16567 -0.00268 0.00188  -0.00306 73  MET A SD  
1176 C  CE  . MET A 73  ? 0.29760 0.15932 0.16408 -0.00226 0.00517  0.01573  73  MET A CE  
1186 N  N   . ILE A 74  ? 0.26771 0.08025 0.16866 -0.00290 0.01458  -0.00684 74  ILE A N   
1187 C  CA  . ILE A 74  ? 0.26830 0.10390 0.18540 -0.00514 0.01508  0.00149  74  ILE A CA  
1188 C  C   . ILE A 74  ? 0.26358 0.09096 0.18000 -0.00734 0.01846  -0.01423 74  ILE A C   
1189 O  O   . ILE A 74  ? 0.27351 0.11638 0.18651 0.00559  0.02712  0.01126  74  ILE A O   
1190 C  CB  . ILE A 74  ? 0.28189 0.10207 0.19937 -0.01008 0.00861  0.00784  74  ILE A CB  
1191 C  CG1 . ILE A 74  ? 0.28448 0.11002 0.20247 -0.02976 0.00243  0.00673  74  ILE A CG1 
1192 C  CG2 . ILE A 74  ? 0.28569 0.11614 0.20950 -0.04828 0.00084  0.00440  74  ILE A CG2 
1193 C  CD1 . ILE A 74  ? 0.29044 0.14364 0.20419 -0.01363 0.00102  -0.00173 74  ILE A CD1 
1205 N  N   . THR A 75  ? 0.25379 0.10082 0.16754 0.00060  0.01580  -0.00343 75  THR A N   
1206 C  CA  . THR A 75  ? 0.26454 0.08139 0.16548 -0.00703 0.01075  0.01085  75  THR A CA  
1207 C  C   . THR A 75  ? 0.27554 0.06932 0.17046 -0.00038 0.01244  -0.00274 75  THR A C   
1208 O  O   . THR A 75  ? 0.29705 0.07892 0.18427 -0.02759 0.00431  -0.00634 75  THR A O   
1209 C  CB  . THR A 75  ? 0.27084 0.09687 0.16571 0.00363  0.00020  -0.00142 75  THR A CB  
1210 O  OG1 . THR A 75  ? 0.28164 0.10345 0.15809 -0.00748 0.00391  0.00517  75  THR A OG1 
1211 C  CG2 . THR A 75  ? 0.28790 0.11099 0.16724 0.00305  0.00269  -0.00762 75  THR A CG2 
1219 N  N   . PRO A 76  ? 0.27442 0.10881 0.16055 -0.00602 0.01043  -0.00175 76  PRO A N   
1220 C  CA  . PRO A 76  ? 0.29537 0.10078 0.15731 0.00358  0.01231  0.00033  76  PRO A CA  
1221 C  C   . PRO A 76  ? 0.29750 0.10968 0.16477 0.00682  0.01226  0.00956  76  PRO A C   
1222 O  O   . PRO A 76  ? 0.30553 0.09593 0.18296 -0.01023 0.01951  0.01117  76  PRO A O   
1223 C  CB  . PRO A 76  ? 0.32881 0.13554 0.16977 -0.01071 0.00811  -0.01563 76  PRO A CB  
1224 C  CG  . PRO A 76  ? 0.30609 0.14276 0.18087 -0.02071 0.02722  -0.01477 76  PRO A CG  
1225 C  CD  . PRO A 76  ? 0.29090 0.11286 0.17076 -0.01748 0.02597  -0.01642 76  PRO A CD  
1233 N  N   . ASN A 77  ? 0.27363 0.10239 0.17316 -0.00123 0.00064  -0.00468 77  ASN A N   
1234 C  CA  . ASN A 77  ? 0.27386 0.08745 0.16784 0.00941  -0.00951 0.00582  77  ASN A CA  
1235 C  C   . ASN A 77  ? 0.29347 0.08565 0.16692 0.00791  -0.00885 0.01557  77  ASN A C   
1236 O  O   . ASN A 77  ? 0.28302 0.11551 0.17103 0.01090  -0.01389 0.01020  77  ASN A O   
1237 C  CB  . ASN A 77  ? 0.29532 0.10528 0.16356 -0.00510 0.00446  0.01591  77  ASN A CB  
1238 C  CG  . ASN A 77  ? 0.29035 0.10670 0.16049 0.00551  0.00291  0.00162  77  ASN A CG  
1239 O  OD1 . ASN A 77  ? 0.30098 0.09778 0.16112 -0.00178 0.00015  0.00048  77  ASN A OD1 
1240 N  ND2 . ASN A 77  ? 0.27684 0.10263 0.17257 -0.02638 0.01301  0.00269  77  ASN A ND2 
1247 N  N   . GLY A 78  ? 0.28909 0.09697 0.16904 -0.00131 0.00533  -0.00953 78  GLY A N   
1248 C  CA  . GLY A 78  ? 0.29051 0.08726 0.16669 -0.00329 -0.00117 -0.00940 78  GLY A CA  
1249 C  C   . GLY A 78  ? 0.28611 0.08649 0.16462 0.01080  0.00966  -0.00516 78  GLY A C   
1250 O  O   . GLY A 78  ? 0.33539 0.11752 0.17050 -0.00599 0.00722  -0.01402 78  GLY A O   
1254 N  N   . ARG A 79  ? 0.27751 0.09813 0.16329 -0.00838 0.00525  0.00751  79  ARG A N   
1255 C  CA  . ARG A 79  ? 0.27106 0.08114 0.17400 -0.00462 -0.00061 -0.01027 79  ARG A CA  
1256 C  C   . ARG A 79  ? 0.28728 0.07631 0.17416 -0.01803 0.01549  -0.00027 79  ARG A C   
1257 O  O   . ARG A 79  ? 0.30296 0.09741 0.17748 0.00939  0.00602  -0.00119 79  ARG A O   
1258 C  CB  . ARG A 79  ? 0.26986 0.11749 0.18492 -0.01444 0.00311  -0.00318 79  ARG A CB  
1259 C  CG  . ARG A 79  ? 0.27132 0.13073 0.18818 -0.01286 -0.00592 -0.01171 79  ARG A CG  
1260 C  CD  . ARG A 79  ? 0.28062 0.11074 0.19520 -0.01253 -0.00387 -0.01772 79  ARG A CD  
1261 N  NE  . ARG A 79  ? 0.27502 0.10167 0.21248 -0.00730 0.01173  -0.01287 79  ARG A NE  
1262 C  CZ  . ARG A 79  ? 0.25106 0.11506 0.21744 -0.00028 0.01039  -0.02931 79  ARG A CZ  
1263 N  NH1 . ARG A 79  ? 0.27683 0.13353 0.23004 -0.01605 0.03602  -0.02948 79  ARG A NH1 
1264 N  NH2 . ARG A 79  ? 0.26635 0.13453 0.21021 -0.00516 -0.00254 -0.02263 79  ARG A NH2 
1278 N  N   . PHE A 80  ? 0.29524 0.07532 0.17651 -0.00820 0.01729  0.00669  80  PHE A N   
1279 C  CA  . PHE A 80  ? 0.28096 0.08905 0.17559 -0.00363 0.01469  0.01023  80  PHE A CA  
1280 C  C   . PHE A 80  ? 0.27337 0.09331 0.17240 0.00010  0.01379  0.01697  80  PHE A C   
1281 O  O   . PHE A 80  ? 0.29001 0.10134 0.16930 0.00260  0.01238  0.02277  80  PHE A O   
1282 C  CB  . PHE A 80  ? 0.29318 0.11201 0.17858 -0.02166 0.01303  0.02106  80  PHE A CB  
1283 C  CG  . PHE A 80  ? 0.25850 0.12877 0.17218 -0.01004 -0.00106 0.02097  80  PHE A CG  
1284 C  CD1 . PHE A 80  ? 0.26138 0.14161 0.17508 -0.01259 -0.00747 0.00277  80  PHE A CD1 
1285 C  CD2 . PHE A 80  ? 0.25759 0.15869 0.17251 0.00235  -0.00436 0.02309  80  PHE A CD2 
1286 C  CE1 . PHE A 80  ? 0.26656 0.12313 0.18272 -0.00646 -0.00240 0.01435  80  PHE A CE1 
1287 C  CE2 . PHE A 80  ? 0.26901 0.15289 0.18395 0.02352  0.00174  0.00010  80  PHE A CE2 
1288 C  CZ  . PHE A 80  ? 0.26973 0.15930 0.17619 -0.00159 0.00756  0.02080  80  PHE A CZ  
1298 N  N   . LYS A 81  ? 0.27884 0.08654 0.17332 -0.00324 0.01447  0.00193  81  LYS A N   
1299 C  CA  . LYS A 81  ? 0.28199 0.10632 0.17151 0.02187  0.02577  0.00097  81  LYS A CA  
1300 C  C   . LYS A 81  ? 0.28720 0.11434 0.16853 0.00684  0.02533  0.00441  81  LYS A C   
1301 O  O   . LYS A 81  ? 0.30423 0.12499 0.16720 0.01396  0.02292  -0.00206 81  LYS A O   
1302 C  CB  . LYS A 81  ? 0.29398 0.12654 0.18737 0.01070  0.01832  0.00112  81  LYS A CB  
1303 C  CG  . LYS A 81  ? 0.30254 0.14015 0.20293 0.03356  0.02052  0.00865  81  LYS A CG  
1304 C  CD  . LYS A 81  ? 0.30594 0.15561 0.21792 0.00901  0.02278  0.00082  81  LYS A CD  
1305 C  CE  . LYS A 81  ? 0.32618 0.14577 0.22911 0.00899  0.04043  -0.00496 81  LYS A CE  
1306 N  NZ  . LYS A 81  ? 0.32530 0.16181 0.24089 0.04262  0.04751  -0.00510 81  LYS A NZ  
1320 N  N   . PRO A 82  ? 0.27991 0.11308 0.17380 0.00007  0.01558  -0.00044 82  PRO A N   
1321 C  CA  . PRO A 82  ? 0.28673 0.11190 0.17374 0.00434  0.01141  0.01304  82  PRO A CA  
1322 C  C   . PRO A 82  ? 0.27532 0.10133 0.17918 -0.00754 0.02044  0.01210  82  PRO A C   
1323 O  O   . PRO A 82  ? 0.28832 0.10787 0.18290 0.00243  0.01794  0.00328  82  PRO A O   
1324 C  CB  . PRO A 82  ? 0.30382 0.10732 0.18916 -0.00380 0.00391  0.03190  82  PRO A CB  
1325 C  CG  . PRO A 82  ? 0.29602 0.13799 0.18965 -0.00955 -0.00212 0.02344  82  PRO A CG  
1326 C  CD  . PRO A 82  ? 0.30074 0.11587 0.17689 0.00128  0.00225  0.02545  82  PRO A CD  
1334 N  N   . ASN A 83  ? 0.26498 0.11493 0.18101 -0.00486 0.01160  0.00059  83  ASN A N   
1335 C  CA  . ASN A 83  ? 0.24840 0.09896 0.18891 -0.01546 0.02203  0.00222  83  ASN A CA  
1336 C  C   . ASN A 83  ? 0.25531 0.11631 0.19064 -0.00006 -0.00213 -0.00461 83  ASN A C   
1337 O  O   . ASN A 83  ? 0.24249 0.13900 0.21609 -0.01129 -0.00934 -0.00938 83  ASN A O   
1338 C  CB  . ASN A 83  ? 0.27611 0.11912 0.20749 -0.00094 0.03159  -0.00114 83  ASN A CB  
1339 C  CG  . ASN A 83  ? 0.30864 0.12590 0.22853 -0.03741 0.05926  -0.02237 83  ASN A CG  
1340 O  OD1 . ASN A 83  ? 0.35461 0.13342 0.24877 -0.04683 0.06063  -0.03331 83  ASN A OD1 
1341 N  ND2 . ASN A 83  ? 0.35187 0.12084 0.25633 -0.01329 0.06697  0.00325  83  ASN A ND2 
1348 N  N   . THR A 84  ? 0.25656 0.10107 0.18278 -0.00386 -0.00509 -0.00420 84  THR A N   
1349 C  CA  . THR A 84  ? 0.26256 0.09002 0.17617 -0.00978 0.00474  0.00301  84  THR A CA  
1350 C  C   . THR A 84  ? 0.26932 0.07958 0.17401 -0.00276 0.01587  -0.00036 84  THR A C   
1351 O  O   . THR A 84  ? 0.27435 0.10824 0.17407 0.01649  0.00812  0.00808  84  THR A O   
1352 C  CB  . THR A 84  ? 0.30924 0.10732 0.17395 -0.01966 0.01560  0.00364  84  THR A CB  
1353 O  OG1 . THR A 84  ? 0.31124 0.11341 0.16465 -0.02359 0.02531  -0.00825 84  THR A OG1 
1354 C  CG2 . THR A 84  ? 0.30726 0.10454 0.17052 -0.02565 0.02562  0.00528  84  THR A CG2 
1362 N  N   . ARG A 85  ? 0.26360 0.08529 0.17858 -0.01466 0.00841  0.00212  85  ARG A N   
1363 C  CA  . ARG A 85  ? 0.26703 0.06742 0.18429 -0.00371 0.00606  0.00349  85  ARG A CA  
1364 C  C   . ARG A 85  ? 0.25072 0.07818 0.17523 -0.01635 -0.00448 -0.00266 85  ARG A C   
1365 O  O   . ARG A 85  ? 0.28538 0.08654 0.17760 -0.00638 0.00089  -0.02110 85  ARG A O   
1366 C  CB  . ARG A 85  ? 0.29887 0.10855 0.18620 0.00369  -0.00011 0.00144  85  ARG A CB  
1367 C  CG  . ARG A 85  ? 0.32610 0.11463 0.19313 0.01027  -0.00692 0.00233  85  ARG A CG  
1368 C  CD  . ARG A 85  ? 0.32735 0.14613 0.20392 -0.00109 -0.02596 0.01367  85  ARG A CD  
1369 N  NE  . ARG A 85  ? 0.35158 0.15997 0.21534 0.02643  -0.02234 0.00231  85  ARG A NE  
1370 C  CZ  . ARG A 85  ? 0.34006 0.15918 0.22270 0.02979  -0.01529 -0.01387 85  ARG A CZ  
1371 N  NH1 . ARG A 85  ? 0.36404 0.21492 0.24517 0.03218  0.00574  -0.02235 85  ARG A NH1 
1372 N  NH2 . ARG A 85  ? 0.32326 0.20098 0.22005 0.01939  -0.02899 -0.02677 85  ARG A NH2 
1386 N  N   . LEU A 86  ? 0.25608 0.08849 0.16807 -0.00428 0.00688  -0.00941 86  LEU A N   
1387 C  CA  . LEU A 86  ? 0.25440 0.06823 0.17505 -0.02473 -0.01018 -0.00472 86  LEU A CA  
1388 C  C   . LEU A 86  ? 0.25731 0.08556 0.17561 -0.01228 -0.01461 0.00013  86  LEU A C   
1389 O  O   . LEU A 86  ? 0.26426 0.09543 0.18853 -0.00409 0.00171  -0.00137 86  LEU A O   
1390 C  CB  . LEU A 86  ? 0.27558 0.11703 0.17387 0.00026  -0.01367 0.00200  86  LEU A CB  
1391 C  CG  . LEU A 86  ? 0.27377 0.10759 0.16698 -0.00385 0.00075  0.00833  86  LEU A CG  
1392 C  CD1 . LEU A 86  ? 0.27399 0.11856 0.16743 -0.00194 -0.00264 0.00493  86  LEU A CD1 
1393 C  CD2 . LEU A 86  ? 0.27877 0.14566 0.16397 -0.00286 -0.00934 0.01767  86  LEU A CD2 
1405 N  N   . CYS A 87  ? 0.26318 0.08472 0.17304 -0.03514 -0.00784 0.00991  87  CYS A N   
1406 C  CA  . CYS A 87  ? 0.24931 0.09325 0.16190 -0.04150 -0.01135 -0.00175 87  CYS A CA  
1407 C  C   . CYS A 87  ? 0.27541 0.06932 0.16658 -0.00020 -0.00634 -0.00506 87  CYS A C   
1408 O  O   . CYS A 87  ? 0.27514 0.13494 0.16893 0.00158  -0.00227 -0.00112 87  CYS A O   
1409 C  CB  . CYS A 87  ? 0.25142 0.10769 0.16065 -0.03119 -0.00586 -0.00106 87  CYS A CB  
1410 S  SG  . CYS A 87  ? 0.27005 0.10091 0.17331 -0.00766 0.01053  0.00075  87  CYS A SG  
1416 N  N   . LEU A 88  ? 0.27298 0.10809 0.16715 0.01120  -0.01286 -0.01137 88  LEU A N   
1417 C  CA  . LEU A 88  ? 0.26381 0.11127 0.16814 0.00491  -0.01531 -0.00337 88  LEU A CA  
1418 C  C   . LEU A 88  ? 0.26029 0.11933 0.16768 -0.00789 -0.00884 -0.00077 88  LEU A C   
1419 O  O   . LEU A 88  ? 0.27454 0.12174 0.17850 0.00364  0.00796  0.00084  88  LEU A O   
1420 C  CB  . LEU A 88  ? 0.27792 0.11220 0.17776 -0.00980 -0.00512 0.00004  88  LEU A CB  
1421 C  CG  . LEU A 88  ? 0.29793 0.12533 0.19124 -0.01244 -0.01525 0.01124  88  LEU A CG  
1422 C  CD1 . LEU A 88  ? 0.32275 0.13095 0.19828 -0.01391 -0.00162 0.00069  88  LEU A CD1 
1423 C  CD2 . LEU A 88  ? 0.31657 0.16350 0.20161 0.00071  -0.02431 0.01572  88  LEU A CD2 
1435 N  N   . SER A 89  ? 0.27204 0.10685 0.17217 0.00004  -0.00454 0.00073  89  SER A N   
1436 C  CA  . SER A 89  ? 0.27742 0.15483 0.18503 -0.01271 -0.01051 0.02080  89  SER A CA  
1437 C  C   . SER A 89  ? 0.26554 0.12804 0.17807 -0.00686 0.00469  0.01417  89  SER A C   
1438 O  O   . SER A 89  ? 0.30267 0.13330 0.18595 -0.01053 0.00142  0.00809  89  SER A O   
1439 C  CB  . SER A 89  ? 0.30190 0.22716 0.21270 -0.03090 -0.01029 0.01599  89  SER A CB  
1440 O  OG  . SER A 89  ? 0.36028 0.28544 0.23809 -0.05477 -0.00587 0.01835  89  SER A OG  
1446 N  N   . MET A 90  ? 0.29002 0.10829 0.17965 -0.00361 0.01233  0.00514  90  MET A N   
1447 C  CA  . MET A 90  ? 0.28795 0.10560 0.18249 0.00130  0.00839  -0.00043 90  MET A CA  
1448 C  C   . MET A 90  ? 0.29670 0.09539 0.19328 0.00695  0.00486  0.00410  90  MET A C   
1449 O  O   . MET A 90  ? 0.30554 0.11043 0.20464 0.01470  -0.01113 0.00778  90  MET A O   
1450 C  CB  . MET A 90  ? 0.30853 0.13133 0.17797 -0.00454 0.00608  -0.01002 90  MET A CB  
1451 C  CG  . MET A 90  ? 0.30630 0.11683 0.17881 0.00844  0.00532  -0.01228 90  MET A CG  
1452 S  SD  . MET A 90  ? 0.32139 0.18080 0.19774 0.02127  0.01730  -0.00665 90  MET A SD  
1453 C  CE  . MET A 90  ? 0.31032 0.15875 0.20337 0.04506  0.01343  -0.01497 90  MET A CE  
1463 N  N   . SER A 91  ? 0.29079 0.09787 0.18911 0.00862  0.00424  -0.00160 91  SER A N   
1464 C  CA  . SER A 91  ? 0.27645 0.11395 0.18143 -0.00281 0.00433  -0.00621 91  SER A CA  
1465 C  C   . SER A 91  ? 0.27429 0.12008 0.17807 0.00698  0.00294  0.00371  91  SER A C   
1466 O  O   . SER A 91  ? 0.28524 0.11416 0.18857 0.00253  0.01105  0.00702  91  SER A O   
1467 C  CB  . SER A 91  ? 0.27415 0.13125 0.18174 -0.02778 0.00310  0.01426  91  SER A CB  
1468 O  OG  . SER A 91  ? 0.29444 0.12166 0.17578 -0.00780 -0.00357 0.00390  91  SER A OG  
1474 N  N   . ASP A 92  ? 0.28555 0.10052 0.17664 -0.01263 -0.00166 -0.00827 92  ASP A N   
1475 C  CA  . ASP A 92  ? 0.28323 0.10730 0.17575 -0.01003 -0.00287 0.00831  92  ASP A CA  
1476 C  C   . ASP A 92  ? 0.26878 0.09811 0.17029 -0.00193 -0.00707 0.00432  92  ASP A C   
1477 O  O   . ASP A 92  ? 0.30367 0.10866 0.17728 0.00835  -0.02867 -0.00606 92  ASP A O   
1478 C  CB  . ASP A 92  ? 0.26868 0.10639 0.20477 -0.00373 -0.01908 -0.00704 92  ASP A CB  
1479 C  CG  . ASP A 92  ? 0.27731 0.09881 0.24397 -0.01598 -0.03115 -0.00536 92  ASP A CG  
1480 O  OD1 . ASP A 92  ? 0.28284 0.10255 0.23986 0.00403  -0.01396 0.01470  92  ASP A OD1 
1481 O  OD2 . ASP A 92  ? 0.31600 0.14827 0.28676 -0.02251 -0.02809 -0.01572 92  ASP A OD2 
1486 N  N   . TYR A 93  ? 0.27399 0.11210 0.15897 -0.00378 -0.01418 -0.00469 93  TYR A N   
1487 C  CA  . TYR A 93  ? 0.26836 0.09191 0.16888 -0.01999 -0.00057 0.00637  93  TYR A CA  
1488 C  C   . TYR A 93  ? 0.27200 0.07916 0.17461 -0.00806 0.00006  0.00130  93  TYR A C   
1489 O  O   . TYR A 93  ? 0.29489 0.10422 0.19492 -0.01133 -0.00040 0.00706  93  TYR A O   
1490 C  CB  . TYR A 93  ? 0.25303 0.10341 0.17115 -0.01773 -0.00944 0.00539  93  TYR A CB  
1491 C  CG  . TYR A 93  ? 0.25094 0.10351 0.16920 -0.02227 -0.00898 -0.00541 93  TYR A CG  
1492 C  CD1 . TYR A 93  ? 0.25759 0.11159 0.17605 -0.01650 0.01066  0.00011  93  TYR A CD1 
1493 C  CD2 . TYR A 93  ? 0.25737 0.11507 0.17319 0.00691  -0.00411 -0.00058 93  TYR A CD2 
1494 C  CE1 . TYR A 93  ? 0.27289 0.11904 0.17247 -0.00858 0.00430  -0.00307 93  TYR A CE1 
1495 C  CE2 . TYR A 93  ? 0.26254 0.10002 0.17790 0.00629  0.01979  -0.00397 93  TYR A CE2 
1496 C  CZ  . TYR A 93  ? 0.26808 0.09905 0.17843 -0.00686 0.02135  0.00510  93  TYR A CZ  
1497 O  OH  . TYR A 93  ? 0.28207 0.10779 0.18473 -0.01847 0.01168  -0.02366 93  TYR A OH  
1507 N  N   . HIS A 94  ? 0.27934 0.10767 0.16705 0.01212  0.01287  0.00522  94  HIS A N   
1508 C  CA  . HIS A 94  ? 0.28623 0.11124 0.17373 0.01865  0.01494  -0.00352 94  HIS A CA  
1509 C  C   . HIS A 94  ? 0.30165 0.07727 0.17315 0.01744  0.00742  0.00295  94  HIS A C   
1510 O  O   . HIS A 94  ? 0.29523 0.11666 0.18252 0.01014  0.00377  -0.01046 94  HIS A O   
1511 C  CB  . HIS A 94  ? 0.28257 0.13454 0.16973 -0.01631 0.01149  0.00103  94  HIS A CB  
1512 C  CG  . HIS A 94  ? 0.28760 0.13175 0.17281 -0.02507 -0.00177 -0.00444 94  HIS A CG  
1513 N  ND1 . HIS A 94  ? 0.30272 0.15050 0.18240 -0.02217 -0.01292 -0.02294 94  HIS A ND1 
1514 C  CD2 . HIS A 94  ? 0.29264 0.11589 0.17788 0.00061  -0.00164 -0.00713 94  HIS A CD2 
1515 C  CE1 . HIS A 94  ? 0.31277 0.11735 0.17789 0.02236  -0.02117 0.00188  94  HIS A CE1 
1516 N  NE2 . HIS A 94  ? 0.32302 0.13537 0.18353 0.00184  -0.00057 -0.00683 94  HIS A NE2 
1524 N  N   . PRO A 95  ? 0.29523 0.10037 0.16122 0.01937  -0.00248 0.01031  95  PRO A N   
1525 C  CA  . PRO A 95  ? 0.32043 0.12570 0.16568 0.00529  -0.00099 0.01892  95  PRO A CA  
1526 C  C   . PRO A 95  ? 0.33611 0.11160 0.17439 -0.01036 0.00685  0.01239  95  PRO A C   
1527 O  O   . PRO A 95  ? 0.36012 0.14101 0.17885 -0.01734 0.01096  0.01902  95  PRO A O   
1528 C  CB  . PRO A 95  ? 0.31913 0.15630 0.16760 0.00134  -0.00132 0.02059  95  PRO A CB  
1529 C  CG  . PRO A 95  ? 0.31336 0.16182 0.17415 -0.01113 0.00810  0.02316  95  PRO A CG  
1530 C  CD  . PRO A 95  ? 0.31502 0.13395 0.17350 0.00583  0.00338  0.01366  95  PRO A CD  
1538 N  N   . ASP A 96  ? 0.33105 0.09713 0.18400 -0.01505 0.01352  0.00400  96  ASP A N   
1539 C  CA  . ASP A 96  ? 0.33611 0.12642 0.18236 -0.01003 0.00353  0.01269  96  ASP A CA  
1540 C  C   . ASP A 96  ? 0.34370 0.13213 0.18127 -0.00720 0.02193  0.01058  96  ASP A C   
1541 O  O   . ASP A 96  ? 0.36457 0.16011 0.19107 -0.00036 0.03756  0.02697  96  ASP A O   
1542 C  CB  . ASP A 96  ? 0.34225 0.12273 0.19268 -0.02087 0.00999  -0.03099 96  ASP A CB  
1543 C  CG  . ASP A 96  ? 0.35800 0.12736 0.19351 -0.03148 0.01631  -0.03544 96  ASP A CG  
1544 O  OD1 . ASP A 96  ? 0.37254 0.10851 0.19327 -0.03121 0.00233  -0.01176 96  ASP A OD1 
1545 O  OD2 . ASP A 96  ? 0.38503 0.13582 0.19557 -0.02749 0.01840  -0.02853 96  ASP A OD2 
1550 N  N   . THR A 97  ? 0.33172 0.12709 0.18484 -0.02454 0.01628  0.00406  97  THR A N   
1551 C  CA  . THR A 97  ? 0.32705 0.13563 0.19592 -0.01963 0.01682  -0.00825 97  THR A CA  
1552 C  C   . THR A 97  ? 0.30746 0.13654 0.19870 -0.03662 0.01771  -0.00552 97  THR A C   
1553 O  O   . THR A 97  ? 0.32504 0.16247 0.22004 0.00149  0.00742  -0.01558 97  THR A O   
1554 C  CB  . THR A 97  ? 0.32837 0.14280 0.20177 -0.02841 0.02148  -0.00049 97  THR A CB  
1555 O  OG1 . THR A 97  ? 0.34869 0.12594 0.20036 -0.02614 0.01327  0.00228  97  THR A OG1 
1556 C  CG2 . THR A 97  ? 0.34620 0.13082 0.20281 -0.04049 0.02089  -0.00286 97  THR A CG2 
1564 N  N   . TRP A 98  ? 0.32450 0.14045 0.20287 -0.02981 0.01468  0.00999  98  TRP A N   
1565 C  CA  . TRP A 98  ? 0.31582 0.12703 0.19226 -0.01206 0.02476  -0.00176 98  TRP A CA  
1566 C  C   . TRP A 98  ? 0.30864 0.13114 0.19245 -0.01244 0.01943  0.01420  98  TRP A C   
1567 O  O   . TRP A 98  ? 0.33383 0.14478 0.20251 -0.00673 0.02004  0.02523  98  TRP A O   
1568 C  CB  . TRP A 98  ? 0.31690 0.12615 0.19040 0.01541  0.01958  -0.01188 98  TRP A CB  
1569 C  CG  . TRP A 98  ? 0.32278 0.14312 0.19893 -0.00249 0.00466  0.00747  98  TRP A CG  
1570 C  CD1 . TRP A 98  ? 0.31896 0.12716 0.20747 0.00867  0.00770  -0.00031 98  TRP A CD1 
1571 C  CD2 . TRP A 98  ? 0.30406 0.12487 0.19574 -0.00931 0.00443  -0.00772 98  TRP A CD2 
1572 N  NE1 . TRP A 98  ? 0.32815 0.11328 0.20539 -0.00598 0.01574  -0.00413 98  TRP A NE1 
1573 C  CE2 . TRP A 98  ? 0.30510 0.11015 0.19654 -0.03472 0.01713  -0.01105 98  TRP A CE2 
1574 C  CE3 . TRP A 98  ? 0.31706 0.11802 0.20541 -0.02080 0.00459  -0.01786 98  TRP A CE3 
1575 C  CZ2 . TRP A 98  ? 0.32578 0.14388 0.19631 -0.04031 0.01495  -0.01802 98  TRP A CZ2 
1576 C  CZ3 . TRP A 98  ? 0.31724 0.12220 0.20036 -0.02061 0.00619  -0.00991 98  TRP A CZ3 
1577 C  CH2 . TRP A 98  ? 0.32754 0.11869 0.19455 -0.02396 0.01850  -0.01904 98  TRP A CH2 
1588 N  N   . ASN A 99  ? 0.31488 0.13278 0.18845 -0.00423 0.00660  -0.00626 99  ASN A N   
1589 C  CA  . ASN A 99  ? 0.32059 0.14597 0.19645 -0.01202 0.01564  -0.00650 99  ASN A CA  
1590 C  C   . ASN A 99  ? 0.32894 0.13256 0.19159 -0.01489 0.01278  -0.00130 99  ASN A C   
1591 O  O   . ASN A 99  ? 0.32544 0.13345 0.18726 -0.01344 0.02004  -0.00791 99  ASN A O   
1592 C  CB  . ASN A 99  ? 0.30868 0.17345 0.22491 -0.02858 0.02309  -0.01977 99  ASN A CB  
1593 C  CG  . ASN A 99  ? 0.30368 0.19232 0.24952 -0.03823 0.02382  -0.03474 99  ASN A CG  
1594 O  OD1 . ASN A 99  ? 0.32517 0.18018 0.26178 -0.05380 0.03319  -0.04280 99  ASN A OD1 
1595 N  ND2 . ASN A 99  ? 0.34395 0.30577 0.27167 -0.03077 0.03085  -0.03514 99  ASN A ND2 
1602 N  N   . PRO A 100 ? 0.32122 0.12157 0.18039 -0.01552 0.01538  -0.00772 100 PRO A N   
1603 C  CA  . PRO A 100 ? 0.30583 0.13055 0.18510 -0.00894 0.02470  -0.00229 100 PRO A CA  
1604 C  C   . PRO A 100 ? 0.31350 0.14047 0.18938 -0.00583 0.01123  -0.00295 100 PRO A C   
1605 O  O   . PRO A 100 ? 0.33848 0.12128 0.19530 0.00011  -0.00317 -0.00458 100 PRO A O   
1606 C  CB  . PRO A 100 ? 0.31678 0.13519 0.18301 0.00772  0.00665  -0.00103 100 PRO A CB  
1607 C  CG  . PRO A 100 ? 0.33381 0.15084 0.18412 -0.01500 0.00125  0.00425  100 PRO A CG  
1608 C  CD  . PRO A 100 ? 0.33451 0.15068 0.18523 -0.02906 0.01113  0.01513  100 PRO A CD  
1616 N  N   . GLY A 101 ? 0.31191 0.14149 0.19528 -0.00145 0.00447  0.00510  101 GLY A N   
1617 C  CA  . GLY A 101 ? 0.33510 0.15520 0.20748 0.00086  0.02080  0.00954  101 GLY A CA  
1618 C  C   . GLY A 101 ? 0.31790 0.15794 0.20820 0.02175  0.02208  0.00893  101 GLY A C   
1619 O  O   . GLY A 101 ? 0.32070 0.18179 0.22016 -0.00375 0.02342  -0.00036 101 GLY A O   
1623 N  N   . TRP A 102 ? 0.30371 0.14530 0.19919 0.00777  0.00382  -0.00321 102 TRP A N   
1624 C  CA  . TRP A 102 ? 0.30440 0.15720 0.20132 0.00635  -0.00044 -0.00583 102 TRP A CA  
1625 C  C   . TRP A 102 ? 0.30206 0.15549 0.19993 0.02199  -0.00591 -0.00611 102 TRP A C   
1626 O  O   . TRP A 102 ? 0.29850 0.15302 0.21883 0.01409  -0.01931 -0.00201 102 TRP A O   
1627 C  CB  . TRP A 102 ? 0.30413 0.16553 0.19536 -0.01879 -0.00453 -0.01599 102 TRP A CB  
1628 C  CG  . TRP A 102 ? 0.29569 0.15213 0.20256 -0.01415 0.00751  -0.01170 102 TRP A CG  
1629 C  CD1 . TRP A 102 ? 0.32674 0.17252 0.21838 -0.00612 0.00529  -0.02366 102 TRP A CD1 
1630 C  CD2 . TRP A 102 ? 0.29655 0.15178 0.20260 -0.01844 0.00807  -0.00437 102 TRP A CD2 
1631 N  NE1 . TRP A 102 ? 0.32223 0.19485 0.22842 -0.02031 0.00995  -0.03638 102 TRP A NE1 
1632 C  CE2 . TRP A 102 ? 0.30973 0.16147 0.21428 -0.01139 0.02726  -0.02157 102 TRP A CE2 
1633 C  CE3 . TRP A 102 ? 0.30646 0.17019 0.19566 -0.00316 -0.00171 0.00575  102 TRP A CE3 
1634 C  CZ2 . TRP A 102 ? 0.30943 0.19801 0.21142 -0.01857 0.01543  -0.01256 102 TRP A CZ2 
1635 C  CZ3 . TRP A 102 ? 0.30600 0.16451 0.20388 0.00230  -0.00168 0.02038  102 TRP A CZ3 
1636 C  CH2 . TRP A 102 ? 0.31571 0.17580 0.20809 -0.00301 0.01223  0.01713  102 TRP A CH2 
1647 N  N   . SER A 103 ? 0.29930 0.14349 0.18030 -0.00165 -0.00123 0.00149  103 SER A N   
1648 C  CA  . SER A 103 ? 0.28827 0.13793 0.18182 -0.00137 -0.00264 -0.01413 103 SER A CA  
1649 C  C   . SER A 103 ? 0.28965 0.15072 0.16865 0.01798  -0.00832 -0.01453 103 SER A C   
1650 O  O   . SER A 103 ? 0.30032 0.14806 0.16978 0.01070  0.00001  -0.02093 103 SER A O   
1651 C  CB  . SER A 103 ? 0.30969 0.15932 0.19430 0.01230  -0.00353 -0.01043 103 SER A CB  
1652 O  OG  . SER A 103 ? 0.30434 0.16360 0.18859 0.02324  -0.00124 -0.00919 103 SER A OG  
1658 N  N   . VAL A 104 ? 0.29880 0.14395 0.16911 -0.00418 -0.00426 0.00043  104 VAL A N   
1659 C  CA  . VAL A 104 ? 0.28440 0.12570 0.18222 0.00283  0.00251  -0.00786 104 VAL A CA  
1660 C  C   . VAL A 104 ? 0.28683 0.12800 0.18464 -0.02283 -0.00133 -0.00843 104 VAL A C   
1661 O  O   . VAL A 104 ? 0.31026 0.12774 0.18549 -0.01137 -0.00001 -0.00788 104 VAL A O   
1662 C  CB  . VAL A 104 ? 0.31789 0.17223 0.19628 -0.00717 0.01328  -0.03513 104 VAL A CB  
1663 C  CG1 . VAL A 104 ? 0.32774 0.21153 0.20232 -0.03501 0.00632  -0.04033 104 VAL A CG1 
1664 C  CG2 . VAL A 104 ? 0.32088 0.23410 0.20818 -0.01170 0.00244  -0.04071 104 VAL A CG2 
1674 N  N   . SER A 105 ? 0.28501 0.14068 0.18337 0.00661  -0.00522 -0.01877 105 SER A N   
1675 C  CA  . SER A 105 ? 0.28677 0.14286 0.20338 0.00860  -0.01695 -0.03089 105 SER A CA  
1676 C  C   . SER A 105 ? 0.28497 0.13457 0.18086 0.01123  0.00035  -0.02095 105 SER A C   
1677 O  O   . SER A 105 ? 0.30362 0.15003 0.16527 0.02992  0.00108  -0.01959 105 SER A O   
1678 C  CB  . SER A 105 ? 0.32555 0.16589 0.24259 0.01557  -0.03781 -0.08591 105 SER A CB  
1679 O  OG  . SER A 105 ? 0.37217 0.24976 0.27826 0.00387  -0.00693 -0.04257 105 SER A OG  
1685 N  N   . THR A 106 ? 0.28513 0.12427 0.18453 0.00598  -0.01029 -0.01299 106 THR A N   
1686 C  CA  . THR A 106 ? 0.28687 0.13670 0.17647 -0.01632 0.00144  -0.02006 106 THR A CA  
1687 C  C   . THR A 106 ? 0.26715 0.13666 0.17457 0.00173  0.01107  -0.01694 106 THR A C   
1688 O  O   . THR A 106 ? 0.27988 0.13374 0.16964 -0.00929 0.00790  -0.01200 106 THR A O   
1689 C  CB  . THR A 106 ? 0.29231 0.15642 0.18582 -0.00880 0.01073  -0.01712 106 THR A CB  
1690 O  OG1 . THR A 106 ? 0.31515 0.16745 0.20312 -0.00893 0.02056  -0.01421 106 THR A OG1 
1691 C  CG2 . THR A 106 ? 0.29992 0.17056 0.18567 -0.01889 0.01923  -0.03032 106 THR A CG2 
1699 N  N   . ILE A 107 ? 0.26536 0.12738 0.16553 -0.01069 0.00511  -0.00163 107 ILE A N   
1700 C  CA  . ILE A 107 ? 0.26381 0.13597 0.16770 0.00835  0.00596  0.00545  107 ILE A CA  
1701 C  C   . ILE A 107 ? 0.26682 0.11536 0.16574 0.00123  -0.00417 0.00589  107 ILE A C   
1702 O  O   . ILE A 107 ? 0.28265 0.13692 0.15981 -0.00745 -0.00467 -0.00933 107 ILE A O   
1703 C  CB  . ILE A 107 ? 0.26904 0.13964 0.18277 0.00560  0.00824  -0.01056 107 ILE A CB  
1704 C  CG1 . ILE A 107 ? 0.27630 0.13584 0.18315 0.02026  0.00514  0.00576  107 ILE A CG1 
1705 C  CG2 . ILE A 107 ? 0.27750 0.14124 0.18679 -0.00536 0.01131  -0.02082 107 ILE A CG2 
1706 C  CD1 . ILE A 107 ? 0.30235 0.16974 0.19485 0.02582  -0.00123 -0.00330 107 ILE A CD1 
1718 N  N   . LEU A 108 ? 0.27825 0.10658 0.17644 0.00008  -0.00551 -0.00130 108 LEU A N   
1719 C  CA  . LEU A 108 ? 0.28291 0.10589 0.17274 -0.00511 -0.00744 -0.00224 108 LEU A CA  
1720 C  C   . LEU A 108 ? 0.27794 0.11902 0.17444 -0.00775 -0.01352 0.00196  108 LEU A C   
1721 O  O   . LEU A 108 ? 0.30018 0.11371 0.16966 0.00901  -0.00623 -0.02099 108 LEU A O   
1722 C  CB  . LEU A 108 ? 0.32576 0.10253 0.19266 -0.01498 -0.02954 0.01084  108 LEU A CB  
1723 C  CG  . LEU A 108 ? 0.33434 0.15434 0.21046 -0.01965 -0.03191 0.00741  108 LEU A CG  
1724 C  CD1 . LEU A 108 ? 0.34374 0.16889 0.22495 -0.02197 -0.04029 0.01047  108 LEU A CD1 
1725 C  CD2 . LEU A 108 ? 0.35102 0.22005 0.21727 -0.04445 -0.02653 0.02809  108 LEU A CD2 
1737 N  N   . ASN A 109 ? 0.28428 0.13989 0.17829 -0.01399 -0.01223 -0.01335 109 ASN A N   
1738 C  CA  . ASN A 109 ? 0.28344 0.17078 0.20250 0.01015  -0.01765 -0.00244 109 ASN A CA  
1739 C  C   . ASN A 109 ? 0.28930 0.14444 0.18897 -0.00975 -0.00865 -0.00336 109 ASN A C   
1740 O  O   . ASN A 109 ? 0.28806 0.15888 0.19132 -0.00996 -0.00992 -0.00311 109 ASN A O   
1741 C  CB  . ASN A 109 ? 0.27258 0.21068 0.23093 -0.00571 -0.01430 0.00055  109 ASN A CB  
1742 C  CG  . ASN A 109 ? 0.35000 0.31321 0.27525 0.03470  0.02169  0.02077  109 ASN A CG  
1743 O  OD1 . ASN A 109 ? 0.41188 0.31601 0.31331 0.05632  0.05739  0.01857  109 ASN A OD1 
1744 N  ND2 . ASN A 109 ? 0.35423 0.34587 0.28903 0.04407  0.01619  -0.00866 109 ASN A ND2 
1751 N  N   . GLY A 110 ? 0.29609 0.13335 0.19290 -0.01560 -0.00304 -0.00766 110 GLY A N   
1752 C  CA  . GLY A 110 ? 0.28023 0.15924 0.18742 -0.01078 -0.01161 -0.00709 110 GLY A CA  
1753 C  C   . GLY A 110 ? 0.28483 0.12961 0.17749 -0.00515 -0.02657 0.01377  110 GLY A C   
1754 O  O   . GLY A 110 ? 0.31580 0.12030 0.16271 -0.01773 -0.02493 0.00232  110 GLY A O   
1758 N  N   . LEU A 111 ? 0.28036 0.12643 0.18104 -0.01289 -0.02202 0.01132  111 LEU A N   
1759 C  CA  . LEU A 111 ? 0.27922 0.10662 0.18007 0.00007  -0.02026 -0.00039 111 LEU A CA  
1760 C  C   . LEU A 111 ? 0.28111 0.09771 0.17043 -0.00532 -0.02483 -0.00258 111 LEU A C   
1761 O  O   . LEU A 111 ? 0.27706 0.13208 0.16808 0.00263  -0.01607 -0.00183 111 LEU A O   
1762 C  CB  . LEU A 111 ? 0.25824 0.10846 0.19362 0.01306  -0.01040 -0.00875 111 LEU A CB  
1763 C  CG  . LEU A 111 ? 0.26856 0.09823 0.19752 -0.01561 -0.00777 -0.00976 111 LEU A CG  
1764 C  CD1 . LEU A 111 ? 0.28640 0.12261 0.19982 0.03241  -0.01109 -0.00928 111 LEU A CD1 
1765 C  CD2 . LEU A 111 ? 0.27241 0.12895 0.20640 -0.02413 0.01169  0.00166  111 LEU A CD2 
1777 N  N   . LEU A 112 ? 0.27685 0.09451 0.17610 -0.01333 -0.02814 -0.00235 112 LEU A N   
1778 C  CA  . LEU A 112 ? 0.23995 0.09471 0.18479 -0.00186 -0.01314 0.00548  112 LEU A CA  
1779 C  C   . LEU A 112 ? 0.26333 0.07505 0.17967 0.00093  -0.01626 -0.00128 112 LEU A C   
1780 O  O   . LEU A 112 ? 0.29098 0.11813 0.17305 0.00421  -0.01084 -0.00518 112 LEU A O   
1781 C  CB  . LEU A 112 ? 0.26185 0.10363 0.21087 -0.00142 -0.02635 -0.00334 112 LEU A CB  
1782 C  CG  . LEU A 112 ? 0.30312 0.11775 0.24093 0.01650  -0.03511 -0.01242 112 LEU A CG  
1783 C  CD1 . LEU A 112 ? 0.32725 0.16036 0.25657 0.00877  -0.05569 0.01459  112 LEU A CD1 
1784 C  CD2 . LEU A 112 ? 0.31758 0.18685 0.25606 0.02950  -0.03726 -0.04257 112 LEU A CD2 
1796 N  N   . SER A 113 ? 0.27514 0.10807 0.18196 -0.01990 -0.00802 -0.00642 113 SER A N   
1797 C  CA  . SER A 113 ? 0.26999 0.12814 0.18613 -0.01699 -0.01272 -0.01064 113 SER A CA  
1798 C  C   . SER A 113 ? 0.28539 0.11193 0.19226 0.00370  -0.02117 -0.00955 113 SER A C   
1799 O  O   . SER A 113 ? 0.29618 0.13588 0.19058 -0.00658 -0.03003 -0.01745 113 SER A O   
1800 C  CB  . SER A 113 ? 0.28539 0.16560 0.20187 -0.05598 -0.00684 -0.02700 113 SER A CB  
1801 O  OG  . SER A 113 ? 0.32475 0.19221 0.22169 -0.03383 -0.01639 -0.01478 113 SER A OG  
1807 N  N   . PHE A 114 ? 0.26066 0.11009 0.18959 0.01042  -0.02390 -0.01696 114 PHE A N   
1808 C  CA  . PHE A 114 ? 0.27106 0.09773 0.17890 0.01927  -0.01197 0.00262  114 PHE A CA  
1809 C  C   . PHE A 114 ? 0.26896 0.12678 0.16932 0.00998  -0.01448 -0.00867 114 PHE A C   
1810 O  O   . PHE A 114 ? 0.28286 0.12241 0.15667 0.00611  -0.00448 -0.01230 114 PHE A O   
1811 C  CB  . PHE A 114 ? 0.27651 0.09396 0.18413 0.01845  -0.01248 0.00627  114 PHE A CB  
1812 C  CG  . PHE A 114 ? 0.27588 0.11039 0.20338 0.01647  -0.01609 -0.01173 114 PHE A CG  
1813 C  CD1 . PHE A 114 ? 0.28903 0.11622 0.20760 0.00993  -0.02635 -0.00081 114 PHE A CD1 
1814 C  CD2 . PHE A 114 ? 0.28382 0.14900 0.21677 0.00615  -0.01823 -0.01494 114 PHE A CD2 
1815 C  CE1 . PHE A 114 ? 0.29459 0.13718 0.22271 0.00803  -0.02864 -0.00850 114 PHE A CE1 
1816 C  CE2 . PHE A 114 ? 0.29762 0.18539 0.22174 0.02910  -0.02710 -0.01120 114 PHE A CE2 
1817 C  CZ  . PHE A 114 ? 0.29655 0.17642 0.22070 0.04930  -0.02212 -0.03216 114 PHE A CZ  
1827 N  N   . MET A 115 ? 0.26495 0.12034 0.18174 -0.00478 -0.00668 -0.00371 115 MET A N   
1828 C  CA  . MET A 115 ? 0.25001 0.11136 0.18255 -0.01559 -0.00009 0.00226  115 MET A CA  
1829 C  C   . MET A 115 ? 0.25175 0.10807 0.18193 -0.00256 -0.00369 -0.00996 115 MET A C   
1830 O  O   . MET A 115 ? 0.25152 0.11221 0.18108 -0.00013 -0.00493 -0.01478 115 MET A O   
1831 C  CB  . MET A 115 ? 0.25550 0.11605 0.18091 -0.02339 0.00708  0.00182  115 MET A CB  
1832 C  CG  . MET A 115 ? 0.27509 0.12715 0.18671 -0.01882 0.00445  0.00140  115 MET A CG  
1833 S  SD  . MET A 115 ? 0.31162 0.12649 0.18187 -0.01737 -0.01156 -0.01107 115 MET A SD  
1834 C  CE  . MET A 115 ? 0.32042 0.13294 0.18695 -0.04724 -0.00332 -0.00420 115 MET A CE  
1844 N  N   . THR A 116 ? 0.25537 0.11319 0.19866 -0.00846 -0.01027 0.00151  116 THR A N   
1845 C  CA  . THR A 116 ? 0.26857 0.10195 0.20215 -0.00182 -0.00019 0.00477  116 THR A CA  
1846 C  C   . THR A 116 ? 0.29061 0.10512 0.21688 0.00290  -0.02465 -0.00221 116 THR A C   
1847 O  O   . THR A 116 ? 0.28393 0.14428 0.23559 -0.00675 -0.03765 -0.00033 116 THR A O   
1848 C  CB  . THR A 116 ? 0.26533 0.12106 0.21352 0.00376  -0.00492 0.01246  116 THR A CB  
1849 O  OG1 . THR A 116 ? 0.28145 0.17243 0.23671 -0.00383 0.01463  0.04065  116 THR A OG1 
1850 C  CG2 . THR A 116 ? 0.28750 0.10272 0.20672 -0.00516 -0.01142 0.01367  116 THR A CG2 
1858 N  N   . SER A 117 ? 0.28410 0.11604 0.20758 0.01312  -0.02696 0.00580  117 SER A N   
1859 C  CA  . SER A 117 ? 0.26371 0.10100 0.21574 -0.00351 -0.02216 -0.00962 117 SER A CA  
1860 C  C   . SER A 117 ? 0.26566 0.11349 0.22084 -0.02053 -0.02631 -0.00752 117 SER A C   
1861 O  O   . SER A 117 ? 0.28568 0.10745 0.24022 -0.01304 -0.01340 -0.01172 117 SER A O   
1862 C  CB  . SER A 117 ? 0.28177 0.11234 0.21350 -0.01922 -0.02834 0.00268  117 SER A CB  
1863 O  OG  . SER A 117 ? 0.30096 0.11701 0.21728 -0.00892 -0.02546 0.00476  117 SER A OG  
1869 N  N   . ASP A 118 ? 0.26453 0.11941 0.21316 -0.00117 -0.02018 -0.01576 118 ASP A N   
1870 C  CA  . ASP A 118 ? 0.27378 0.12660 0.21699 0.01721  -0.01455 -0.00374 118 ASP A CA  
1871 C  C   . ASP A 118 ? 0.25300 0.12759 0.21295 0.01363  -0.01571 -0.01193 118 ASP A C   
1872 O  O   . ASP A 118 ? 0.30009 0.16443 0.21257 0.03408  -0.02076 -0.02613 118 ASP A O   
1873 C  CB  . ASP A 118 ? 0.30278 0.17336 0.22774 0.02570  0.00408  0.01585  118 ASP A CB  
1874 C  CG  . ASP A 118 ? 0.33578 0.19498 0.24771 -0.01122 -0.00940 0.02438  118 ASP A CG  
1875 O  OD1 . ASP A 118 ? 0.38431 0.24055 0.29125 -0.01682 -0.01320 0.07409  118 ASP A OD1 
1876 O  OD2 . ASP A 118 ? 0.31906 0.16446 0.22769 0.01387  -0.01382 0.00224  118 ASP A OD2 
1881 N  N   . GLU A 119 ? 0.26936 0.10675 0.21471 0.00879  -0.01037 -0.01108 119 GLU A N   
1882 C  CA  . GLU A 119 ? 0.26598 0.10467 0.21926 0.01355  -0.02002 0.00040  119 GLU A CA  
1883 C  C   . GLU A 119 ? 0.27417 0.10655 0.21046 0.01203  -0.01971 -0.00462 119 GLU A C   
1884 O  O   . GLU A 119 ? 0.28452 0.13022 0.20892 0.00374  -0.00596 -0.01389 119 GLU A O   
1885 C  CB  . GLU A 119 ? 0.27004 0.13659 0.23693 -0.02222 -0.03596 0.00712  119 GLU A CB  
1886 C  CG  . GLU A 119 ? 0.28579 0.17237 0.26363 -0.02606 -0.03161 0.03089  119 GLU A CG  
1887 C  CD  . GLU A 119 ? 0.30620 0.20408 0.27832 -0.00433 -0.04803 0.06281  119 GLU A CD  
1888 O  OE1 . GLU A 119 ? 0.33436 0.20513 0.28211 -0.00783 -0.05168 0.04054  119 GLU A OE1 
1889 O  OE2 . GLU A 119 ? 0.31883 0.28117 0.30422 -0.00306 -0.04551 0.07609  119 GLU A OE2 
1896 N  N   . ALA A 120 ? 0.28168 0.11186 0.20458 0.01072  -0.02779 -0.00970 120 ALA A N   
1897 C  CA  . ALA A 120 ? 0.28976 0.10256 0.19317 0.00599  -0.01247 -0.02498 120 ALA A CA  
1898 C  C   . ALA A 120 ? 0.29184 0.11781 0.18009 0.00347  -0.00308 0.00107  120 ALA A C   
1899 O  O   . ALA A 120 ? 0.28920 0.13834 0.19958 -0.00127 -0.02037 0.00954  120 ALA A O   
1900 C  CB  . ALA A 120 ? 0.30504 0.17227 0.20099 0.02815  -0.00224 -0.03691 120 ALA A CB  
1906 N  N   . THR A 121 ? 0.26977 0.11294 0.16274 0.01567  -0.00583 0.00906  121 THR A N   
1907 C  CA  . THR A 121 ? 0.28645 0.09926 0.17152 0.00086  -0.01014 0.00514  121 THR A CA  
1908 C  C   . THR A 121 ? 0.26336 0.10195 0.19324 0.00057  -0.01664 -0.00067 121 THR A C   
1909 O  O   . THR A 121 ? 0.27906 0.09757 0.20747 -0.00229 -0.00045 0.00284  121 THR A O   
1910 C  CB  . THR A 121 ? 0.29492 0.09180 0.16663 -0.00659 -0.01635 0.00097  121 THR A CB  
1911 O  OG1 . THR A 121 ? 0.29776 0.12640 0.15724 0.02250  -0.00902 0.00963  121 THR A OG1 
1912 C  CG2 . THR A 121 ? 0.27669 0.13290 0.17703 0.01421  -0.01371 0.00639  121 THR A CG2 
1920 N  N   . THR A 122 ? 0.25486 0.10251 0.18828 0.00800  -0.01192 -0.01032 122 THR A N   
1921 C  CA  . THR A 122 ? 0.25744 0.10396 0.19361 0.00437  -0.00291 0.00362  122 THR A CA  
1922 C  C   . THR A 122 ? 0.26417 0.07896 0.18826 0.00465  0.00135  0.01068  122 THR A C   
1923 O  O   . THR A 122 ? 0.28769 0.10124 0.17157 0.02449  -0.01286 -0.01034 122 THR A O   
1924 C  CB  . THR A 122 ? 0.25299 0.08806 0.20931 0.00759  -0.00850 -0.00845 122 THR A CB  
1925 O  OG1 . THR A 122 ? 0.26816 0.10415 0.21312 0.01618  -0.00190 0.00095  122 THR A OG1 
1926 C  CG2 . THR A 122 ? 0.26770 0.12955 0.20787 -0.00577 -0.02767 0.00700  122 THR A CG2 
1934 N  N   A GLY A 123 ? 0.25630 0.08697 0.19868 -0.00730 0.02175  0.00802  123 GLY A N   
1935 N  N   B GLY A 123 ? 0.25627 0.08688 0.19857 -0.00743 0.02182  0.00808  123 GLY A N   
1936 C  CA  A GLY A 123 ? 0.26623 0.10565 0.20745 0.00940  0.01012  -0.00508 123 GLY A CA  
1937 C  CA  B GLY A 123 ? 0.26616 0.10536 0.20732 0.00935  0.01008  -0.00517 123 GLY A CA  
1938 C  C   A GLY A 123 ? 0.27649 0.11500 0.21308 0.03966  0.01995  0.01468  123 GLY A C   
1939 C  C   B GLY A 123 ? 0.27641 0.11455 0.21295 0.03985  0.01994  0.01476  123 GLY A C   
1940 O  O   A GLY A 123 ? 0.32251 0.10113 0.21786 0.00303  0.01609  0.01591  123 GLY A O   
1941 O  O   B GLY A 123 ? 0.32275 0.10064 0.21767 0.00302  0.01596  0.01619  123 GLY A O   
1948 N  N   . SER A 124 ? 0.25690 0.18851 0.19561 0.03906  0.00603  0.04230  124 SER A N   
1949 C  CA  . SER A 124 ? 0.26952 0.19451 0.20517 0.03234  -0.00371 0.03799  124 SER A CA  
1950 C  C   . SER A 124 ? 0.27077 0.21367 0.20121 -0.00871 0.02141  0.01302  124 SER A C   
1951 O  O   . SER A 124 ? 0.27936 0.18851 0.19186 0.00048  0.01867  0.01431  124 SER A O   
1952 C  CB  . SER A 124 ? 0.28576 0.20394 0.21348 0.05244  -0.00492 0.02832  124 SER A CB  
1953 O  OG  . SER A 124 ? 0.29302 0.18851 0.22548 0.01622  0.00005  0.02975  124 SER A OG  
1960 N  N   . ILE A 125 ? 0.30907 0.14886 0.19467 -0.00662 0.02818  -0.03034 125 ILE A N   
1961 C  CA  . ILE A 125 ? 0.31594 0.12633 0.20128 0.02703  0.01628  -0.02722 125 ILE A CA  
1962 C  C   . ILE A 125 ? 0.34336 0.13110 0.20160 0.02890  -0.00085 -0.01864 125 ILE A C   
1963 O  O   . ILE A 125 ? 0.35407 0.19733 0.20155 0.01613  0.00414  -0.00617 125 ILE A O   
1964 C  CB  . ILE A 125 ? 0.31200 0.11633 0.19367 0.02793  0.01813  -0.00301 125 ILE A CB  
1965 C  CG1 . ILE A 125 ? 0.33067 0.13420 0.19720 0.01373  0.02194  -0.00942 125 ILE A CG1 
1966 C  CG2 . ILE A 125 ? 0.31214 0.14379 0.20130 0.02942  0.01451  0.00822  125 ILE A CG2 
1967 C  CD1 . ILE A 125 ? 0.36032 0.13799 0.21207 -0.00182 0.01795  -0.01252 125 ILE A CD1 
1979 N  N   . THR A 126 ? 0.38446 0.16868 0.19934 0.02741  -0.02468 -0.01875 126 THR A N   
1980 C  CA  . THR A 126 ? 0.44235 0.19239 0.20348 0.03458  -0.05232 -0.02128 126 THR A CA  
1981 C  C   . THR A 126 ? 0.40868 0.18213 0.19783 0.05113  -0.01287 -0.00999 126 THR A C   
1982 O  O   . THR A 126 ? 0.40306 0.22145 0.21298 0.06369  0.00786  -0.00277 126 THR A O   
1983 C  CB  . THR A 126 ? 0.53367 0.24764 0.22887 0.01945  -0.08459 -0.02416 126 THR A CB  
1984 O  OG1 . THR A 126 ? 0.57736 0.25357 0.25942 0.01689  -0.08736 -0.01639 126 THR A OG1 
1985 C  CG2 . THR A 126 ? 0.56106 0.27704 0.24540 0.03797  -0.08640 -0.02872 126 THR A CG2 
1993 N  N   . THR A 127 ? 0.38861 0.13788 0.18932 0.02291  -0.00199 -0.01841 127 THR A N   
1994 C  CA  . THR A 127 ? 0.36523 0.16510 0.19329 0.02427  0.00342  -0.01589 127 THR A CA  
1995 C  C   . THR A 127 ? 0.35635 0.15103 0.19999 0.00997  -0.00115 -0.01858 127 THR A C   
1996 O  O   . THR A 127 ? 0.36849 0.16951 0.21370 -0.00302 0.00631  -0.02571 127 THR A O   
1997 C  CB  . THR A 127 ? 0.35016 0.16686 0.19219 0.00878  0.00434  -0.00669 127 THR A CB  
1998 O  OG1 . THR A 127 ? 0.35678 0.14485 0.18969 0.02305  -0.00381 -0.01267 127 THR A OG1 
1999 C  CG2 . THR A 127 ? 0.35328 0.22298 0.19507 -0.00903 0.00388  -0.03416 127 THR A CG2 
2007 N  N   . SER A 128 ? 0.36273 0.17514 0.19138 0.02607  -0.01826 -0.02163 128 SER A N   
2008 C  CA  . SER A 128 ? 0.37220 0.16631 0.20221 0.01410  -0.02463 -0.02220 128 SER A CA  
2009 C  C   . SER A 128 ? 0.35549 0.15048 0.21714 0.02801  -0.03209 -0.01315 128 SER A C   
2010 O  O   . SER A 128 ? 0.34330 0.15941 0.21046 0.00802  -0.03502 -0.01630 128 SER A O   
2011 C  CB  . SER A 128 ? 0.40051 0.16741 0.19866 0.02365  -0.03005 -0.00965 128 SER A CB  
2012 O  OG  . SER A 128 ? 0.41437 0.19132 0.19060 0.03643  -0.02404 0.00929  128 SER A OG  
2018 N  N   . ASP A 129 ? 0.35669 0.16617 0.23284 -0.00239 -0.05253 -0.02448 129 ASP A N   
2019 C  CA  . ASP A 129 ? 0.37346 0.21769 0.24819 0.02685  -0.05250 -0.02788 129 ASP A CA  
2020 C  C   . ASP A 129 ? 0.34993 0.17825 0.22668 0.01313  -0.04827 -0.01097 129 ASP A C   
2021 O  O   . ASP A 129 ? 0.34626 0.15655 0.22568 -0.00467 -0.04716 -0.00121 129 ASP A O   
2022 C  CB  . ASP A 129 ? 0.42137 0.27258 0.28900 0.03376  -0.05019 -0.02762 129 ASP A CB  
2023 C  CG  . ASP A 129 ? 0.47033 0.33311 0.31059 0.02937  -0.06785 -0.01492 129 ASP A CG  
2024 O  OD1 . ASP A 129 ? 0.48567 0.37673 0.32956 0.05195  -0.05491 -0.01714 129 ASP A OD1 
2025 O  OD2 . ASP A 129 ? 0.52027 0.38228 0.32213 -0.00119 -0.06262 -0.00268 129 ASP A OD2 
2030 N  N   . HIS A 130 ? 0.37473 0.16885 0.22066 -0.01177 -0.03500 -0.01718 130 HIS A N   
2031 C  CA  . HIS A 130 ? 0.40007 0.18530 0.21267 -0.00131 -0.02723 -0.00925 130 HIS A CA  
2032 C  C   . HIS A 130 ? 0.37791 0.17102 0.19376 -0.00742 -0.01710 -0.00134 130 HIS A C   
2033 O  O   . HIS A 130 ? 0.40016 0.16018 0.18064 -0.00448 -0.02124 0.00759  130 HIS A O   
2034 C  CB  . HIS A 130 ? 0.47439 0.28211 0.25418 -0.01400 -0.01545 0.00814  130 HIS A CB  
2035 C  CG  . HIS A 130 ? 0.56399 0.37387 0.30600 0.01744  0.00020  0.04186  130 HIS A CG  
2036 N  ND1 . HIS A 130 ? 0.62358 0.42796 0.33464 0.02483  -0.00289 0.04631  130 HIS A ND1 
2037 C  CD2 . HIS A 130 ? 0.59932 0.39998 0.34019 0.03055  0.00741  0.05923  130 HIS A CD2 
2038 C  CE1 . HIS A 130 ? 0.63737 0.42167 0.35227 0.03080  0.00619  0.06068  130 HIS A CE1 
2039 N  NE2 . HIS A 130 ? 0.61957 0.42102 0.36347 0.04697  0.00231  0.08447  130 HIS A NE2 
2047 N  N   . GLN A 131 ? 0.37968 0.16168 0.18821 0.00065  -0.00618 -0.00436 131 GLN A N   
2048 C  CA  . GLN A 131 ? 0.36241 0.17330 0.18621 -0.00600 0.01663  -0.00677 131 GLN A CA  
2049 C  C   . GLN A 131 ? 0.33068 0.13088 0.17535 0.00292  0.00404  -0.00379 131 GLN A C   
2050 O  O   . GLN A 131 ? 0.33502 0.14891 0.17498 -0.01270 -0.00969 -0.00860 131 GLN A O   
2051 C  CB  . GLN A 131 ? 0.38808 0.20045 0.20543 0.01644  0.03467  -0.01182 131 GLN A CB  
2052 C  CG  . GLN A 131 ? 0.44394 0.26282 0.23644 0.02877  0.05815  -0.01310 131 GLN A CG  
2053 C  CD  . GLN A 131 ? 0.47532 0.27938 0.26042 0.02848  0.08997  -0.01829 131 GLN A CD  
2054 O  OE1 . GLN A 131 ? 0.47250 0.24637 0.25289 0.01753  0.08085  0.01243  131 GLN A OE1 
2055 N  NE2 . GLN A 131 ? 0.54053 0.32106 0.29632 0.03272  0.08691  -0.03194 131 GLN A NE2 
2064 N  N   . LYS A 132 ? 0.31716 0.15036 0.16879 -0.02139 -0.00467 -0.00373 132 LYS A N   
2065 C  CA  . LYS A 132 ? 0.31168 0.11905 0.16765 0.01923  -0.00204 0.00273  132 LYS A CA  
2066 C  C   . LYS A 132 ? 0.30811 0.13001 0.16675 0.00328  -0.01742 0.00889  132 LYS A C   
2067 O  O   . LYS A 132 ? 0.30004 0.13433 0.17439 0.00050  -0.02706 0.00691  132 LYS A O   
2068 C  CB  . LYS A 132 ? 0.31300 0.12864 0.17305 0.00866  -0.00703 0.00767  132 LYS A CB  
2069 C  CG  . LYS A 132 ? 0.31867 0.14187 0.18354 -0.00115 0.00863  0.00132  132 LYS A CG  
2070 C  CD  . LYS A 132 ? 0.32089 0.14753 0.20699 -0.01386 0.01828  -0.00536 132 LYS A CD  
2071 C  CE  . LYS A 132 ? 0.33424 0.13443 0.21360 -0.02712 0.00849  -0.02173 132 LYS A CE  
2072 N  NZ  . LYS A 132 ? 0.34932 0.14775 0.21772 -0.01257 0.01366  -0.01396 132 LYS A NZ  
2086 N  N   . LYS A 133 ? 0.32117 0.12080 0.16970 0.00182  -0.02121 0.00547  133 LYS A N   
2087 C  CA  . LYS A 133 ? 0.31816 0.12937 0.17092 0.01309  -0.01933 0.01215  133 LYS A CA  
2088 C  C   . LYS A 133 ? 0.31734 0.13085 0.17359 0.01668  -0.02430 0.00663  133 LYS A C   
2089 O  O   . LYS A 133 ? 0.33739 0.14190 0.18242 0.00571  -0.03052 -0.01042 133 LYS A O   
2090 C  CB  . LYS A 133 ? 0.35334 0.15840 0.19005 0.03121  -0.01150 0.03145  133 LYS A CB  
2091 C  CG  . LYS A 133 ? 0.36118 0.22468 0.20647 0.01488  -0.02558 0.00335  133 LYS A CG  
2092 C  CD  . LYS A 133 ? 0.39048 0.28190 0.21932 0.02445  -0.02239 0.02241  133 LYS A CD  
2093 C  CE  . LYS A 133 ? 0.42706 0.34254 0.23238 0.03159  -0.02925 0.02227  133 LYS A CE  
2094 N  NZ  . LYS A 133 ? 0.47295 0.39440 0.24986 0.03811  -0.02250 0.02146  133 LYS A NZ  
2108 N  N   . THR A 134 ? 0.30794 0.16445 0.18197 -0.00601 -0.01743 0.01932  134 THR A N   
2109 C  CA  . THR A 134 ? 0.31658 0.15736 0.18269 -0.00169 -0.01632 0.02276  134 THR A CA  
2110 C  C   . THR A 134 ? 0.32196 0.13851 0.17461 -0.01255 -0.00807 0.02267  134 THR A C   
2111 O  O   . THR A 134 ? 0.32442 0.12632 0.17477 -0.03151 -0.01894 0.01806  134 THR A O   
2112 C  CB  . THR A 134 ? 0.34328 0.20570 0.18474 -0.03277 -0.00701 0.01312  134 THR A CB  
2113 O  OG1 . THR A 134 ? 0.39269 0.24246 0.18053 -0.03426 -0.00705 0.03166  134 THR A OG1 
2114 C  CG2 . THR A 134 ? 0.37471 0.23310 0.19935 -0.02890 0.00142  -0.00430 134 THR A CG2 
2122 N  N   . LEU A 135 ? 0.30867 0.13175 0.17671 -0.00821 0.00762  0.01179  135 LEU A N   
2123 C  CA  . LEU A 135 ? 0.29492 0.11055 0.17637 -0.00068 0.00014  -0.00018 135 LEU A CA  
2124 C  C   . LEU A 135 ? 0.29340 0.10753 0.17882 0.01823  -0.01612 0.01010  135 LEU A C   
2125 O  O   . LEU A 135 ? 0.29576 0.12612 0.17665 -0.01301 -0.01932 -0.00140 135 LEU A O   
2126 C  CB  . LEU A 135 ? 0.29577 0.10901 0.18103 0.00726  0.00917  0.00002  135 LEU A CB  
2127 C  CG  . LEU A 135 ? 0.31357 0.12093 0.19602 -0.00103 0.00963  -0.00272 135 LEU A CG  
2128 C  CD1 . LEU A 135 ? 0.32576 0.16307 0.20776 0.02158  0.02984  -0.00674 135 LEU A CD1 
2129 C  CD2 . LEU A 135 ? 0.34168 0.18058 0.21222 0.00983  0.01525  -0.01395 135 LEU A CD2 
2141 N  N   . ALA A 136 ? 0.28116 0.11208 0.17389 0.00062  -0.00728 0.01114  136 ALA A N   
2142 C  CA  . ALA A 136 ? 0.28288 0.11881 0.18170 -0.00402 -0.00605 0.00449  136 ALA A CA  
2143 C  C   . ALA A 136 ? 0.29407 0.13145 0.18771 -0.00609 -0.00562 0.00970  136 ALA A C   
2144 O  O   . ALA A 136 ? 0.32762 0.12192 0.19076 0.00372  -0.00945 -0.00377 136 ALA A O   
2145 C  CB  . ALA A 136 ? 0.29691 0.12890 0.18289 0.01149  0.00425  0.01468  136 ALA A CB  
2151 N  N   . ARG A 137 ? 0.31912 0.11663 0.20567 0.01675  -0.01448 0.01744  137 ARG A N   
2152 C  CA  . ARG A 137 ? 0.35165 0.11519 0.22793 -0.00386 -0.01565 0.02932  137 ARG A CA  
2153 C  C   . ARG A 137 ? 0.35296 0.09333 0.22831 -0.00978 -0.00051 0.00859  137 ARG A C   
2154 O  O   . ARG A 137 ? 0.38088 0.12550 0.25520 0.00580  -0.00165 -0.00681 137 ARG A O   
2155 C  CB  . ARG A 137 ? 0.41171 0.12718 0.25504 0.00122  -0.01651 0.05569  137 ARG A CB  
2156 C  CG  . ARG A 137 ? 0.48527 0.28367 0.28570 0.00672  -0.01534 0.06786  137 ARG A CG  
2157 C  CD  . ARG A 137 ? 0.57449 0.46232 0.31981 0.03459  -0.01016 0.05768  137 ARG A CD  
2158 N  NE  . ARG A 137 ? 0.65185 0.59846 0.35065 0.04887  -0.00737 0.04504  137 ARG A NE  
2159 C  CZ  . ARG A 137 ? 0.69628 0.69631 0.37803 0.06184  -0.00752 0.04581  137 ARG A CZ  
2160 N  NH1 . ARG A 137 ? 0.71106 0.72783 0.38844 0.06650  -0.02308 0.05220  137 ARG A NH1 
2161 N  NH2 . ARG A 137 ? 0.71048 0.72320 0.38683 0.07794  0.00615  0.04222  137 ARG A NH2 
2175 N  N   . ASN A 138 ? 0.33651 0.10829 0.20428 -0.02025 -0.00416 0.00198  138 ASN A N   
2176 C  CA  . ASN A 138 ? 0.34012 0.11990 0.19024 -0.01630 0.00438  -0.00073 138 ASN A CA  
2177 C  C   . ASN A 138 ? 0.34155 0.11048 0.18195 -0.02229 0.00029  0.00949  138 ASN A C   
2178 O  O   . ASN A 138 ? 0.33673 0.13961 0.17350 -0.02335 -0.00116 0.01387  138 ASN A O   
2179 C  CB  . ASN A 138 ? 0.37134 0.16739 0.19771 -0.01683 0.02113  -0.00351 138 ASN A CB  
2180 C  CG  . ASN A 138 ? 0.44073 0.19095 0.21352 -0.04406 0.02484  -0.00692 138 ASN A CG  
2181 O  OD1 . ASN A 138 ? 0.47577 0.25155 0.22836 -0.02435 0.01298  0.01555  138 ASN A OD1 
2182 N  ND2 . ASN A 138 ? 0.48769 0.22239 0.21725 -0.05578 0.02776  -0.00727 138 ASN A ND2 
2189 N  N   . SER A 139 ? 0.33716 0.09616 0.18683 0.01148  0.00360  0.00666  139 SER A N   
2190 C  CA  . SER A 139 ? 0.30968 0.08566 0.17992 -0.00319 0.00482  0.00999  139 SER A CA  
2191 C  C   . SER A 139 ? 0.30708 0.11025 0.18480 -0.00777 0.00095  0.01340  139 SER A C   
2192 O  O   . SER A 139 ? 0.29246 0.10881 0.18752 0.00560  0.00245  0.00580  139 SER A O   
2193 C  CB  . SER A 139 ? 0.32272 0.11064 0.18977 0.00720  -0.00314 0.00759  139 SER A CB  
2194 O  OG  . SER A 139 ? 0.34030 0.10181 0.17936 0.01570  -0.00492 0.00724  139 SER A OG  
2200 N  N   . ILE A 140 ? 0.30623 0.10206 0.19054 0.00573  -0.01454 0.00195  140 ILE A N   
2201 C  CA  . ILE A 140 ? 0.31915 0.11528 0.19269 -0.00340 -0.00641 -0.01579 140 ILE A CA  
2202 C  C   . ILE A 140 ? 0.33675 0.09964 0.19622 -0.01445 -0.00434 -0.00881 140 ILE A C   
2203 O  O   . ILE A 140 ? 0.32973 0.12583 0.20125 -0.00482 -0.01365 0.00496  140 ILE A O   
2204 C  CB  . ILE A 140 ? 0.33580 0.10472 0.20860 -0.00080 -0.01242 -0.02217 140 ILE A CB  
2205 C  CG1 . ILE A 140 ? 0.33051 0.12575 0.22829 0.03241  -0.00791 0.00238  140 ILE A CG1 
2206 C  CG2 . ILE A 140 ? 0.33940 0.13916 0.21321 0.01688  -0.01469 -0.03378 140 ILE A CG2 
2207 C  CD1 . ILE A 140 ? 0.36658 0.18245 0.24403 0.00117  0.00850  0.00584  140 ILE A CD1 
2219 N  N   . SER A 141 ? 0.34624 0.08924 0.19546 -0.01999 -0.00985 -0.00735 141 SER A N   
2220 C  CA  . SER A 141 ? 0.34622 0.10472 0.19538 -0.03642 -0.00359 0.01940  141 SER A CA  
2221 C  C   . SER A 141 ? 0.32051 0.10415 0.20066 -0.03458 0.00095  0.00860  141 SER A C   
2222 O  O   . SER A 141 ? 0.32245 0.12021 0.20260 -0.02140 -0.00396 0.01360  141 SER A O   
2223 C  CB  . SER A 141 ? 0.38100 0.17857 0.21019 -0.02942 0.00628  0.04648  141 SER A CB  
2224 O  OG  . SER A 141 ? 0.43290 0.23765 0.22707 -0.04891 0.00037  0.02158  141 SER A OG  
2230 N  N   . TYR A 142 ? 0.31296 0.10736 0.19514 -0.01600 0.01570  0.01276  142 TYR A N   
2231 C  CA  . TYR A 142 ? 0.29478 0.11210 0.20385 -0.00290 0.00893  -0.00437 142 TYR A CA  
2232 C  C   . TYR A 142 ? 0.28937 0.10072 0.20338 -0.00866 0.00358  0.00118  142 TYR A C   
2233 O  O   . TYR A 142 ? 0.30112 0.10470 0.20767 -0.03305 0.01532  0.01046  142 TYR A O   
2234 C  CB  . TYR A 142 ? 0.30484 0.11876 0.22024 -0.02227 0.00252  -0.01409 142 TYR A CB  
2235 C  CG  . TYR A 142 ? 0.29389 0.10048 0.24138 -0.01726 0.01232  -0.01016 142 TYR A CG  
2236 C  CD1 . TYR A 142 ? 0.28840 0.09399 0.24648 -0.02183 0.01001  0.00252  142 TYR A CD1 
2237 C  CD2 . TYR A 142 ? 0.31815 0.11278 0.26490 0.00135  0.01344  0.00111  142 TYR A CD2 
2238 C  CE1 . TYR A 142 ? 0.30853 0.10131 0.26380 -0.00726 0.00452  -0.01085 142 TYR A CE1 
2239 C  CE2 . TYR A 142 ? 0.31925 0.10793 0.28644 -0.00743 0.01927  0.00332  142 TYR A CE2 
2240 C  CZ  . TYR A 142 ? 0.31406 0.11616 0.28718 0.00411  0.00607  -0.00436 142 TYR A CZ  
2241 O  OH  . TYR A 142 ? 0.33894 0.12777 0.31482 -0.01068 0.00668  0.00837  142 TYR A OH  
2251 N  N   . ASN A 143 ? 0.27499 0.11023 0.19906 -0.00209 0.00393  0.00389  143 ASN A N   
2252 C  CA  . ASN A 143 ? 0.26838 0.10651 0.19562 -0.03018 -0.00557 -0.00027 143 ASN A CA  
2253 C  C   . ASN A 143 ? 0.27394 0.09766 0.20470 -0.01758 -0.00080 0.00646  143 ASN A C   
2254 O  O   . ASN A 143 ? 0.30308 0.10564 0.21925 -0.02409 -0.01200 0.01091  143 ASN A O   
2255 C  CB  . ASN A 143 ? 0.26760 0.09973 0.18204 -0.02071 -0.00170 -0.01330 143 ASN A CB  
2256 C  CG  . ASN A 143 ? 0.28353 0.11990 0.17576 -0.01710 0.00795  -0.01664 143 ASN A CG  
2257 O  OD1 . ASN A 143 ? 0.29182 0.11210 0.17125 -0.01611 0.00991  -0.00930 143 ASN A OD1 
2258 N  ND2 . ASN A 143 ? 0.27739 0.10582 0.18137 -0.02012 0.00877  -0.01051 143 ASN A ND2 
2265 N  N   . THR A 144 ? 0.30081 0.08368 0.21081 -0.00846 -0.00121 0.00395  144 THR A N   
2266 C  CA  . THR A 144 ? 0.30572 0.07716 0.23414 -0.01015 0.00396  -0.00432 144 THR A CA  
2267 C  C   . THR A 144 ? 0.29523 0.13264 0.25305 -0.04019 -0.00214 -0.01200 144 THR A C   
2268 O  O   . THR A 144 ? 0.31242 0.16854 0.25943 -0.05595 0.00220  -0.00712 144 THR A O   
2269 C  CB  . THR A 144 ? 0.32235 0.11335 0.23778 -0.01031 0.00382  -0.00020 144 THR A CB  
2270 O  OG1 . THR A 144 ? 0.31998 0.10275 0.22035 -0.00580 -0.00231 -0.02108 144 THR A OG1 
2271 C  CG2 . THR A 144 ? 0.33370 0.10655 0.24739 -0.02144 0.00591  0.00544  144 THR A CG2 
2279 N  N   . PHE A 145 ? 0.29565 0.14532 0.26635 -0.00174 0.00999  0.00028  145 PHE A N   
2280 C  CA  . PHE A 145 ? 0.31081 0.15967 0.28176 -0.00598 0.00274  0.00663  145 PHE A CA  
2281 C  C   . PHE A 145 ? 0.29632 0.17803 0.31175 -0.00505 0.01071  0.00683  145 PHE A C   
2282 O  O   . PHE A 145 ? 0.34401 0.23840 0.35615 -0.00059 -0.00504 -0.01383 145 PHE A O   
2283 C  CB  . PHE A 145 ? 0.33302 0.17611 0.27932 -0.01459 0.02132  0.01055  145 PHE A CB  
2284 C  CG  . PHE A 145 ? 0.35104 0.15635 0.28401 -0.02121 0.01838  0.01572  145 PHE A CG  
2285 C  CD1 . PHE A 145 ? 0.37074 0.13439 0.29238 -0.02706 0.01219  0.02940  145 PHE A CD1 
2286 C  CD2 . PHE A 145 ? 0.34805 0.14725 0.28871 -0.03374 0.01899  0.02611  145 PHE A CD2 
2287 C  CE1 . PHE A 145 ? 0.37074 0.15167 0.29844 -0.02106 0.00690  0.02341  145 PHE A CE1 
2288 C  CE2 . PHE A 145 ? 0.36008 0.15341 0.28856 -0.02158 0.01657  0.02358  145 PHE A CE2 
2289 C  CZ  . PHE A 145 ? 0.37324 0.15505 0.29474 -0.00618 0.00969  0.02920  145 PHE A CZ  
2299 N  N   . GLN A 146 ? 0.28104 0.14926 0.29038 -0.00406 0.02607  0.02180  146 GLN A N   
2300 C  CA  . GLN A 146 ? 0.33166 0.18317 0.28736 0.03212  0.05897  0.04417  146 GLN A CA  
2301 C  C   . GLN A 146 ? 0.38402 0.17099 0.27832 0.04862  0.07043  0.04185  146 GLN A C   
2302 O  O   . GLN A 146 ? 0.47216 0.26461 0.29561 0.12109  0.09459  0.07427  146 GLN A O   
2303 C  CB  . GLN A 146 ? 0.39520 0.21425 0.29662 0.06562  0.07038  0.04173  146 GLN A CB  
2304 C  CG  . GLN A 146 ? 0.49352 0.30203 0.32413 0.04833  0.07237  0.05040  146 GLN A CG  
2305 C  CD  . GLN A 146 ? 0.59113 0.38136 0.35237 0.05995  0.07247  0.05043  146 GLN A CD  
2306 O  OE1 . GLN A 146 ? 0.65622 0.40935 0.36580 0.05345  0.05978  0.05157  146 GLN A OE1 
2307 N  NE2 . GLN A 146 ? 0.60332 0.41493 0.35933 0.07143  0.08931  0.03583  146 GLN A NE2 
2316 N  N   . ASN A 147 ? 0.36583 0.15112 0.26581 0.01981  0.07384  0.02305  147 ASN A N   
2317 C  CA  . ASN A 147 ? 0.34032 0.14785 0.25207 0.03608  0.04862  0.02744  147 ASN A CA  
2318 C  C   . ASN A 147 ? 0.30232 0.16967 0.26570 0.01922  0.03464  0.03981  147 ASN A C   
2319 O  O   . ASN A 147 ? 0.30711 0.13676 0.26100 0.00742  0.02658  0.02769  147 ASN A O   
2320 C  CB  . ASN A 147 ? 0.31280 0.13186 0.22428 0.04678  0.02825  0.02180  147 ASN A CB  
2321 C  CG  . ASN A 147 ? 0.29683 0.14185 0.20140 0.03049  0.02205  0.00940  147 ASN A CG  
2322 O  OD1 . ASN A 147 ? 0.28416 0.15175 0.20866 0.00126  0.00813  -0.00137 147 ASN A OD1 
2323 N  ND2 . ASN A 147 ? 0.30611 0.14882 0.18856 0.02329  0.01439  0.01226  147 ASN A ND2 
2330 N  N   . VAL A 148 ? 0.29607 0.18949 0.28503 -0.00116 0.04198  0.06184  148 VAL A N   
2331 C  CA  . VAL A 148 ? 0.30253 0.26575 0.30525 -0.00646 0.02142  0.06413  148 VAL A CA  
2332 C  C   . VAL A 148 ? 0.30748 0.21263 0.30030 0.00574  -0.00347 0.02411  148 VAL A C   
2333 O  O   . VAL A 148 ? 0.31755 0.18774 0.32079 -0.00736 -0.02163 -0.00066 148 VAL A O   
2334 C  CB  . VAL A 148 ? 0.33066 0.41352 0.32252 0.00384  0.01717  0.07716  148 VAL A CB  
2335 C  CG1 . VAL A 148 ? 0.34901 0.48685 0.32721 0.01850  0.01202  0.08020  148 VAL A CG1 
2336 C  CG2 . VAL A 148 ? 0.35835 0.43566 0.33757 0.00550  0.01993  0.07351  148 VAL A CG2 
2346 N  N   . ARG A 149 ? 0.30557 0.15781 0.27880 0.00958  0.00557  0.02105  149 ARG A N   
2347 C  CA  . ARG A 149 ? 0.29023 0.13013 0.25893 0.01907  -0.01185 0.01117  149 ARG A CA  
2348 C  C   . ARG A 149 ? 0.28675 0.13904 0.23907 0.01452  -0.01426 0.00548  149 ARG A C   
2349 O  O   . ARG A 149 ? 0.31078 0.14358 0.23519 -0.00342 -0.00964 -0.01853 149 ARG A O   
2350 C  CB  . ARG A 149 ? 0.31040 0.11893 0.26783 0.01628  -0.00029 0.00941  149 ARG A CB  
2351 C  CG  . ARG A 149 ? 0.33932 0.12129 0.27910 0.02518  -0.01101 0.00396  149 ARG A CG  
2352 C  CD  . ARG A 149 ? 0.36069 0.16568 0.29761 0.01675  -0.01057 -0.00578 149 ARG A CD  
2353 N  NE  . ARG A 149 ? 0.37431 0.18897 0.31449 -0.01786 -0.01884 -0.01861 149 ARG A NE  
2354 C  CZ  . ARG A 149 ? 0.38362 0.17792 0.33312 0.02574  -0.01545 -0.00314 149 ARG A CZ  
2355 N  NH1 . ARG A 149 ? 0.40426 0.17508 0.34915 0.02069  -0.00649 0.00087  149 ARG A NH1 
2356 N  NH2 . ARG A 149 ? 0.38234 0.17360 0.34073 0.01354  -0.00667 0.00234  149 ARG A NH2 
2370 N  N   . PHE A 150 ? 0.29567 0.13308 0.22612 0.00203  -0.02183 0.01639  150 PHE A N   
2371 C  CA  . PHE A 150 ? 0.27322 0.16558 0.22260 0.00553  -0.01531 -0.00501 150 PHE A CA  
2372 C  C   . PHE A 150 ? 0.26767 0.17081 0.24564 -0.00602 -0.00782 0.00523  150 PHE A C   
2373 O  O   . PHE A 150 ? 0.28133 0.17561 0.24113 0.00074  -0.01155 -0.00822 150 PHE A O   
2374 C  CB  . PHE A 150 ? 0.27879 0.14923 0.21123 0.01609  -0.00532 -0.00383 150 PHE A CB  
2375 C  CG  . PHE A 150 ? 0.27029 0.10134 0.19888 0.01173  -0.00760 -0.00093 150 PHE A CG  
2376 C  CD1 . PHE A 150 ? 0.28271 0.10669 0.19880 0.00732  -0.01185 -0.00630 150 PHE A CD1 
2377 C  CD2 . PHE A 150 ? 0.29598 0.08391 0.21047 0.01058  -0.00563 0.00300  150 PHE A CD2 
2378 C  CE1 . PHE A 150 ? 0.30020 0.08987 0.20749 0.00703  -0.01546 0.00589  150 PHE A CE1 
2379 C  CE2 . PHE A 150 ? 0.27792 0.11536 0.20465 -0.01906 0.00175  -0.00920 150 PHE A CE2 
2380 C  CZ  . PHE A 150 ? 0.28955 0.10073 0.20634 -0.00002 -0.00484 -0.00956 150 PHE A CZ  
2390 N  N   . LYS A 151 ? 0.29840 0.13685 0.28221 -0.01808 -0.00013 0.00630  151 LYS A N   
2391 C  CA  . LYS A 151 ? 0.30851 0.16324 0.31939 0.01706  0.00160  -0.00868 151 LYS A CA  
2392 C  C   . LYS A 151 ? 0.31170 0.19483 0.32789 -0.00057 -0.02245 -0.03883 151 LYS A C   
2393 O  O   . LYS A 151 ? 0.33630 0.21853 0.33847 -0.00016 -0.03919 -0.07632 151 LYS A O   
2394 C  CB  . LYS A 151 ? 0.36798 0.23909 0.33660 -0.00346 0.03339  0.00551  151 LYS A CB  
2395 C  CG  . LYS A 151 ? 0.45366 0.35789 0.36073 -0.00131 0.05625  0.02983  151 LYS A CG  
2396 C  CD  . LYS A 151 ? 0.52362 0.46814 0.37337 0.01688  0.05123  0.03677  151 LYS A CD  
2397 C  CE  . LYS A 151 ? 0.55263 0.53402 0.37543 0.01705  0.05489  0.03230  151 LYS A CE  
2398 N  NZ  . LYS A 151 ? 0.57022 0.56724 0.38119 -0.00718 0.04027  0.02275  151 LYS A NZ  
2412 N  N   . LEU A 152 ? 0.30049 0.17738 0.32124 -0.00139 -0.03721 -0.04136 152 LEU A N   
2413 C  CA  . LEU A 152 ? 0.31383 0.21618 0.31387 0.00235  -0.05190 -0.05245 152 LEU A CA  
2414 C  C   . LEU A 152 ? 0.30875 0.20229 0.29116 0.01263  -0.05069 -0.04776 152 LEU A C   
2415 O  O   . LEU A 152 ? 0.33920 0.21650 0.29215 -0.01985 -0.04722 -0.06456 152 LEU A O   
2416 C  CB  . LEU A 152 ? 0.33703 0.31228 0.33831 0.03506  -0.05667 -0.04682 152 LEU A CB  
2417 C  CG  . LEU A 152 ? 0.39758 0.39072 0.36398 0.04150  -0.06163 -0.04825 152 LEU A CG  
2418 C  CD1 . LEU A 152 ? 0.40893 0.41153 0.37612 0.05474  -0.06152 -0.03435 152 LEU A CD1 
2419 C  CD2 . LEU A 152 ? 0.40753 0.44235 0.37249 0.04150  -0.06341 -0.05071 152 LEU A CD2 
2431 N  N   . ILE A 153 ? 0.30821 0.14715 0.26374 -0.01007 -0.04855 -0.02664 153 ILE A N   
2432 C  CA  . ILE A 153 ? 0.32304 0.12712 0.23361 -0.00306 -0.04157 -0.03468 153 ILE A CA  
2433 C  C   . ILE A 153 ? 0.33188 0.10576 0.21219 0.00145  -0.03868 -0.03512 153 ILE A C   
2434 O  O   . ILE A 153 ? 0.35762 0.16419 0.21263 0.03249  -0.04794 -0.04150 153 ILE A O   
2435 C  CB  . ILE A 153 ? 0.34612 0.10824 0.23024 0.00857  -0.03163 -0.03125 153 ILE A CB  
2436 C  CG1 . ILE A 153 ? 0.34961 0.14714 0.23036 0.03252  -0.03855 -0.01920 153 ILE A CG1 
2437 C  CG2 . ILE A 153 ? 0.35755 0.13806 0.23026 0.00648  -0.01248 -0.01841 153 ILE A CG2 
2438 C  CD1 . ILE A 153 ? 0.36443 0.18726 0.23873 0.05474  -0.04688 -0.00791 153 ILE A CD1 
2450 N  N   . PHE A 154 ? 0.30657 0.12056 0.20667 0.00584  -0.02608 -0.01190 154 PHE A N   
2451 C  CA  . PHE A 154 ? 0.30089 0.12558 0.20736 0.00699  -0.02150 -0.01680 154 PHE A CA  
2452 C  C   . PHE A 154 ? 0.29021 0.13339 0.21058 -0.00199 -0.01953 -0.01754 154 PHE A C   
2453 O  O   . PHE A 154 ? 0.29881 0.13328 0.20762 0.01604  -0.01348 -0.01308 154 PHE A O   
2454 C  CB  . PHE A 154 ? 0.29295 0.10012 0.20226 0.00114  -0.01304 0.00255  154 PHE A CB  
2455 C  CG  . PHE A 154 ? 0.29278 0.08939 0.19634 0.00770  -0.01693 0.00425  154 PHE A CG  
2456 C  CD1 . PHE A 154 ? 0.31029 0.12752 0.19969 -0.00253 -0.01552 -0.00656 154 PHE A CD1 
2457 C  CD2 . PHE A 154 ? 0.30050 0.10257 0.20128 0.01915  -0.01714 0.00425  154 PHE A CD2 
2458 C  CE1 . PHE A 154 ? 0.30587 0.15263 0.19859 -0.01123 -0.01279 0.00087  154 PHE A CE1 
2459 C  CE2 . PHE A 154 ? 0.31472 0.12562 0.20473 0.02061  -0.02066 -0.00905 154 PHE A CE2 
2460 C  CZ  . PHE A 154 ? 0.31126 0.12707 0.20094 -0.00901 -0.01290 -0.00234 154 PHE A CZ  
2470 N  N   . PRO A 155 ? 0.30806 0.12493 0.21112 -0.00340 -0.01681 -0.01171 155 PRO A N   
2471 C  CA  . PRO A 155 ? 0.32463 0.13416 0.21820 -0.01478 -0.00154 -0.02381 155 PRO A CA  
2472 C  C   . PRO A 155 ? 0.33358 0.11747 0.21272 0.00962  0.00736  -0.00968 155 PRO A C   
2473 O  O   . PRO A 155 ? 0.35728 0.12455 0.22279 -0.00380 0.00642  0.00033  155 PRO A O   
2474 C  CB  . PRO A 155 ? 0.33361 0.17469 0.21779 -0.00336 -0.00608 -0.04405 155 PRO A CB  
2475 C  CG  . PRO A 155 ? 0.33455 0.17266 0.20361 0.00963  -0.01662 -0.04720 155 PRO A CG  
2476 C  CD  . PRO A 155 ? 0.32490 0.14230 0.20929 -0.00222 -0.02387 -0.03562 155 PRO A CD  
2484 N  N   . GLU A 156 ? 0.33369 0.09359 0.20661 0.00987  0.00286  -0.01524 156 GLU A N   
2485 C  CA  . GLU A 156 ? 0.32244 0.10370 0.21356 0.00317  -0.00028 -0.00119 156 GLU A CA  
2486 C  C   . GLU A 156 ? 0.31742 0.10866 0.20326 0.01867  -0.00051 -0.00073 156 GLU A C   
2487 O  O   . GLU A 156 ? 0.34846 0.11670 0.20442 0.01263  0.00880  -0.00144 156 GLU A O   
2488 C  CB  . GLU A 156 ? 0.31973 0.13148 0.22735 0.00045  0.00516  0.00501  156 GLU A CB  
2489 C  CG  . GLU A 156 ? 0.35243 0.13203 0.23664 0.02685  0.00471  0.03449  156 GLU A CG  
2490 C  CD  . GLU A 156 ? 0.39041 0.14849 0.24551 0.00669  0.01531  0.02476  156 GLU A CD  
2491 O  OE1 . GLU A 156 ? 0.40713 0.16899 0.24385 0.00434  0.00600  0.01849  156 GLU A OE1 
2492 O  OE2 . GLU A 156 ? 0.42716 0.16056 0.26427 0.02558  0.02375  0.03615  156 GLU A OE2 
2499 N  N   . VAL A 157 ? 0.29712 0.10007 0.20076 -0.01351 0.00039  -0.00713 157 VAL A N   
2500 C  CA  . VAL A 157 ? 0.27720 0.11366 0.19830 -0.02079 0.00159  0.00366  157 VAL A CA  
2501 C  C   . VAL A 157 ? 0.29758 0.10724 0.20448 0.00147  -0.00154 0.01617  157 VAL A C   
2502 O  O   . VAL A 157 ? 0.30950 0.11681 0.20973 -0.00564 -0.01689 0.01631  157 VAL A O   
2503 C  CB  . VAL A 157 ? 0.28640 0.09757 0.20273 -0.02518 0.01585  0.00070  157 VAL A CB  
2504 C  CG1 . VAL A 157 ? 0.30202 0.11814 0.20284 -0.01155 0.01102  0.00398  157 VAL A CG1 
2505 C  CG2 . VAL A 157 ? 0.30932 0.11040 0.21398 -0.00572 0.02028  0.00983  157 VAL A CG2 
2515 N  N   . VAL A 158 ? 0.29252 0.12165 0.19614 0.00068  -0.01233 0.01584  158 VAL A N   
2516 C  CA  . VAL A 158 ? 0.29348 0.11567 0.19630 -0.01236 0.00729  0.00748  158 VAL A CA  
2517 C  C   . VAL A 158 ? 0.30516 0.13406 0.19914 -0.01282 -0.00283 -0.00609 158 VAL A C   
2518 O  O   . VAL A 158 ? 0.30397 0.12083 0.19503 -0.00946 -0.01536 0.01785  158 VAL A O   
2519 C  CB  . VAL A 158 ? 0.29201 0.12393 0.20499 -0.00282 0.00481  0.01049  158 VAL A CB  
2520 C  CG1 . VAL A 158 ? 0.29238 0.13430 0.21818 -0.01785 0.00938  0.01668  158 VAL A CG1 
2521 C  CG2 . VAL A 158 ? 0.32282 0.17465 0.21806 -0.00699 0.00247  0.01380  158 VAL A CG2 
2531 N  N   . GLN A 159 ? 0.31220 0.12798 0.19447 -0.01783 0.00699  0.00026  159 GLN A N   
2532 C  CA  . GLN A 159 ? 0.32679 0.11615 0.20342 -0.02156 0.01208  -0.01528 159 GLN A CA  
2533 C  C   . GLN A 159 ? 0.32832 0.10438 0.19567 -0.01782 0.01271  -0.00666 159 GLN A C   
2534 O  O   . GLN A 159 ? 0.35094 0.10564 0.19279 0.00748  0.01608  0.00768  159 GLN A O   
2535 C  CB  . GLN A 159 ? 0.35236 0.15777 0.22834 -0.02974 0.00441  -0.02161 159 GLN A CB  
2536 C  CG  . GLN A 159 ? 0.37339 0.24302 0.25590 -0.01773 -0.01406 -0.04378 159 GLN A CG  
2537 C  CD  . GLN A 159 ? 0.40399 0.35441 0.27804 0.01608  -0.01962 -0.05329 159 GLN A CD  
2538 O  OE1 . GLN A 159 ? 0.42522 0.39032 0.28066 0.05466  -0.00312 -0.05744 159 GLN A OE1 
2539 N  NE2 . GLN A 159 ? 0.41711 0.38674 0.29067 0.01606  -0.01793 -0.05222 159 GLN A NE2 
2548 N  N   . GLU A 160 ? 0.31500 0.11725 0.20135 -0.01165 0.01083  0.00200  160 GLU A N   
2549 C  CA  . GLU A 160 ? 0.31727 0.14309 0.21247 -0.02978 0.02331  0.00750  160 GLU A CA  
2550 C  C   . GLU A 160 ? 0.30042 0.11229 0.20394 0.00165  0.01599  0.01125  160 GLU A C   
2551 O  O   . GLU A 160 ? 0.32518 0.12893 0.20696 0.02668  -0.00076 0.01949  160 GLU A O   
2552 C  CB  . GLU A 160 ? 0.33761 0.20629 0.22863 -0.01649 0.02858  0.01218  160 GLU A CB  
2553 C  CG  . GLU A 160 ? 0.36370 0.24511 0.25351 -0.03615 0.04829  0.01108  160 GLU A CG  
2554 C  CD  . GLU A 160 ? 0.38853 0.27838 0.27593 -0.08068 0.06715  0.00182  160 GLU A CD  
2555 O  OE1 . GLU A 160 ? 0.42835 0.29599 0.30827 -0.10419 0.07031  -0.00937 160 GLU A OE1 
2556 O  OE2 . GLU A 160 ? 0.40512 0.26253 0.26690 -0.09093 0.06058  0.02328  160 GLU A OE2 
2563 N  N   . ASN A 161 ? 0.29093 0.10125 0.19214 0.00528  0.00182  -0.00214 161 ASN A N   
2564 C  CA  . ASN A 161 ? 0.28934 0.07713 0.19099 -0.01047 -0.00509 0.00627  161 ASN A CA  
2565 C  C   . ASN A 161 ? 0.30057 0.07953 0.18663 -0.02261 -0.00577 -0.00390 161 ASN A C   
2566 O  O   . ASN A 161 ? 0.32316 0.10675 0.18421 -0.00269 -0.01946 -0.01046 161 ASN A O   
2567 C  CB  . ASN A 161 ? 0.29609 0.08449 0.19843 -0.04132 -0.01145 0.00886  161 ASN A CB  
2568 C  CG  . ASN A 161 ? 0.29834 0.09988 0.20166 -0.02054 -0.00721 0.00225  161 ASN A CG  
2569 O  OD1 . ASN A 161 ? 0.30393 0.10662 0.20622 -0.03809 -0.00037 -0.01289 161 ASN A OD1 
2570 N  ND2 . ASN A 161 ? 0.30526 0.10524 0.19679 -0.00173 0.00413  0.00228  161 ASN A ND2 
2577 N  N   . VAL A 162 ? 0.28157 0.08416 0.18468 -0.02367 -0.00574 -0.00549 162 VAL A N   
2578 C  CA  . VAL A 162 ? 0.27198 0.07195 0.18967 -0.02040 0.01810  -0.00852 162 VAL A CA  
2579 C  C   . VAL A 162 ? 0.30041 0.07781 0.17573 -0.01434 0.02166  -0.00904 162 VAL A C   
2580 O  O   . VAL A 162 ? 0.33794 0.09744 0.16434 0.00785  0.00792  0.00603  162 VAL A O   
2581 C  CB  . VAL A 162 ? 0.26306 0.09901 0.21070 -0.03894 0.00180  0.01527  162 VAL A CB  
2582 C  CG1 . VAL A 162 ? 0.26628 0.09788 0.22415 -0.03266 -0.00492 0.00773  162 VAL A CG1 
2583 C  CG2 . VAL A 162 ? 0.27531 0.12012 0.22334 -0.02714 0.00917  0.02534  162 VAL A CG2 
2593 N  N   . GLU A 163 ? 0.30813 0.09348 0.17893 -0.00141 0.01580  0.00407  163 GLU A N   
2594 C  CA  . GLU A 163 ? 0.28619 0.11331 0.18842 0.01729  0.00075  0.01598  163 GLU A CA  
2595 C  C   . GLU A 163 ? 0.30174 0.09600 0.20111 0.00011  -0.01582 0.01468  163 GLU A C   
2596 O  O   . GLU A 163 ? 0.29646 0.11670 0.20525 0.00745  -0.01643 0.00237  163 GLU A O   
2597 C  CB  . GLU A 163 ? 0.29781 0.10034 0.18934 0.02714  0.00019  0.01320  163 GLU A CB  
2598 C  CG  . GLU A 163 ? 0.28851 0.12375 0.19980 -0.00471 0.00824  -0.00742 163 GLU A CG  
2599 C  CD  . GLU A 163 ? 0.29207 0.09842 0.20193 -0.00146 0.00284  0.01337  163 GLU A CD  
2600 O  OE1 . GLU A 163 ? 0.31792 0.09789 0.18837 -0.00267 0.01182  0.01023  163 GLU A OE1 
2601 O  OE2 . GLU A 163 ? 0.27804 0.14188 0.20288 0.01635  0.00386  0.01205  163 GLU A OE2 
2608 N  N   . THR A 164 ? 0.29645 0.10347 0.20817 -0.02279 -0.03935 0.02269  164 THR A N   
2609 C  CA  . THR A 164 ? 0.32037 0.10037 0.21702 -0.02275 -0.03958 0.01177  164 THR A CA  
2610 C  C   . THR A 164 ? 0.34231 0.12066 0.20928 -0.00738 -0.04129 0.00889  164 THR A C   
2611 O  O   . THR A 164 ? 0.37548 0.11754 0.21270 0.01590  -0.04822 -0.00248 164 THR A O   
2612 C  CB  . THR A 164 ? 0.35016 0.11972 0.23612 -0.03644 -0.02961 -0.00229 164 THR A CB  
2613 O  OG1 . THR A 164 ? 0.36951 0.15106 0.24556 -0.05311 -0.01455 0.00842  164 THR A OG1 
2614 C  CG2 . THR A 164 ? 0.37698 0.10900 0.25012 -0.02722 -0.02729 0.00185  164 THR A CG2 
2622 N  N   . LEU A 165 ? 0.33424 0.11096 0.19546 -0.00406 -0.02590 0.00621  165 LEU A N   
2623 C  CA  . LEU A 165 ? 0.36754 0.11391 0.18678 0.01167  -0.01318 0.00071  165 LEU A CA  
2624 C  C   . LEU A 165 ? 0.37096 0.09546 0.17893 0.00546  -0.02599 -0.01239 165 LEU A C   
2625 O  O   . LEU A 165 ? 0.40717 0.11965 0.17267 0.02977  -0.02187 -0.02724 165 LEU A O   
2626 C  CB  . LEU A 165 ? 0.38379 0.13827 0.19517 0.04748  -0.00144 0.00643  165 LEU A CB  
2627 C  CG  . LEU A 165 ? 0.43153 0.16164 0.20699 0.06266  0.00062  0.00420  165 LEU A CG  
2628 C  CD1 . LEU A 165 ? 0.44316 0.19662 0.22235 0.05119  0.03263  0.01935  165 LEU A CD1 
2629 C  CD2 . LEU A 165 ? 0.48339 0.18045 0.21612 0.04363  -0.01825 -0.01422 165 LEU A CD2 
2641 N  N   . GLU A 166 ? 0.36714 0.09592 0.18140 0.01321  -0.00985 -0.01596 166 GLU A N   
2642 C  CA  . GLU A 166 ? 0.34562 0.09669 0.18626 0.02235  0.00276  -0.01241 166 GLU A CA  
2643 C  C   . GLU A 166 ? 0.36071 0.11478 0.21212 0.03298  -0.03429 0.01084  166 GLU A C   
2644 O  O   . GLU A 166 ? 0.38515 0.12181 0.19990 0.00894  -0.04352 0.00518  166 GLU A O   
2645 C  CB  . GLU A 166 ? 0.34040 0.09899 0.18918 0.01653  0.02678  -0.02525 166 GLU A CB  
2646 C  CG  . GLU A 166 ? 0.32326 0.09927 0.19597 0.00334  0.01305  -0.01134 166 GLU A CG  
2647 C  CD  . GLU A 166 ? 0.27273 0.09277 0.18947 0.02469  0.01846  -0.01657 166 GLU A CD  
2648 O  OE1 . GLU A 166 ? 0.29366 0.10854 0.18947 0.01392  -0.02236 -0.02021 166 GLU A OE1 
2649 O  OE2 . GLU A 166 ? 0.27371 0.10174 0.18442 0.02201  0.01169  -0.00185 166 GLU A OE2 
2656 N  N   . LYS A 167 ? 0.37518 0.14011 0.25803 0.02550  -0.05880 0.01957  167 LYS A N   
2657 C  CA  . LYS A 167 ? 0.41072 0.17218 0.30135 0.02472  -0.07626 0.03406  167 LYS A CA  
2658 C  C   . LYS A 167 ? 0.45006 0.17735 0.32142 0.05150  -0.11331 0.02267  167 LYS A C   
2659 O  O   . LYS A 167 ? 0.44426 0.20482 0.32655 0.05306  -0.11391 0.02549  167 LYS A O   
2660 C  CB  . LYS A 167 ? 0.41105 0.22413 0.32877 -0.01293 -0.05699 0.02896  167 LYS A CB  
2661 C  CG  . LYS A 167 ? 0.43361 0.28624 0.35082 -0.06031 -0.04090 0.01874  167 LYS A CG  
2662 C  CD  . LYS A 167 ? 0.47379 0.33713 0.37266 -0.09138 -0.03414 0.00469  167 LYS A CD  
2663 C  CE  . LYS A 167 ? 0.49486 0.35445 0.38766 -0.11857 -0.02732 0.00356  167 LYS A CE  
2664 N  NZ  . LYS A 167 ? 0.50471 0.32773 0.39496 -0.13670 -0.01420 0.00158  167 LYS A NZ  
2678 N  N   . ARG A 168 ? 0.50138 0.16264 0.33916 0.05231  -0.13722 -0.00357 168 ARG A N   
2679 C  CA  . ARG A 168 ? 0.54943 0.21644 0.36288 0.06293  -0.13321 -0.00873 168 ARG A CA  
2680 C  C   . ARG A 168 ? 0.55499 0.28142 0.36557 0.05818  -0.10096 -0.00687 168 ARG A C   
2681 O  O   . ARG A 168 ? 0.55620 0.29912 0.35672 0.05667  -0.11755 0.00778  168 ARG A O   
2682 C  CB  . ARG A 168 ? 0.58862 0.25557 0.39072 0.07333  -0.15302 -0.01184 168 ARG A CB  
2683 C  CG  . ARG A 168 ? 0.63665 0.29177 0.41953 0.08609  -0.15752 -0.03038 168 ARG A CG  
2684 C  CD  . ARG A 168 ? 0.65612 0.28745 0.43848 0.10387  -0.16524 -0.03956 168 ARG A CD  
2685 N  NE  . ARG A 168 ? 0.65996 0.28955 0.45149 0.09243  -0.17016 -0.06237 168 ARG A NE  
2686 C  CZ  . ARG A 168 ? 0.65237 0.30054 0.45744 0.11499  -0.18219 -0.06767 168 ARG A CZ  
2687 N  NH1 . ARG A 168 ? 0.64594 0.30211 0.46342 0.12723  -0.17817 -0.06615 168 ARG A NH1 
2688 N  NH2 . ARG A 168 ? 0.66061 0.35210 0.45761 0.10703  -0.18736 -0.06617 168 ARG A NH2 
2702 N  N   . LYS A 169 ? 0.56491 0.31519 0.37759 0.06992  -0.06602 -0.01698 169 LYS A N   
2703 C  CA  . LYS A 169 ? 0.59999 0.37576 0.39264 0.04211  -0.03605 0.00144  169 LYS A CA  
2704 C  C   . LYS A 169 ? 0.61838 0.36850 0.40080 0.04079  -0.02892 0.04067  169 LYS A C   
2705 O  O   . LYS A 169 ? 0.63601 0.35638 0.39309 0.04760  -0.03767 0.01931  169 LYS A O   
2706 C  CB  . LYS A 169 ? 0.61720 0.46304 0.40179 0.03174  -0.02377 -0.00899 169 LYS A CB  
2707 C  CG  . LYS A 169 ? 0.64575 0.53780 0.41376 0.02640  -0.01659 -0.02287 169 LYS A CG  
2708 C  CD  . LYS A 169 ? 0.67676 0.61456 0.42378 0.03461  -0.01732 -0.04063 169 LYS A CD  
2709 C  CE  . LYS A 169 ? 0.70152 0.67585 0.43139 0.04003  -0.01747 -0.04958 169 LYS A CE  
2710 N  NZ  . LYS A 169 ? 0.71681 0.70662 0.43664 0.04453  -0.01774 -0.05451 169 LYS A NZ  
2724 N  N   . LEU A 170 ? 0.60341 0.37129 0.41337 0.02365  -0.02388 0.09539  170 LEU A N   
2725 C  CA  . LEU A 170 ? 0.59848 0.43986 0.44011 0.01760  -0.01517 0.12723  170 LEU A CA  
2726 C  C   . LEU A 170 ? 0.61804 0.56143 0.47479 -0.00153 -0.01841 0.14872  170 LEU A C   
2727 O  O   . LEU A 170 ? 0.60590 0.55779 0.47406 0.01723  -0.02068 0.17395  170 LEU A O   
2728 C  CB  . LEU A 170 ? 0.58052 0.39584 0.43455 0.02318  -0.00528 0.13243  170 LEU A CB  
2729 C  CG  . LEU A 170 ? 0.57183 0.34779 0.42590 0.01975  0.00705  0.15558  170 LEU A CG  
2730 C  CD1 . LEU A 170 ? 0.55827 0.30860 0.41632 0.04026  0.00822  0.16875  170 LEU A CD1 
2731 C  CD2 . LEU A 170 ? 0.58202 0.35244 0.42765 -0.00824 0.01150  0.15652  170 LEU A CD2 
2743 N  N   . ASP A 171 ? 0.65785 0.64763 0.50897 -0.03483 -0.01825 0.14605  171 ASP A N   
2744 C  CA  . ASP A 171 ? 0.71289 0.74051 0.54190 -0.05192 -0.00924 0.13782  171 ASP A CA  
2745 C  C   . ASP A 171 ? 0.75019 0.79777 0.56273 -0.07303 0.01785  0.12936  171 ASP A C   
2746 O  O   . ASP A 171 ? 0.76256 0.82284 0.55990 -0.08135 0.02144  0.13500  171 ASP A O   
2747 C  CB  . ASP A 171 ? 0.72588 0.77062 0.55013 -0.04148 -0.02368 0.13748  171 ASP A CB  
2748 C  CG  . ASP A 171 ? 0.74584 0.79446 0.55721 -0.02338 -0.03716 0.13924  171 ASP A CG  
2749 O  OD1 . ASP A 171 ? 0.74723 0.78475 0.56110 -0.02763 -0.04111 0.13048  171 ASP A OD1 
2750 O  OD2 . ASP A 171 ? 0.76564 0.81455 0.55902 0.00065  -0.04989 0.14625  171 ASP A OD2 
2755 N  N   . GLU A 172 ? 0.77367 0.82410 0.58703 -0.07539 0.03473  0.11015  172 GLU A N   
2756 C  CA  . GLU A 172 ? 0.80626 0.86310 0.61214 -0.07716 0.04767  0.09060  172 GLU A CA  
2757 C  C   . GLU A 172 ? 0.83049 0.89114 0.62267 -0.08730 0.04240  0.08364  172 GLU A C   
2758 O  O   . GLU A 172 ? 0.84404 0.91754 0.62577 -0.06830 0.03788  0.07124  172 GLU A O   
2759 C  CB  . GLU A 172 ? 0.81471 0.88096 0.62635 -0.06646 0.06298  0.07934  172 GLU A CB  
2760 C  CG  . GLU A 172 ? 0.82322 0.90188 0.63824 -0.05261 0.07461  0.07233  172 GLU A CG  
2761 C  CD  . GLU A 172 ? 0.83137 0.92138 0.64690 -0.04054 0.08201  0.06805  172 GLU A CD  
2762 O  OE1 . GLU A 172 ? 0.81562 0.91734 0.64836 -0.03431 0.08294  0.07018  172 GLU A OE1 
2763 O  OE2 . GLU A 172 ? 0.85346 0.94072 0.65123 -0.04261 0.08466  0.06632  172 GLU A OE2 
2770 N  N   . LEU A 173 ? 0.83385 0.87651 0.62712 -0.12225 0.04409  0.09558  173 LEU A N   
2771 C  CA  . LEU A 173 ? 0.83224 0.85069 0.62977 -0.15473 0.04392  0.11288  173 LEU A CA  
2772 C  C   . LEU A 173 ? 0.83257 0.83344 0.63188 -0.17107 0.04285  0.12992  173 LEU A C   
2773 O  O   . LEU A 173 ? 0.83764 0.82318 0.63177 -0.17561 0.04095  0.13905  173 LEU A O   
2776 C  C1  . EDO B .   ? 0.26705 0.24510 0.26009 -0.00901 0.06576  -0.04928 201 EDO A C1  
2777 O  O1  . EDO B .   ? 0.22977 0.20257 0.23813 0.02184  0.05535  -0.03481 201 EDO A O1  
2778 C  C2  . EDO B .   ? 0.33768 0.24576 0.26982 0.03706  0.04559  -0.04650 201 EDO A C2  
2779 O  O2  . EDO B .   ? 0.32531 0.22254 0.27587 0.04114  0.02121  -0.03872 201 EDO A O2  
2786 C  C1  . EDO C .   ? 0.36815 0.23867 0.28102 0.01173  0.06271  0.07212  202 EDO A C1  
2787 O  O1  . EDO C .   ? 0.35125 0.24151 0.27436 0.02976  0.06351  0.04546  202 EDO A O1  
2788 C  C2  . EDO C .   ? 0.39612 0.21634 0.28976 0.01133  0.04334  0.04802  202 EDO A C2  
2789 O  O2  . EDO C .   ? 0.39176 0.21844 0.29249 0.02001  0.04907  0.01449  202 EDO A O2  
2796 C  C1  . EDO D .   ? 0.41299 0.32065 0.34388 -0.01389 -0.07762 -0.00907 203 EDO A C1  
2797 O  O1  . EDO D .   ? 0.43392 0.36237 0.36082 -0.04088 -0.07938 0.00289  203 EDO A O1  
2798 C  C2  . EDO D .   ? 0.39166 0.25358 0.32963 0.02652  -0.08182 -0.01265 203 EDO A C2  
2799 O  O2  . EDO D .   ? 0.35779 0.15888 0.31233 0.01959  -0.09068 -0.02186 203 EDO A O2  
2806 CD CD  . CD  E .   ? 0.28043 0.10177 0.17588 -0.00077 0.00388  -0.00209 204 CD  A CD  
2807 CD CD  . CD  F .   ? 0.26889 0.10832 0.17835 -0.00239 -0.00227 0.00242  205 CD  A CD  
2808 CD CD  . CD  G .   ? 0.33254 0.11688 0.18894 -0.01659 0.01195  -0.01053 206 CD  A CD  
2809 CD CD  . CD  H .   ? 0.60937 0.41544 0.36608 0.08896  -0.01910 0.12745  207 CD  A CD  
2810 NA NA  . NA  I .   ? 0.60081 0.47738 0.44007 -0.04740 0.04355  0.01056  208 NA  A NA  
2811 NA NA  . NA  J .   ? 0.45813 0.33200 0.41832 -0.00384 -0.01072 -0.03706 209 NA  A NA  
2812 CL CL  . CL  K .   ? 0.37974 0.13753 0.19611 -0.02277 0.00812  -0.01572 210 CL  A CL  
2813 CL CL  . CL  L .   ? 0.32124 0.25793 0.27084 0.00562  0.01861  -0.01172 211 CL  A CL  
2814 CL CL  . CL  M .   ? 0.77589 0.45929 0.62319 -0.14322 -0.08592 0.08688  212 CL  A CL  
# 
