data_8RLI
# 
_entry.id   8RLI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8RLI         pdb_00008rli 10.2210/pdb8rli/pdb 
WWPDB D_1292133861 ?            ?                   
# 
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 2024-11-06 
2 'Structure model' 1 1 2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
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 2 'Structure model' citation_author 
# 
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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.title'                   
12 2 'Structure model' '_citation.year'                    
13 2 'Structure model' '_citation_author.identifier_ORCID' 
14 2 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RLI 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              annette.langkilde@sund.ku.dk 
_pdbx_contact_author.name_first         Annette 
_pdbx_contact_author.name_last          Langkilde 
_pdbx_contact_author.name_mi            E. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2467-4205 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ramos, J.'       1  0000-0002-1473-9303 
'Laux, V.'        2  ?                   
'Mason, S.A.'     3  ?                   
'Lemee, M.'       4  ?                   
'Bowler, M.'      5  0000-0003-0465-3351 
'Diederichs, K.'  6  0000-0001-5360-0905 
'Haertlein, M.'   7  ?                   
'Forsyth, V.T.'   8  0000-0003-0380-3477 
'Mossou, E.'      9  0000-0002-1899-4942 
'Larsen, S.'      10 0000-0003-3848-1789 
'Langkilde, A.E.' 11 0000-0003-2467-4205 
# 
_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            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                136 
_citation.page_last                 148.e3 
_citation.title                     
'Structure and dynamics of the active site of hen egg-white lysozyme from atomic resolution neutron crystallography.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2024.10.030 
_citation.pdbx_database_id_PubMed   39577430 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ramos, J.'       1  ? 
primary 'Laux, V.'        2  ? 
primary 'Mason, S.A.'     3  ? 
primary 'Lemee, M.H.'     4  ? 
primary 'Bowler, M.W.'    5  ? 
primary 'Diederichs, K.'  6  ? 
primary 'Haertlein, M.'   7  ? 
primary 'Forsyth, V.T.'   8  ? 
primary 'Mossou, E.'      9  ? 
primary 'Larsen, S.'      10 ? 
primary 'Langkilde, A.E.' 11 ? 
# 
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 'Lysozyme C'  14388.211 1  3.2.1.17 ? ? ? 
2 non-polymer syn 'NITRATE ION' 62.005    8  ?        ? ? ? 
3 non-polymer syn 'ACETATE ION' 59.044    1  ?        ? ? ? 
4 water       nat water         18.015    88 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '1,4-beta-N-acetylmuramidase C,Allergen Gal d IV' 
# 
_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       
;GKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIP
CSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIP
CSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
;
_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 'NITRATE ION' NO3 
3 'ACETATE ION' ACT 
4 water         DOD 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   LYS n 
1 3   VAL n 
1 4   PHE n 
1 5   GLY n 
1 6   ARG n 
1 7   CYS n 
1 8   GLU n 
1 9   LEU n 
1 10  ALA n 
1 11  ALA n 
1 12  ALA n 
1 13  MET n 
1 14  LYS n 
1 15  ARG n 
1 16  HIS n 
1 17  GLY n 
1 18  LEU n 
1 19  ASP n 
1 20  ASN n 
1 21  TYR n 
1 22  ARG n 
1 23  GLY n 
1 24  TYR n 
1 25  SER n 
1 26  LEU n 
1 27  GLY n 
1 28  ASN n 
1 29  TRP n 
1 30  VAL n 
1 31  CYS n 
1 32  ALA n 
1 33  ALA n 
1 34  LYS n 
1 35  PHE n 
1 36  GLU n 
1 37  SER n 
1 38  ASN n 
1 39  PHE n 
1 40  ASN n 
1 41  THR n 
1 42  GLN n 
1 43  ALA n 
1 44  THR n 
1 45  ASN n 
1 46  ARG n 
1 47  ASN n 
1 48  THR n 
1 49  ASP n 
1 50  GLY n 
1 51  SER n 
1 52  THR n 
1 53  ASP n 
1 54  TYR n 
1 55  GLY n 
1 56  ILE n 
1 57  LEU n 
1 58  GLN n 
1 59  ILE n 
1 60  ASN n 
1 61  SER n 
1 62  ARG n 
1 63  TRP n 
1 64  TRP n 
1 65  CYS n 
1 66  ASN n 
1 67  ASP n 
1 68  GLY n 
1 69  ARG n 
1 70  THR n 
1 71  PRO n 
1 72  GLY n 
1 73  SER n 
1 74  ARG n 
1 75  ASN n 
1 76  LEU n 
1 77  CYS n 
1 78  ASN n 
1 79  ILE n 
1 80  PRO n 
1 81  CYS n 
1 82  SER n 
1 83  ALA n 
1 84  LEU n 
1 85  LEU n 
1 86  SER n 
1 87  SER n 
1 88  ASP n 
1 89  ILE n 
1 90  THR n 
1 91  ALA n 
1 92  SER n 
1 93  VAL n 
1 94  ASN n 
1 95  CYS n 
1 96  ALA n 
1 97  LYS n 
1 98  LYS n 
1 99  ILE n 
1 100 VAL n 
1 101 SER n 
1 102 ASP n 
1 103 GLY n 
1 104 ASN n 
1 105 GLY n 
1 106 MET n 
1 107 ASN n 
1 108 ALA n 
1 109 TRP n 
1 110 VAL n 
1 111 ALA n 
1 112 TRP n 
1 113 ARG n 
1 114 ASN n 
1 115 ARG n 
1 116 CYS n 
1 117 LYS n 
1 118 GLY n 
1 119 THR n 
1 120 ASP n 
1 121 VAL n 
1 122 GLN n 
1 123 ALA n 
1 124 TRP n 
1 125 ILE n 
1 126 ARG n 
1 127 GLY n 
1 128 CYS n 
1 129 ARG n 
1 130 LEU 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                   130 
_entity_src_gen.gene_src_common_name               chicken 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 LYZ 
_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      'Gallus gallus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9031 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer         . 'ACETATE ION'      ? 'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking' y ALANINE            ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE           ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE         ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'    ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE           ? 'C3 H7 N O2 S'   121.158 
DOD non-polymer         . 'DEUTERATED WATER' ? 'D2 O'           20.028  
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 
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 
NO3 non-polymer         . 'NITRATE ION'      ? 'N O3 -1'        62.005  
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   GLY 1   0   0   GLY GLY A . n 
A 1 2   LYS 2   1   1   LYS LYS A . n 
A 1 3   VAL 3   2   2   VAL VAL A . n 
A 1 4   PHE 4   3   3   PHE PHE A . n 
A 1 5   GLY 5   4   4   GLY GLY A . n 
A 1 6   ARG 6   5   5   ARG ARG A . n 
A 1 7   CYS 7   6   6   CYS CYS A . n 
A 1 8   GLU 8   7   7   GLU GLU A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  ALA 10  9   9   ALA ALA A . n 
A 1 11  ALA 11  10  10  ALA ALA A . n 
A 1 12  ALA 12  11  11  ALA ALA A . n 
A 1 13  MET 13  12  12  MET MET A . n 
A 1 14  LYS 14  13  13  LYS LYS A . n 
A 1 15  ARG 15  14  14  ARG ARG A . n 
A 1 16  HIS 16  15  15  HIS HIS A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  LEU 18  17  17  LEU LEU A . n 
A 1 19  ASP 19  18  18  ASP ASP A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  TYR 21  20  20  TYR TYR A . n 
A 1 22  ARG 22  21  21  ARG ARG A . n 
A 1 23  GLY 23  22  22  GLY GLY A . n 
A 1 24  TYR 24  23  23  TYR TYR A . n 
A 1 25  SER 25  24  24  SER SER A . n 
A 1 26  LEU 26  25  25  LEU LEU A . n 
A 1 27  GLY 27  26  26  GLY GLY A . n 
A 1 28  ASN 28  27  27  ASN ASN A . n 
A 1 29  TRP 29  28  28  TRP TRP A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  CYS 31  30  30  CYS CYS A . n 
A 1 32  ALA 32  31  31  ALA ALA A . n 
A 1 33  ALA 33  32  32  ALA ALA A . n 
A 1 34  LYS 34  33  33  LYS LYS A . n 
A 1 35  PHE 35  34  34  PHE PHE A . n 
A 1 36  GLU 36  35  35  GLU GLU A . n 
A 1 37  SER 37  36  36  SER SER A . n 
A 1 38  ASN 38  37  37  ASN ASN A . n 
A 1 39  PHE 39  38  38  PHE PHE A . n 
A 1 40  ASN 40  39  39  ASN ASN A . n 
A 1 41  THR 41  40  40  THR THR A . n 
A 1 42  GLN 42  41  41  GLN GLN A . n 
A 1 43  ALA 43  42  42  ALA ALA A . n 
A 1 44  THR 44  43  43  THR THR A . n 
A 1 45  ASN 45  44  44  ASN ASN A . n 
A 1 46  ARG 46  45  45  ARG ARG A . n 
A 1 47  ASN 47  46  46  ASN ASN A . n 
A 1 48  THR 48  47  47  THR THR A . n 
A 1 49  ASP 49  48  48  ASP ASP A . n 
A 1 50  GLY 50  49  49  GLY GLY A . n 
A 1 51  SER 51  50  50  SER SER A . n 
A 1 52  THR 52  51  51  THR THR A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  TYR 54  53  53  TYR TYR A . n 
A 1 55  GLY 55  54  54  GLY GLY A . n 
A 1 56  ILE 56  55  55  ILE ILE A . n 
A 1 57  LEU 57  56  56  LEU LEU A . n 
A 1 58  GLN 58  57  57  GLN GLN A . n 
A 1 59  ILE 59  58  58  ILE ILE A . n 
A 1 60  ASN 60  59  59  ASN ASN A . n 
A 1 61  SER 61  60  60  SER SER A . n 
A 1 62  ARG 62  61  61  ARG ARG A . n 
A 1 63  TRP 63  62  62  TRP TRP A . n 
A 1 64  TRP 64  63  63  TRP TRP A . n 
A 1 65  CYS 65  64  64  CYS CYS A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  ASP 67  66  66  ASP ASP A . n 
A 1 68  GLY 68  67  67  GLY GLY A . n 
A 1 69  ARG 69  68  68  ARG ARG A . n 
A 1 70  THR 70  69  69  THR THR A . n 
A 1 71  PRO 71  70  70  PRO PRO A . n 
A 1 72  GLY 72  71  71  GLY GLY A . n 
A 1 73  SER 73  72  72  SER SER A . n 
A 1 74  ARG 74  73  73  ARG ARG A . n 
A 1 75  ASN 75  74  74  ASN ASN A . n 
A 1 76  LEU 76  75  75  LEU LEU A . n 
A 1 77  CYS 77  76  76  CYS CYS A . n 
A 1 78  ASN 78  77  77  ASN ASN A . n 
A 1 79  ILE 79  78  78  ILE ILE A . n 
A 1 80  PRO 80  79  79  PRO PRO A . n 
A 1 81  CYS 81  80  80  CYS CYS A . n 
A 1 82  SER 82  81  81  SER SER A . n 
A 1 83  ALA 83  82  82  ALA ALA A . n 
A 1 84  LEU 84  83  83  LEU LEU A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  SER 86  85  85  SER SER A . n 
A 1 87  SER 87  86  86  SER SER A . n 
A 1 88  ASP 88  87  87  ASP ASP A . n 
A 1 89  ILE 89  88  88  ILE ILE A . n 
A 1 90  THR 90  89  89  THR THR A . n 
A 1 91  ALA 91  90  90  ALA ALA A . n 
A 1 92  SER 92  91  91  SER SER A . n 
A 1 93  VAL 93  92  92  VAL VAL A . n 
A 1 94  ASN 94  93  93  ASN ASN A . n 
A 1 95  CYS 95  94  94  CYS CYS A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  LYS 97  96  96  LYS LYS A . n 
A 1 98  LYS 98  97  97  LYS LYS A . n 
A 1 99  ILE 99  98  98  ILE ILE A . n 
A 1 100 VAL 100 99  99  VAL VAL A . n 
A 1 101 SER 101 100 100 SER SER A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 GLY 103 102 102 GLY GLY A . n 
A 1 104 ASN 104 103 103 ASN ASN A . n 
A 1 105 GLY 105 104 104 GLY GLY A . n 
A 1 106 MET 106 105 105 MET MET A . n 
A 1 107 ASN 107 106 106 ASN ASN A . n 
A 1 108 ALA 108 107 107 ALA ALA A . n 
A 1 109 TRP 109 108 108 TRP TRP A . n 
A 1 110 VAL 110 109 109 VAL VAL A . n 
A 1 111 ALA 111 110 110 ALA ALA A . n 
A 1 112 TRP 112 111 111 TRP TRP A . n 
A 1 113 ARG 113 112 112 ARG ARG A . n 
A 1 114 ASN 114 113 113 ASN ASN A . n 
A 1 115 ARG 115 114 114 ARG ARG A . n 
A 1 116 CYS 116 115 115 CYS CYS A . n 
A 1 117 LYS 117 116 116 LYS LYS A . n 
A 1 118 GLY 118 117 117 GLY GLY A . n 
A 1 119 THR 119 118 118 THR THR A . n 
A 1 120 ASP 120 119 119 ASP ASP A . n 
A 1 121 VAL 121 120 120 VAL VAL A . n 
A 1 122 GLN 122 121 121 GLN GLN A . n 
A 1 123 ALA 123 122 122 ALA ALA A . n 
A 1 124 TRP 124 123 123 TRP TRP A . n 
A 1 125 ILE 125 124 124 ILE ILE A . n 
A 1 126 ARG 126 125 125 ARG ARG A . n 
A 1 127 GLY 127 126 126 GLY GLY A . n 
A 1 128 CYS 128 127 127 CYS CYS A . n 
A 1 129 ARG 129 128 128 ARG ARG A . n 
A 1 130 LEU 130 129 129 LEU LEU 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 NO3 1  201 201 NO3 NO3 A . 
C 2 NO3 1  202 202 NO3 NO3 A . 
D 2 NO3 1  203 203 NO3 NO3 A . 
E 2 NO3 1  204 204 NO3 NO3 A . 
F 2 NO3 1  205 206 NO3 NO3 A . 
G 2 NO3 1  206 207 NO3 NO3 A . 
H 2 NO3 1  207 208 NO3 NO3 A . 
I 2 NO3 1  208 209 NO3 NO3 A . 
J 3 ACT 1  209 210 ACT ACT A . 
K 4 DOD 1  301 370 DOD DOD A . 
K 4 DOD 2  302 375 DOD DOD A . 
K 4 DOD 3  303 316 DOD DOD A . 
K 4 DOD 4  304 362 DOD DOD A . 
K 4 DOD 5  305 377 DOD DOD A . 
K 4 DOD 6  306 349 DOD DOD A . 
K 4 DOD 7  307 358 DOD DOD A . 
K 4 DOD 8  308 345 DOD DOD A . 
K 4 DOD 9  309 364 DOD DOD A . 
K 4 DOD 10 310 344 DOD DOD A . 
K 4 DOD 11 311 340 DOD DOD A . 
K 4 DOD 12 312 353 DOD DOD A . 
K 4 DOD 13 313 352 DOD DOD A . 
K 4 DOD 14 314 365 DOD DOD A . 
K 4 DOD 15 315 386 DOD DOD A . 
K 4 DOD 16 316 338 DOD DOD A . 
K 4 DOD 17 317 356 DOD DOD A . 
K 4 DOD 18 318 321 DOD DOD A . 
K 4 DOD 19 319 360 DOD DOD A . 
K 4 DOD 20 320 330 DOD DOD A . 
K 4 DOD 21 321 383 DOD DOD A . 
K 4 DOD 22 322 347 DOD DOD A . 
K 4 DOD 23 323 332 DOD DOD A . 
K 4 DOD 24 324 326 DOD DOD A . 
K 4 DOD 25 325 322 DOD DOD A . 
K 4 DOD 26 326 382 DOD DOD A . 
K 4 DOD 27 327 304 DOD DOD A . 
K 4 DOD 28 328 313 DOD DOD A . 
K 4 DOD 29 329 359 DOD DOD A . 
K 4 DOD 30 330 314 DOD DOD A . 
K 4 DOD 31 331 325 DOD DOD A . 
K 4 DOD 32 332 308 DOD DOD A . 
K 4 DOD 33 333 307 DOD DOD A . 
K 4 DOD 34 334 366 DOD DOD A . 
K 4 DOD 35 335 317 DOD DOD A . 
K 4 DOD 36 336 303 DOD DOD A . 
K 4 DOD 37 337 320 DOD DOD A . 
K 4 DOD 38 338 329 DOD DOD A . 
K 4 DOD 39 339 331 DOD DOD A . 
K 4 DOD 40 340 312 DOD DOD A . 
K 4 DOD 41 341 388 DOD DOD A . 
K 4 DOD 42 342 305 DOD DOD A . 
K 4 DOD 43 343 381 DOD DOD A . 
K 4 DOD 44 344 374 DOD DOD A . 
K 4 DOD 45 345 323 DOD DOD A . 
K 4 DOD 46 346 309 DOD DOD A . 
K 4 DOD 47 347 310 DOD DOD A . 
K 4 DOD 48 348 306 DOD DOD A . 
K 4 DOD 49 349 368 DOD DOD A . 
K 4 DOD 50 350 311 DOD DOD A . 
K 4 DOD 51 351 301 DOD DOD A . 
K 4 DOD 52 352 315 DOD DOD A . 
K 4 DOD 53 353 318 DOD DOD A . 
K 4 DOD 54 354 355 DOD DOD A . 
K 4 DOD 55 355 319 DOD DOD A . 
K 4 DOD 56 356 324 DOD DOD A . 
K 4 DOD 57 357 339 DOD DOD A . 
K 4 DOD 58 358 380 DOD DOD A . 
K 4 DOD 59 359 343 DOD DOD A . 
K 4 DOD 60 360 385 DOD DOD A . 
K 4 DOD 61 361 302 DOD DOD A . 
K 4 DOD 62 362 387 DOD DOD A . 
K 4 DOD 63 363 333 DOD DOD A . 
K 4 DOD 64 364 342 DOD DOD A . 
K 4 DOD 65 365 350 DOD DOD A . 
K 4 DOD 66 366 337 DOD DOD A . 
K 4 DOD 67 367 335 DOD DOD A . 
K 4 DOD 68 368 328 DOD DOD A . 
K 4 DOD 69 369 369 DOD DOD A . 
K 4 DOD 70 370 354 DOD DOD A . 
K 4 DOD 71 371 376 DOD DOD A . 
K 4 DOD 72 372 357 DOD DOD A . 
K 4 DOD 73 373 371 DOD DOD A . 
K 4 DOD 74 374 336 DOD DOD A . 
K 4 DOD 75 375 379 DOD DOD A . 
K 4 DOD 76 376 361 DOD DOD A . 
K 4 DOD 77 377 378 DOD DOD A . 
K 4 DOD 78 378 384 DOD DOD A . 
K 4 DOD 79 379 367 DOD DOD A . 
K 4 DOD 80 380 351 DOD DOD A . 
K 4 DOD 81 381 346 DOD DOD A . 
K 4 DOD 82 382 334 DOD DOD A . 
K 4 DOD 83 383 348 DOD DOD A . 
K 4 DOD 84 384 373 DOD DOD A . 
K 4 DOD 85 385 372 DOD DOD A . 
K 4 DOD 86 386 327 DOD DOD A . 
K 4 DOD 87 387 341 DOD DOD A . 
K 4 DOD 88 388 363 DOD DOD A . 
# 
_cell.angle_alpha                  89.16 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   72.05 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  67.74 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RLI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     27.120 
_cell.length_a_esd                 ? 
_cell.length_b                     31.630 
_cell.length_b_esd                 ? 
_cell.length_c                     34.150 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        1 
_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                         8RLI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   8RLI 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'NEUTRON DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_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          MICROBATCH 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.5 
_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    '0.15 M sodium nitrate, 0.05 M sodium acetate pH 4.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     298 
_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                     'POSITION SENSITIVE DETECTOR' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         '5ATM 3HE, CURVED 120X30 DEGREES' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-02-12 
_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             neutron 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.455 
_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                      'NUCLEAR REACTOR' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ILL BEAMLINE D19' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.455 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   D19 
_diffrn_source.pdbx_synchrotron_site       ILL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RLI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              0.91 
_reflns.d_resolution_low                               9.96 
_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                                     67975 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           95.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.089 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.076 
_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                                    0.91 
_reflns_shell.d_res_low                                     0.94 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6381 
_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                               1.7 
_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                               1.451 
_reflns_shell.pdbx_Rpim_I_all                               0.908 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.148 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          89.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.120 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8RLI 
_refine.pdbx_refine_id                           'NEUTRON 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                            0.91 
_refine.ls_d_res_low                             9.96 
_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                     64576 
_refine.ls_number_reflns_R_free                  3399 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.5 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2472 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1981 
_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                    ? 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            Random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_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                            ? 
_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                    ? 
# 
_struct.entry_id                     8RLI 
_struct.title                        'Neutron structure of perdeuterated hen egg-white lysozyme at room temperature' 
_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        8RLI 
_struct_keywords.text            'lysozyme, perdeuterated, room temperature, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LYSC_CHICK 
_struct_ref.pdbx_db_accession          P00698 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIP
CSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
;
_struct_ref.pdbx_align_begin           18 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8RLI 
_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                 130 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00698 
_struct_ref_seq.db_align_beg                  18 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  147 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       0 
_struct_ref_seq.pdbx_auth_seq_align_end       129 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9550 ? 
1 MORE         49   ? 
1 'SSA (A^2)'  8520 ? 
# 
_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 5   ? HIS A 16  ? GLY A 4   HIS A 15  1 ? 12 
HELX_P HELX_P2 AA2 ASN A 20  ? TYR A 24  ? ASN A 19  TYR A 23  5 ? 5  
HELX_P HELX_P3 AA3 SER A 25  ? ASN A 38  ? SER A 24  ASN A 37  1 ? 14 
HELX_P HELX_P4 AA4 PRO A 80  ? SER A 86  ? PRO A 79  SER A 85  5 ? 7  
HELX_P HELX_P5 AA5 ILE A 89  ? ASP A 102 ? ILE A 88  ASP A 101 1 ? 14 
HELX_P HELX_P6 AA6 GLY A 105 ? ALA A 108 ? GLY A 104 ALA A 107 5 ? 4  
HELX_P HELX_P7 AA7 TRP A 109 ? CYS A 116 ? TRP A 108 CYS A 115 1 ? 8  
HELX_P HELX_P8 AA8 ASP A 120 ? ILE A 125 ? ASP A 119 ILE A 124 5 ? 6  
# 
_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 
disulf1 disulf ? ? A CYS 7  SG ? ? ? 1_555 A CYS 128 SG ? ? A CYS 6  A CYS 127 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf2 disulf ? ? A CYS 31 SG ? ? ? 1_555 A CYS 116 SG ? ? A CYS 30 A CYS 115 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf3 disulf ? ? A CYS 65 SG ? ? ? 1_555 A CYS 81  SG ? ? A CYS 64 A CYS 80  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf4 disulf ? ? A CYS 77 SG ? ? ? 1_555 A CYS 95  SG ? ? A CYS 76 A CYS 94  1_555 ? ? ? ? ? ? ? 2.020 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 7  ? CYS A 128 ? CYS A 6  ? 1_555 CYS A 127 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 31 ? CYS A 116 ? CYS A 30 ? 1_555 CYS A 115 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 65 ? CYS A 81  ? CYS A 64 ? 1_555 CYS A 80  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 77 ? CYS A 95  ? CYS A 76 ? 1_555 CYS A 94  ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_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 
# 
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 THR A 44 ? ARG A 46 ? THR A 43 ARG A 45 
AA1 2 THR A 52 ? TYR A 54 ? THR A 51 TYR A 53 
AA1 3 ILE A 59 ? ASN A 60 ? ILE A 58 ASN A 59 
# 
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 45 ? N ASN A 44 O ASP A 53 ? O ASP A 52 
AA1 2 3 N TYR A 54 ? N TYR A 53 O ILE A 59 ? O ILE A 58 
# 
_pdbx_entry_details.entry_id                   8RLI 
_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   Y 
# 
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 OD2  A ASP 87  ? A DG1 A THR 89  ? ? 1.52 
2 1 DH12 A ARG 45  ? B O   A DOD 301 ? ? 1.52 
3 1 DG   A SER 24  ? ? O3  A NO3 206 ? ? 1.53 
4 1 OG1  A THR 118 ? ? D2  A DOD 311 ? ? 1.56 
5 1 D    A THR 47  ? ? OXT A ACT 209 ? ? 1.57 
6 1 DD22 A ASN 113 ? ? O   A DOD 313 ? ? 1.58 
7 1 NH1  A ARG 45  ? B O   A DOD 301 ? ? 1.80 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 DE22 A GLN 41  ? B 1_555 DE22 A GLN 121 ? ? 1_565 1.32 
2 1 DD21 A ASN 37  ? B 1_555 O3   A NO3 203 ? ? 1_556 1.54 
3 1 DH22 A ARG 128 ? ? 1_555 O    A DOD 310 ? ? 1_556 1.57 
4 1 D1   A DOD 331 ? ? 1_555 O    A DOD 367 ? ? 1_455 1.58 
# 
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 5   ? B CZ A ARG 5   ? B NH1 A ARG 5   ? B 116.09 120.30 -4.21 0.50 N 
2  1 NE  A ARG 21  ? ? CZ A ARG 21  ? ? NH2 A ARG 21  ? ? 115.69 120.30 -4.61 0.50 N 
3  1 NE  A ARG 45  ? B CZ A ARG 45  ? B NH1 A ARG 45  ? B 112.32 120.30 -7.98 0.50 N 
4  1 NE  A ARG 45  ? A CZ A ARG 45  ? A NH2 A ARG 45  ? A 116.71 120.30 -3.59 0.50 N 
5  1 NE  A ARG 45  ? B CZ A ARG 45  ? B NH2 A ARG 45  ? B 125.11 120.30 4.81  0.50 N 
6  1 CD  A ARG 114 ? A NE A ARG 114 ? A CZ  A ARG 114 ? A 136.86 123.60 13.26 1.40 N 
7  1 CD  A ARG 114 ? B NE A ARG 114 ? B CZ  A ARG 114 ? B 132.48 123.60 8.88  1.40 N 
8  1 NH1 A ARG 114 ? A CZ A ARG 114 ? A NH2 A ARG 114 ? A 112.66 119.40 -6.74 1.10 N 
9  1 NE  A ARG 114 ? A CZ A ARG 114 ? A NH1 A ARG 114 ? A 133.79 120.30 13.49 0.50 N 
10 1 NE  A ARG 114 ? A CZ A ARG 114 ? A NH2 A ARG 114 ? A 113.55 120.30 -6.75 0.50 N 
11 1 NE  A ARG 114 ? B CZ A ARG 114 ? B NH2 A ARG 114 ? B 125.91 120.30 5.61  0.50 N 
12 1 NE  A ARG 125 ? ? CZ A ARG 125 ? ? NH2 A ARG 125 ? ? 116.73 120.30 -3.57 0.50 N 
13 1 CD  A ARG 128 ? ? NE A ARG 128 ? ? CZ  A ARG 128 ? ? 133.50 123.60 9.90  1.40 N 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    0 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   A 
_pdbx_validate_peptide_omega.auth_comp_id_2   LYS 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    1 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   A 
_pdbx_validate_peptide_omega.omega            143.33 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 45  ? A 0.079 'SIDE CHAIN' 
2 1 ARG A 114 ? A 0.129 'SIDE CHAIN' 
# 
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 
ACT C    C N N 1   
ACT O    O N N 2   
ACT OXT  O N N 3   
ACT CH3  C N N 4   
ACT H1   H N N 5   
ACT H2   H N N 6   
ACT H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
DOD O    O N N 95  
DOD D1   D N N 96  
DOD D2   D N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
ILE N    N N N 168 
ILE CA   C N S 169 
ILE C    C N N 170 
ILE O    O N N 171 
ILE CB   C N S 172 
ILE CG1  C N N 173 
ILE CG2  C N N 174 
ILE CD1  C N N 175 
ILE OXT  O N N 176 
ILE H    H N N 177 
ILE H2   H N N 178 
ILE HA   H N N 179 
ILE HB   H N N 180 
ILE HG12 H N N 181 
ILE HG13 H N N 182 
ILE HG21 H N N 183 
ILE HG22 H N N 184 
ILE HG23 H N N 185 
ILE HD11 H N N 186 
ILE HD12 H N N 187 
ILE HD13 H N N 188 
ILE HXT  H N N 189 
LEU N    N N N 190 
LEU CA   C N S 191 
LEU C    C N N 192 
LEU O    O N N 193 
LEU CB   C N N 194 
LEU CG   C N N 195 
LEU CD1  C N N 196 
LEU CD2  C N N 197 
LEU OXT  O N N 198 
LEU H    H N N 199 
LEU H2   H N N 200 
LEU HA   H N N 201 
LEU HB2  H N N 202 
LEU HB3  H N N 203 
LEU HG   H N N 204 
LEU HD11 H N N 205 
LEU HD12 H N N 206 
LEU HD13 H N N 207 
LEU HD21 H N N 208 
LEU HD22 H N N 209 
LEU HD23 H N N 210 
LEU HXT  H N N 211 
LYS N    N N N 212 
LYS CA   C N S 213 
LYS C    C N N 214 
LYS O    O N N 215 
LYS CB   C N N 216 
LYS CG   C N N 217 
LYS CD   C N N 218 
LYS CE   C N N 219 
LYS NZ   N N N 220 
LYS OXT  O N N 221 
LYS H    H N N 222 
LYS H2   H N N 223 
LYS HA   H N N 224 
LYS HB2  H N N 225 
LYS HB3  H N N 226 
LYS HG2  H N N 227 
LYS HG3  H N N 228 
LYS HD2  H N N 229 
LYS HD3  H N N 230 
LYS HE2  H N N 231 
LYS HE3  H N N 232 
LYS HZ1  H N N 233 
LYS HZ2  H N N 234 
LYS HZ3  H N N 235 
LYS HXT  H N N 236 
MET N    N N N 237 
MET CA   C N S 238 
MET C    C N N 239 
MET O    O N N 240 
MET CB   C N N 241 
MET CG   C N N 242 
MET SD   S N N 243 
MET CE   C N N 244 
MET OXT  O N N 245 
MET H    H N N 246 
MET H2   H N N 247 
MET HA   H N N 248 
MET HB2  H N N 249 
MET HB3  H N N 250 
MET HG2  H N N 251 
MET HG3  H N N 252 
MET HE1  H N N 253 
MET HE2  H N N 254 
MET HE3  H N N 255 
MET HXT  H N N 256 
NO3 N    N N N 257 
NO3 O1   O N N 258 
NO3 O2   O N N 259 
NO3 O3   O N N 260 
PHE N    N N N 261 
PHE CA   C N S 262 
PHE C    C N N 263 
PHE O    O N N 264 
PHE CB   C N N 265 
PHE CG   C Y N 266 
PHE CD1  C Y N 267 
PHE CD2  C Y N 268 
PHE CE1  C Y N 269 
PHE CE2  C Y N 270 
PHE CZ   C Y N 271 
PHE OXT  O N N 272 
PHE H    H N N 273 
PHE H2   H N N 274 
PHE HA   H N N 275 
PHE HB2  H N N 276 
PHE HB3  H N N 277 
PHE HD1  H N N 278 
PHE HD2  H N N 279 
PHE HE1  H N N 280 
PHE HE2  H N N 281 
PHE HZ   H N N 282 
PHE HXT  H N N 283 
PRO N    N N N 284 
PRO CA   C N S 285 
PRO C    C N N 286 
PRO O    O N N 287 
PRO CB   C N N 288 
PRO CG   C N N 289 
PRO CD   C N N 290 
PRO OXT  O N N 291 
PRO H    H N N 292 
PRO HA   H N N 293 
PRO HB2  H N N 294 
PRO HB3  H N N 295 
PRO HG2  H N N 296 
PRO HG3  H N N 297 
PRO HD2  H N N 298 
PRO HD3  H N N 299 
PRO HXT  H N N 300 
SER N    N N N 301 
SER CA   C N S 302 
SER C    C N N 303 
SER O    O N N 304 
SER CB   C N N 305 
SER OG   O N N 306 
SER OXT  O N N 307 
SER H    H N N 308 
SER H2   H N N 309 
SER HA   H N N 310 
SER HB2  H N N 311 
SER HB3  H N N 312 
SER HG   H N N 313 
SER HXT  H N N 314 
THR N    N N N 315 
THR CA   C N S 316 
THR C    C N N 317 
THR O    O N N 318 
THR CB   C N R 319 
THR OG1  O N N 320 
THR CG2  C N N 321 
THR OXT  O N N 322 
THR H    H N N 323 
THR H2   H N N 324 
THR HA   H N N 325 
THR HB   H N N 326 
THR HG1  H N N 327 
THR HG21 H N N 328 
THR HG22 H N N 329 
THR HG23 H N N 330 
THR HXT  H N N 331 
TRP N    N N N 332 
TRP CA   C N S 333 
TRP C    C N N 334 
TRP O    O N N 335 
TRP CB   C N N 336 
TRP CG   C Y N 337 
TRP CD1  C Y N 338 
TRP CD2  C Y N 339 
TRP NE1  N Y N 340 
TRP CE2  C Y N 341 
TRP CE3  C Y N 342 
TRP CZ2  C Y N 343 
TRP CZ3  C Y N 344 
TRP CH2  C Y N 345 
TRP OXT  O N N 346 
TRP H    H N N 347 
TRP H2   H N N 348 
TRP HA   H N N 349 
TRP HB2  H N N 350 
TRP HB3  H N N 351 
TRP HD1  H N N 352 
TRP HE1  H N N 353 
TRP HE3  H N N 354 
TRP HZ2  H N N 355 
TRP HZ3  H N N 356 
TRP HH2  H N N 357 
TRP HXT  H N N 358 
TYR N    N N N 359 
TYR CA   C N S 360 
TYR C    C N N 361 
TYR O    O N N 362 
TYR CB   C N N 363 
TYR CG   C Y N 364 
TYR CD1  C Y N 365 
TYR CD2  C Y N 366 
TYR CE1  C Y N 367 
TYR CE2  C Y N 368 
TYR CZ   C Y N 369 
TYR OH   O N N 370 
TYR OXT  O N N 371 
TYR H    H N N 372 
TYR H2   H N N 373 
TYR HA   H N N 374 
TYR HB2  H N N 375 
TYR HB3  H N N 376 
TYR HD1  H N N 377 
TYR HD2  H N N 378 
TYR HE1  H N N 379 
TYR HE2  H N N 380 
TYR HH   H N N 381 
TYR HXT  H N N 382 
VAL N    N N N 383 
VAL CA   C N S 384 
VAL C    C N N 385 
VAL O    O N N 386 
VAL CB   C N N 387 
VAL CG1  C N N 388 
VAL CG2  C N N 389 
VAL OXT  O N N 390 
VAL H    H N N 391 
VAL H2   H N N 392 
VAL HA   H N N 393 
VAL HB   H N N 394 
VAL HG11 H N N 395 
VAL HG12 H N N 396 
VAL HG13 H N N 397 
VAL HG21 H N N 398 
VAL HG22 H N N 399 
VAL HG23 H N N 400 
VAL HXT  H N N 401 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
DOD O   D1   sing N N 89  
DOD O   D2   sing N N 90  
GLN N   CA   sing N N 91  
GLN N   H    sing N N 92  
GLN N   H2   sing N N 93  
GLN CA  C    sing N N 94  
GLN CA  CB   sing N N 95  
GLN CA  HA   sing N N 96  
GLN C   O    doub N N 97  
GLN C   OXT  sing N N 98  
GLN CB  CG   sing N N 99  
GLN CB  HB2  sing N N 100 
GLN CB  HB3  sing N N 101 
GLN CG  CD   sing N N 102 
GLN CG  HG2  sing N N 103 
GLN CG  HG3  sing N N 104 
GLN CD  OE1  doub N N 105 
GLN CD  NE2  sing N N 106 
GLN NE2 HE21 sing N N 107 
GLN NE2 HE22 sing N N 108 
GLN OXT HXT  sing N N 109 
GLU N   CA   sing N N 110 
GLU N   H    sing N N 111 
GLU N   H2   sing N N 112 
GLU CA  C    sing N N 113 
GLU CA  CB   sing N N 114 
GLU CA  HA   sing N N 115 
GLU C   O    doub N N 116 
GLU C   OXT  sing N N 117 
GLU CB  CG   sing N N 118 
GLU CB  HB2  sing N N 119 
GLU CB  HB3  sing N N 120 
GLU CG  CD   sing N N 121 
GLU CG  HG2  sing N N 122 
GLU CG  HG3  sing N N 123 
GLU CD  OE1  doub N N 124 
GLU CD  OE2  sing N N 125 
GLU OE2 HE2  sing N N 126 
GLU OXT HXT  sing N N 127 
GLY N   CA   sing N N 128 
GLY N   H    sing N N 129 
GLY N   H2   sing N N 130 
GLY CA  C    sing N N 131 
GLY CA  HA2  sing N N 132 
GLY CA  HA3  sing N N 133 
GLY C   O    doub N N 134 
GLY C   OXT  sing N N 135 
GLY OXT HXT  sing N N 136 
HIS N   CA   sing N N 137 
HIS N   H    sing N N 138 
HIS N   H2   sing N N 139 
HIS CA  C    sing N N 140 
HIS CA  CB   sing N N 141 
HIS CA  HA   sing N N 142 
HIS C   O    doub N N 143 
HIS C   OXT  sing N N 144 
HIS CB  CG   sing N N 145 
HIS CB  HB2  sing N N 146 
HIS CB  HB3  sing N N 147 
HIS CG  ND1  sing Y N 148 
HIS CG  CD2  doub Y N 149 
HIS ND1 CE1  doub Y N 150 
HIS ND1 HD1  sing N N 151 
HIS CD2 NE2  sing Y N 152 
HIS CD2 HD2  sing N N 153 
HIS CE1 NE2  sing Y N 154 
HIS CE1 HE1  sing N N 155 
HIS NE2 HE2  sing N N 156 
HIS OXT HXT  sing N N 157 
ILE N   CA   sing N N 158 
ILE N   H    sing N N 159 
ILE N   H2   sing N N 160 
ILE CA  C    sing N N 161 
ILE CA  CB   sing N N 162 
ILE CA  HA   sing N N 163 
ILE C   O    doub N N 164 
ILE C   OXT  sing N N 165 
ILE CB  CG1  sing N N 166 
ILE CB  CG2  sing N N 167 
ILE CB  HB   sing N N 168 
ILE CG1 CD1  sing N N 169 
ILE CG1 HG12 sing N N 170 
ILE CG1 HG13 sing N N 171 
ILE CG2 HG21 sing N N 172 
ILE CG2 HG22 sing N N 173 
ILE CG2 HG23 sing N N 174 
ILE CD1 HD11 sing N N 175 
ILE CD1 HD12 sing N N 176 
ILE CD1 HD13 sing N N 177 
ILE OXT HXT  sing N N 178 
LEU N   CA   sing N N 179 
LEU N   H    sing N N 180 
LEU N   H2   sing N N 181 
LEU CA  C    sing N N 182 
LEU CA  CB   sing N N 183 
LEU CA  HA   sing N N 184 
LEU C   O    doub N N 185 
LEU C   OXT  sing N N 186 
LEU CB  CG   sing N N 187 
LEU CB  HB2  sing N N 188 
LEU CB  HB3  sing N N 189 
LEU CG  CD1  sing N N 190 
LEU CG  CD2  sing N N 191 
LEU CG  HG   sing N N 192 
LEU CD1 HD11 sing N N 193 
LEU CD1 HD12 sing N N 194 
LEU CD1 HD13 sing N N 195 
LEU CD2 HD21 sing N N 196 
LEU CD2 HD22 sing N N 197 
LEU CD2 HD23 sing N N 198 
LEU OXT HXT  sing N N 199 
LYS N   CA   sing N N 200 
LYS N   H    sing N N 201 
LYS N   H2   sing N N 202 
LYS CA  C    sing N N 203 
LYS CA  CB   sing N N 204 
LYS CA  HA   sing N N 205 
LYS C   O    doub N N 206 
LYS C   OXT  sing N N 207 
LYS CB  CG   sing N N 208 
LYS CB  HB2  sing N N 209 
LYS CB  HB3  sing N N 210 
LYS CG  CD   sing N N 211 
LYS CG  HG2  sing N N 212 
LYS CG  HG3  sing N N 213 
LYS CD  CE   sing N N 214 
LYS CD  HD2  sing N N 215 
LYS CD  HD3  sing N N 216 
LYS CE  NZ   sing N N 217 
LYS CE  HE2  sing N N 218 
LYS CE  HE3  sing N N 219 
LYS NZ  HZ1  sing N N 220 
LYS NZ  HZ2  sing N N 221 
LYS NZ  HZ3  sing N N 222 
LYS OXT HXT  sing N N 223 
MET N   CA   sing N N 224 
MET N   H    sing N N 225 
MET N   H2   sing N N 226 
MET CA  C    sing N N 227 
MET CA  CB   sing N N 228 
MET CA  HA   sing N N 229 
MET C   O    doub N N 230 
MET C   OXT  sing N N 231 
MET CB  CG   sing N N 232 
MET CB  HB2  sing N N 233 
MET CB  HB3  sing N N 234 
MET CG  SD   sing N N 235 
MET CG  HG2  sing N N 236 
MET CG  HG3  sing N N 237 
MET SD  CE   sing N N 238 
MET CE  HE1  sing N N 239 
MET CE  HE2  sing N N 240 
MET CE  HE3  sing N N 241 
MET OXT HXT  sing N N 242 
NO3 N   O1   doub N N 243 
NO3 N   O2   sing N N 244 
NO3 N   O3   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 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7ave 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RLI 
_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]   0.036873 
_atom_sites.fract_transf_matrix[1][2]   -0.015096 
_atom_sites.fract_transf_matrix[1][3]   -0.013788 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.034162 
_atom_sites.fract_transf_matrix[2][3]   0.003989 
_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]   0.030990 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
D 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A GLY A 1 1   ? 29.398 26.994 28.427 0.467 31.74  ? 0   GLY A N    1 
ATOM   2    N N    B GLY A 1 1   ? 29.141 26.196 26.583 0.533 29.54  ? 0   GLY A N    1 
ATOM   3    C CA   A GLY A 1 1   ? 29.807 25.717 27.864 0.467 27.44  ? 0   GLY A CA   1 
ATOM   4    C CA   B GLY A 1 1   ? 30.348 25.407 26.634 0.533 25.01  ? 0   GLY A CA   1 
ATOM   5    C C    A GLY A 1 1   ? 28.754 24.664 28.177 0.467 22.63  ? 0   GLY A C    1 
ATOM   6    C C    B GLY A 1 1   ? 30.238 24.136 27.458 0.533 23.03  ? 0   GLY A C    1 
ATOM   7    O O    A GLY A 1 1   ? 27.817 24.946 28.922 0.467 29.28  ? 0   GLY A O    1 
ATOM   8    O O    B GLY A 1 1   ? 31.160 23.703 28.141 0.533 24.50  ? 0   GLY A O    1 
ATOM   9    D D1   A GLY A 1 1   ? 29.789 27.117 29.377 0.467 47.60  ? 0   GLY A D1   1 
ATOM   10   D D1   B GLY A 1 1   ? 28.562 26.061 27.429 0.533 44.31  ? 0   GLY A D1   1 
ATOM   11   D D2   A GLY A 1 1   ? 29.692 27.775 27.823 0.467 47.60  ? 0   GLY A D2   1 
ATOM   12   D D2   B GLY A 1 1   ? 29.352 27.208 26.516 0.533 44.31  ? 0   GLY A D2   1 
ATOM   13   D D3   A GLY A 1 1   ? 28.363 27.032 28.521 0.467 47.60  ? 0   GLY A D3   1 
ATOM   14   D D3   B GLY A 1 1   ? 28.561 25.947 25.760 0.533 44.31  ? 0   GLY A D3   1 
ATOM   15   D DA2  A GLY A 1 1   ? 29.939 25.817 26.798 0.467 32.93  ? 0   GLY A DA2  1 
ATOM   16   D DA2  B GLY A 1 1   ? 30.572 25.083 25.615 0.533 30.01  ? 0   GLY A DA2  1 
ATOM   17   D DA3  A GLY A 1 1   ? 30.731 25.362 28.310 0.467 32.93  ? 0   GLY A DA3  1 
ATOM   18   D DA3  B GLY A 1 1   ? 31.178 25.974 27.026 0.533 30.01  ? 0   GLY A DA3  1 
ATOM   19   N N    A LYS A 1 2   ? 28.928 23.470 27.627 0.548 24.47  ? 1   LYS A N    1 
ATOM   20   N N    B LYS A 1 2   ? 29.052 23.551 27.371 0.452 23.28  ? 1   LYS A N    1 
ATOM   21   C CA   A LYS A 1 2   ? 28.606 22.222 28.281 0.548 17.00  ? 1   LYS A CA   1 
ATOM   22   C CA   B LYS A 1 2   ? 28.739 22.309 28.052 0.452 16.78  ? 1   LYS A CA   1 
ATOM   23   C C    A LYS A 1 2   ? 29.277 21.041 27.575 0.548 12.29  ? 1   LYS A C    1 
ATOM   24   C C    B LYS A 1 2   ? 29.538 21.139 27.492 0.452 13.06  ? 1   LYS A C    1 
ATOM   25   O O    A LYS A 1 2   ? 29.153 20.840 26.374 0.548 11.15  ? 1   LYS A O    1 
ATOM   26   O O    B LYS A 1 2   ? 29.767 21.032 26.292 0.452 15.05  ? 1   LYS A O    1 
ATOM   27   C CB   A LYS A 1 2   ? 27.093 21.982 28.381 0.548 18.51  ? 1   LYS A CB   1 
ATOM   28   C CB   B LYS A 1 2   ? 27.224 22.044 28.001 0.452 18.70  ? 1   LYS A CB   1 
ATOM   29   C CG   A LYS A 1 2   ? 26.738 20.758 29.202 0.548 18.88  ? 1   LYS A CG   1 
ATOM   30   C CG   B LYS A 1 2   ? 26.809 20.813 28.773 0.452 18.93  ? 1   LYS A CG   1 
ATOM   31   C CD   A LYS A 1 2   ? 25.243 20.499 29.290 0.548 20.04  ? 1   LYS A CD   1 
ATOM   32   C CD   B LYS A 1 2   ? 25.397 20.889 29.337 0.452 20.36  ? 1   LYS A CD   1 
ATOM   33   C CE   A LYS A 1 2   ? 24.954 19.260 30.111 0.548 20.22  ? 1   LYS A CE   1 
ATOM   34   C CE   B LYS A 1 2   ? 24.962 19.608 30.015 0.452 20.03  ? 1   LYS A CE   1 
ATOM   35   N NZ   A LYS A 1 2   ? 25.158 19.462 31.572 0.548 19.52  ? 1   LYS A NZ   1 
ATOM   36   N NZ   B LYS A 1 2   ? 23.573 19.642 30.543 0.452 21.04  ? 1   LYS A NZ   1 
ATOM   37   D D    A LYS A 1 2   ? 29.329 23.420 26.708 0.548 25.98  ? 1   LYS A D    1 
ATOM   38   D D    B LYS A 1 2   ? 28.317 24.002 26.852 0.452 24.48  ? 1   LYS A D    1 
ATOM   39   D DA   A LYS A 1 2   ? 29.017 22.247 29.298 0.548 17.62  ? 1   LYS A DA   1 
ATOM   40   D DA   B LYS A 1 2   ? 29.021 22.447 29.108 0.452 16.74  ? 1   LYS A DA   1 
ATOM   41   D DB2  A LYS A 1 2   ? 26.648 22.863 28.838 0.548 20.48  ? 1   LYS A DB2  1 
ATOM   42   D DB2  B LYS A 1 2   ? 26.720 22.916 28.384 0.452 17.49  ? 1   LYS A DB2  1 
ATOM   43   D DB3  A LYS A 1 2   ? 26.702 21.880 27.377 0.548 19.68  ? 1   LYS A DB3  1 
ATOM   44   D DB3  B LYS A 1 2   ? 26.947 21.933 26.956 0.452 19.81  ? 1   LYS A DB3  1 
ATOM   45   D DG2  A LYS A 1 2   ? 27.222 19.870 28.747 0.548 18.36  ? 1   LYS A DG2  1 
ATOM   46   D DG2  B LYS A 1 2   ? 26.896 19.929 28.127 0.452 20.66  ? 1   LYS A DG2  1 
ATOM   47   D DG3  A LYS A 1 2   ? 27.147 20.855 30.211 0.548 16.90  ? 1   LYS A DG3  1 
ATOM   48   D DG3  B LYS A 1 2   ? 27.508 20.658 29.621 0.452 18.85  ? 1   LYS A DG3  1 
ATOM   49   D DD2  A LYS A 1 2   ? 24.771 21.358 29.780 0.548 20.66  ? 1   LYS A DD2  1 
ATOM   50   D DD2  B LYS A 1 2   ? 25.374 21.700 30.080 0.452 21.05  ? 1   LYS A DD2  1 
ATOM   51   D DD3  A LYS A 1 2   ? 24.861 20.355 28.276 0.548 21.47  ? 1   LYS A DD3  1 
ATOM   52   D DD3  B LYS A 1 2   ? 24.712 21.112 28.518 0.452 22.15  ? 1   LYS A DD3  1 
ATOM   53   D DE2  A LYS A 1 2   ? 23.925 18.970 29.885 0.548 22.74  ? 1   LYS A DE2  1 
ATOM   54   D DE2  B LYS A 1 2   ? 25.096 18.746 29.377 0.452 18.58  ? 1   LYS A DE2  1 
ATOM   55   D DE3  A LYS A 1 2   ? 25.580 18.444 29.762 0.548 19.50  ? 1   LYS A DE3  1 
ATOM   56   D DE3  B LYS A 1 2   ? 25.625 19.462 30.874 0.452 19.85  ? 1   LYS A DE3  1 
ATOM   57   D DZ1  A LYS A 1 2   ? 26.161 19.361 31.781 0.548 19.83  ? 1   LYS A DZ1  1 
ATOM   58   D DZ1  B LYS A 1 2   ? 23.255 18.673 30.681 0.452 24.67  ? 1   LYS A DZ1  1 
ATOM   59   D DZ2  A LYS A 1 2   ? 24.888 20.416 31.816 0.548 20.88  ? 1   LYS A DZ2  1 
ATOM   60   D DZ2  B LYS A 1 2   ? 23.573 20.131 31.441 0.452 22.69  ? 1   LYS A DZ2  1 
ATOM   61   D DZ3  A LYS A 1 2   ? 24.649 18.739 32.080 0.548 20.64  ? 1   LYS A DZ3  1 
ATOM   62   D DZ3  B LYS A 1 2   ? 22.966 20.106 29.859 0.452 25.36  ? 1   LYS A DZ3  1 
ATOM   63   N N    . VAL A 1 3   ? 29.987 20.280 28.386 1.000 11.83  ? 2   VAL A N    1 
ATOM   64   C CA   . VAL A 1 3   ? 30.490 18.985 28.041 1.000 11.58  ? 2   VAL A CA   1 
ATOM   65   C C    . VAL A 1 3   ? 29.680 17.960 28.841 1.000 11.11  ? 2   VAL A C    1 
ATOM   66   O O    . VAL A 1 3   ? 29.687 18.007 30.065 1.000 11.39  ? 2   VAL A O    1 
ATOM   67   C CB   . VAL A 1 3   ? 31.974 18.867 28.369 1.000 12.73  ? 2   VAL A CB   1 
ATOM   68   C CG1  . VAL A 1 3   ? 32.507 17.492 27.943 1.000 13.45  ? 2   VAL A CG1  1 
ATOM   69   C CG2  . VAL A 1 3   ? 32.798 19.978 27.725 1.000 15.08  ? 2   VAL A CG2  1 
ATOM   70   D D    . VAL A 1 3   ? 30.079 20.547 29.357 1.000 13.61  ? 2   VAL A D    1 
ATOM   71   D DA   . VAL A 1 3   ? 30.368 18.803 26.976 1.000 12.03  ? 2   VAL A DA   1 
ATOM   72   D DB   . VAL A 1 3   ? 32.087 18.931 29.468 1.000 13.51  ? 2   VAL A DB   1 
ATOM   73   D DG11 . VAL A 1 3   ? 32.385 17.385 26.894 1.000 16.84  ? 2   VAL A DG11 1 
ATOM   74   D DG12 . VAL A 1 3   ? 33.532 17.422 28.239 1.000 16.60  ? 2   VAL A DG12 1 
ATOM   75   D DG13 . VAL A 1 3   ? 31.920 16.723 28.353 1.000 14.92  ? 2   VAL A DG13 1 
ATOM   76   D DG21 . VAL A 1 3   ? 32.692 19.976 26.684 1.000 18.79  ? 2   VAL A DG21 1 
ATOM   77   D DG22 . VAL A 1 3   ? 32.475 20.930 28.052 1.000 18.90  ? 2   VAL A DG22 1 
ATOM   78   D DG23 . VAL A 1 3   ? 33.817 19.877 27.945 1.000 18.78  ? 2   VAL A DG23 1 
ATOM   79   N N    . PHE A 1 4   ? 28.994 17.059 28.154 1.000 10.40  ? 3   PHE A N    1 
ATOM   80   C CA   . PHE A 1 4   ? 28.134 16.097 28.810 1.000 10.16  ? 3   PHE A CA   1 
ATOM   81   C C    . PHE A 1 4   ? 28.961 14.949 29.401 1.000 9.85   ? 3   PHE A C    1 
ATOM   82   O O    . PHE A 1 4   ? 30.034 14.628 28.904 1.000 11.85  ? 3   PHE A O    1 
ATOM   83   C CB   . PHE A 1 4   ? 27.175 15.475 27.808 1.000 11.13  ? 3   PHE A CB   1 
ATOM   84   C CG   . PHE A 1 4   ? 25.885 16.232 27.593 1.000 11.40  ? 3   PHE A CG   1 
ATOM   85   C CD1  . PHE A 1 4   ? 25.788 17.282 26.706 1.000 12.80  ? 3   PHE A CD1  1 
ATOM   86   C CD2  . PHE A 1 4   ? 24.743 15.868 28.309 1.000 12.47  ? 3   PHE A CD2  1 
ATOM   87   C CE1  . PHE A 1 4   ? 24.610 17.968 26.497 1.000 14.96  ? 3   PHE A CE1  1 
ATOM   88   C CE2  . PHE A 1 4   ? 23.547 16.571 28.132 1.000 13.50  ? 3   PHE A CE2  1 
ATOM   89   C CZ   . PHE A 1 4   ? 23.493 17.616 27.235 1.000 14.92  ? 3   PHE A CZ   1 
ATOM   90   D D    . PHE A 1 4   ? 29.157 17.023 27.168 1.000 12.29  ? 3   PHE A D    1 
ATOM   91   D DA   . PHE A 1 4   ? 27.580 16.586 29.622 1.000 10.53  ? 3   PHE A DA   1 
ATOM   92   D DB2  . PHE A 1 4   ? 27.672 15.350 26.873 1.000 14.00  ? 3   PHE A DB2  1 
ATOM   93   D DB3  . PHE A 1 4   ? 26.930 14.467 28.146 1.000 13.85  ? 3   PHE A DB3  1 
ATOM   94   D DD1  . PHE A 1 4   ? 26.671 17.592 26.140 1.000 17.33  ? 3   PHE A DD1  1 
ATOM   95   D DD2  . PHE A 1 4   ? 24.796 15.064 29.006 1.000 15.58  ? 3   PHE A DD2  1 
ATOM   96   D DE1  . PHE A 1 4   ? 24.561 18.746 25.765 1.000 22.57  ? 3   PHE A DE1  1 
ATOM   97   D DE2  . PHE A 1 4   ? 22.689 16.303 28.715 1.000 19.66  ? 3   PHE A DE2  1 
ATOM   98   D DZ   . PHE A 1 4   ? 22.596 18.228 27.161 1.000 19.58  ? 3   PHE A DZ   1 
ATOM   99   N N    . GLY A 1 5   ? 28.368 14.354 30.429 1.000 10.19  ? 4   GLY A N    1 
ATOM   100  C CA   . GLY A 1 5   ? 28.747 13.022 30.852 1.000 10.62  ? 4   GLY A CA   1 
ATOM   101  C C    . GLY A 1 5   ? 28.027 11.971 30.011 1.000 9.30   ? 4   GLY A C    1 
ATOM   102  O O    . GLY A 1 5   ? 27.005 12.199 29.409 1.000 10.07  ? 4   GLY A O    1 
ATOM   103  D D    . GLY A 1 5   ? 27.574 14.811 30.834 1.000 11.84  ? 4   GLY A D    1 
ATOM   104  D DA2  . GLY A 1 5   ? 29.823 12.867 30.745 1.000 13.66  ? 4   GLY A DA2  1 
ATOM   105  D DA3  . GLY A 1 5   ? 28.475 12.854 31.889 1.000 13.97  ? 4   GLY A DA3  1 
ATOM   106  N N    A ARG A 1 6   ? 28.644 10.812 30.033 0.612 10.11  ? 5   ARG A N    1 
ATOM   107  N N    B ARG A 1 6   ? 28.495 10.710 29.978 0.388 10.47  ? 5   ARG A N    1 
ATOM   108  C CA   A ARG A 1 6   ? 28.101 9.683  29.298 0.612 10.47  ? 5   ARG A CA   1 
ATOM   109  C CA   B ARG A 1 6   ? 27.911 9.711  29.082 0.388 11.36  ? 5   ARG A CA   1 
ATOM   110  C C    A ARG A 1 6   ? 26.647 9.370  29.606 0.612 10.28  ? 5   ARG A C    1 
ATOM   111  C C    B ARG A 1 6   ? 26.516 9.330  29.580 0.388 10.53  ? 5   ARG A C    1 
ATOM   112  O O    A ARG A 1 6   ? 25.809 9.330  28.717 0.612 9.66   ? 5   ARG A O    1 
ATOM   113  O O    B ARG A 1 6   ? 25.573 9.214  28.793 0.388 10.13  ? 5   ARG A O    1 
ATOM   114  C CB   A ARG A 1 6   ? 29.015 8.500  29.628 0.612 11.75  ? 5   ARG A CB   1 
ATOM   115  C CB   B ARG A 1 6   ? 28.725 8.427  28.857 0.388 12.25  ? 5   ARG A CB   1 
ATOM   116  C CG   A ARG A 1 6   ? 28.603 7.246  28.905 0.612 13.71  ? 5   ARG A CG   1 
ATOM   117  C CG   B ARG A 1 6   ? 28.960 7.513  30.041 0.388 14.76  ? 5   ARG A CG   1 
ATOM   118  C CD   A ARG A 1 6   ? 29.569 6.107  29.181 0.612 15.62  ? 5   ARG A CD   1 
ATOM   119  C CD   B ARG A 1 6   ? 29.877 6.357  29.694 0.388 15.66  ? 5   ARG A CD   1 
ATOM   120  N NE   A ARG A 1 6   ? 29.561 5.754  30.596 0.612 17.80  ? 5   ARG A NE   1 
ATOM   121  N NE   B ARG A 1 6   ? 30.100 5.523  30.865 0.388 17.78  ? 5   ARG A NE   1 
ATOM   122  C CZ   A ARG A 1 6   ? 28.890 4.774  31.194 0.612 19.21  ? 5   ARG A CZ   1 
ATOM   123  C CZ   B ARG A 1 6   ? 29.281 4.568  31.265 0.388 18.67  ? 5   ARG A CZ   1 
ATOM   124  N NH1  A ARG A 1 6   ? 28.080 4.000  30.480 0.612 18.83  ? 5   ARG A NH1  1 
ATOM   125  N NH1  B ARG A 1 6   ? 29.717 3.803  32.263 0.388 19.48  ? 5   ARG A NH1  1 
ATOM   126  N NH2  A ARG A 1 6   ? 29.001 4.568  32.502 0.612 20.48  ? 5   ARG A NH2  1 
ATOM   127  N NH2  B ARG A 1 6   ? 28.084 4.399  30.742 0.388 18.72  ? 5   ARG A NH2  1 
ATOM   128  D D    A ARG A 1 6   ? 29.521 10.674 30.509 0.612 12.98  ? 5   ARG A D    1 
ATOM   129  D D    B ARG A 1 6   ? 29.264 10.443 30.571 0.388 20.69  ? 5   ARG A D    1 
ATOM   130  D DA   A ARG A 1 6   ? 28.168 9.917  28.223 0.612 10.81  ? 5   ARG A DA   1 
ATOM   131  D DA   B ARG A 1 6   ? 27.753 10.213 28.105 0.388 10.56  ? 5   ARG A DA   1 
ATOM   132  D DB2  A ARG A 1 6   ? 30.028 8.776  29.321 0.612 12.38  ? 5   ARG A DB2  1 
ATOM   133  D DB2  B ARG A 1 6   ? 28.191 7.848  28.086 0.388 13.98  ? 5   ARG A DB2  1 
ATOM   134  D DB3  A ARG A 1 6   ? 28.983 8.342  30.689 0.612 13.31  ? 5   ARG A DB3  1 
ATOM   135  D DB3  B ARG A 1 6   ? 29.694 8.732  28.462 0.388 13.72  ? 5   ARG A DB3  1 
ATOM   136  D DG2  A ARG A 1 6   ? 27.613 6.939  29.235 0.612 14.73  ? 5   ARG A DG2  1 
ATOM   137  D DG2  B ARG A 1 6   ? 29.418 8.091  30.840 0.388 13.50  ? 5   ARG A DG2  1 
ATOM   138  D DG3  A ARG A 1 6   ? 28.518 7.422  27.854 0.612 15.17  ? 5   ARG A DG3  1 
ATOM   139  D DG3  B ARG A 1 6   ? 28.000 7.115  30.367 0.388 14.30  ? 5   ARG A DG3  1 
ATOM   140  D DD2  A ARG A 1 6   ? 29.217 5.262  28.586 0.612 17.55  ? 5   ARG A DD2  1 
ATOM   141  D DD2  B ARG A 1 6   ? 29.463 5.753  28.887 0.388 16.27  ? 5   ARG A DD2  1 
ATOM   142  D DD3  A ARG A 1 6   ? 30.563 6.342  28.815 0.612 17.25  ? 5   ARG A DD3  1 
ATOM   143  D DD3  B ARG A 1 6   ? 30.835 6.725  29.321 0.388 16.35  ? 5   ARG A DD3  1 
ATOM   144  D DE   A ARG A 1 6   ? 30.153 6.376  31.129 0.612 20.58  ? 5   ARG A DE   1 
ATOM   145  D DE   B ARG A 1 6   ? 30.943 5.762  31.338 0.388 21.56  ? 5   ARG A DE   1 
ATOM   146  D DH11 A ARG A 1 6   ? 27.755 3.131  30.881 0.612 19.05  ? 5   ARG A DH11 1 
ATOM   147  D DH11 B ARG A 1 6   ? 29.324 2.878  32.376 0.388 26.11  ? 5   ARG A DH11 1 
ATOM   148  D DH12 A ARG A 1 6   ? 27.784 4.320  29.567 0.612 18.18  ? 5   ARG A DH12 1 
ATOM   149  D DH12 B ARG A 1 6   ? 30.434 4.161  32.875 0.388 24.96  ? 5   ARG A DH12 1 
ATOM   150  D DH21 A ARG A 1 6   ? 28.442 3.863  32.952 0.612 28.37  ? 5   ARG A DH21 1 
ATOM   151  D DH21 B ARG A 1 6   ? 27.438 3.734  31.140 0.388 19.34  ? 5   ARG A DH21 1 
ATOM   152  D DH22 A ARG A 1 6   ? 29.630 5.151  33.039 0.612 31.63  ? 5   ARG A DH22 1 
ATOM   153  D DH22 B ARG A 1 6   ? 27.793 4.946  29.943 0.388 17.16  ? 5   ARG A DH22 1 
ATOM   154  N N    . CYS A 1 7   ? 26.357 9.137  30.884 1.000 10.69  ? 6   CYS A N    1 
ATOM   155  C CA   . CYS A 1 7   ? 25.019 8.741  31.319 1.000 11.06  ? 6   CYS A CA   1 
ATOM   156  C C    . CYS A 1 7   ? 24.029 9.902  31.189 1.000 9.69   ? 6   CYS A C    1 
ATOM   157  O O    . CYS A 1 7   ? 22.878 9.649  30.855 1.000 11.02  ? 6   CYS A O    1 
ATOM   158  C CB   . CYS A 1 7   ? 25.021 8.236  32.745 1.000 12.57  ? 6   CYS A CB   1 
ATOM   159  S SG   . CYS A 1 7   ? 25.900 6.667  32.967 1.000 15.68  ? 6   CYS A SG   1 
ATOM   160  D D    . CYS A 1 7   ? 27.076 9.285  31.572 1.000 13.01  ? 6   CYS A D    1 
ATOM   161  D DA   . CYS A 1 7   ? 24.645 7.936  30.666 1.000 11.96  ? 6   CYS A DA   1 
ATOM   162  D DB2  . CYS A 1 7   ? 25.515 8.977  33.396 1.000 15.55  ? 6   CYS A DB2  1 
ATOM   163  D DB3  . CYS A 1 7   ? 24.008 8.130  33.116 1.000 14.47  ? 6   CYS A DB3  1 
ATOM   164  N N    . GLU A 1 8   ? 24.494 11.094 31.452 1.000 9.91   ? 7   GLU A N    1 
ATOM   165  C CA   . GLU A 1 8   ? 23.649 12.288 31.301 1.000 9.94   ? 7   GLU A CA   1 
ATOM   166  C C    . GLU A 1 8   ? 23.218 12.472 29.852 1.000 9.74   ? 7   GLU A C    1 
ATOM   167  O O    . GLU A 1 8   ? 22.071 12.778 29.575 1.000 10.96  ? 7   GLU A O    1 
ATOM   168  C CB   . GLU A 1 8   ? 24.390 13.514 31.795 1.000 11.28  ? 7   GLU A CB   1 
ATOM   169  C CG   . GLU A 1 8   ? 24.648 13.487 33.274 1.000 12.92  ? 7   GLU A CG   1 
ATOM   170  C CD   . GLU A 1 8   ? 25.733 12.596 33.868 1.000 12.70  ? 7   GLU A CD   1 
ATOM   171  O OE1  . GLU A 1 8   ? 26.467 11.936 33.135 1.000 13.62  ? 7   GLU A OE1  1 
ATOM   172  O OE2  . GLU A 1 8   ? 25.764 12.669 35.126 1.000 13.87  ? 7   GLU A OE2  1 
ATOM   173  D D    . GLU A 1 8   ? 25.453 11.267 31.756 1.000 11.58  ? 7   GLU A D    1 
ATOM   174  D DA   . GLU A 1 8   ? 22.712 12.156 31.863 1.000 10.56  ? 7   GLU A DA   1 
ATOM   175  D DB2  . GLU A 1 8   ? 25.322 13.615 31.249 1.000 11.75  ? 7   GLU A DB2  1 
ATOM   176  D DB3  . GLU A 1 8   ? 23.789 14.410 31.548 1.000 12.61  ? 7   GLU A DB3  1 
ATOM   177  D DG2  . GLU A 1 8   ? 24.888 14.523 33.605 1.000 16.56  ? 7   GLU A DG2  1 
ATOM   178  D DG3  . GLU A 1 8   ? 23.730 13.295 33.821 1.000 16.33  ? 7   GLU A DG3  1 
ATOM   179  N N    . LEU A 1 9   ? 24.146 12.256 28.923 1.000 9.31   ? 8   LEU A N    1 
ATOM   180  C CA   . LEU A 1 9   ? 23.799 12.334 27.524 1.000 9.47   ? 8   LEU A CA   1 
ATOM   181  C C    . LEU A 1 9   ? 22.857 11.192 27.114 1.000 9.72   ? 8   LEU A C    1 
ATOM   182  O O    . LEU A 1 9   ? 21.887 11.418 26.388 1.000 10.45  ? 8   LEU A O    1 
ATOM   183  C CB   . LEU A 1 9   ? 25.037 12.309 26.632 1.000 10.07  ? 8   LEU A CB   1 
ATOM   184  C CG   . LEU A 1 9   ? 24.735 12.496 25.140 1.000 11.42  ? 8   LEU A CG   1 
ATOM   185  C CD1  . LEU A 1 9   ? 24.097 13.832 24.828 1.000 12.56  ? 8   LEU A CD1  1 
ATOM   186  C CD2  . LEU A 1 9   ? 26.045 12.327 24.362 1.000 14.61  ? 8   LEU A CD2  1 
ATOM   187  H H    . LEU A 1 9   ? 25.093 12.037 29.196 1.000 17.90  ? 8   LEU A H    1 
ATOM   188  D DA   . LEU A 1 9   ? 23.229 13.280 27.351 1.000 10.08  ? 8   LEU A DA   1 
ATOM   189  D DB2  . LEU A 1 9   ? 25.708 13.119 26.953 1.000 12.54  ? 8   LEU A DB2  1 
ATOM   190  D DB3  . LEU A 1 9   ? 25.585 11.377 26.778 1.000 12.44  ? 8   LEU A DB3  1 
ATOM   191  D DG   . LEU A 1 9   ? 24.068 11.694 24.837 1.000 12.78  ? 8   LEU A DG   1 
ATOM   192  D DD11 . LEU A 1 9   ? 24.704 14.627 25.198 1.000 17.69  ? 8   LEU A DD11 1 
ATOM   193  D DD12 . LEU A 1 9   ? 23.962 13.959 23.785 1.000 16.09  ? 8   LEU A DD12 1 
ATOM   194  D DD13 . LEU A 1 9   ? 23.128 13.890 25.287 1.000 16.97  ? 8   LEU A DD13 1 
ATOM   195  D DD21 . LEU A 1 9   ? 26.717 13.074 24.700 1.000 18.45  ? 8   LEU A DD21 1 
ATOM   196  D DD22 . LEU A 1 9   ? 26.428 11.357 24.573 1.000 19.48  ? 8   LEU A DD22 1 
ATOM   197  D DD23 . LEU A 1 9   ? 25.825 12.397 23.328 1.000 20.18  ? 8   LEU A DD23 1 
ATOM   198  N N    . ALA A 1 10  ? 23.122 9.988  27.605 1.000 10.11  ? 9   ALA A N    1 
ATOM   199  C CA   . ALA A 1 10  ? 22.214 8.890  27.298 1.000 10.84  ? 9   ALA A CA   1 
ATOM   200  C C    . ALA A 1 10  ? 20.790 9.205  27.745 1.000 10.75  ? 9   ALA A C    1 
ATOM   201  O O    . ALA A 1 10  ? 19.836 8.952  26.995 1.000 11.81  ? 9   ALA A O    1 
ATOM   202  C CB   . ALA A 1 10  ? 22.693 7.615  27.971 1.000 12.56  ? 9   ALA A CB   1 
ATOM   203  H H    . ALA A 1 10  ? 23.938 9.836  28.181 1.000 13.13  ? 9   ALA A H    1 
ATOM   204  D DA   . ALA A 1 10  ? 22.126 8.752  26.220 1.000 12.52  ? 9   ALA A DA   1 
ATOM   205  D DB1  . ALA A 1 10  ? 22.699 7.722  29.032 1.000 14.50  ? 9   ALA A DB1  1 
ATOM   206  D DB2  . ALA A 1 10  ? 22.107 6.790  27.679 1.000 15.48  ? 9   ALA A DB2  1 
ATOM   207  D DB3  . ALA A 1 10  ? 23.713 7.422  27.682 1.000 16.06  ? 9   ALA A DB3  1 
ATOM   208  N N    . ALA A 1 11  ? 20.626 9.752  28.951 1.000 11.30  ? 10  ALA A N    1 
ATOM   209  C CA   . ALA A 1 11  ? 19.283 10.073 29.445 1.000 12.18  ? 10  ALA A CA   1 
ATOM   210  C C    . ALA A 1 11  ? 18.623 11.155 28.581 1.000 12.22  ? 10  ALA A C    1 
ATOM   211  O O    . ALA A 1 11  ? 17.433 11.102 28.320 1.000 13.57  ? 10  ALA A O    1 
ATOM   212  C CB   . ALA A 1 11  ? 19.335 10.506 30.900 1.000 13.87  ? 10  ALA A CB   1 
ATOM   213  H H    . ALA A 1 11  ? 21.433 9.946  29.528 1.000 15.84  ? 10  ALA A H    1 
ATOM   214  D DA   . ALA A 1 11  ? 18.713 9.162  29.321 1.000 13.95  ? 10  ALA A DA   1 
ATOM   215  D DB1  . ALA A 1 11  ? 19.978 11.328 31.033 1.000 14.49  ? 10  ALA A DB1  1 
ATOM   216  D DB2  . ALA A 1 11  ? 18.365 10.728 31.273 1.000 17.01  ? 10  ALA A DB2  1 
ATOM   217  D DB3  . ALA A 1 11  ? 19.719 9.714  31.507 1.000 17.86  ? 10  ALA A DB3  1 
ATOM   218  N N    . ALA A 1 12  ? 19.408 12.177 28.214 1.000 11.19  ? 11  ALA A N    1 
ATOM   219  C CA   . ALA A 1 12  ? 18.868 13.230 27.378 1.000 11.34  ? 11  ALA A CA   1 
ATOM   220  C C    . ALA A 1 12  ? 18.432 12.701 25.999 1.000 11.80  ? 11  ALA A C    1 
ATOM   221  O O    . ALA A 1 12  ? 17.404 13.090 25.478 1.000 11.96  ? 11  ALA A O    1 
ATOM   222  C CB   . ALA A 1 12  ? 19.865 14.357 27.242 1.000 12.99  ? 11  ALA A CB   1 
ATOM   223  H H    . ALA A 1 12  ? 20.370 12.213 28.519 1.000 16.83  ? 11  ALA A H    1 
ATOM   224  D DA   . ALA A 1 12  ? 17.930 13.552 27.790 1.000 12.26  ? 11  ALA A DA   1 
ATOM   225  D DB1  . ALA A 1 12  ? 20.775 14.028 26.800 1.000 13.71  ? 11  ALA A DB1  1 
ATOM   226  D DB2  . ALA A 1 12  ? 19.487 15.122 26.614 1.000 15.29  ? 11  ALA A DB2  1 
ATOM   227  D DB3  . ALA A 1 12  ? 20.094 14.769 28.216 1.000 15.40  ? 11  ALA A DB3  1 
ATOM   228  N N    . MET A 1 13  ? 19.266 11.835 25.425 1.000 10.72  ? 12  MET A N    1 
ATOM   229  C CA   . MET A 1 13  ? 18.932 11.246 24.149 1.000 11.33  ? 12  MET A CA   1 
ATOM   230  C C    . MET A 1 13  ? 17.698 10.338 24.256 1.000 11.84  ? 12  MET A C    1 
ATOM   231  O O    . MET A 1 13  ? 16.867 10.325 23.331 1.000 14.18  ? 12  MET A O    1 
ATOM   232  C CB   . MET A 1 13  ? 20.126 10.482 23.580 1.000 10.50  ? 12  MET A CB   1 
ATOM   233  C CG   . MET A 1 13  ? 21.214 11.414 23.053 1.000 11.05  ? 12  MET A CG   1 
ATOM   234  S SD   . MET A 1 13  ? 22.624 10.454 22.467 1.000 13.74  ? 12  MET A SD   1 
ATOM   235  C CE   . MET A 1 13  ? 23.376 11.590 21.327 1.000 16.61  ? 12  MET A CE   1 
ATOM   236  H H    . MET A 1 13  ? 20.133 11.590 25.883 1.000 15.75  ? 12  MET A H    1 
ATOM   237  D DA   . MET A 1 13  ? 18.653 12.063 23.446 1.000 12.61  ? 12  MET A DA   1 
ATOM   238  D DB2  . MET A 1 13  ? 20.550 9.858  24.359 1.000 12.32  ? 12  MET A DB2  1 
ATOM   239  D DB3  . MET A 1 13  ? 19.778 9.848  22.768 1.000 11.80  ? 12  MET A DB3  1 
ATOM   240  D DG2  . MET A 1 13  ? 20.811 12.013 22.233 1.000 13.55  ? 12  MET A DG2  1 
ATOM   241  D DG3  . MET A 1 13  ? 21.534 12.084 23.855 1.000 12.75  ? 12  MET A DG3  1 
ATOM   242  D DE1  . MET A 1 13  ? 24.247 11.144 20.931 1.000 20.13  ? 12  MET A DE1  1 
ATOM   243  D DE2  . MET A 1 13  ? 22.689 11.754 20.518 1.000 21.91  ? 12  MET A DE2  1 
ATOM   244  D DE3  . MET A 1 13  ? 23.560 12.498 21.819 1.000 21.61  ? 12  MET A DE3  1 
ATOM   245  N N    . LYS A 1 14  ? 17.587 9.598  25.357 1.000 13.02  ? 13  LYS A N    1 
ATOM   246  C CA   . LYS A 1 14  ? 16.409 8.771  25.540 1.000 14.99  ? 13  LYS A CA   1 
ATOM   247  C C    . LYS A 1 14  ? 15.143 9.641  25.624 1.000 14.53  ? 13  LYS A C    1 
ATOM   248  O O    . LYS A 1 14  ? 14.116 9.292  25.061 1.000 15.59  ? 13  LYS A O    1 
ATOM   249  C CB   . LYS A 1 14  ? 16.584 7.877  26.757 1.000 16.61  ? 13  LYS A CB   1 
ATOM   250  C CG   . LYS A 1 14  ? 15.410 6.953  26.995 1.000 21.21  ? 13  LYS A CG   1 
ATOM   251  C CD   . LYS A 1 14  ? 15.713 6.007  28.145 1.000 26.33  ? 13  LYS A CD   1 
ATOM   252  C CE   . LYS A 1 14  ? 14.510 5.129  28.433 1.000 33.70  ? 13  LYS A CE   1 
ATOM   253  N NZ   . LYS A 1 14  ? 13.364 5.971  28.850 1.000 40.95  ? 13  LYS A NZ   1 
ATOM   254  H H    . LYS A 1 14  ? 18.314 9.612  26.058 1.000 15.36  ? 13  LYS A H    1 
ATOM   255  D DA   . LYS A 1 14  ? 16.250 8.141  24.643 1.000 16.63  ? 13  LYS A DA   1 
ATOM   256  D DB2  . LYS A 1 14  ? 17.488 7.272  26.623 1.000 18.25  ? 13  LYS A DB2  1 
ATOM   257  D DB3  . LYS A 1 14  ? 16.741 8.496  27.631 1.000 17.65  ? 13  LYS A DB3  1 
ATOM   258  D DG2  . LYS A 1 14  ? 14.520 7.536  27.233 1.000 26.36  ? 13  LYS A DG2  1 
ATOM   259  D DG3  . LYS A 1 14  ? 15.204 6.372  26.090 1.000 28.65  ? 13  LYS A DG3  1 
ATOM   260  D DD2  . LYS A 1 14  ? 16.560 5.389  27.885 1.000 34.98  ? 13  LYS A DD2  1 
ATOM   261  D DD3  . LYS A 1 14  ? 15.944 6.597  29.032 1.000 31.56  ? 13  LYS A DD3  1 
ATOM   262  D DE2  . LYS A 1 14  ? 14.213 4.619  27.515 1.000 40.44  ? 13  LYS A DE2  1 
ATOM   263  D DE3  . LYS A 1 14  ? 14.779 4.421  29.218 1.000 40.44  ? 13  LYS A DE3  1 
ATOM   264  D DZ1  . LYS A 1 14  ? 13.231 5.874  29.866 1.000 61.42  ? 13  LYS A DZ1  1 
ATOM   265  D DZ2  . LYS A 1 14  ? 13.576 6.954  28.620 1.000 61.42  ? 13  LYS A DZ2  1 
ATOM   266  D DZ3  . LYS A 1 14  ? 12.530 5.680  28.319 1.000 61.42  ? 13  LYS A DZ3  1 
ATOM   267  N N    . ARG A 1 15  ? 15.214 10.733 26.358 1.000 14.65  ? 14  ARG A N    1 
ATOM   268  C CA   . ARG A 1 15  ? 14.084 11.644 26.483 1.000 15.94  ? 14  ARG A CA   1 
ATOM   269  C C    . ARG A 1 15  ? 13.661 12.209 25.136 1.000 16.34  ? 14  ARG A C    1 
ATOM   270  O O    . ARG A 1 15  ? 12.474 12.536 24.947 1.000 18.27  ? 14  ARG A O    1 
ATOM   271  C CB   . ARG A 1 15  ? 14.337 12.811 27.435 1.000 18.86  ? 14  ARG A CB   1 
ATOM   272  C CG   . ARG A 1 15  ? 14.332 12.353 28.884 1.000 20.49  ? 14  ARG A CG   1 
ATOM   273  C CD   . ARG A 1 15  ? 14.369 13.533 29.819 1.000 25.36  ? 14  ARG A CD   1 
ATOM   274  N NE   . ARG A 1 15  ? 15.589 14.324 29.759 1.000 26.33  ? 14  ARG A NE   1 
ATOM   275  C CZ   . ARG A 1 15  ? 16.643 14.109 30.514 1.000 28.96  ? 14  ARG A CZ   1 
ATOM   276  N NH1  . ARG A 1 15  ? 16.676 13.149 31.429 1.000 29.15  ? 14  ARG A NH1  1 
ATOM   277  N NH2  . ARG A 1 15  ? 17.745 14.836 30.418 1.000 30.06  ? 14  ARG A NH2  1 
ATOM   278  D D    . ARG A 1 15  ? 16.056 10.928 26.847 1.000 18.19  ? 14  ARG A D    1 
ATOM   279  D DA   . ARG A 1 15  ? 13.216 11.081 26.838 1.000 17.46  ? 14  ARG A DA   1 
ATOM   280  D DB2  . ARG A 1 15  ? 15.287 13.252 27.208 1.000 19.23  ? 14  ARG A DB2  1 
ATOM   281  D DB3  . ARG A 1 15  ? 13.541 13.537 27.304 1.000 20.51  ? 14  ARG A DB3  1 
ATOM   282  D DG2  . ARG A 1 15  ? 13.395 11.799 29.049 1.000 23.26  ? 14  ARG A DG2  1 
ATOM   283  D DG3  . ARG A 1 15  ? 15.156 11.703 29.048 1.000 23.39  ? 14  ARG A DG3  1 
ATOM   284  D DD2  . ARG A 1 15  ? 13.556 14.236 29.653 1.000 25.59  ? 14  ARG A DD2  1 
ATOM   285  D DD3  . ARG A 1 15  ? 14.281 13.175 30.853 1.000 27.08  ? 14  ARG A DD3  1 
ATOM   286  D DE   . ARG A 1 15  ? 15.510 15.072 29.102 1.000 31.21  ? 14  ARG A DE   1 
ATOM   287  D DH11 . ARG A 1 15  ? 17.508 13.048 32.005 1.000 33.95  ? 14  ARG A DH11 1 
ATOM   288  D DH12 . ARG A 1 15  ? 15.893 12.533 31.541 1.000 33.45  ? 14  ARG A DH12 1 
ATOM   289  D DH21 . ARG A 1 15  ? 18.603 14.473 30.841 1.000 33.63  ? 14  ARG A DH21 1 
ATOM   290  D DH22 . ARG A 1 15  ? 17.734 15.703 29.903 1.000 32.61  ? 14  ARG A DH22 1 
ATOM   291  N N    A HIS A 1 16  ? 14.603 12.331 24.220 0.442 16.27  ? 15  HIS A N    1 
ATOM   292  N N    B HIS A 1 16  ? 14.610 12.325 24.231 0.558 15.93  ? 15  HIS A N    1 
ATOM   293  C CA   A HIS A 1 16  ? 14.232 13.045 23.006 0.442 17.00  ? 15  HIS A CA   1 
ATOM   294  C CA   B HIS A 1 16  ? 14.343 12.786 22.879 0.558 17.13  ? 15  HIS A CA   1 
ATOM   295  C C    A HIS A 1 16  ? 13.930 12.088 21.855 0.442 17.75  ? 15  HIS A C    1 
ATOM   296  C C    B HIS A 1 16  ? 14.055 11.653 21.892 0.558 17.16  ? 15  HIS A C    1 
ATOM   297  O O    A HIS A 1 16  ? 13.800 12.555 20.724 0.442 19.71  ? 15  HIS A O    1 
ATOM   298  O O    B HIS A 1 16  ? 14.059 11.868 20.679 0.558 18.50  ? 15  HIS A O    1 
ATOM   299  C CB   A HIS A 1 16  ? 15.311 14.046 22.592 0.442 18.66  ? 15  HIS A CB   1 
ATOM   300  C CB   B HIS A 1 16  ? 15.546 13.582 22.376 0.558 18.69  ? 15  HIS A CB   1 
ATOM   301  C CG   A HIS A 1 16  ? 15.392 15.275 23.442 0.442 20.84  ? 15  HIS A CG   1 
ATOM   302  C CG   B HIS A 1 16  ? 15.695 14.940 22.966 0.558 20.50  ? 15  HIS A CG   1 
ATOM   303  N ND1  A HIS A 1 16  ? 14.844 16.462 23.009 0.442 22.61  ? 15  HIS A ND1  1 
ATOM   304  N ND1  B HIS A 1 16  ? 15.283 16.120 22.410 0.558 21.82  ? 15  HIS A ND1  1 
ATOM   305  C CD2  A HIS A 1 16  ? 15.929 15.547 24.643 0.442 21.91  ? 15  HIS A CD2  1 
ATOM   306  C CD2  B HIS A 1 16  ? 16.276 15.280 24.151 0.558 21.48  ? 15  HIS A CD2  1 
ATOM   307  C CE1  A HIS A 1 16  ? 15.039 17.411 23.901 0.442 23.10  ? 15  HIS A CE1  1 
ATOM   308  C CE1  B HIS A 1 16  ? 15.591 17.126 23.219 0.558 22.56  ? 15  HIS A CE1  1 
ATOM   309  N NE2  A HIS A 1 16  ? 15.693 16.878 24.915 0.442 22.80  ? 15  HIS A NE2  1 
ATOM   310  N NE2  B HIS A 1 16  ? 16.193 16.633 24.284 0.558 23.16  ? 15  HIS A NE2  1 
ATOM   311  D D    A HIS A 1 16  ? 15.514 11.944 24.355 0.442 23.47  ? 15  HIS A D    1 
ATOM   312  D D    B HIS A 1 16  ? 15.542 12.076 24.523 0.558 19.96  ? 15  HIS A D    1 
ATOM   313  D DA   A HIS A 1 16  ? 13.288 13.570 23.257 0.442 18.82  ? 15  HIS A DA   1 
ATOM   314  D DA   B HIS A 1 16  ? 13.424 13.391 22.912 0.558 17.53  ? 15  HIS A DA   1 
ATOM   315  D DB2  A HIS A 1 16  ? 16.267 13.534 22.567 0.442 18.13  ? 15  HIS A DB2  1 
ATOM   316  D DB2  B HIS A 1 16  ? 16.450 12.985 22.577 0.558 20.54  ? 15  HIS A DB2  1 
ATOM   317  D DB3  A HIS A 1 16  ? 15.092 14.338 21.547 0.442 19.20  ? 15  HIS A DB3  1 
ATOM   318  D DB3  B HIS A 1 16  ? 15.489 13.632 21.282 0.558 19.31  ? 15  HIS A DB3  1 
ATOM   319  D DD1  A HIS A 1 16  ? 14.355 16.532 22.120 0.442 38.28  ? 15  HIS A DD1  1 
ATOM   320  D DD1  B HIS A 1 16  ? 14.809 16.173 21.517 0.558 31.19  ? 15  HIS A DD1  1 
ATOM   321  D DD2  A HIS A 1 16  ? 16.446 14.865 25.300 0.442 22.62  ? 15  HIS A DD2  1 
ATOM   322  D DD2  B HIS A 1 16  ? 16.719 14.523 24.777 0.558 22.48  ? 15  HIS A DD2  1 
ATOM   323  D DE1  A HIS A 1 16  ? 14.722 18.445 23.819 0.442 24.54  ? 15  HIS A DE1  1 
ATOM   324  D DE1  B HIS A 1 16  ? 15.376 18.170 23.035 0.558 26.60  ? 15  HIS A DE1  1 
ATOM   325  D DE2  A HIS A 1 16  ? 16.002 17.323 25.770 0.442 21.98  ? 15  HIS A DE2  1 
ATOM   326  D DE2  B HIS A 1 16  ? 16.516 17.139 25.107 0.558 22.05  ? 15  HIS A DE2  1 
ATOM   327  N N    A GLY A 1 17  ? 13.804 10.794 22.121 0.442 16.92  ? 16  GLY A N    1 
ATOM   328  N N    B GLY A 1 17  ? 13.808 10.451 22.400 0.558 16.16  ? 16  GLY A N    1 
ATOM   329  C CA   A GLY A 1 17  ? 13.363 9.847  21.127 0.442 17.34  ? 16  GLY A CA   1 
ATOM   330  C CA   B GLY A 1 17  ? 13.313 9.372  21.575 0.558 16.64  ? 16  GLY A CA   1 
ATOM   331  C C    A GLY A 1 17  ? 14.380 8.991  20.410 0.442 16.34  ? 16  GLY A C    1 
ATOM   332  C C    B GLY A 1 17  ? 14.312 8.643  20.703 0.558 16.48  ? 16  GLY A C    1 
ATOM   333  O O    A GLY A 1 17  ? 13.995 8.436  19.364 0.442 14.78  ? 16  GLY A O    1 
ATOM   334  O O    B GLY A 1 17  ? 13.869 7.878  19.834 0.558 15.56  ? 16  GLY A O    1 
ATOM   335  D D    A GLY A 1 17  ? 14.031 10.474 23.059 0.442 17.42  ? 16  GLY A D    1 
ATOM   336  D D    B GLY A 1 17  ? 13.974 10.320 23.386 0.558 19.44  ? 16  GLY A D    1 
ATOM   337  D DA2  A GLY A 1 17  ? 12.660 9.147  21.573 0.442 17.35  ? 16  GLY A DA2  1 
ATOM   338  D DA2  B GLY A 1 17  ? 12.817 8.655  22.232 0.558 16.96  ? 16  GLY A DA2  1 
ATOM   339  D DA3  A GLY A 1 17  ? 12.809 10.399 20.360 0.442 16.47  ? 16  GLY A DA3  1 
ATOM   340  D DA3  B GLY A 1 17  ? 12.559 9.784  20.904 0.558 17.71  ? 16  GLY A DA3  1 
ATOM   341  N N    . LEU A 1 18  ? 15.626 8.858  20.890 1.000 15.94  ? 17  LEU A N    1 
ATOM   342  C CA   . LEU A 1 18  ? 16.579 8.133  20.049 1.000 15.31  ? 17  LEU A CA   1 
ATOM   343  C C    . LEU A 1 18  ? 16.770 6.656  20.330 1.000 14.75  ? 17  LEU A C    1 
ATOM   344  O O    . LEU A 1 18  ? 17.362 5.962  19.509 1.000 16.37  ? 17  LEU A O    1 
ATOM   345  C CB   . LEU A 1 18  ? 17.952 8.793  20.149 1.000 15.22  ? 17  LEU A CB   1 
ATOM   346  C CG   . LEU A 1 18  ? 18.082 10.123 19.410 1.000 16.69  ? 17  LEU A CG   1 
ATOM   347  C CD1  . LEU A 1 18  ? 19.472 10.687 19.600 1.000 17.90  ? 17  LEU A CD1  1 
ATOM   348  C CD2  . LEU A 1 18  ? 17.768 9.994  17.927 1.000 18.47  ? 17  LEU A CD2  1 
ATOM   349  D D    . LEU A 1 18  ? 15.946 9.405  21.665 1.000 19.89  ? 17  LEU A D    1 
ATOM   350  D DA   . LEU A 1 18  ? 16.184 8.235  19.040 1.000 16.03  ? 17  LEU A DA   1 
ATOM   351  D DB2  . LEU A 1 18  ? 18.215 8.927  21.190 1.000 15.20  ? 17  LEU A DB2  1 
ATOM   352  D DB3  . LEU A 1 18  ? 18.697 8.084  19.686 1.000 17.08  ? 17  LEU A DB3  1 
ATOM   353  D DG   . LEU A 1 18  ? 17.347 10.806 19.850 1.000 19.33  ? 17  LEU A DG   1 
ATOM   354  D DD11 . LEU A 1 18  ? 20.210 10.032 19.211 1.000 20.80  ? 17  LEU A DD11 1 
ATOM   355  D DD12 . LEU A 1 18  ? 19.593 11.605 19.079 1.000 20.65  ? 17  LEU A DD12 1 
ATOM   356  D DD13 . LEU A 1 18  ? 19.691 10.878 20.606 1.000 22.42  ? 17  LEU A DD13 1 
ATOM   357  D DD21 . LEU A 1 18  ? 18.476 9.374  17.463 1.000 21.39  ? 17  LEU A DD21 1 
ATOM   358  D DD22 . LEU A 1 18  ? 16.794 9.599  17.800 1.000 21.87  ? 17  LEU A DD22 1 
ATOM   359  D DD23 . LEU A 1 18  ? 17.856 10.962 17.482 1.000 22.21  ? 17  LEU A DD23 1 
ATOM   360  N N    . ASP A 1 19  ? 16.302 6.098  21.419 1.000 16.36  ? 18  ASP A N    1 
ATOM   361  C CA   . ASP A 1 19  ? 16.552 4.697  21.692 1.000 17.05  ? 18  ASP A CA   1 
ATOM   362  C C    . ASP A 1 19  ? 15.694 3.896  20.698 1.000 15.54  ? 18  ASP A C    1 
ATOM   363  O O    . ASP A 1 19  ? 14.479 4.024  20.738 1.000 19.45  ? 18  ASP A O    1 
ATOM   364  C CB   . ASP A 1 19  ? 16.222 4.257  23.092 1.000 19.55  ? 18  ASP A CB   1 
ATOM   365  C CG   . ASP A 1 19  ? 16.593 2.825  23.414 1.000 21.60  ? 18  ASP A CG   1 
ATOM   366  O OD1  . ASP A 1 19  ? 17.412 2.162  22.756 1.000 21.56  ? 18  ASP A OD1  1 
ATOM   367  O OD2  . ASP A 1 19  ? 15.997 2.354  24.415 1.000 31.61  ? 18  ASP A OD2  1 
ATOM   368  D D    . ASP A 1 19  ? 15.719 6.632  22.017 1.000 17.04  ? 18  ASP A D    1 
ATOM   369  D DA   . ASP A 1 19  ? 17.590 4.508  21.446 1.000 17.41  ? 18  ASP A DA   1 
ATOM   370  D DB2  . ASP A 1 19  ? 16.724 4.915  23.803 1.000 21.51  ? 18  ASP A DB2  1 
ATOM   371  D DB3  . ASP A 1 19  ? 15.154 4.378  23.257 1.000 23.82  ? 18  ASP A DB3  1 
ATOM   372  N N    A ASN A 1 20  ? 16.370 3.180  19.800 0.645 13.49  ? 19  ASN A N    1 
ATOM   373  N N    B ASN A 1 20  ? 16.388 3.140  19.853 0.355 13.52  ? 19  ASN A N    1 
ATOM   374  C CA   A ASN A 1 20  ? 15.893 2.242  18.779 0.645 13.77  ? 19  ASN A CA   1 
ATOM   375  C CA   B ASN A 1 20  ? 15.647 2.359  18.879 0.355 14.20  ? 19  ASN A CA   1 
ATOM   376  C C    A ASN A 1 20  ? 15.289 3.062  17.611 0.645 13.41  ? 19  ASN A C    1 
ATOM   377  C C    B ASN A 1 20  ? 14.940 3.242  17.855 0.355 13.72  ? 19  ASN A C    1 
ATOM   378  O O    A ASN A 1 20  ? 14.618 2.470  16.767 0.645 14.06  ? 19  ASN A O    1 
ATOM   379  O O    B ASN A 1 20  ? 13.873 2.881  17.381 0.355 15.51  ? 19  ASN A O    1 
ATOM   380  C CB   A ASN A 1 20  ? 14.940 1.139  19.254 0.645 15.23  ? 19  ASN A CB   1 
ATOM   381  C CB   B ASN A 1 20  ? 14.578 1.502  19.571 0.355 14.39  ? 19  ASN A CB   1 
ATOM   382  C CG   A ASN A 1 20  ? 15.582 0.053  20.101 0.645 16.06  ? 19  ASN A CG   1 
ATOM   383  C CG   B ASN A 1 20  ? 14.250 0.319  18.693 0.355 14.37  ? 19  ASN A CG   1 
ATOM   384  O OD1  A ASN A 1 20  ? 16.782 -0.223 19.981 0.645 16.84  ? 19  ASN A OD1  1 
ATOM   385  O OD1  B ASN A 1 20  ? 15.091 -0.022 17.863 0.355 15.91  ? 19  ASN A OD1  1 
ATOM   386  N ND2  A ASN A 1 20  ? 14.807 -0.616 20.931 0.645 18.16  ? 19  ASN A ND2  1 
ATOM   387  N ND2  B ASN A 1 20  ? 13.069 -0.215 18.888 0.355 13.66  ? 19  ASN A ND2  1 
ATOM   388  D D    A ASN A 1 20  ? 17.376 3.387  19.738 0.645 13.29  ? 19  ASN A D    1 
ATOM   389  D D    B ASN A 1 20  ? 17.395 3.142  19.863 0.355 16.66  ? 19  ASN A D    1 
ATOM   390  D DA   A ASN A 1 20  ? 16.785 1.749  18.352 0.645 14.64  ? 19  ASN A DA   1 
ATOM   391  D DA   B ASN A 1 20  ? 16.349 1.710  18.340 0.355 13.73  ? 19  ASN A DA   1 
ATOM   392  D DB2  A ASN A 1 20  ? 14.101 1.584  19.770 0.645 16.15  ? 19  ASN A DB2  1 
ATOM   393  D DB2  B ASN A 1 20  ? 14.965 1.177  20.534 0.355 15.39  ? 19  ASN A DB2  1 
ATOM   394  D DB3  A ASN A 1 20  ? 14.477 0.674  18.379 0.645 16.44  ? 19  ASN A DB3  1 
ATOM   395  D DB3  B ASN A 1 20  ? 13.687 2.117  19.718 0.355 14.43  ? 19  ASN A DB3  1 
ATOM   396  D DD21 A ASN A 1 20  ? 15.172 -1.426 21.404 0.645 22.76  ? 19  ASN A DD21 1 
ATOM   397  D DD21 B ASN A 1 20  ? 12.811 -1.066 18.425 0.355 15.85  ? 19  ASN A DD21 1 
ATOM   398  D DD22 A ASN A 1 20  ? 13.840 -0.392 21.012 0.645 18.69  ? 19  ASN A DD22 1 
ATOM   399  D DD22 B ASN A 1 20  ? 12.425 0.198  19.539 0.355 16.01  ? 19  ASN A DD22 1 
ATOM   400  N N    . TYR A 1 21  ? 15.549 4.360  17.544 1.000 12.76  ? 20  TYR A N    1 
ATOM   401  C CA   . TYR A 1 21  ? 15.120 5.170  16.402 1.000 12.03  ? 20  TYR A CA   1 
ATOM   402  C C    . TYR A 1 21  ? 15.693 4.562  15.120 1.000 10.93  ? 20  TYR A C    1 
ATOM   403  O O    . TYR A 1 21  ? 16.895 4.441  14.980 1.000 11.34  ? 20  TYR A O    1 
ATOM   404  C CB   . TYR A 1 21  ? 15.558 6.641  16.564 1.000 12.97  ? 20  TYR A CB   1 
ATOM   405  C CG   . TYR A 1 21  ? 15.098 7.494  15.420 1.000 12.12  ? 20  TYR A CG   1 
ATOM   406  C CD1  . TYR A 1 21  ? 13.770 7.938  15.374 1.000 15.02  ? 20  TYR A CD1  1 
ATOM   407  C CD2  . TYR A 1 21  ? 15.900 7.838  14.347 1.000 13.73  ? 20  TYR A CD2  1 
ATOM   408  C CE1  . TYR A 1 21  ? 13.307 8.700  14.335 1.000 16.46  ? 20  TYR A CE1  1 
ATOM   409  C CE2  . TYR A 1 21  ? 15.442 8.600  13.297 1.000 15.80  ? 20  TYR A CE2  1 
ATOM   410  C CZ   . TYR A 1 21  ? 14.159 9.025  13.320 1.000 16.42  ? 20  TYR A CZ   1 
ATOM   411  O OH   . TYR A 1 21  ? 13.655 9.786  12.273 1.000 18.69  ? 20  TYR A OH   1 
ATOM   412  D D    . TYR A 1 21  ? 16.231 4.754  18.154 1.000 17.51  ? 20  TYR A D    1 
ATOM   413  D DA   . TYR A 1 21  ? 14.029 5.112  16.367 1.000 13.10  ? 20  TYR A DA   1 
ATOM   414  D DB2  . TYR A 1 21  ? 15.157 7.004  17.514 1.000 16.54  ? 20  TYR A DB2  1 
ATOM   415  D DB3  . TYR A 1 21  ? 16.656 6.660  16.638 1.000 16.02  ? 20  TYR A DB3  1 
ATOM   416  D DD1  . TYR A 1 21  ? 13.132 7.681  16.196 1.000 25.06  ? 20  TYR A DD1  1 
ATOM   417  D DD2  . TYR A 1 21  ? 16.910 7.463  14.332 1.000 19.33  ? 20  TYR A DD2  1 
ATOM   418  D DE1  . TYR A 1 21  ? 12.276 9.008  14.294 1.000 25.82  ? 20  TYR A DE1  1 
ATOM   419  D DE2  . TYR A 1 21  ? 16.089 8.827  12.461 1.000 21.00  ? 20  TYR A DE2  1 
ATOM   420  D DH   . TYR A 1 21  ? 14.393 9.822  11.606 1.000 33.02  ? 20  TYR A DH   1 
ATOM   421  N N    . ARG A 1 22  ? 14.787 4.178  14.202 1.000 12.16  ? 21  ARG A N    1 
ATOM   422  C CA   . ARG A 1 22  ? 15.114 3.548  12.935 1.000 12.15  ? 21  ARG A CA   1 
ATOM   423  C C    . ARG A 1 22  ? 16.088 2.379  13.132 1.000 12.77  ? 21  ARG A C    1 
ATOM   424  O O    . ARG A 1 22  ? 16.930 2.073  12.295 1.000 13.11  ? 21  ARG A O    1 
ATOM   425  C CB   . ARG A 1 22  ? 15.647 4.589  11.972 1.000 13.92  ? 21  ARG A CB   1 
ATOM   426  C CG   . ARG A 1 22  ? 14.546 5.556  11.603 1.000 17.01  ? 21  ARG A CG   1 
ATOM   427  C CD   . ARG A 1 22  ? 13.389 4.930  10.820 1.000 20.49  ? 21  ARG A CD   1 
ATOM   428  N NE   . ARG A 1 22  ? 13.895 4.248  9.646  1.000 25.25  ? 21  ARG A NE   1 
ATOM   429  C CZ   . ARG A 1 22  ? 14.130 4.871  8.512  1.000 28.26  ? 21  ARG A CZ   1 
ATOM   430  N NH1  . ARG A 1 22  ? 14.710 4.245  7.497  1.000 32.28  ? 21  ARG A NH1  1 
ATOM   431  N NH2  . ARG A 1 22  ? 13.726 6.135  8.455  1.000 28.21  ? 21  ARG A NH2  1 
ATOM   432  D D    . ARG A 1 22  ? 13.821 4.337  14.425 1.000 14.70  ? 21  ARG A D    1 
ATOM   433  D DA   . ARG A 1 22  ? 14.174 3.128  12.538 1.000 15.26  ? 21  ARG A DA   1 
ATOM   434  D DB2  . ARG A 1 22  ? 16.466 5.110  12.424 1.000 15.63  ? 21  ARG A DB2  1 
ATOM   435  D DB3  . ARG A 1 22  ? 15.999 4.087  11.075 1.000 19.39  ? 21  ARG A DB3  1 
ATOM   436  D DG2  . ARG A 1 22  ? 14.144 5.987  12.515 1.000 20.78  ? 21  ARG A DG2  1 
ATOM   437  D DG3  . ARG A 1 22  ? 14.970 6.348  10.987 1.000 18.63  ? 21  ARG A DG3  1 
ATOM   438  D DD2  . ARG A 1 22  ? 12.857 4.232  11.441 1.000 25.54  ? 21  ARG A DD2  1 
ATOM   439  D DD3  . ARG A 1 22  ? 12.688 5.712  10.482 1.000 26.30  ? 21  ARG A DD3  1 
ATOM   440  D DE   . ARG A 1 22  ? 14.041 3.273  9.792  1.000 58.70  ? 21  ARG A DE   1 
ATOM   441  D DH11 . ARG A 1 22  ? 14.939 3.256  7.599  1.000 28.71  ? 21  ARG A DH11 1 
ATOM   442  D DH12 . ARG A 1 22  ? 14.879 4.758  6.634  1.000 42.42  ? 21  ARG A DH12 1 
ATOM   443  D DH21 . ARG A 1 22  ? 13.580 6.561  7.538  1.000 33.80  ? 21  ARG A DH21 1 
ATOM   444  D DH22 . ARG A 1 22  ? 13.539 6.634  9.313  1.000 35.53  ? 21  ARG A DH22 1 
ATOM   445  N N    . GLY A 1 23  ? 15.896 1.677  14.241 1.000 13.20  ? 22  GLY A N    1 
ATOM   446  C CA   . GLY A 1 23  ? 16.628 0.450  14.464 1.000 14.60  ? 22  GLY A CA   1 
ATOM   447  C C    . GLY A 1 23  ? 17.991 0.569  15.111 1.000 13.31  ? 22  GLY A C    1 
ATOM   448  O O    . GLY A 1 23  ? 18.732 -0.406 15.138 1.000 15.92  ? 22  GLY A O    1 
ATOM   449  D D    . GLY A 1 23  ? 15.222 2.004  14.904 1.000 14.64  ? 22  GLY A D    1 
ATOM   450  D DA2  . GLY A 1 23  ? 16.037 -0.160 15.155 1.000 18.34  ? 22  GLY A DA2  1 
ATOM   451  D DA3  . GLY A 1 23  ? 16.774 -0.089 13.537 1.000 17.89  ? 22  GLY A DA3  1 
ATOM   452  N N    . TYR A 1 24  ? 18.327 1.772  15.591 1.000 11.02  ? 23  TYR A N    1 
ATOM   453  C CA   . TYR A 1 24  ? 19.606 2.038  16.214 1.000 10.90  ? 23  TYR A CA   1 
ATOM   454  C C    . TYR A 1 24  ? 19.400 2.175  17.728 1.000 11.96  ? 23  TYR A C    1 
ATOM   455  O O    . TYR A 1 24  ? 18.832 3.174  18.148 1.000 12.33  ? 23  TYR A O    1 
ATOM   456  C CB   . TYR A 1 24  ? 20.243 3.285  15.638 1.000 11.91  ? 23  TYR A CB   1 
ATOM   457  C CG   . TYR A 1 24  ? 20.675 3.080  14.212 1.000 10.91  ? 23  TYR A CG   1 
ATOM   458  C CD1  . TYR A 1 24  ? 21.852 2.422  13.889 1.000 11.33  ? 23  TYR A CD1  1 
ATOM   459  C CD2  . TYR A 1 24  ? 19.917 3.562  13.177 1.000 12.10  ? 23  TYR A CD2  1 
ATOM   460  C CE1  . TYR A 1 24  ? 22.231 2.242  12.573 1.000 12.49  ? 23  TYR A CE1  1 
ATOM   461  C CE2  . TYR A 1 24  ? 20.287 3.390  11.865 1.000 13.13  ? 23  TYR A CE2  1 
ATOM   462  C CZ   . TYR A 1 24  ? 21.456 2.735  11.548 1.000 12.39  ? 23  TYR A CZ   1 
ATOM   463  O OH   . TYR A 1 24  ? 21.796 2.597  10.225 1.000 14.83  ? 23  TYR A OH   1 
ATOM   464  H H    A TYR A 1 24  ? 17.659 2.526  15.517 0.497 8.61   ? 23  TYR A H    1 
ATOM   465  D D    B TYR A 1 24  ? 17.663 2.517  15.488 0.503 12.46  ? 23  TYR A D    1 
ATOM   466  D DA   . TYR A 1 24  ? 20.211 1.138  16.034 1.000 11.89  ? 23  TYR A DA   1 
ATOM   467  D DB2  . TYR A 1 24  ? 19.574 4.131  15.726 1.000 12.97  ? 23  TYR A DB2  1 
ATOM   468  D DB3  . TYR A 1 24  ? 21.139 3.544  16.232 1.000 13.63  ? 23  TYR A DB3  1 
ATOM   469  D DD1  . TYR A 1 24  ? 22.480 2.062  14.686 1.000 13.47  ? 23  TYR A DD1  1 
ATOM   470  D DD2  . TYR A 1 24  ? 18.987 4.091  13.406 1.000 14.41  ? 23  TYR A DD2  1 
ATOM   471  D DE1  . TYR A 1 24  ? 23.143 1.718  12.354 1.000 16.66  ? 23  TYR A DE1  1 
ATOM   472  D DE2  . TYR A 1 24  ? 19.636 3.743  11.083 1.000 16.65  ? 23  TYR A DE2  1 
ATOM   473  D DH   . TYR A 1 24  ? 22.569 2.014  10.076 1.000 19.95  ? 23  TYR A DH   1 
ATOM   474  N N    . SER A 1 25  ? 19.872 1.198  18.501 1.000 12.46  ? 24  SER A N    1 
ATOM   475  C CA   . SER A 1 25  ? 19.788 1.276  19.946 1.000 13.01  ? 24  SER A CA   1 
ATOM   476  C C    . SER A 1 25  ? 20.546 2.475  20.505 1.000 12.39  ? 24  SER A C    1 
ATOM   477  O O    . SER A 1 25  ? 21.465 2.972  19.853 1.000 13.60  ? 24  SER A O    1 
ATOM   478  C CB   . SER A 1 25  ? 20.313 -0.045 20.543 1.000 15.63  ? 24  SER A CB   1 
ATOM   479  O OG   . SER A 1 25  ? 21.669 -0.258 20.295 1.000 18.07  ? 24  SER A OG   1 
ATOM   480  D D    . SER A 1 25  ? 20.300 0.402  18.064 1.000 13.75  ? 24  SER A D    1 
ATOM   481  D DA   . SER A 1 25  ? 18.727 1.370  20.179 1.000 13.21  ? 24  SER A DA   1 
ATOM   482  D DB2  . SER A 1 25  ? 20.091 -0.080 21.595 1.000 19.51  ? 24  SER A DB2  1 
ATOM   483  D DB3  . SER A 1 25  ? 19.681 -0.850 20.108 1.000 18.49  ? 24  SER A DB3  1 
ATOM   484  D DG   . SER A 1 25  ? 22.198 0.014  21.076 1.000 73.15  ? 24  SER A DG   1 
ATOM   485  N N    . LEU A 1 26  ? 20.140 2.916  21.686 1.000 13.13  ? 25  LEU A N    1 
ATOM   486  C CA   . LEU A 1 26  ? 20.703 4.092  22.324 1.000 12.31  ? 25  LEU A CA   1 
ATOM   487  C C    . LEU A 1 26  ? 22.231 4.128  22.417 1.000 11.18  ? 25  LEU A C    1 
ATOM   488  O O    . LEU A 1 26  ? 22.814 5.201  22.209 1.000 11.62  ? 25  LEU A O    1 
ATOM   489  C CB   . LEU A 1 26  ? 20.082 4.205  23.734 1.000 13.43  ? 25  LEU A CB   1 
ATOM   490  C CG   . LEU A 1 26  ? 20.366 5.497  24.466 1.000 14.42  ? 25  LEU A CG   1 
ATOM   491  C CD1  . LEU A 1 26  ? 19.836 6.724  23.753 1.000 18.75  ? 25  LEU A CD1  1 
ATOM   492  C CD2  . LEU A 1 26  ? 19.773 5.443  25.866 1.000 16.33  ? 25  LEU A CD2  1 
ATOM   493  D D    . LEU A 1 26  ? 19.335 2.484  22.111 1.000 13.47  ? 25  LEU A D    1 
ATOM   494  D DA   . LEU A 1 26  ? 20.376 4.953  21.734 1.000 14.03  ? 25  LEU A DA   1 
ATOM   495  D DB2  . LEU A 1 26  ? 18.999 4.060  23.627 1.000 14.04  ? 25  LEU A DB2  1 
ATOM   496  D DB3  . LEU A 1 26  ? 20.423 3.356  24.322 1.000 15.29  ? 25  LEU A DB3  1 
ATOM   497  D DG   . LEU A 1 26  ? 21.464 5.590  24.562 1.000 15.20  ? 25  LEU A DG   1 
ATOM   498  D DD11 . LEU A 1 26  ? 18.826 6.593  23.465 1.000 23.15  ? 25  LEU A DD11 1 
ATOM   499  D DD12 . LEU A 1 26  ? 19.881 7.575  24.389 1.000 23.78  ? 25  LEU A DD12 1 
ATOM   500  D DD13 . LEU A 1 26  ? 20.410 6.917  22.876 1.000 24.19  ? 25  LEU A DD13 1 
ATOM   501  D DD21 . LEU A 1 26  ? 18.720 5.298  25.810 1.000 19.05  ? 25  LEU A DD21 1 
ATOM   502  D DD22 . LEU A 1 26  ? 20.193 4.645  26.411 1.000 19.83  ? 25  LEU A DD22 1 
ATOM   503  D DD23 . LEU A 1 26  ? 19.924 6.373  26.357 1.000 20.18  ? 25  LEU A DD23 1 
ATOM   504  N N    . GLY A 1 27  ? 22.867 3.023  22.702 1.000 10.62  ? 26  GLY A N    1 
ATOM   505  C CA   . GLY A 1 27  ? 24.313 3.010  22.772 1.000 10.90  ? 26  GLY A CA   1 
ATOM   506  C C    . GLY A 1 27  ? 25.005 3.430  21.505 1.000 9.51   ? 26  GLY A C    1 
ATOM   507  O O    . GLY A 1 27  ? 26.092 3.985  21.573 1.000 11.21  ? 26  GLY A O    1 
ATOM   508  D D    . GLY A 1 27  ? 22.384 2.156  22.875 1.000 13.17  ? 26  GLY A D    1 
ATOM   509  D DA2  . GLY A 1 27  ? 24.620 3.692  23.563 1.000 13.40  ? 26  GLY A DA2  1 
ATOM   510  D DA3  . GLY A 1 27  ? 24.671 2.026  23.032 1.000 12.95  ? 26  GLY A DA3  1 
ATOM   511  N N    . ASN A 1 28  ? 24.399 3.167  20.345 1.000 9.39   ? 27  ASN A N    1 
ATOM   512  C CA   . ASN A 1 28  ? 24.991 3.677  19.114 1.000 8.98   ? 27  ASN A CA   1 
ATOM   513  C C    . ASN A 1 28  ? 25.116 5.183  19.083 1.000 8.96   ? 27  ASN A C    1 
ATOM   514  O O    . ASN A 1 28  ? 26.112 5.742  18.621 1.000 10.08  ? 27  ASN A O    1 
ATOM   515  C CB   . ASN A 1 28  ? 24.134 3.264  17.912 1.000 10.00  ? 27  ASN A CB   1 
ATOM   516  C CG   . ASN A 1 28  ? 24.249 1.786  17.607 1.000 11.56  ? 27  ASN A CG   1 
ATOM   517  O OD1  . ASN A 1 28  ? 25.274 1.380  17.074 1.000 12.98  ? 27  ASN A OD1  1 
ATOM   518  N ND2  . ASN A 1 28  ? 23.238 0.994  17.914 1.000 14.39  ? 27  ASN A ND2  1 
ATOM   519  H H    . ASN A 1 28  ? 23.547 2.626  20.321 1.000 23.83  ? 27  ASN A H    1 
ATOM   520  D DA   . ASN A 1 28  ? 25.987 3.268  18.994 1.000 10.14  ? 27  ASN A DA   1 
ATOM   521  D DB2  . ASN A 1 28  ? 23.102 3.535  18.090 1.000 11.68  ? 27  ASN A DB2  1 
ATOM   522  D DB3  . ASN A 1 28  ? 24.427 3.835  17.046 1.000 10.61  ? 27  ASN A DB3  1 
ATOM   523  D DD21 . ASN A 1 28  ? 23.309 0.015  17.655 1.000 17.35  ? 27  ASN A DD21 1 
ATOM   524  D DD22 . ASN A 1 28  ? 22.483 1.375  18.469 1.000 17.33  ? 27  ASN A DD22 1 
ATOM   525  N N    A TRP A 1 29  ? 24.080 5.878  19.557 0.553 9.39   ? 28  TRP A N    1 
ATOM   526  N N    B TRP A 1 29  ? 24.095 5.888  19.570 0.447 9.04   ? 28  TRP A N    1 
ATOM   527  C CA   A TRP A 1 29  ? 24.029 7.332  19.545 0.553 9.03   ? 28  TRP A CA   1 
ATOM   528  C CA   B TRP A 1 29  ? 24.144 7.345  19.493 0.447 8.83   ? 28  TRP A CA   1 
ATOM   529  C C    A TRP A 1 29  ? 25.017 7.944  20.539 0.553 9.46   ? 28  TRP A C    1 
ATOM   530  C C    B TRP A 1 29  ? 25.140 7.906  20.510 0.447 9.01   ? 28  TRP A C    1 
ATOM   531  O O    A TRP A 1 29  ? 25.617 8.992  20.248 0.553 8.92   ? 28  TRP A O    1 
ATOM   532  O O    B TRP A 1 29  ? 25.871 8.871  20.229 0.447 9.35   ? 28  TRP A O    1 
ATOM   533  C CB   A TRP A 1 29  ? 22.588 7.757  19.871 0.553 9.17   ? 28  TRP A CB   1 
ATOM   534  C CB   B TRP A 1 29  ? 22.760 7.957  19.723 0.447 9.46   ? 28  TRP A CB   1 
ATOM   535  C CG   A TRP A 1 29  ? 21.606 7.282  18.850 0.553 9.31   ? 28  TRP A CG   1 
ATOM   536  C CG   B TRP A 1 29  ? 21.726 7.464  18.766 0.447 9.48   ? 28  TRP A CG   1 
ATOM   537  C CD1  A TRP A 1 29  ? 20.818 6.167  19.059 0.553 10.00  ? 28  TRP A CD1  1 
ATOM   538  C CD1  B TRP A 1 29  ? 20.779 6.494  18.833 0.447 10.59  ? 28  TRP A CD1  1 
ATOM   539  C CD2  A TRP A 1 29  ? 21.270 7.788  17.561 0.553 9.86   ? 28  TRP A CD2  1 
ATOM   540  C CD2  B TRP A 1 29  ? 21.614 8.071  17.468 0.447 10.39  ? 28  TRP A CD2  1 
ATOM   541  N NE1  A TRP A 1 29  ? 20.018 5.971  17.967 0.553 10.36  ? 28  TRP A NE1  1 
ATOM   542  N NE1  B TRP A 1 29  ? 20.078 6.454  17.647 0.447 11.28  ? 28  TRP A NE1  1 
ATOM   543  C CE2  A TRP A 1 29  ? 20.273 6.938  17.030 0.553 10.21  ? 28  TRP A CE2  1 
ATOM   544  C CE2  B TRP A 1 29  ? 20.571 7.402  16.806 0.447 10.95  ? 28  TRP A CE2  1 
ATOM   545  C CE3  A TRP A 1 29  ? 21.695 8.857  16.763 0.553 11.05  ? 28  TRP A CE3  1 
ATOM   546  C CE3  B TRP A 1 29  ? 22.319 9.101  16.852 0.447 11.65  ? 28  TRP A CE3  1 
ATOM   547  C CZ2  A TRP A 1 29  ? 19.700 7.105  15.787 0.553 12.17  ? 28  TRP A CZ2  1 
ATOM   548  C CZ2  B TRP A 1 29  ? 20.231 7.776  15.510 0.447 12.46  ? 28  TRP A CZ2  1 
ATOM   549  C CZ3  A TRP A 1 29  ? 21.123 9.041  15.519 0.553 13.10  ? 28  TRP A CZ3  1 
ATOM   550  C CZ3  B TRP A 1 29  ? 21.975 9.465  15.570 0.447 12.89  ? 28  TRP A CZ3  1 
ATOM   551  C CH2  A TRP A 1 29  ? 20.134 8.173  15.046 0.553 13.53  ? 28  TRP A CH2  1 
ATOM   552  C CH2  B TRP A 1 29  ? 20.931 8.791  14.918 0.447 13.51  ? 28  TRP A CH2  1 
ATOM   553  H H    A TRP A 1 29  ? 23.295 5.371  19.942 0.553 167.91 ? 28  TRP A H    1 
ATOM   554  H H    B TRP A 1 29  ? 23.301 5.422  19.985 0.447 8.11   ? 28  TRP A H    1 
ATOM   555  D DA   A TRP A 1 29  ? 24.324 7.721  18.553 0.553 10.11  ? 28  TRP A DA   1 
ATOM   556  D DA   B TRP A 1 29  ? 24.547 7.651  18.504 0.447 9.77   ? 28  TRP A DA   1 
ATOM   557  D DB2  A TRP A 1 29  ? 22.324 7.289  20.820 0.553 10.98  ? 28  TRP A DB2  1 
ATOM   558  D DB2  B TRP A 1 29  ? 22.450 7.798  20.738 0.447 9.89   ? 28  TRP A DB2  1 
ATOM   559  D DB3  A TRP A 1 29  ? 22.549 8.830  19.971 0.553 9.58   ? 28  TRP A DB3  1 
ATOM   560  D DB3  B TRP A 1 29  ? 22.881 9.030  19.532 0.447 11.26  ? 28  TRP A DB3  1 
ATOM   561  D DD1  A TRP A 1 29  ? 20.840 5.591  19.965 0.553 13.37  ? 28  TRP A DD1  1 
ATOM   562  D DD1  B TRP A 1 29  ? 20.536 5.867  19.689 0.447 13.98  ? 28  TRP A DD1  1 
ATOM   563  H HE1  A TRP A 1 29  ? 19.316 5.247  17.879 0.553 15.61  ? 28  TRP A HE1  1 
ATOM   564  H HE1  B TRP A 1 29  ? 19.322 5.813  17.452 0.447 95.10  ? 28  TRP A HE1  1 
ATOM   565  D DE3  A TRP A 1 29  ? 22.478 9.500  17.117 0.553 17.01  ? 28  TRP A DE3  1 
ATOM   566  D DE3  B TRP A 1 29  ? 23.111 9.612  17.379 0.447 14.42  ? 28  TRP A DE3  1 
ATOM   567  D DZ2  A TRP A 1 29  ? 18.977 6.402  15.408 0.553 15.87  ? 28  TRP A DZ2  1 
ATOM   568  D DZ2  B TRP A 1 29  ? 19.439 7.254  14.991 0.447 14.41  ? 28  TRP A DZ2  1 
ATOM   569  D DZ3  A TRP A 1 29  ? 21.448 9.856  14.889 0.553 16.61  ? 28  TRP A DZ3  1 
ATOM   570  D DZ3  B TRP A 1 29  ? 22.498 10.249 15.054 0.447 16.85  ? 28  TRP A DZ3  1 
ATOM   571  D DH2  A TRP A 1 29  ? 19.696 8.372  14.071 0.553 22.16  ? 28  TRP A DH2  1 
ATOM   572  D DH2  B TRP A 1 29  ? 20.698 9.103  13.901 0.447 20.05  ? 28  TRP A DH2  1 
ATOM   573  N N    . VAL A 1 30  ? 25.156 7.325  21.707 1.000 9.46   ? 29  VAL A N    1 
ATOM   574  C CA   . VAL A 1 30  ? 26.122 7.792  22.693 1.000 9.16   ? 29  VAL A CA   1 
ATOM   575  C C    . VAL A 1 30  ? 27.555 7.557  22.168 1.000 8.84   ? 29  VAL A C    1 
ATOM   576  O O    . VAL A 1 30  ? 28.398 8.443  22.316 1.000 10.22  ? 29  VAL A O    1 
ATOM   577  C CB   . VAL A 1 30  ? 25.898 7.101  24.043 1.000 10.32  ? 29  VAL A CB   1 
ATOM   578  C CG1  . VAL A 1 30  ? 26.926 7.508  25.075 1.000 11.92  ? 29  VAL A CG1  1 
ATOM   579  C CG2  . VAL A 1 30  ? 24.488 7.413  24.566 1.000 12.14  ? 29  VAL A CG2  1 
ATOM   580  H H    A VAL A 1 30  ? 24.584 6.519  21.914 1.000 13.52  ? 29  VAL A H    1 
ATOM   581  D DA   . VAL A 1 30  ? 26.016 8.904  22.791 1.000 9.62   ? 29  VAL A DA   1 
ATOM   582  D DB   . VAL A 1 30  ? 25.963 6.018  23.864 1.000 11.50  ? 29  VAL A DB   1 
ATOM   583  D DG11 . VAL A 1 30  ? 26.944 8.559  25.190 1.000 16.42  ? 29  VAL A DG11 1 
ATOM   584  D DG12 . VAL A 1 30  ? 26.787 6.963  25.981 1.000 15.55  ? 29  VAL A DG12 1 
ATOM   585  D DG13 . VAL A 1 30  ? 27.907 7.203  24.781 1.000 14.40  ? 29  VAL A DG13 1 
ATOM   586  D DG21 . VAL A 1 30  ? 24.392 8.473  24.696 1.000 17.17  ? 29  VAL A DG21 1 
ATOM   587  D DG22 . VAL A 1 30  ? 23.758 7.097  23.881 1.000 16.87  ? 29  VAL A DG22 1 
ATOM   588  D DG23 . VAL A 1 30  ? 24.366 6.923  25.515 1.000 16.41  ? 29  VAL A DG23 1 
ATOM   589  N N    . CYS A 1 31  ? 27.803 6.376  21.581 1.000 9.60   ? 30  CYS A N    1 
ATOM   590  C CA   . CYS A 1 31  ? 29.122 6.069  21.034 1.000 9.25   ? 30  CYS A CA   1 
ATOM   591  C C    . CYS A 1 31  ? 29.484 7.063  19.929 1.000 9.40   ? 30  CYS A C    1 
ATOM   592  O O    . CYS A 1 31  ? 30.596 7.563  19.870 1.000 10.05  ? 30  CYS A O    1 
ATOM   593  C CB   . CYS A 1 31  ? 29.094 4.624  20.522 1.000 10.36  ? 30  CYS A CB   1 
ATOM   594  S SG   . CYS A 1 31  ? 30.708 4.073  19.909 1.000 10.59  ? 30  CYS A SG   1 
ATOM   595  H H    . CYS A 1 31  ? 27.066 5.688  21.517 1.000 16.19  ? 30  CYS A H    1 
ATOM   596  D DA   . CYS A 1 31  ? 29.902 6.169  21.811 1.000 10.39  ? 30  CYS A DA   1 
ATOM   597  D DB2  . CYS A 1 31  ? 28.853 3.970  21.358 1.000 12.68  ? 30  CYS A DB2  1 
ATOM   598  D DB3  . CYS A 1 31  ? 28.341 4.547  19.748 1.000 12.07  ? 30  CYS A DB3  1 
ATOM   599  N N    . ALA A 1 32  ? 28.524 7.374  19.072 1.000 9.08   ? 31  ALA A N    1 
ATOM   600  C CA   . ALA A 1 32  ? 28.795 8.320  18.006 1.000 9.54   ? 31  ALA A CA   1 
ATOM   601  C C    . ALA A 1 32  ? 29.203 9.693  18.567 1.000 8.81   ? 31  ALA A C    1 
ATOM   602  O O    . ALA A 1 32  ? 30.189 10.283 18.117 1.000 10.22  ? 31  ALA A O    1 
ATOM   603  C CB   . ALA A 1 32  ? 27.593 8.452  17.084 1.000 11.31  ? 31  ALA A CB   1 
ATOM   604  H H    A ALA A 1 32  ? 27.609 6.955  19.159 0.747 8.45   ? 31  ALA A H    1 
ATOM   605  D D    B ALA A 1 32  ? 27.565 7.150  19.309 0.253 11.66  ? 31  ALA A D    1 
ATOM   606  D DA   . ALA A 1 32  ? 29.669 7.970  17.448 1.000 11.42  ? 31  ALA A DA   1 
ATOM   607  D DB1  . ALA A 1 32  ? 26.748 8.823  17.639 1.000 12.97  ? 31  ALA A DB1  1 
ATOM   608  D DB2  . ALA A 1 32  ? 27.789 9.157  16.327 1.000 14.43  ? 31  ALA A DB2  1 
ATOM   609  D DB3  . ALA A 1 32  ? 27.360 7.524  16.634 1.000 13.43  ? 31  ALA A DB3  1 
ATOM   610  N N    . ALA A 1 33  ? 28.460 10.168 19.549 1.000 8.91   ? 32  ALA A N    1 
ATOM   611  C CA   . ALA A 1 33  ? 28.797 11.450 20.141 1.000 8.92   ? 32  ALA A CA   1 
ATOM   612  C C    . ALA A 1 33  ? 30.158 11.435 20.838 1.000 8.87   ? 32  ALA A C    1 
ATOM   613  O O    . ALA A 1 33  ? 30.884 12.435 20.762 1.000 9.76   ? 32  ALA A O    1 
ATOM   614  C CB   . ALA A 1 33  ? 27.716 11.848 21.135 1.000 10.26  ? 32  ALA A CB   1 
ATOM   615  H H    . ALA A 1 33  ? 27.664 9.644  19.885 1.000 13.63  ? 32  ALA A H    1 
ATOM   616  D DA   . ALA A 1 33  ? 28.865 12.201 19.336 1.000 10.41  ? 32  ALA A DA   1 
ATOM   617  D DB1  . ALA A 1 33  ? 27.632 11.117 21.896 1.000 12.29  ? 32  ALA A DB1  1 
ATOM   618  D DB2  . ALA A 1 33  ? 27.993 12.794 21.580 1.000 13.55  ? 32  ALA A DB2  1 
ATOM   619  D DB3  . ALA A 1 33  ? 26.783 11.979 20.647 1.000 14.90  ? 32  ALA A DB3  1 
ATOM   620  N N    . LYS A 1 34  ? 30.476 10.322 21.503 1.000 9.30   ? 33  LYS A N    1 
ATOM   621  C CA   . LYS A 1 34  ? 31.758 10.225 22.167 1.000 9.31   ? 33  LYS A CA   1 
ATOM   622  C C    . LYS A 1 34  ? 32.898 10.448 21.169 1.000 9.55   ? 33  LYS A C    1 
ATOM   623  O O    . LYS A 1 34  ? 33.802 11.237 21.462 1.000 10.94  ? 33  LYS A O    1 
ATOM   624  C CB   . LYS A 1 34  ? 31.900 8.837  22.807 1.000 10.59  ? 33  LYS A CB   1 
ATOM   625  C CG   . LYS A 1 34  ? 33.279 8.498  23.341 1.000 12.87  ? 33  LYS A CG   1 
ATOM   626  C CD   . LYS A 1 34  ? 33.740 9.337  24.496 1.000 15.45  ? 33  LYS A CD   1 
ATOM   627  C CE   . LYS A 1 34  ? 35.175 8.989  24.878 1.000 18.67  ? 33  LYS A CE   1 
ATOM   628  N NZ   . LYS A 1 34  ? 35.689 9.907  25.921 1.000 20.71  ? 33  LYS A NZ   1 
ATOM   629  H H    . LYS A 1 34  ? 29.824 9.551  21.542 1.000 12.92  ? 33  LYS A H    1 
ATOM   630  D DA   . LYS A 1 34  ? 31.839 11.018 22.914 1.000 10.48  ? 33  LYS A DA   1 
ATOM   631  D DB2  . LYS A 1 34  ? 31.182 8.783  23.620 1.000 12.91  ? 33  LYS A DB2  1 
ATOM   632  D DB3  . LYS A 1 34  ? 31.636 8.113  22.035 1.000 12.34  ? 33  LYS A DB3  1 
ATOM   633  D DG2  . LYS A 1 34  ? 33.307 7.429  23.613 1.000 17.10  ? 33  LYS A DG2  1 
ATOM   634  D DG3  . LYS A 1 34  ? 34.016 8.566  22.508 1.000 14.48  ? 33  LYS A DG3  1 
ATOM   635  D DD2  . LYS A 1 34  ? 33.694 10.394 24.256 1.000 17.74  ? 33  LYS A DD2  1 
ATOM   636  D DD3  . LYS A 1 34  ? 33.095 9.183  25.352 1.000 20.27  ? 33  LYS A DD3  1 
ATOM   637  D DE2  . LYS A 1 34  ? 35.236 7.972  25.210 1.000 21.96  ? 33  LYS A DE2  1 
ATOM   638  D DE3  . LYS A 1 34  ? 35.791 9.084  23.991 1.000 22.41  ? 33  LYS A DE3  1 
ATOM   639  D DZ1  . LYS A 1 34  ? 35.750 10.859 25.527 1.000 25.91  ? 33  LYS A DZ1  1 
ATOM   640  D DZ2  . LYS A 1 34  ? 35.004 9.923  26.703 1.000 24.24  ? 33  LYS A DZ2  1 
ATOM   641  D DZ3  . LYS A 1 34  ? 36.630 9.584  26.205 1.000 25.12  ? 33  LYS A DZ3  1 
ATOM   642  N N    . PHE A 1 35  ? 32.847 9.745  20.042 1.000 9.28   ? 34  PHE A N    1 
ATOM   643  C CA   . PHE A 1 35  ? 33.981 9.806  19.134 1.000 10.45  ? 34  PHE A CA   1 
ATOM   644  C C    . PHE A 1 35  ? 33.913 10.946 18.140 1.000 10.70  ? 34  PHE A C    1 
ATOM   645  O O    . PHE A 1 35  ? 34.930 11.322 17.585 1.000 14.05  ? 34  PHE A O    1 
ATOM   646  C CB   . PHE A 1 35  ? 34.182 8.429  18.454 1.000 10.71  ? 34  PHE A CB   1 
ATOM   647  C CG   . PHE A 1 35  ? 34.647 7.430  19.486 1.000 11.39  ? 34  PHE A CG   1 
ATOM   648  C CD1  . PHE A 1 35  ? 35.893 7.524  20.079 1.000 13.48  ? 34  PHE A CD1  1 
ATOM   649  C CD2  . PHE A 1 35  ? 33.817 6.373  19.894 1.000 12.94  ? 34  PHE A CD2  1 
ATOM   650  C CE1  . PHE A 1 35  ? 36.317 6.601  21.015 1.000 15.64  ? 34  PHE A CE1  1 
ATOM   651  C CE2  . PHE A 1 35  ? 34.238 5.450  20.833 1.000 16.39  ? 34  PHE A CE2  1 
ATOM   652  C CZ   . PHE A 1 35  ? 35.488 5.552  21.397 1.000 16.77  ? 34  PHE A CZ   1 
ATOM   653  H H    . PHE A 1 35  ? 32.038 9.182  19.821 1.000 14.86  ? 34  PHE A H    1 
ATOM   654  D DA   . PHE A 1 35  ? 34.871 10.042 19.729 1.000 11.61  ? 34  PHE A DA   1 
ATOM   655  D DB2  . PHE A 1 35  ? 33.244 8.118  18.056 1.000 12.82  ? 34  PHE A DB2  1 
ATOM   656  D DB3  . PHE A 1 35  ? 34.946 8.558  17.704 1.000 13.80  ? 34  PHE A DB3  1 
ATOM   657  D DD1  . PHE A 1 35  ? 36.534 8.357  19.828 1.000 18.52  ? 34  PHE A DD1  1 
ATOM   658  D DD2  . PHE A 1 35  ? 32.850 6.284  19.448 1.000 17.64  ? 34  PHE A DD2  1 
ATOM   659  D DE1  . PHE A 1 35  ? 37.320 6.661  21.402 1.000 20.48  ? 34  PHE A DE1  1 
ATOM   660  D DE2  . PHE A 1 35  ? 33.553 4.674  21.145 1.000 25.18  ? 34  PHE A DE2  1 
ATOM   661  D DZ   . PHE A 1 35  ? 35.831 4.840  22.117 1.000 21.57  ? 34  PHE A DZ   1 
ATOM   662  N N    . GLU A 1 36  ? 32.746 11.555 17.937 1.000 9.62   ? 35  GLU A N    1 
ATOM   663  C CA   . GLU A 1 36  ? 32.656 12.735 17.116 1.000 9.21   ? 35  GLU A CA   1 
ATOM   664  C C    . GLU A 1 36  ? 33.161 13.976 17.848 1.000 9.85   ? 35  GLU A C    1 
ATOM   665  O O    . GLU A 1 36  ? 33.910 14.774 17.277 1.000 10.81  ? 35  GLU A O    1 
ATOM   666  C CB   . GLU A 1 36  ? 31.230 12.968 16.629 1.000 8.78   ? 35  GLU A CB   1 
ATOM   667  C CG   . GLU A 1 36  ? 30.762 11.999 15.552 1.000 10.11  ? 35  GLU A CG   1 
ATOM   668  C CD   . GLU A 1 36  ? 31.470 12.135 14.228 1.000 11.02  ? 35  GLU A CD   1 
ATOM   669  O OE1  . GLU A 1 36  ? 31.321 11.258 13.353 1.000 13.38  ? 35  GLU A OE1  1 
ATOM   670  O OE2  . GLU A 1 36  ? 32.182 13.161 14.031 1.000 13.00  ? 35  GLU A OE2  1 
ATOM   671  D D    . GLU A 1 36  ? 31.887 11.175 18.329 1.000 10.97  ? 35  GLU A D    1 
ATOM   672  D DA   . GLU A 1 36  ? 33.311 12.600 16.257 1.000 10.35  ? 35  GLU A DA   1 
ATOM   673  D DB2  . GLU A 1 36  ? 30.547 12.936 17.473 1.000 10.04  ? 35  GLU A DB2  1 
ATOM   674  D DB3  . GLU A 1 36  ? 31.166 13.978 16.221 1.000 10.23  ? 35  GLU A DB3  1 
ATOM   675  D DG2  . GLU A 1 36  ? 30.873 10.987 15.909 1.000 12.84  ? 35  GLU A DG2  1 
ATOM   676  D DG3  . GLU A 1 36  ? 29.687 12.179 15.373 1.000 13.40  ? 35  GLU A DG3  1 
ATOM   677  D DE2  . GLU A 1 36  ? 32.664 13.241 13.095 1.000 16.26  ? 35  GLU A DE2  1 
ATOM   678  N N    . SER A 1 37  ? 32.712 14.190 19.097 1.000 10.33  ? 36  SER A N    1 
ATOM   679  C CA   . SER A 1 37  ? 32.956 15.438 19.768 1.000 10.92  ? 36  SER A CA   1 
ATOM   680  C C    . SER A 1 37  ? 33.487 15.308 21.186 1.000 10.25  ? 36  SER A C    1 
ATOM   681  O O    . SER A 1 37  ? 33.677 16.348 21.821 1.000 11.53  ? 36  SER A O    1 
ATOM   682  C CB   . SER A 1 37  ? 31.627 16.205 19.888 1.000 10.42  ? 36  SER A CB   1 
ATOM   683  O OG   . SER A 1 37  ? 30.746 15.463 20.729 1.000 9.65   ? 36  SER A OG   1 
ATOM   684  D D    . SER A 1 37  ? 32.094 13.544 19.522 1.000 14.31  ? 36  SER A D    1 
ATOM   685  D DA   . SER A 1 37  ? 33.673 16.023 19.205 1.000 13.86  ? 36  SER A DA   1 
ATOM   686  D DB2  . SER A 1 37  ? 31.824 17.174 20.318 1.000 12.84  ? 36  SER A DB2  1 
ATOM   687  D DB3  . SER A 1 37  ? 31.159 16.335 18.904 1.000 12.69  ? 36  SER A DB3  1 
ATOM   688  D DG   . SER A 1 37  ? 30.057 15.096 20.215 1.000 12.26  ? 36  SER A DG   1 
ATOM   689  N N    A ASN A 1 38  ? 33.643 14.108 21.710 0.335 10.75  ? 37  ASN A N    1 
ATOM   690  N N    B ASN A 1 38  ? 33.708 14.091 21.660 0.665 11.21  ? 37  ASN A N    1 
ATOM   691  C CA   A ASN A 1 38  ? 34.031 13.928 23.111 0.335 11.80  ? 37  ASN A CA   1 
ATOM   692  C CA   B ASN A 1 38  ? 33.940 13.836 23.078 0.665 12.05  ? 37  ASN A CA   1 
ATOM   693  C C    A ASN A 1 38  ? 32.953 14.457 24.056 0.335 10.68  ? 37  ASN A C    1 
ATOM   694  C C    B ASN A 1 38  ? 32.983 14.632 23.986 0.665 10.52  ? 37  ASN A C    1 
ATOM   695  O O    A ASN A 1 38  ? 33.189 14.732 25.226 0.335 8.92   ? 37  ASN A O    1 
ATOM   696  O O    B ASN A 1 38  ? 33.411 15.177 24.984 0.665 11.80  ? 37  ASN A O    1 
ATOM   697  C CB   A ASN A 1 38  ? 35.383 14.576 23.414 0.335 13.78  ? 37  ASN A CB   1 
ATOM   698  C CB   B ASN A 1 38  ? 35.375 14.128 23.515 0.665 14.52  ? 37  ASN A CB   1 
ATOM   699  C CG   A ASN A 1 38  ? 36.281 13.611 24.170 0.335 15.78  ? 37  ASN A CG   1 
ATOM   700  C CG   B ASN A 1 38  ? 35.741 13.362 24.778 0.665 15.82  ? 37  ASN A CG   1 
ATOM   701  O OD1  A ASN A 1 38  ? 35.919 12.481 24.489 0.335 15.00  ? 37  ASN A OD1  1 
ATOM   702  O OD1  B ASN A 1 38  ? 35.158 12.330 25.115 0.665 15.78  ? 37  ASN A OD1  1 
ATOM   703  N ND2  A ASN A 1 38  ? 37.488 14.073 24.454 0.335 16.65  ? 37  ASN A ND2  1 
ATOM   704  N ND2  B ASN A 1 38  ? 36.697 13.876 25.515 0.665 17.53  ? 37  ASN A ND2  1 
ATOM   705  D D    A ASN A 1 38  ? 33.490 13.272 21.179 0.335 10.48  ? 37  ASN A D    1 
ATOM   706  D D    B ASN A 1 38  ? 33.723 13.322 21.008 0.665 36.57  ? 37  ASN A D    1 
ATOM   707  D DA   A ASN A 1 38  ? 34.144 12.837 23.267 0.335 13.02  ? 37  ASN A DA   1 
ATOM   708  D DA   B ASN A 1 38  ? 33.723 12.761 23.289 0.665 12.62  ? 37  ASN A DA   1 
ATOM   709  D DB2  A ASN A 1 38  ? 35.861 14.861 22.475 0.335 14.56  ? 37  ASN A DB2  1 
ATOM   710  D DB2  B ASN A 1 38  ? 36.054 13.875 22.710 0.665 17.60  ? 37  ASN A DB2  1 
ATOM   711  D DB3  A ASN A 1 38  ? 35.220 15.471 24.016 0.335 15.67  ? 37  ASN A DB3  1 
ATOM   712  D DB3  B ASN A 1 38  ? 35.489 15.197 23.688 0.665 15.83  ? 37  ASN A DB3  1 
ATOM   713  D DD21 A ASN A 1 38  ? 37.987 13.686 25.236 0.335 24.60  ? 37  ASN A DD21 1 
ATOM   714  D DD21 B ASN A 1 38  ? 36.982 13.402 26.361 0.665 22.29  ? 37  ASN A DD21 1 
ATOM   715  D DD22 A ASN A 1 38  ? 37.876 14.794 23.861 0.335 24.39  ? 37  ASN A DD22 1 
ATOM   716  D DD22 B ASN A 1 38  ? 37.097 14.769 25.254 0.665 24.59  ? 37  ASN A DD22 1 
ATOM   717  N N    . PHE A 1 39  ? 31.726 14.569 23.560 1.000 9.35   ? 38  PHE A N    1 
ATOM   718  C CA   . PHE A 1 39  ? 30.582 15.053 24.322 1.000 10.04  ? 38  PHE A CA   1 
ATOM   719  C C    . PHE A 1 39  ? 30.568 16.593 24.493 1.000 10.09  ? 38  PHE A C    1 
ATOM   720  O O    . PHE A 1 39  ? 29.805 17.100 25.308 1.000 11.35  ? 38  PHE A O    1 
ATOM   721  C CB   . PHE A 1 39  ? 30.436 14.382 25.684 1.000 11.48  ? 38  PHE A CB   1 
ATOM   722  C CG   . PHE A 1 39  ? 30.283 12.887 25.664 1.000 11.09  ? 38  PHE A CG   1 
ATOM   723  C CD1  . PHE A 1 39  ? 29.578 12.185 24.711 1.000 11.78  ? 38  PHE A CD1  1 
ATOM   724  C CD2  . PHE A 1 39  ? 30.860 12.165 26.701 1.000 13.22  ? 38  PHE A CD2  1 
ATOM   725  C CE1  . PHE A 1 39  ? 29.440 10.813 24.754 1.000 12.59  ? 38  PHE A CE1  1 
ATOM   726  C CE2  . PHE A 1 39  ? 30.733 10.785 26.746 1.000 14.53  ? 38  PHE A CE2  1 
ATOM   727  C CZ   . PHE A 1 39  ? 29.998 10.111 25.808 1.000 12.95  ? 38  PHE A CZ   1 
ATOM   728  H H    A PHE A 1 39  ? 31.576 14.302 22.597 1.000 18.57  ? 38  PHE A H    1 
ATOM   729  D DA   . PHE A 1 39  ? 29.720 14.845 23.691 1.000 10.86  ? 38  PHE A DA   1 
ATOM   730  D DB2  . PHE A 1 39  ? 31.270 14.664 26.299 1.000 15.86  ? 38  PHE A DB2  1 
ATOM   731  D DB3  . PHE A 1 39  ? 29.570 14.826 26.166 1.000 15.90  ? 38  PHE A DB3  1 
ATOM   732  D DD1  . PHE A 1 39  ? 29.132 12.728 23.874 1.000 14.57  ? 38  PHE A DD1  1 
ATOM   733  D DD2  . PHE A 1 39  ? 31.408 12.691 27.467 1.000 19.39  ? 38  PHE A DD2  1 
ATOM   734  D DE1  . PHE A 1 39  ? 28.933 10.292 23.963 1.000 16.63  ? 38  PHE A DE1  1 
ATOM   735  D DE2  . PHE A 1 39  ? 31.193 10.248 27.574 1.000 24.99  ? 38  PHE A DE2  1 
ATOM   736  D DZ   . PHE A 1 39  ? 29.808 9.059  25.890 1.000 14.80  ? 38  PHE A DZ   1 
ATOM   737  N N    A ASN A 1 40  ? 31.360 17.272 23.677 0.380 10.75  ? 39  ASN A N    1 
ATOM   738  N N    B ASN A 1 40  ? 31.392 17.292 23.723 0.620 10.33  ? 39  ASN A N    1 
ATOM   739  C CA   A ASN A 1 40  ? 31.466 18.728 23.728 0.380 10.60  ? 39  ASN A CA   1 
ATOM   740  C CA   B ASN A 1 40  ? 31.471 18.755 23.826 0.620 10.33  ? 39  ASN A CA   1 
ATOM   741  C C    A ASN A 1 40  ? 30.452 19.419 22.834 0.380 9.52   ? 39  ASN A C    1 
ATOM   742  C C    B ASN A 1 40  ? 30.469 19.410 22.880 0.620 9.52   ? 39  ASN A C    1 
ATOM   743  O O    A ASN A 1 40  ? 30.525 19.354 21.605 0.380 9.74   ? 39  ASN A O    1 
ATOM   744  O O    B ASN A 1 40  ? 30.606 19.258 21.667 0.620 9.96   ? 39  ASN A O    1 
ATOM   745  C CB   A ASN A 1 40  ? 32.888 19.122 23.306 0.380 12.00  ? 39  ASN A CB   1 
ATOM   746  C CB   B ASN A 1 40  ? 32.893 19.182 23.494 0.620 12.61  ? 39  ASN A CB   1 
ATOM   747  C CG   A ASN A 1 40  ? 33.237 20.508 23.788 0.380 13.87  ? 39  ASN A CG   1 
ATOM   748  C CG   B ASN A 1 40  ? 33.056 20.682 23.359 0.620 13.47  ? 39  ASN A CG   1 
ATOM   749  O OD1  A ASN A 1 40  ? 32.322 21.316 23.964 0.380 14.34  ? 39  ASN A OD1  1 
ATOM   750  O OD1  B ASN A 1 40  ? 32.182 21.462 23.710 0.620 15.05  ? 39  ASN A OD1  1 
ATOM   751  N ND2  A ASN A 1 40  ? 34.496 20.843 24.005 0.380 14.49  ? 39  ASN A ND2  1 
ATOM   752  N ND2  B ASN A 1 40  ? 34.220 21.078 22.854 0.620 14.90  ? 39  ASN A ND2  1 
ATOM   753  H H    A ASN A 1 40  ? 31.910 16.767 22.996 0.380 167.91 ? 39  ASN A H    1 
ATOM   754  H H    B ASN A 1 40  ? 31.976 16.810 23.054 0.620 15.68  ? 39  ASN A H    1 
ATOM   755  D DA   A ASN A 1 40  ? 31.311 19.027 24.761 0.380 11.46  ? 39  ASN A DA   1 
ATOM   756  D DA   B ASN A 1 40  ? 31.243 19.009 24.852 0.620 12.43  ? 39  ASN A DA   1 
ATOM   757  D DB2  A ASN A 1 40  ? 33.586 18.393 23.694 0.380 12.90  ? 39  ASN A DB2  1 
ATOM   758  D DB2  B ASN A 1 40  ? 33.582 18.788 24.234 0.620 13.33  ? 39  ASN A DB2  1 
ATOM   759  D DB3  A ASN A 1 40  ? 32.937 19.081 22.207 0.380 11.27  ? 39  ASN A DB3  1 
ATOM   760  D DB3  B ASN A 1 40  ? 33.177 18.710 22.530 0.620 12.52  ? 39  ASN A DB3  1 
ATOM   761  D DD21 A ASN A 1 40  ? 34.804 21.760 23.699 0.380 20.98  ? 39  ASN A DD21 1 
ATOM   762  D DD21 B ASN A 1 40  ? 34.369 22.058 22.703 0.620 24.92  ? 39  ASN A DD21 1 
ATOM   763  D DD22 A ASN A 1 40  ? 35.122 20.210 24.447 0.380 20.17  ? 39  ASN A DD22 1 
ATOM   764  D DD22 B ASN A 1 40  ? 34.914 20.377 22.650 0.620 25.06  ? 39  ASN A DD22 1 
ATOM   765  N N    . THR A 1 41  ? 29.484 20.089 23.438 1.000 9.64   ? 40  THR A N    1 
ATOM   766  C CA   . THR A 1 41  ? 28.447 20.715 22.634 1.000 9.91   ? 40  THR A CA   1 
ATOM   767  C C    . THR A 1 41  ? 28.946 21.823 21.703 1.000 9.49   ? 40  THR A C    1 
ATOM   768  O O    . THR A 1 41  ? 28.234 22.158 20.759 1.000 11.17  ? 40  THR A O    1 
ATOM   769  C CB   . THR A 1 41  ? 27.296 21.276 23.503 1.000 11.17  ? 40  THR A CB   1 
ATOM   770  O OG1  . THR A 1 41  ? 27.844 22.258 24.390 1.000 13.27  ? 40  THR A OG1  1 
ATOM   771  C CG2  . THR A 1 41  ? 26.613 20.167 24.277 1.000 13.20  ? 40  THR A CG2  1 
ATOM   772  H H    A THR A 1 41  ? 29.466 20.164 24.445 0.442 9.65   ? 40  THR A H    1 
ATOM   773  D D    B THR A 1 41  ? 29.436 20.108 24.447 0.558 10.12  ? 40  THR A D    1 
ATOM   774  D DA   . THR A 1 41  ? 27.989 19.952 21.980 1.000 10.24  ? 40  THR A DA   1 
ATOM   775  D DB   . THR A 1 41  ? 26.594 21.770 22.841 1.000 12.71  ? 40  THR A DB   1 
ATOM   776  D DG1  . THR A 1 41  ? 28.323 21.813 25.124 1.000 16.37  ? 40  THR A DG1  1 
ATOM   777  D DG21 . THR A 1 41  ? 27.266 19.677 24.938 1.000 16.38  ? 40  THR A DG21 1 
ATOM   778  D DG22 . THR A 1 41  ? 25.804 20.576 24.848 1.000 17.18  ? 40  THR A DG22 1 
ATOM   779  D DG23 . THR A 1 41  ? 26.195 19.461 23.626 1.000 17.71  ? 40  THR A DG23 1 
ATOM   780  N N    A GLN A 1 42  ? 30.079 22.464 21.969 0.482 10.10  ? 41  GLN A N    1 
ATOM   781  N N    B GLN A 1 42  ? 30.143 22.331 21.969 0.518 9.54   ? 41  GLN A N    1 
ATOM   782  C CA   A GLN A 1 42  ? 30.532 23.527 21.066 0.482 11.43  ? 41  GLN A CA   1 
ATOM   783  C CA   B GLN A 1 42  ? 30.700 23.468 21.232 0.518 10.70  ? 41  GLN A CA   1 
ATOM   784  C C    A GLN A 1 42  ? 31.695 23.047 20.194 0.482 10.47  ? 41  GLN A C    1 
ATOM   785  C C    B GLN A 1 42  ? 31.669 23.046 20.136 0.518 10.24  ? 41  GLN A C    1 
ATOM   786  O O    A GLN A 1 42  ? 32.436 23.877 19.644 0.482 12.39  ? 41  GLN A O    1 
ATOM   787  O O    B GLN A 1 42  ? 32.195 23.890 19.395 0.518 11.26  ? 41  GLN A O    1 
ATOM   788  C CB   A GLN A 1 42  ? 30.933 24.809 21.797 0.482 12.64  ? 41  GLN A CB   1 
ATOM   789  C CB   B GLN A 1 42  ? 31.365 24.431 22.218 0.518 12.17  ? 41  GLN A CB   1 
ATOM   790  C CG   A GLN A 1 42  ? 29.814 25.613 22.434 0.482 17.81  ? 41  GLN A CG   1 
ATOM   791  C CG   B GLN A 1 42  ? 30.307 24.991 23.154 0.518 15.15  ? 41  GLN A CG   1 
ATOM   792  C CD   A GLN A 1 42  ? 30.236 27.019 22.796 0.482 16.55  ? 41  GLN A CD   1 
ATOM   793  C CD   B GLN A 1 42  ? 30.673 26.257 23.888 0.518 18.54  ? 41  GLN A CD   1 
ATOM   794  O OE1  A GLN A 1 42  ? 29.661 28.051 22.438 0.482 14.53  ? 41  GLN A OE1  1 
ATOM   795  O OE1  B GLN A 1 42  ? 30.089 27.311 23.626 0.518 23.86  ? 41  GLN A OE1  1 
ATOM   796  N NE2  A GLN A 1 42  ? 31.334 27.125 23.552 0.482 23.75  ? 41  GLN A NE2  1 
ATOM   797  N NE2  B GLN A 1 42  ? 31.605 26.223 24.828 0.518 28.05  ? 41  GLN A NE2  1 
ATOM   798  D D    A GLN A 1 42  ? 30.603 22.229 22.781 0.482 10.14  ? 41  GLN A D    1 
ATOM   799  D D    B GLN A 1 42  ? 30.680 21.904 22.705 0.518 11.68  ? 41  GLN A D    1 
ATOM   800  D DA   A GLN A 1 42  ? 29.669 23.731 20.413 0.482 11.29  ? 41  GLN A DA   1 
ATOM   801  D DA   B GLN A 1 42  ? 29.855 23.977 20.751 0.518 10.96  ? 41  GLN A DA   1 
ATOM   802  D DB2  A GLN A 1 42  ? 31.674 24.562 22.556 0.482 14.38  ? 41  GLN A DB2  1 
ATOM   803  D DB2  B GLN A 1 42  ? 32.111 23.896 22.793 0.518 13.96  ? 41  GLN A DB2  1 
ATOM   804  D DB3  A GLN A 1 42  ? 31.472 25.454 21.094 0.482 15.66  ? 41  GLN A DB3  1 
ATOM   805  D DB3  B GLN A 1 42  ? 31.848 25.227 21.686 0.518 14.65  ? 41  GLN A DB3  1 
ATOM   806  D DG2  A GLN A 1 42  ? 28.967 25.664 21.746 0.482 22.47  ? 41  GLN A DG2  1 
ATOM   807  D DG2  B GLN A 1 42  ? 29.385 25.158 22.586 0.518 20.16  ? 41  GLN A DG2  1 
ATOM   808  D DG3  A GLN A 1 42  ? 29.471 25.090 23.330 0.482 20.84  ? 41  GLN A DG3  1 
ATOM   809  D DG3  B GLN A 1 42  ? 30.042 24.215 23.882 0.518 18.43  ? 41  GLN A DG3  1 
ATOM   810  D DE21 A GLN A 1 42  ? 31.454 27.913 24.183 0.482 28.51  ? 41  GLN A DE21 1 
ATOM   811  D DE21 B GLN A 1 42  ? 31.446 25.789 25.730 0.518 33.66  ? 41  GLN A DE21 1 
ATOM   812  D DE22 A GLN A 1 42  ? 32.073 26.428 23.479 0.482 28.51  ? 41  GLN A DE22 1 
ATOM   813  D DE22 B GLN A 1 42  ? 32.525 26.649 24.673 0.518 33.66  ? 41  GLN A DE22 1 
ATOM   814  N N    . ALA A 1 43  ? 31.876 21.753 20.023 1.000 10.33  ? 42  ALA A N    1 
ATOM   815  C CA   . ALA A 1 43  ? 32.893 21.264 19.087 1.000 10.62  ? 42  ALA A CA   1 
ATOM   816  C C    . ALA A 1 43  ? 32.624 21.732 17.669 1.000 9.29   ? 42  ALA A C    1 
ATOM   817  O O    . ALA A 1 43  ? 31.526 21.633 17.150 1.000 11.06  ? 42  ALA A O    1 
ATOM   818  C CB   . ALA A 1 43  ? 32.929 19.745 19.091 1.000 12.84  ? 42  ALA A CB   1 
ATOM   819  H H    A ALA A 1 43  ? 31.311 21.095 20.539 0.674 8.75   ? 42  ALA A H    1 
ATOM   820  D D    B ALA A 1 43  ? 31.282 21.104 20.518 0.326 8.29   ? 42  ALA A D    1 
ATOM   821  D DA   . ALA A 1 43  ? 33.868 21.670 19.375 1.000 11.36  ? 42  ALA A DA   1 
ATOM   822  D DB1  . ALA A 1 43  ? 31.991 19.343 18.809 1.000 14.63  ? 42  ALA A DB1  1 
ATOM   823  D DB2  . ALA A 1 43  ? 33.665 19.398 18.381 1.000 16.21  ? 42  ALA A DB2  1 
ATOM   824  D DB3  . ALA A 1 43  ? 33.225 19.374 20.033 1.000 15.46  ? 42  ALA A DB3  1 
ATOM   825  N N    . THR A 1 44  ? 33.669 22.235 17.026 1.000 10.14  ? 43  THR A N    1 
ATOM   826  C CA   . THR A 1 44  ? 33.571 22.733 15.661 1.000 11.23  ? 43  THR A CA   1 
ATOM   827  C C    . THR A 1 44  ? 34.807 22.236 14.904 1.000 11.82  ? 43  THR A C    1 
ATOM   828  O O    . THR A 1 44  ? 35.890 22.377 15.447 1.000 18.76  ? 43  THR A O    1 
ATOM   829  C CB   . THR A 1 44  ? 33.535 24.256 15.693 1.000 15.09  ? 43  THR A CB   1 
ATOM   830  O OG1  . THR A 1 44  ? 32.412 24.764 16.436 1.000 17.77  ? 43  THR A OG1  1 
ATOM   831  C CG2  . THR A 1 44  ? 33.296 24.825 14.303 1.000 18.94  ? 43  THR A CG2  1 
ATOM   832  D D    . THR A 1 44  ? 34.579 22.319 17.482 1.000 13.29  ? 43  THR A D    1 
ATOM   833  D DA   . THR A 1 44  ? 32.672 22.338 15.209 1.000 11.07  ? 43  THR A DA   1 
ATOM   834  D DB   . THR A 1 44  ? 34.494 24.724 16.060 1.000 18.03  ? 43  THR A DB   1 
ATOM   835  D DG1  . THR A 1 44  ? 32.393 24.361 17.320 1.000 18.97  ? 43  THR A DG1  1 
ATOM   836  D DG21 . THR A 1 44  ? 32.366 24.435 13.935 1.000 22.96  ? 43  THR A DG21 1 
ATOM   837  D DG22 . THR A 1 44  ? 33.118 25.879 14.383 1.000 23.30  ? 43  THR A DG22 1 
ATOM   838  D DG23 . THR A 1 44  ? 34.132 24.634 13.699 1.000 26.33  ? 43  THR A DG23 1 
ATOM   839  N N    . ASN A 1 45  ? 34.629 21.715 13.707 1.000 10.51  ? 44  ASN A N    1 
ATOM   840  C CA   . ASN A 1 45  ? 35.738 21.270 12.887 1.000 10.74  ? 44  ASN A CA   1 
ATOM   841  C C    . ASN A 1 45  ? 35.590 21.936 11.523 1.000 9.55   ? 44  ASN A C    1 
ATOM   842  O O    . ASN A 1 45  ? 34.641 21.651 10.813 1.000 10.77  ? 44  ASN A O    1 
ATOM   843  C CB   . ASN A 1 45  ? 35.752 19.746 12.710 1.000 13.18  ? 44  ASN A CB   1 
ATOM   844  C CG   . ASN A 1 45  ? 36.877 19.261 11.809 1.000 17.56  ? 44  ASN A CG   1 
ATOM   845  O OD1  . ASN A 1 45  ? 38.063 19.526 12.023 1.000 25.43  ? 44  ASN A OD1  1 
ATOM   846  N ND2  . ASN A 1 45  ? 36.570 18.589 10.687 1.000 26.09  ? 44  ASN A ND2  1 
ATOM   847  H H    . ASN A 1 45  ? 33.689 21.623 13.349 1.000 16.99  ? 44  ASN A H    1 
ATOM   848  D DA   . ASN A 1 45  ? 36.655 21.629 13.351 1.000 12.40  ? 44  ASN A DA   1 
ATOM   849  D DB2  . ASN A 1 45  ? 35.805 19.251 13.661 1.000 18.80  ? 44  ASN A DB2  1 
ATOM   850  D DB3  . ASN A 1 45  ? 34.797 19.436 12.292 1.000 16.32  ? 44  ASN A DB3  1 
ATOM   851  D DD21 . ASN A 1 45  ? 37.312 18.135 10.200 1.000 36.09  ? 44  ASN A DD21 1 
ATOM   852  D DD22 . ASN A 1 45  ? 35.611 18.609 10.383 1.000 37.96  ? 44  ASN A DD22 1 
ATOM   853  N N    A ARG A 1 46  ? 36.523 22.810 11.151 0.573 10.23  ? 45  ARG A N    1 
ATOM   854  N N    B ARG A 1 46  ? 36.525 22.809 11.204 0.427 10.41  ? 45  ARG A N    1 
ATOM   855  C CA   A ARG A 1 46  ? 36.427 23.581 9.915  0.573 11.19  ? 45  ARG A CA   1 
ATOM   856  C CA   B ARG A 1 46  ? 36.479 23.513 9.929  0.427 10.42  ? 45  ARG A CA   1 
ATOM   857  C C    A ARG A 1 46  ? 37.280 22.918 8.831  0.573 11.05  ? 45  ARG A C    1 
ATOM   858  C C    B ARG A 1 46  ? 37.281 22.737 8.899  0.427 10.85  ? 45  ARG A C    1 
ATOM   859  O O    A ARG A 1 46  ? 38.507 22.913 8.904  0.573 12.82  ? 45  ARG A O    1 
ATOM   860  O O    B ARG A 1 46  ? 38.463 22.478 9.104  0.427 11.99  ? 45  ARG A O    1 
ATOM   861  C CB   A ARG A 1 46  ? 36.838 25.037 10.162 0.573 13.84  ? 45  ARG A CB   1 
ATOM   862  C CB   B ARG A 1 46  ? 37.017 24.918 10.174 0.427 12.02  ? 45  ARG A CB   1 
ATOM   863  C CG   A ARG A 1 46  ? 36.097 25.665 11.317 0.573 16.26  ? 45  ARG A CG   1 
ATOM   864  C CG   B ARG A 1 46  ? 36.126 25.698 11.099 0.427 15.09  ? 45  ARG A CG   1 
ATOM   865  C CD   A ARG A 1 46  ? 36.243 27.173 11.508 0.573 19.53  ? 45  ARG A CD   1 
ATOM   866  C CD   B ARG A 1 46  ? 36.735 27.039 11.448 0.427 18.81  ? 45  ARG A CD   1 
ATOM   867  N NE   A ARG A 1 46  ? 35.185 27.702 12.366 0.573 21.43  ? 45  ARG A NE   1 
ATOM   868  N NE   B ARG A 1 46  ? 35.979 27.736 12.477 0.427 20.38  ? 45  ARG A NE   1 
ATOM   869  C CZ   A ARG A 1 46  ? 33.967 28.074 12.010 0.573 22.46  ? 45  ARG A CZ   1 
ATOM   870  C CZ   B ARG A 1 46  ? 36.189 27.550 13.767 0.427 22.49  ? 45  ARG A CZ   1 
ATOM   871  N NH1  A ARG A 1 46  ? 33.596 28.076 10.744 0.573 25.11  ? 45  ARG A NH1  1 
ATOM   872  N NH1  B ARG A 1 46  ? 37.351 26.927 14.009 0.427 23.55  ? 45  ARG A NH1  1 
ATOM   873  N NH2  A ARG A 1 46  ? 33.129 28.389 12.990 0.573 23.32  ? 45  ARG A NH2  1 
ATOM   874  N NH2  B ARG A 1 46  ? 35.367 27.918 14.730 0.427 24.73  ? 45  ARG A NH2  1 
ATOM   875  D D    A ARG A 1 46  ? 37.329 22.932 11.735 0.573 15.54  ? 45  ARG A D    1 
ATOM   876  D D    B ARG A 1 46  ? 37.280 22.988 11.839 0.427 15.68  ? 45  ARG A D    1 
ATOM   877  D DA   A ARG A 1 46  ? 35.385 23.533 9.594  0.573 10.43  ? 45  ARG A DA   1 
ATOM   878  D DA   B ARG A 1 46  ? 35.438 23.576 9.613  0.427 10.00  ? 45  ARG A DA   1 
ATOM   879  D DB2  A ARG A 1 46  ? 37.902 25.064 10.343 0.573 15.90  ? 45  ARG A DB2  1 
ATOM   880  D DB2  B ARG A 1 46  ? 38.014 24.825 10.613 0.427 14.59  ? 45  ARG A DB2  1 
ATOM   881  D DB3  A ARG A 1 46  ? 36.648 25.596 9.255  0.573 14.59  ? 45  ARG A DB3  1 
ATOM   882  D DB3  B ARG A 1 46  ? 37.114 25.426 9.227  0.427 12.52  ? 45  ARG A DB3  1 
ATOM   883  D DG2  A ARG A 1 46  ? 35.026 25.462 11.186 0.573 17.26  ? 45  ARG A DG2  1 
ATOM   884  D DG2  B ARG A 1 46  ? 35.152 25.850 10.643 0.427 14.49  ? 45  ARG A DG2  1 
ATOM   885  D DG3  A ARG A 1 46  ? 36.410 25.184 12.245 0.573 17.52  ? 45  ARG A DG3  1 
ATOM   886  D DG3  B ARG A 1 46  ? 35.941 25.139 12.005 0.427 14.19  ? 45  ARG A DG3  1 
ATOM   887  D DD2  A ARG A 1 46  ? 37.211 27.367 11.963 0.573 21.47  ? 45  ARG A DD2  1 
ATOM   888  D DD2  B ARG A 1 46  ? 37.744 26.821 11.806 0.427 18.66  ? 45  ARG A DD2  1 
ATOM   889  D DD3  A ARG A 1 46  ? 36.158 27.681 10.552 0.573 21.76  ? 45  ARG A DD3  1 
ATOM   890  D DD3  B ARG A 1 46  ? 36.826 27.657 10.560 0.427 19.73  ? 45  ARG A DD3  1 
ATOM   891  D DE   A ARG A 1 46  ? 35.495 27.744 13.325 0.573 20.10  ? 45  ARG A DE   1 
ATOM   892  D DE   B ARG A 1 46  ? 35.299 28.349 12.100 0.427 29.72  ? 45  ARG A DE   1 
ATOM   893  D DH11 A ARG A 1 46  ? 32.616 28.010 10.502 0.573 31.32  ? 45  ARG A DH11 1 
ATOM   894  D DH11 B ARG A 1 46  ? 37.904 27.255 14.803 0.427 29.58  ? 45  ARG A DH11 1 
ATOM   895  D DH12 A ARG A 1 46  ? 34.283 28.111 10.007 0.573 29.65  ? 45  ARG A DH12 1 
ATOM   896  D DH12 B ARG A 1 46  ? 37.881 26.596 13.209 0.427 27.94  ? 45  ARG A DH12 1 
ATOM   897  D DH21 A ARG A 1 46  ? 32.193 28.691 12.768 0.573 25.51  ? 45  ARG A DH21 1 
ATOM   898  D DH21 B ARG A 1 46  ? 35.564 27.686 15.691 0.427 26.36  ? 45  ARG A DH21 1 
ATOM   899  D DH22 A ARG A 1 46  ? 33.440 28.312 13.952 0.573 21.71  ? 45  ARG A DH22 1 
ATOM   900  D DH22 B ARG A 1 46  ? 34.507 28.395 14.522 0.427 23.12  ? 45  ARG A DH22 1 
ATOM   901  N N    . ASN A 1 47  ? 36.635 22.379 7.802  1.000 11.26  ? 46  ASN A N    1 
ATOM   902  C CA   . ASN A 1 47  ? 37.252 21.571 6.767  1.000 12.44  ? 46  ASN A CA   1 
ATOM   903  C C    . ASN A 1 47  ? 37.804 22.456 5.645  1.000 11.80  ? 46  ASN A C    1 
ATOM   904  O O    . ASN A 1 47  ? 37.433 23.594 5.416  1.000 13.18  ? 46  ASN A O    1 
ATOM   905  C CB   . ASN A 1 47  ? 36.226 20.589 6.190  1.000 13.06  ? 46  ASN A CB   1 
ATOM   906  C CG   . ASN A 1 47  ? 35.662 19.678 7.261  1.000 14.43  ? 46  ASN A CG   1 
ATOM   907  O OD1  . ASN A 1 47  ? 36.385 18.965 7.908  1.000 17.18  ? 46  ASN A OD1  1 
ATOM   908  N ND2  . ASN A 1 47  ? 34.356 19.709 7.467  1.000 15.33  ? 46  ASN A ND2  1 
ATOM   909  D D    . ASN A 1 47  ? 35.664 22.624 7.668  1.000 12.94  ? 46  ASN A D    1 
ATOM   910  D DA   . ASN A 1 47  ? 38.087 21.033 7.242  1.000 14.75  ? 46  ASN A DA   1 
ATOM   911  D DB2  . ASN A 1 47  ? 35.407 21.156 5.733  1.000 13.96  ? 46  ASN A DB2  1 
ATOM   912  D DB3  . ASN A 1 47  ? 36.695 20.000 5.406  1.000 16.99  ? 46  ASN A DB3  1 
ATOM   913  D DD21 . ASN A 1 47  ? 33.952 19.082 8.148  1.000 21.70  ? 46  ASN A DD21 1 
ATOM   914  D DD22 . ASN A 1 47  ? 33.798 20.347 6.941  1.000 18.23  ? 46  ASN A DD22 1 
ATOM   915  N N    . THR A 1 48  ? 38.711 21.865 4.853  1.000 14.32  ? 47  THR A N    1 
ATOM   916  C CA   . THR A 1 48  ? 39.298 22.587 3.745  1.000 14.61  ? 47  THR A CA   1 
ATOM   917  C C    . THR A 1 48  ? 38.383 22.719 2.519  1.000 15.67  ? 47  THR A C    1 
ATOM   918  O O    . THR A 1 48  ? 38.707 23.530 1.653  1.000 18.01  ? 47  THR A O    1 
ATOM   919  C CB   . THR A 1 48  ? 40.592 21.916 3.257  1.000 16.02  ? 47  THR A CB   1 
ATOM   920  O OG1  . THR A 1 48  ? 40.331 20.564 2.873  1.000 16.23  ? 47  THR A OG1  1 
ATOM   921  C CG2  . THR A 1 48  ? 41.623 21.952 4.373  1.000 17.02  ? 47  THR A CG2  1 
ATOM   922  D D    . THR A 1 48  ? 38.975 20.920 5.078  1.000 16.87  ? 47  THR A D    1 
ATOM   923  D DA   . THR A 1 48  ? 39.584 23.607 4.065  1.000 17.72  ? 47  THR A DA   1 
ATOM   924  D DB   . THR A 1 48  ? 40.960 22.458 2.366  1.000 18.10  ? 47  THR A DB   1 
ATOM   925  D DG1  . THR A 1 48  ? 40.879 19.921 3.330  1.000 20.87  ? 47  THR A DG1  1 
ATOM   926  D DG21 . THR A 1 48  ? 41.304 21.391 5.204  1.000 18.18  ? 47  THR A DG21 1 
ATOM   927  D DG22 . THR A 1 48  ? 42.545 21.566 3.995  1.000 22.69  ? 47  THR A DG22 1 
ATOM   928  D DG23 . THR A 1 48  ? 41.736 22.961 4.714  1.000 21.15  ? 47  THR A DG23 1 
ATOM   929  N N    . ASP A 1 49  ? 37.285 21.991 2.449  1.000 16.07  ? 48  ASP A N    1 
ATOM   930  C CA   . ASP A 1 49  ? 36.317 22.079 1.366  1.000 17.08  ? 48  ASP A CA   1 
ATOM   931  C C    . ASP A 1 49  ? 35.334 23.218 1.570  1.000 16.76  ? 48  ASP A C    1 
ATOM   932  O O    . ASP A 1 49  ? 34.410 23.358 0.763  1.000 22.61  ? 48  ASP A O    1 
ATOM   933  C CB   . ASP A 1 49  ? 35.646 20.719 1.195  1.000 19.01  ? 48  ASP A CB   1 
ATOM   934  C CG   . ASP A 1 49  ? 34.764 20.281 2.344  1.000 18.87  ? 48  ASP A CG   1 
ATOM   935  O OD1  . ASP A 1 49  ? 34.531 21.058 3.278  1.000 15.03  ? 48  ASP A OD1  1 
ATOM   936  O OD2  . ASP A 1 49  ? 34.314 19.110 2.275  1.000 24.93  ? 48  ASP A OD2  1 
ATOM   937  D D    . ASP A 1 49  ? 37.139 21.345 3.199  1.000 19.09  ? 48  ASP A D    1 
ATOM   938  D DA   . ASP A 1 49  ? 36.853 22.328 0.447  1.000 18.00  ? 48  ASP A DA   1 
ATOM   939  D DB2  . ASP A 1 49  ? 35.049 20.746 0.285  1.000 23.56  ? 48  ASP A DB2  1 
ATOM   940  D DB3  . ASP A 1 49  ? 36.433 19.975 1.067  1.000 21.62  ? 48  ASP A DB3  1 
ATOM   941  N N    . GLY A 1 50  ? 35.532 23.986 2.642  1.000 15.50  ? 49  GLY A N    1 
ATOM   942  C CA   . GLY A 1 50  ? 34.637 25.082 2.893  1.000 16.31  ? 49  GLY A CA   1 
ATOM   943  C C    . GLY A 1 50  ? 33.442 24.785 3.768  1.000 13.52  ? 49  GLY A C    1 
ATOM   944  O O    . GLY A 1 50  ? 32.644 25.666 4.095  1.000 17.29  ? 49  GLY A O    1 
ATOM   945  D D    . GLY A 1 50  ? 36.287 23.787 3.321  1.000 16.36  ? 49  GLY A D    1 
ATOM   946  D DA2  . GLY A 1 50  ? 35.186 25.892 3.347  1.000 20.63  ? 49  GLY A DA2  1 
ATOM   947  D DA3  . GLY A 1 50  ? 34.209 25.408 1.948  1.000 20.48  ? 49  GLY A DA3  1 
ATOM   948  N N    . SER A 1 51  ? 33.298 23.529 4.147  1.000 11.32  ? 50  SER A N    1 
ATOM   949  C CA   . SER A 1 51  ? 32.270 23.118 5.086  1.000 9.55   ? 50  SER A CA   1 
ATOM   950  C C    . SER A 1 51  ? 32.838 23.022 6.494  1.000 9.27   ? 50  SER A C    1 
ATOM   951  O O    . SER A 1 51  ? 34.031 22.975 6.715  1.000 10.11  ? 50  SER A O    1 
ATOM   952  C CB   . SER A 1 51  ? 31.649 21.784 4.681  1.000 10.80  ? 50  SER A CB   1 
ATOM   953  O OG   . SER A 1 51  ? 32.557 20.726 4.984  1.000 11.24  ? 50  SER A OG   1 
ATOM   954  D D    . SER A 1 51  ? 33.939 22.820 3.831  1.000 14.31  ? 50  SER A D    1 
ATOM   955  D DA   . SER A 1 51  ? 31.476 23.880 5.042  1.000 10.90  ? 50  SER A DA   1 
ATOM   956  D DB2  . SER A 1 51  ? 30.748 21.601 5.247  1.000 12.79  ? 50  SER A DB2  1 
ATOM   957  D DB3  . SER A 1 51  ? 31.469 21.770 3.594  1.000 14.42  ? 50  SER A DB3  1 
ATOM   958  D DG   . SER A 1 51  ? 33.287 20.655 4.321  1.000 13.86  ? 50  SER A DG   1 
ATOM   959  N N    . THR A 1 52  ? 31.901 22.988 7.455  1.000 8.56   ? 51  THR A N    1 
ATOM   960  C CA   . THR A 1 52  ? 32.241 22.896 8.856  1.000 7.71   ? 51  THR A CA   1 
ATOM   961  C C    . THR A 1 52  ? 31.315 21.865 9.518  1.000 7.33   ? 51  THR A C    1 
ATOM   962  O O    . THR A 1 52  ? 30.153 21.757 9.117  1.000 8.35   ? 51  THR A O    1 
ATOM   963  C CB   . THR A 1 52  ? 32.078 24.287 9.521  1.000 8.51   ? 51  THR A CB   1 
ATOM   964  O OG1  . THR A 1 52  ? 33.002 25.192 8.887  1.000 10.14  ? 51  THR A OG1  1 
ATOM   965  C CG2  . THR A 1 52  ? 32.362 24.303 11.001 1.000 9.76   ? 51  THR A CG2  1 
ATOM   966  D D    . THR A 1 52  ? 30.930 23.079 7.204  1.000 10.50  ? 51  THR A D    1 
ATOM   967  D DA   . THR A 1 52  ? 33.282 22.584 8.940  1.000 8.44   ? 51  THR A DA   1 
ATOM   968  D DB   . THR A 1 52  ? 31.057 24.631 9.333  1.000 10.00  ? 51  THR A DB   1 
ATOM   969  D DG1  . THR A 1 52  ? 32.583 25.531 8.058  1.000 11.57  ? 51  THR A DG1  1 
ATOM   970  D DG21 . THR A 1 52  ? 33.358 23.943 11.191 1.000 12.21  ? 51  THR A DG21 1 
ATOM   971  D DG22 . THR A 1 52  ? 32.297 25.304 11.369 1.000 12.80  ? 51  THR A DG22 1 
ATOM   972  D DG23 . THR A 1 52  ? 31.639 23.717 11.518 1.000 11.90  ? 51  THR A DG23 1 
ATOM   973  N N    . ASP A 1 53  ? 31.868 21.139 10.464 1.000 7.91   ? 52  ASP A N    1 
ATOM   974  C CA   . ASP A 1 53  ? 31.081 20.179 11.260 1.000 7.76   ? 52  ASP A CA   1 
ATOM   975  C C    . ASP A 1 53  ? 30.818 20.792 12.623 1.000 7.84   ? 52  ASP A C    1 
ATOM   976  O O    . ASP A 1 53  ? 31.747 21.287 13.262 1.000 9.61   ? 52  ASP A O    1 
ATOM   977  C CB   . ASP A 1 53  ? 31.867 18.883 11.434 1.000 9.44   ? 52  ASP A CB   1 
ATOM   978  C CG   . ASP A 1 53  ? 32.333 18.294 10.118 1.000 11.20  ? 52  ASP A CG   1 
ATOM   979  O OD1  . ASP A 1 53  ? 31.562 18.299 9.158  1.000 16.26  ? 52  ASP A OD1  1 
ATOM   980  O OD2  . ASP A 1 53  ? 33.508 17.828 10.129 1.000 17.57  ? 52  ASP A OD2  1 
ATOM   981  H H    . ASP A 1 53  ? 32.855 21.241 10.649 1.000 12.03  ? 52  ASP A H    1 
ATOM   982  D DA   . ASP A 1 53  ? 30.167 19.987 10.726 1.000 9.07   ? 52  ASP A DA   1 
ATOM   983  D DB2  . ASP A 1 53  ? 32.740 19.102 12.044 1.000 11.37  ? 52  ASP A DB2  1 
ATOM   984  D DB3  . ASP A 1 53  ? 31.234 18.154 11.917 1.000 11.63  ? 52  ASP A DB3  1 
ATOM   985  N N    . TYR A 1 54  ? 29.570 20.751 13.048 1.000 7.63   ? 53  TYR A N    1 
ATOM   986  C CA   . TYR A 1 54  ? 29.093 21.475 14.221 1.000 8.01   ? 53  TYR A CA   1 
ATOM   987  C C    . TYR A 1 54  ? 28.489 20.588 15.289 1.000 7.47   ? 53  TYR A C    1 
ATOM   988  O O    . TYR A 1 54  ? 27.574 19.804 15.061 1.000 8.62   ? 53  TYR A O    1 
ATOM   989  C CB   . TYR A 1 54  ? 28.014 22.492 13.828 1.000 8.66   ? 53  TYR A CB   1 
ATOM   990  C CG   . TYR A 1 54  ? 28.498 23.640 12.931 1.000 8.62   ? 53  TYR A CG   1 
ATOM   991  C CD1  . TYR A 1 54  ? 28.982 24.816 13.492 1.000 10.08  ? 53  TYR A CD1  1 
ATOM   992  C CD2  . TYR A 1 54  ? 28.461 23.544 11.566 1.000 8.46   ? 53  TYR A CD2  1 
ATOM   993  C CE1  . TYR A 1 54  ? 29.403 25.878 12.734 1.000 10.30  ? 53  TYR A CE1  1 
ATOM   994  C CE2  . TYR A 1 54  ? 28.876 24.610 10.790 1.000 8.84   ? 53  TYR A CE2  1 
ATOM   995  C CZ   . TYR A 1 54  ? 29.371 25.772 11.357 1.000 9.44   ? 53  TYR A CZ   1 
ATOM   996  O OH   . TYR A 1 54  ? 29.794 26.818 10.596 1.000 10.58  ? 53  TYR A OH   1 
ATOM   997  H H    A TYR A 1 54  ? 28.909 20.188 12.533 0.882 9.49   ? 53  TYR A H    1 
ATOM   998  D D    B TYR A 1 54  ? 28.958 20.045 12.649 0.118 5.71   ? 53  TYR A D    1 
ATOM   999  D DA   . TYR A 1 54  ? 29.969 22.004 14.608 1.000 9.12   ? 53  TYR A DA   1 
ATOM   1000 D DB2  . TYR A 1 54  ? 27.217 21.945 13.316 1.000 11.51  ? 53  TYR A DB2  1 
ATOM   1001 D DB3  . TYR A 1 54  ? 27.578 22.903 14.721 1.000 11.45  ? 53  TYR A DB3  1 
ATOM   1002 D DD1  . TYR A 1 54  ? 29.042 24.883 14.582 1.000 13.24  ? 53  TYR A DD1  1 
ATOM   1003 D DD2  . TYR A 1 54  ? 28.106 22.655 11.092 1.000 10.27  ? 53  TYR A DD2  1 
ATOM   1004 D DE1  . TYR A 1 54  ? 29.714 26.809 13.176 1.000 16.08  ? 53  TYR A DE1  1 
ATOM   1005 D DE2  . TYR A 1 54  ? 28.826 24.546 9.714  1.000 10.66  ? 53  TYR A DE2  1 
ATOM   1006 D DH   . TYR A 1 54  ? 29.568 26.739 9.666  1.000 12.02  ? 53  TYR A DH   1 
ATOM   1007 N N    . GLY A 1 55  ? 28.945 20.830 16.523 1.000 8.45   ? 54  GLY A N    1 
ATOM   1008 C CA   . GLY A 1 55  ? 28.269 20.364 17.714 1.000 9.14   ? 54  GLY A CA   1 
ATOM   1009 C C    . GLY A 1 55  ? 28.571 18.938 18.109 1.000 7.91   ? 54  GLY A C    1 
ATOM   1010 O O    . GLY A 1 55  ? 29.480 18.298 17.584 1.000 8.36   ? 54  GLY A O    1 
ATOM   1011 H H    . GLY A 1 55  ? 29.798 21.360 16.628 1.000 12.83  ? 54  GLY A H    1 
ATOM   1012 D DA2  . GLY A 1 55  ? 28.560 21.012 18.537 1.000 11.58  ? 54  GLY A DA2  1 
ATOM   1013 D DA3  . GLY A 1 55  ? 27.201 20.460 17.591 1.000 10.78  ? 54  GLY A DA3  1 
ATOM   1014 N N    . ILE A 1 56  ? 27.762 18.461 19.047 1.000 8.34   ? 55  ILE A N    1 
ATOM   1015 C CA   . ILE A 1 56  ? 28.015 17.184 19.690 1.000 8.78   ? 55  ILE A CA   1 
ATOM   1016 C C    . ILE A 1 56  ? 27.998 15.997 18.725 1.000 8.36   ? 55  ILE A C    1 
ATOM   1017 O O    . ILE A 1 56  ? 28.670 15.002 18.994 1.000 10.18  ? 55  ILE A O    1 
ATOM   1018 C CB   . ILE A 1 56  ? 26.996 17.048 20.847 1.000 11.92  ? 55  ILE A CB   1 
ATOM   1019 C CG1  . ILE A 1 56  ? 27.464 15.939 21.825 1.000 16.56  ? 55  ILE A CG1  1 
ATOM   1020 C CG2  . ILE A 1 56  ? 25.575 16.872 20.401 1.000 14.20  ? 55  ILE A CG2  1 
ATOM   1021 C CD1  . ILE A 1 56  ? 26.775 16.040 23.179 1.000 19.18  ? 55  ILE A CD1  1 
ATOM   1022 H H    A ILE A 1 56  ? 26.953 18.999 19.321 0.317 6.28   ? 55  ILE A H    1 
ATOM   1023 D D    B ILE A 1 56  ? 27.035 19.047 19.365 0.683 9.20   ? 55  ILE A D    1 
ATOM   1024 D DA   . ILE A 1 56  ? 29.024 17.171 20.126 1.000 10.17  ? 55  ILE A DA   1 
ATOM   1025 D DB   . ILE A 1 56  ? 27.078 17.999 21.446 1.000 13.94  ? 55  ILE A DB   1 
ATOM   1026 D DG12 . ILE A 1 56  ? 27.226 15.006 21.361 1.000 20.56  ? 55  ILE A DG12 1 
ATOM   1027 D DG13 . ILE A 1 56  ? 28.531 16.124 22.000 1.000 18.62  ? 55  ILE A DG13 1 
ATOM   1028 D DG21 . ILE A 1 56  ? 25.421 15.970 19.850 1.000 19.24  ? 55  ILE A DG21 1 
ATOM   1029 D DG22 . ILE A 1 56  ? 24.869 16.931 21.223 1.000 20.88  ? 55  ILE A DG22 1 
ATOM   1030 D DG23 . ILE A 1 56  ? 25.245 17.662 19.754 1.000 18.71  ? 55  ILE A DG23 1 
ATOM   1031 D DD11 . ILE A 1 56  ? 27.114 16.956 23.633 1.000 24.89  ? 55  ILE A DD11 1 
ATOM   1032 D DD12 . ILE A 1 56  ? 25.733 16.114 23.011 1.000 24.27  ? 55  ILE A DD12 1 
ATOM   1033 D DD13 . ILE A 1 56  ? 27.121 15.250 23.804 1.000 22.05  ? 55  ILE A DD13 1 
ATOM   1034 N N    A LEU A 1 57  ? 27.240 16.115 17.638 0.387 8.27   ? 56  LEU A N    1 
ATOM   1035 N N    C LEU A 1 57  ? 27.250 16.074 17.627 0.613 8.50   ? 56  LEU A N    1 
ATOM   1036 C CA   A LEU A 1 57  ? 27.183 15.107 16.600 0.387 7.89   ? 56  LEU A CA   1 
ATOM   1037 C CA   C LEU A 1 57  ? 27.294 15.029 16.624 0.613 8.47   ? 56  LEU A CA   1 
ATOM   1038 C C    A LEU A 1 57  ? 27.861 15.550 15.294 0.387 8.08   ? 56  LEU A C    1 
ATOM   1039 C C    C LEU A 1 57  ? 28.011 15.456 15.337 0.613 8.42   ? 56  LEU A C    1 
ATOM   1040 O O    A LEU A 1 57  ? 27.619 14.864 14.291 0.387 9.29   ? 56  LEU A O    1 
ATOM   1041 O O    C LEU A 1 57  ? 27.999 14.718 14.338 0.613 9.56   ? 56  LEU A O    1 
ATOM   1042 C CB   A LEU A 1 57  ? 25.724 14.702 16.334 0.387 9.27   ? 56  LEU A CB   1 
ATOM   1043 C CB   C LEU A 1 57  ? 25.860 14.512 16.371 0.613 9.43   ? 56  LEU A CB   1 
ATOM   1044 C CG   A LEU A 1 57  ? 25.025 13.976 17.477 0.387 10.99  ? 56  LEU A CG   1 
ATOM   1045 C CG   C LEU A 1 57  ? 25.383 13.521 17.434 0.613 11.25  ? 56  LEU A CG   1 
ATOM   1046 C CD1  A LEU A 1 57  ? 23.565 13.706 17.087 0.387 12.90  ? 56  LEU A CD1  1 
ATOM   1047 C CD1  C LEU A 1 57  ? 23.900 13.244 17.288 0.613 12.91  ? 56  LEU A CD1  1 
ATOM   1048 C CD2  A LEU A 1 57  ? 25.701 12.670 17.846 0.387 12.08  ? 56  LEU A CD2  1 
ATOM   1049 C CD2  C LEU A 1 57  ? 26.141 12.197 17.354 0.613 11.89  ? 56  LEU A CD2  1 
ATOM   1050 H H    A LEU A 1 57  ? 26.677 16.947 17.531 0.387 64.55  ? 56  LEU A H    1 
ATOM   1051 H H    C LEU A 1 57  ? 26.645 16.871 17.491 0.613 163.24 ? 56  LEU A H    1 
ATOM   1052 D DA   A LEU A 1 57  ? 27.718 14.208 16.936 0.387 9.18   ? 56  LEU A DA   1 
ATOM   1053 D DA   C LEU A 1 57  ? 27.878 14.192 17.032 0.613 8.91   ? 56  LEU A DA   1 
ATOM   1054 D DB2  A LEU A 1 57  ? 25.155 15.621 16.100 0.387 10.21  ? 56  LEU A DB2  1 
ATOM   1055 D DB2  C LEU A 1 57  ? 25.185 15.368 16.332 0.613 12.26  ? 56  LEU A DB2  1 
ATOM   1056 D DB3  A LEU A 1 57  ? 25.686 14.081 15.435 0.387 11.88  ? 56  LEU A DB3  1 
ATOM   1057 D DB3  C LEU A 1 57  ? 25.844 14.013 15.394 0.613 12.61  ? 56  LEU A DB3  1 
ATOM   1058 D DG   A LEU A 1 57  ? 25.025 14.632 18.343 0.387 11.41  ? 56  LEU A DG   1 
ATOM   1059 D DG   C LEU A 1 57  ? 25.590 13.954 18.406 0.613 11.69  ? 56  LEU A DG   1 
ATOM   1060 D DD11 A LEU A 1 57  ? 23.542 13.035 16.268 0.387 16.27  ? 56  LEU A DD11 1 
ATOM   1061 D DD11 C LEU A 1 57  ? 23.708 12.866 16.299 0.613 17.55  ? 56  LEU A DD11 1 
ATOM   1062 D DD12 A LEU A 1 57  ? 23.061 13.266 17.917 0.387 14.98  ? 56  LEU A DD12 1 
ATOM   1063 D DD12 C LEU A 1 57  ? 23.573 12.511 17.989 0.613 16.61  ? 56  LEU A DD12 1 
ATOM   1064 D DD13 A LEU A 1 57  ? 23.109 14.611 16.784 0.387 14.05  ? 56  LEU A DD13 1 
ATOM   1065 D DD13 C LEU A 1 57  ? 23.340 14.142 17.345 0.613 16.36  ? 56  LEU A DD13 1 
ATOM   1066 D DD21 A LEU A 1 57  ? 25.830 12.087 16.961 0.387 17.45  ? 56  LEU A DD21 1 
ATOM   1067 D DD21 C LEU A 1 57  ? 25.908 11.741 16.411 0.613 15.97  ? 56  LEU A DD21 1 
ATOM   1068 D DD22 A LEU A 1 57  ? 26.632 12.864 18.301 0.387 13.26  ? 56  LEU A DD22 1 
ATOM   1069 D DD22 C LEU A 1 57  ? 27.170 12.368 17.430 0.613 15.24  ? 56  LEU A DD22 1 
ATOM   1070 D DD23 A LEU A 1 57  ? 25.075 12.111 18.494 0.387 16.02  ? 56  LEU A DD23 1 
ATOM   1071 D DD23 C LEU A 1 57  ? 25.823 11.572 18.146 0.613 15.29  ? 56  LEU A DD23 1 
ATOM   1072 N N    . GLN A 1 58  ? 28.648 16.620 15.322 1.000 7.61   ? 57  GLN A N    1 
ATOM   1073 C CA   . GLN A 1 58  ? 29.499 17.018 14.197 1.000 7.63   ? 57  GLN A CA   1 
ATOM   1074 C C    . GLN A 1 58  ? 28.769 16.947 12.861 1.000 7.90   ? 57  GLN A C    1 
ATOM   1075 O O    . GLN A 1 58  ? 29.204 16.334 11.878 1.000 10.32  ? 57  GLN A O    1 
ATOM   1076 C CB   . GLN A 1 58  ? 30.781 16.196 14.173 1.000 8.30   ? 57  GLN A CB   1 
ATOM   1077 C CG   . GLN A 1 58  ? 31.708 16.513 15.335 1.000 9.09   ? 57  GLN A CG   1 
ATOM   1078 C CD   . GLN A 1 58  ? 32.316 17.906 15.179 1.000 9.31   ? 57  GLN A CD   1 
ATOM   1079 O OE1  . GLN A 1 58  ? 33.314 18.035 14.438 1.000 11.56  ? 57  GLN A OE1  1 
ATOM   1080 N NE2  . GLN A 1 58  ? 31.730 18.935 15.774 1.000 10.17  ? 57  GLN A NE2  1 
ATOM   1081 H H    A GLN A 1 58  ? 28.660 17.187 16.158 1.000 12.95  ? 57  GLN A H    1 
ATOM   1082 D DA   . GLN A 1 58  ? 29.739 18.074 14.373 1.000 8.27   ? 57  GLN A DA   1 
ATOM   1083 D DB2  . GLN A 1 58  ? 30.502 15.136 14.238 1.000 10.50  ? 57  GLN A DB2  1 
ATOM   1084 D DB3  . GLN A 1 58  ? 31.312 16.361 13.244 1.000 9.63   ? 57  GLN A DB3  1 
ATOM   1085 D DG2  . GLN A 1 58  ? 31.148 16.475 16.270 1.000 11.47  ? 57  GLN A DG2  1 
ATOM   1086 D DG3  . GLN A 1 58  ? 32.512 15.790 15.371 1.000 11.44  ? 57  GLN A DG3  1 
ATOM   1087 D DE21 . GLN A 1 58  ? 32.075 19.884 15.630 1.000 13.16  ? 57  GLN A DE21 1 
ATOM   1088 D DE22 . GLN A 1 58  ? 30.966 18.836 16.428 1.000 11.09  ? 57  GLN A DE22 1 
ATOM   1089 N N    . ILE A 1 59  ? 27.624 17.638 12.829 1.000 7.92   ? 58  ILE A N    1 
ATOM   1090 C CA   . ILE A 1 59  ? 26.778 17.658 11.646 1.000 8.12   ? 58  ILE A CA   1 
ATOM   1091 C C    . ILE A 1 59  ? 27.334 18.701 10.668 1.000 8.19   ? 58  ILE A C    1 
ATOM   1092 O O    . ILE A 1 59  ? 27.693 19.824 11.024 1.000 9.28   ? 58  ILE A O    1 
ATOM   1093 C CB   . ILE A 1 59  ? 25.340 17.931 12.078 1.000 8.92   ? 58  ILE A CB   1 
ATOM   1094 C CG1  . ILE A 1 59  ? 24.799 16.729 12.824 1.000 10.94  ? 58  ILE A CG1  1 
ATOM   1095 C CG2  . ILE A 1 59  ? 24.464 18.310 10.888 1.000 11.11  ? 58  ILE A CG2  1 
ATOM   1096 C CD1  . ILE A 1 59  ? 23.492 16.930 13.516 1.000 12.82  ? 58  ILE A CD1  1 
ATOM   1097 H H    . ILE A 1 59  ? 27.340 18.159 13.646 1.000 12.93  ? 58  ILE A H    1 
ATOM   1098 D DA   . ILE A 1 59  ? 26.829 16.690 11.165 1.000 9.29   ? 58  ILE A DA   1 
ATOM   1099 D DB   . ILE A 1 59  ? 25.373 18.802 12.760 1.000 10.74  ? 58  ILE A DB   1 
ATOM   1100 D DG12 . ILE A 1 59  ? 24.710 15.895 12.117 1.000 15.17  ? 58  ILE A DG12 1 
ATOM   1101 D DG13 . ILE A 1 59  ? 25.553 16.384 13.529 1.000 14.58  ? 58  ILE A DG13 1 
ATOM   1102 D DG21 . ILE A 1 59  ? 24.461 17.521 10.162 1.000 14.26  ? 58  ILE A DG21 1 
ATOM   1103 D DG22 . ILE A 1 59  ? 23.481 18.548 11.209 1.000 14.57  ? 58  ILE A DG22 1 
ATOM   1104 D DG23 . ILE A 1 59  ? 24.818 19.193 10.396 1.000 13.04  ? 58  ILE A DG23 1 
ATOM   1105 D DD11 . ILE A 1 59  ? 23.550 17.706 14.215 1.000 19.42  ? 58  ILE A DD11 1 
ATOM   1106 D DD12 . ILE A 1 59  ? 22.715 17.113 12.809 1.000 18.64  ? 58  ILE A DD12 1 
ATOM   1107 D DD13 . ILE A 1 59  ? 23.164 16.041 14.000 1.000 17.59  ? 58  ILE A DD13 1 
ATOM   1108 N N    . ASN A 1 60  ? 27.418 18.290 9.400  1.000 8.71   ? 59  ASN A N    1 
ATOM   1109 C CA   . ASN A 1 60  ? 28.130 19.058 8.394  1.000 8.82   ? 59  ASN A CA   1 
ATOM   1110 C C    . ASN A 1 60  ? 27.230 20.087 7.665  1.000 8.49   ? 59  ASN A C    1 
ATOM   1111 O O    . ASN A 1 60  ? 26.095 19.817 7.367  1.000 10.55  ? 59  ASN A O    1 
ATOM   1112 C CB   . ASN A 1 60  ? 28.741 18.069 7.395  1.000 10.10  ? 59  ASN A CB   1 
ATOM   1113 C CG   . ASN A 1 60  ? 29.601 18.717 6.343  1.000 10.59  ? 59  ASN A CG   1 
ATOM   1114 O OD1  . ASN A 1 60  ? 29.137 18.935 5.225  1.000 11.35  ? 59  ASN A OD1  1 
ATOM   1115 N ND2  . ASN A 1 60  ? 30.841 18.989 6.685  1.000 12.31  ? 59  ASN A ND2  1 
ATOM   1116 H H    A ASN A 1 60  ? 26.974 17.422 9.134  0.725 25.04  ? 59  ASN A H    1 
ATOM   1117 D D    B ASN A 1 60  ? 27.160 17.336 9.179  0.275 8.56   ? 59  ASN A D    1 
ATOM   1118 D DA   . ASN A 1 60  ? 28.919 19.628 8.913  1.000 9.87   ? 59  ASN A DA   1 
ATOM   1119 D DB2  . ASN A 1 60  ? 29.340 17.343 7.956  1.000 12.15  ? 59  ASN A DB2  1 
ATOM   1120 D DB3  . ASN A 1 60  ? 27.932 17.505 6.915  1.000 12.06  ? 59  ASN A DB3  1 
ATOM   1121 D DD21 . ASN A 1 60  ? 31.434 19.450 5.990  1.000 14.85  ? 59  ASN A DD21 1 
ATOM   1122 D DD22 . ASN A 1 60  ? 31.174 18.810 7.611  1.000 15.38  ? 59  ASN A DD22 1 
ATOM   1123 N N    . SER A 1 61  ? 27.859 21.214 7.354  1.000 8.63   ? 60  SER A N    1 
ATOM   1124 C CA   . SER A 1 61  ? 27.156 22.355 6.776  1.000 8.40   ? 60  SER A CA   1 
ATOM   1125 C C    . SER A 1 61  ? 26.932 22.274 5.267  1.000 9.15   ? 60  SER A C    1 
ATOM   1126 O O    . SER A 1 61  ? 26.245 23.173 4.747  1.000 11.38  ? 60  SER A O    1 
ATOM   1127 C CB   . SER A 1 61  ? 27.937 23.624 7.089  1.000 9.06   ? 60  SER A CB   1 
ATOM   1128 O OG   . SER A 1 61  ? 29.211 23.568 6.455  1.000 10.12  ? 60  SER A OG   1 
ATOM   1129 H H    . SER A 1 61  ? 28.853 21.283 7.523  1.000 12.87  ? 60  SER A H    1 
ATOM   1130 D DA   . SER A 1 61  ? 26.161 22.470 7.223  1.000 10.17  ? 60  SER A DA   1 
ATOM   1131 D DB2  . SER A 1 61  ? 27.345 24.466 6.755  1.000 11.46  ? 60  SER A DB2  1 
ATOM   1132 D DB3  . SER A 1 61  ? 28.087 23.669 8.162  1.000 11.11  ? 60  SER A DB3  1 
ATOM   1133 D DG   . SER A 1 61  ? 29.281 24.344 5.855  1.000 10.65  ? 60  SER A DG   1 
ATOM   1134 N N    . ARG A 1 62  ? 27.413 21.264 4.559  1.000 9.09   ? 61  ARG A N    1 
ATOM   1135 C CA   . ARG A 1 62  ? 27.099 21.224 3.139  1.000 9.50   ? 61  ARG A CA   1 
ATOM   1136 C C    . ARG A 1 62  ? 25.670 20.734 2.936  1.000 8.92   ? 61  ARG A C    1 
ATOM   1137 O O    . ARG A 1 62  ? 24.950 21.351 2.170  1.000 11.81  ? 61  ARG A O    1 
ATOM   1138 C CB   . ARG A 1 62  ? 28.116 20.385 2.381  1.000 11.32  ? 61  ARG A CB   1 
ATOM   1139 C CG   . ARG A 1 62  ? 27.914 20.486 0.880  1.000 15.84  ? 61  ARG A CG   1 
ATOM   1140 C CD   . ARG A 1 62  ? 28.899 19.653 0.094  1.000 21.36  ? 61  ARG A CD   1 
ATOM   1141 N NE   . ARG A 1 62  ? 30.280 19.778 0.468  1.000 25.37  ? 61  ARG A NE   1 
ATOM   1142 C CZ   . ARG A 1 62  ? 31.204 20.593 -0.019 1.000 29.32  ? 61  ARG A CZ   1 
ATOM   1143 N NH1  . ARG A 1 62  ? 30.934 21.369 -1.060 1.000 32.66  ? 61  ARG A NH1  1 
ATOM   1144 N NH2  . ARG A 1 62  ? 32.420 20.637 0.506  1.000 30.25  ? 61  ARG A NH2  1 
ATOM   1145 H H    . ARG A 1 62  ? 27.978 20.546 4.989  1.000 14.93  ? 61  ARG A H    1 
ATOM   1146 D DA   . ARG A 1 62  ? 27.120 22.243 2.747  1.000 10.93  ? 61  ARG A DA   1 
ATOM   1147 D DB2  . ARG A 1 62  ? 29.116 20.732 2.618  1.000 14.35  ? 61  ARG A DB2  1 
ATOM   1148 D DB3  . ARG A 1 62  ? 28.029 19.363 2.686  1.000 12.72  ? 61  ARG A DB3  1 
ATOM   1149 D DG2  . ARG A 1 62  ? 26.915 20.193 0.634  1.000 21.51  ? 61  ARG A DG2  1 
ATOM   1150 D DG3  . ARG A 1 62  ? 28.016 21.528 0.589  1.000 19.29  ? 61  ARG A DG3  1 
ATOM   1151 D DD2  . ARG A 1 62  ? 28.599 18.611 0.268  1.000 27.95  ? 61  ARG A DD2  1 
ATOM   1152 D DD3  . ARG A 1 62  ? 28.753 19.770 -0.981 1.000 30.50  ? 61  ARG A DD3  1 
ATOM   1153 D DE   . ARG A 1 62  ? 30.532 19.101 1.199  1.000 29.35  ? 61  ARG A DE   1 
ATOM   1154 D DH11 . ARG A 1 62  ? 30.008 21.318 -1.481 1.000 34.07  ? 61  ARG A DH11 1 
ATOM   1155 D DH12 . ARG A 1 62  ? 31.671 21.974 -1.420 1.000 41.66  ? 61  ARG A DH12 1 
ATOM   1156 D DH21 . ARG A 1 62  ? 32.869 21.527 0.662  1.000 50.37  ? 61  ARG A DH21 1 
ATOM   1157 D DH22 . ARG A 1 62  ? 32.888 19.778 0.750  1.000 51.77  ? 61  ARG A DH22 1 
ATOM   1158 N N    . TRP A 1 63  ? 25.262 19.623 3.539  1.000 9.65   ? 62  TRP A N    1 
ATOM   1159 C CA   . TRP A 1 63  ? 23.914 19.159 3.286  1.000 10.27  ? 62  TRP A CA   1 
ATOM   1160 C C    . TRP A 1 63  ? 22.954 19.552 4.414  1.000 9.17   ? 62  TRP A C    1 
ATOM   1161 O O    . TRP A 1 63  ? 21.779 19.649 4.061  1.000 9.82   ? 62  TRP A O    1 
ATOM   1162 C CB   . TRP A 1 63  ? 23.751 17.649 3.120  1.000 11.83  ? 62  TRP A CB   1 
ATOM   1163 C CG   . TRP A 1 63  ? 24.304 17.116 1.840  1.000 14.32  ? 62  TRP A CG   1 
ATOM   1164 C CD1  . TRP A 1 63  ? 25.006 17.771 0.867  1.000 14.28  ? 62  TRP A CD1  1 
ATOM   1165 C CD2  . TRP A 1 63  ? 24.162 15.774 1.388  1.000 15.64  ? 62  TRP A CD2  1 
ATOM   1166 N NE1  . TRP A 1 63  ? 25.340 16.909 -0.154 1.000 16.84  ? 62  TRP A NE1  1 
ATOM   1167 C CE2  . TRP A 1 63  ? 24.822 15.691 0.142  1.000 17.84  ? 62  TRP A CE2  1 
ATOM   1168 C CE3  . TRP A 1 63  ? 23.531 14.654 1.932  1.000 18.70  ? 62  TRP A CE3  1 
ATOM   1169 C CZ2  . TRP A 1 63  ? 24.886 14.512 -0.590 1.000 21.92  ? 62  TRP A CZ2  1 
ATOM   1170 C CZ3  . TRP A 1 63  ? 23.600 13.487 1.211  1.000 22.68  ? 62  TRP A CZ3  1 
ATOM   1171 C CH2  . TRP A 1 63  ? 24.266 13.425 -0.025 1.000 23.53  ? 62  TRP A CH2  1 
ATOM   1172 D D    . TRP A 1 63  ? 25.876 19.097 4.069  1.000 14.30  ? 62  TRP A D    1 
ATOM   1173 D DA   . TRP A 1 63  ? 23.558 19.643 2.376  1.000 11.69  ? 62  TRP A DA   1 
ATOM   1174 D DB2  . TRP A 1 63  ? 24.211 17.208 3.992  1.000 13.11  ? 62  TRP A DB2  1 
ATOM   1175 D DB3  . TRP A 1 63  ? 22.705 17.334 3.151  1.000 15.58  ? 62  TRP A DB3  1 
ATOM   1176 D DD1  . TRP A 1 63  ? 25.203 18.847 0.794  1.000 19.10  ? 62  TRP A DD1  1 
ATOM   1177 D DE1  . TRP A 1 63  ? 25.871 17.178 -0.973 1.000 22.73  ? 62  TRP A DE1  1 
ATOM   1178 D DE3  . TRP A 1 63  ? 22.955 14.738 2.832  1.000 24.89  ? 62  TRP A DE3  1 
ATOM   1179 D DZ2  . TRP A 1 63  ? 25.393 14.471 -1.527 1.000 26.79  ? 62  TRP A DZ2  1 
ATOM   1180 D DZ3  . TRP A 1 63  ? 23.113 12.582 1.569  1.000 30.30  ? 62  TRP A DZ3  1 
ATOM   1181 D DH2  . TRP A 1 63  ? 24.294 12.463 -0.526 1.000 39.05  ? 62  TRP A DH2  1 
ATOM   1182 N N    . TRP A 1 64  ? 23.362 19.755 5.677  1.000 8.30   ? 63  TRP A N    1 
ATOM   1183 C CA   . TRP A 1 64  ? 22.388 19.627 6.763  1.000 8.30   ? 63  TRP A CA   1 
ATOM   1184 C C    . TRP A 1 64  ? 21.966 20.932 7.403  1.000 8.11   ? 63  TRP A C    1 
ATOM   1185 O O    . TRP A 1 64  ? 20.805 21.073 7.746  1.000 10.29  ? 63  TRP A O    1 
ATOM   1186 C CB   . TRP A 1 64  ? 22.888 18.619 7.827  1.000 8.69   ? 63  TRP A CB   1 
ATOM   1187 C CG   . TRP A 1 64  ? 23.162 17.306 7.152  1.000 9.94   ? 63  TRP A CG   1 
ATOM   1188 C CD1  . TRP A 1 64  ? 24.380 16.738 6.960  1.000 12.11  ? 63  TRP A CD1  1 
ATOM   1189 C CD2  . TRP A 1 64  ? 22.188 16.419 6.572  1.000 10.44  ? 63  TRP A CD2  1 
ATOM   1190 N NE1  . TRP A 1 64  ? 24.224 15.532 6.287  1.000 13.66  ? 63  TRP A NE1  1 
ATOM   1191 C CE2  . TRP A 1 64  ? 22.902 15.344 6.048  1.000 11.57  ? 63  TRP A CE2  1 
ATOM   1192 C CE3  . TRP A 1 64  ? 20.807 16.452 6.450  1.000 10.78  ? 63  TRP A CE3  1 
ATOM   1193 C CZ2  . TRP A 1 64  ? 22.274 14.282 5.406  1.000 14.50  ? 63  TRP A CZ2  1 
ATOM   1194 C CZ3  . TRP A 1 64  ? 20.178 15.392 5.802  1.000 12.70  ? 63  TRP A CZ3  1 
ATOM   1195 C CH2  . TRP A 1 64  ? 20.911 14.320 5.286  1.000 15.00  ? 63  TRP A CH2  1 
ATOM   1196 H H    . TRP A 1 64  ? 24.323 19.992 5.875  1.000 19.36  ? 63  TRP A H    1 
ATOM   1197 D DA   . TRP A 1 64  ? 21.455 19.225 6.331  1.000 9.13   ? 63  TRP A DA   1 
ATOM   1198 D DB2  . TRP A 1 64  ? 23.807 19.030 8.228  1.000 11.38  ? 63  TRP A DB2  1 
ATOM   1199 D DB3  . TRP A 1 64  ? 22.121 18.521 8.571  1.000 10.87  ? 63  TRP A DB3  1 
ATOM   1200 D DD1  . TRP A 1 64  ? 25.359 17.102 7.244  1.000 16.47  ? 63  TRP A DD1  1 
ATOM   1201 D DE1  . TRP A 1 64  ? 24.996 14.934 6.015  1.000 19.06  ? 63  TRP A DE1  1 
ATOM   1202 D DE3  . TRP A 1 64  ? 20.221 17.238 6.880  1.000 11.72  ? 63  TRP A DE3  1 
ATOM   1203 D DZ2  . TRP A 1 64  ? 22.851 13.441 5.058  1.000 18.34  ? 63  TRP A DZ2  1 
ATOM   1204 D DZ3  . TRP A 1 64  ? 19.099 15.371 5.738  1.000 15.90  ? 63  TRP A DZ3  1 
ATOM   1205 D DH2  . TRP A 1 64  ? 20.376 13.543 4.756  1.000 20.45  ? 63  TRP A DH2  1 
ATOM   1206 N N    . CYS A 1 65  ? 22.878 21.847 7.655  1.000 10.01  ? 64  CYS A N    1 
ATOM   1207 C CA   . CYS A 1 65  ? 22.528 23.105 8.329  1.000 9.76   ? 64  CYS A CA   1 
ATOM   1208 C C    . CYS A 1 65  ? 23.112 24.259 7.520  1.000 9.92   ? 64  CYS A C    1 
ATOM   1209 O O    . CYS A 1 65  ? 24.024 24.061 6.746  1.000 10.59  ? 64  CYS A O    1 
ATOM   1210 C CB   . CYS A 1 65  ? 23.044 23.138 9.773  1.000 10.00  ? 64  CYS A CB   1 
ATOM   1211 S SG   . CYS A 1 65  ? 24.824 23.062 10.001 1.000 10.39  ? 64  CYS A SG   1 
ATOM   1212 H H    . CYS A 1 65  ? 23.835 21.682 7.379  1.000 27.74  ? 64  CYS A H    1 
ATOM   1213 D DA   . CYS A 1 65  ? 21.434 23.190 8.323  1.000 10.96  ? 64  CYS A DA   1 
ATOM   1214 D DB2  . CYS A 1 65  ? 22.670 24.037 10.233 1.000 10.40  ? 64  CYS A DB2  1 
ATOM   1215 D DB3  . CYS A 1 65  ? 22.643 22.288 10.326 1.000 12.28  ? 64  CYS A DB3  1 
ATOM   1216 N N    . ASN A 1 66  ? 22.584 25.466 7.726  1.000 9.89   ? 65  ASN A N    1 
ATOM   1217 C CA   . ASN A 1 66  ? 23.046 26.626 6.971  1.000 10.93  ? 65  ASN A CA   1 
ATOM   1218 C C    . ASN A 1 66  ? 23.987 27.472 7.823  1.000 9.70   ? 65  ASN A C    1 
ATOM   1219 O O    . ASN A 1 66  ? 23.609 27.959 8.905  1.000 10.64  ? 65  ASN A O    1 
ATOM   1220 C CB   . ASN A 1 66  ? 21.839 27.458 6.552  1.000 13.95  ? 65  ASN A CB   1 
ATOM   1221 C CG   . ASN A 1 66  ? 22.265 28.640 5.725  1.000 19.39  ? 65  ASN A CG   1 
ATOM   1222 O OD1  . ASN A 1 66  ? 23.262 28.632 5.004  1.000 19.32  ? 65  ASN A OD1  1 
ATOM   1223 N ND2  . ASN A 1 66  ? 21.477 29.689 5.850  1.000 30.30  ? 65  ASN A ND2  1 
ATOM   1224 H H    . ASN A 1 66  ? 21.854 25.578 8.415  1.000 17.88  ? 65  ASN A H    1 
ATOM   1225 D DA   . ASN A 1 66  ? 23.601 26.263 6.107  1.000 12.43  ? 65  ASN A DA   1 
ATOM   1226 D DB2  . ASN A 1 66  ? 21.139 26.835 5.997  1.000 19.01  ? 65  ASN A DB2  1 
ATOM   1227 D DB3  . ASN A 1 66  ? 21.326 27.797 7.467  1.000 17.16  ? 65  ASN A DB3  1 
ATOM   1228 D DD21 . ASN A 1 66  ? 21.729 30.545 5.370  1.000 40.70  ? 65  ASN A DD21 1 
ATOM   1229 D DD22 . ASN A 1 66  ? 20.654 29.601 6.437  1.000 38.66  ? 65  ASN A DD22 1 
ATOM   1230 N N    . ASP A 1 67  ? 25.200 27.634 7.353  1.000 9.92   ? 66  ASP A N    1 
ATOM   1231 C CA   . ASP A 1 67  ? 26.118 28.595 7.977  1.000 10.54  ? 66  ASP A CA   1 
ATOM   1232 C C    . ASP A 1 67  ? 26.437 29.760 7.041  1.000 12.16  ? 66  ASP A C    1 
ATOM   1233 O O    . ASP A 1 67  ? 27.216 30.641 7.415  1.000 13.30  ? 66  ASP A O    1 
ATOM   1234 C CB   . ASP A 1 67  ? 27.409 27.972 8.488  1.000 10.29  ? 66  ASP A CB   1 
ATOM   1235 C CG   . ASP A 1 67  ? 28.380 27.412 7.465  1.000 9.31   ? 66  ASP A CG   1 
ATOM   1236 O OD1  . ASP A 1 67  ? 28.169 27.651 6.277  1.000 11.52  ? 66  ASP A OD1  1 
ATOM   1237 O OD2  . ASP A 1 67  ? 29.324 26.741 7.945  1.000 10.50  ? 66  ASP A OD2  1 
ATOM   1238 D D    . ASP A 1 67  ? 25.536 27.103 6.542  1.000 11.70  ? 66  ASP A D    1 
ATOM   1239 D DA   . ASP A 1 67  ? 25.581 29.042 8.826  1.000 12.02  ? 66  ASP A DA   1 
ATOM   1240 D DB2  . ASP A 1 67  ? 27.915 28.705 9.101  1.000 12.19  ? 66  ASP A DB2  1 
ATOM   1241 D DB3  . ASP A 1 67  ? 27.164 27.161 9.166  1.000 11.62  ? 66  ASP A DB3  1 
ATOM   1242 N N    . GLY A 1 68  ? 25.826 29.832 5.878  1.000 12.76  ? 67  GLY A N    1 
ATOM   1243 C CA   . GLY A 1 68  ? 25.991 30.914 4.935  1.000 15.89  ? 67  GLY A CA   1 
ATOM   1244 C C    . GLY A 1 68  ? 27.289 31.016 4.194  1.000 16.98  ? 67  GLY A C    1 
ATOM   1245 O O    . GLY A 1 68  ? 27.460 31.905 3.349  1.000 25.06  ? 67  GLY A O    1 
ATOM   1246 D D    . GLY A 1 68  ? 25.130 29.135 5.672  1.000 14.25  ? 67  GLY A D    1 
ATOM   1247 D DA2  . GLY A 1 68  ? 25.201 30.856 4.172  1.000 20.39  ? 67  GLY A DA2  1 
ATOM   1248 D DA3  . GLY A 1 68  ? 25.867 31.830 5.513  1.000 18.23  ? 67  GLY A DA3  1 
ATOM   1249 N N    A ARG A 1 69  ? 28.241 30.164 4.535  0.506 15.55  ? 68  ARG A N    1 
ATOM   1250 N N    B ARG A 1 69  ? 28.215 30.118 4.419  0.494 14.59  ? 68  ARG A N    1 
ATOM   1251 C CA   A ARG A 1 69  ? 29.608 30.171 4.016  0.506 16.54  ? 68  ARG A CA   1 
ATOM   1252 C CA   B ARG A 1 69  ? 29.522 30.235 3.784  0.494 16.04  ? 68  ARG A CA   1 
ATOM   1253 C C    A ARG A 1 69  ? 29.866 29.001 3.070  0.506 15.07  ? 68  ARG A C    1 
ATOM   1254 C C    B ARG A 1 69  ? 29.980 28.907 3.198  0.494 15.12  ? 68  ARG A C    1 
ATOM   1255 O O    A ARG A 1 69  ? 30.794 29.055 2.274  0.506 15.70  ? 68  ARG A O    1 
ATOM   1256 O O    B ARG A 1 69  ? 31.156 28.770 2.864  0.494 15.11  ? 68  ARG A O    1 
ATOM   1257 C CB   A ARG A 1 69  ? 30.620 30.169 5.174  0.506 18.78  ? 68  ARG A CB   1 
ATOM   1258 C CB   B ARG A 1 69  ? 30.526 30.730 4.823  0.494 17.62  ? 68  ARG A CB   1 
ATOM   1259 C CG   A ARG A 1 69  ? 30.536 31.430 6.014  0.506 21.03  ? 68  ARG A CG   1 
ATOM   1260 C CG   B ARG A 1 69  ? 30.160 32.070 5.414  0.494 20.19  ? 68  ARG A CG   1 
ATOM   1261 C CD   A ARG A 1 69  ? 31.610 31.574 7.069  0.506 22.20  ? 68  ARG A CD   1 
ATOM   1262 C CD   B ARG A 1 69  ? 31.158 32.485 6.475  0.494 22.07  ? 68  ARG A CD   1 
ATOM   1263 N NE   A ARG A 1 69  ? 31.540 30.606 8.149  0.506 22.09  ? 68  ARG A NE   1 
ATOM   1264 N NE   B ARG A 1 69  ? 31.244 31.551 7.593  0.494 21.48  ? 68  ARG A NE   1 
ATOM   1265 C CZ   A ARG A 1 69  ? 30.689 30.586 9.172  0.506 22.04  ? 68  ARG A CZ   1 
ATOM   1266 C CZ   B ARG A 1 69  ? 32.037 30.499 7.695  0.494 22.01  ? 68  ARG A CZ   1 
ATOM   1267 N NH1  A ARG A 1 69  ? 29.729 31.494 9.262  0.506 23.53  ? 68  ARG A NH1  1 
ATOM   1268 N NH1  B ARG A 1 69  ? 33.024 30.302 6.842  0.494 23.34  ? 68  ARG A NH1  1 
ATOM   1269 N NH2  A ARG A 1 69  ? 30.820 29.627 10.070 0.506 24.56  ? 68  ARG A NH2  1 
ATOM   1270 N NH2  B ARG A 1 69  ? 31.860 29.615 8.670  0.494 23.45  ? 68  ARG A NH2  1 
ATOM   1271 D D    A ARG A 1 69  ? 28.023 29.459 5.246  0.506 14.79  ? 68  ARG A D    1 
ATOM   1272 D D    B ARG A 1 69  ? 28.000 29.363 5.061  0.494 15.74  ? 68  ARG A D    1 
ATOM   1273 D DA   A ARG A 1 69  ? 29.742 31.125 3.480  0.506 18.70  ? 68  ARG A DA   1 
ATOM   1274 D DA   B ARG A 1 69  ? 29.422 31.013 2.996  0.494 17.43  ? 68  ARG A DA   1 
ATOM   1275 D DB2  A ARG A 1 69  ? 30.417 29.312 5.803  0.506 18.44  ? 68  ARG A DB2  1 
ATOM   1276 D DB2  B ARG A 1 69  ? 30.569 29.992 5.632  0.494 17.80  ? 68  ARG A DB2  1 
ATOM   1277 D DB3  A ARG A 1 69  ? 31.614 30.093 4.740  0.506 21.23  ? 68  ARG A DB3  1 
ATOM   1278 D DB3  B ARG A 1 69  ? 31.500 30.793 4.351  0.494 18.65  ? 68  ARG A DB3  1 
ATOM   1279 D DG2  A ARG A 1 69  ? 30.588 32.288 5.341  0.506 23.66  ? 68  ARG A DG2  1 
ATOM   1280 D DG2  B ARG A 1 69  ? 30.148 32.816 4.625  0.494 22.48  ? 68  ARG A DG2  1 
ATOM   1281 D DG3  A ARG A 1 69  ? 29.559 31.447 6.506  0.506 21.06  ? 68  ARG A DG3  1 
ATOM   1282 D DG3  B ARG A 1 69  ? 29.174 32.016 5.853  0.494 20.80  ? 68  ARG A DG3  1 
ATOM   1283 D DD2  A ARG A 1 69  ? 32.592 31.515 6.600  0.506 23.60  ? 68  ARG A DD2  1 
ATOM   1284 D DD2  B ARG A 1 69  ? 32.116 32.549 5.950  0.494 22.44  ? 68  ARG A DD2  1 
ATOM   1285 D DD3  A ARG A 1 69  ? 31.515 32.580 7.510  0.506 23.88  ? 68  ARG A DD3  1 
ATOM   1286 D DD3  B ARG A 1 69  ? 30.893 33.472 6.861  0.494 25.54  ? 68  ARG A DD3  1 
ATOM   1287 D DE   A ARG A 1 69  ? 32.251 29.894 8.044  0.506 27.22  ? 68  ARG A DE   1 
ATOM   1288 D DE   B ARG A 1 69  ? 30.596 31.812 8.322  0.494 25.02  ? 68  ARG A DE   1 
ATOM   1289 D DH11 A ARG A 1 69  ? 28.876 31.274 9.762  0.506 26.54  ? 68  ARG A DH11 1 
ATOM   1290 D DH11 B ARG A 1 69  ? 33.619 29.487 6.943  0.494 30.82  ? 68  ARG A DH11 1 
ATOM   1291 D DH12 A ARG A 1 69  ? 29.835 32.374 8.759  0.506 21.73  ? 68  ARG A DH12 1 
ATOM   1292 D DH12 B ARG A 1 69  ? 33.175 30.952 6.082  0.494 26.88  ? 68  ARG A DH12 1 
ATOM   1293 D DH21 A ARG A 1 69  ? 30.424 29.725 10.997 0.506 23.32  ? 68  ARG A DH21 1 
ATOM   1294 D DH21 B ARG A 1 69  ? 31.071 29.721 9.295  0.494 23.47  ? 68  ARG A DH21 1 
ATOM   1295 D DH22 A ARG A 1 69  ? 31.309 28.769 9.809  0.506 32.33  ? 68  ARG A DH22 1 
ATOM   1296 D DH22 B ARG A 1 69  ? 32.501 28.851 8.782  0.494 27.28  ? 68  ARG A DH22 1 
ATOM   1297 N N    . THR A 1 70  ? 29.078 27.930 3.105  1.000 13.14  ? 69  THR A N    1 
ATOM   1298 C CA   . THR A 1 70  ? 29.440 26.648 2.570  1.000 12.09  ? 69  THR A CA   1 
ATOM   1299 C C    . THR A 1 70  ? 28.945 26.507 1.144  1.000 11.61  ? 69  THR A C    1 
ATOM   1300 O O    . THR A 1 70  ? 27.736 26.681 0.870  1.000 13.33  ? 69  THR A O    1 
ATOM   1301 C CB   . THR A 1 70  ? 28.864 25.520 3.448  1.000 10.84  ? 69  THR A CB   1 
ATOM   1302 O OG1  . THR A 1 70  ? 29.368 25.642 4.782  1.000 10.53  ? 69  THR A OG1  1 
ATOM   1303 C CG2  . THR A 1 70  ? 29.298 24.162 2.925  1.000 11.58  ? 69  THR A CG2  1 
ATOM   1304 D D    . THR A 1 70  ? 28.182 28.069 3.508  1.000 16.49  ? 69  THR A D    1 
ATOM   1305 D DA   . THR A 1 70  ? 30.540 26.525 2.601  1.000 12.98  ? 69  THR A DA   1 
ATOM   1306 D DB   . THR A 1 70  ? 27.783 25.589 3.443  1.000 12.73  ? 69  THR A DB   1 
ATOM   1307 D DG1  . THR A 1 70  ? 29.005 26.425 5.229  1.000 12.04  ? 69  THR A DG1  1 
ATOM   1308 D DG21 . THR A 1 70  ? 30.357 24.116 2.862  1.000 13.86  ? 69  THR A DG21 1 
ATOM   1309 D DG22 . THR A 1 70  ? 28.998 23.407 3.610  1.000 13.20  ? 69  THR A DG22 1 
ATOM   1310 D DG23 . THR A 1 70  ? 28.902 24.005 1.948  1.000 15.31  ? 69  THR A DG23 1 
ATOM   1311 N N    . PRO A 1 71  ? 29.795 26.189 0.174  1.000 12.36  ? 70  PRO A N    1 
ATOM   1312 C CA   . PRO A 1 71  ? 29.293 25.962 -1.184 1.000 13.87  ? 70  PRO A CA   1 
ATOM   1313 C C    . PRO A 1 71  ? 28.347 24.758 -1.233 1.000 15.09  ? 70  PRO A C    1 
ATOM   1314 O O    . PRO A 1 71  ? 28.513 23.765 -0.548 1.000 17.07  ? 70  PRO A O    1 
ATOM   1315 C CB   . PRO A 1 71  ? 30.544 25.688 -2.022 1.000 17.50  ? 70  PRO A CB   1 
ATOM   1316 C CG   . PRO A 1 71  ? 31.663 26.242 -1.195 1.000 18.72  ? 70  PRO A CG   1 
ATOM   1317 C CD   . PRO A 1 71  ? 31.259 26.052 0.238  1.000 15.59  ? 70  PRO A CD   1 
ATOM   1318 D DA   . PRO A 1 71  ? 28.798 26.867 -1.543 1.000 15.08  ? 70  PRO A DA   1 
ATOM   1319 D DB2  . PRO A 1 71  ? 30.663 24.620 -2.212 1.000 21.75  ? 70  PRO A DB2  1 
ATOM   1320 D DB3  . PRO A 1 71  ? 30.463 26.165 -2.999 1.000 21.67  ? 70  PRO A DB3  1 
ATOM   1321 D DG2  . PRO A 1 71  ? 32.579 25.680 -1.403 1.000 23.03  ? 70  PRO A DG2  1 
ATOM   1322 D DG3  . PRO A 1 71  ? 31.796 27.301 -1.417 1.000 20.96  ? 70  PRO A DG3  1 
ATOM   1323 D DD2  . PRO A 1 71  ? 31.542 25.077 0.615  1.000 20.54  ? 70  PRO A DD2  1 
ATOM   1324 D DD3  . PRO A 1 71  ? 31.681 26.792 0.909  1.000 18.78  ? 70  PRO A DD3  1 
ATOM   1325 N N    . GLY A 1 72  ? 27.367 24.885 -2.122 1.000 15.29  ? 71  GLY A N    1 
ATOM   1326 C CA   . GLY A 1 72  ? 26.456 23.784 -2.390 1.000 16.74  ? 71  GLY A CA   1 
ATOM   1327 C C    . GLY A 1 72  ? 25.460 23.499 -1.281 1.000 15.30  ? 71  GLY A C    1 
ATOM   1328 O O    . GLY A 1 72  ? 24.884 22.429 -1.192 1.000 16.52  ? 71  GLY A O    1 
ATOM   1329 D D    . GLY A 1 72  ? 27.276 25.761 -2.610 1.000 20.20  ? 71  GLY A D    1 
ATOM   1330 D DA2  . GLY A 1 72  ? 25.932 23.987 -3.299 1.000 22.50  ? 71  GLY A DA2  1 
ATOM   1331 D DA3  . GLY A 1 72  ? 27.042 22.870 -2.458 1.000 20.60  ? 71  GLY A DA3  1 
ATOM   1332 N N    . SER A 1 73  ? 25.237 24.432 -0.394 1.000 13.92  ? 72  SER A N    1 
ATOM   1333 C CA   . SER A 1 73  ? 24.410 24.206 0.774  1.000 12.66  ? 72  SER A CA   1 
ATOM   1334 C C    . SER A 1 73  ? 22.988 23.758 0.427  1.000 11.50  ? 72  SER A C    1 
ATOM   1335 O O    . SER A 1 73  ? 22.326 24.383 -0.404 1.000 15.73  ? 72  SER A O    1 
ATOM   1336 C CB   . SER A 1 73  ? 24.399 25.504 1.592  1.000 16.78  ? 72  SER A CB   1 
ATOM   1337 O OG   . SER A 1 73  ? 23.434 25.463 2.607  1.000 18.29  ? 72  SER A OG   1 
ATOM   1338 D D    . SER A 1 73  ? 25.717 25.344 -0.462 1.000 18.48  ? 72  SER A D    1 
ATOM   1339 D DA   . SER A 1 73  ? 24.884 23.376 1.328  1.000 14.96  ? 72  SER A DA   1 
ATOM   1340 D DB2  . SER A 1 73  ? 25.415 25.757 1.939  1.000 19.48  ? 72  SER A DB2  1 
ATOM   1341 D DB3  . SER A 1 73  ? 24.029 26.303 0.916  1.000 18.78  ? 72  SER A DB3  1 
ATOM   1342 D DG   . SER A 1 73  ? 23.648 25.186 3.499  1.000 36.33  ? 72  SER A DG   1 
ATOM   1343 N N    . ARG A 1 74  ? 22.531 22.680 1.059  1.000 9.72   ? 73  ARG A N    1 
ATOM   1344 C CA   . ARG A 1 74  ? 21.170 22.206 0.921  1.000 10.08  ? 73  ARG A CA   1 
ATOM   1345 C C    . ARG A 1 74  ? 20.256 22.493 2.112  1.000 9.40   ? 73  ARG A C    1 
ATOM   1346 O O    . ARG A 1 74  ? 19.047 22.500 1.974  1.000 11.83  ? 73  ARG A O    1 
ATOM   1347 C CB   . ARG A 1 74  ? 21.178 20.684 0.682  1.000 10.55  ? 73  ARG A CB   1 
ATOM   1348 C CG   . ARG A 1 74  ? 21.992 20.270 -0.519 1.000 11.66  ? 73  ARG A CG   1 
ATOM   1349 C CD   . ARG A 1 74  ? 21.889 18.775 -0.778 1.000 13.58  ? 73  ARG A CD   1 
ATOM   1350 N NE   . ARG A 1 74  ? 22.756 18.414 -1.887 1.000 15.75  ? 73  ARG A NE   1 
ATOM   1351 C CZ   . ARG A 1 74  ? 22.808 17.234 -2.457 1.000 18.59  ? 73  ARG A CZ   1 
ATOM   1352 N NH1  . ARG A 1 74  ? 22.096 16.231 -1.938 1.000 21.10  ? 73  ARG A NH1  1 
ATOM   1353 N NH2  . ARG A 1 74  ? 23.607 17.028 -3.482 1.000 21.96  ? 73  ARG A NH2  1 
ATOM   1354 D D    . ARG A 1 74  ? 23.207 22.159 1.588  1.000 11.20  ? 73  ARG A D    1 
ATOM   1355 D DA   . ARG A 1 74  ? 20.703 22.684 0.045  1.000 11.83  ? 73  ARG A DA   1 
ATOM   1356 D DB2  . ARG A 1 74  ? 21.542 20.207 1.579  1.000 11.59  ? 73  ARG A DB2  1 
ATOM   1357 D DB3  . ARG A 1 74  ? 20.152 20.374 0.548  1.000 13.25  ? 73  ARG A DB3  1 
ATOM   1358 D DG2  . ARG A 1 74  ? 21.648 20.799 -1.393 1.000 16.07  ? 73  ARG A DG2  1 
ATOM   1359 D DG3  . ARG A 1 74  ? 23.030 20.518 -0.392 1.000 14.93  ? 73  ARG A DG3  1 
ATOM   1360 D DD2  . ARG A 1 74  ? 22.198 18.255 0.115  1.000 16.14  ? 73  ARG A DD2  1 
ATOM   1361 D DD3  . ARG A 1 74  ? 20.877 18.522 -1.043 1.000 16.65  ? 73  ARG A DD3  1 
ATOM   1362 D DE   . ARG A 1 74  ? 23.417 19.146 -2.096 1.000 16.74  ? 73  ARG A DE   1 
ATOM   1363 D DH11 . ARG A 1 74  ? 22.068 15.350 -2.422 1.000 25.84  ? 73  ARG A DH11 1 
ATOM   1364 D DH12 . ARG A 1 74  ? 21.713 16.358 -1.009 1.000 25.35  ? 73  ARG A DH12 1 
ATOM   1365 D DH21 . ARG A 1 74  ? 23.631 16.106 -3.921 1.000 28.87  ? 73  ARG A DH21 1 
ATOM   1366 D DH22 . ARG A 1 74  ? 24.228 17.773 -3.791 1.000 28.46  ? 73  ARG A DH22 1 
ATOM   1367 N N    . ASN A 1 75  ? 20.838 22.716 3.277  1.000 9.08   ? 74  ASN A N    1 
ATOM   1368 C CA   . ASN A 1 75  ? 20.111 22.968 4.517  1.000 9.23   ? 74  ASN A CA   1 
ATOM   1369 C C    . ASN A 1 75  ? 18.899 22.061 4.707  1.000 8.61   ? 74  ASN A C    1 
ATOM   1370 O O    . ASN A 1 75  ? 17.778 22.511 4.915  1.000 9.81   ? 74  ASN A O    1 
ATOM   1371 C CB   . ASN A 1 75  ? 19.726 24.452 4.577  1.000 11.04  ? 74  ASN A CB   1 
ATOM   1372 C CG   . ASN A 1 75  ? 19.228 24.825 5.962  1.000 10.78  ? 74  ASN A CG   1 
ATOM   1373 O OD1  . ASN A 1 75  ? 19.448 24.119 6.952  1.000 11.62  ? 74  ASN A OD1  1 
ATOM   1374 N ND2  . ASN A 1 75  ? 18.594 25.960 6.067  1.000 13.75  ? 74  ASN A ND2  1 
ATOM   1375 D D    . ASN A 1 75  ? 21.844 22.779 3.335  1.000 11.05  ? 74  ASN A D    1 
ATOM   1376 D DA   . ASN A 1 75  ? 20.810 22.776 5.339  1.000 9.33   ? 74  ASN A DA   1 
ATOM   1377 D DB2  . ASN A 1 75  ? 20.641 25.033 4.356  1.000 13.29  ? 74  ASN A DB2  1 
ATOM   1378 D DB3  . ASN A 1 75  ? 18.986 24.657 3.824  1.000 13.33  ? 74  ASN A DB3  1 
ATOM   1379 D DD21 . ASN A 1 75  ? 18.315 26.290 6.993  1.000 17.30  ? 74  ASN A DD21 1 
ATOM   1380 D DD22 . ASN A 1 75  ? 18.472 26.548 5.247  1.000 20.17  ? 74  ASN A DD22 1 
ATOM   1381 N N    . LEU A 1 76  ? 19.166 20.746 4.691  1.000 8.46   ? 75  LEU A N    1 
ATOM   1382 C CA   . LEU A 1 76  ? 18.045 19.800 4.743  1.000 8.64   ? 75  LEU A CA   1 
ATOM   1383 C C    . LEU A 1 76  ? 17.440 19.695 6.130  1.000 8.32   ? 75  LEU A C    1 
ATOM   1384 O O    . LEU A 1 76  ? 16.282 19.268 6.247  1.000 10.23  ? 75  LEU A O    1 
ATOM   1385 C CB   . LEU A 1 76  ? 18.507 18.412 4.258  1.000 9.30   ? 75  LEU A CB   1 
ATOM   1386 C CG   . LEU A 1 76  ? 18.968 18.407 2.814  1.000 9.73   ? 75  LEU A CG   1 
ATOM   1387 C CD1  . LEU A 1 76  ? 19.452 17.014 2.440  1.000 12.64  ? 75  LEU A CD1  1 
ATOM   1388 C CD2  . LEU A 1 76  ? 17.888 18.873 1.851  1.000 12.27  ? 75  LEU A CD2  1 
ATOM   1389 H H    . LEU A 1 76  ? 20.119 20.414 4.643  1.000 17.35  ? 75  LEU A H    1 
ATOM   1390 D DA   . LEU A 1 76  ? 17.256 20.170 4.085  1.000 9.89   ? 75  LEU A DA   1 
ATOM   1391 D DB2  . LEU A 1 76  ? 19.314 18.051 4.909  1.000 10.88  ? 75  LEU A DB2  1 
ATOM   1392 D DB3  . LEU A 1 76  ? 17.668 17.719 4.384  1.000 11.29  ? 75  LEU A DB3  1 
ATOM   1393 D DG   . LEU A 1 76  ? 19.816 19.092 2.718  1.000 12.02  ? 75  LEU A DG   1 
ATOM   1394 D DD11 . LEU A 1 76  ? 18.682 16.305 2.482  1.000 15.36  ? 75  LEU A DD11 1 
ATOM   1395 D DD12 . LEU A 1 76  ? 19.789 16.994 1.420  1.000 15.96  ? 75  LEU A DD12 1 
ATOM   1396 D DD13 . LEU A 1 76  ? 20.244 16.716 3.078  1.000 15.99  ? 75  LEU A DD13 1 
ATOM   1397 D DD21 . LEU A 1 76  ? 17.032 18.273 1.947  1.000 16.54  ? 75  LEU A DD21 1 
ATOM   1398 D DD22 . LEU A 1 76  ? 17.670 19.894 2.034  1.000 14.96  ? 75  LEU A DD22 1 
ATOM   1399 D DD23 . LEU A 1 76  ? 18.236 18.852 0.858  1.000 14.49  ? 75  LEU A DD23 1 
ATOM   1400 N N    . CYS A 1 77  ? 18.153 20.074 7.195  1.000 7.79   ? 76  CYS A N    1 
ATOM   1401 C CA   . CYS A 1 77  ? 17.536 20.155 8.518  1.000 8.24   ? 76  CYS A CA   1 
ATOM   1402 C C    . CYS A 1 77  ? 16.788 21.479 8.748  1.000 8.47   ? 76  CYS A C    1 
ATOM   1403 O O    . CYS A 1 77  ? 16.081 21.596 9.746  1.000 10.26  ? 76  CYS A O    1 
ATOM   1404 C CB   . CYS A 1 77  ? 18.581 19.966 9.614  1.000 8.25   ? 76  CYS A CB   1 
ATOM   1405 S SG   . CYS A 1 77  ? 19.155 18.232 9.610  1.000 8.26   ? 76  CYS A SG   1 
ATOM   1406 H H    A CYS A 1 77  ? 19.129 20.307 7.085  0.848 8.80   ? 76  CYS A H    1 
ATOM   1407 D D    B CYS A 1 77  ? 19.142 20.185 7.040  0.152 7.17   ? 76  CYS A D    1 
ATOM   1408 D DA   . CYS A 1 77  ? 16.800 19.343 8.586  1.000 9.58   ? 76  CYS A DA   1 
ATOM   1409 D DB2  . CYS A 1 77  ? 19.436 20.614 9.472  1.000 9.73   ? 76  CYS A DB2  1 
ATOM   1410 D DB3  . CYS A 1 77  ? 18.087 20.177 10.558 1.000 10.43  ? 76  CYS A DB3  1 
ATOM   1411 N N    A ASN A 1 78  ? 16.879 22.423 7.817  0.616 8.70   ? 77  ASN A N    1 
ATOM   1412 N N    B ASN A 1 78  ? 17.038 22.428 7.851  0.384 7.88   ? 77  ASN A N    1 
ATOM   1413 C CA   A ASN A 1 78  ? 16.197 23.729 7.910  0.616 8.06   ? 77  ASN A CA   1 
ATOM   1414 C CA   B ASN A 1 78  ? 16.302 23.706 7.901  0.384 7.92   ? 77  ASN A CA   1 
ATOM   1415 C C    A ASN A 1 78  ? 16.573 24.526 9.156  0.616 8.75   ? 77  ASN A C    1 
ATOM   1416 C C    B ASN A 1 78  ? 16.556 24.366 9.258  0.384 8.00   ? 77  ASN A C    1 
ATOM   1417 O O    A ASN A 1 78  ? 15.695 25.124 9.771  0.616 8.53   ? 77  ASN A O    1 
ATOM   1418 O O    B ASN A 1 78  ? 15.661 24.679 10.026 0.384 9.06   ? 77  ASN A O    1 
ATOM   1419 C CB   A ASN A 1 78  ? 14.669 23.568 7.852  0.616 8.76   ? 77  ASN A CB   1 
ATOM   1420 C CB   B ASN A 1 78  ? 14.830 23.486 7.605  0.384 9.46   ? 77  ASN A CB   1 
ATOM   1421 C CG   A ASN A 1 78  ? 14.018 24.886 7.451  0.616 10.27  ? 77  ASN A CG   1 
ATOM   1422 C CG   B ASN A 1 78  ? 14.133 24.815 7.328  0.384 9.97   ? 77  ASN A CG   1 
ATOM   1423 O OD1  A ASN A 1 78  ? 14.611 25.677 6.728  0.616 10.94  ? 77  ASN A OD1  1 
ATOM   1424 O OD1  B ASN A 1 78  ? 14.804 25.816 7.136  0.384 9.84   ? 77  ASN A OD1  1 
ATOM   1425 N ND2  A ASN A 1 78  ? 12.806 25.082 7.930  0.616 11.58  ? 77  ASN A ND2  1 
ATOM   1426 N ND2  B ASN A 1 78  ? 12.818 24.719 7.349  0.384 10.99  ? 77  ASN A ND2  1 
ATOM   1427 D D    A ASN A 1 78  ? 17.419 22.266 6.971  0.616 8.38   ? 77  ASN A D    1 
ATOM   1428 D D    B ASN A 1 78  ? 17.726 22.326 7.123  0.384 13.58  ? 77  ASN A D    1 
ATOM   1429 D DA   A ASN A 1 78  ? 16.505 24.299 7.029  0.616 9.49   ? 77  ASN A DA   1 
ATOM   1430 D DA   B ASN A 1 78  ? 16.776 24.336 7.133  0.384 8.81   ? 77  ASN A DA   1 
ATOM   1431 D DB2  A ASN A 1 78  ? 14.434 22.819 7.084  0.616 12.28  ? 77  ASN A DB2  1 
ATOM   1432 D DB2  B ASN A 1 78  ? 14.729 22.852 6.708  0.384 10.37  ? 77  ASN A DB2  1 
ATOM   1433 D DB3  A ASN A 1 78  ? 14.295 23.239 8.806  0.616 11.29  ? 77  ASN A DB3  1 
ATOM   1434 D DB3  B ASN A 1 78  ? 14.341 22.976 8.418  0.384 9.66   ? 77  ASN A DB3  1 
ATOM   1435 D DD21 A ASN A 1 78  ? 12.335 25.951 7.707  0.616 12.40  ? 77  ASN A DD21 1 
ATOM   1436 D DD21 B ASN A 1 78  ? 12.259 25.502 7.056  0.384 11.64  ? 77  ASN A DD21 1 
ATOM   1437 D DD22 A ASN A 1 78  ? 12.330 24.329 8.403  0.616 11.58  ? 77  ASN A DD22 1 
ATOM   1438 D DD22 B ASN A 1 78  ? 12.404 23.865 7.691  0.384 11.06  ? 77  ASN A DD22 1 
ATOM   1439 N N    . ILE A 1 79  ? 17.855 24.574 9.497  1.000 8.72   ? 78  ILE A N    1 
ATOM   1440 C CA   . ILE A 1 79  ? 18.287 25.259 10.711 1.000 9.53   ? 78  ILE A CA   1 
ATOM   1441 C C    . ILE A 1 79  ? 19.589 25.972 10.435 1.000 9.45   ? 78  ILE A C    1 
ATOM   1442 O O    . ILE A 1 79  ? 20.426 25.510 9.646  1.000 10.64  ? 78  ILE A O    1 
ATOM   1443 C CB   . ILE A 1 79  ? 18.521 24.293 11.882 1.000 11.59  ? 78  ILE A CB   1 
ATOM   1444 C CG1  . ILE A 1 79  ? 19.424 23.125 11.475 1.000 12.67  ? 78  ILE A CG1  1 
ATOM   1445 C CG2  . ILE A 1 79  ? 17.188 23.845 12.461 1.000 13.86  ? 78  ILE A CG2  1 
ATOM   1446 C CD1  . ILE A 1 79  ? 20.020 22.375 12.645 1.000 15.63  ? 78  ILE A CD1  1 
ATOM   1447 H H    A ILE A 1 79  ? 18.543 24.129 8.907  1.000 14.72  ? 78  ILE A H    1 
ATOM   1448 D DA   . ILE A 1 79  ? 17.500 25.967 11.013 1.000 10.78  ? 78  ILE A DA   1 
ATOM   1449 D DB   . ILE A 1 79  ? 19.062 24.858 12.676 1.000 14.14  ? 78  ILE A DB   1 
ATOM   1450 D DG12 . ILE A 1 79  ? 18.828 22.438 10.898 1.000 19.52  ? 78  ILE A DG12 1 
ATOM   1451 D DG13 . ILE A 1 79  ? 20.186 23.461 10.827 1.000 18.93  ? 78  ILE A DG13 1 
ATOM   1452 D DG21 . ILE A 1 79  ? 16.656 23.233 11.766 1.000 18.28  ? 78  ILE A DG21 1 
ATOM   1453 D DG22 . ILE A 1 79  ? 17.327 23.308 13.380 1.000 18.68  ? 78  ILE A DG22 1 
ATOM   1454 D DG23 . ILE A 1 79  ? 16.577 24.675 12.752 1.000 19.82  ? 78  ILE A DG23 1 
ATOM   1455 D DD11 . ILE A 1 79  ? 19.243 22.026 13.268 1.000 22.71  ? 78  ILE A DD11 1 
ATOM   1456 D DD12 . ILE A 1 79  ? 20.639 21.596 12.302 1.000 20.09  ? 78  ILE A DD12 1 
ATOM   1457 D DD13 . ILE A 1 79  ? 20.612 23.046 13.226 1.000 23.87  ? 78  ILE A DD13 1 
ATOM   1458 N N    . PRO A 1 80  ? 19.835 27.052 11.194 1.000 9.59   ? 79  PRO A N    1 
ATOM   1459 C CA   . PRO A 1 80  ? 21.176 27.622 11.190 1.000 9.41   ? 79  PRO A CA   1 
ATOM   1460 C C    . PRO A 1 80  ? 22.107 26.674 11.913 1.000 8.76   ? 79  PRO A C    1 
ATOM   1461 O O    . PRO A 1 80  ? 21.717 26.049 12.910 1.000 9.47   ? 79  PRO A O    1 
ATOM   1462 C CB   . PRO A 1 80  ? 20.992 28.947 11.968 1.000 11.47  ? 79  PRO A CB   1 
ATOM   1463 C CG   . PRO A 1 80  ? 19.841 28.668 12.891 1.000 12.58  ? 79  PRO A CG   1 
ATOM   1464 C CD   . PRO A 1 80  ? 18.950 27.767 12.099 1.000 10.93  ? 79  PRO A CD   1 
ATOM   1465 D DA   . PRO A 1 80  ? 21.516 27.784 10.182 1.000 10.68  ? 79  PRO A DA   1 
ATOM   1466 D DB2  . PRO A 1 80  ? 21.901 29.201 12.503 1.000 14.39  ? 79  PRO A DB2  1 
ATOM   1467 D DB3  . PRO A 1 80  ? 20.800 29.751 11.275 1.000 14.85  ? 79  PRO A DB3  1 
ATOM   1468 D DG2  . PRO A 1 80  ? 20.202 28.160 13.784 1.000 15.09  ? 79  PRO A DG2  1 
ATOM   1469 D DG3  . PRO A 1 80  ? 19.328 29.578 13.161 1.000 15.11  ? 79  PRO A DG3  1 
ATOM   1470 D DD2  . PRO A 1 80  ? 18.423 27.075 12.742 1.000 13.31  ? 79  PRO A DD2  1 
ATOM   1471 D DD3  . PRO A 1 80  ? 18.162 28.289 11.581 1.000 13.98  ? 79  PRO A DD3  1 
ATOM   1472 N N    . CYS A 1 81  ? 23.351 26.577 11.467 1.000 8.35   ? 80  CYS A N    1 
ATOM   1473 C CA   . CYS A 1 81  ? 24.321 25.691 12.099 1.000 8.49   ? 80  CYS A CA   1 
ATOM   1474 C C    . CYS A 1 81  ? 24.575 26.125 13.546 1.000 9.49   ? 80  CYS A C    1 
ATOM   1475 O O    . CYS A 1 81  ? 24.896 25.262 14.362 1.000 10.53  ? 80  CYS A O    1 
ATOM   1476 C CB   . CYS A 1 81  ? 25.630 25.622 11.349 1.000 8.94   ? 80  CYS A CB   1 
ATOM   1477 S SG   . CYS A 1 81  ? 25.480 24.955 9.665  1.000 9.60   ? 80  CYS A SG   1 
ATOM   1478 H H    A CYS A 1 81  ? 23.634 27.130 10.671 0.728 6.60   ? 80  CYS A H    1 
ATOM   1479 D D    B CYS A 1 81  ? 23.662 27.126 10.685 0.272 7.54   ? 80  CYS A D    1 
ATOM   1480 D DA   . CYS A 1 81  ? 23.865 24.690 12.192 1.000 9.68   ? 80  CYS A DA   1 
ATOM   1481 D DB2  . CYS A 1 81  ? 26.037 26.610 11.208 1.000 10.55  ? 80  CYS A DB2  1 
ATOM   1482 D DB3  . CYS A 1 81  ? 26.331 24.982 11.924 1.000 10.00  ? 80  CYS A DB3  1 
ATOM   1483 N N    . SER A 1 82  ? 24.440 27.418 13.871 1.000 8.98   ? 81  SER A N    1 
ATOM   1484 C CA   . SER A 1 82  ? 24.629 27.839 15.232 1.000 10.52  ? 81  SER A CA   1 
ATOM   1485 C C    . SER A 1 82  ? 23.673 27.147 16.216 1.000 9.64   ? 81  SER A C    1 
ATOM   1486 O O    . SER A 1 82  ? 24.000 27.022 17.383 1.000 11.28  ? 81  SER A O    1 
ATOM   1487 C CB   . SER A 1 82  ? 24.445 29.361 15.318 1.000 12.63  ? 81  SER A CB   1 
ATOM   1488 O OG   . SER A 1 82  ? 23.205 29.732 14.875 1.000 14.80  ? 81  SER A OG   1 
ATOM   1489 D D    . SER A 1 82  ? 24.297 28.095 13.147 1.000 10.22  ? 81  SER A D    1 
ATOM   1490 D DA   . SER A 1 82  ? 25.643 27.586 15.580 1.000 13.44  ? 81  SER A DA   1 
ATOM   1491 D DB2  . SER A 1 82  ? 24.689 29.614 16.338 1.000 18.09  ? 81  SER A DB2  1 
ATOM   1492 D DB3  . SER A 1 82  ? 25.196 29.780 14.652 1.000 15.25  ? 81  SER A DB3  1 
ATOM   1493 D DG   . SER A 1 82  ? 22.524 30.061 15.410 1.000 25.91  ? 81  SER A DG   1 
ATOM   1494 N N    . ALA A 1 83  ? 22.500 26.693 15.748 1.000 9.59   ? 82  ALA A N    1 
ATOM   1495 C CA   . ALA A 1 83  ? 21.591 25.977 16.631 1.000 9.96   ? 82  ALA A CA   1 
ATOM   1496 C C    . ALA A 1 83  ? 22.190 24.664 17.140 1.000 9.07   ? 82  ALA A C    1 
ATOM   1497 O O    . ALA A 1 83  ? 21.770 24.154 18.158 1.000 12.82  ? 82  ALA A O    1 
ATOM   1498 C CB   . ALA A 1 83  ? 20.281 25.685 15.912 1.000 11.75  ? 82  ALA A CB   1 
ATOM   1499 H H    A ALA A 1 83  ? 22.248 26.849 14.783 0.405 5.40   ? 82  ALA A H    1 
ATOM   1500 D D    B ALA A 1 83  ? 22.264 26.859 14.776 0.595 10.20  ? 82  ALA A D    1 
ATOM   1501 D DA   . ALA A 1 83  ? 21.383 26.623 17.507 1.000 12.18  ? 82  ALA A DA   1 
ATOM   1502 D DB1  . ALA A 1 83  ? 20.474 25.101 15.039 1.000 13.82  ? 82  ALA A DB1  1 
ATOM   1503 D DB2  . ALA A 1 83  ? 19.613 25.166 16.567 1.000 14.37  ? 82  ALA A DB2  1 
ATOM   1504 D DB3  . ALA A 1 83  ? 19.798 26.602 15.639 1.000 14.96  ? 82  ALA A DB3  1 
ATOM   1505 N N    . LEU A 1 84  ? 23.166 24.140 16.418 1.000 9.21   ? 83  LEU A N    1 
ATOM   1506 C CA   . LEU A 1 84  ? 23.800 22.905 16.762 1.000 9.58   ? 83  LEU A CA   1 
ATOM   1507 C C    . LEU A 1 84  ? 24.932 23.079 17.778 1.000 10.30  ? 83  LEU A C    1 
ATOM   1508 O O    . LEU A 1 84  ? 25.513 22.080 18.200 1.000 12.50  ? 83  LEU A O    1 
ATOM   1509 C CB   . LEU A 1 84  ? 24.417 22.248 15.500 1.000 10.30  ? 83  LEU A CB   1 
ATOM   1510 C CG   . LEU A 1 84  ? 23.385 21.895 14.433 1.000 11.88  ? 83  LEU A CG   1 
ATOM   1511 C CD1  . LEU A 1 84  ? 24.131 21.355 13.211 1.000 14.28  ? 83  LEU A CD1  1 
ATOM   1512 C CD2  . LEU A 1 84  ? 22.398 20.860 14.895 1.000 15.42  ? 83  LEU A CD2  1 
ATOM   1513 H H    . LEU A 1 84  ? 23.476 24.631 15.592 1.000 11.72  ? 83  LEU A H    1 
ATOM   1514 D DA   . LEU A 1 84  ? 23.043 22.253 17.225 1.000 10.68  ? 83  LEU A DA   1 
ATOM   1515 D DB2  . LEU A 1 84  ? 25.171 22.907 15.088 1.000 12.42  ? 83  LEU A DB2  1 
ATOM   1516 D DB3  . LEU A 1 84  ? 24.935 21.344 15.826 1.000 13.62  ? 83  LEU A DB3  1 
ATOM   1517 D DG   . LEU A 1 84  ? 22.882 22.813 14.150 1.000 13.60  ? 83  LEU A DG   1 
ATOM   1518 D DD11 . LEU A 1 84  ? 24.669 20.507 13.444 1.000 20.03  ? 83  LEU A DD11 1 
ATOM   1519 D DD12 . LEU A 1 84  ? 23.424 21.132 12.435 1.000 18.18  ? 83  LEU A DD12 1 
ATOM   1520 D DD13 . LEU A 1 84  ? 24.746 22.133 12.802 1.000 18.58  ? 83  LEU A DD13 1 
ATOM   1521 D DD21 . LEU A 1 84  ? 22.911 19.979 15.199 1.000 19.27  ? 83  LEU A DD21 1 
ATOM   1522 D DD22 . LEU A 1 84  ? 21.837 21.182 15.722 1.000 18.85  ? 83  LEU A DD22 1 
ATOM   1523 D DD23 . LEU A 1 84  ? 21.723 20.604 14.128 1.000 19.61  ? 83  LEU A DD23 1 
ATOM   1524 N N    . LEU A 1 85  ? 25.208 24.303 18.207 1.000 10.35  ? 84  LEU A N    1 
ATOM   1525 C CA   . LEU A 1 85  ? 26.211 24.613 19.222 1.000 10.82  ? 84  LEU A CA   1 
ATOM   1526 C C    . LEU A 1 85  ? 25.617 25.022 20.547 1.000 13.80  ? 84  LEU A C    1 
ATOM   1527 O O    . LEU A 1 85  ? 26.329 25.513 21.426 1.000 18.91  ? 84  LEU A O    1 
ATOM   1528 C CB   . LEU A 1 85  ? 27.121 25.753 18.720 1.000 11.68  ? 84  LEU A CB   1 
ATOM   1529 C CG   . LEU A 1 85  ? 27.895 25.456 17.439 1.000 11.64  ? 84  LEU A CG   1 
ATOM   1530 C CD1  . LEU A 1 85  ? 28.630 26.707 16.997 1.000 14.19  ? 84  LEU A CD1  1 
ATOM   1531 C CD2  . LEU A 1 85  ? 28.864 24.294 17.600 1.000 15.24  ? 84  LEU A CD2  1 
ATOM   1532 H H    A LEU A 1 85  ? 24.690 25.071 17.804 0.635 6.25   ? 84  LEU A H    1 
ATOM   1533 D D    B LEU A 1 85  ? 24.650 25.087 17.877 0.365 7.70   ? 84  LEU A D    1 
ATOM   1534 D DA   . LEU A 1 85  ? 26.818 23.714 19.370 1.000 12.12  ? 84  LEU A DA   1 
ATOM   1535 D DB2  . LEU A 1 85  ? 26.506 26.643 18.573 1.000 12.93  ? 84  LEU A DB2  1 
ATOM   1536 D DB3  . LEU A 1 85  ? 27.812 26.022 19.517 1.000 13.58  ? 84  LEU A DB3  1 
ATOM   1537 D DG   . LEU A 1 85  ? 27.180 25.186 16.660 1.000 13.36  ? 84  LEU A DG   1 
ATOM   1538 D DD11 . LEU A 1 85  ? 29.313 27.006 17.763 1.000 18.82  ? 84  LEU A DD11 1 
ATOM   1539 D DD12 . LEU A 1 85  ? 29.174 26.530 16.101 1.000 17.67  ? 84  LEU A DD12 1 
ATOM   1540 D DD13 . LEU A 1 85  ? 27.983 27.510 16.843 1.000 20.52  ? 84  LEU A DD13 1 
ATOM   1541 D DD21 . LEU A 1 85  ? 29.558 24.508 18.357 1.000 19.75  ? 84  LEU A DD21 1 
ATOM   1542 D DD22 . LEU A 1 85  ? 28.331 23.427 17.864 1.000 19.75  ? 84  LEU A DD22 1 
ATOM   1543 D DD23 . LEU A 1 85  ? 29.374 24.146 16.680 1.000 17.70  ? 84  LEU A DD23 1 
ATOM   1544 N N    . SER A 1 86  ? 24.355 24.760 20.727 1.000 15.52  ? 85  SER A N    1 
ATOM   1545 C CA   . SER A 1 86  ? 23.702 24.979 22.011 1.000 16.24  ? 85  SER A CA   1 
ATOM   1546 C C    . SER A 1 86  ? 24.018 23.950 23.072 1.000 14.27  ? 85  SER A C    1 
ATOM   1547 O O    . SER A 1 86  ? 24.372 22.831 22.758 1.000 15.00  ? 85  SER A O    1 
ATOM   1548 C CB   . SER A 1 86  ? 22.198 24.949 21.692 1.000 17.34  ? 85  SER A CB   1 
ATOM   1549 O OG   . SER A 1 86  ? 21.456 25.183 22.862 1.000 16.78  ? 85  SER A OG   1 
ATOM   1550 D D    . SER A 1 86  ? 23.807 24.363 19.984 1.000 16.76  ? 85  SER A D    1 
ATOM   1551 D DA   . SER A 1 86  ? 23.969 25.964 22.394 1.000 18.32  ? 85  SER A DA   1 
ATOM   1552 D DB2  . SER A 1 86  ? 21.976 25.721 20.973 1.000 24.63  ? 85  SER A DB2  1 
ATOM   1553 D DB3  . SER A 1 86  ? 21.940 23.965 21.326 1.000 19.61  ? 85  SER A DB3  1 
ATOM   1554 D DG   . SER A 1 86  ? 21.298 26.124 23.003 1.000 36.82  ? 85  SER A DG   1 
ATOM   1555 N N    . SER A 1 87  ? 23.858 24.324 24.361 1.000 16.05  ? 86  SER A N    1 
ATOM   1556 C CA   . SER A 1 87  ? 23.990 23.395 25.451 1.000 17.06  ? 86  SER A CA   1 
ATOM   1557 C C    . SER A 1 87  ? 22.831 22.419 25.549 1.000 14.75  ? 86  SER A C    1 
ATOM   1558 O O    . SER A 1 87  ? 22.960 21.317 26.067 1.000 18.39  ? 86  SER A O    1 
ATOM   1559 C CB   . SER A 1 87  ? 24.124 24.162 26.771 1.000 20.88  ? 86  SER A CB   1 
ATOM   1560 O OG   . SER A 1 87  ? 23.106 25.111 26.897 1.000 20.69  ? 86  SER A OG   1 
ATOM   1561 D D    . SER A 1 87  ? 23.620 25.260 24.570 1.000 20.56  ? 86  SER A D    1 
ATOM   1562 D DA   . SER A 1 87  ? 24.895 22.814 25.299 1.000 20.67  ? 86  SER A DA   1 
ATOM   1563 D DB2  . SER A 1 87  ? 24.025 23.434 27.568 1.000 23.37  ? 86  SER A DB2  1 
ATOM   1564 D DB3  . SER A 1 87  ? 25.118 24.618 26.814 1.000 26.13  ? 86  SER A DB3  1 
ATOM   1565 D DG   . SER A 1 87  ? 22.244 24.685 26.717 1.000 32.50  ? 86  SER A DG   1 
ATOM   1566 N N    A ASP A 1 88  ? 21.724 22.774 24.906 0.659 14.03  ? 87  ASP A N    1 
ATOM   1567 N N    B ASP A 1 88  ? 21.621 22.798 25.151 0.341 13.87  ? 87  ASP A N    1 
ATOM   1568 C CA   A ASP A 1 88  ? 20.488 22.004 24.786 0.659 14.51  ? 87  ASP A CA   1 
ATOM   1569 C CA   B ASP A 1 88  ? 20.629 21.726 25.015 0.341 14.56  ? 87  ASP A CA   1 
ATOM   1570 C C    A ASP A 1 88  ? 20.568 21.159 23.519 0.659 13.86  ? 87  ASP A C    1 
ATOM   1571 C C    B ASP A 1 88  ? 20.803 21.110 23.623 0.341 13.98  ? 87  ASP A C    1 
ATOM   1572 O O    A ASP A 1 88  ? 20.769 21.725 22.427 0.659 12.78  ? 87  ASP A O    1 
ATOM   1573 O O    B ASP A 1 88  ? 21.253 21.717 22.656 0.341 13.83  ? 87  ASP A O    1 
ATOM   1574 C CB   A ASP A 1 88  ? 19.311 22.967 24.751 0.659 16.46  ? 87  ASP A CB   1 
ATOM   1575 C CB   B ASP A 1 88  ? 19.213 22.197 25.237 0.341 15.82  ? 87  ASP A CB   1 
ATOM   1576 C CG   A ASP A 1 88  ? 17.976 22.284 24.581 0.659 16.94  ? 87  ASP A CG   1 
ATOM   1577 C CG   B ASP A 1 88  ? 18.689 23.003 24.067 0.341 16.37  ? 87  ASP A CG   1 
ATOM   1578 O OD1  A ASP A 1 88  ? 17.113 22.361 25.488 0.659 25.48  ? 87  ASP A OD1  1 
ATOM   1579 O OD1  B ASP A 1 88  ? 19.125 24.164 23.927 0.341 16.89  ? 87  ASP A OD1  1 
ATOM   1580 O OD2  A ASP A 1 88  ? 17.748 21.643 23.548 0.659 18.54  ? 87  ASP A OD2  1 
ATOM   1581 O OD2  B ASP A 1 88  ? 17.861 22.430 23.330 0.341 16.92  ? 87  ASP A OD2  1 
ATOM   1582 D D    A ASP A 1 88  ? 21.704 23.632 24.376 0.659 13.45  ? 87  ASP A D    1 
ATOM   1583 D D    B ASP A 1 88  ? 21.404 23.754 24.956 0.341 13.63  ? 87  ASP A D    1 
ATOM   1584 D DA   A ASP A 1 88  ? 20.404 21.326 25.638 0.659 14.91  ? 87  ASP A DA   1 
ATOM   1585 D DA   B ASP A 1 88  ? 20.884 20.956 25.764 0.341 13.71  ? 87  ASP A DA   1 
ATOM   1586 D DB2  A ASP A 1 88  ? 19.302 23.534 25.675 0.659 20.00  ? 87  ASP A DB2  1 
ATOM   1587 D DB2  B ASP A 1 88  ? 18.565 21.337 25.383 0.341 16.53  ? 87  ASP A DB2  1 
ATOM   1588 D DB3  A ASP A 1 88  ? 19.472 23.664 23.934 0.659 16.80  ? 87  ASP A DB3  1 
ATOM   1589 D DB3  B ASP A 1 88  ? 19.170 22.806 26.135 0.341 15.62  ? 87  ASP A DB3  1 
ATOM   1590 N N    . ILE A 1 89  ? 20.415 19.840 23.556 1.000 13.02  ? 88  ILE A N    1 
ATOM   1591 C CA   . ILE A 1 89  ? 20.715 19.009 22.421 1.000 12.65  ? 88  ILE A CA   1 
ATOM   1592 C C    . ILE A 1 89  ? 19.557 18.898 21.420 1.000 11.95  ? 88  ILE A C    1 
ATOM   1593 O O    . ILE A 1 89  ? 19.666 18.131 20.450 1.000 13.17  ? 88  ILE A O    1 
ATOM   1594 C CB   . ILE A 1 89  ? 21.151 17.585 22.823 1.000 14.79  ? 88  ILE A CB   1 
ATOM   1595 C CG1  . ILE A 1 89  ? 20.044 16.759 23.489 1.000 16.63  ? 88  ILE A CG1  1 
ATOM   1596 C CG2  . ILE A 1 89  ? 22.419 17.691 23.654 1.000 18.79  ? 88  ILE A CG2  1 
ATOM   1597 C CD1  . ILE A 1 89  ? 20.409 15.299 23.607 1.000 21.50  ? 88  ILE A CD1  1 
ATOM   1598 D D    . ILE A 1 89  ? 20.153 19.444 24.465 1.000 15.83  ? 88  ILE A D    1 
ATOM   1599 D DA   . ILE A 1 89  ? 21.548 19.455 21.864 1.000 14.02  ? 88  ILE A DA   1 
ATOM   1600 D DB   . ILE A 1 89  ? 21.405 17.066 21.878 1.000 15.28  ? 88  ILE A DB   1 
ATOM   1601 D DG12 . ILE A 1 89  ? 19.853 17.180 24.460 1.000 20.15  ? 88  ILE A DG12 1 
ATOM   1602 D DG13 . ILE A 1 89  ? 19.159 16.829 22.838 1.000 18.52  ? 88  ILE A DG13 1 
ATOM   1603 D DG21 . ILE A 1 89  ? 22.256 18.187 24.583 1.000 22.83  ? 88  ILE A DG21 1 
ATOM   1604 D DG22 . ILE A 1 89  ? 22.819 16.728 23.881 1.000 22.19  ? 88  ILE A DG22 1 
ATOM   1605 D DG23 . ILE A 1 89  ? 23.168 18.263 23.133 1.000 20.46  ? 88  ILE A DG23 1 
ATOM   1606 D DD11 . ILE A 1 89  ? 20.661 14.918 22.663 1.000 25.45  ? 88  ILE A DD11 1 
ATOM   1607 D DD12 . ILE A 1 89  ? 21.271 15.194 24.239 1.000 24.87  ? 88  ILE A DD12 1 
ATOM   1608 D DD13 . ILE A 1 89  ? 19.604 14.774 24.072 1.000 25.69  ? 88  ILE A DD13 1 
ATOM   1609 N N    . THR A 1 90  ? 18.462 19.615 21.655 1.000 14.10  ? 89  THR A N    1 
ATOM   1610 C CA   . THR A 1 90  ? 17.291 19.499 20.810 1.000 15.58  ? 89  THR A CA   1 
ATOM   1611 C C    . THR A 1 90  ? 17.583 19.612 19.315 1.000 12.25  ? 89  THR A C    1 
ATOM   1612 O O    . THR A 1 90  ? 17.159 18.735 18.553 1.000 11.57  ? 89  THR A O    1 
ATOM   1613 C CB   . THR A 1 90  ? 16.255 20.576 21.198 1.000 20.40  ? 89  THR A CB   1 
ATOM   1614 O OG1  . THR A 1 90  ? 15.882 20.374 22.575 1.000 23.26  ? 89  THR A OG1  1 
ATOM   1615 C CG2  . THR A 1 90  ? 15.025 20.515 20.317 1.000 24.48  ? 89  THR A CG2  1 
ATOM   1616 D D    . THR A 1 90  ? 18.415 20.239 22.455 1.000 16.40  ? 89  THR A D    1 
ATOM   1617 D DA   . THR A 1 90  ? 16.921 18.485 20.984 1.000 16.74  ? 89  THR A DA   1 
ATOM   1618 D DB   . THR A 1 90  ? 16.719 21.565 21.127 1.000 22.55  ? 89  THR A DB   1 
ATOM   1619 D DG1  . THR A 1 90  ? 16.475 20.935 23.121 1.000 23.60  ? 89  THR A DG1  1 
ATOM   1620 D DG21 . THR A 1 90  ? 14.596 19.537 20.362 1.000 31.36  ? 89  THR A DG21 1 
ATOM   1621 D DG22 . THR A 1 90  ? 14.308 21.227 20.660 1.000 29.72  ? 89  THR A DG22 1 
ATOM   1622 D DG23 . THR A 1 90  ? 15.296 20.716 19.304 1.000 31.43  ? 89  THR A DG23 1 
ATOM   1623 N N    . ALA A 1 91  ? 18.229 20.679 18.879 1.000 12.20  ? 90  ALA A N    1 
ATOM   1624 C CA   . ALA A 1 91  ? 18.382 20.810 17.456 1.000 11.29  ? 90  ALA A CA   1 
ATOM   1625 C C    . ALA A 1 91  ? 19.283 19.720 16.860 1.000 9.70   ? 90  ALA A C    1 
ATOM   1626 O O    . ALA A 1 91  ? 19.053 19.234 15.763 1.000 10.58  ? 90  ALA A O    1 
ATOM   1627 C CB   . ALA A 1 91  ? 18.941 22.176 17.075 1.000 13.69  ? 90  ALA A CB   1 
ATOM   1628 D D    . ALA A 1 91  ? 18.553 21.362 19.545 1.000 15.42  ? 90  ALA A D    1 
ATOM   1629 D DA   . ALA A 1 91  ? 17.410 20.689 16.974 1.000 12.48  ? 90  ALA A DA   1 
ATOM   1630 D DB1  . ALA A 1 91  ? 19.867 22.337 17.567 1.000 15.83  ? 90  ALA A DB1  1 
ATOM   1631 D DB2  . ALA A 1 91  ? 19.064 22.225 16.025 1.000 16.05  ? 90  ALA A DB2  1 
ATOM   1632 D DB3  . ALA A 1 91  ? 18.300 22.934 17.413 1.000 16.27  ? 90  ALA A DB3  1 
ATOM   1633 N N    . SER A 1 92  ? 20.304 19.311 17.600 1.000 9.51   ? 91  SER A N    1 
ATOM   1634 C CA   . SER A 1 92  ? 21.183 18.258 17.143 1.000 9.07   ? 91  SER A CA   1 
ATOM   1635 C C    . SER A 1 92  ? 20.428 16.928 16.996 1.000 9.08   ? 91  SER A C    1 
ATOM   1636 O O    . SER A 1 92  ? 20.603 16.236 16.011 1.000 10.77  ? 91  SER A O    1 
ATOM   1637 C CB   . SER A 1 92  ? 22.387 18.088 18.077 1.000 10.20  ? 91  SER A CB   1 
ATOM   1638 O OG   . SER A 1 92  ? 23.311 19.160 17.878 1.000 11.31  ? 91  SER A OG   1 
ATOM   1639 D D    . SER A 1 92  ? 20.442 19.739 18.500 1.000 12.56  ? 91  SER A D    1 
ATOM   1640 D DA   . SER A 1 92  ? 21.572 18.484 16.152 1.000 10.54  ? 91  SER A DA   1 
ATOM   1641 D DB2  . SER A 1 92  ? 22.040 18.057 19.111 1.000 11.80  ? 91  SER A DB2  1 
ATOM   1642 D DB3  . SER A 1 92  ? 22.893 17.161 17.791 1.000 13.22  ? 91  SER A DB3  1 
ATOM   1643 D DG   . SER A 1 92  ? 23.033 19.891 18.409 1.000 14.04  ? 91  SER A DG   1 
ATOM   1644 N N    . VAL A 1 93  ? 19.600 16.620 17.987 1.000 9.59   ? 92  VAL A N    1 
ATOM   1645 C CA   . VAL A 1 93  ? 18.820 15.387 17.891 1.000 10.66  ? 92  VAL A CA   1 
ATOM   1646 C C    . VAL A 1 93  ? 17.841 15.438 16.749 1.000 9.64   ? 92  VAL A C    1 
ATOM   1647 O O    . VAL A 1 93  ? 17.667 14.471 16.022 1.000 10.09  ? 92  VAL A O    1 
ATOM   1648 C CB   . VAL A 1 93  ? 18.098 15.072 19.215 1.000 13.73  ? 92  VAL A CB   1 
ATOM   1649 C CG1  . VAL A 1 93  ? 17.133 13.905 19.040 1.000 16.15  ? 92  VAL A CG1  1 
ATOM   1650 C CG2  . VAL A 1 93  ? 19.149 14.787 20.272 1.000 15.97  ? 92  VAL A CG2  1 
ATOM   1651 H H    A VAL A 1 93  ? 19.511 17.224 18.792 0.862 9.14   ? 92  VAL A H    1 
ATOM   1652 D D    B VAL A 1 93  ? 19.567 17.159 18.832 0.138 8.33   ? 92  VAL A D    1 
ATOM   1653 D DA   . VAL A 1 93  ? 19.535 14.584 17.661 1.000 12.37  ? 92  VAL A DA   1 
ATOM   1654 D DB   . VAL A 1 93  ? 17.521 15.960 19.515 1.000 15.56  ? 92  VAL A DB   1 
ATOM   1655 D DG11 . VAL A 1 93  ? 17.628 13.089 18.585 1.000 19.10  ? 92  VAL A DG11 1 
ATOM   1656 D DG12 . VAL A 1 93  ? 16.791 13.587 19.992 1.000 22.51  ? 92  VAL A DG12 1 
ATOM   1657 D DG13 . VAL A 1 93  ? 16.337 14.195 18.402 1.000 18.55  ? 92  VAL A DG13 1 
ATOM   1658 D DG21 . VAL A 1 93  ? 19.738 13.956 20.008 1.000 20.40  ? 92  VAL A DG21 1 
ATOM   1659 D DG22 . VAL A 1 93  ? 19.780 15.620 20.413 1.000 19.31  ? 92  VAL A DG22 1 
ATOM   1660 D DG23 . VAL A 1 93  ? 18.686 14.585 21.202 1.000 20.15  ? 92  VAL A DG23 1 
ATOM   1661 N N    . ASN A 1 94  ? 17.144 16.569 16.601 1.000 9.51   ? 93  ASN A N    1 
ATOM   1662 C CA   . ASN A 1 94  ? 16.174 16.643 15.551 1.000 10.18  ? 93  ASN A CA   1 
ATOM   1663 C C    . ASN A 1 94  ? 16.815 16.510 14.180 1.000 9.33   ? 93  ASN A C    1 
ATOM   1664 O O    . ASN A 1 94  ? 16.278 15.888 13.269 1.000 10.63  ? 93  ASN A O    1 
ATOM   1665 C CB   . ASN A 1 94  ? 15.382 17.944 15.614 1.000 11.50  ? 93  ASN A CB   1 
ATOM   1666 C CG   . ASN A 1 94  ? 14.426 17.938 16.772 1.000 14.67  ? 93  ASN A CG   1 
ATOM   1667 O OD1  . ASN A 1 94  ? 14.034 16.867 17.245 1.000 20.26  ? 93  ASN A OD1  1 
ATOM   1668 N ND2  . ASN A 1 94  ? 13.983 19.117 17.142 1.000 16.73  ? 93  ASN A ND2  1 
ATOM   1669 H H    A ASN A 1 94  ? 17.300 17.355 17.216 0.667 10.79  ? 93  ASN A H    1 
ATOM   1670 D D    B ASN A 1 94  ? 17.257 17.311 17.283 0.333 14.62  ? 93  ASN A D    1 
ATOM   1671 D DA   . ASN A 1 94  ? 15.484 15.804 15.676 1.000 11.68  ? 93  ASN A DA   1 
ATOM   1672 D DB2  . ASN A 1 94  ? 16.067 18.789 15.678 1.000 14.15  ? 93  ASN A DB2  1 
ATOM   1673 D DB3  . ASN A 1 94  ? 14.798 18.029 14.676 1.000 14.22  ? 93  ASN A DB3  1 
ATOM   1674 D DD21 . ASN A 1 94  ? 13.300 19.218 17.851 1.000 23.23  ? 93  ASN A DD21 1 
ATOM   1675 D DD22 . ASN A 1 94  ? 14.392 19.940 16.685 1.000 20.19  ? 93  ASN A DD22 1 
ATOM   1676 N N    . CYS A 1 95  ? 17.970 17.105 13.997 1.000 8.49   ? 94  CYS A N    1 
ATOM   1677 C CA   . CYS A 1 95  ? 18.672 17.009 12.719 1.000 8.60   ? 94  CYS A CA   1 
ATOM   1678 C C    . CYS A 1 95  ? 19.266 15.614 12.538 1.000 8.47   ? 94  CYS A C    1 
ATOM   1679 O O    . CYS A 1 95  ? 19.193 15.080 11.434 1.000 9.81   ? 94  CYS A O    1 
ATOM   1680 C CB   . CYS A 1 95  ? 19.715 18.118 12.630 1.000 8.66   ? 94  CYS A CB   1 
ATOM   1681 S SG   . CYS A 1 95  ? 20.585 18.162 11.035 1.000 8.76   ? 94  CYS A SG   1 
ATOM   1682 H H    A CYS A 1 95  ? 18.380 17.638 14.751 0.614 7.69   ? 94  CYS A H    1 
ATOM   1683 D D    B CYS A 1 95  ? 18.382 17.664 14.738 0.386 8.06   ? 94  CYS A D    1 
ATOM   1684 D DA   . CYS A 1 95  ? 17.957 17.122 11.899 1.000 9.63   ? 94  CYS A DA   1 
ATOM   1685 D DB2  . CYS A 1 95  ? 19.207 19.050 12.788 1.000 10.67  ? 94  CYS A DB2  1 
ATOM   1686 D DB3  . CYS A 1 95  ? 20.473 18.007 13.398 1.000 10.70  ? 94  CYS A DB3  1 
ATOM   1687 N N    . ALA A 1 96  ? 19.784 15.004 13.591 1.000 8.46   ? 95  ALA A N    1 
ATOM   1688 C CA   . ALA A 1 96  ? 20.242 13.609 13.468 1.000 9.35   ? 95  ALA A CA   1 
ATOM   1689 C C    . ALA A 1 96  ? 19.128 12.669 13.007 1.000 9.48   ? 95  ALA A C    1 
ATOM   1690 O O    . ALA A 1 96  ? 19.357 11.755 12.225 1.000 10.28  ? 95  ALA A O    1 
ATOM   1691 C CB   . ALA A 1 96  ? 20.824 13.155 14.785 1.000 11.73  ? 95  ALA A CB   1 
ATOM   1692 H H    . ALA A 1 96  ? 19.864 15.490 14.472 1.000 14.00  ? 95  ALA A H    1 
ATOM   1693 D DA   . ALA A 1 96  ? 21.006 13.560 12.683 1.000 10.96  ? 95  ALA A DA   1 
ATOM   1694 D DB1  . ALA A 1 96  ? 20.097 13.171 15.553 1.000 13.10  ? 95  ALA A DB1  1 
ATOM   1695 D DB2  . ALA A 1 96  ? 21.191 12.176 14.720 1.000 14.83  ? 95  ALA A DB2  1 
ATOM   1696 D DB3  . ALA A 1 96  ? 21.632 13.798 15.083 1.000 14.33  ? 95  ALA A DB3  1 
ATOM   1697 N N    . LYS A 1 97  ? 17.909 12.858 13.530 1.000 9.44   ? 96  LYS A N    1 
ATOM   1698 C CA   . LYS A 1 97  ? 16.780 12.041 13.096 1.000 10.48  ? 96  LYS A CA   1 
ATOM   1699 C C    . LYS A 1 97  ? 16.519 12.250 11.608 1.000 11.57  ? 96  LYS A C    1 
ATOM   1700 O O    . LYS A 1 97  ? 16.208 11.299 10.906 1.000 12.76  ? 96  LYS A O    1 
ATOM   1701 C CB   . LYS A 1 97  ? 15.532 12.406 13.886 1.000 11.99  ? 96  LYS A CB   1 
ATOM   1702 C CG   . LYS A 1 97  ? 15.548 11.913 15.324 1.000 13.20  ? 96  LYS A CG   1 
ATOM   1703 C CD   . LYS A 1 97  ? 14.262 12.339 15.986 1.000 17.13  ? 96  LYS A CD   1 
ATOM   1704 C CE   . LYS A 1 97  ? 14.145 11.845 17.427 1.000 20.63  ? 96  LYS A CE   1 
ATOM   1705 N NZ   . LYS A 1 97  ? 12.921 12.403 18.058 1.000 22.68  ? 96  LYS A NZ   1 
ATOM   1706 H H    . LYS A 1 97  ? 17.770 13.572 14.230 1.000 14.27  ? 96  LYS A H    1 
ATOM   1707 D DA   . LYS A 1 97  ? 17.052 10.994 13.208 1.000 12.15  ? 96  LYS A DA   1 
ATOM   1708 D DB2  . LYS A 1 97  ? 15.429 13.486 13.881 1.000 13.43  ? 96  LYS A DB2  1 
ATOM   1709 D DB3  . LYS A 1 97  ? 14.663 11.978 13.392 1.000 14.05  ? 96  LYS A DB3  1 
ATOM   1710 D DG2  . LYS A 1 97  ? 15.649 10.833 15.330 1.000 14.82  ? 96  LYS A DG2  1 
ATOM   1711 D DG3  . LYS A 1 97  ? 16.413 12.301 15.844 1.000 14.36  ? 96  LYS A DG3  1 
ATOM   1712 D DD2  . LYS A 1 97  ? 14.241 13.444 16.011 1.000 21.02  ? 96  LYS A DD2  1 
ATOM   1713 D DD3  . LYS A 1 97  ? 13.405 11.945 15.434 1.000 21.26  ? 96  LYS A DD3  1 
ATOM   1714 D DE2  . LYS A 1 97  ? 14.092 10.756 17.360 1.000 24.11  ? 96  LYS A DE2  1 
ATOM   1715 D DE3  . LYS A 1 97  ? 15.024 12.149 17.960 1.000 25.01  ? 96  LYS A DE3  1 
ATOM   1716 D DZ1  . LYS A 1 97  ? 12.094 12.005 17.581 1.000 28.35  ? 96  LYS A DZ1  1 
ATOM   1717 D DZ2  . LYS A 1 97  ? 12.933 12.142 19.060 1.000 27.19  ? 96  LYS A DZ2  1 
ATOM   1718 D DZ3  . LYS A 1 97  ? 12.892 13.408 17.889 1.000 27.98  ? 96  LYS A DZ3  1 
ATOM   1719 N N    . LYS A 1 98  ? 16.619 13.489 11.135 1.000 11.15  ? 97  LYS A N    1 
ATOM   1720 C CA   . LYS A 1 98  ? 16.464 13.761 9.709  1.000 12.82  ? 97  LYS A CA   1 
ATOM   1721 C C    . LYS A 1 98  ? 17.536 13.070 8.857  1.000 12.91  ? 97  LYS A C    1 
ATOM   1722 O O    . LYS A 1 98  ? 17.212 12.511 7.799  1.000 16.33  ? 97  LYS A O    1 
ATOM   1723 C CB   . LYS A 1 98  ? 16.442 15.277 9.494  1.000 15.41  ? 97  LYS A CB   1 
ATOM   1724 C CG   . LYS A 1 98  ? 16.281 15.761 8.079  1.000 19.14  ? 97  LYS A CG   1 
ATOM   1725 C CD   . LYS A 1 98  ? 14.847 15.509 7.638  1.000 26.92  ? 97  LYS A CD   1 
ATOM   1726 C CE   . LYS A 1 98  ? 14.642 16.167 6.285  1.000 32.68  ? 97  LYS A CE   1 
ATOM   1727 N NZ   . LYS A 1 98  ? 13.211 15.825 5.994  1.000 35.78  ? 97  LYS A NZ   1 
ATOM   1728 H H    . LYS A 1 98  ? 16.806 14.252 11.770 1.000 17.59  ? 97  LYS A H    1 
ATOM   1729 D DA   . LYS A 1 98  ? 15.535 13.328 9.331  1.000 14.89  ? 97  LYS A DA   1 
ATOM   1730 D DB2  . LYS A 1 98  ? 15.579 15.659 10.079 1.000 17.85  ? 97  LYS A DB2  1 
ATOM   1731 D DB3  . LYS A 1 98  ? 17.330 15.705 9.923  1.000 15.21  ? 97  LYS A DB3  1 
ATOM   1732 D DG2  . LYS A 1 98  ? 16.459 16.860 8.028  1.000 20.49  ? 97  LYS A DG2  1 
ATOM   1733 D DG3  . LYS A 1 98  ? 16.971 15.271 7.411  1.000 24.72  ? 97  LYS A DG3  1 
ATOM   1734 D DD2  . LYS A 1 98  ? 14.690 14.441 7.549  1.000 30.40  ? 97  LYS A DD2  1 
ATOM   1735 D DD3  . LYS A 1 98  ? 14.168 15.980 8.353  1.000 29.25  ? 97  LYS A DD3  1 
ATOM   1736 D DE2  . LYS A 1 98  ? 14.709 17.242 6.413  1.000 38.56  ? 97  LYS A DE2  1 
ATOM   1737 D DE3  . LYS A 1 98  ? 15.318 15.741 5.570  1.000 33.97  ? 97  LYS A DE3  1 
ATOM   1738 D DZ1  . LYS A 1 98  ? 12.973 15.046 6.657  1.000 41.44  ? 97  LYS A DZ1  1 
ATOM   1739 D DZ2  . LYS A 1 98  ? 12.647 16.648 6.284  1.000 43.10  ? 97  LYS A DZ2  1 
ATOM   1740 D DZ3  . LYS A 1 98  ? 13.118 15.623 5.001  1.000 39.88  ? 97  LYS A DZ3  1 
ATOM   1741 N N    . ILE A 1 99  ? 18.784 13.154 9.328  1.000 11.24  ? 98  ILE A N    1 
ATOM   1742 C CA   . ILE A 1 99  ? 19.877 12.518 8.587  1.000 12.39  ? 98  ILE A CA   1 
ATOM   1743 C C    . ILE A 1 99  ? 19.525 11.058 8.343  1.000 15.53  ? 98  ILE A C    1 
ATOM   1744 O O    . ILE A 1 99  ? 19.516 10.575 7.211  1.000 19.18  ? 98  ILE A O    1 
ATOM   1745 C CB   . ILE A 1 99  ? 21.197 12.742 9.320  1.000 12.03  ? 98  ILE A CB   1 
ATOM   1746 C CG1  . ILE A 1 99  ? 21.593 14.220 9.238  1.000 11.99  ? 98  ILE A CG1  1 
ATOM   1747 C CG2  . ILE A 1 99  ? 22.336 11.906 8.737  1.000 15.45  ? 98  ILE A CG2  1 
ATOM   1748 C CD1  . ILE A 1 99  ? 22.732 14.643 10.107 1.000 15.46  ? 98  ILE A CD1  1 
ATOM   1749 H H    . ILE A 1 99  ? 18.972 13.650 10.187 1.000 13.06  ? 98  ILE A H    1 
ATOM   1750 D DA   . ILE A 1 99  ? 19.945 12.959 7.583  1.000 13.01  ? 98  ILE A DA   1 
ATOM   1751 D DB   . ILE A 1 99  ? 21.081 12.474 10.372 1.000 12.51  ? 98  ILE A DB   1 
ATOM   1752 D DG12 . ILE A 1 99  ? 21.821 14.416 8.184  1.000 16.03  ? 98  ILE A DG12 1 
ATOM   1753 D DG13 . ILE A 1 99  ? 20.705 14.810 9.491  1.000 13.33  ? 98  ILE A DG13 1 
ATOM   1754 D DG21 . ILE A 1 99  ? 22.522 12.143 7.719  1.000 20.56  ? 98  ILE A DG21 1 
ATOM   1755 D DG22 . ILE A 1 99  ? 23.223 12.028 9.298  1.000 21.10  ? 98  ILE A DG22 1 
ATOM   1756 D DG23 . ILE A 1 99  ? 22.094 10.865 8.766  1.000 20.23  ? 98  ILE A DG23 1 
ATOM   1757 D DD11 . ILE A 1 99  ? 23.611 14.096 9.888  1.000 21.93  ? 98  ILE A DD11 1 
ATOM   1758 D DD12 . ILE A 1 99  ? 22.919 15.687 10.015 1.000 18.38  ? 98  ILE A DD12 1 
ATOM   1759 D DD13 . ILE A 1 99  ? 22.508 14.453 11.139 1.000 20.85  ? 98  ILE A DD13 1 
ATOM   1760 N N    A VAL A 1 100 ? 19.204 10.356 9.422  0.627 15.40  ? 99  VAL A N    1 
ATOM   1761 N N    B VAL A 1 100 ? 19.171 10.298 9.384  0.373 15.85  ? 99  VAL A N    1 
ATOM   1762 C CA   A VAL A 1 100 ? 18.855 8.946  9.263  0.627 17.75  ? 99  VAL A CA   1 
ATOM   1763 C CA   B VAL A 1 100 ? 18.910 8.877  9.156  0.373 17.99  ? 99  VAL A CA   1 
ATOM   1764 C C    A VAL A 1 100 ? 17.673 8.766  8.312  0.627 19.92  ? 99  VAL A C    1 
ATOM   1765 C C    B VAL A 1 100 ? 17.508 8.594  8.597  0.373 20.34  ? 99  VAL A C    1 
ATOM   1766 O O    A VAL A 1 100 ? 17.698 7.896  7.436  0.627 23.83  ? 99  VAL A O    1 
ATOM   1767 O O    B VAL A 1 100 ? 17.218 7.433  8.266  0.373 23.23  ? 99  VAL A O    1 
ATOM   1768 C CB   A VAL A 1 100 ? 18.681 8.365  10.681 0.627 18.52  ? 99  VAL A CB   1 
ATOM   1769 C CB   B VAL A 1 100 ? 19.184 8.060  10.436 0.373 19.09  ? 99  VAL A CB   1 
ATOM   1770 C CG1  A VAL A 1 100 ? 18.152 6.945  10.672 0.627 20.16  ? 99  VAL A CG1  1 
ATOM   1771 C CG1  B VAL A 1 100 ? 20.578 8.363  11.011 0.373 19.31  ? 99  VAL A CG1  1 
ATOM   1772 C CG2  A VAL A 1 100 ? 20.042 8.438  11.356 0.627 18.79  ? 99  VAL A CG2  1 
ATOM   1773 C CG2  B VAL A 1 100 ? 18.181 8.313  11.526 0.373 19.11  ? 99  VAL A CG2  1 
ATOM   1774 H H    A VAL A 1 100 ? 19.202 10.787 10.335 0.627 12.94  ? 99  VAL A H    1 
ATOM   1775 H H    B VAL A 1 100 ? 19.085 10.696 10.308 0.373 167.91 ? 99  VAL A H    1 
ATOM   1776 D DA   A VAL A 1 100 ? 19.716 8.410  8.837  0.627 21.26  ? 99  VAL A DA   1 
ATOM   1777 D DA   B VAL A 1 100 ? 19.611 8.557  8.372  0.373 19.83  ? 99  VAL A DA   1 
ATOM   1778 D DB   A VAL A 1 100 ? 17.973 9.007  11.227 0.627 19.71  ? 99  VAL A DB   1 
ATOM   1779 D DB   B VAL A 1 100 ? 19.172 6.991  10.150 0.373 21.39  ? 99  VAL A DB   1 
ATOM   1780 D DG11 A VAL A 1 100 ? 17.394 6.839  9.936  0.627 24.95  ? 99  VAL A DG11 1 
ATOM   1781 D DG11 B VAL A 1 100 ? 21.272 8.402  10.214 0.373 19.18  ? 99  VAL A DG11 1 
ATOM   1782 D DG12 A VAL A 1 100 ? 18.946 6.266  10.432 0.627 26.23  ? 99  VAL A DG12 1 
ATOM   1783 D DG12 B VAL A 1 100 ? 20.544 9.262  11.555 0.373 20.37  ? 99  VAL A DG12 1 
ATOM   1784 D DG13 A VAL A 1 100 ? 17.771 6.685  11.605 0.627 23.97  ? 99  VAL A DG13 1 
ATOM   1785 D DG13 B VAL A 1 100 ? 20.828 7.582  11.698 0.373 20.37  ? 99  VAL A DG13 1 
ATOM   1786 D DG21 A VAL A 1 100 ? 20.764 7.893  10.758 0.627 22.96  ? 99  VAL A DG21 1 
ATOM   1787 D DG21 B VAL A 1 100 ? 18.062 9.349  11.725 0.373 20.09  ? 99  VAL A DG21 1 
ATOM   1788 D DG22 A VAL A 1 100 ? 20.398 9.437  11.380 0.627 22.39  ? 99  VAL A DG22 1 
ATOM   1789 D DG22 B VAL A 1 100 ? 17.225 7.919  11.276 0.373 20.82  ? 99  VAL A DG22 1 
ATOM   1790 D DG23 A VAL A 1 100 ? 20.038 8.039  12.312 0.627 23.81  ? 99  VAL A DG23 1 
ATOM   1791 D DG23 B VAL A 1 100 ? 18.483 7.867  12.448 0.373 21.71  ? 99  VAL A DG23 1 
ATOM   1792 N N    . SER A 1 101 ? 16.650 9.592  8.441  1.000 20.07  ? 100 SER A N    1 
ATOM   1793 C CA   . SER A 1 101 ? 15.374 9.566  7.747  1.000 23.41  ? 100 SER A CA   1 
ATOM   1794 C C    . SER A 1 101 ? 15.475 9.910  6.243  1.000 23.89  ? 100 SER A C    1 
ATOM   1795 O O    . SER A 1 101 ? 14.538 9.602  5.500  1.000 25.52  ? 100 SER A O    1 
ATOM   1796 C CB   . SER A 1 101 ? 14.403 10.618 8.278  1.000 28.18  ? 100 SER A CB   1 
ATOM   1797 O OG   . SER A 1 101 ? 13.204 10.650 7.532  1.000 31.36  ? 100 SER A OG   1 
ATOM   1798 D D    . SER A 1 101 ? 16.770 10.379 9.081  1.000 21.80  ? 100 SER A D    1 
ATOM   1799 D DA   . SER A 1 101 ? 14.929 8.575  7.737  1.000 29.59  ? 100 SER A DA   1 
ATOM   1800 D DB2  . SER A 1 101 ? 14.212 10.525 9.338  1.000 31.80  ? 100 SER A DB2  1 
ATOM   1801 D DB3  . SER A 1 101 ? 14.840 11.618 8.088  1.000 35.94  ? 100 SER A DB3  1 
ATOM   1802 D DG   . SER A 1 101 ? 13.317 11.289 6.788  1.000 104.50 ? 100 SER A DG   1 
ATOM   1803 N N    . ASP A 1 102 ? 16.552 10.602 5.889  1.000 21.31  ? 101 ASP A N    1 
ATOM   1804 C CA   . ASP A 1 102 ? 16.717 11.081 4.508  1.000 22.85  ? 101 ASP A CA   1 
ATOM   1805 C C    . ASP A 1 102 ? 17.600 10.122 3.716  1.000 26.42  ? 101 ASP A C    1 
ATOM   1806 O O    . ASP A 1 102 ? 18.276 10.480 2.761  1.000 33.12  ? 101 ASP A O    1 
ATOM   1807 C CB   . ASP A 1 102 ? 17.304 12.472 4.421  1.000 22.30  ? 101 ASP A CB   1 
ATOM   1808 C CG   . ASP A 1 102 ? 16.318 13.554 3.995  1.000 19.36  ? 101 ASP A CG   1 
ATOM   1809 O OD1  . ASP A 1 102 ? 15.210 13.235 3.568  1.000 21.50  ? 101 ASP A OD1  1 
ATOM   1810 O OD2  . ASP A 1 102 ? 16.765 14.726 4.104  1.000 20.15  ? 101 ASP A OD2  1 
ATOM   1811 D D    . ASP A 1 102 ? 17.235 10.846 6.568  1.000 23.17  ? 101 ASP A D    1 
ATOM   1812 D DA   . ASP A 1 102 ? 15.709 11.086 4.031  1.000 25.30  ? 101 ASP A DA   1 
ATOM   1813 D DB2  . ASP A 1 102 ? 17.735 12.742 5.357  1.000 25.72  ? 101 ASP A DB2  1 
ATOM   1814 D DB3  . ASP A 1 102 ? 18.077 12.442 3.617  1.000 29.54  ? 101 ASP A DB3  1 
ATOM   1815 D DD2  . ASP A 1 102 ? 16.265 15.296 3.460  1.000 18.95  ? 101 ASP A DD2  1 
ATOM   1816 N N    . GLY A 1 103 ? 17.534 8.876  4.135  1.000 28.47  ? 102 GLY A N    1 
ATOM   1817 C CA   . GLY A 1 103 ? 18.126 7.762  3.418  1.000 31.65  ? 102 GLY A CA   1 
ATOM   1818 C C    . GLY A 1 103 ? 19.335 7.148  4.073  1.000 33.40  ? 102 GLY A C    1 
ATOM   1819 O O    . GLY A 1 103 ? 19.616 5.941  3.948  1.000 34.44  ? 102 GLY A O    1 
ATOM   1820 D D    . GLY A 1 103 ? 17.035 8.701  5.002  1.000 32.64  ? 102 GLY A D    1 
ATOM   1821 D DA2  . GLY A 1 103 ? 17.374 6.982  3.343  1.000 42.45  ? 102 GLY A DA2  1 
ATOM   1822 D DA3  . GLY A 1 103 ? 18.390 8.111  2.420  1.000 39.48  ? 102 GLY A DA3  1 
ATOM   1823 N N    . ASN A 1 104 ? 20.056 7.986  4.788  1.000 31.37  ? 103 ASN A N    1 
ATOM   1824 C CA   . ASN A 1 104 ? 21.320 7.597  5.389  1.000 30.00  ? 103 ASN A CA   1 
ATOM   1825 C C    . ASN A 1 104 ? 20.968 6.648  6.520  1.000 27.41  ? 103 ASN A C    1 
ATOM   1826 O O    . ASN A 1 104 ? 19.874 6.710  7.087  1.000 32.86  ? 103 ASN A O    1 
ATOM   1827 C CB   . ASN A 1 104 ? 22.004 8.878  5.835  1.000 32.45  ? 103 ASN A CB   1 
ATOM   1828 C CG   . ASN A 1 104 ? 22.155 9.761  4.612  1.000 34.38  ? 103 ASN A CG   1 
ATOM   1829 O OD1  . ASN A 1 104 ? 23.038 9.577  3.783  1.000 38.15  ? 103 ASN A OD1  1 
ATOM   1830 N ND2  . ASN A 1 104 ? 21.220 10.693 4.539  1.000 37.19  ? 103 ASN A ND2  1 
ATOM   1831 D D    . ASN A 1 104 ? 19.747 8.937  4.939  1.000 49.33  ? 103 ASN A D    1 
ATOM   1832 D DA   . ASN A 1 104 ? 21.854 7.141  4.529  1.000 32.19  ? 103 ASN A DA   1 
ATOM   1833 D DB2  . ASN A 1 104 ? 21.391 9.386  6.586  1.000 32.71  ? 103 ASN A DB2  1 
ATOM   1834 D DB3  . ASN A 1 104 ? 22.951 8.677  6.296  1.000 36.45  ? 103 ASN A DB3  1 
ATOM   1835 D DD21 . ASN A 1 104 ? 21.188 11.280 3.708  1.000 29.12  ? 103 ASN A DD21 1 
ATOM   1836 D DD22 . ASN A 1 104 ? 20.549 10.750 5.302  1.000 37.55  ? 103 ASN A DD22 1 
ATOM   1837 N N    . GLY A 1 105 ? 21.867 5.770  6.873  1.000 25.17  ? 104 GLY A N    1 
ATOM   1838 C CA   . GLY A 1 105 ? 21.964 5.181  8.181  1.000 20.34  ? 104 GLY A CA   1 
ATOM   1839 C C    . GLY A 1 105 ? 22.910 5.976  9.045  1.000 16.23  ? 104 GLY A C    1 
ATOM   1840 O O    . GLY A 1 105 ? 23.310 7.098  8.777  1.000 18.77  ? 104 GLY A O    1 
ATOM   1841 D D    . GLY A 1 105 ? 22.544 5.514  6.149  1.000 26.78  ? 104 GLY A D    1 
ATOM   1842 D DA2  . GLY A 1 105 ? 21.051 5.086  8.723  1.000 24.37  ? 104 GLY A DA2  1 
ATOM   1843 D DA3  . GLY A 1 105 ? 22.336 4.170  8.041  1.000 25.61  ? 104 GLY A DA3  1 
ATOM   1844 N N    . MET A 1 106 ? 23.336 5.332  10.109 1.000 12.96  ? 105 MET A N    1 
ATOM   1845 C CA   . MET A 1 106 ? 24.339 5.941  10.942 1.000 11.94  ? 105 MET A CA   1 
ATOM   1846 C C    . MET A 1 106 ? 25.706 5.921  10.274 1.000 12.72  ? 105 MET A C    1 
ATOM   1847 O O    . MET A 1 106 ? 26.634 6.543  10.779 1.000 12.15  ? 105 MET A O    1 
ATOM   1848 C CB   . MET A 1 106 ? 24.410 5.294  12.340 1.000 11.72  ? 105 MET A CB   1 
ATOM   1849 C CG   . MET A 1 106 ? 23.207 5.683  13.185 1.000 11.26  ? 105 MET A CG   1 
ATOM   1850 S SD   . MET A 1 106 ? 23.366 5.408  14.959 1.000 12.81  ? 105 MET A SD   1 
ATOM   1851 C CE   . MET A 1 106 ? 24.533 6.669  15.439 1.000 15.50  ? 105 MET A CE   1 
ATOM   1852 D D    . MET A 1 106 ? 23.008 4.382  10.256 1.000 15.26  ? 105 MET A D    1 
ATOM   1853 D DA   . MET A 1 106 ? 24.101 7.012  11.021 1.000 12.98  ? 105 MET A DA   1 
ATOM   1854 D DB2  . MET A 1 106 ? 24.462 4.222  12.236 1.000 13.35  ? 105 MET A DB2  1 
ATOM   1855 D DB3  . MET A 1 106 ? 25.326 5.639  12.805 1.000 13.61  ? 105 MET A DB3  1 
ATOM   1856 D DG2  . MET A 1 106 ? 23.024 6.757  13.076 1.000 12.54  ? 105 MET A DG2  1 
ATOM   1857 D DG3  . MET A 1 106 ? 22.309 5.177  12.860 1.000 13.03  ? 105 MET A DG3  1 
ATOM   1858 D DE1  . MET A 1 106 ? 24.732 6.570  16.465 1.000 22.20  ? 105 MET A DE1  1 
ATOM   1859 D DE2  . MET A 1 106 ? 25.407 6.563  14.848 1.000 19.08  ? 105 MET A DE2  1 
ATOM   1860 D DE3  . MET A 1 106 ? 24.138 7.615  15.205 1.000 20.36  ? 105 MET A DE3  1 
ATOM   1861 N N    A ASN A 1 107 ? 25.868 5.181  9.186  0.488 15.55  ? 106 ASN A N    1 
ATOM   1862 N N    B ASN A 1 107 ? 25.830 5.329  9.084  0.512 15.43  ? 106 ASN A N    1 
ATOM   1863 C CA   A ASN A 1 107 ? 27.007 5.301  8.289  0.488 18.42  ? 106 ASN A CA   1 
ATOM   1864 C CA   B ASN A 1 107 ? 27.091 5.372  8.370  0.512 17.44  ? 106 ASN A CA   1 
ATOM   1865 C C    A ASN A 1 107 ? 27.377 6.744  7.955  0.488 18.19  ? 106 ASN A C    1 
ATOM   1866 C C    B ASN A 1 107 ? 27.418 6.796  7.937  0.512 15.96  ? 106 ASN A C    1 
ATOM   1867 O O    A ASN A 1 107 ? 28.562 6.955  7.665  0.488 20.88  ? 106 ASN A O    1 
ATOM   1868 O O    B ASN A 1 107 ? 28.553 7.057  7.554  0.512 18.95  ? 106 ASN A O    1 
ATOM   1869 C CB   A ASN A 1 107 ? 26.755 4.488  7.007  0.488 20.64  ? 106 ASN A CB   1 
ATOM   1870 C CB   B ASN A 1 107 ? 27.162 4.471  7.133  0.512 20.32  ? 106 ASN A CB   1 
ATOM   1871 C CG   A ASN A 1 107 ? 28.022 4.268  6.208  0.488 20.20  ? 106 ASN A CG   1 
ATOM   1872 C CG   B ASN A 1 107 ? 27.554 3.085  7.555  0.512 21.57  ? 106 ASN A CG   1 
ATOM   1873 O OD1  A ASN A 1 107 ? 28.987 3.684  6.690  0.488 24.31  ? 106 ASN A OD1  1 
ATOM   1874 O OD1  B ASN A 1 107 ? 27.977 2.894  8.699  0.512 27.28  ? 106 ASN A OD1  1 
ATOM   1875 N ND2  A ASN A 1 107 ? 28.008 4.754  4.974  0.488 29.10  ? 106 ASN A ND2  1 
ATOM   1876 N ND2  B ASN A 1 107 ? 27.466 2.093  6.687  0.512 26.50  ? 106 ASN A ND2  1 
ATOM   1877 D D    A ASN A 1 107 ? 25.166 4.487  8.971  0.488 20.43  ? 106 ASN A D    1 
ATOM   1878 D D    B ASN A 1 107 ? 25.027 4.883  8.669  0.512 20.16  ? 106 ASN A D    1 
ATOM   1879 D DA   A ASN A 1 107 ? 27.874 4.875  8.819  0.488 17.60  ? 106 ASN A DA   1 
ATOM   1880 D DA   B ASN A 1 107 ? 27.864 5.058  9.090  0.512 16.97  ? 106 ASN A DA   1 
ATOM   1881 D DB2  A ASN A 1 107 ? 26.340 3.515  7.298  0.488 23.84  ? 106 ASN A DB2  1 
ATOM   1882 D DB2  B ASN A 1 107 ? 26.217 4.482  6.611  0.512 21.71  ? 106 ASN A DB2  1 
ATOM   1883 D DB3  A ASN A 1 107 ? 26.020 5.023  6.401  0.488 22.42  ? 106 ASN A DB3  1 
ATOM   1884 D DB3  B ASN A 1 107 ? 27.888 4.886  6.437  0.512 22.49  ? 106 ASN A DB3  1 
ATOM   1885 D DD21 A ASN A 1 107 ? 28.877 5.063  4.565  0.488 34.93  ? 106 ASN A DD21 1 
ATOM   1886 D DD21 B ASN A 1 107 ? 28.056 1.274  6.848  0.512 31.79  ? 106 ASN A DD21 1 
ATOM   1887 D DD22 A ASN A 1 107 ? 27.125 4.784  4.484  0.488 34.93  ? 106 ASN A DD22 1 
ATOM   1888 D DD22 B ASN A 1 107 ? 26.826 2.195  5.907  0.512 31.79  ? 106 ASN A DD22 1 
ATOM   1889 N N    . ALA A 1 108 ? 26.452 7.692  7.984  1.000 15.16  ? 107 ALA A N    1 
ATOM   1890 C CA   . ALA A 1 108 ? 26.702 9.106  7.762  1.000 14.50  ? 107 ALA A CA   1 
ATOM   1891 C C    . ALA A 1 108 ? 27.752 9.691  8.700  1.000 13.84  ? 107 ALA A C    1 
ATOM   1892 O O    . ALA A 1 108 ? 28.444 10.640 8.355  1.000 16.09  ? 107 ALA A O    1 
ATOM   1893 C CB   . ALA A 1 108 ? 25.420 9.914  7.915  1.000 16.41  ? 107 ALA A CB   1 
ATOM   1894 D D    . ALA A 1 108 ? 25.515 7.394  8.279  1.000 16.56  ? 107 ALA A D    1 
ATOM   1895 D DA   . ALA A 1 108 ? 27.107 9.267  6.752  1.000 18.76  ? 107 ALA A DA   1 
ATOM   1896 D DB1  . ALA A 1 108 ? 25.016 9.803  8.883  1.000 19.78  ? 107 ALA A DB1  1 
ATOM   1897 D DB2  . ALA A 1 108 ? 25.621 10.942 7.753  1.000 20.47  ? 107 ALA A DB2  1 
ATOM   1898 D DB3  . ALA A 1 108 ? 24.701 9.606  7.210  1.000 23.19  ? 107 ALA A DB3  1 
ATOM   1899 N N    . TRP A 1 109 ? 27.886 9.131  9.887  1.000 11.23  ? 108 TRP A N    1 
ATOM   1900 C CA   . TRP A 1 109 ? 28.862 9.563  10.876 1.000 10.81  ? 108 TRP A CA   1 
ATOM   1901 C C    . TRP A 1 109 ? 30.111 8.709  10.785 1.000 10.89  ? 108 TRP A C    1 
ATOM   1902 O O    . TRP A 1 109 ? 30.083 7.523  11.090 1.000 11.06  ? 108 TRP A O    1 
ATOM   1903 C CB   . TRP A 1 109 ? 28.311 9.468  12.303 1.000 10.82  ? 108 TRP A CB   1 
ATOM   1904 C CG   . TRP A 1 109 ? 27.335 10.557 12.577 1.000 10.64  ? 108 TRP A CG   1 
ATOM   1905 C CD1  . TRP A 1 109 ? 27.652 11.832 12.998 1.000 11.96  ? 108 TRP A CD1  1 
ATOM   1906 C CD2  . TRP A 1 109 ? 25.919 10.538 12.466 1.000 9.87   ? 108 TRP A CD2  1 
ATOM   1907 N NE1  . TRP A 1 109 ? 26.495 12.571 13.150 1.000 12.07  ? 108 TRP A NE1  1 
ATOM   1908 C CE2  . TRP A 1 109 ? 25.428 11.805 12.826 1.000 9.98   ? 108 TRP A CE2  1 
ATOM   1909 C CE3  . TRP A 1 109 ? 24.999 9.552  12.080 1.000 11.78  ? 108 TRP A CE3  1 
ATOM   1910 C CZ2  . TRP A 1 109 ? 24.065 12.090 12.816 1.000 11.96  ? 108 TRP A CZ2  1 
ATOM   1911 C CZ3  . TRP A 1 109 ? 23.647 9.824  12.070 1.000 13.11  ? 108 TRP A CZ3  1 
ATOM   1912 C CH2  . TRP A 1 109 ? 23.197 11.104 12.434 1.000 12.64  ? 108 TRP A CH2  1 
ATOM   1913 H H    A TRP A 1 109 ? 27.278 8.359  10.122 0.525 9.12   ? 108 TRP A H    1 
ATOM   1914 D D    B TRP A 1 109 ? 27.279 8.353  10.135 0.475 12.74  ? 108 TRP A D    1 
ATOM   1915 D DA   . TRP A 1 109 ? 29.160 10.586 10.606 1.000 12.64  ? 108 TRP A DA   1 
ATOM   1916 D DB2  . TRP A 1 109 ? 27.866 8.500  12.434 1.000 11.57  ? 108 TRP A DB2  1 
ATOM   1917 D DB3  . TRP A 1 109 ? 29.133 9.595  13.002 1.000 13.59  ? 108 TRP A DB3  1 
ATOM   1918 D DD1  . TRP A 1 109 ? 28.640 12.250 13.187 1.000 16.23  ? 108 TRP A DD1  1 
ATOM   1919 D DE1  . TRP A 1 109 ? 26.495 13.547 13.442 1.000 14.04  ? 108 TRP A DE1  1 
ATOM   1920 D DE3  . TRP A 1 109 ? 25.361 8.590  11.747 1.000 14.61  ? 108 TRP A DE3  1 
ATOM   1921 D DZ2  . TRP A 1 109 ? 23.731 13.072 13.112 1.000 15.61  ? 108 TRP A DZ2  1 
ATOM   1922 D DZ3  . TRP A 1 109 ? 22.942 9.085  11.754 1.000 18.78  ? 108 TRP A DZ3  1 
ATOM   1923 D DH2  . TRP A 1 109 ? 22.126 11.293 12.366 1.000 14.71  ? 108 TRP A DH2  1 
ATOM   1924 N N    . VAL A 1 110 ? 31.217 9.317  10.314 1.000 10.62  ? 109 VAL A N    1 
ATOM   1925 C CA   . VAL A 1 110 ? 32.460 8.597  10.119 1.000 12.43  ? 109 VAL A CA   1 
ATOM   1926 C C    . VAL A 1 110 ? 32.911 7.960  11.430 1.000 10.58  ? 109 VAL A C    1 
ATOM   1927 O O    . VAL A 1 110 ? 33.406 6.816  11.395 1.000 12.13  ? 109 VAL A O    1 
ATOM   1928 C CB   . VAL A 1 110 ? 33.515 9.509  9.506  1.000 17.49  ? 109 VAL A CB   1 
ATOM   1929 C CG1  . VAL A 1 110 ? 33.990 10.579 10.461 1.000 20.95  ? 109 VAL A CG1  1 
ATOM   1930 C CG2  . VAL A 1 110 ? 34.754 8.716  9.126  1.000 21.46  ? 109 VAL A CG2  1 
ATOM   1931 D D    . VAL A 1 110 ? 31.137 10.311 10.079 1.000 12.63  ? 109 VAL A D    1 
ATOM   1932 D DA   . VAL A 1 110 ? 32.283 7.731  9.446  1.000 14.48  ? 109 VAL A DA   1 
ATOM   1933 D DB   . VAL A 1 110 ? 33.112 9.992  8.590  1.000 22.55  ? 109 VAL A DB   1 
ATOM   1934 D DG11 . VAL A 1 110 ? 34.484 10.129 11.296 1.000 26.02  ? 109 VAL A DG11 1 
ATOM   1935 D DG12 . VAL A 1 110 ? 34.699 11.218 9.962  1.000 28.63  ? 109 VAL A DG12 1 
ATOM   1936 D DG13 . VAL A 1 110 ? 33.190 11.162 10.815 1.000 24.91  ? 109 VAL A DG13 1 
ATOM   1937 D DG21 . VAL A 1 110 ? 35.254 8.389  10.023 1.000 25.90  ? 109 VAL A DG21 1 
ATOM   1938 D DG22 . VAL A 1 110 ? 34.486 7.856  8.557  1.000 30.79  ? 109 VAL A DG22 1 
ATOM   1939 D DG23 . VAL A 1 110 ? 35.432 9.330  8.568  1.000 26.80  ? 109 VAL A DG23 1 
ATOM   1940 N N    . ALA A 1 111 ? 32.750 8.621  12.567 1.000 10.56  ? 110 ALA A N    1 
ATOM   1941 C CA   . ALA A 1 111 ? 33.196 7.997  13.815 1.000 11.88  ? 110 ALA A CA   1 
ATOM   1942 C C    . ALA A 1 111 ? 32.335 6.805  14.205 1.000 11.17  ? 110 ALA A C    1 
ATOM   1943 O O    . ALA A 1 111 ? 32.827 5.848  14.797 1.000 12.57  ? 110 ALA A O    1 
ATOM   1944 C CB   . ALA A 1 111 ? 33.220 9.029  14.920 1.000 14.90  ? 110 ALA A CB   1 
ATOM   1945 D D    . ALA A 1 111 ? 32.383 9.572  12.599 1.000 11.92  ? 110 ALA A D    1 
ATOM   1946 D DA   . ALA A 1 111 ? 34.215 7.637  13.636 1.000 14.39  ? 110 ALA A DA   1 
ATOM   1947 D DB1  . ALA A 1 111 ? 32.261 9.425  15.117 1.000 16.48  ? 110 ALA A DB1  1 
ATOM   1948 D DB2  . ALA A 1 111 ? 33.668 8.597  15.796 1.000 20.92  ? 110 ALA A DB2  1 
ATOM   1949 D DB3  . ALA A 1 111 ? 33.804 9.861  14.627 1.000 18.52  ? 110 ALA A DB3  1 
ATOM   1950 N N    . TRP A 1 112 ? 31.059 6.837  13.859 1.000 10.55  ? 111 TRP A N    1 
ATOM   1951 C CA   . TRP A 1 112 ? 30.233 5.661  14.154 1.000 11.58  ? 111 TRP A CA   1 
ATOM   1952 C C    . TRP A 1 112 ? 30.728 4.457  13.337 1.000 11.32  ? 111 TRP A C    1 
ATOM   1953 O O    . TRP A 1 112 ? 30.948 3.369  13.876 1.000 12.23  ? 111 TRP A O    1 
ATOM   1954 C CB   . TRP A 1 112 ? 28.734 5.936  13.927 1.000 11.80  ? 111 TRP A CB   1 
ATOM   1955 C CG   . TRP A 1 112 ? 27.931 4.713  14.234 1.000 11.43  ? 111 TRP A CG   1 
ATOM   1956 C CD1  . TRP A 1 112 ? 27.442 4.312  15.447 1.000 11.84  ? 111 TRP A CD1  1 
ATOM   1957 C CD2  . TRP A 1 112 ? 27.532 3.696  13.294 1.000 11.78  ? 111 TRP A CD2  1 
ATOM   1958 N NE1  . TRP A 1 112 ? 26.767 3.130  15.353 1.000 12.36  ? 111 TRP A NE1  1 
ATOM   1959 C CE2  . TRP A 1 112 ? 26.809 2.741  14.036 1.000 12.30  ? 111 TRP A CE2  1 
ATOM   1960 C CE3  . TRP A 1 112 ? 27.698 3.497  11.921 1.000 13.50  ? 111 TRP A CE3  1 
ATOM   1961 C CZ2  . TRP A 1 112 ? 26.265 1.604  13.430 1.000 14.52  ? 111 TRP A CZ2  1 
ATOM   1962 C CZ3  . TRP A 1 112 ? 27.153 2.372  11.315 1.000 14.84  ? 111 TRP A CZ3  1 
ATOM   1963 C CH2  . TRP A 1 112 ? 26.436 1.442  12.084 1.000 15.81  ? 111 TRP A CH2  1 
ATOM   1964 H H    A TRP A 1 112 ? 30.664 7.648  13.404 0.860 22.67  ? 111 TRP A H    1 
ATOM   1965 D D    B TRP A 1 112 ? 30.602 7.708  13.632 0.140 12.62  ? 111 TRP A D    1 
ATOM   1966 D DA   . TRP A 1 112 ? 30.390 5.412  15.200 1.000 13.28  ? 111 TRP A DA   1 
ATOM   1967 D DB2  . TRP A 1 112 ? 28.491 6.789  14.529 1.000 13.89  ? 111 TRP A DB2  1 
ATOM   1968 D DB3  . TRP A 1 112 ? 28.598 6.220  12.883 1.000 12.88  ? 111 TRP A DB3  1 
ATOM   1969 D DD1  . TRP A 1 112 ? 27.517 4.850  16.396 1.000 14.63  ? 111 TRP A DD1  1 
ATOM   1970 D DE1  . TRP A 1 112 ? 26.303 2.631  16.095 1.000 16.33  ? 111 TRP A DE1  1 
ATOM   1971 D DE3  . TRP A 1 112 ? 28.201 4.242  11.330 1.000 15.65  ? 111 TRP A DE3  1 
ATOM   1972 D DZ2  . TRP A 1 112 ? 25.705 0.902  14.035 1.000 17.70  ? 111 TRP A DZ2  1 
ATOM   1973 D DZ3  . TRP A 1 112 ? 27.238 2.238  10.258 1.000 17.69  ? 111 TRP A DZ3  1 
ATOM   1974 D DH2  . TRP A 1 112 ? 25.977 0.601  11.562 1.000 19.33  ? 111 TRP A DH2  1 
ATOM   1975 N N    . ARG A 1 113 ? 30.923 4.677  12.029 1.000 11.24  ? 112 ARG A N    1 
ATOM   1976 C CA   . ARG A 1 113 ? 31.361 3.607  11.133 1.000 13.42  ? 112 ARG A CA   1 
ATOM   1977 C C    . ARG A 1 113 ? 32.708 3.039  11.531 1.000 13.83  ? 112 ARG A C    1 
ATOM   1978 O O    . ARG A 1 113 ? 32.919 1.829  11.414 1.000 18.60  ? 112 ARG A O    1 
ATOM   1979 C CB   . ARG A 1 113 ? 31.372 4.187  9.728  1.000 19.55  ? 112 ARG A CB   1 
ATOM   1980 C CG   . ARG A 1 113 ? 31.661 3.166  8.637  1.000 28.43  ? 112 ARG A CG   1 
ATOM   1981 C CD   . ARG A 1 113 ? 31.948 3.925  7.346  1.000 35.26  ? 112 ARG A CD   1 
ATOM   1982 N NE   . ARG A 1 113 ? 31.203 5.168  7.299  1.000 40.20  ? 112 ARG A NE   1 
ATOM   1983 C CZ   . ARG A 1 113 ? 31.638 6.276  6.731  1.000 43.74  ? 112 ARG A CZ   1 
ATOM   1984 N NH1  . ARG A 1 113 ? 30.940 7.391  6.908  1.000 44.38  ? 112 ARG A NH1  1 
ATOM   1985 N NH2  . ARG A 1 113 ? 32.741 6.283  6.007  1.000 45.02  ? 112 ARG A NH2  1 
ATOM   1986 H H    . ARG A 1 113 ? 30.763 5.601  11.654 1.000 53.95  ? 112 ARG A H    1 
ATOM   1987 D DA   . ARG A 1 113 ? 30.652 2.786  11.237 1.000 15.53  ? 112 ARG A DA   1 
ATOM   1988 D DB2  . ARG A 1 113 ? 30.375 4.610  9.517  1.000 27.59  ? 112 ARG A DB2  1 
ATOM   1989 D DB3  . ARG A 1 113 ? 32.126 4.966  9.654  1.000 22.56  ? 112 ARG A DB3  1 
ATOM   1990 D DG2  . ARG A 1 113 ? 32.543 2.616  8.920  1.000 33.21  ? 112 ARG A DG2  1 
ATOM   1991 D DG3  . ARG A 1 113 ? 30.766 2.573  8.491  1.000 35.98  ? 112 ARG A DG3  1 
ATOM   1992 D DD2  . ARG A 1 113 ? 33.002 4.211  7.355  1.000 44.64  ? 112 ARG A DD2  1 
ATOM   1993 D DD3  . ARG A 1 113 ? 31.704 3.323  6.485  1.000 49.19  ? 112 ARG A DD3  1 
ATOM   1994 D DE   . ARG A 1 113 ? 30.321 5.092  7.759  1.000 50.54  ? 112 ARG A DE   1 
ATOM   1995 D DH11 . ARG A 1 113 ? 30.835 8.036  6.137  1.000 38.82  ? 112 ARG A DH11 1 
ATOM   1996 D DH12 . ARG A 1 113 ? 30.508 7.565  7.808  1.000 43.58  ? 112 ARG A DH12 1 
ATOM   1997 D DH21 . ARG A 1 113 ? 33.111 7.158  5.660  1.000 56.78  ? 112 ARG A DH21 1 
ATOM   1998 D DH22 . ARG A 1 113 ? 33.221 5.417  5.806  1.000 53.78  ? 112 ARG A DH22 1 
ATOM   1999 N N    . ASN A 1 114 ? 33.625 3.912  11.960 1.000 13.29  ? 113 ASN A N    1 
ATOM   2000 C CA   . ASN A 1 114 ? 34.990 3.484  12.234 1.000 14.95  ? 113 ASN A CA   1 
ATOM   2001 C C    . ASN A 1 114 ? 35.217 3.071  13.680 1.000 14.96  ? 113 ASN A C    1 
ATOM   2002 O O    . ASN A 1 114 ? 36.222 2.386  13.947 1.000 19.30  ? 113 ASN A O    1 
ATOM   2003 C CB   . ASN A 1 114 ? 35.975 4.579  11.789 1.000 18.26  ? 113 ASN A CB   1 
ATOM   2004 C CG   . ASN A 1 114 ? 35.993 4.755  10.280 1.000 23.18  ? 113 ASN A CG   1 
ATOM   2005 O OD1  . ASN A 1 114 ? 35.509 3.950  9.492  1.000 25.85  ? 113 ASN A OD1  1 
ATOM   2006 N ND2  . ASN A 1 114 ? 36.562 5.894  9.906  1.000 27.12  ? 113 ASN A ND2  1 
ATOM   2007 D D    . ASN A 1 114 ? 33.399 4.894  12.026 1.000 13.85  ? 113 ASN A D    1 
ATOM   2008 D DA   . ASN A 1 114 ? 35.230 2.651  11.569 1.000 16.74  ? 113 ASN A DA   1 
ATOM   2009 D DB2  . ASN A 1 114 ? 35.680 5.521  12.260 1.000 19.58  ? 113 ASN A DB2  1 
ATOM   2010 D DB3  . ASN A 1 114 ? 36.967 4.314  12.136 1.000 22.28  ? 113 ASN A DB3  1 
ATOM   2011 D DD21 . ASN A 1 114 ? 36.890 5.973  8.954  1.000 52.47  ? 113 ASN A DD21 1 
ATOM   2012 D DD22 . ASN A 1 114 ? 36.643 6.627  10.608 1.000 47.08  ? 113 ASN A DD22 1 
ATOM   2013 N N    A ARG A 1 115 ? 34.395 3.486  14.653 0.613 14.61  ? 114 ARG A N    1 
ATOM   2014 N N    B ARG A 1 115 ? 34.342 3.451  14.606 0.387 14.55  ? 114 ARG A N    1 
ATOM   2015 C CA   A ARG A 1 115 ? 34.685 3.194  16.066 0.613 15.39  ? 114 ARG A CA   1 
ATOM   2016 C CA   B ARG A 1 115 ? 34.645 3.238  16.022 0.387 15.92  ? 114 ARG A CA   1 
ATOM   2017 C C    A ARG A 1 115 ? 33.527 2.592  16.860 0.613 15.53  ? 114 ARG A C    1 
ATOM   2018 C C    B ARG A 1 115 ? 33.597 2.329  16.671 0.387 15.43  ? 114 ARG A C    1 
ATOM   2019 O O    A ARG A 1 115 ? 33.674 2.185  18.019 0.613 17.21  ? 114 ARG A O    1 
ATOM   2020 O O    B ARG A 1 115 ? 33.897 1.487  17.507 0.387 15.13  ? 114 ARG A O    1 
ATOM   2021 C CB   A ARG A 1 115 ? 35.113 4.455  16.829 0.613 16.69  ? 114 ARG A CB   1 
ATOM   2022 C CB   B ARG A 1 115 ? 34.678 4.533  16.827 0.387 17.20  ? 114 ARG A CB   1 
ATOM   2023 C CG   A ARG A 1 115 ? 36.175 5.341  16.201 0.613 18.86  ? 114 ARG A CG   1 
ATOM   2024 C CG   B ARG A 1 115 ? 35.577 5.694  16.484 0.387 18.34  ? 114 ARG A CG   1 
ATOM   2025 C CD   A ARG A 1 115 ? 37.535 4.643  16.321 0.613 21.21  ? 114 ARG A CD   1 
ATOM   2026 C CD   B ARG A 1 115 ? 37.056 5.377  16.337 0.387 20.88  ? 114 ARG A CD   1 
ATOM   2027 N NE   A ARG A 1 115 ? 38.032 4.988  17.654 0.613 21.58  ? 114 ARG A NE   1 
ATOM   2028 N NE   B ARG A 1 115 ? 37.663 4.724  17.490 0.387 21.06  ? 114 ARG A NE   1 
ATOM   2029 C CZ   A ARG A 1 115 ? 38.675 6.011  18.218 0.613 21.74  ? 114 ARG A CZ   1 
ATOM   2030 C CZ   B ARG A 1 115 ? 38.614 5.102  18.338 0.387 22.05  ? 114 ARG A CZ   1 
ATOM   2031 N NH1  A ARG A 1 115 ? 38.654 7.315  18.032 0.613 22.63  ? 114 ARG A NH1  1 
ATOM   2032 N NH1  B ARG A 1 115 ? 38.981 4.236  19.287 0.387 23.22  ? 114 ARG A NH1  1 
ATOM   2033 N NH2  A ARG A 1 115 ? 39.526 5.640  19.191 0.613 23.02  ? 114 ARG A NH2  1 
ATOM   2034 N NH2  B ARG A 1 115 ? 39.253 6.257  18.320 0.387 22.70  ? 114 ARG A NH2  1 
ATOM   2035 D D    A ARG A 1 115 ? 33.617 4.069  14.417 0.613 15.62  ? 114 ARG A D    1 
ATOM   2036 D D    B ARG A 1 115 ? 33.489 3.909  14.340 0.387 19.43  ? 114 ARG A D    1 
ATOM   2037 D DA   A ARG A 1 115 ? 35.481 2.438  16.032 0.613 16.40  ? 114 ARG A DA   1 
ATOM   2038 D DA   B ARG A 1 115 ? 35.616 2.718  16.050 0.387 17.75  ? 114 ARG A DA   1 
ATOM   2039 D DB2  A ARG A 1 115 ? 34.203 5.074  16.937 0.613 16.24  ? 114 ARG A DB2  1 
ATOM   2040 D DB2  B ARG A 1 115 ? 33.634 4.918  16.840 0.387 16.60  ? 114 ARG A DB2  1 
ATOM   2041 D DB3  A ARG A 1 115 ? 35.488 4.143  17.806 0.613 17.50  ? 114 ARG A DB3  1 
ATOM   2042 D DB3  B ARG A 1 115 ? 34.860 4.260  17.879 0.387 19.68  ? 114 ARG A DB3  1 
ATOM   2043 D DG2  A ARG A 1 115 ? 35.936 5.517  15.196 0.613 18.23  ? 114 ARG A DG2  1 
ATOM   2044 D DG2  B ARG A 1 115 ? 35.231 6.137  15.543 0.387 19.41  ? 114 ARG A DG2  1 
ATOM   2045 D DG3  A ARG A 1 115 ? 36.278 6.247  16.872 0.613 17.79  ? 114 ARG A DG3  1 
ATOM   2046 D DG3  B ARG A 1 115 ? 35.483 6.454  17.276 0.387 20.76  ? 114 ARG A DG3  1 
ATOM   2047 D DD2  A ARG A 1 115 ? 37.257 3.591  16.275 0.613 25.01  ? 114 ARG A DD2  1 
ATOM   2048 D DD2  B ARG A 1 115 ? 37.035 4.688  15.469 0.387 17.89  ? 114 ARG A DD2  1 
ATOM   2049 D DD3  A ARG A 1 115 ? 38.187 4.893  15.506 0.613 25.26  ? 114 ARG A DD3  1 
ATOM   2050 D DD3  B ARG A 1 115 ? 37.540 6.331  16.129 0.387 18.87  ? 114 ARG A DD3  1 
ATOM   2051 D DE   A ARG A 1 115 ? 37.839 4.160  18.272 0.613 28.13  ? 114 ARG A DE   1 
ATOM   2052 D DE   B ARG A 1 115 ? 37.245 3.787  17.600 0.387 20.03  ? 114 ARG A DE   1 
ATOM   2053 D DH11 A ARG A 1 115 ? 39.339 7.898  18.510 0.613 24.01  ? 114 ARG A DH11 1 
ATOM   2054 D DH11 B ARG A 1 115 ? 39.489 4.577  20.089 0.387 29.95  ? 114 ARG A DH11 1 
ATOM   2055 D DH12 A ARG A 1 115 ? 37.972 7.740  17.425 0.613 24.68  ? 114 ARG A DH12 1 
ATOM   2056 D DH12 B ARG A 1 115 ? 38.719 3.266  19.184 0.387 28.50  ? 114 ARG A DH12 1 
ATOM   2057 D DH21 A ARG A 1 115 ? 40.151 6.331  19.576 0.613 23.25  ? 114 ARG A DH21 1 
ATOM   2058 D DH21 B ARG A 1 115 ? 38.748 7.124  18.355 0.387 18.99  ? 114 ARG A DH21 1 
ATOM   2059 D DH22 A ARG A 1 115 ? 39.525 4.677  19.479 0.613 28.32  ? 114 ARG A DH22 1 
ATOM   2060 D DH22 B ARG A 1 115 ? 40.271 6.257  18.294 0.387 23.60  ? 114 ARG A DH22 1 
ATOM   2061 N N    . CYS A 1 116 ? 32.342 2.525  16.286 1.000 13.29  ? 115 CYS A N    1 
ATOM   2062 C CA   . CYS A 1 116 ? 31.195 1.969  17.003 1.000 12.43  ? 115 CYS A CA   1 
ATOM   2063 C C    . CYS A 1 116 ? 30.566 0.761  16.355 1.000 12.33  ? 115 CYS A C    1 
ATOM   2064 O O    . CYS A 1 116 ? 30.146 -0.148 17.060 1.000 12.98  ? 115 CYS A O    1 
ATOM   2065 C CB   . CYS A 1 116 ? 30.095 3.044  17.131 1.000 11.37  ? 115 CYS A CB   1 
ATOM   2066 S SG   . CYS A 1 116 ? 30.653 4.560  17.940 1.000 12.36  ? 115 CYS A SG   1 
ATOM   2067 D D    . CYS A 1 116 ? 32.181 3.083  15.453 1.000 15.66  ? 115 CYS A D    1 
ATOM   2068 D DA   . CYS A 1 116 ? 31.519 1.703  18.027 1.000 15.31  ? 115 CYS A DA   1 
ATOM   2069 D DB2  . CYS A 1 116 ? 29.717 3.315  16.172 1.000 12.03  ? 115 CYS A DB2  1 
ATOM   2070 D DB3  . CYS A 1 116 ? 29.229 2.682  17.691 1.000 13.27  ? 115 CYS A DB3  1 
ATOM   2071 N N    . LYS A 1 117 ? 30.491 0.751  15.028 1.000 12.58  ? 116 LYS A N    1 
ATOM   2072 C CA   . LYS A 1 117 ? 29.822 -0.314 14.289 1.000 13.16  ? 116 LYS A CA   1 
ATOM   2073 C C    . LYS A 1 117 ? 30.463 -1.652 14.600 1.000 14.24  ? 116 LYS A C    1 
ATOM   2074 O O    . LYS A 1 117 ? 31.681 -1.804 14.479 1.000 19.29  ? 116 LYS A O    1 
ATOM   2075 C CB   . LYS A 1 117 ? 29.975 0.015  12.800 1.000 13.85  ? 116 LYS A CB   1 
ATOM   2076 C CG   . LYS A 1 117 ? 29.416 -1.028 11.850 1.000 16.17  ? 116 LYS A CG   1 
ATOM   2077 C CD   . LYS A 1 117 ? 29.646 -0.557 10.443 1.000 20.32  ? 116 LYS A CD   1 
ATOM   2078 C CE   . LYS A 1 117 ? 29.216 -1.608 9.409  1.000 23.73  ? 116 LYS A CE   1 
ATOM   2079 N NZ   . LYS A 1 117 ? 29.837 -1.168 8.129  1.000 25.56  ? 116 LYS A NZ   1 
ATOM   2080 H H    A LYS A 1 117 ? 30.912 1.510  14.512 0.612 155.59 ? 116 LYS A H    1 
ATOM   2081 D D    B LYS A 1 117 ? 30.753 1.599  14.526 0.388 11.63  ? 116 LYS A D    1 
ATOM   2082 D DA   . LYS A 1 117 ? 28.769 -0.368 14.577 1.000 15.38  ? 116 LYS A DA   1 
ATOM   2083 D DB2  . LYS A 1 117 ? 29.488 0.958  12.612 1.000 16.18  ? 116 LYS A DB2  1 
ATOM   2084 D DB3  . LYS A 1 117 ? 31.030 0.143  12.596 1.000 15.06  ? 116 LYS A DB3  1 
ATOM   2085 D DG2  . LYS A 1 117 ? 29.850 -1.990 12.040 1.000 17.27  ? 116 LYS A DG2  1 
ATOM   2086 D DG3  . LYS A 1 117 ? 28.353 -1.160 12.049 1.000 19.50  ? 116 LYS A DG3  1 
ATOM   2087 D DD2  . LYS A 1 117 ? 29.049 0.338  10.248 1.000 22.05  ? 116 LYS A DD2  1 
ATOM   2088 D DD3  . LYS A 1 117 ? 30.700 -0.354 10.252 1.000 23.04  ? 116 LYS A DD3  1 
ATOM   2089 D DE2  . LYS A 1 117 ? 29.631 -2.549 9.732  1.000 29.25  ? 116 LYS A DE2  1 
ATOM   2090 D DE3  . LYS A 1 117 ? 28.152 -1.600 9.536  1.000 27.11  ? 116 LYS A DE3  1 
ATOM   2091 D DZ1  . LYS A 1 117 ? 29.448 -0.272 7.852  1.000 27.31  ? 116 LYS A DZ1  1 
ATOM   2092 D DZ2  . LYS A 1 117 ? 30.844 -1.000 8.300  1.000 27.52  ? 116 LYS A DZ2  1 
ATOM   2093 D DZ3  . LYS A 1 117 ? 29.717 -1.895 7.431  1.000 27.29  ? 116 LYS A DZ3  1 
ATOM   2094 N N    . GLY A 1 118 ? 29.647 -2.625 14.998 1.000 16.86  ? 117 GLY A N    1 
ATOM   2095 C CA   . GLY A 1 118 ? 30.150 -3.963 15.260 1.000 19.26  ? 117 GLY A CA   1 
ATOM   2096 C C    . GLY A 1 118 ? 30.631 -4.218 16.659 1.000 17.49  ? 117 GLY A C    1 
ATOM   2097 O O    . GLY A 1 118 ? 30.988 -5.356 16.995 1.000 19.81  ? 117 GLY A O    1 
ATOM   2098 D D    . GLY A 1 118 ? 28.666 -2.436 15.110 1.000 23.30  ? 117 GLY A D    1 
ATOM   2099 D DA2  . GLY A 1 118 ? 29.339 -4.659 15.054 1.000 24.74  ? 117 GLY A DA2  1 
ATOM   2100 D DA3  . GLY A 1 118 ? 30.961 -4.206 14.569 1.000 25.07  ? 117 GLY A DA3  1 
ATOM   2101 N N    . THR A 1 119 ? 30.684 -3.185 17.478 1.000 16.87  ? 118 THR A N    1 
ATOM   2102 C CA   . THR A 1 119 ? 31.164 -3.294 18.842 1.000 17.75  ? 118 THR A CA   1 
ATOM   2103 C C    . THR A 1 119 ? 30.008 -3.515 19.801 1.000 16.71  ? 118 THR A C    1 
ATOM   2104 O O    . THR A 1 119 ? 28.838 -3.443 19.441 1.000 16.57  ? 118 THR A O    1 
ATOM   2105 C CB   . THR A 1 119 ? 31.939 -2.040 19.278 1.000 18.35  ? 118 THR A CB   1 
ATOM   2106 O OG1  . THR A 1 119 ? 31.116 -0.887 19.451 1.000 18.39  ? 118 THR A OG1  1 
ATOM   2107 C CG2  . THR A 1 119 ? 32.998 -1.652 18.233 1.000 19.55  ? 118 THR A CG2  1 
ATOM   2108 D D    . THR A 1 119 ? 30.393 -2.258 17.189 1.000 19.46  ? 118 THR A D    1 
ATOM   2109 D DA   . THR A 1 119 ? 31.871 -4.132 18.914 1.000 19.72  ? 118 THR A DA   1 
ATOM   2110 D DB   . THR A 1 119 ? 32.426 -2.261 20.223 1.000 20.81  ? 118 THR A DB   1 
ATOM   2111 D DG1  . THR A 1 119 ? 30.682 -0.619 18.620 1.000 19.82  ? 118 THR A DG1  1 
ATOM   2112 D DG21 . THR A 1 119 ? 32.509 -1.410 17.323 1.000 22.63  ? 118 THR A DG21 1 
ATOM   2113 D DG22 . THR A 1 119 ? 33.528 -0.805 18.619 1.000 24.97  ? 118 THR A DG22 1 
ATOM   2114 D DG23 . THR A 1 119 ? 33.675 -2.448 18.117 1.000 24.63  ? 118 THR A DG23 1 
ATOM   2115 N N    . ASP A 1 120 ? 30.310 -3.753 21.071 1.000 17.97  ? 119 ASP A N    1 
ATOM   2116 C CA   . ASP A 1 120 ? 29.294 -3.893 22.087 1.000 18.22  ? 119 ASP A CA   1 
ATOM   2117 C C    . ASP A 1 120 ? 28.880 -2.500 22.561 1.000 15.36  ? 119 ASP A C    1 
ATOM   2118 O O    . ASP A 1 120 ? 29.329 -1.991 23.571 1.000 16.98  ? 119 ASP A O    1 
ATOM   2119 C CB   . ASP A 1 120 ? 29.766 -4.762 23.245 1.000 22.41  ? 119 ASP A CB   1 
ATOM   2120 C CG   . ASP A 1 120 ? 28.768 -4.702 24.360 1.000 25.37  ? 119 ASP A CG   1 
ATOM   2121 O OD1  . ASP A 1 120 ? 27.581 -4.336 24.202 1.000 26.98  ? 119 ASP A OD1  1 
ATOM   2122 O OD2  . ASP A 1 120 ? 29.200 -5.016 25.505 1.000 28.17  ? 119 ASP A OD2  1 
ATOM   2123 D D    . ASP A 1 120 ? 31.301 -3.836 21.299 1.000 20.03  ? 119 ASP A D    1 
ATOM   2124 D DA   . ASP A 1 120 ? 28.405 -4.357 21.645 1.000 19.68  ? 119 ASP A DA   1 
ATOM   2125 D DB2  . ASP A 1 120 ? 29.891 -5.769 22.898 1.000 27.95  ? 119 ASP A DB2  1 
ATOM   2126 D DB3  . ASP A 1 120 ? 30.725 -4.377 23.586 1.000 24.63  ? 119 ASP A DB3  1 
ATOM   2127 N N    . VAL A 1 121 ? 28.003 -1.889 21.777 1.000 15.65  ? 120 VAL A N    1 
ATOM   2128 C CA   . VAL A 1 121 ? 27.603 -0.510 22.052 1.000 16.05  ? 120 VAL A CA   1 
ATOM   2129 C C    . VAL A 1 121 ? 26.755 -0.404 23.326 1.000 15.74  ? 120 VAL A C    1 
ATOM   2130 O O    . VAL A 1 121 ? 26.634 0.709  23.828 1.000 17.61  ? 120 VAL A O    1 
ATOM   2131 C CB   . VAL A 1 121 ? 26.860 0.193  20.906 1.000 18.62  ? 120 VAL A CB   1 
ATOM   2132 C CG1  . VAL A 1 121 ? 27.781 0.345  19.708 1.000 20.17  ? 120 VAL A CG1  1 
ATOM   2133 C CG2  . VAL A 1 121 ? 25.580 -0.528 20.502 1.000 20.73  ? 120 VAL A CG2  1 
ATOM   2134 D D    . VAL A 1 121 ? 27.617 -2.360 20.973 1.000 21.19  ? 120 VAL A D    1 
ATOM   2135 D DA   . VAL A 1 121 ? 28.504 0.070  22.251 1.000 17.56  ? 120 VAL A DA   1 
ATOM   2136 D DB   . VAL A 1 121 ? 26.588 1.204  21.275 1.000 20.02  ? 120 VAL A DB   1 
ATOM   2137 D DG11 . VAL A 1 121 ? 28.108 -0.596 19.371 1.000 21.42  ? 120 VAL A DG11 1 
ATOM   2138 D DG12 . VAL A 1 121 ? 27.258 0.875  18.932 1.000 21.62  ? 120 VAL A DG12 1 
ATOM   2139 D DG13 . VAL A 1 121 ? 28.616 0.942  19.946 1.000 23.41  ? 120 VAL A DG13 1 
ATOM   2140 D DG21 . VAL A 1 121 ? 25.782 -1.531 20.235 1.000 25.11  ? 120 VAL A DG21 1 
ATOM   2141 D DG22 . VAL A 1 121 ? 24.882 -0.532 21.293 1.000 24.72  ? 120 VAL A DG22 1 
ATOM   2142 D DG23 . VAL A 1 121 ? 25.143 -0.054 19.655 1.000 27.15  ? 120 VAL A DG23 1 
ATOM   2143 N N    . GLN A 1 122 ? 26.248 -1.518 23.873 1.000 17.20  ? 121 GLN A N    1 
ATOM   2144 C CA   . GLN A 1 122 ? 25.530 -1.399 25.141 1.000 18.64  ? 121 GLN A CA   1 
ATOM   2145 C C    . GLN A 1 122 ? 26.454 -0.956 26.261 1.000 17.16  ? 121 GLN A C    1 
ATOM   2146 O O    . GLN A 1 122 ? 25.961 -0.419 27.269 1.000 18.69  ? 121 GLN A O    1 
ATOM   2147 C CB   . GLN A 1 122 ? 24.844 -2.738 25.451 1.000 23.98  ? 121 GLN A CB   1 
ATOM   2148 C CG   . GLN A 1 122 ? 23.983 -3.264 24.332 1.000 31.51  ? 121 GLN A CG   1 
ATOM   2149 C CD   . GLN A 1 122 ? 23.246 -4.559 24.655 1.000 44.38  ? 121 GLN A CD   1 
ATOM   2150 O OE1  . GLN A 1 122 ? 23.847 -5.622 24.793 1.000 51.29  ? 121 GLN A OE1  1 
ATOM   2151 N NE2  . GLN A 1 122 ? 21.926 -4.424 24.742 1.000 50.69  ? 121 GLN A NE2  1 
ATOM   2152 D D    . GLN A 1 122 ? 26.389 -2.435 23.461 1.000 20.35  ? 121 GLN A D    1 
ATOM   2153 D DA   . GLN A 1 122 ? 24.754 -0.642 25.004 1.000 20.64  ? 121 GLN A DA   1 
ATOM   2154 D DB2  . GLN A 1 122 ? 25.631 -3.472 25.674 1.000 21.42  ? 121 GLN A DB2  1 
ATOM   2155 D DB3  . GLN A 1 122 ? 24.255 -2.621 26.361 1.000 28.09  ? 121 GLN A DB3  1 
ATOM   2156 D DG2  . GLN A 1 122 ? 23.250 -2.511 24.033 1.000 37.81  ? 121 GLN A DG2  1 
ATOM   2157 D DG3  . GLN A 1 122 ? 24.628 -3.459 23.451 1.000 37.81  ? 121 GLN A DG3  1 
ATOM   2158 D DE21 . GLN A 1 122 ? 21.332 -5.179 25.066 1.000 60.83  ? 121 GLN A DE21 1 
ATOM   2159 D DE22 . GLN A 1 122 ? 21.477 -3.543 24.478 1.000 60.83  ? 121 GLN A DE22 1 
ATOM   2160 N N    . ALA A 1 123 ? 27.752 -1.116 26.100 1.000 16.93  ? 122 ALA A N    1 
ATOM   2161 C CA   . ALA A 1 123 ? 28.692 -0.641 27.097 1.000 18.57  ? 122 ALA A CA   1 
ATOM   2162 C C    . ALA A 1 123 ? 28.572 0.857  27.317 1.000 17.09  ? 122 ALA A C    1 
ATOM   2163 O O    . ALA A 1 123 ? 28.877 1.333  28.411 1.000 18.30  ? 122 ALA A O    1 
ATOM   2164 C CB   . ALA A 1 123 ? 30.120 -0.995 26.695 1.000 20.73  ? 122 ALA A CB   1 
ATOM   2165 D D    . ALA A 1 123 ? 28.104 -1.571 25.257 1.000 17.64  ? 122 ALA A D    1 
ATOM   2166 D DA   . ALA A 1 123 ? 28.499 -1.073 28.098 1.000 20.93  ? 122 ALA A DA   1 
ATOM   2167 D DB1  . ALA A 1 123 ? 30.361 -0.560 25.766 1.000 22.46  ? 122 ALA A DB1  1 
ATOM   2168 D DB2  . ALA A 1 123 ? 30.802 -0.638 27.440 1.000 23.78  ? 122 ALA A DB2  1 
ATOM   2169 D DB3  . ALA A 1 123 ? 30.204 -2.050 26.592 1.000 24.82  ? 122 ALA A DB3  1 
ATOM   2170 N N    A TRP A 1 124 ? 28.129 1.604  26.322 0.538 14.98  ? 123 TRP A N    1 
ATOM   2171 N N    B TRP A 1 124 ? 28.140 1.606  26.321 0.462 15.18  ? 123 TRP A N    1 
ATOM   2172 C CA   A TRP A 1 124 ? 28.051 3.054  26.459 0.538 15.48  ? 123 TRP A CA   1 
ATOM   2173 C CA   B TRP A 1 124 ? 28.093 3.061  26.474 0.462 15.39  ? 123 TRP A CA   1 
ATOM   2174 C C    A TRP A 1 124 ? 26.865 3.504  27.302 0.538 14.56  ? 123 TRP A C    1 
ATOM   2175 C C    B TRP A 1 124 ? 27.027 3.493  27.458 0.462 15.29  ? 123 TRP A C    1 
ATOM   2176 O O    A TRP A 1 124 ? 26.827 4.682  27.668 0.538 14.18  ? 123 TRP A O    1 
ATOM   2177 O O    B TRP A 1 124 ? 27.123 4.591  28.019 0.462 14.25  ? 123 TRP A O    1 
ATOM   2178 C CB   A TRP A 1 124 ? 27.989 3.740  25.077 0.538 16.04  ? 123 TRP A CB   1 
ATOM   2179 C CB   B TRP A 1 124 ? 27.895 3.718  25.085 0.462 15.72  ? 123 TRP A CB   1 
ATOM   2180 C CG   A TRP A 1 124 ? 29.350 3.594  24.464 0.538 16.10  ? 123 TRP A CG   1 
ATOM   2181 C CG   B TRP A 1 124 ? 29.184 3.432  24.369 0.462 15.89  ? 123 TRP A CG   1 
ATOM   2182 C CD1  A TRP A 1 124 ? 29.739 2.756  23.465 0.538 16.27  ? 123 TRP A CD1  1 
ATOM   2183 C CD1  B TRP A 1 124 ? 29.415 2.439  23.465 0.462 15.73  ? 123 TRP A CD1  1 
ATOM   2184 C CD2  A TRP A 1 124 ? 30.499 4.337  24.884 0.538 16.64  ? 123 TRP A CD2  1 
ATOM   2185 C CD2  B TRP A 1 124 ? 30.403 4.151  24.551 0.462 16.49  ? 123 TRP A CD2  1 
ATOM   2186 N NE1  A TRP A 1 124 ? 31.080 2.922  23.209 0.538 16.65  ? 123 TRP A NE1  1 
ATOM   2187 N NE1  B TRP A 1 124 ? 30.720 2.489  23.046 0.462 16.09  ? 123 TRP A NE1  1 
ATOM   2188 C CE2  A TRP A 1 124 ? 31.553 3.882  24.065 0.538 17.17  ? 123 TRP A CE2  1 
ATOM   2189 C CE2  B TRP A 1 124 ? 31.337 3.528  23.697 0.462 16.36  ? 123 TRP A CE2  1 
ATOM   2190 C CE3  A TRP A 1 124 ? 30.759 5.318  25.840 0.538 18.38  ? 123 TRP A CE3  1 
ATOM   2191 C CE3  B TRP A 1 124 ? 30.808 5.239  25.317 0.462 17.18  ? 123 TRP A CE3  1 
ATOM   2192 C CZ2  A TRP A 1 124 ? 32.830 4.398  24.200 0.538 18.09  ? 123 TRP A CZ2  1 
ATOM   2193 C CZ2  B TRP A 1 124 ? 32.648 3.977  23.612 0.462 17.75  ? 123 TRP A CZ2  1 
ATOM   2194 C CZ3  A TRP A 1 124 ? 32.035 5.835  25.969 0.538 18.17  ? 123 TRP A CZ3  1 
ATOM   2195 C CZ3  B TRP A 1 124 ? 32.114 5.684  25.233 0.462 18.48  ? 123 TRP A CZ3  1 
ATOM   2196 C CH2  A TRP A 1 124 ? 33.065 5.366  25.146 0.538 18.56  ? 123 TRP A CH2  1 
ATOM   2197 C CH2  B TRP A 1 124 ? 33.026 5.055  24.381 0.462 18.54  ? 123 TRP A CH2  1 
ATOM   2198 H H    A TRP A 1 124 ? 27.842 1.167  25.458 0.538 167.91 ? 123 TRP A H    1 
ATOM   2199 H H    B TRP A 1 124 ? 27.843 1.178  25.456 0.462 24.71  ? 123 TRP A H    1 
ATOM   2200 D DA   A TRP A 1 124 ? 28.946 3.411  26.978 0.538 15.56  ? 123 TRP A DA   1 
ATOM   2201 D DA   B TRP A 1 124 ? 29.071 3.390  26.846 0.462 16.95  ? 123 TRP A DA   1 
ATOM   2202 D DB2  A TRP A 1 124 ? 27.281 3.220  24.455 0.538 16.63  ? 123 TRP A DB2  1 
ATOM   2203 D DB2  B TRP A 1 124 ? 27.100 3.198  24.586 0.462 17.00  ? 123 TRP A DB2  1 
ATOM   2204 D DB3  A TRP A 1 124 ? 27.741 4.769  25.244 0.538 17.83  ? 123 TRP A DB3  1 
ATOM   2205 D DB3  B TRP A 1 124 ? 27.734 4.762  25.232 0.462 17.12  ? 123 TRP A DB3  1 
ATOM   2206 D DD1  A TRP A 1 124 ? 29.123 2.058  22.927 0.538 18.66  ? 123 TRP A DD1  1 
ATOM   2207 D DD1  B TRP A 1 124 ? 28.696 1.704  23.127 0.462 21.80  ? 123 TRP A DD1  1 
ATOM   2208 D DE1  A TRP A 1 124 ? 31.620 2.393  22.545 0.538 20.30  ? 123 TRP A DE1  1 
ATOM   2209 D DE1  B TRP A 1 124 ? 31.161 1.845  22.408 0.462 16.49  ? 123 TRP A DE1  1 
ATOM   2210 D DE3  A TRP A 1 124 ? 29.962 5.676  26.478 0.538 19.27  ? 123 TRP A DE3  1 
ATOM   2211 D DE3  B TRP A 1 124 ? 30.088 5.782  25.917 0.462 17.09  ? 123 TRP A DE3  1 
ATOM   2212 D DZ2  A TRP A 1 124 ? 33.633 4.017  23.585 0.538 26.84  ? 123 TRP A DZ2  1 
ATOM   2213 D DZ2  B TRP A 1 124 ? 33.356 3.462  22.985 0.462 22.59  ? 123 TRP A DZ2  1 
ATOM   2214 D DZ3  A TRP A 1 124 ? 32.230 6.647  26.654 0.538 20.89  ? 123 TRP A DZ3  1 
ATOM   2215 D DZ3  B TRP A 1 124 ? 32.449 6.511  25.842 0.462 25.70  ? 123 TRP A DZ3  1 
ATOM   2216 D DH2  A TRP A 1 124 ? 34.066 5.753  25.297 0.538 29.52  ? 123 TRP A DH2  1 
ATOM   2217 D DH2  B TRP A 1 124 ? 34.053 5.399  24.371 0.462 28.45  ? 123 TRP A DH2  1 
ATOM   2218 N N    A ILE A 1 125 ? 25.926 2.616  27.613 0.538 14.63  ? 124 ILE A N    1 
ATOM   2219 N N    B ILE A 1 125 ? 26.011 2.670  27.711 0.462 15.16  ? 124 ILE A N    1 
ATOM   2220 C CA   A ILE A 1 125 ? 24.831 2.946  28.518 0.538 14.73  ? 124 ILE A CA   1 
ATOM   2221 C CA   B ILE A 1 125 ? 24.984 3.083  28.659 0.462 15.23  ? 124 ILE A CA   1 
ATOM   2222 C C    A ILE A 1 125 ? 24.925 2.159  29.826 0.538 14.26  ? 124 ILE A C    1 
ATOM   2223 C C    B ILE A 1 125 ? 24.874 2.107  29.833 0.462 15.08  ? 124 ILE A C    1 
ATOM   2224 O O    A ILE A 1 125 ? 24.152 2.424  30.752 0.538 14.57  ? 124 ILE A O    1 
ATOM   2225 O O    B ILE A 1 125 ? 23.925 2.165  30.609 0.462 16.90  ? 124 ILE A O    1 
ATOM   2226 C CB   A ILE A 1 125 ? 23.511 2.733  27.780 0.538 16.58  ? 124 ILE A CB   1 
ATOM   2227 C CB   B ILE A 1 125 ? 23.611 3.237  27.995 0.462 16.42  ? 124 ILE A CB   1 
ATOM   2228 C CG1  A ILE A 1 125 ? 23.273 1.289  27.359 0.538 18.92  ? 124 ILE A CG1  1 
ATOM   2229 C CG1  B ILE A 1 125 ? 23.073 1.911  27.460 0.462 18.71  ? 124 ILE A CG1  1 
ATOM   2230 C CG2  A ILE A 1 125 ? 23.469 3.618  26.530 0.538 17.69  ? 124 ILE A CG2  1 
ATOM   2231 C CG2  B ILE A 1 125 ? 23.647 4.298  26.902 0.462 17.30  ? 124 ILE A CG2  1 
ATOM   2232 C CD1  A ILE A 1 125 ? 21.794 1.098  27.079 0.538 19.98  ? 124 ILE A CD1  1 
ATOM   2233 C CD1  B ILE A 1 125 ? 21.623 2.086  27.057 0.462 20.22  ? 124 ILE A CD1  1 
ATOM   2234 H H    A ILE A 1 125 ? 25.973 1.690  27.213 0.538 167.91 ? 124 ILE A H    1 
ATOM   2235 H H    B ILE A 1 125 ? 25.952 1.773  27.251 0.462 9.17   ? 124 ILE A H    1 
ATOM   2236 D DA   A ILE A 1 125 ? 24.917 4.020  28.776 0.538 14.89  ? 124 ILE A DA   1 
ATOM   2237 D DA   B ILE A 1 125 ? 25.298 4.056  29.089 0.462 15.65  ? 124 ILE A DA   1 
ATOM   2238 D DB   A ILE A 1 125 ? 22.689 3.038  28.442 0.538 16.86  ? 124 ILE A DB   1 
ATOM   2239 D DB   B ILE A 1 125 ? 22.905 3.584  28.778 0.462 16.38  ? 124 ILE A DB   1 
ATOM   2240 D DG12 A ILE A 1 125 ? 23.831 1.103  26.453 0.538 20.82  ? 124 ILE A DG12 1 
ATOM   2241 D DG12 B ILE A 1 125 ? 23.654 1.629  26.600 0.462 20.93  ? 124 ILE A DG12 1 
ATOM   2242 D DG13 A ILE A 1 125 ? 23.573 0.637  28.159 0.538 20.08  ? 124 ILE A DG13 1 
ATOM   2243 D DG13 B ILE A 1 125 ? 23.136 1.177  28.252 0.462 20.02  ? 124 ILE A DG13 1 
ATOM   2244 D DG21 A ILE A 1 125 ? 24.054 3.181  25.752 0.538 20.79  ? 124 ILE A DG21 1 
ATOM   2245 D DG21 B ILE A 1 125 ? 24.167 3.950  26.039 0.462 17.38  ? 124 ILE A DG21 1 
ATOM   2246 D DG22 A ILE A 1 125 ? 22.484 3.719  26.157 0.538 19.96  ? 124 ILE A DG22 1 
ATOM   2247 D DG22 B ILE A 1 125 ? 22.668 4.540  26.559 0.462 19.64  ? 124 ILE A DG22 1 
ATOM   2248 D DG23 A ILE A 1 125 ? 23.884 4.579  26.731 0.538 19.40  ? 124 ILE A DG23 1 
ATOM   2249 D DG23 B ILE A 1 125 ? 24.122 5.187  27.235 0.462 18.37  ? 124 ILE A DG23 1 
ATOM   2250 D DD11 A ILE A 1 125 ? 21.619 1.224  26.042 0.538 25.12  ? 124 ILE A DD11 1 
ATOM   2251 D DD11 B ILE A 1 125 ? 21.571 2.553  26.116 0.462 21.75  ? 124 ILE A DD11 1 
ATOM   2252 D DD12 A ILE A 1 125 ? 21.504 0.131  27.408 0.538 24.27  ? 124 ILE A DD12 1 
ATOM   2253 D DD12 B ILE A 1 125 ? 21.139 1.154  27.057 0.462 22.42  ? 124 ILE A DD12 1 
ATOM   2254 D DD13 A ILE A 1 125 ? 21.244 1.816  27.631 0.538 23.05  ? 124 ILE A DD13 1 
ATOM   2255 D DD13 B ILE A 1 125 ? 21.155 2.738  27.768 0.462 22.34  ? 124 ILE A DD13 1 
ATOM   2256 N N    . ARG A 1 126 ? 25.864 1.229  29.945 1.000 15.72  ? 125 ARG A N    1 
ATOM   2257 C CA   . ARG A 1 126 ? 25.943 0.383  31.110 1.000 20.94  ? 125 ARG A CA   1 
ATOM   2258 C C    . ARG A 1 126 ? 26.195 1.180  32.379 1.000 22.22  ? 125 ARG A C    1 
ATOM   2259 O O    . ARG A 1 126 ? 27.050 2.062  32.357 1.000 24.67  ? 125 ARG A O    1 
ATOM   2260 C CB   . ARG A 1 126 ? 27.057 -0.646 30.899 1.000 25.06  ? 125 ARG A CB   1 
ATOM   2261 C CG   . ARG A 1 126 ? 27.107 -1.729 31.935 1.000 30.05  ? 125 ARG A CG   1 
ATOM   2262 C CD   . ARG A 1 126 ? 28.013 -2.889 31.558 1.000 34.61  ? 125 ARG A CD   1 
ATOM   2263 N NE   . ARG A 1 126 ? 27.690 -3.484 30.268 1.000 35.92  ? 125 ARG A NE   1 
ATOM   2264 C CZ   . ARG A 1 126 ? 28.513 -3.735 29.262 1.000 38.86  ? 125 ARG A CZ   1 
ATOM   2265 N NH1  . ARG A 1 126 ? 29.804 -3.478 29.380 1.000 41.36  ? 125 ARG A NH1  1 
ATOM   2266 N NH2  . ARG A 1 126 ? 27.978 -4.271 28.173 1.000 39.11  ? 125 ARG A NH2  1 
ATOM   2267 H H    A ARG A 1 126 ? 26.539 1.112  29.202 0.432 17.10  ? 125 ARG A H    1 
ATOM   2268 D D    B ARG A 1 126 ? 26.420 1.057  29.119 0.568 17.39  ? 125 ARG A D    1 
ATOM   2269 D DA   . ARG A 1 126 ? 24.963 -0.123 31.219 1.000 23.14  ? 125 ARG A DA   1 
ATOM   2270 D DB2  . ARG A 1 126 ? 26.898 -1.089 29.914 1.000 26.53  ? 125 ARG A DB2  1 
ATOM   2271 D DB3  . ARG A 1 126 ? 27.996 -0.108 30.857 1.000 27.12  ? 125 ARG A DB3  1 
ATOM   2272 D DG2  . ARG A 1 126 ? 27.447 -1.326 32.887 1.000 36.76  ? 125 ARG A DG2  1 
ATOM   2273 D DG3  . ARG A 1 126 ? 26.096 -2.123 32.096 1.000 35.33  ? 125 ARG A DG3  1 
ATOM   2274 D DD2  . ARG A 1 126 ? 29.049 -2.531 31.535 1.000 39.47  ? 125 ARG A DD2  1 
ATOM   2275 D DD3  . ARG A 1 126 ? 27.928 -3.631 32.348 1.000 38.57  ? 125 ARG A DD3  1 
ATOM   2276 D DE   . ARG A 1 126 ? 26.703 -3.704 30.207 1.000 42.91  ? 125 ARG A DE   1 
ATOM   2277 D DH11 . ARG A 1 126 ? 30.463 -3.888 28.741 1.000 50.98  ? 125 ARG A DH11 1 
ATOM   2278 D DH12 . ARG A 1 126 ? 30.119 -2.894 30.155 1.000 45.69  ? 125 ARG A DH12 1 
ATOM   2279 D DH21 . ARG A 1 126 ? 28.441 -4.168 27.284 1.000 67.42  ? 125 ARG A DH21 1 
ATOM   2280 D DH22 . ARG A 1 126 ? 27.105 -4.789 28.267 1.000 61.36  ? 125 ARG A DH22 1 
ATOM   2281 N N    . GLY A 1 127 ? 25.407 0.829  33.387 1.000 23.54  ? 126 GLY A N    1 
ATOM   2282 C CA   . GLY A 1 127 ? 25.481 1.512  34.657 1.000 25.51  ? 126 GLY A CA   1 
ATOM   2283 C C    . GLY A 1 127 ? 24.758 2.831  34.729 1.000 23.98  ? 126 GLY A C    1 
ATOM   2284 O O    . GLY A 1 127 ? 24.793 3.493  35.756 1.000 27.97  ? 126 GLY A O    1 
ATOM   2285 D D    . GLY A 1 127 ? 24.737 0.093  33.264 1.000 29.67  ? 126 GLY A D    1 
ATOM   2286 D DA2  . GLY A 1 127 ? 25.209 0.854  35.473 1.000 27.83  ? 126 GLY A DA2  1 
ATOM   2287 D DA3  . GLY A 1 127 ? 26.547 1.742  34.805 1.000 29.83  ? 126 GLY A DA3  1 
ATOM   2288 N N    . CYS A 1 128 ? 24.083 3.280  33.686 1.000 22.43  ? 127 CYS A N    1 
ATOM   2289 C CA   . CYS A 1 128 ? 23.372 4.548  33.728 1.000 22.19  ? 127 CYS A CA   1 
ATOM   2290 C C    . CYS A 1 128 ? 21.923 4.429  34.176 1.000 24.17  ? 127 CYS A C    1 
ATOM   2291 O O    . CYS A 1 128 ? 21.232 3.458  33.904 1.000 28.54  ? 127 CYS A O    1 
ATOM   2292 C CB   . CYS A 1 128 ? 23.360 5.158  32.330 1.000 19.02  ? 127 CYS A CB   1 
ATOM   2293 S SG   . CYS A 1 128 ? 24.991 5.458  31.602 1.000 19.43  ? 127 CYS A SG   1 
ATOM   2294 D D    . CYS A 1 128 ? 24.084 2.777  32.816 1.000 23.99  ? 127 CYS A D    1 
ATOM   2295 D DA   . CYS A 1 128 ? 23.922 5.233  34.383 1.000 22.14  ? 127 CYS A DA   1 
ATOM   2296 D DB2  . CYS A 1 128 ? 22.855 4.448  31.679 1.000 21.77  ? 127 CYS A DB2  1 
ATOM   2297 D DB3  . CYS A 1 128 ? 22.781 6.085  32.404 1.000 19.20  ? 127 CYS A DB3  1 
ATOM   2298 N N    . ARG A 1 129 ? 21.459 5.486  34.841 1.000 25.85  ? 128 ARG A N    1 
ATOM   2299 C CA   . ARG A 1 129 ? 20.050 5.606  35.183 1.000 29.05  ? 128 ARG A CA   1 
ATOM   2300 C C    . ARG A 1 129 ? 19.266 6.136  34.007 1.000 32.04  ? 128 ARG A C    1 
ATOM   2301 O O    . ARG A 1 129 ? 19.498 7.303  33.663 1.000 39.20  ? 128 ARG A O    1 
ATOM   2302 C CB   . ARG A 1 129 ? 19.916 6.555  36.374 1.000 32.20  ? 128 ARG A CB   1 
ATOM   2303 C CG   . ARG A 1 129 ? 20.213 5.842  37.684 1.000 44.19  ? 128 ARG A CG   1 
ATOM   2304 C CD   . ARG A 1 129 ? 20.653 6.784  38.777 1.000 51.40  ? 128 ARG A CD   1 
ATOM   2305 N NE   . ARG A 1 129 ? 21.034 6.240  40.074 1.000 53.99  ? 128 ARG A NE   1 
ATOM   2306 C CZ   . ARG A 1 129 ? 21.480 5.051  40.474 1.000 55.93  ? 128 ARG A CZ   1 
ATOM   2307 N NH1  . ARG A 1 129 ? 21.848 4.831  41.738 1.000 54.00  ? 128 ARG A NH1  1 
ATOM   2308 N NH2  . ARG A 1 129 ? 21.582 4.009  39.663 1.000 58.65  ? 128 ARG A NH2  1 
ATOM   2309 D D    . ARG A 1 129 ? 22.111 6.223  35.081 1.000 26.86  ? 128 ARG A D    1 
ATOM   2310 D DA   . ARG A 1 129 ? 19.700 4.602  35.467 1.000 37.91  ? 128 ARG A DA   1 
ATOM   2311 D DB2  . ARG A 1 129 ? 20.626 7.360  36.244 1.000 38.65  ? 128 ARG A DB2  1 
ATOM   2312 D DB3  . ARG A 1 129 ? 18.916 6.946  36.400 1.000 38.65  ? 128 ARG A DB3  1 
ATOM   2313 D DG2  . ARG A 1 129 ? 19.312 5.317  37.996 1.000 53.03  ? 128 ARG A DG2  1 
ATOM   2314 D DG3  . ARG A 1 129 ? 21.000 5.109  37.497 1.000 53.03  ? 128 ARG A DG3  1 
ATOM   2315 D DD2  . ARG A 1 129 ? 21.465 7.425  38.400 1.000 61.68  ? 128 ARG A DD2  1 
ATOM   2316 D DD3  . ARG A 1 129 ? 19.826 7.502  38.939 1.000 61.68  ? 128 ARG A DD3  1 
ATOM   2317 D DE   . ARG A 1 129 ? 20.905 6.980  40.789 1.000 64.79  ? 128 ARG A DE   1 
ATOM   2318 D DH11 . ARG A 1 129 ? 22.155 3.914  42.010 1.000 64.79  ? 128 ARG A DH11 1 
ATOM   2319 D DH12 . ARG A 1 129 ? 21.808 5.581  42.405 1.000 64.79  ? 128 ARG A DH12 1 
ATOM   2320 D DH21 . ARG A 1 129 ? 20.808 3.363  39.582 1.000 70.37  ? 128 ARG A DH21 1 
ATOM   2321 D DH22 . ARG A 1 129 ? 22.442 3.850  39.157 1.000 70.37  ? 128 ARG A DH22 1 
ATOM   2322 N N    . LEU A 1 130 ? 18.370 5.404  33.357 1.000 35.00  ? 129 LEU A N    1 
ATOM   2323 C CA   . LEU A 1 130 ? 17.819 5.958  32.116 1.000 41.87  ? 129 LEU A CA   1 
ATOM   2324 C C    . LEU A 1 130 ? 16.375 6.402  32.120 1.000 48.62  ? 129 LEU A C    1 
ATOM   2325 O O    . LEU A 1 130 ? 15.505 5.610  31.698 1.000 49.51  ? 129 LEU A O    1 
ATOM   2326 C CB   . LEU A 1 130 ? 18.046 4.855  31.059 1.000 42.08  ? 129 LEU A CB   1 
ATOM   2327 C CG   . LEU A 1 130 ? 19.501 4.859  30.590 1.000 43.12  ? 129 LEU A CG   1 
ATOM   2328 C CD1  . LEU A 1 130 ? 19.698 3.967  29.380 1.000 43.05  ? 129 LEU A CD1  1 
ATOM   2329 C CD2  . LEU A 1 130 ? 19.934 6.293  30.292 1.000 43.60  ? 129 LEU A CD2  1 
ATOM   2330 O OXT  . LEU A 1 130 ? 16.118 7.565  32.509 1.000 51.20  ? 129 LEU A OXT  1 
ATOM   2331 D D    . LEU A 1 130 ? 18.088 4.490  33.666 1.000 42.00  ? 129 LEU A D    1 
ATOM   2332 D DA   . LEU A 1 130 ? 18.454 6.813  31.829 1.000 50.24  ? 129 LEU A DA   1 
ATOM   2333 D DB2  . LEU A 1 130 ? 17.807 3.893  31.505 1.000 50.50  ? 129 LEU A DB2  1 
ATOM   2334 D DB3  . LEU A 1 130 ? 17.389 5.049  30.213 1.000 50.50  ? 129 LEU A DB3  1 
ATOM   2335 D DG   . LEU A 1 130 ? 20.119 4.484  31.409 1.000 86.44  ? 129 LEU A DG   1 
ATOM   2336 D DD11 . LEU A 1 130 ? 19.179 4.363  28.539 1.000 64.57  ? 129 LEU A DD11 1 
ATOM   2337 D DD12 . LEU A 1 130 ? 20.731 3.902  29.133 1.000 64.57  ? 129 LEU A DD12 1 
ATOM   2338 D DD13 . LEU A 1 130 ? 19.310 2.993  29.569 1.000 64.57  ? 129 LEU A DD13 1 
ATOM   2339 D DD21 . LEU A 1 130 ? 20.788 6.270  29.665 1.000 65.40  ? 129 LEU A DD21 1 
ATOM   2340 D DD22 . LEU A 1 130 ? 19.139 6.799  29.807 1.000 65.40  ? 129 LEU A DD22 1 
ATOM   2341 D DD23 . LEU A 1 130 ? 20.182 6.772  31.206 1.000 65.40  ? 129 LEU A DD23 1 
HETATM 2342 N N    . NO3 B 2 .   ? 33.363 9.380  28.694 1.000 22.40  ? 201 NO3 A N    1 
HETATM 2343 O O1   . NO3 B 2 .   ? 33.897 10.387 28.205 1.000 20.49  ? 201 NO3 A O1   1 
HETATM 2344 O O2   . NO3 B 2 .   ? 32.465 9.440  29.535 1.000 26.30  ? 201 NO3 A O2   1 
HETATM 2345 O O3   . NO3 B 2 .   ? 33.772 8.268  28.308 1.000 28.94  ? 201 NO3 A O3   1 
HETATM 2346 N N    . NO3 C 2 .   ? 24.386 1.234  9.049  1.000 31.56  ? 202 NO3 A N    1 
HETATM 2347 O O1   . NO3 C 2 .   ? 23.575 0.707  9.822  1.000 25.39  ? 202 NO3 A O1   1 
HETATM 2348 O O2   . NO3 C 2 .   ? 24.159 2.376  8.614  1.000 31.86  ? 202 NO3 A O2   1 
HETATM 2349 O O3   . NO3 C 2 .   ? 25.408 0.603  8.723  1.000 41.19  ? 202 NO3 A O3   1 
HETATM 2350 N N    . NO3 D 2 .   ? 27.191 16.042 -3.876 1.000 40.51  ? 203 NO3 A N    1 
HETATM 2351 O O1   . NO3 D 2 .   ? 27.139 16.909 -2.982 1.000 27.70  ? 203 NO3 A O1   1 
HETATM 2352 O O2   . NO3 D 2 .   ? 26.999 14.827 -3.698 1.000 39.03  ? 203 NO3 A O2   1 
HETATM 2353 O O3   . NO3 D 2 .   ? 27.469 16.403 -5.032 1.000 41.74  ? 203 NO3 A O3   1 
HETATM 2354 N N    . NO3 E 2 .   ? 13.671 0.497  11.433 1.000 15.86  ? 204 NO3 A N    1 
HETATM 2355 O O1   . NO3 E 2 .   ? 14.066 1.452  10.699 1.000 20.25  ? 204 NO3 A O1   1 
HETATM 2356 O O2   . NO3 E 2 .   ? 12.547 0.583  11.874 1.000 19.70  ? 204 NO3 A O2   1 
HETATM 2357 O O3   . NO3 E 2 .   ? 14.496 -0.396 11.644 1.000 19.17  ? 204 NO3 A O3   1 
HETATM 2358 N N    . NO3 F 2 .   ? 27.320 14.113 8.907  1.000 46.54  ? 205 NO3 A N    1 
HETATM 2359 O O1   . NO3 F 2 .   ? 27.036 15.323 8.835  1.000 19.41  ? 205 NO3 A O1   1 
HETATM 2360 O O2   . NO3 F 2 .   ? 28.200 13.668 8.138  1.000 50.74  ? 205 NO3 A O2   1 
HETATM 2361 O O3   . NO3 F 2 .   ? 26.762 13.323 9.710  1.000 36.76  ? 205 NO3 A O3   1 
HETATM 2362 N N    . NO3 G 2 .   ? 21.981 -0.092 23.577 1.000 29.01  ? 206 NO3 A N    1 
HETATM 2363 O O1   . NO3 G 2 .   ? 22.095 -1.147 24.231 1.000 49.51  ? 206 NO3 A O1   1 
HETATM 2364 O O2   . NO3 G 2 .   ? 21.200 0.783  23.986 1.000 26.41  ? 206 NO3 A O2   1 
HETATM 2365 O O3   . NO3 G 2 .   ? 22.642 0.031  22.536 1.000 28.84  ? 206 NO3 A O3   1 
HETATM 2366 N N    . NO3 H 2 .   ? 18.139 28.624 8.069  1.000 30.80  ? 207 NO3 A N    1 
HETATM 2367 O O1   . NO3 H 2 .   ? 19.238 29.043 8.484  1.000 32.65  ? 207 NO3 A O1   1 
HETATM 2368 O O2   . NO3 H 2 .   ? 17.470 29.335 7.295  1.000 42.62  ? 207 NO3 A O2   1 
HETATM 2369 O O3   . NO3 H 2 .   ? 17.688 27.513 8.403  1.000 25.72  ? 207 NO3 A O3   1 
HETATM 2370 N N    . NO3 I 2 .   ? 18.630 18.531 26.233 1.000 34.61  ? 208 NO3 A N    1 
HETATM 2371 O O1   . NO3 I 2 .   ? 19.772 18.872 26.579 1.000 24.65  ? 208 NO3 A O1   1 
HETATM 2372 O O2   . NO3 I 2 .   ? 17.986 19.196 25.399 1.000 41.03  ? 208 NO3 A O2   1 
HETATM 2373 O O3   . NO3 I 2 .   ? 18.067 17.524 26.702 1.000 38.24  ? 208 NO3 A O3   1 
HETATM 2374 C C    . ACT J 3 .   ? 39.103 18.828 5.254  1.000 43.67  ? 209 ACT A C    1 
HETATM 2375 O O    . ACT J 3 .   ? 38.499 18.367 4.237  1.000 33.78  ? 209 ACT A O    1 
HETATM 2376 O OXT  . ACT J 3 .   ? 39.968 19.722 5.260  1.000 51.07  ? 209 ACT A OXT  1 
HETATM 2377 C CH3  . ACT J 3 .   ? 38.776 18.290 6.649  1.000 43.46  ? 209 ACT A CH3  1 
HETATM 2378 H H1   . ACT J 3 .   ? 38.036 17.535 6.572  1.000 65.19  ? 209 ACT A H1   1 
HETATM 2379 H H2   . ACT J 3 .   ? 39.651 17.882 7.086  1.000 65.19  ? 209 ACT A H2   1 
HETATM 2380 H H3   . ACT J 3 .   ? 38.413 19.079 7.256  1.000 65.19  ? 209 ACT A H3   1 
HETATM 2381 O O    . DOD K 4 .   ? 38.779 25.836 14.173 1.000 24.88  ? 301 DOD A O    1 
HETATM 2382 O O    . DOD K 4 .   ? 16.195 9.786  29.739 1.000 31.92  ? 302 DOD A O    1 
HETATM 2383 O O    . DOD K 4 .   ? 21.400 8.522  33.244 1.000 27.58  ? 303 DOD A O    1 
HETATM 2384 O O    . DOD K 4 .   ? 41.036 19.808 7.293  1.000 24.52  ? 304 DOD A O    1 
HETATM 2385 O O    . DOD K 4 .   ? 16.888 21.609 27.651 1.000 36.75  ? 305 DOD A O    1 
HETATM 2386 O O    . DOD K 4 .   ? 33.793 22.962 -1.428 1.000 34.17  ? 306 DOD A O    1 
HETATM 2387 O O    . DOD K 4 .   ? 22.832 26.290 -1.703 1.000 32.28  ? 307 DOD A O    1 
HETATM 2388 O O    . DOD K 4 .   ? 35.871 0.219  17.176 1.000 25.07  ? 308 DOD A O    1 
HETATM 2389 O O    . DOD K 4 .   ? 35.045 17.150 1.153  1.000 44.76  ? 309 DOD A O    1 
HETATM 2390 O O    . DOD K 4 .   ? 12.944 7.772  5.705  1.000 33.27  ? 310 DOD A O    1 
HETATM 2391 O O    . DOD K 4 .   ? 31.774 0.370  21.477 1.000 28.43  ? 311 DOD A O    1 
HETATM 2392 D D1   . DOD K 4 .   ? 32.544 0.916  21.268 1.000 33.54  ? 311 DOD A D1   1 
HETATM 2393 D D2   . DOD K 4 .   ? 31.454 0.103  20.610 1.000 23.20  ? 311 DOD A D2   1 
HETATM 2394 O O    . DOD K 4 .   ? 33.457 28.250 3.626  1.000 29.31  ? 312 DOD A O    1 
HETATM 2395 O O    . DOD K 4 .   ? 37.612 7.469  11.535 1.000 53.24  ? 313 DOD A O    1 
HETATM 2396 D D1   . DOD K 4 .   ? 38.259 7.033  12.091 1.000 32.32  ? 313 DOD A D1   1 
HETATM 2397 D D2   . DOD K 4 .   ? 37.227 8.142  12.100 1.000 42.47  ? 313 DOD A D2   1 
HETATM 2398 O O    . DOD K 4 .   ? 16.335 16.326 28.461 1.000 76.62  ? 314 DOD A O    1 
HETATM 2399 D D1   . DOD K 4 .   ? 17.140 16.787 28.703 1.000 38.73  ? 314 DOD A D1   1 
HETATM 2400 D D2   . DOD K 4 .   ? 16.392 16.216 27.511 1.000 44.15  ? 314 DOD A D2   1 
HETATM 2401 O O    . DOD K 4 .   ? 16.916 23.671 2.847  1.000 29.79  ? 315 DOD A O    1 
HETATM 2402 O O    . DOD K 4 .   ? 13.097 11.063 4.001  1.000 28.18  ? 316 DOD A O    1 
HETATM 2403 D D1   . DOD K 4 .   ? 14.032 11.268 4.040  1.000 38.27  ? 316 DOD A D1   1 
HETATM 2404 D D2   . DOD K 4 .   ? 12.737 11.754 3.433  1.000 26.42  ? 316 DOD A D2   1 
HETATM 2405 O O    . DOD K 4 .   ? 19.817 25.150 19.473 1.000 24.09  ? 317 DOD A O    1 
HETATM 2406 O O    . DOD K 4 .   ? 21.867 20.711 28.304 1.000 31.54  ? 318 DOD A O    1 
HETATM 2407 D D1   . DOD K 4 .   ? 21.333 19.946 28.066 1.000 49.90  ? 318 DOD A D1   1 
HETATM 2408 D D2   . DOD K 4 .   ? 22.561 20.729 27.642 1.000 41.12  ? 318 DOD A D2   1 
HETATM 2409 O O    . DOD K 4 .   ? 18.126 24.625 21.599 1.000 167.91 ? 319 DOD A O    1 
HETATM 2410 D D1   . DOD K 4 .   ? 17.488 24.249 22.207 1.000 28.56  ? 319 DOD A D1   1 
HETATM 2411 D D2   . DOD K 4 .   ? 18.323 25.484 21.977 1.000 26.28  ? 319 DOD A D2   1 
HETATM 2412 O O    . DOD K 4 .   ? 25.106 20.064 -2.305 1.000 22.77  ? 320 DOD A O    1 
HETATM 2413 D D1   . DOD K 4 .   ? 25.230 20.953 -1.962 1.000 21.16  ? 320 DOD A D1   1 
HETATM 2414 D D2   . DOD K 4 .   ? 25.535 20.121 -3.162 1.000 25.44  ? 320 DOD A D2   1 
HETATM 2415 O O    . DOD K 4 .   ? 30.195 0.732  30.598 1.000 40.36  ? 321 DOD A O    1 
HETATM 2416 O O    . DOD K 4 .   ? 13.761 15.473 12.595 1.000 27.72  ? 322 DOD A O    1 
HETATM 2417 O O    . DOD K 4 .   ? 30.993 14.783 10.692 1.000 38.78  ? 323 DOD A O    1 
HETATM 2418 D D1   . DOD K 4 .   ? 30.756 15.132 9.824  1.000 38.03  ? 323 DOD A D1   1 
HETATM 2419 D D2   . DOD K 4 .   ? 30.320 15.157 11.266 1.000 35.92  ? 323 DOD A D2   1 
HETATM 2420 O O    . DOD K 4 .   ? 25.052 14.893 36.376 1.000 19.74  ? 324 DOD A O    1 
HETATM 2421 D D1   . DOD K 4 .   ? 25.270 14.011 36.072 1.000 19.94  ? 324 DOD A D1   1 
HETATM 2422 D D2   . DOD K 4 .   ? 25.660 15.073 37.109 1.000 18.70  ? 324 DOD A D2   1 
HETATM 2423 O O    . DOD K 4 .   ? 27.082 -3.223 17.456 1.000 38.20  ? 325 DOD A O    1 
HETATM 2424 D D1   . DOD K 4 .   ? 26.758 -4.053 17.096 1.000 39.46  ? 325 DOD A D1   1 
HETATM 2425 D D2   . DOD K 4 .   ? 27.840 -3.499 17.976 1.000 33.67  ? 325 DOD A D2   1 
HETATM 2426 O O    . DOD K 4 .   ? 27.071 24.201 31.365 1.000 32.97  ? 326 DOD A O    1 
HETATM 2427 O O    . DOD K 4 .   ? 26.116 20.457 20.222 1.000 12.81  ? 327 DOD A O    1 
HETATM 2428 D D1   . DOD K 4 .   ? 26.765 21.106 20.508 1.000 12.91  ? 327 DOD A D1   1 
HETATM 2429 D D2   . DOD K 4 .   ? 25.688 20.951 19.501 1.000 12.87  ? 327 DOD A D2   1 
HETATM 2430 O O    A DOD K 4 .   ? 34.290 16.567 12.437 0.602 13.76  ? 328 DOD A O    1 
HETATM 2431 O O    B DOD K 4 .   ? 34.344 16.092 13.195 0.398 16.83  ? 328 DOD A O    1 
HETATM 2432 D D1   A DOD K 4 .   ? 33.545 16.781 13.012 0.602 26.03  ? 328 DOD A D1   1 
HETATM 2433 D D1   B DOD K 4 .   ? 34.081 17.000 13.368 0.398 11.02  ? 328 DOD A D1   1 
HETATM 2434 D D2   A DOD K 4 .   ? 33.972 16.847 11.571 0.602 15.73  ? 328 DOD A D2   1 
HETATM 2435 D D2   B DOD K 4 .   ? 33.840 15.897 12.388 0.398 19.71  ? 328 DOD A D2   1 
HETATM 2436 O O    . DOD K 4 .   ? 19.481 23.075 20.511 1.000 22.42  ? 329 DOD A O    1 
HETATM 2437 O O    . DOD K 4 .   ? 30.187 -7.611 15.777 1.000 22.03  ? 330 DOD A O    1 
HETATM 2438 D D1   . DOD K 4 .   ? 30.635 -6.865 16.187 1.000 24.20  ? 330 DOD A D1   1 
HETATM 2439 D D2   . DOD K 4 .   ? 30.663 -7.694 14.943 1.000 28.79  ? 330 DOD A D2   1 
HETATM 2440 O O    . DOD K 4 .   ? 13.413 24.599 11.498 1.000 36.81  ? 331 DOD A O    1 
HETATM 2441 D D1   . DOD K 4 .   ? 13.048 23.778 11.843 1.000 27.54  ? 331 DOD A D1   1 
HETATM 2442 D D2   . DOD K 4 .   ? 14.215 24.309 11.062 1.000 25.91  ? 331 DOD A D2   1 
HETATM 2443 O O    . DOD K 4 .   ? 23.367 23.296 4.251  1.000 16.15  ? 332 DOD A O    1 
HETATM 2444 D D1   . DOD K 4 .   ? 23.661 23.479 5.131  1.000 17.45  ? 332 DOD A D1   1 
HETATM 2445 D D2   . DOD K 4 .   ? 24.157 22.918 3.872  1.000 15.44  ? 332 DOD A D2   1 
HETATM 2446 O O    . DOD K 4 .   ? 21.683 21.174 19.954 1.000 38.66  ? 333 DOD A O    1 
HETATM 2447 D D1   . DOD K 4 .   ? 22.568 21.090 20.305 1.000 20.88  ? 333 DOD A D1   1 
HETATM 2448 D D2   . DOD K 4 .   ? 21.828 21.843 19.276 1.000 22.02  ? 333 DOD A D2   1 
HETATM 2449 O O    . DOD K 4 .   ? 40.314 20.927 10.344 1.000 80.76  ? 334 DOD A O    1 
HETATM 2450 D D1   . DOD K 4 .   ? 39.606 21.332 9.841  1.000 33.17  ? 334 DOD A D1   1 
HETATM 2451 D D2   . DOD K 4 .   ? 40.811 20.394 9.722  1.000 41.98  ? 334 DOD A D2   1 
HETATM 2452 O O    . DOD K 4 .   ? 27.002 17.466 4.401  1.000 17.98  ? 335 DOD A O    1 
HETATM 2453 D D1   . DOD K 4 .   ? 27.830 17.872 4.671  1.000 18.79  ? 335 DOD A D1   1 
HETATM 2454 D D2   . DOD K 4 .   ? 27.226 16.935 3.633  1.000 22.74  ? 335 DOD A D2   1 
HETATM 2455 O O    . DOD K 4 .   ? 31.834 26.460 6.780  1.000 12.28  ? 336 DOD A O    1 
HETATM 2456 D D1   . DOD K 4 .   ? 31.771 26.168 5.883  1.000 14.60  ? 336 DOD A D1   1 
HETATM 2457 D D2   . DOD K 4 .   ? 30.897 26.533 7.031  1.000 13.95  ? 336 DOD A D2   1 
HETATM 2458 O O    . DOD K 4 .   ? 20.524 14.509 31.014 1.000 26.00  ? 337 DOD A O    1 
HETATM 2459 D D1   . DOD K 4 .   ? 20.181 14.038 31.774 1.000 27.18  ? 337 DOD A D1   1 
HETATM 2460 D D2   . DOD K 4 .   ? 20.927 13.755 30.553 1.000 21.17  ? 337 DOD A D2   1 
HETATM 2461 O O    . DOD K 4 .   ? 23.839 17.170 32.263 1.000 20.30  ? 338 DOD A O    1 
HETATM 2462 D D1   . DOD K 4 .   ? 23.024 16.922 31.822 1.000 21.10  ? 338 DOD A D1   1 
HETATM 2463 D D2   . DOD K 4 .   ? 23.707 16.919 33.191 1.000 22.13  ? 338 DOD A D2   1 
HETATM 2464 O O    . DOD K 4 .   ? 33.349 13.852 11.639 1.000 23.80  ? 339 DOD A O    1 
HETATM 2465 D D1   . DOD K 4 .   ? 33.600 14.702 12.047 1.000 22.52  ? 339 DOD A D1   1 
HETATM 2466 D D2   . DOD K 4 .   ? 32.537 14.155 11.184 1.000 30.99  ? 339 DOD A D2   1 
HETATM 2467 O O    . DOD K 4 .   ? 35.349 25.402 6.609  1.000 24.06  ? 340 DOD A O    1 
HETATM 2468 D D1   . DOD K 4 .   ? 36.065 24.821 6.327  1.000 31.42  ? 340 DOD A D1   1 
HETATM 2469 D D2   . DOD K 4 .   ? 34.778 24.804 7.078  1.000 25.39  ? 340 DOD A D2   1 
HETATM 2470 O O    . DOD K 4 .   ? 30.366 18.074 2.896  1.000 76.15  ? 341 DOD A O    1 
HETATM 2471 D D1   . DOD K 4 .   ? 31.112 18.184 2.302  1.000 45.04  ? 341 DOD A D1   1 
HETATM 2472 D D2   . DOD K 4 .   ? 30.536 18.683 3.626  1.000 26.62  ? 341 DOD A D2   1 
HETATM 2473 O O    . DOD K 4 .   ? 27.884 18.262 32.168 1.000 14.38  ? 342 DOD A O    1 
HETATM 2474 D D1   . DOD K 4 .   ? 28.463 18.363 32.914 1.000 16.05  ? 342 DOD A D1   1 
HETATM 2475 D D2   . DOD K 4 .   ? 28.412 18.347 31.407 1.000 15.46  ? 342 DOD A D2   1 
HETATM 2476 O O    . DOD K 4 .   ? 27.994 19.277 -4.174 1.000 35.29  ? 343 DOD A O    1 
HETATM 2477 O O    . DOD K 4 .   ? 13.902 16.459 20.002 1.000 40.34  ? 344 DOD A O    1 
HETATM 2478 O O    . DOD K 4 .   ? 28.111 9.688  33.369 1.000 17.33  ? 345 DOD A O    1 
HETATM 2479 D D1   . DOD K 4 .   ? 29.051 9.811  33.236 1.000 36.62  ? 345 DOD A D1   1 
HETATM 2480 D D2   . DOD K 4 .   ? 27.745 10.574 33.361 1.000 15.09  ? 345 DOD A D2   1 
HETATM 2481 O O    . DOD K 4 .   ? 14.235 6.904  23.135 1.000 35.65  ? 346 DOD A O    1 
HETATM 2482 D D1   . DOD K 4 .   ? 13.443 6.344  23.258 1.000 31.02  ? 346 DOD A D1   1 
HETATM 2483 D D2   . DOD K 4 .   ? 14.095 7.442  23.945 1.000 25.81  ? 346 DOD A D2   1 
HETATM 2484 O O    . DOD K 4 .   ? 19.799 25.269 -1.239 1.000 26.71  ? 347 DOD A O    1 
HETATM 2485 D D1   . DOD K 4 .   ? 20.477 24.827 -0.726 1.000 21.35  ? 347 DOD A D1   1 
HETATM 2486 D D2   . DOD K 4 .   ? 19.032 25.140 -0.664 1.000 29.28  ? 347 DOD A D2   1 
HETATM 2487 O O    . DOD K 4 .   ? 23.758 20.360 21.571 1.000 20.16  ? 348 DOD A O    1 
HETATM 2488 D D1   . DOD K 4 .   ? 23.714 21.157 22.095 1.000 21.15  ? 348 DOD A D1   1 
HETATM 2489 D D2   . DOD K 4 .   ? 24.612 20.364 21.149 1.000 18.27  ? 348 DOD A D2   1 
HETATM 2490 O O    . DOD K 4 .   ? 35.515 16.355 8.807  1.000 134.42 ? 349 DOD A O    1 
HETATM 2491 D D1   . DOD K 4 .   ? 35.896 17.041 8.255  1.000 37.50  ? 349 DOD A D1   1 
HETATM 2492 D D2   . DOD K 4 .   ? 34.609 16.636 8.946  1.000 46.46  ? 349 DOD A D2   1 
HETATM 2493 O O    . DOD K 4 .   ? 17.047 20.665 14.383 1.000 44.59  ? 350 DOD A O    1 
HETATM 2494 D D1   . DOD K 4 .   ? 17.826 20.155 14.625 1.000 20.25  ? 350 DOD A D1   1 
HETATM 2495 D D2   . DOD K 4 .   ? 16.903 20.367 13.481 1.000 24.88  ? 350 DOD A D2   1 
HETATM 2496 O O    . DOD K 4 .   ? 25.682 18.190 16.445 1.000 9.65   ? 351 DOD A O    1 
HETATM 2497 D D1   . DOD K 4 .   ? 26.180 18.862 16.003 1.000 11.59  ? 351 DOD A D1   1 
HETATM 2498 D D2   . DOD K 4 .   ? 24.982 18.680 16.890 1.000 11.07  ? 351 DOD A D2   1 
HETATM 2499 O O    . DOD K 4 .   ? 15.916 19.813 11.969 1.000 27.52  ? 352 DOD A O    1 
HETATM 2500 D D1   . DOD K 4 .   ? 15.886 20.335 11.149 1.000 22.54  ? 352 DOD A D1   1 
HETATM 2501 D D2   . DOD K 4 .   ? 15.607 18.939 11.734 1.000 31.68  ? 352 DOD A D2   1 
HETATM 2502 O O    . DOD K 4 .   ? 20.593 -1.360 17.092 1.000 19.82  ? 353 DOD A O    1 
HETATM 2503 D D1   . DOD K 4 .   ? 19.941 -1.156 16.390 1.000 19.27  ? 353 DOD A D1   1 
HETATM 2504 D D2   . DOD K 4 .   ? 20.629 -2.319 17.055 1.000 33.83  ? 353 DOD A D2   1 
HETATM 2505 O O    . DOD K 4 .   ? 25.173 31.342 1.677  1.000 37.14  ? 354 DOD A O    1 
HETATM 2506 D D1   . DOD K 4 .   ? 24.881 31.718 0.844  1.000 38.46  ? 354 DOD A D1   1 
HETATM 2507 D D2   . DOD K 4 .   ? 24.834 30.443 1.657  1.000 51.37  ? 354 DOD A D2   1 
HETATM 2508 O O    . DOD K 4 .   ? 25.778 26.084 4.964  1.000 13.68  ? 355 DOD A O    1 
HETATM 2509 D D1   . DOD K 4 .   ? 25.445 26.327 4.121  1.000 24.22  ? 355 DOD A D1   1 
HETATM 2510 D D2   . DOD K 4 .   ? 25.795 25.134 5.047  1.000 15.15  ? 355 DOD A D2   1 
HETATM 2511 O O    . DOD K 4 .   ? 27.415 25.134 24.480 1.000 57.51  ? 356 DOD A O    1 
HETATM 2512 D D1   . DOD K 4 .   ? 27.490 24.186 24.613 1.000 30.65  ? 356 DOD A D1   1 
HETATM 2513 D D2   . DOD K 4 .   ? 27.100 25.195 23.573 1.000 39.26  ? 356 DOD A D2   1 
HETATM 2514 O O    . DOD K 4 .   ? 35.885 18.215 21.488 1.000 47.96  ? 357 DOD A O    1 
HETATM 2515 D D1   . DOD K 4 .   ? 35.192 17.555 21.581 1.000 30.15  ? 357 DOD A D1   1 
HETATM 2516 D D2   . DOD K 4 .   ? 36.353 18.176 22.327 1.000 48.60  ? 357 DOD A D2   1 
HETATM 2517 O O    . DOD K 4 .   ? 27.323 14.213 5.410  1.000 35.45  ? 358 DOD A O    1 
HETATM 2518 O O    . DOD K 4 .   ? 35.767 26.945 17.460 1.000 22.55  ? 359 DOD A O    1 
HETATM 2519 O O    . DOD K 4 .   ? 37.699 9.901  17.027 1.000 31.24  ? 360 DOD A O    1 
HETATM 2520 O O    . DOD K 4 .   ? 26.268 16.089 31.555 1.000 13.76  ? 361 DOD A O    1 
HETATM 2521 D D1   . DOD K 4 .   ? 26.799 16.769 31.968 1.000 15.68  ? 361 DOD A D1   1 
HETATM 2522 D D2   . DOD K 4 .   ? 25.391 16.373 31.848 1.000 16.56  ? 361 DOD A D2   1 
HETATM 2523 O O    . DOD K 4 .   ? 15.683 26.035 3.995  1.000 35.36  ? 362 DOD A O    1 
HETATM 2524 O O    . DOD K 4 .   ? 31.251 10.360 32.076 1.000 24.37  ? 363 DOD A O    1 
HETATM 2525 O O    . DOD K 4 .   ? 22.955 30.855 9.105  1.000 44.38  ? 364 DOD A O    1 
HETATM 2526 D D1   . DOD K 4 .   ? 22.738 29.923 9.049  1.000 26.73  ? 364 DOD A D1   1 
HETATM 2527 D D2   . DOD K 4 .   ? 22.621 31.143 9.959  1.000 33.87  ? 364 DOD A D2   1 
HETATM 2528 O O    . DOD K 4 .   ? 34.373 26.142 19.786 1.000 43.25  ? 365 DOD A O    1 
HETATM 2529 D D1   . DOD K 4 .   ? 35.048 25.566 19.416 1.000 54.31  ? 365 DOD A D1   1 
HETATM 2530 D D2   . DOD K 4 .   ? 33.535 25.797 19.453 1.000 41.13  ? 365 DOD A D2   1 
HETATM 2531 O O    . DOD K 4 .   ? 26.999 -0.913 16.196 1.000 79.79  ? 366 DOD A O    1 
HETATM 2532 D D1   . DOD K 4 .   ? 26.190 -0.414 16.316 1.000 28.00  ? 366 DOD A D1   1 
HETATM 2533 D D2   . DOD K 4 .   ? 26.945 -1.686 16.759 1.000 27.40  ? 366 DOD A D2   1 
HETATM 2534 O O    . DOD K 4 .   ? 38.937 23.612 12.822 1.000 23.57  ? 367 DOD A O    1 
HETATM 2535 D D1   . DOD K 4 .   ? 39.112 22.713 13.151 1.000 27.65  ? 367 DOD A D1   1 
HETATM 2536 D D2   . DOD K 4 .   ? 38.507 23.985 13.605 1.000 27.44  ? 367 DOD A D2   1 
HETATM 2537 O O    . DOD K 4 .   ? 30.855 12.205 9.272  1.000 21.56  ? 368 DOD A O    1 
HETATM 2538 D D1   . DOD K 4 .   ? 30.961 12.768 10.042 1.000 24.63  ? 368 DOD A D1   1 
HETATM 2539 D D2   . DOD K 4 .   ? 29.931 11.943 9.241  1.000 27.15  ? 368 DOD A D2   1 
HETATM 2540 O O    . DOD K 4 .   ? 38.461 23.812 16.137 1.000 72.01  ? 369 DOD A O    1 
HETATM 2541 D D1   . DOD K 4 .   ? 37.932 24.029 15.367 1.000 37.52  ? 369 DOD A D1   1 
HETATM 2542 D D2   . DOD K 4 .   ? 38.920 22.996 15.929 1.000 48.42  ? 369 DOD A D2   1 
HETATM 2543 O O    . DOD K 4 .   ? 26.654 -1.320 6.736  1.000 167.91 ? 370 DOD A O    1 
HETATM 2544 D D1   . DOD K 4 .   ? 26.461 -2.033 6.125  1.000 27.36  ? 370 DOD A D1   1 
HETATM 2545 D D2   . DOD K 4 .   ? 26.037 -1.454 7.457  1.000 28.71  ? 370 DOD A D2   1 
HETATM 2546 O O    . DOD K 4 .   ? 17.371 25.459 26.073 1.000 32.73  ? 371 DOD A O    1 
HETATM 2547 O O    . DOD K 4 .   ? 20.626 12.126 1.639  1.000 30.52  ? 372 DOD A O    1 
HETATM 2548 O O    . DOD K 4 .   ? 35.571 17.231 25.829 1.000 35.51  ? 373 DOD A O    1 
HETATM 2549 O O    . DOD K 4 .   ? 25.910 27.885 3.065  1.000 25.55  ? 374 DOD A O    1 
HETATM 2550 D D1   . DOD K 4 .   ? 26.538 27.756 2.339  1.000 25.36  ? 374 DOD A D1   1 
HETATM 2551 D D2   . DOD K 4 .   ? 25.352 28.607 2.759  1.000 38.78  ? 374 DOD A D2   1 
HETATM 2552 O O    . DOD K 4 .   ? 25.778 27.846 -1.243 1.000 33.47  ? 375 DOD A O    1 
HETATM 2553 O O    . DOD K 4 .   ? 11.333 8.007  25.597 1.000 45.01  ? 376 DOD A O    1 
HETATM 2554 D D1   . DOD K 4 .   ? 10.865 7.435  26.211 1.000 41.71  ? 376 DOD A D1   1 
HETATM 2555 D D2   . DOD K 4 .   ? 11.449 8.847  26.053 1.000 30.49  ? 376 DOD A D2   1 
HETATM 2556 O O    . DOD K 4 .   ? 40.567 18.114 10.786 1.000 31.92  ? 377 DOD A O    1 
HETATM 2557 O O    . DOD K 4 .   ? 29.666 15.014 5.696  1.000 34.62  ? 378 DOD A O    1 
HETATM 2558 O O    . DOD K 4 .   ? 37.730 10.090 23.462 1.000 83.77  ? 379 DOD A O    1 
HETATM 2559 D D1   . DOD K 4 .   ? 38.108 9.344  23.930 1.000 40.13  ? 379 DOD A D1   1 
HETATM 2560 D D2   . DOD K 4 .   ? 38.123 10.856 23.886 1.000 31.35  ? 379 DOD A D2   1 
HETATM 2561 O O    A DOD K 4 .   ? 36.971 11.282 21.649 0.667 23.18  ? 380 DOD A O    1 
HETATM 2562 O O    B DOD K 4 .   ? 37.117 11.863 19.125 0.333 36.91  ? 380 DOD A O    1 
HETATM 2563 D D1   A DOD K 4 .   ? 36.977 12.123 21.187 0.667 28.20  ? 380 DOD A D1   1 
HETATM 2564 D D1   B DOD K 4 .   ? 36.996 12.273 19.983 0.333 28.93  ? 380 DOD A D1   1 
HETATM 2565 D D2   A DOD K 4 .   ? 36.034 11.052 21.672 0.667 29.19  ? 380 DOD A D2   1 
HETATM 2566 D D2   B DOD K 4 .   ? 37.620 11.066 19.298 0.333 13.66  ? 380 DOD A D2   1 
HETATM 2567 O O    . DOD K 4 .   ? 20.735 27.086 2.052  1.000 28.53  ? 381 DOD A O    1 
HETATM 2568 O O    A DOD K 4 .   ? 23.398 31.927 12.497 0.519 19.67  ? 382 DOD A O    1 
HETATM 2569 O O    B DOD K 4 .   ? 24.187 34.002 14.354 0.481 21.63  ? 382 DOD A O    1 
HETATM 2570 D D1   A DOD K 4 .   ? 23.887 31.118 12.320 0.519 18.62  ? 382 DOD A D1   1 
HETATM 2571 D D1   B DOD K 4 .   ? 23.806 33.170 14.089 0.481 26.43  ? 382 DOD A D1   1 
HETATM 2572 D D2   A DOD K 4 .   ? 22.507 31.616 12.687 0.519 18.83  ? 382 DOD A D2   1 
HETATM 2573 D D2   B DOD K 4 .   ? 23.598 34.685 14.039 0.481 21.62  ? 382 DOD A D2   1 
HETATM 2574 O O    . DOD K 4 .   ? 12.159 14.115 2.768  1.000 31.28  ? 383 DOD A O    1 
HETATM 2575 O O    . DOD K 4 .   ? 11.700 19.443 19.511 1.000 31.96  ? 384 DOD A O    1 
HETATM 2576 O O    . DOD K 4 .   ? 14.245 11.351 32.789 1.000 39.36  ? 385 DOD A O    1 
HETATM 2577 O O    . DOD K 4 .   ? 21.502 17.055 30.786 1.000 24.47  ? 386 DOD A O    1 
HETATM 2578 D D1   . DOD K 4 .   ? 20.988 17.622 30.208 1.000 38.52  ? 386 DOD A D1   1 
HETATM 2579 D D2   . DOD K 4 .   ? 21.064 16.190 30.781 1.000 26.95  ? 386 DOD A D2   1 
HETATM 2580 O O    . DOD K 4 .   ? 36.226 22.316 19.326 1.000 53.14  ? 387 DOD A O    1 
HETATM 2581 D D1   . DOD K 4 .   ? 36.109 23.208 18.998 1.000 35.78  ? 387 DOD A D1   1 
HETATM 2582 D D2   . DOD K 4 .   ? 36.589 21.808 18.596 1.000 28.38  ? 387 DOD A D2   1 
HETATM 2583 O O    . DOD K 4 .   ? 36.712 8.829  14.614 1.000 35.19  ? 388 DOD 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 
19   N N    A LYS A 2   ? 0.4581 0.2038 0.2126 0.1361  0.1932  0.0844  1   LYS A N    
20   N N    B LYS A 2   ? 0.4334 0.2092 0.1893 0.1293  0.1893  0.0913  1   LYS A N    
21   C CA   A LYS A 2   ? 0.3013 0.1935 0.1128 0.0644  0.0146  0.0390  1   LYS A CA   
22   C CA   B LYS A 2   ? 0.2935 0.1916 0.1146 0.0597  0.0239  0.0436  1   LYS A CA   
23   C C    A LYS A 2   ? 0.1823 0.1609 0.0960 -0.0069 -0.0301 0.0160  1   LYS A C    
24   C C    B LYS A 2   ? 0.2085 0.1584 0.0996 0.0013  -0.0337 0.0110  1   LYS A C    
25   O O    A LYS A 2   ? 0.1260 0.1781 0.0943 -0.0134 -0.0215 0.0258  1   LYS A O    
26   O O    B LYS A 2   ? 0.2875 0.1448 0.1054 0.0376  -0.0106 0.0261  1   LYS A O    
27   C CB   A LYS A 2   ? 0.2920 0.2407 0.1289 0.0994  0.0218  0.0314  1   LYS A CB   
28   C CB   B LYS A 2   ? 0.2865 0.2454 0.1363 0.0840  0.0160  0.0212  1   LYS A CB   
29   C CG   A LYS A 2   ? 0.2768 0.2328 0.1648 0.0620  0.0201  0.0228  1   LYS A CG   
30   C CG   B LYS A 2   ? 0.2773 0.2284 0.1707 0.0479  0.0211  0.0059  1   LYS A CG   
31   C CD   A LYS A 2   ? 0.2758 0.2570 0.1834 0.0593  0.0080  -0.0062 1   LYS A CD   
32   C CD   B LYS A 2   ? 0.2806 0.2559 0.1909 0.0508  0.0261  0.0047  1   LYS A CD   
33   C CE   A LYS A 2   ? 0.2544 0.2700 0.1982 0.0432  0.0211  0.0003  1   LYS A CE   
34   C CE   B LYS A 2   ? 0.2599 0.2601 0.1956 0.0411  0.0224  0.0033  1   LYS A CE   
35   N NZ   A LYS A 2   ? 0.2422 0.2605 0.1947 0.0282  0.0416  0.0025  1   LYS A NZ   
36   N NZ   B LYS A 2   ? 0.2649 0.2695 0.2176 0.0408  0.0300  -0.0038 1   LYS A NZ   
37   D D    A LYS A 2   ? 0.5367 0.1668 0.2248 0.0936  0.2191  0.0294  1   LYS A D    
38   D D    B LYS A 2   ? 0.5095 0.0761 0.2890 0.1049  0.0786  0.0354  1   LYS A D    
39   D DA   A LYS A 2   ? 0.3221 0.1895 0.1178 0.0753  0.0001  -0.0012 1   LYS A DA   
40   D DA   B LYS A 2   ? 0.3286 0.1479 0.1216 0.0100  0.0131  0.0210  1   LYS A DA   
41   D DB2  A LYS A 2   ? 0.3236 0.2278 0.1803 0.0646  0.0399  -0.0002 1   LYS A DB2  
42   D DB2  B LYS A 2   ? 0.2854 0.2283 0.1113 0.0700  0.0147  0.0366  1   LYS A DB2  
43   D DB3  A LYS A 2   ? 0.2719 0.2946 0.1367 0.0889  0.0229  0.0100  1   LYS A DB3  
44   D DB3  B LYS A 2   ? 0.3031 0.2650 0.1398 0.0341  0.0144  -0.0001 1   LYS A DB3  
45   D DG2  A LYS A 2   ? 0.2239 0.2076 0.2245 0.0092  -0.0225 -0.0286 1   LYS A DG2  
46   D DG2  B LYS A 2   ? 0.2462 0.2660 0.2260 -0.0128 0.0349  -0.0472 1   LYS A DG2  
47   D DG3  A LYS A 2   ? 0.3037 0.1454 0.1547 -0.0640 0.0304  0.0460  1   LYS A DG3  
48   D DG3  B LYS A 2   ? 0.2888 0.2004 0.1842 0.0128  0.0045  0.0280  1   LYS A DG3  
49   D DD2  A LYS A 2   ? 0.2612 0.2743 0.2025 0.0710  -0.0112 -0.0243 1   LYS A DD2  
50   D DD2  B LYS A 2   ? 0.3099 0.2562 0.1860 0.0320  0.0575  0.0068  1   LYS A DD2  
51   D DD3  A LYS A 2   ? 0.3278 0.2383 0.2012 0.0979  -0.0326 -0.0120 1   LYS A DD3  
52   D DD3  B LYS A 2   ? 0.3042 0.2620 0.2253 0.0747  -0.0026 0.0054  1   LYS A DD3  
53   D DE2  A LYS A 2   ? 0.2542 0.3303 0.2282 0.0349  0.0147  0.0121  1   LYS A DE2  
54   D DE2  B LYS A 2   ? 0.2288 0.2525 0.1828 0.0449  -0.0013 0.0141  1   LYS A DE2  
55   D DE3  A LYS A 2   ? 0.2582 0.2541 0.1843 0.0300  0.0299  0.0071  1   LYS A DE3  
56   D DE3  B LYS A 2   ? 0.2687 0.2244 0.2163 -0.0147 -0.0028 0.0057  1   LYS A DE3  
57   D DZ1  A LYS A 2   ? 0.2454 0.2860 0.1773 0.0221  0.0400  0.0412  1   LYS A DZ1  
58   D DZ1  B LYS A 2   ? 0.3126 0.2814 0.2875 0.0135  0.0737  -0.0134 1   LYS A DZ1  
59   D DZ2  A LYS A 2   ? 0.2331 0.2653 0.2476 0.0070  0.0360  -0.0350 1   LYS A DZ2  
60   D DZ2  B LYS A 2   ? 0.1975 0.3651 0.2482 -0.0464 0.0497  -0.0544 1   LYS A DZ2  
61   D DZ3  A LYS A 2   ? 0.2517 0.2789 0.2071 0.0140  0.0399  0.0108  1   LYS A DZ3  
62   D DZ3  B LYS A 2   ? 0.2578 0.3956 0.2527 0.0442  0.0276  0.0515  1   LYS A DZ3  
63   N N    . VAL A 3   ? 0.1715 0.1510 0.1002 -0.0182 -0.0382 0.0120  2   VAL A N    
64   C CA   . VAL A 3   ? 0.1609 0.1490 0.1038 -0.0210 -0.0239 0.0213  2   VAL A CA   
65   C C    . VAL A 3   ? 0.1648 0.1464 0.0858 -0.0255 -0.0432 0.0170  2   VAL A C    
66   O O    . VAL A 3   ? 0.1637 0.1524 0.0909 -0.0496 -0.0310 0.0071  2   VAL A O    
67   C CB   . VAL A 3   ? 0.1604 0.1734 0.1212 -0.0227 -0.0327 0.0246  2   VAL A CB   
68   C CG1  . VAL A 3   ? 0.1525 0.1887 0.1394 -0.0160 -0.0191 0.0094  2   VAL A CG1  
69   C CG2  . VAL A 3   ? 0.1756 0.1986 0.1646 -0.0433 -0.0290 0.0391  2   VAL A CG2  
70   D D    . VAL A 3   ? 0.2150 0.1617 0.1096 -0.0221 -0.0587 -0.0014 2   VAL A D    
71   D DA   . VAL A 3   ? 0.1884 0.1379 0.1037 -0.0322 -0.0267 0.0179  2   VAL A DA   
72   D DB   . VAL A 3   ? 0.1759 0.1864 0.1206 -0.0330 -0.0318 0.0127  2   VAL A DB   
73   D DG11 . VAL A 3   ? 0.2252 0.2439 0.1325 0.0235  -0.0089 0.0075  2   VAL A DG11 
74   D DG12 . VAL A 3   ? 0.1521 0.2439 0.1971 0.0052  -0.0223 0.0227  2   VAL A DG12 
75   D DG13 . VAL A 3   ? 0.1783 0.1954 0.1595 -0.0203 -0.0004 0.0068  2   VAL A DG13 
76   D DG21 . VAL A 3   ? 0.2333 0.2743 0.1636 -0.0645 -0.0143 0.0671  2   VAL A DG21 
77   D DG22 . VAL A 3   ? 0.2305 0.1892 0.2557 -0.0519 -0.0005 0.0307  2   VAL A DG22 
78   D DG23 . VAL A 3   ? 0.1754 0.2389 0.2568 -0.0598 -0.0411 0.0114  2   VAL A DG23 
79   N N    . PHE A 4   ? 0.1509 0.1390 0.0818 -0.0123 -0.0211 0.0014  3   PHE A N    
80   C CA   . PHE A 4   ? 0.1347 0.1418 0.0864 -0.0144 -0.0222 -0.0019 3   PHE A CA   
81   C C    . PHE A 4   ? 0.1192 0.1553 0.0775 -0.0171 -0.0235 0.0069  3   PHE A C    
82   O O    . PHE A 4   ? 0.1282 0.1719 0.1234 -0.0097 -0.0002 0.0298  3   PHE A O    
83   C CB   . PHE A 4   ? 0.1416 0.1564 0.0997 -0.0067 -0.0356 -0.0086 3   PHE A CB   
84   C CG   . PHE A 4   ? 0.1342 0.1732 0.1000 -0.0081 -0.0200 0.0116  3   PHE A CG   
85   C CD1  . PHE A 4   ? 0.1549 0.2007 0.1016 0.0006  -0.0243 0.0256  3   PHE A CD1  
86   C CD2  . PHE A 4   ? 0.1524 0.1915 0.1016 -0.0063 0.0018  -0.0054 3   PHE A CD2  
87   C CE1  . PHE A 4   ? 0.1573 0.2194 0.1578 -0.0015 -0.0408 0.0452  3   PHE A CE1  
88   C CE2  . PHE A 4   ? 0.1487 0.1921 0.1414 0.0017  0.0233  -0.0232 3   PHE A CE2  
89   C CZ   . PHE A 4   ? 0.1376 0.2245 0.1708 -0.0065 -0.0389 0.0058  3   PHE A CZ   
90   D D    . PHE A 4   ? 0.1604 0.1898 0.0890 -0.0168 -0.0060 0.0009  3   PHE A D    
91   D DA   . PHE A 4   ? 0.1496 0.1391 0.0875 -0.0178 -0.0157 0.0022  3   PHE A DA   
92   D DB2  . PHE A 4   ? 0.1394 0.2473 0.1134 -0.0020 -0.0353 -0.0505 3   PHE A DB2  
93   D DB3  . PHE A 4   ? 0.1601 0.1467 0.1881 -0.0204 -0.0623 -0.0111 3   PHE A DB3  
94   D DD1  . PHE A 4   ? 0.1801 0.2878 0.1514 0.0154  0.0122  0.0777  3   PHE A DD1  
95   D DD2  . PHE A 4   ? 0.1634 0.2158 0.1774 -0.0373 -0.0028 0.0439  3   PHE A DD2  
96   D DE1  . PHE A 4   ? 0.1963 0.3224 0.2880 0.0130  -0.0544 0.1617  3   PHE A DE1  
97   D DE2  . PHE A 4   ? 0.1329 0.3617 0.2077 -0.0236 0.0116  0.0465  3   PHE A DE2  
98   D DZ   . PHE A 4   ? 0.1679 0.2978 0.2340 0.0422  -0.0311 0.0091  3   PHE A DZ   
99   N N    . GLY A 5   ? 0.1352 0.1345 0.0942 -0.0037 0.0012  0.0029  4   GLY A N    
100  C CA   . GLY A 5   ? 0.1303 0.1514 0.0978 -0.0030 -0.0416 0.0141  4   GLY A CA   
101  C C    . GLY A 5   ? 0.1010 0.1307 0.1006 -0.0036 -0.0205 0.0231  4   GLY A C    
102  O O    . GLY A 5   ? 0.1152 0.1297 0.1149 -0.0010 -0.0393 0.0051  4   GLY A O    
103  D D    . GLY A 5   ? 0.1590 0.1586 0.1055 0.0183  0.0080  0.0093  4   GLY A D    
104  D DA2  . GLY A 5   ? 0.1221 0.1789 0.1870 -0.0152 -0.0514 0.0303  4   GLY A DA2  
105  D DA3  . GLY A 5   ? 0.2273 0.1722 0.0996 -0.0350 -0.0345 0.0225  4   GLY A DA3  
106  N N    A ARG A 6   ? 0.1123 0.1381 0.1108 0.0055  -0.0281 0.0177  5   ARG A N    
107  N N    B ARG A 6   ? 0.1285 0.1344 0.1113 0.0079  -0.0119 0.0255  5   ARG A N    
108  C CA   A ARG A 6   ? 0.1225 0.1386 0.1131 0.0062  -0.0302 0.0133  5   ARG A CA   
109  C CA   B ARG A 6   ? 0.1393 0.1374 0.1292 0.0071  -0.0122 0.0110  5   ARG A CA   
110  C C    A ARG A 6   ? 0.1279 0.1372 0.1023 -0.0007 -0.0241 -0.0005 5   ARG A C    
111  C C    B ARG A 6   ? 0.1381 0.1336 0.1046 0.0074  -0.0199 0.0101  5   ARG A C    
112  O O    A ARG A 6   ? 0.1205 0.1293 0.0954 -0.0025 -0.0150 -0.0076 5   ARG A O    
113  O O    B ARG A 6   ? 0.1497 0.1130 0.0994 -0.0060 -0.0206 0.0126  5   ARG A O    
114  C CB   A ARG A 6   ? 0.1397 0.1342 0.1459 0.0095  -0.0455 0.0130  5   ARG A CB   
115  C CB   B ARG A 6   ? 0.1315 0.1475 0.1586 0.0138  -0.0331 0.0021  5   ARG A CB   
116  C CG   A ARG A 6   ? 0.1714 0.1399 0.1786 0.0033  -0.0433 -0.0057 5   ARG A CG   
117  C CG   B ARG A 6   ? 0.2087 0.1300 0.1887 0.0156  -0.0309 0.0158  5   ARG A CG   
118  C CD   A ARG A 6   ? 0.1947 0.1415 0.2218 0.0119  -0.0624 -0.0139 5   ARG A CD   
119  C CD   B ARG A 6   ? 0.2083 0.1374 0.2138 0.0225  -0.0545 -0.0039 5   ARG A CD   
120  N NE   A ARG A 6   ? 0.2560 0.1519 0.2282 0.0373  -0.0721 0.0022  5   ARG A NE   
121  N NE   B ARG A 6   ? 0.2544 0.1497 0.2312 0.0388  -0.0685 0.0091  5   ARG A NE   
122  C CZ   A ARG A 6   ? 0.2938 0.1674 0.2252 0.0292  -0.0691 0.0150  5   ARG A CZ   
123  C CZ   B ARG A 6   ? 0.2916 0.1559 0.2196 0.0242  -0.0638 0.0147  5   ARG A CZ   
124  N NH1  A ARG A 6   ? 0.3028 0.1503 0.2198 0.0187  -0.0583 0.0212  5   ARG A NH1  
125  N NH1  B ARG A 6   ? 0.3110 0.1665 0.2185 0.0366  -0.0649 0.0135  5   ARG A NH1  
126  N NH2  A ARG A 6   ? 0.3232 0.1821 0.2263 0.0284  -0.0739 0.0146  5   ARG A NH2  
127  N NH2  B ARG A 6   ? 0.2917 0.1565 0.2207 0.0054  -0.0617 0.0224  5   ARG A NH2  
128  D D    A ARG A 6   ? 0.1245 0.1534 0.1859 -0.0008 -0.0678 0.0310  5   ARG A D    
129  D D    B ARG A 6   ? 0.2785 0.1606 0.3001 0.0645  -0.1804 -0.0304 5   ARG A D    
130  D DA   A ARG A 6   ? 0.1158 0.1641 0.1063 0.0247  -0.0256 0.0016  5   ARG A DA   
131  D DA   B ARG A 6   ? 0.1301 0.1296 0.1174 0.0154  -0.0083 -0.0039 5   ARG A DA   
132  D DB2  A ARG A 6   ? 0.1394 0.1252 0.1777 0.0145  -0.0455 0.0226  5   ARG A DB2  
133  D DB2  B ARG A 6   ? 0.1524 0.1670 0.1803 0.0208  -0.0189 -0.0412 5   ARG A DB2  
134  D DB3  A ARG A 6   ? 0.1845 0.1459 0.1453 0.0260  -0.0480 0.0151  5   ARG A DB3  
135  D DB3  B ARG A 6   ? 0.1412 0.1656 0.1835 0.0217  -0.0056 0.0055  5   ARG A DB3  
136  D DG2  A ARG A 6   ? 0.1758 0.1455 0.2051 -0.0074 -0.0392 -0.0184 5   ARG A DG2  
137  D DG2  B ARG A 6   ? 0.1990 0.0963 0.1872 0.0495  -0.0593 0.0360  5   ARG A DG2  
138  D DG3  A ARG A 6   ? 0.2053 0.1614 0.1754 0.0127  -0.0434 -0.0224 5   ARG A DG3  
139  D DG3  B ARG A 6   ? 0.2138 0.1776 0.1197 0.0087  -0.0275 -0.0069 5   ARG A DG3  
140  D DD2  A ARG A 6   ? 0.2019 0.1672 0.2581 0.0270  -0.0721 -0.0512 5   ARG A DD2  
141  D DD2  B ARG A 6   ? 0.1988 0.1721 0.2103 0.0015  -0.0255 -0.0239 5   ARG A DD2  
142  D DD3  A ARG A 6   ? 0.2012 0.1516 0.2636 0.0210  -0.0375 -0.0230 5   ARG A DD3  
143  D DD3  B ARG A 6   ? 0.2013 0.1426 0.2402 0.0179  -0.0592 -0.0026 5   ARG A DD3  
144  D DE   A ARG A 6   ? 0.3083 0.1836 0.2434 0.0224  -0.1000 -0.0126 5   ARG A DE   
145  D DE   B ARG A 6   ? 0.2970 0.2300 0.2435 0.0039  -0.0988 0.0041  5   ARG A DE   
146  D DH11 A ARG A 6   ? 0.2711 0.1577 0.2519 0.0332  -0.0682 0.0453  5   ARG A DH11 
147  D DH11 B ARG A 6   ? 0.5399 0.2252 0.1679 -0.0827 -0.1909 0.0511  5   ARG A DH11 
148  D DH12 A ARG A 6   ? 0.3120 0.1181 0.2194 0.0041  -0.0684 0.0117  5   ARG A DH12 
149  D DH12 B ARG A 6   ? 0.4158 0.2168 0.2594 -0.0759 -0.1301 0.0999  5   ARG A DH12 
150  D DH21 A ARG A 6   ? 0.4027 0.3303 0.2806 -0.0578 -0.1179 0.1156  5   ARG A DH21 
151  D DH21 B ARG A 6   ? 0.3234 0.1566 0.2111 -0.0118 -0.0444 0.0005  5   ARG A DH21 
152  D DH22 A ARG A 6   ? 0.5201 0.3275 0.2825 -0.0976 -0.1412 0.0008  5   ARG A DH22 
153  D DH22 B ARG A 6   ? 0.2911 0.1254 0.1968 0.0117  -0.0626 -0.0086 5   ARG A DH22 
154  N N    . CYS A 7   ? 0.1427 0.1354 0.1039 0.0086  -0.0236 0.0114  6   CYS A N    
155  C CA   . CYS A 7   ? 0.1546 0.1377 0.1030 0.0026  -0.0049 -0.0047 6   CYS A CA   
156  C C    . CYS A 7   ? 0.1189 0.1288 0.0984 -0.0213 0.0023  0.0012  6   CYS A C    
157  O O    . CYS A 7   ? 0.1233 0.1487 0.1217 -0.0301 -0.0032 0.0144  6   CYS A O    
158  C CB   . CYS A 7   ? 0.1867 0.1518 0.1106 -0.0169 -0.0161 0.0114  6   CYS A CB   
159  S SG   . CYS A 7   ? 0.2500 0.1699 0.1405 0.0097  0.0107  0.0442  6   CYS A SG   
160  D D    . CYS A 7   ? 0.1723 0.1778 0.1149 -0.0035 -0.0425 -0.0009 6   CYS A D    
161  D DA   . CYS A 7   ? 0.1764 0.1431 0.1079 -0.0099 -0.0125 -0.0023 6   CYS A DA   
162  D DB2  . CYS A 7   ? 0.2415 0.1946 0.1196 -0.0336 -0.0231 -0.0157 6   CYS A DB2  
163  D DB3  . CYS A 7   ? 0.2026 0.1724 0.1422 -0.0239 0.0054  0.0391  6   CYS A DB3  
164  N N    . GLU A 8   ? 0.1253 0.1296 0.0991 -0.0167 -0.0124 0.0019  7   GLU A N    
165  C CA   . GLU A 8   ? 0.1339 0.1379 0.0833 -0.0084 -0.0033 -0.0020 7   GLU A CA   
166  C C    . GLU A 8   ? 0.1131 0.1423 0.0926 -0.0027 -0.0072 -0.0009 7   GLU A C    
167  O O    . GLU A 8   ? 0.1127 0.1873 0.0917 0.0074  -0.0072 -0.0219 7   GLU A O    
168  C CB   . GLU A 8   ? 0.1547 0.1309 0.1176 -0.0121 -0.0204 -0.0024 7   GLU A CB   
169  C CG   . GLU A 8   ? 0.1611 0.1812 0.1193 -0.0221 -0.0325 -0.0039 7   GLU A CG   
170  C CD   . GLU A 8   ? 0.1714 0.1857 0.0968 -0.0084 -0.0217 -0.0086 7   GLU A CD   
171  O OE1  . GLU A 8   ? 0.1765 0.2010 0.1091 -0.0165 -0.0088 -0.0250 7   GLU A OE1  
172  O OE2  . GLU A 8   ? 0.1802 0.2188 0.0967 0.0203  -0.0009 0.0074  7   GLU A OE2  
173  D D    . GLU A 8   ? 0.1354 0.1440 0.1344 -0.0209 -0.0288 -0.0039 7   GLU A D    
174  D DA   . GLU A 8   ? 0.1341 0.1442 0.0992 0.0058  0.0014  0.0055  7   GLU A DA   
175  D DB2  . GLU A 8   ? 0.1571 0.1415 0.1214 -0.0230 -0.0250 -0.0050 7   GLU A DB2  
176  D DB3  . GLU A 8   ? 0.1832 0.1425 0.1248 -0.0010 -0.0134 -0.0068 7   GLU A DB3  
177  D DG2  . GLU A 8   ? 0.2465 0.1885 0.1567 -0.0135 -0.0705 -0.0211 7   GLU A DG2  
178  D DG3  . GLU A 8   ? 0.1721 0.2684 0.1431 -0.0097 -0.0075 -0.0024 7   GLU A DG3  
179  N N    . LEU A 9   ? 0.1025 0.1393 0.0910 0.0057  -0.0149 0.0062  8   LEU A N    
180  C CA   . LEU A 9   ? 0.1058 0.1434 0.0893 0.0020  -0.0101 0.0026  8   LEU A CA   
181  C C    . LEU A 9   ? 0.1002 0.1573 0.0898 -0.0009 -0.0074 -0.0068 8   LEU A C    
182  O O    . LEU A 9   ? 0.1112 0.1779 0.0842 -0.0156 -0.0152 0.0063  8   LEU A O    
183  C CB   . LEU A 9   ? 0.1045 0.1633 0.0920 -0.0023 -0.0117 -0.0026 8   LEU A CB   
184  C CG   . LEU A 9   ? 0.1359 0.1863 0.0860 -0.0128 -0.0062 -0.0044 8   LEU A CG   
185  C CD1  . LEU A 9   ? 0.1589 0.1942 0.0957 -0.0069 0.0034  0.0205  8   LEU A CD1  
186  C CD2  . LEU A 9   ? 0.1583 0.2393 0.1246 -0.0052 0.0297  -0.0095 8   LEU A CD2  
188  D DA   . LEU A 9   ? 0.1135 0.1454 0.1015 0.0070  -0.0197 0.0114  8   LEU A DA   
189  D DB2  . LEU A 9   ? 0.1169 0.2002 0.1309 -0.0322 -0.0217 -0.0058 8   LEU A DB2  
190  D DB3  . LEU A 9   ? 0.1242 0.1850 0.1353 0.0241  -0.0134 0.0139  8   LEU A DB3  
191  D DG   . LEU A 9   ? 0.1430 0.1961 0.1177 -0.0115 -0.0048 -0.0288 8   LEU A DG   
192  D DD11 . LEU A 9   ? 0.2535 0.1997 0.1790 -0.0300 -0.0342 0.0027  8   LEU A DD11 
193  D DD12 . LEU A 9   ? 0.2087 0.2566 0.1098 -0.0083 -0.0118 0.0460  8   LEU A DD12 
194  D DD13 . LEU A 9   ? 0.1893 0.2298 0.1872 0.0397  0.0522  0.0708  8   LEU A DD13 
195  D DD21 . LEU A 9   ? 0.1582 0.2978 0.2034 -0.0474 0.0328  -0.0115 8   LEU A DD21 
196  D DD22 . LEU A 9   ? 0.2056 0.2711 0.2195 0.0411  0.0581  0.0230  8   LEU A DD22 
197  D DD23 . LEU A 9   ? 0.2170 0.3823 0.1219 0.0420  0.0294  -0.0151 8   LEU A DD23 
198  N N    . ALA A 10  ? 0.1116 0.1529 0.0968 -0.0096 -0.0062 -0.0075 9   ALA A N    
199  C CA   . ALA A 10  ? 0.1316 0.1574 0.0984 -0.0163 -0.0132 -0.0143 9   ALA A CA   
200  C C    . ALA A 10  ? 0.1272 0.1527 0.1043 -0.0217 -0.0100 -0.0007 9   ALA A C    
201  O O    . ALA A 10  ? 0.1340 0.1689 0.1193 -0.0249 -0.0149 -0.0103 9   ALA A O    
202  C CB   . ALA A 10  ? 0.1646 0.1449 0.1394 -0.0076 -0.0269 -0.0121 9   ALA A CB   
204  D DA   . ALA A 10  ? 0.1605 0.1839 0.1028 -0.0209 -0.0131 -0.0243 9   ALA A DA   
205  D DB1  . ALA A 10  ? 0.2172 0.1593 0.1418 -0.0242 -0.0256 0.0070  9   ALA A DB1  
206  D DB2  . ALA A 10  ? 0.1832 0.1497 0.2201 -0.0048 -0.0498 -0.0330 9   ALA A DB2  
207  D DB3  . ALA A 10  ? 0.1775 0.1846 0.2116 0.0078  -0.0074 -0.0121 9   ALA A DB3  
208  N N    . ALA A 11  ? 0.1257 0.1751 0.1030 -0.0197 0.0023  -0.0034 10  ALA A N    
209  C CA   . ALA A 11  ? 0.1234 0.1907 0.1211 -0.0248 0.0091  -0.0068 10  ALA A CA   
210  C C    . ALA A 11  ? 0.1070 0.2129 0.1165 -0.0132 0.0120  -0.0077 10  ALA A C    
211  O O    . ALA A 11  ? 0.1032 0.2325 0.1491 -0.0067 0.0143  -0.0127 10  ALA A O    
212  C CB   . ALA A 11  ? 0.1654 0.2119 0.1183 0.0046  0.0183  -0.0052 10  ALA A CB   
214  D DA   . ALA A 11  ? 0.1392 0.2081 0.1513 -0.0469 0.0266  -0.0063 10  ALA A DA   
215  D DB1  . ALA A 11  ? 0.1799 0.2185 0.1192 0.0035  -0.0015 -0.0219 10  ALA A DB1  
216  D DB2  . ALA A 11  ? 0.1834 0.2852 0.1392 0.0160  0.0432  0.0013  10  ALA A DB2  
217  D DB3  . ALA A 11  ? 0.2511 0.2449 0.1421 0.0248  0.0020  0.0191  10  ALA A DB3  
218  N N    . ALA A 12  ? 0.1124 0.1918 0.0958 -0.0069 0.0049  -0.0169 11  ALA A N    
219  C CA   . ALA A 12  ? 0.0958 0.2010 0.1083 -0.0020 0.0096  -0.0111 11  ALA A CA   
220  C C    . ALA A 12  ? 0.0926 0.2154 0.1136 0.0151  -0.0022 -0.0162 11  ALA A C    
221  O O    . ALA A 12  ? 0.1082 0.1924 0.1268 0.0219  -0.0099 -0.0158 11  ALA A O    
222  C CB   . ALA A 12  ? 0.1226 0.2097 0.1319 -0.0185 -0.0219 0.0122  11  ALA A CB   
224  D DA   . ALA A 12  ? 0.1198 0.1947 0.1236 0.0116  0.0261  -0.0224 11  ALA A DA   
225  D DB1  . ALA A 12  ? 0.1325 0.1918 0.1656 -0.0292 0.0024  0.0178  11  ALA A DB1  
226  D DB2  . ALA A 12  ? 0.1832 0.1977 0.1655 0.0015  -0.0178 0.0206  11  ALA A DB2  
227  D DB3  . ALA A 12  ? 0.2067 0.1933 0.1504 -0.0330 -0.0307 -0.0012 11  ALA A DB3  
228  N N    . MET A 13  ? 0.0884 0.1826 0.1120 0.0017  -0.0076 -0.0098 12  MET A N    
229  C CA   . MET A 13  ? 0.1018 0.1894 0.1137 0.0016  -0.0195 -0.0115 12  MET A CA   
230  C C    . MET A 13  ? 0.1000 0.2140 0.1092 -0.0064 -0.0089 -0.0250 12  MET A C    
231  O O    . MET A 13  ? 0.1111 0.2678 0.1277 -0.0243 -0.0240 -0.0055 12  MET A O    
232  C CB   . MET A 13  ? 0.1010 0.1598 0.1145 -0.0144 -0.0127 -0.0073 12  MET A CB   
233  C CG   . MET A 13  ? 0.1055 0.1444 0.1450 -0.0115 -0.0031 -0.0069 12  MET A CG   
234  S SD   . MET A 13  ? 0.1346 0.1864 0.1699 0.0037  0.0300  -0.0105 12  MET A SD   
235  C CE   . MET A 13  ? 0.1759 0.2086 0.2089 -0.0146 0.0641  0.0027  12  MET A CE   
237  D DA   . MET A 13  ? 0.0985 0.2213 0.1306 0.0034  -0.0242 0.0093  12  MET A DA   
238  D DB2  . MET A 13  ? 0.1293 0.1855 0.1253 0.0074  0.0002  0.0143  12  MET A DB2  
239  D DB3  . MET A 13  ? 0.1285 0.1749 0.1183 -0.0177 -0.0042 -0.0194 12  MET A DB3  
240  D DG2  . MET A 13  ? 0.1304 0.1759 0.1778 -0.0055 -0.0049 0.0250  12  MET A DG2  
241  D DG3  . MET A 13  ? 0.1286 0.1643 0.1625 -0.0306 0.0207  -0.0275 12  MET A DG3  
242  D DE1  . MET A 13  ? 0.1900 0.2366 0.2928 -0.0198 0.0946  -0.0224 12  MET A DE1  
243  D DE2  . MET A 13  ? 0.2073 0.3327 0.2429 -0.0442 0.0357  0.0698  12  MET A DE2  
244  D DE3  . MET A 13  ? 0.2718 0.2064 0.2941 -0.0238 0.0678  -0.0192 12  MET A DE3  
245  N N    . LYS A 14  ? 0.1102 0.2316 0.1234 -0.0197 -0.0124 -0.0067 13  LYS A N    
246  C CA   . LYS A 14  ? 0.1208 0.2504 0.1644 -0.0300 0.0080  -0.0152 13  LYS A CA   
247  C C    . LYS A 14  ? 0.1080 0.2674 0.1438 -0.0316 0.0030  -0.0195 13  LYS A C    
248  O O    . LYS A 14  ? 0.1150 0.2902 0.1520 -0.0540 0.0054  -0.0275 13  LYS A O    
249  C CB   . LYS A 14  ? 0.1411 0.2527 0.1998 -0.0436 0.0011  0.0128  13  LYS A CB   
250  C CG   . LYS A 14  ? 0.1942 0.3017 0.2619 -0.0931 0.0289  0.0125  13  LYS A CG   
251  C CD   . LYS A 14  ? 0.2994 0.3071 0.3342 -0.0796 0.0585  0.0692  13  LYS A CD   
255  D DA   . LYS A 14  ? 0.1528 0.2628 0.1786 -0.0562 0.0289  -0.0358 13  LYS A DA   
256  D DB2  . LYS A 14  ? 0.1634 0.2594 0.2293 -0.0243 0.0178  0.0215  13  LYS A DB2  
257  D DB3  . LYS A 14  ? 0.1771 0.2676 0.1861 -0.0478 0.0140  0.0136  13  LYS A DB3  
258  D DG2  . LYS A 14  ? 0.1820 0.4448 0.3152 -0.0490 0.0656  0.0713  13  LYS A DG2  
259  D DG3  . LYS A 14  ? 0.3006 0.4155 0.3077 -0.2030 0.0269  -0.0387 13  LYS A DG3  
260  D DD2  . LYS A 14  ? 0.4571 0.4365 0.3562 0.0714  0.0970  0.0978  13  LYS A DD2  
261  D DD3  . LYS A 14  ? 0.5069 0.3435 0.2775 -0.0300 0.0370  0.0889  13  LYS A DD3  
267  N N    . ARG A 15  ? 0.1027 0.2725 0.1483 -0.0192 -0.0142 -0.0300 14  ARG A N    
268  C CA   . ARG A 15  ? 0.1081 0.2932 0.1682 -0.0095 0.0012  -0.0252 14  ARG A CA   
269  C C    . ARG A 15  ? 0.1247 0.2861 0.1733 0.0167  0.0091  -0.0162 14  ARG A C    
270  O O    . ARG A 15  ? 0.1238 0.3664 0.1626 0.0309  0.0127  -0.0226 14  ARG A O    
271  C CB   . ARG A 15  ? 0.1371 0.3268 0.2101 0.0290  -0.0116 -0.0705 14  ARG A CB   
272  C CG   . ARG A 15  ? 0.1764 0.3550 0.2008 0.0534  -0.0122 -0.0785 14  ARG A CG   
273  C CD   . ARG A 15  ? 0.2590 0.4054 0.2419 0.0551  -0.0222 -0.1287 14  ARG A CD   
274  N NE   . ARG A 15  ? 0.2731 0.3980 0.2696 0.0418  -0.0287 -0.1429 14  ARG A NE   
275  C CZ   . ARG A 15  ? 0.2856 0.4409 0.3083 0.0590  -0.0587 -0.1805 14  ARG A CZ   
276  N NH1  . ARG A 15  ? 0.2746 0.4485 0.3186 0.0690  -0.0911 -0.1707 14  ARG A NH1  
277  N NH2  . ARG A 15  ? 0.2956 0.4400 0.3385 0.0481  -0.0736 -0.1981 14  ARG A NH2  
278  D D    . ARG A 15  ? 0.1154 0.3362 0.1981 -0.0161 -0.0233 -0.0677 14  ARG A D    
279  D DA   . ARG A 15  ? 0.1188 0.3417 0.1633 -0.0213 0.0127  -0.0200 14  ARG A DA   
280  D DB2  . ARG A 15  ? 0.1512 0.3018 0.2343 0.0188  -0.0050 -0.0982 14  ARG A DB2  
281  D DB3  . ARG A 15  ? 0.1543 0.3440 0.2345 0.0477  0.0061  -0.0507 14  ARG A DB3  
282  D DG2  . ARG A 15  ? 0.2090 0.3909 0.2311 0.0214  0.0189  -0.0670 14  ARG A DG2  
283  D DG3  . ARG A 15  ? 0.2115 0.3666 0.2576 0.0781  0.0109  -0.0354 14  ARG A DG3  
284  D DD2  . ARG A 15  ? 0.2617 0.3910 0.2617 0.0580  -0.0318 -0.1616 14  ARG A DD2  
285  D DD3  . ARG A 15  ? 0.2864 0.4430 0.2382 0.0458  -0.0120 -0.1362 14  ARG A DD3  
286  D DE   . ARG A 15  ? 0.3632 0.4209 0.3312 0.0361  -0.0244 -0.0952 14  ARG A DE   
287  D DH11 . ARG A 15  ? 0.3888 0.3710 0.4531 0.0292  -0.2243 -0.1904 14  ARG A DH11 
288  D DH12 . ARG A 15  ? 0.2963 0.4858 0.4133 0.0449  -0.1053 -0.1077 14  ARG A DH12 
289  D DH21 . ARG A 15  ? 0.3317 0.3987 0.4714 0.0465  -0.1500 -0.2334 14  ARG A DH21 
290  D DH22 . ARG A 15  ? 0.3076 0.4169 0.4409 0.0840  -0.0130 -0.1816 14  ARG A DH22 
291  N N    A HIS A 16  ? 0.1207 0.2967 0.1639 0.0388  0.0053  -0.0187 15  HIS A N    
292  N N    B HIS A 16  ? 0.1138 0.2931 0.1625 0.0358  0.0011  -0.0186 15  HIS A N    
293  C CA   A HIS A 16  ? 0.1368 0.3035 0.1671 0.0635  0.0194  -0.0124 15  HIS A CA   
294  C CA   B HIS A 16  ? 0.1431 0.3018 0.1673 0.0617  0.0149  -0.0064 15  HIS A CA   
295  C C    A HIS A 16  ? 0.1614 0.3077 0.1651 0.0712  -0.0100 -0.0056 15  HIS A C    
296  C C    B HIS A 16  ? 0.1587 0.3024 0.1523 0.0820  -0.0224 0.0031  15  HIS A C    
297  O O    A HIS A 16  ? 0.2278 0.3069 0.1696 0.0921  -0.0126 -0.0029 15  HIS A O    
298  O O    B HIS A 16  ? 0.1823 0.3238 0.1551 0.1101  -0.0248 0.0128  15  HIS A O    
299  C CB   A HIS A 16  ? 0.1778 0.3113 0.1778 0.0470  0.0494  -0.0164 15  HIS A CB   
300  C CB   B HIS A 16  ? 0.1698 0.3160 0.1822 0.0565  0.0600  -0.0201 15  HIS A CB   
301  C CG   A HIS A 16  ? 0.2253 0.3194 0.1999 0.0211  0.0871  -0.0330 15  HIS A CG   
302  C CG   B HIS A 16  ? 0.2155 0.3190 0.1981 0.0271  0.0849  -0.0254 15  HIS A CG   
303  N ND1  A HIS A 16  ? 0.2798 0.3202 0.2079 0.0421  0.0909  -0.0391 15  HIS A ND1  
304  N ND1  B HIS A 16  ? 0.2633 0.3114 0.2051 0.0351  0.1028  -0.0265 15  HIS A ND1  
305  C CD2  A HIS A 16  ? 0.2486 0.3296 0.2048 0.0315  0.0824  -0.0526 15  HIS A CD2  
306  C CD2  B HIS A 16  ? 0.2364 0.3358 0.1953 0.0248  0.0937  -0.0421 15  HIS A CD2  
307  C CE1  A HIS A 16  ? 0.2875 0.3276 0.2105 0.0374  0.0961  -0.0442 15  HIS A CE1  
308  C CE1  B HIS A 16  ? 0.2664 0.3223 0.2176 0.0246  0.1116  -0.0391 15  HIS A CE1  
309  N NE2  A HIS A 16  ? 0.2739 0.3329 0.2080 0.0416  0.0963  -0.0527 15  HIS A NE2  
310  N NE2  B HIS A 16  ? 0.2827 0.3380 0.2070 0.0265  0.1083  -0.0500 15  HIS A NE2  
311  D D    A HIS A 16  ? 0.1463 0.4798 0.2124 0.0997  0.0353  0.0801  15  HIS A D    
312  D D    B HIS A 16  ? 0.1100 0.3581 0.2452 0.0116  -0.0022 0.0857  15  HIS A D    
313  D DA   A HIS A 16  ? 0.1605 0.3361 0.1758 0.0899  0.0502  0.0190  15  HIS A DA   
314  D DA   B HIS A 16  ? 0.1355 0.3085 0.1824 0.0558  -0.0116 -0.0216 15  HIS A DA   
315  D DB2  A HIS A 16  ? 0.1590 0.2915 0.1972 0.0248  0.0229  -0.0202 15  HIS A DB2  
316  D DB2  B HIS A 16  ? 0.1606 0.3441 0.2293 0.0587  0.0431  -0.0277 15  HIS A DB2  
317  D DB3  A HIS A 16  ? 0.1644 0.3480 0.1737 0.1060  0.0821  -0.0084 15  HIS A DB3  
318  D DB3  B HIS A 16  ? 0.1088 0.4023 0.1789 0.0794  0.0787  -0.0455 15  HIS A DB3  
319  D DD1  A HIS A 16  ? 0.7107 0.3407 0.3166 0.1693  -0.1250 -0.0964 15  HIS A DD1  
320  D DD1  B HIS A 16  ? 0.5620 0.2837 0.2689 0.1205  -0.0347 -0.0637 15  HIS A DD1  
321  D DD2  A HIS A 16  ? 0.2651 0.3462 0.1969 0.0654  0.0819  -0.0698 15  HIS A DD2  
322  D DD2  B HIS A 16  ? 0.2518 0.3704 0.1811 0.0292  0.0912  -0.0288 15  HIS A DD2  
323  D DE1  A HIS A 16  ? 0.3174 0.3245 0.2349 0.0360  0.0626  -0.0525 15  HIS A DE1  
324  D DE1  B HIS A 16  ? 0.3228 0.3172 0.3104 0.0208  0.0784  -0.0366 15  HIS A DE1  
325  D DE2  A HIS A 16  ? 0.2329 0.3587 0.1938 0.0496  0.1240  -0.0642 15  HIS A DE2  
326  D DE2  B HIS A 16  ? 0.2299 0.3661 0.1918 -0.0013 0.1580  -0.0606 15  HIS A DE2  
327  N N    A GLY A 17  ? 0.1427 0.3123 0.1495 0.0487  -0.0179 -0.0082 16  GLY A N    
328  N N    B GLY A 17  ? 0.1222 0.3111 0.1440 0.0523  -0.0362 -0.0052 16  GLY A N    
329  C CA   A GLY A 17  ? 0.1445 0.3248 0.1504 0.0425  -0.0270 -0.0083 16  GLY A CA   
330  C CA   B GLY A 17  ? 0.1333 0.3283 0.1330 0.0443  -0.0354 -0.0074 16  GLY A CA   
331  C C    A GLY A 17  ? 0.1331 0.3088 0.1420 0.0223  -0.0307 -0.0172 16  GLY A C    
332  C C    B GLY A 17  ? 0.1246 0.3109 0.1534 0.0145  -0.0232 -0.0200 16  GLY A C    
333  O O    A GLY A 17  ? 0.0823 0.2965 0.1492 -0.0463 -0.0015 -0.0123 16  GLY A O    
334  O O    B GLY A 17  ? 0.0866 0.3078 0.1617 0.0050  -0.0190 -0.0160 16  GLY A O    
335  D D    A GLY A 17  ? 0.1756 0.2995 0.1474 0.0483  -0.0224 -0.0130 16  GLY A D    
336  D D    B GLY A 17  ? 0.2856 0.2604 0.1485 0.0472  -0.0673 -0.0062 16  GLY A D    
337  D DA2  A GLY A 17  ? 0.1790 0.3363 0.1047 0.0296  -0.0116 -0.0230 16  GLY A DA2  
338  D DA2  B GLY A 17  ? 0.1366 0.3375 0.1321 0.0253  -0.0471 -0.0076 16  GLY A DA2  
339  D DA3  A GLY A 17  ? 0.0687 0.3735 0.1464 0.0276  0.0010  0.0164  16  GLY A DA3  
340  D DA3  B GLY A 17  ? 0.1511 0.3674 0.1144 0.0602  -0.0356 -0.0120 16  GLY A DA3  
341  N N    . LEU A 18  ? 0.1279 0.2980 0.1437 0.0088  -0.0327 -0.0410 17  LEU A N    
342  C CA   . LEU A 18  ? 0.1192 0.2947 0.1331 -0.0041 -0.0218 -0.0289 17  LEU A CA   
343  C C    . LEU A 18  ? 0.1036 0.2923 0.1311 -0.0122 0.0053  -0.0277 17  LEU A C    
344  O O    . LEU A 18  ? 0.1385 0.3199 0.1264 0.0385  0.0055  -0.0115 17  LEU A O    
345  C CB   . LEU A 18  ? 0.1235 0.2698 0.1507 -0.0015 -0.0269 -0.0102 17  LEU A CB   
346  C CG   . LEU A 18  ? 0.1419 0.2692 0.1853 0.0137  -0.0316 0.0080  17  LEU A CG   
347  C CD1  . LEU A 18  ? 0.1542 0.2759 0.2096 -0.0075 -0.0250 0.0178  17  LEU A CD1  
348  C CD2  . LEU A 18  ? 0.1973 0.2759 0.1867 0.0305  -0.0483 0.0217  17  LEU A CD2  
349  D D    . LEU A 18  ? 0.1829 0.3520 0.1760 0.0147  -0.0490 -0.0781 17  LEU A D    
350  D DA   . LEU A 18  ? 0.1143 0.3218 0.1367 -0.0067 -0.0179 -0.0209 17  LEU A DA   
351  D DB2  . LEU A 18  ? 0.1268 0.2559 0.1603 -0.0307 -0.0393 0.0024  17  LEU A DB2  
352  D DB3  . LEU A 18  ? 0.1248 0.2610 0.2247 0.0018  -0.0147 -0.0214 17  LEU A DB3  
353  D DG   . LEU A 18  ? 0.1622 0.2635 0.2651 -0.0015 -0.0056 -0.0286 17  LEU A DG   
354  D DD11 . LEU A 18  ? 0.1421 0.2601 0.3410 -0.0360 0.0072  -0.0092 17  LEU A DD11 
355  D DD12 . LEU A 18  ? 0.2037 0.2776 0.2565 -0.0066 0.0056  0.0284  17  LEU A DD12 
356  D DD13 . LEU A 18  ? 0.2810 0.2887 0.2316 -0.0791 -0.0630 0.0017  17  LEU A DD13 
357  D DD21 . LEU A 18  ? 0.2601 0.3107 0.1936 0.0699  -0.0512 -0.0052 17  LEU A DD21 
358  D DD22 . LEU A 18  ? 0.2271 0.3568 0.1977 -0.0121 -0.0694 0.0139  17  LEU A DD22 
359  D DD23 . LEU A 18  ? 0.2649 0.2918 0.2368 0.0413  -0.0278 0.0540  17  LEU A DD23 
360  N N    . ASP A 19  ? 0.1449 0.3212 0.1184 -0.0213 0.0015  -0.0271 18  ASP A N    
361  C CA   . ASP A 19  ? 0.1450 0.3249 0.1392 -0.0253 -0.0012 -0.0032 18  ASP A CA   
362  C C    . ASP A 19  ? 0.1208 0.2839 0.1504 -0.0139 -0.0159 0.0185  18  ASP A C    
363  O O    . ASP A 19  ? 0.1289 0.3926 0.1735 0.0020  -0.0106 -0.0152 18  ASP A O    
364  C CB   . ASP A 19  ? 0.1706 0.3836 0.1445 -0.0380 -0.0005 0.0161  18  ASP A CB   
365  C CG   . ASP A 19  ? 0.2265 0.3754 0.1699 -0.0422 0.0339  0.0310  18  ASP A CG   
366  O OD1  . ASP A 19  ? 0.2068 0.4017 0.1619 -0.0196 0.0069  0.0251  18  ASP A OD1  
367  O OD2  . ASP A 19  ? 0.4258 0.4516 0.2522 0.0229  0.1563  0.0925  18  ASP A OD2  
368  D D    . ASP A 19  ? 0.1699 0.3231 0.1159 -0.0392 0.0216  -0.0435 18  ASP A D    
369  D DA   . ASP A 19  ? 0.1395 0.3429 0.1397 -0.0212 -0.0186 0.0149  18  ASP A DA   
370  D DB2  . ASP A 19  ? 0.2319 0.3921 0.1445 -0.0173 -0.0014 -0.0149 18  ASP A DB2  
371  D DB3  . ASP A 19  ? 0.1764 0.4880 0.1869 -0.0199 0.0251  0.0710  18  ASP A DB3  
372  N N    A ASN A 20  ? 0.1165 0.2179 0.1476 -0.0341 -0.0164 0.0354  19  ASN A N    
373  N N    B ASN A 20  ? 0.1244 0.2162 0.1424 -0.0238 -0.0157 0.0436  19  ASN A N    
374  C CA   A ASN A 20  ? 0.1263 0.2012 0.1645 -0.0374 -0.0254 0.0363  19  ASN A CA   
375  C CA   B ASN A 20  ? 0.1375 0.2082 0.1617 -0.0265 -0.0190 0.0385  19  ASN A CA   
376  C C    A ASN A 20  ? 0.1230 0.2086 0.1474 -0.0387 -0.0139 0.0345  19  ASN A C    
377  C C    B ASN A 20  ? 0.1311 0.2076 0.1516 -0.0234 -0.0262 0.0267  19  ASN A C    
378  O O    A ASN A 20  ? 0.1538 0.2017 0.1470 -0.0449 -0.0219 0.0401  19  ASN A O    
379  O O    B ASN A 20  ? 0.1371 0.2410 0.1763 -0.0312 -0.0335 0.0066  19  ASN A O    
380  C CB   A ASN A 20  ? 0.1735 0.1908 0.1800 -0.0391 0.0086  0.0350  19  ASN A CB   
381  C CB   B ASN A 20  ? 0.1488 0.1944 0.1709 -0.0280 -0.0074 0.0286  19  ASN A CB   
382  C CG   A ASN A 20  ? 0.2154 0.1731 0.1852 -0.0128 0.0073  0.0188  19  ASN A CG   
383  C CG   B ASN A 20  ? 0.1814 0.1723 0.1599 -0.0134 -0.0119 0.0406  19  ASN A CG   
384  O OD1  A ASN A 20  ? 0.2117 0.1428 0.2471 -0.0197 -0.0032 0.0062  19  ASN A OD1  
385  O OD1  B ASN A 20  ? 0.1799 0.1794 0.2092 -0.0272 0.0090  0.0169  19  ASN A OD1  
386  N ND2  A ASN A 20  ? 0.2588 0.2004 0.1898 0.0053  0.0307  0.0450  19  ASN A ND2  
387  N ND2  B ASN A 20  ? 0.1834 0.1735 0.1313 -0.0169 -0.0033 -0.0028 19  ASN A ND2  
388  D D    A ASN A 20  ? 0.1187 0.2063 0.1500 -0.0424 -0.0016 0.0203  19  ASN A D    
389  D D    B ASN A 20  ? 0.1244 0.2799 0.1911 -0.0230 -0.0100 -0.0139 19  ASN A D    
390  D DA   A ASN A 20  ? 0.1306 0.2265 0.1660 -0.0299 -0.0298 0.0204  19  ASN A DA   
391  D DA   B ASN A 20  ? 0.1230 0.2016 0.1661 -0.0358 -0.0221 0.0366  19  ASN A DA   
392  D DB2  A ASN A 20  ? 0.1729 0.2183 0.1859 -0.0136 0.0175  0.0768  19  ASN A DB2  
393  D DB2  B ASN A 20  ? 0.1756 0.1959 0.1784 -0.0416 -0.0185 0.0388  19  ASN A DB2  
394  D DB3  A ASN A 20  ? 0.2213 0.1658 0.2003 -0.0818 -0.0077 0.0482  19  ASN A DB3  
395  D DB3  B ASN A 20  ? 0.1268 0.1606 0.2283 -0.0543 -0.0152 0.0129  19  ASN A DB3  
396  D DD21 A ASN A 20  ? 0.3223 0.2447 0.2463 0.0216  0.0233  0.0919  19  ASN A DD21 
397  D DD21 B ASN A 20  ? 0.1704 0.2086 0.1875 -0.0191 0.0179  -0.0561 19  ASN A DD21 
398  D DD22 A ASN A 20  ? 0.2522 0.1719 0.2436 -0.0194 0.0387  -0.0020 19  ASN A DD22 
399  D DD22 B ASN A 20  ? 0.1886 0.2189 0.1648 -0.0315 -0.0039 -0.0649 19  ASN A DD22 
400  N N    . TYR A 21  ? 0.1296 0.1956 0.1308 -0.0124 -0.0206 0.0150  20  TYR A N    
401  C CA   . TYR A 21  ? 0.1133 0.1813 0.1353 0.0013  -0.0122 0.0089  20  TYR A CA   
402  C C    . TYR A 21  ? 0.1170 0.1460 0.1275 0.0071  -0.0290 0.0154  20  TYR A C    
403  O O    . TYR A 21  ? 0.1198 0.1441 0.1412 -0.0050 -0.0239 -0.0174 20  TYR A O    
404  C CB   . TYR A 21  ? 0.1519 0.1768 0.1347 0.0021  -0.0191 -0.0079 20  TYR A CB   
405  C CG   . TYR A 21  ? 0.1348 0.1582 0.1402 -0.0254 -0.0141 -0.0040 20  TYR A CG   
406  C CD1  . TYR A 21  ? 0.1379 0.1920 0.2067 -0.0152 -0.0134 0.0502  20  TYR A CD1  
407  C CD2  . TYR A 21  ? 0.1865 0.1563 0.1477 -0.0267 0.0142  -0.0088 20  TYR A CD2  
408  C CE1  . TYR A 21  ? 0.1796 0.1891 0.2196 -0.0147 -0.0363 0.0525  20  TYR A CE1  
409  C CE2  . TYR A 21  ? 0.2528 0.1477 0.1640 -0.0286 0.0167  0.0107  20  TYR A CE2  
410  C CZ   . TYR A 21  ? 0.2283 0.1695 0.1890 -0.0577 -0.0447 0.0304  20  TYR A CZ   
411  O OH   . TYR A 21  ? 0.3178 0.1773 0.1726 -0.0533 -0.0690 0.0188  20  TYR A OH   
412  D D    . TYR A 21  ? 0.2037 0.2197 0.2021 -0.0486 -0.0925 0.0520  20  TYR A D    
413  D DA   . TYR A 21  ? 0.1157 0.1887 0.1637 0.0002  -0.0124 0.0297  20  TYR A DA   
414  D DB2  . TYR A 21  ? 0.2412 0.2234 0.1264 0.0252  -0.0179 -0.0161 20  TYR A DB2  
415  D DB3  . TYR A 21  ? 0.1605 0.2325 0.1795 -0.0193 -0.0462 0.0152  20  TYR A DB3  
416  D DD1  . TYR A 21  ? 0.1472 0.4108 0.3376 0.0751  0.0572  0.2020  20  TYR A DD1  
417  D DD2  . TYR A 21  ? 0.2185 0.2596 0.2127 0.0341  0.0504  0.0259  20  TYR A DD2  
418  D DE1  . TYR A 21  ? 0.1885 0.2821 0.4518 0.0236  -0.0258 0.1696  20  TYR A DE1  
419  D DE2  . TYR A 21  ? 0.3304 0.2062 0.2139 0.0088  0.0728  0.0477  20  TYR A DE2  
420  D DH   . TYR A 21  ? 0.4958 0.4433 0.2407 0.1044  0.0618  0.1270  20  TYR A DH   
421  N N    . ARG A 22  ? 0.1290 0.1617 0.1438 -0.0021 -0.0399 0.0110  21  ARG A N    
422  C CA   . ARG A 22  ? 0.1479 0.1298 0.1565 -0.0126 -0.0403 0.0018  21  ARG A CA   
423  C C    . ARG A 22  ? 0.1407 0.1288 0.1867 -0.0160 -0.0438 0.0085  21  ARG A C    
424  O O    . ARG A 22  ? 0.1508 0.1294 0.1882 -0.0061 -0.0453 0.0047  21  ARG A O    
425  C CB   . ARG A 22  ? 0.2168 0.1416 0.1389 -0.0110 -0.0331 0.0082  21  ARG A CB   
426  C CG   . ARG A 22  ? 0.2336 0.1762 0.1979 0.0086  -0.0246 0.0497  21  ARG A CG   
427  C CD   . ARG A 22  ? 0.2577 0.2188 0.2556 0.0059  -0.0854 0.0713  21  ARG A CD   
428  N NE   . ARG A 22  ? 0.4287 0.2213 0.2523 0.0138  -0.1138 0.0305  21  ARG A NE   
429  C CZ   . ARG A 22  ? 0.5429 0.2281 0.2390 0.0274  -0.0874 0.0227  21  ARG A CZ   
430  N NH1  . ARG A 22  ? 0.6397 0.2283 0.2856 0.0489  -0.0292 0.0273  21  ARG A NH1  
431  N NH2  . ARG A 22  ? 0.5771 0.2109 0.2199 0.0101  -0.0776 0.0196  21  ARG A NH2  
432  D D    . ARG A 22  ? 0.1308 0.2102 0.1842 0.0062  -0.0321 0.0026  21  ARG A D    
433  D DA   . ARG A 22  ? 0.1754 0.1885 0.1815 -0.0279 -0.0784 -0.0056 21  ARG A DA   
434  D DB2  . ARG A 22  ? 0.1905 0.1613 0.2065 -0.0379 -0.0237 0.0286  21  ARG A DB2  
435  D DB3  . ARG A 22  ? 0.3556 0.1895 0.1477 0.0414  -0.0016 0.0086  21  ARG A DB3  
436  D DG2  . ARG A 22  ? 0.2676 0.2527 0.2223 0.0581  -0.0103 0.0259  21  ARG A DG2  
437  D DG3  . ARG A 22  ? 0.2398 0.1543 0.2715 0.0343  0.0161  0.0587  21  ARG A DG3  
438  D DD2  . ARG A 22  ? 0.2682 0.3012 0.3431 -0.0561 -0.0961 0.1122  21  ARG A DD2  
439  D DD3  . ARG A 22  ? 0.2939 0.3089 0.3369 0.0552  -0.0914 0.0993  21  ARG A DD3  
440  D DE   . ARG A 22  ? 1.2378 0.2725 0.5872 0.2364  0.4983  0.1817  21  ARG A DE   
441  D DH11 . ARG A 22  ? 0.5657 0.2319 0.2281 0.0512  -0.1991 -0.0119 21  ARG A DH11 
442  D DH12 . ARG A 22  ? 1.0319 0.2159 0.2680 0.0585  0.0400  -0.0060 21  ARG A DH12 
443  D DH21 . ARG A 22  ? 0.6230 0.3226 0.2623 0.0011  -0.0633 0.1067  21  ARG A DH21 
444  D DH22 . ARG A 22  ? 0.6990 0.3100 0.2603 0.0816  -0.0267 -0.0136 21  ARG A DH22 
445  N N    . GLY A 23  ? 0.1387 0.1394 0.1936 -0.0324 -0.0577 0.0211  22  GLY A N    
446  C CA   . GLY A 23  ? 0.1532 0.1268 0.2416 -0.0394 -0.0705 0.0246  22  GLY A CA   
447  C C    . GLY A 23  ? 0.1506 0.1154 0.2095 -0.0326 -0.0609 0.0478  22  GLY A C    
448  O O    . GLY A 23  ? 0.1742 0.1156 0.2792 -0.0268 -0.0834 0.0417  22  GLY A O    
449  D D    . GLY A 23  ? 0.1845 0.1480 0.1908 -0.0175 -0.0385 0.0312  22  GLY A D    
450  D DA2  . GLY A 23  ? 0.1649 0.1474 0.3432 -0.0419 -0.0468 0.0733  22  GLY A DA2  
451  D DA3  . GLY A 23  ? 0.2134 0.1492 0.2768 -0.0211 -0.0929 -0.0182 22  GLY A DA3  
452  N N    . TYR A 24  ? 0.1190 0.1305 0.1443 -0.0209 -0.0317 0.0312  23  TYR A N    
453  C CA   . TYR A 24  ? 0.1121 0.1404 0.1368 -0.0152 -0.0228 0.0162  23  TYR A CA   
454  C C    . TYR A 24  ? 0.1209 0.1705 0.1357 -0.0111 -0.0194 0.0190  23  TYR A C    
455  O O    . TYR A 24  ? 0.1252 0.1807 0.1346 -0.0057 -0.0270 0.0097  23  TYR A O    
456  C CB   . TYR A 24  ? 0.1400 0.1483 0.1372 -0.0363 -0.0086 0.0010  23  TYR A CB   
457  C CG   . TYR A 24  ? 0.1231 0.1331 0.1336 -0.0370 -0.0190 0.0008  23  TYR A CG   
458  C CD1  . TYR A 24  ? 0.1502 0.1118 0.1427 -0.0153 -0.0096 0.0105  23  TYR A CD1  
459  C CD2  . TYR A 24  ? 0.1454 0.1484 0.1387 -0.0190 -0.0192 0.0110  23  TYR A CD2  
460  C CE1  . TYR A 24  ? 0.1576 0.1380 0.1508 -0.0294 -0.0021 -0.0141 23  TYR A CE1  
461  C CE2  . TYR A 24  ? 0.1585 0.1760 0.1346 -0.0352 -0.0255 -0.0096 23  TYR A CE2  
462  C CZ   . TYR A 24  ? 0.1665 0.1379 0.1381 -0.0534 0.0032  0.0010  23  TYR A CZ   
463  O OH   . TYR A 24  ? 0.2186 0.1666 0.1446 -0.0563 0.0128  -0.0186 23  TYR A OH   
465  D D    B TYR A 24  ? 0.1358 0.1375 0.1718 -0.0098 -0.0431 0.0338  23  TYR A D    
466  D DA   . TYR A 24  ? 0.1127 0.1533 0.1589 -0.0037 -0.0149 0.0068  23  TYR A DA   
467  D DB2  . TYR A 24  ? 0.1834 0.1309 0.1493 -0.0340 0.0017  -0.0031 23  TYR A DB2  
468  D DB3  . TYR A 24  ? 0.1540 0.1800 0.1530 -0.0534 -0.0081 -0.0352 23  TYR A DB3  
469  D DD1  . TYR A 24  ? 0.1792 0.1523 0.1497 0.0075  -0.0174 0.0151  23  TYR A DD1  
470  D DD2  . TYR A 24  ? 0.1433 0.2079 0.1638 0.0091  -0.0290 0.0007  23  TYR A DD2  
471  D DE1  . TYR A 24  ? 0.2051 0.2061 0.1841 0.0225  0.0390  0.0114  23  TYR A DE1  
472  D DE2  . TYR A 24  ? 0.1977 0.2676 0.1297 -0.0229 -0.0455 -0.0146 23  TYR A DE2  
473  D DH   . TYR A 24  ? 0.2669 0.2311 0.2150 -0.0061 0.0438  -0.0166 23  TYR A DH   
474  N N    . SER A 25  ? 0.1172 0.1901 0.1381 0.0033  0.0057  0.0348  24  SER A N    
475  C CA   . SER A 25  ? 0.1275 0.2005 0.1369 -0.0033 0.0092  0.0417  24  SER A CA   
476  C C    . SER A 25  ? 0.1010 0.2133 0.1285 0.0001  0.0015  0.0419  24  SER A C    
477  O O    . SER A 25  ? 0.1084 0.2435 0.1339 -0.0138 -0.0016 0.0558  24  SER A O    
478  C CB   . SER A 25  ? 0.1899 0.2101 0.1585 0.0232  0.0028  0.0559  24  SER A CB   
479  O OG   . SER A 25  ? 0.1870 0.2583 0.2004 0.0368  -0.0074 0.0617  24  SER A OG   
480  D D    . SER A 25  ? 0.1114 0.2174 0.1626 0.0220  -0.0085 0.0185  24  SER A D    
481  D DA   . SER A 25  ? 0.1230 0.1942 0.1549 -0.0079 0.0104  0.0370  24  SER A DA   
482  D DB2  . SER A 25  ? 0.2968 0.2367 0.1635 0.0541  0.0293  0.0643  24  SER A DB2  
483  D DB3  . SER A 25  ? 0.2210 0.2157 0.2240 0.0081  0.0017  0.0416  24  SER A DB3  
484  D DG   . SER A 25  ? 0.2870 1.8519 0.4749 0.1409  -0.1346 -0.4582 24  SER A DG   
485  N N    . LEU A 26  ? 0.1199 0.2086 0.1405 -0.0199 0.0112  0.0296  25  LEU A N    
486  C CA   . LEU A 26  ? 0.1236 0.1819 0.1344 -0.0033 0.0041  0.0486  25  LEU A CA   
487  C C    . LEU A 26  ? 0.1267 0.1572 0.1154 -0.0079 -0.0045 0.0389  25  LEU A C    
488  O O    . LEU A 26  ? 0.1358 0.1517 0.1276 -0.0056 0.0031  0.0315  25  LEU A O    
489  C CB   . LEU A 26  ? 0.1442 0.1958 0.1398 -0.0116 0.0165  0.0313  25  LEU A CB   
490  C CG   . LEU A 26  ? 0.1607 0.1979 0.1568 -0.0264 0.0168  0.0292  25  LEU A CG   
491  C CD1  . LEU A 26  ? 0.2752 0.2064 0.1885 0.0303  0.0143  0.0242  25  LEU A CD1  
492  C CD2  . LEU A 26  ? 0.2051 0.2146 0.1637 -0.0282 0.0349  0.0053  25  LEU A CD2  
493  D D    . LEU A 26  ? 0.1319 0.2126 0.1367 -0.0283 0.0161  0.0089  25  LEU A D    
494  D DA   . LEU A 26  ? 0.1390 0.2001 0.1621 0.0159  -0.0088 0.0557  25  LEU A DA   
495  D DB2  . LEU A 26  ? 0.1473 0.2208 0.1335 -0.0170 0.0274  0.0025  25  LEU A DB2  
496  D DB3  . LEU A 26  ? 0.1874 0.2089 0.1501 -0.0014 0.0289  0.0483  25  LEU A DB3  
497  D DG   . LEU A 26  ? 0.1568 0.2023 0.1841 -0.0127 0.0380  -0.0183 25  LEU A DG   
498  D DD11 . LEU A 26  ? 0.2986 0.2312 0.2976 0.0195  -0.0482 0.0784  25  LEU A DD11 
499  D DD12 . LEU A 26  ? 0.3967 0.2148 0.2380 0.0325  0.0005  -0.0003 25  LEU A DD12 
500  D DD13 . LEU A 26  ? 0.3716 0.2814 0.2113 0.0879  0.0585  0.0889  25  LEU A DD13 
501  D DD21 . LEU A 26  ? 0.2129 0.2990 0.1687 -0.0488 0.0347  -0.0115 25  LEU A DD21 
502  D DD22 . LEU A 26  ? 0.3036 0.2616 0.1432 0.0264  0.0338  0.0132  25  LEU A DD22 
503  D DD23 . LEU A 26  ? 0.2670 0.2432 0.2108 -0.0292 0.0216  -0.0354 25  LEU A DD23 
504  N N    . GLY A 27  ? 0.1254 0.1429 0.1111 -0.0174 -0.0152 0.0235  26  GLY A N    
505  C CA   . GLY A 27  ? 0.1242 0.1465 0.1188 -0.0210 -0.0201 0.0212  26  GLY A CA   
506  C C    . GLY A 27  ? 0.1085 0.1123 0.1192 -0.0044 -0.0224 0.0208  26  GLY A C    
507  O O    . GLY A 27  ? 0.1200 0.1611 0.1195 -0.0292 -0.0266 0.0209  26  GLY A O    
508  D D    . GLY A 27  ? 0.1317 0.1588 0.1801 -0.0289 -0.0304 0.0445  26  GLY A D    
509  D DA2  . GLY A 27  ? 0.1496 0.1939 0.1353 -0.0253 -0.0129 -0.0095 26  GLY A DA2  
510  D DA3  . GLY A 27  ? 0.1371 0.1638 0.1618 -0.0043 0.0066  0.0456  26  GLY A DA3  
511  N N    . ASN A 28  ? 0.0952 0.1236 0.1167 -0.0034 -0.0122 0.0124  27  ASN A N    
512  C CA   . ASN A 28  ? 0.0973 0.1077 0.1159 -0.0055 -0.0071 0.0021  27  ASN A CA   
513  C C    . ASN A 28  ? 0.1002 0.1055 0.1145 -0.0028 -0.0139 0.0092  27  ASN A C    
514  O O    . ASN A 28  ? 0.1079 0.1045 0.1480 -0.0012 -0.0003 0.0148  27  ASN A O    
515  C CB   . ASN A 28  ? 0.1170 0.1237 0.1166 -0.0058 -0.0188 0.0077  27  ASN A CB   
516  C CG   . ASN A 28  ? 0.1621 0.1238 0.1270 -0.0289 -0.0064 -0.0044 27  ASN A CG   
517  O OD1  . ASN A 28  ? 0.1890 0.1141 0.1607 -0.0063 0.0130  -0.0037 27  ASN A OD1  
518  N ND2  . ASN A 28  ? 0.1933 0.1534 0.1674 -0.0627 -0.0018 -0.0055 27  ASN A ND2  
520  D DA   . ASN A 28  ? 0.0990 0.1136 0.1496 0.0044  -0.0020 0.0127  27  ASN A DA   
521  D DB2  . ASN A 28  ? 0.1213 0.1582 0.1377 -0.0005 -0.0193 -0.0107 27  ASN A DB2  
522  D DB3  . ASN A 28  ? 0.1340 0.1189 0.1264 -0.0086 -0.0163 0.0126  27  ASN A DB3  
523  D DD21 . ASN A 28  ? 0.2392 0.1564 0.2242 -0.0772 -0.0032 -0.0209 27  ASN A DD21 
524  D DD22 . ASN A 28  ? 0.2015 0.1899 0.2279 -0.0822 0.0290  -0.0349 27  ASN A DD22 
525  N N    A TRP A 29  ? 0.1137 0.1174 0.1043 0.0073  -0.0109 0.0072  28  TRP A N    
526  N N    B TRP A 29  ? 0.1084 0.1120 0.1026 0.0037  -0.0147 0.0078  28  TRP A N    
527  C CA   A TRP A 29  ? 0.1064 0.1162 0.0999 0.0080  -0.0131 0.0084  28  TRP A CA   
528  C CA   B TRP A 29  ? 0.1047 0.1117 0.0992 0.0022  -0.0109 0.0107  28  TRP A CA   
529  C C    A TRP A 29  ? 0.1110 0.1215 0.1056 0.0022  -0.0192 0.0139  28  TRP A C    
530  C C    B TRP A 29  ? 0.1018 0.1160 0.1040 -0.0081 -0.0125 0.0161  28  TRP A C    
531  O O    A TRP A 29  ? 0.1249 0.1045 0.0895 0.0085  -0.0200 0.0039  28  TRP A O    
532  O O    B TRP A 29  ? 0.0927 0.1094 0.1322 -0.0008 -0.0028 0.0184  28  TRP A O    
533  C CB   A TRP A 29  ? 0.1070 0.1107 0.1100 0.0021  -0.0043 0.0140  28  TRP A CB   
534  C CB   B TRP A 29  ? 0.1082 0.1123 0.1175 0.0080  -0.0136 0.0092  28  TRP A CB   
535  C CG   A TRP A 29  ? 0.1053 0.1131 0.1142 -0.0080 -0.0060 0.0220  28  TRP A CG   
536  C CG   B TRP A 29  ? 0.1098 0.1170 0.1121 0.0023  -0.0144 0.0217  28  TRP A CG   
537  C CD1  A TRP A 29  ? 0.1165 0.1066 0.1345 -0.0042 -0.0185 0.0354  28  TRP A CD1  
538  C CD1  B TRP A 29  ? 0.1234 0.1265 0.1285 -0.0094 -0.0159 0.0238  28  TRP A CD1  
539  C CD2  A TRP A 29  ? 0.1097 0.1214 0.1212 -0.0100 -0.0140 0.0328  28  TRP A CD2  
540  C CD2  B TRP A 29  ? 0.1294 0.1257 0.1161 0.0032  -0.0233 0.0278  28  TRP A CD2  
541  N NE1  A TRP A 29  ? 0.1039 0.1277 0.1384 -0.0146 -0.0132 0.0264  28  TRP A NE1  
542  N NE1  B TRP A 29  ? 0.1368 0.1303 0.1361 -0.0066 -0.0273 0.0129  28  TRP A NE1  
543  C CE2  A TRP A 29  ? 0.1188 0.1195 0.1266 -0.0054 -0.0199 0.0237  28  TRP A CE2  
544  C CE2  B TRP A 29  ? 0.1272 0.1346 0.1294 0.0120  -0.0337 0.0233  28  TRP A CE2  
545  C CE3  A TRP A 29  ? 0.1327 0.1231 0.1392 -0.0061 -0.0013 0.0414  28  TRP A CE3  
546  C CE3  B TRP A 29  ? 0.1509 0.1312 0.1344 0.0015  -0.0061 0.0366  28  TRP A CE3  
547  C CZ2  A TRP A 29  ? 0.1575 0.1460 0.1314 0.0063  -0.0374 0.0111  28  TRP A CZ2  
548  C CZ2  B TRP A 29  ? 0.1631 0.1563 0.1259 0.0109  -0.0426 0.0183  28  TRP A CZ2  
549  C CZ3  A TRP A 29  ? 0.1822 0.1488 0.1371 0.0102  -0.0071 0.0511  28  TRP A CZ3  
550  C CZ3  B TRP A 29  ? 0.1639 0.1602 0.1364 0.0080  -0.0026 0.0476  28  TRP A CZ3  
551  C CH2  A TRP A 29  ? 0.1942 0.1564 0.1330 0.0228  -0.0303 0.0325  28  TRP A CH2  
552  C CH2  B TRP A 29  ? 0.1810 0.1651 0.1366 0.0219  -0.0232 0.0363  28  TRP A CH2  
555  D DA   A TRP A 29  ? 0.1288 0.1322 0.1003 0.0213  -0.0086 0.0133  28  TRP A DA   
556  D DA   B TRP A 29  ? 0.1085 0.1375 0.1033 -0.0131 -0.0095 0.0145  28  TRP A DA   
557  D DB2  A TRP A 29  ? 0.1528 0.1332 0.1062 0.0137  0.0076  0.0172  28  TRP A DB2  
558  D DB2  B TRP A 29  ? 0.1000 0.1375 0.1159 -0.0024 -0.0176 0.0013  28  TRP A DB2  
559  D DB3  A TRP A 29  ? 0.0882 0.1129 0.1411 -0.0029 0.0169  0.0034  28  TRP A DB3  
560  D DB3  B TRP A 29  ? 0.1100 0.1098 0.1827 0.0052  -0.0014 0.0164  28  TRP A DB3  
561  D DD1  A TRP A 29  ? 0.1587 0.1553 0.1638 -0.0400 -0.0322 0.0787  28  TRP A DD1  
562  D DD1  B TRP A 29  ? 0.1214 0.2117 0.1664 -0.0481 -0.0357 0.0816  28  TRP A DD1  
565  D DE3  A TRP A 29  ? 0.2025 0.1665 0.2386 -0.0583 -0.0650 0.0730  28  TRP A DE3  
566  D DE3  B TRP A 29  ? 0.1792 0.1625 0.1735 -0.0282 -0.0358 0.0571  28  TRP A DE3  
567  D DZ2  A TRP A 29  ? 0.2067 0.1471 0.2134 0.0077  -0.1012 -0.0033 28  TRP A DZ2  
568  D DZ2  B TRP A 29  ? 0.2002 0.1241 0.1907 0.0330  -0.1022 0.0146  28  TRP A DZ2  
569  D DZ3  A TRP A 29  ? 0.2960 0.1621 0.1356 -0.0145 0.0099  0.0522  28  TRP A DZ3  
570  D DZ3  B TRP A 29  ? 0.2165 0.2298 0.1556 -0.0333 -0.0216 0.0945  28  TRP A DZ3  
571  D DH2  A TRP A 29  ? 0.3593 0.2633 0.1690 -0.0186 -0.1018 0.0715  28  TRP A DH2  
572  D DH2  B TRP A 29  ? 0.1731 0.3710 0.1723 -0.0417 -0.0536 0.1188  28  TRP A DH2  
573  N N    . VAL A 30  ? 0.1093 0.1272 0.1016 -0.0086 -0.0125 0.0157  29  VAL A N    
574  C CA   . VAL A 30  ? 0.0978 0.1301 0.0994 -0.0054 -0.0085 0.0177  29  VAL A CA   
575  C C    . VAL A 30  ? 0.1072 0.1101 0.0985 0.0021  -0.0098 0.0239  29  VAL A C    
576  O O    . VAL A 30  ? 0.1018 0.1404 0.1228 -0.0140 0.0284  -0.0035 29  VAL A O    
577  C CB   . VAL A 30  ? 0.1317 0.1455 0.0915 -0.0190 -0.0052 0.0159  29  VAL A CB   
578  C CG1  . VAL A 30  ? 0.1540 0.1689 0.1031 -0.0133 -0.0277 0.0186  29  VAL A CG1  
579  C CG2  . VAL A 30  ? 0.1334 0.1803 0.1200 -0.0187 0.0120  0.0239  29  VAL A CG2  
581  D DA   . VAL A 30  ? 0.1007 0.1307 0.1124 -0.0042 0.0010  0.0078  29  VAL A DA   
582  D DB   . VAL A 30  ? 0.1403 0.1390 0.1317 -0.0210 -0.0158 0.0271  29  VAL A DB   
583  D DG11 . VAL A 30  ? 0.2536 0.1732 0.1599 -0.0274 -0.0445 -0.0134 29  VAL A DG11 
584  D DG12 . VAL A 30  ? 0.2155 0.2393 0.1009 -0.0130 -0.0362 0.0391  29  VAL A DG12 
585  D DG13 . VAL A 30  ? 0.1453 0.2140 0.1551 -0.0142 -0.0292 0.0264  29  VAL A DG13 
586  D DG21 . VAL A 30  ? 0.2036 0.1872 0.2226 0.0005  0.0682  0.0122  29  VAL A DG21 
587  D DG22 . VAL A 30  ? 0.1434 0.3034 0.1559 -0.0001 -0.0014 -0.0292 29  VAL A DG22 
588  D DG23 . VAL A 30  ? 0.1702 0.2723 0.1438 0.0036  0.0440  0.0613  29  VAL A DG23 
589  N N    . CYS A 31  ? 0.1061 0.1192 0.1176 -0.0061 -0.0025 0.0124  30  CYS A N    
590  C CA   . CYS A 31  ? 0.0994 0.1125 0.1187 -0.0021 -0.0096 0.0193  30  CYS A CA   
591  C C    . CYS A 31  ? 0.1063 0.1086 0.1211 -0.0066 -0.0083 0.0210  30  CYS A C    
592  O O    . CYS A 31  ? 0.1068 0.1186 0.1339 -0.0168 -0.0090 0.0143  30  CYS A O    
593  C CB   . CYS A 31  ? 0.1269 0.1038 0.1394 -0.0064 -0.0071 0.0187  30  CYS A CB   
594  S SG   . CYS A 31  ? 0.1323 0.0999 0.1465 -0.0003 -0.0098 0.0083  30  CYS A SG   
596  D DA   . CYS A 31  ? 0.1096 0.1438 0.1178 0.0065  -0.0130 0.0053  30  CYS A DA   
597  D DB2  . CYS A 31  ? 0.1679 0.1247 0.1607 -0.0072 0.0133  0.0374  30  CYS A DB2  
598  D DB3  . CYS A 31  ? 0.1381 0.1335 0.1598 -0.0145 -0.0243 0.0062  30  CYS A DB3  
599  N N    . ALA A 32  ? 0.1072 0.1100 0.1074 -0.0070 -0.0104 0.0042  31  ALA A N    
600  C CA   . ALA A 32  ? 0.1164 0.1128 0.1115 -0.0083 -0.0075 0.0074  31  ALA A CA   
601  C C    . ALA A 32  ? 0.0990 0.1042 0.1117 -0.0029 -0.0077 0.0151  31  ALA A C    
602  O O    . ALA A 32  ? 0.1207 0.1172 0.1272 -0.0202 0.0074  0.0059  31  ALA A O    
603  C CB   . ALA A 32  ? 0.1579 0.1339 0.1121 -0.0176 -0.0304 0.0171  31  ALA A CB   
605  D D    B ALA A 32  ? 0.1076 0.1750 0.1341 -0.0087 -0.0118 0.0461  31  ALA A D    
606  D DA   . ALA A 32  ? 0.1420 0.1297 0.1362 -0.0119 0.0174  -0.0083 31  ALA A DA   
607  D DB1  . ALA A 32  ? 0.1358 0.1710 0.1568 -0.0157 -0.0314 0.0101  31  ALA A DB1  
608  D DB2  . ALA A 32  ? 0.2052 0.1825 0.1280 -0.0163 -0.0448 0.0536  31  ALA A DB2  
609  D DB3  . ALA A 32  ? 0.1833 0.1578 0.1389 -0.0177 -0.0523 -0.0042 31  ALA A DB3  
610  N N    . ALA A 33  ? 0.0974 0.1085 0.1124 0.0002  -0.0085 0.0149  32  ALA A N    
611  C CA   . ALA A 33  ? 0.0965 0.1010 0.1212 0.0042  -0.0080 0.0147  32  ALA A CA   
612  C C    . ALA A 33  ? 0.0870 0.1050 0.1251 -0.0010 -0.0020 0.0108  32  ALA A C    
613  O O    . ALA A 33  ? 0.0967 0.1121 0.1401 -0.0075 -0.0166 0.0006  32  ALA A O    
614  C CB   . ALA A 33  ? 0.1037 0.1341 0.1287 0.0221  -0.0091 0.0004  32  ALA A CB   
616  D DA   . ALA A 33  ? 0.1128 0.1161 0.1432 0.0042  -0.0103 0.0304  32  ALA A DA   
617  D DB1  . ALA A 33  ? 0.1614 0.1388 0.1390 0.0307  0.0278  0.0026  32  ALA A DB1  
618  D DB2  . ALA A 33  ? 0.1370 0.1429 0.2042 0.0108  0.0154  -0.0314 32  ALA A DB2  
619  D DB3  . ALA A 33  ? 0.1224 0.2373 0.1726 0.0400  -0.0268 -0.0054 32  ALA A DB3  
620  N N    . LYS A 34  ? 0.0988 0.1194 0.1142 0.0063  -0.0103 0.0053  33  LYS A N    
621  C CA   . LYS A 34  ? 0.0954 0.1219 0.1155 0.0080  -0.0099 0.0073  33  LYS A CA   
622  C C    . LYS A 34  ? 0.0993 0.1136 0.1282 0.0070  -0.0062 0.0030  33  LYS A C    
623  O O    . LYS A 34  ? 0.0980 0.1472 0.1457 -0.0066 -0.0016 -0.0062 33  LYS A O    
624  C CB   . LYS A 34  ? 0.1124 0.1352 0.1308 0.0039  -0.0195 0.0264  33  LYS A CB   
625  C CG   . LYS A 34  ? 0.1196 0.1907 0.1495 0.0258  -0.0185 0.0399  33  LYS A CG   
626  C CD   . LYS A 34  ? 0.1536 0.2444 0.1541 0.0325  -0.0574 0.0302  33  LYS A CD   
627  C CE   . LYS A 34  ? 0.1649 0.3075 0.1948 0.0418  -0.0747 0.0398  33  LYS A CE   
628  N NZ   . LYS A 34  ? 0.1667 0.3426 0.2307 -0.0019 -0.0856 0.0297  33  LYS A NZ   
630  D DA   . LYS A 34  ? 0.1242 0.1352 0.1152 0.0093  -0.0162 0.0048  33  LYS A DA   
631  D DB2  . LYS A 34  ? 0.1276 0.1824 0.1513 -0.0033 -0.0058 0.0343  33  LYS A DB2  
632  D DB3  . LYS A 34  ? 0.1579 0.1270 0.1560 0.0145  -0.0367 0.0184  33  LYS A DB3  
633  D DG2  . LYS A 34  ? 0.1979 0.2003 0.2128 0.0288  -0.0525 0.0710  33  LYS A DG2  
634  D DG3  . LYS A 34  ? 0.1063 0.2280 0.1831 0.0410  0.0018  0.0296  33  LYS A DG3  
635  D DD2  . LYS A 34  ? 0.1947 0.2296 0.2095 0.0428  -0.0725 0.0049  33  LYS A DD2  
636  D DD3  . LYS A 34  ? 0.2091 0.3561 0.1593 0.0421  -0.0256 0.0165  33  LYS A DD3  
637  D DE2  . LYS A 34  ? 0.1652 0.3060 0.3133 0.0227  -0.1112 0.0607  33  LYS A DE2  
638  D DE3  . LYS A 34  ? 0.1677 0.3966 0.2367 0.0393  -0.0388 0.0307  33  LYS A DE3  
639  D DZ1  . LYS A 34  ? 0.2621 0.3429 0.3208 -0.0248 -0.1005 0.0499  33  LYS A DZ1  
640  D DZ2  . LYS A 34  ? 0.2129 0.4314 0.2218 -0.0253 -0.0758 -0.0136 33  LYS A DZ2  
641  D DZ3  . LYS A 34  ? 0.1860 0.3957 0.3159 0.0077  -0.1216 0.0120  33  LYS A DZ3  
642  N N    . PHE A 35  ? 0.0997 0.1111 0.1207 0.0127  0.0031  0.0072  34  PHE A N    
643  C CA   . PHE A 35  ? 0.1102 0.1279 0.1352 0.0204  0.0063  0.0167  34  PHE A CA   
644  C C    . PHE A 35  ? 0.1130 0.1335 0.1358 0.0239  0.0139  0.0174  34  PHE A C    
645  O O    . PHE A 35  ? 0.1267 0.1578 0.2176 0.0482  0.0485  0.0680  34  PHE A O    
646  C CB   . PHE A 35  ? 0.1063 0.1403 0.1362 0.0404  0.0251  0.0167  34  PHE A CB   
647  C CG   . PHE A 35  ? 0.1137 0.1369 0.1564 0.0394  0.0161  0.0226  34  PHE A CG   
648  C CD1  . PHE A 35  ? 0.1183 0.1620 0.2013 0.0355  -0.0053 0.0364  34  PHE A CD1  
649  C CD2  . PHE A 35  ? 0.1347 0.1307 0.1971 0.0239  0.0017  0.0339  34  PHE A CD2  
650  C CE1  . PHE A 35  ? 0.1476 0.1859 0.2256 0.0576  -0.0134 0.0515  34  PHE A CE1  
651  C CE2  . PHE A 35  ? 0.1902 0.1550 0.2405 0.0299  -0.0062 0.0684  34  PHE A CE2  
652  C CZ   . PHE A 35  ? 0.1885 0.1766 0.2340 0.0550  -0.0101 0.0720  34  PHE A CZ   
654  D DA   . PHE A 35  ? 0.0967 0.1546 0.1635 0.0251  0.0012  0.0237  34  PHE A DA   
655  D DB2  . PHE A 35  ? 0.1496 0.1466 0.1620 0.0189  -0.0168 0.0064  34  PHE A DB2  
656  D DB3  . PHE A 35  ? 0.1671 0.1579 0.1680 0.0617  0.0699  0.0347  34  PHE A DB3  
657  D DD1  . PHE A 35  ? 0.1546 0.1951 0.3120 0.0026  -0.0322 0.0915  34  PHE A DD1  
658  D DD2  . PHE A 35  ? 0.1693 0.1780 0.2830 -0.0060 -0.0495 0.0398  34  PHE A DD2  
659  D DE1  . PHE A 35  ? 0.1577 0.2667 0.3072 0.0514  -0.0524 0.0774  34  PHE A DE1  
660  D DE2  . PHE A 35  ? 0.2179 0.2089 0.4729 -0.0018 -0.0531 0.1869  34  PHE A DE2  
661  D DZ   . PHE A 35  ? 0.2688 0.2366 0.2654 0.0422  -0.0557 0.1115  34  PHE A DZ   
662  N N    . GLU A 36  ? 0.1030 0.1301 0.1105 0.0097  -0.0011 0.0213  35  GLU A N    
663  C CA   . GLU A 36  ? 0.0952 0.1312 0.1027 0.0124  0.0136  0.0192  35  GLU A CA   
664  C C    . GLU A 36  ? 0.0943 0.1339 0.1239 0.0019  0.0095  0.0160  35  GLU A C    
665  O O    . GLU A 36  ? 0.1097 0.1592 0.1174 -0.0163 0.0132  0.0160  35  GLU A O    
666  C CB   . GLU A 36  ? 0.0992 0.1086 0.1057 0.0202  0.0096  0.0099  35  GLU A CB   
667  C CG   . GLU A 36  ? 0.1303 0.1223 0.1087 0.0094  -0.0107 0.0082  35  GLU A CG   
668  C CD   . GLU A 36  ? 0.1522 0.1368 0.1047 0.0198  -0.0102 0.0048  35  GLU A CD   
669  O OE1  . GLU A 36  ? 0.1935 0.1575 0.1271 0.0106  -0.0122 -0.0171 35  GLU A OE1  
670  O OE2  . GLU A 36  ? 0.2195 0.1191 0.1259 0.0115  0.0307  0.0058  35  GLU A OE2  
671  D D    . GLU A 36  ? 0.1136 0.1425 0.1357 0.0068  0.0054  0.0267  35  GLU A D    
672  D DA   . GLU A 36  ? 0.1095 0.1585 0.1017 0.0143  0.0134  0.0115  35  GLU A DA   
673  D DB2  . GLU A 36  ? 0.1083 0.1447 0.1057 0.0124  0.0184  -0.0067 35  GLU A DB2  
674  D DB3  . GLU A 36  ? 0.1249 0.1102 0.1303 0.0226  -0.0088 0.0182  35  GLU A DB3  
675  D DG2  . GLU A 36  ? 0.2048 0.1112 0.1429 -0.0033 -0.0095 0.0039  35  GLU A DG2  
676  D DG3  . GLU A 36  ? 0.1290 0.1797 0.1702 -0.0105 -0.0224 0.0081  35  GLU A DG3  
677  D DE2  . GLU A 36  ? 0.2612 0.1878 0.1319 -0.0068 0.0371  0.0108  35  GLU A DE2  
678  N N    . SER A 37  ? 0.1194 0.1213 0.1285 -0.0141 0.0208  0.0094  36  SER A N    
679  C CA   . SER A 37  ? 0.1262 0.1264 0.1376 -0.0175 0.0045  0.0068  36  SER A CA   
680  C C    . SER A 37  ? 0.0899 0.1282 0.1481 -0.0092 -0.0025 -0.0026 36  SER A C    
681  O O    . SER A 37  ? 0.1036 0.1337 0.1747 -0.0067 -0.0095 -0.0211 36  SER A O    
682  C CB   . SER A 37  ? 0.1367 0.1112 0.1244 -0.0093 -0.0205 0.0083  36  SER A CB   
683  O OG   . SER A 37  ? 0.1125 0.1091 0.1230 0.0010  -0.0261 0.0065  36  SER A OG   
684  D D    . SER A 37  ? 0.1768 0.1616 0.1730 -0.0532 0.0466  0.0162  36  SER A D    
685  D DA   . SER A 37  ? 0.1883 0.1429 0.1640 -0.0528 0.0392  -0.0043 36  SER A DA   
686  D DB2  . SER A 37  ? 0.1653 0.1132 0.1803 -0.0099 0.0027  -0.0105 36  SER A DB2  
687  D DB3  . SER A 37  ? 0.1815 0.1441 0.1278 -0.0003 -0.0253 0.0300  36  SER A DB3  
688  D DG   . SER A 37  ? 0.1420 0.1728 0.1233 -0.0405 -0.0253 0.0128  36  SER A DG   
689  N N    A ASN A 38  ? 0.1036 0.1308 0.1497 -0.0041 -0.0134 0.0009  37  ASN A N    
690  N N    B ASN A 38  ? 0.1217 0.1292 0.1498 0.0036  -0.0133 -0.0059 37  ASN A N    
691  C CA   A ASN A 38  ? 0.1162 0.1460 0.1595 0.0104  -0.0313 -0.0007 37  ASN A CA   
692  C CA   B ASN A 38  ? 0.1240 0.1433 0.1632 0.0236  -0.0351 0.0021  37  ASN A CA   
693  C C    A ASN A 38  ? 0.1217 0.1292 0.1306 0.0055  -0.0393 0.0160  37  ASN A C    
694  C C    B ASN A 38  ? 0.1220 0.1300 0.1238 0.0040  -0.0488 0.0007  37  ASN A C    
695  O O    A ASN A 38  ? 0.0781 0.1200 0.1204 -0.0135 -0.0293 0.0434  37  ASN A O    
696  O O    B ASN A 38  ? 0.1696 0.1143 0.1378 -0.0094 -0.0670 0.0033  37  ASN A O    
697  C CB   A ASN A 38  ? 0.1147 0.1727 0.2050 0.0110  -0.0440 -0.0135 37  ASN A CB   
698  C CB   B ASN A 38  ? 0.1239 0.1814 0.2136 0.0233  -0.0435 -0.0076 37  ASN A CB   
699  C CG   A ASN A 38  ? 0.1226 0.2084 0.2328 0.0274  -0.0523 -0.0027 37  ASN A CG   
700  C CG   B ASN A 38  ? 0.1259 0.2098 0.2295 0.0348  -0.0651 -0.0011 37  ASN A CG   
701  O OD1  A ASN A 38  ? 0.1065 0.2146 0.2148 0.0328  -0.0650 0.0116  37  ASN A OD1  
702  O OD1  B ASN A 38  ? 0.1296 0.2096 0.2247 0.0385  -0.0718 0.0134  37  ASN A OD1  
703  N ND2  A ASN A 38  ? 0.1236 0.2204 0.2511 0.0241  -0.0587 -0.0089 37  ASN A ND2  
704  N ND2  B ASN A 38  ? 0.1525 0.2346 0.2394 0.0173  -0.0714 -0.0137 37  ASN A ND2  
705  D D    A ASN A 38  ? 0.0674 0.1419 0.1651 -0.0167 0.0137  -0.0126 37  ASN A D    
706  D D    B ASN A 38  ? 0.9324 0.1699 0.2045 0.1091  -0.0734 -0.0474 37  ASN A D    
707  D DA   A ASN A 38  ? 0.1767 0.1438 0.1447 0.0159  -0.0627 -0.0137 37  ASN A DA   
708  D DA   B ASN A 38  ? 0.1007 0.1448 0.2055 0.0437  -0.0402 0.0280  37  ASN A DA   
709  D DB2  A ASN A 38  ? 0.0901 0.2139 0.2164 -0.0079 -0.0470 -0.0037 37  ASN A DB2  
710  D DB2  B ASN A 38  ? 0.1345 0.2498 0.2445 0.0160  -0.0213 -0.0317 37  ASN A DB2  
711  D DB3  A ASN A 38  ? 0.1622 0.1744 0.2233 0.0108  -0.0593 -0.0261 37  ASN A DB3  
712  D DB3  B ASN A 38  ? 0.1237 0.1857 0.2563 0.0074  -0.0308 -0.0095 37  ASN A DB3  
713  D DD21 A ASN A 38  ? 0.1837 0.3602 0.3351 -0.0148 -0.1228 0.0787  37  ASN A DD21 
714  D DD21 B ASN A 38  ? 0.1784 0.3450 0.2731 -0.0161 -0.1048 0.0393  37  ASN A DD21 
715  D DD22 A ASN A 38  ? 0.0939 0.3232 0.4543 0.0380  -0.0634 0.1449  37  ASN A DD22 
716  D DD22 B ASN A 38  ? 0.2642 0.2768 0.3377 -0.0563 -0.1106 0.0214  37  ASN A DD22 
717  N N    . PHE A 39  ? 0.1138 0.1227 0.0976 0.0009  -0.0269 0.0106  38  PHE A N    
718  C CA   . PHE A 39  ? 0.1340 0.1376 0.0871 0.0124  -0.0149 0.0145  38  PHE A CA   
719  C C    . PHE A 39  ? 0.1297 0.1408 0.0900 0.0108  -0.0088 0.0102  38  PHE A C    
720  O O    . PHE A 39  ? 0.1522 0.1524 0.1009 -0.0098 0.0088  -0.0125 38  PHE A O    
721  C CB   . PHE A 39  ? 0.1662 0.1497 0.0943 -0.0070 -0.0108 0.0186  38  PHE A CB   
722  C CG   . PHE A 39  ? 0.1436 0.1487 0.1039 0.0005  -0.0151 0.0198  38  PHE A CG   
723  C CD1  . PHE A 39  ? 0.1470 0.1502 0.1236 0.0043  -0.0225 0.0076  38  PHE A CD1  
724  C CD2  . PHE A 39  ? 0.1716 0.1604 0.1402 -0.0026 -0.0474 0.0345  38  PHE A CD2  
725  C CE1  . PHE A 39  ? 0.1505 0.1531 0.1462 -0.0129 -0.0046 0.0154  38  PHE A CE1  
726  C CE2  . PHE A 39  ? 0.1830 0.1595 0.1766 -0.0013 -0.0439 0.0466  38  PHE A CE2  
727  C CZ   . PHE A 39  ? 0.1517 0.1460 0.1650 0.0028  -0.0011 0.0211  38  PHE A CZ   
729  D DA   . PHE A 39  ? 0.1237 0.1736 0.0909 -0.0097 -0.0024 0.0094  38  PHE A DA   
730  D DB2  . PHE A 39  ? 0.2662 0.1928 0.1078 -0.0563 -0.0663 0.0389  38  PHE A DB2  
731  D DB3  . PHE A 39  ? 0.2604 0.1806 0.1271 0.0282  0.0527  0.0267  38  PHE A DB3  
732  D DD1  . PHE A 39  ? 0.2172 0.1783 0.1251 0.0243  -0.0381 0.0104  38  PHE A DD1  
733  D DD2  . PHE A 39  ? 0.3125 0.1821 0.1982 0.0005  -0.1349 0.0224  38  PHE A DD2  
734  D DE1  . PHE A 39  ? 0.2345 0.1827 0.1771 -0.0469 -0.0418 0.0171  38  PHE A DE1  
735  D DE2  . PHE A 39  ? 0.4201 0.1989 0.2738 -0.0107 -0.1740 0.0863  38  PHE A DE2  
736  D DZ   . PHE A 39  ? 0.1897 0.1437 0.1954 0.0073  -0.0013 0.0270  38  PHE A DZ   
737  N N    A ASN A 40  ? 0.1445 0.1367 0.1028 0.0189  0.0088  0.0123  39  ASN A N    
738  N N    B ASN A 40  ? 0.1329 0.1372 0.0990 0.0192  0.0032  0.0104  39  ASN A N    
739  C CA   A ASN A 40  ? 0.1377 0.1379 0.1030 0.0152  -0.0073 0.0081  39  ASN A CA   
740  C CA   B ASN A 40  ? 0.1388 0.1391 0.0912 0.0136  -0.0109 0.0058  39  ASN A CA   
741  C C    A ASN A 40  ? 0.1272 0.1271 0.0860 0.0049  0.0025  0.0102  39  ASN A C    
742  C C    B ASN A 40  ? 0.1309 0.1262 0.0833 0.0078  0.0000  0.0109  39  ASN A C    
743  O O    A ASN A 40  ? 0.1181 0.1431 0.0869 -0.0025 0.0102  0.0070  39  ASN A O    
744  O O    B ASN A 40  ? 0.1818 0.0882 0.0860 0.0573  -0.0025 0.0091  39  ASN A O    
745  C CB   A ASN A 40  ? 0.1326 0.1504 0.1456 0.0101  -0.0152 0.0196  39  ASN A CB   
746  C CB   B ASN A 40  ? 0.1358 0.1586 0.1562 -0.0009 -0.0207 0.0001  39  ASN A CB   
747  C CG   A ASN A 40  ? 0.1652 0.1547 0.1757 -0.0043 -0.0250 0.0168  39  ASN A CG   
748  C CG   B ASN A 40  ? 0.1478 0.1598 0.1736 -0.0118 -0.0396 0.0039  39  ASN A CG   
749  O OD1  A ASN A 40  ? 0.1776 0.1670 0.1679 0.0091  -0.0626 -0.0227 39  ASN A OD1  
750  O OD1  B ASN A 40  ? 0.1945 0.1628 0.1805 0.0139  -0.0193 0.0209  39  ASN A OD1  
751  N ND2  A ASN A 40  ? 0.1717 0.1457 0.2004 -0.0064 -0.0439 0.0338  39  ASN A ND2  
752  N ND2  B ASN A 40  ? 0.1570 0.1826 0.1929 -0.0247 -0.0382 0.0221  39  ASN A ND2  
755  D DA   A ASN A 40  ? 0.1355 0.1695 0.1045 0.0039  -0.0241 -0.0126 39  ASN A DA   
756  D DA   B ASN A 40  ? 0.2140 0.1456 0.0847 0.0442  -0.0064 0.0134  39  ASN A DA   
757  D DB2  A ASN A 40  ? 0.1523 0.1698 0.1389 0.0432  -0.0002 0.0151  39  ASN A DB2  
758  D DB2  B ASN A 40  ? 0.1633 0.1307 0.1822 0.0116  -0.0491 -0.0290 39  ASN A DB2  
759  D DB3  A ASN A 40  ? 0.1113 0.1439 0.1475 0.0120  -0.0013 0.0310  39  ASN A DB3  
760  D DB3  B ASN A 40  ? 0.1530 0.1368 0.1574 0.0376  0.0126  0.0345  39  ASN A DB3  
761  D DD21 A ASN A 40  ? 0.1827 0.1686 0.3983 -0.0174 -0.0916 0.1158  39  ASN A DD21 
762  D DD21 B ASN A 40  ? 0.1929 0.1925 0.5051 -0.0326 -0.0184 0.0715  39  ASN A DD21 
763  D DD22 A ASN A 40  ? 0.2067 0.1290 0.3850 -0.0286 -0.1085 0.0803  39  ASN A DD22 
764  D DD22 B ASN A 40  ? 0.2012 0.2105 0.4836 0.0021  0.0836  0.0666  39  ASN A DD22 
765  N N    . THR A 41  ? 0.1334 0.1295 0.0817 0.0133  -0.0020 0.0107  40  THR A N    
766  C CA   . THR A 41  ? 0.1240 0.1317 0.0983 0.0015  -0.0097 0.0190  40  THR A CA   
767  C C    . THR A 41  ? 0.1302 0.1146 0.0942 0.0061  -0.0149 0.0072  40  THR A C    
768  O O    . THR A 41  ? 0.1466 0.1442 0.1084 -0.0092 -0.0290 0.0263  40  THR A O    
769  C CB   . THR A 41  ? 0.1359 0.1440 0.1192 0.0192  0.0025  0.0159  40  THR A CB   
770  O OG1  . THR A 41  ? 0.1662 0.1618 0.1460 0.0169  -0.0036 -0.0125 40  THR A OG1  
771  C CG2  . THR A 41  ? 0.1656 0.1763 0.1297 -0.0006 0.0318  0.0168  40  THR A CG2  
773  D D    B THR A 41  ? 0.1448 0.1355 0.0812 0.0141  -0.0012 0.0065  40  THR A D    
774  D DA   . THR A 41  ? 0.1265 0.1317 0.1076 0.0017  -0.0192 0.0176  40  THR A DA   
775  D DB   . THR A 41  ? 0.1492 0.1579 0.1472 0.0310  -0.0085 0.0232  40  THR A DB   
776  D DG1  . THR A 41  ? 0.2140 0.2117 0.1594 0.0202  -0.0361 -0.0102 40  THR A DG1  
777  D DG21 . THR A 41  ? 0.1971 0.2120 0.1762 0.0117  0.0279  0.0626  40  THR A DG21 
778  D DG22 . THR A 41  ? 0.1955 0.2331 0.1853 0.0188  0.0716  0.0316  40  THR A DG22 
779  D DG23 . THR A 41  ? 0.2325 0.2186 0.1816 -0.0691 0.0368  0.0026  40  THR A DG23 
780  N N    A GLN A 42  ? 0.1395 0.1258 0.0955 -0.0098 -0.0137 -0.0002 41  GLN A N    
781  N N    B GLN A 42  ? 0.1360 0.1144 0.0906 -0.0004 -0.0189 0.0154  41  GLN A N    
782  C CA   A GLN A 42  ? 0.1656 0.1303 0.1123 -0.0159 -0.0085 0.0080  41  GLN A CA   
783  C CA   B GLN A 42  ? 0.1694 0.1157 0.0972 -0.0110 -0.0187 0.0177  41  GLN A CA   
784  C C    A GLN A 42  ? 0.1474 0.1139 0.1127 -0.0274 -0.0136 0.0166  41  GLN A C    
785  C C    B GLN A 42  ? 0.1460 0.1118 0.1083 -0.0297 -0.0166 0.0150  41  GLN A C    
786  O O    A GLN A 42  ? 0.1872 0.1166 0.1388 -0.0489 0.0142  -0.0031 41  GLN A O    
787  O O    B GLN A 42  ? 0.1522 0.1172 0.1327 -0.0228 -0.0045 0.0272  41  GLN A O    
788  C CB   A GLN A 42  ? 0.1937 0.1325 0.1254 -0.0269 -0.0082 0.0028  41  GLN A CB   
789  C CB   B GLN A 42  ? 0.1845 0.1298 0.1207 -0.0217 -0.0205 0.0016  41  GLN A CB   
790  C CG   A GLN A 42  ? 0.3125 0.1655 0.1586 0.0444  0.0401  0.0084  41  GLN A CG   
791  C CG   B GLN A 42  ? 0.2370 0.1658 0.1384 0.0039  -0.0030 -0.0186 41  GLN A CG   
798  D D    A GLN A 42  ? 0.1127 0.1650 0.0846 0.0116  0.0035  -0.0076 41  GLN A D    
799  D D    B GLN A 42  ? 0.1676 0.1279 0.1219 0.0035  -0.0447 0.0271  41  GLN A D    
800  D DA   A GLN A 42  ? 0.1765 0.1333 0.0936 0.0047  -0.0037 -0.0063 41  GLN A DA   
801  D DA   B GLN A 42  ? 0.1818 0.1325 0.0774 0.0040  -0.0114 0.0193  41  GLN A DA   
802  D DB2  A GLN A 42  ? 0.2118 0.1682 0.1339 -0.0504 -0.0267 0.0099  41  GLN A DB2  
803  D DB2  B GLN A 42  ? 0.2040 0.1493 0.1454 -0.0167 -0.0465 0.0007  41  GLN A DB2  
804  D DB3  A GLN A 42  ? 0.2094 0.1898 0.1604 -0.0631 -0.0195 0.0340  41  GLN A DB3  
805  D DB3  B GLN A 42  ? 0.2204 0.1696 0.1336 -0.0587 -0.0407 0.0227  41  GLN A DB3  
806  D DG2  A GLN A 42  ? 0.3107 0.2947 0.1973 0.1287  0.0285  0.0298  41  GLN A DG2  
807  D DG2  B GLN A 42  ? 0.2294 0.3727 0.1181 0.0462  0.0189  -0.0076 41  GLN A DG2  
808  D DG3  A GLN A 42  ? 0.3205 0.2560 0.1683 0.0441  0.0513  0.0348  41  GLN A DG3  
809  D DG3  B GLN A 42  ? 0.2755 0.2325 0.1506 -0.0011 0.0311  0.0087  41  GLN A DG3  
814  N N    . ALA A 43  ? 0.1452 0.1141 0.1098 -0.0259 -0.0051 0.0159  42  ALA A N    
815  C CA   . ALA A 43  ? 0.1334 0.1340 0.1122 -0.0154 -0.0125 0.0160  42  ALA A CA   
816  C C    . ALA A 43  ? 0.1066 0.1198 0.1057 -0.0260 -0.0107 0.0023  42  ALA A C    
817  O O    . ALA A 43  ? 0.1031 0.1660 0.1261 -0.0195 -0.0144 0.0049  42  ALA A O    
818  C CB   . ALA A 43  ? 0.2041 0.1322 0.1224 0.0094  0.0047  0.0132  42  ALA A CB   
820  D D    B ALA A 43  ? 0.0827 0.1033 0.1104 -0.0039 -0.0361 0.0263  42  ALA A D    
821  D DA   . ALA A 43  ? 0.1368 0.1784 0.0908 -0.0272 -0.0017 0.0097  42  ALA A DA   
822  D DB1  . ALA A 43  ? 0.2261 0.1255 0.1713 -0.0081 -0.0004 -0.0002 42  ALA A DB1  
823  D DB2  . ALA A 43  ? 0.2405 0.1914 0.1474 0.0489  0.0231  0.0103  42  ALA A DB2  
824  D DB3  . ALA A 43  ? 0.2324 0.1779 0.1420 0.0529  0.0152  0.0483  42  ALA A DB3  
825  N N    . THR A 44  ? 0.0991 0.1664 0.0971 -0.0160 -0.0080 0.0007  43  THR A N    
826  C CA   . THR A 44  ? 0.1089 0.1871 0.1055 -0.0351 -0.0064 0.0163  43  THR A CA   
827  C C    . THR A 44  ? 0.0956 0.2236 0.1031 -0.0358 -0.0048 0.0290  43  THR A C    
828  O O    . THR A 44  ? 0.1077 0.4292 0.1336 -0.0338 -0.0128 -0.0334 43  THR A O    
829  C CB   . THR A 44  ? 0.1424 0.1795 0.2174 -0.0335 -0.0123 0.0447  43  THR A CB   
830  O OG1  . THR A 44  ? 0.2153 0.1588 0.2607 -0.0167 0.0365  0.0289  43  THR A OG1  
831  C CG2  . THR A 44  ? 0.2668 0.1985 0.2116 -0.0161 -0.0114 0.0511  43  THR A CG2  
832  D D    . THR A 44  ? 0.1104 0.2345 0.1299 -0.0308 -0.0205 0.0123  43  THR A D    
833  D DA   . THR A 44  ? 0.0971 0.1722 0.1261 -0.0192 -0.0185 0.0358  43  THR A DA   
834  D DB   . THR A 44  ? 0.1906 0.2056 0.2481 -0.0773 -0.0321 0.0272  43  THR A DB   
835  D DG1  . THR A 44  ? 0.2806 0.1403 0.2569 -0.0255 0.0524  0.0192  43  THR A DG1  
836  D DG21 . THR A 44  ? 0.3246 0.2566 0.2394 -0.0499 -0.0734 0.0905  43  THR A DG21 
837  D DG22 . THR A 44  ? 0.3755 0.2018 0.2552 0.0051  -0.0401 0.0434  43  THR A DG22 
838  D DG23 . THR A 44  ? 0.3379 0.3496 0.2533 0.0315  0.0448  0.0466  43  THR A DG23 
839  N N    . ASN A 45  ? 0.0875 0.1809 0.1071 -0.0110 -0.0034 0.0260  44  ASN A N    
840  C CA   . ASN A 45  ? 0.0915 0.1747 0.1175 0.0044  -0.0010 0.0373  44  ASN A CA   
841  C C    . ASN A 45  ? 0.0842 0.1465 0.1106 -0.0117 -0.0101 0.0273  44  ASN A C    
842  O O    . ASN A 45  ? 0.0762 0.1716 0.1370 -0.0261 -0.0135 0.0408  44  ASN A O    
843  C CB   . ASN A 45  ? 0.1345 0.1622 0.1743 0.0264  -0.0021 0.0609  44  ASN A CB   
844  C CG   . ASN A 45  ? 0.1879 0.1779 0.2617 0.0322  0.0508  0.0314  44  ASN A CG   
845  O OD1  . ASN A 45  ? 0.1697 0.3438 0.3950 0.0313  0.0673  0.0011  44  ASN A OD1  
846  N ND2  . ASN A 45  ? 0.3153 0.3228 0.2943 0.0474  0.0628  -0.0568 44  ASN A ND2  
848  D DA   . ASN A 45  ? 0.0896 0.2158 0.1376 0.0047  -0.0170 0.0342  44  ASN A DA   
849  D DB2  . ASN A 45  ? 0.2872 0.2009 0.1838 0.0373  0.0135  0.0700  44  ASN A DB2  
850  D DB3  . ASN A 45  ? 0.1629 0.1728 0.2475 0.0008  -0.0082 0.0024  44  ASN A DB3  
851  D DD21 . ASN A 45  ? 0.3784 0.4859 0.4254 0.0721  0.1173  -0.1603 44  ASN A DD21 
852  D DD22 . ASN A 45  ? 0.3395 0.7064 0.3106 0.0506  0.0124  -0.1714 44  ASN A DD22 
853  N N    A ARG A 46  ? 0.0879 0.1618 0.1160 -0.0230 -0.0105 0.0253  45  ARG A N    
854  N N    B ARG A 46  ? 0.0893 0.1613 0.1212 -0.0247 -0.0078 0.0218  45  ARG A N    
855  C CA   A ARG A 46  ? 0.1264 0.1597 0.1136 -0.0134 0.0025  0.0300  45  ARG A CA   
856  C CA   B ARG A 46  ? 0.0976 0.1549 0.1197 -0.0326 -0.0050 0.0222  45  ARG A CA   
857  C C    A ARG A 46  ? 0.1000 0.1725 0.1222 -0.0043 0.0008  0.0364  45  ARG A C    
858  C C    B ARG A 46  ? 0.1055 0.1571 0.1250 -0.0081 0.0006  0.0384  45  ARG A C    
859  O O    A ARG A 46  ? 0.0971 0.1676 0.1933 0.0024  -0.0098 0.0373  45  ARG A O    
860  O O    B ARG A 46  ? 0.1058 0.1694 0.1532 -0.0006 -0.0016 0.0548  45  ARG A O    
861  C CB   A ARG A 46  ? 0.1701 0.1640 0.1603 -0.0376 0.0183  0.0259  45  ARG A CB   
862  C CB   B ARG A 46  ? 0.1218 0.1653 0.1425 -0.0560 -0.0131 0.0168  45  ARG A CB   
863  C CG   A ARG A 46  ? 0.2381 0.1568 0.1860 -0.0586 0.0498  0.0052  45  ARG A CG   
864  C CG   B ARG A 46  ? 0.1964 0.1551 0.1878 -0.0592 0.0249  -0.0015 45  ARG A CG   
865  C CD   A ARG A 46  ? 0.2992 0.1570 0.2417 -0.0682 0.0608  -0.0011 45  ARG A CD   
866  C CD   B ARG A 46  ? 0.2589 0.1633 0.2501 -0.0870 0.0518  -0.0183 45  ARG A CD   
867  N NE   A ARG A 46  ? 0.3294 0.1615 0.2749 -0.0573 0.0725  -0.0279 45  ARG A NE   
868  N NE   B ARG A 46  ? 0.3053 0.1453 0.2777 -0.0895 0.0781  -0.0262 45  ARG A NE   
869  C CZ   A ARG A 46  ? 0.3355 0.1435 0.3235 -0.0376 0.0782  0.0043  45  ARG A CZ   
870  C CZ   B ARG A 46  ? 0.3497 0.1808 0.2731 -0.0518 0.0711  -0.0452 45  ARG A CZ   
871  N NH1  A ARG A 46  ? 0.3582 0.2126 0.3263 0.0296  0.0662  0.0239  45  ARG A NH1  
872  N NH1  B ARG A 46  ? 0.3361 0.2146 0.2907 -0.0597 0.0422  -0.0645 45  ARG A NH1  
873  N NH2  A ARG A 46  ? 0.3435 0.1596 0.3300 -0.0300 0.0831  0.0099  45  ARG A NH2  
874  N NH2  B ARG A 46  ? 0.4062 0.1889 0.2886 -0.0286 0.0980  -0.0407 45  ARG A NH2  
875  D D    A ARG A 46  ? 0.1023 0.3276 0.1252 -0.0699 -0.0196 0.0605  45  ARG A D    
876  D D    B ARG A 46  ? 0.1448 0.2634 0.1522 -0.0811 -0.0477 0.0566  45  ARG A D    
877  D DA   A ARG A 46  ? 0.1277 0.1706 0.0742 0.0093  0.0089  -0.0097 45  ARG A DA   
878  D DA   B ARG A 46  ? 0.1005 0.1224 0.1344 -0.0247 -0.0120 0.0097  45  ARG A DA   
879  D DB2  A ARG A 46  ? 0.1757 0.1873 0.2053 -0.0538 0.0044  0.0290  45  ARG A DB2  
880  D DB2  B ARG A 46  ? 0.1299 0.2249 0.1665 -0.0768 -0.0302 0.0393  45  ARG A DB2  
881  D DB3  A ARG A 46  ? 0.1916 0.1569 0.1726 -0.0244 0.0262  0.0320  45  ARG A DB3  
882  D DB3  B ARG A 46  ? 0.1264 0.1707 0.1501 -0.0647 -0.0182 0.0250  45  ARG A DB3  
883  D DG2  A ARG A 46  ? 0.2297 0.1674 0.2196 -0.0485 0.0688  -0.0028 45  ARG A DG2  
884  D DG2  B ARG A 46  ? 0.1702 0.1592 0.1885 -0.0526 0.0578  0.0366  45  ARG A DG2  
885  D DG3  A ARG A 46  ? 0.2950 0.1557 0.1754 -0.0720 0.0350  -0.0079 45  ARG A DG3  
886  D DG3  B ARG A 46  ? 0.1636 0.1480 0.1955 -0.0354 0.0359  0.0036  45  ARG A DG3  
887  D DD2  A ARG A 46  ? 0.3056 0.1239 0.3379 -0.0551 0.0239  0.0036  45  ARG A DD2  
888  D DD2  B ARG A 46  ? 0.2593 0.1792 0.2283 -0.1052 0.0408  -0.0450 45  ARG A DD2  
889  D DD3  A ARG A 46  ? 0.3100 0.1854 0.2823 -0.0729 0.0686  0.0479  45  ARG A DD3  
890  D DD3  B ARG A 46  ? 0.2802 0.1600 0.2649 -0.0884 0.0586  -0.0106 45  ARG A DD3  
891  D DE   A ARG A 46  ? 0.3440 0.1194 0.2548 -0.1110 0.0922  0.0252  45  ARG A DE   
892  D DE   B ARG A 46  ? 0.4435 0.3241 0.2944 0.0724  0.1135  0.0150  45  ARG A DE   
893  D DH11 A ARG A 46  ? 0.3764 0.3449 0.3977 -0.0054 0.0214  0.0614  45  ARG A DH11 
894  D DH11 B ARG A 46  ? 0.4370 0.2826 0.3374 -0.0620 -0.0278 -0.0729 45  ARG A DH11 
895  D DH12 A ARG A 46  ? 0.4164 0.3105 0.3326 0.1307  0.0972  0.1062  45  ARG A DH12 
896  D DH12 B ARG A 46  ? 0.4050 0.3037 0.2896 0.0403  0.0584  -0.0234 45  ARG A DH12 
897  D DH21 A ARG A 46  ? 0.3539 0.2200 0.3376 0.0029  0.0875  0.0067  45  ARG A DH21 
898  D DH21 B ARG A 46  ? 0.4700 0.1974 0.2746 0.0279  0.0947  -0.0839 45  ARG A DH21 
899  D DH22 A ARG A 46  ? 0.3764 0.0679 0.3314 -0.0624 0.0605  -0.0228 45  ARG A DH22 
900  D DH22 B ARG A 46  ? 0.4267 0.1025 0.2971 -0.0236 0.0915  -0.0879 45  ARG A DH22 
901  N N    . ASN A 47  ? 0.1068 0.1754 0.1201 0.0062  0.0125  0.0174  46  ASN A N    
902  C CA   . ASN A 47  ? 0.1138 0.1882 0.1425 0.0115  0.0314  0.0113  46  ASN A CA   
903  C C    . ASN A 47  ? 0.1203 0.1636 0.1380 0.0038  0.0347  -0.0122 46  ASN A C    
904  O O    . ASN A 47  ? 0.1691 0.1545 0.1475 0.0118  0.0531  -0.0209 46  ASN A O    
905  C CB   . ASN A 47  ? 0.1444 0.1611 0.1612 -0.0006 0.0413  0.0008  46  ASN A CB   
906  C CG   . ASN A 47  ? 0.1582 0.1723 0.1853 -0.0033 0.0314  0.0252  46  ASN A CG   
907  O OD1  . ASN A 47  ? 0.2019 0.1929 0.2192 0.0151  0.0105  0.0407  46  ASN A OD1  
908  N ND2  . ASN A 47  ? 0.1646 0.1842 0.1988 -0.0052 0.0564  0.0198  46  ASN A ND2  
909  D D    . ASN A 47  ? 0.1170 0.2252 0.1202 0.0180  -0.0040 -0.0180 46  ASN A D    
910  D DA   . ASN A 47  ? 0.1231 0.2428 0.1611 0.0274  0.0280  0.0283  46  ASN A DA   
911  D DB2  . ASN A 47  ? 0.1416 0.2027 0.1547 -0.0130 0.0260  0.0089  46  ASN A DB2  
912  D DB3  . ASN A 47  ? 0.2115 0.1978 0.1978 -0.0031 0.0803  -0.0219 46  ASN A DB3  
913  D DD21 . ASN A 47  ? 0.2313 0.2672 0.2768 -0.0041 0.0958  0.0875  46  ASN A DD21 
914  D DD22 . ASN A 47  ? 0.1554 0.2322 0.2639 -0.0100 0.0446  0.0612  46  ASN A DD22 
915  N N    . THR A 48  ? 0.1736 0.1595 0.1785 0.0319  0.0818  0.0186  47  THR A N    
916  C CA   . THR A 48  ? 0.1583 0.1987 0.1650 -0.0010 0.0650  0.0110  47  THR A CA   
917  C C    . THR A 48  ? 0.1411 0.2501 0.1687 0.0103  0.0720  0.0180  47  THR A C    
918  O O    . THR A 48  ? 0.1670 0.2985 0.1780 -0.0192 0.0513  0.0422  47  THR A O    
919  C CB   . THR A 48  ? 0.1302 0.2471 0.1951 -0.0092 0.0520  -0.0156 47  THR A CB   
920  O OG1  . THR A 48  ? 0.1646 0.2310 0.1845 0.0370  0.0004  -0.0113 47  THR A OG1  
921  C CG2  . THR A 48  ? 0.1607 0.2195 0.2278 0.0008  0.0220  -0.0191 47  THR A CG2  
922  D D    . THR A 48  ? 0.1985 0.1690 0.2353 0.0542  0.1058  0.0285  47  THR A D    
923  D DA   . THR A 48  ? 0.2512 0.2052 0.1769 -0.0309 0.0834  0.0028  47  THR A DA   
924  D DB   . THR A 48  ? 0.2002 0.2595 0.1871 -0.0091 0.0718  -0.0244 47  THR A DB   
925  D DG1  . THR A 48  ? 0.2180 0.2731 0.2546 0.0639  -0.0468 -0.0014 47  THR A DG1  
926  D DG21 . THR A 48  ? 0.1259 0.2621 0.2618 -0.0096 -0.0096 0.0254  47  THR A DG21 
927  D DG22 . THR A 48  ? 0.1767 0.3843 0.2498 0.0684  0.0127  -0.0112 47  THR A DG22 
928  D DG23 . THR A 48  ? 0.2759 0.2291 0.2505 -0.0065 -0.0292 -0.0172 47  THR A DG23 
929  N N    . ASP A 49  ? 0.1707 0.2493 0.1540 -0.0119 0.0683  -0.0081 48  ASP A N    
930  C CA   . ASP A 49  ? 0.1933 0.2646 0.1524 -0.0141 0.0592  -0.0192 48  ASP A CA   
931  C C    . ASP A 49  ? 0.1968 0.2773 0.1247 0.0006  0.0617  0.0047  48  ASP A C    
932  O O    . ASP A 49  ? 0.2504 0.4378 0.1198 0.0725  0.0383  -0.0178 48  ASP A O    
933  C CB   . ASP A 49  ? 0.2307 0.2856 0.1628 -0.0364 0.0799  -0.0637 48  ASP A CB   
934  C CG   . ASP A 49  ? 0.2589 0.2426 0.1728 -0.0532 0.0825  -0.0593 48  ASP A CG   
935  O OD1  . ASP A 49  ? 0.1994 0.1894 0.1481 -0.0096 0.0673  -0.0144 48  ASP A OD1  
936  O OD2  . ASP A 49  ? 0.3530 0.2647 0.2732 -0.1003 0.1318  -0.1049 48  ASP A OD2  
937  D D    . ASP A 49  ? 0.2783 0.2543 0.1496 -0.0773 0.0348  -0.0075 48  ASP A D    
938  D DA   . ASP A 49  ? 0.2134 0.2768 0.1532 0.0070  0.0637  -0.0089 48  ASP A DA   
939  D DB2  . ASP A 49  ? 0.2759 0.4066 0.1592 -0.0557 0.0651  -0.0927 48  ASP A DB2  
940  D DB3  . ASP A 49  ? 0.2614 0.2836 0.2277 -0.0323 0.1076  -0.0976 48  ASP A DB3  
941  N N    . GLY A 50  ? 0.1576 0.2372 0.1589 -0.0295 0.0719  -0.0026 49  GLY A N    
942  C CA   . GLY A 50  ? 0.1930 0.2128 0.1770 -0.0182 0.0929  0.0294  49  GLY A CA   
943  C C    . GLY A 50  ? 0.1474 0.1752 0.1604 -0.0127 0.0558  0.0351  49  GLY A C    
944  O O    . GLY A 50  ? 0.1965 0.1759 0.2454 0.0118  0.1053  0.0603  49  GLY A O    
945  D D    . GLY A 50  ? 0.1842 0.1979 0.2025 -0.0274 0.0337  -0.0145 49  GLY A D    
946  D DA2  . GLY A 50  ? 0.2233 0.2250 0.2889 -0.0619 0.1157  0.0026  49  GLY A DA2  
947  D DA3  . GLY A 50  ? 0.2632 0.2717 0.1970 0.0117  0.1023  0.0910  49  GLY A DA3  
948  N N    . SER A 51  ? 0.1376 0.1591 0.1079 -0.0172 0.0232  0.0110  50  SER A N    
949  C CA   . SER A 51  ? 0.1088 0.1358 0.0965 -0.0085 0.0050  0.0224  50  SER A CA   
950  C C    . SER A 51  ? 0.0922 0.1428 0.0962 -0.0036 0.0048  0.0157  50  SER A C    
951  O O    . SER A 51  ? 0.0917 0.1544 0.1151 -0.0032 0.0097  -0.0044 50  SER A O    
952  C CB   . SER A 51  ? 0.1327 0.1511 0.1023 -0.0191 0.0113  0.0111  50  SER A CB   
953  O OG   . SER A 51  ? 0.1603 0.1379 0.1034 -0.0022 0.0205  -0.0070 50  SER A OG   
954  D D    . SER A 51  ? 0.1761 0.1883 0.1471 0.0111  0.0532  0.0197  50  SER A D    
955  D DA   . SER A 51  ? 0.1292 0.1536 0.1066 0.0078  -0.0017 0.0337  50  SER A DA   
956  D DB2  . SER A 51  ? 0.1304 0.1578 0.1688 -0.0218 0.0389  0.0098  50  SER A DB2  
957  D DB3  . SER A 51  ? 0.2064 0.2004 0.1086 -0.0168 -0.0099 -0.0030 50  SER A DB3  
958  D DG   . SER A 51  ? 0.1830 0.2043 0.1080 0.0157  0.0328  -0.0255 50  SER A DG   
959  N N    . THR A 52  ? 0.0848 0.1264 0.0946 0.0055  0.0050  0.0156  51  THR A N    
960  C CA   . THR A 52  ? 0.0767 0.1038 0.0949 -0.0003 0.0082  0.0148  51  THR A CA   
961  C C    . THR A 52  ? 0.0727 0.0992 0.0902 -0.0069 0.0011  0.0077  51  THR A C    
962  O O    . THR A 52  ? 0.0815 0.1302 0.0865 -0.0131 -0.0073 0.0208  51  THR A O    
963  C CB   . THR A 52  ? 0.0884 0.1004 0.1152 -0.0021 0.0029  0.0057  51  THR A CB   
964  O OG1  . THR A 52  ? 0.1211 0.1135 0.1278 -0.0213 0.0093  0.0078  51  THR A OG1  
965  C CG2  . THR A 52  ? 0.1073 0.1275 0.1139 -0.0283 -0.0059 -0.0050 51  THR A CG2  
966  D D    . THR A 52  ? 0.0902 0.1583 0.1268 0.0000  0.0028  0.0327  51  THR A D    
967  D DA   . THR A 52  ? 0.0706 0.1153 0.1155 -0.0085 0.0007  0.0129  51  THR A DA   
968  D DB   . THR A 52  ? 0.0979 0.1149 0.1447 0.0098  -0.0022 0.0078  51  THR A DB   
969  D DG1  . THR A 52  ? 0.1637 0.1155 0.1344 -0.0385 -0.0116 0.0102  51  THR A DG1  
970  D DG21 . THR A 52  ? 0.1228 0.1916 0.1220 -0.0071 -0.0090 0.0017  51  THR A DG21 
971  D DG22 . THR A 52  ? 0.1649 0.1390 0.1534 -0.0298 -0.0257 -0.0279 51  THR A DG22 
972  D DG23 . THR A 52  ? 0.1365 0.1631 0.1255 -0.0477 -0.0016 0.0019  51  THR A DG23 
973  N N    . ASP A 53  ? 0.0786 0.1152 0.0888 -0.0128 -0.0034 0.0175  52  ASP A N    
974  C CA   . ASP A 53  ? 0.0848 0.1063 0.0861 -0.0154 -0.0060 0.0129  52  ASP A CA   
975  C C    . ASP A 53  ? 0.0755 0.1192 0.0855 -0.0037 -0.0078 0.0151  52  ASP A C    
976  O O    . ASP A 53  ? 0.0752 0.1653 0.1031 -0.0042 -0.0072 -0.0160 52  ASP A O    
977  C CB   . ASP A 53  ? 0.1196 0.1109 0.1069 -0.0012 -0.0038 0.0136  52  ASP A CB   
978  C CG   . ASP A 53  ? 0.1522 0.1320 0.1162 0.0097  -0.0003 -0.0055 52  ASP A CG   
979  O OD1  . ASP A 53  ? 0.2128 0.2314 0.1369 0.0508  -0.0375 -0.0455 52  ASP A OD1  
980  O OD2  . ASP A 53  ? 0.1801 0.2845 0.1632 0.0755  -0.0044 -0.0595 52  ASP A OD2  
982  D DA   . ASP A 53  ? 0.1026 0.1175 0.1038 -0.0257 -0.0265 0.0160  52  ASP A DA   
983  D DB2  . ASP A 53  ? 0.1268 0.1497 0.1299 0.0177  -0.0204 -0.0027 52  ASP A DB2  
984  D DB3  . ASP A 53  ? 0.1575 0.1096 0.1486 -0.0043 0.0214  0.0212  52  ASP A DB3  
985  N N    . TYR A 54  ? 0.0762 0.1016 0.0947 0.0004  -0.0015 0.0159  53  TYR A N    
986  C CA   . TYR A 54  ? 0.0871 0.1016 0.0975 0.0024  0.0028  0.0168  53  TYR A CA   
987  C C    . TYR A 54  ? 0.0909 0.0913 0.0848 0.0008  -0.0020 0.0039  53  TYR A C    
988  O O    . TYR A 54  ? 0.1060 0.1037 0.0984 -0.0142 0.0033  -0.0014 53  TYR A O    
989  C CB   . TYR A 54  ? 0.0819 0.1164 0.1112 0.0133  0.0168  0.0212  53  TYR A CB   
990  C CG   . TYR A 54  ? 0.0982 0.1046 0.1053 0.0084  0.0017  0.0160  53  TYR A CG   
991  C CD1  . TYR A 54  ? 0.1546 0.1064 0.0993 -0.0027 -0.0049 0.0185  53  TYR A CD1  
992  C CD2  . TYR A 54  ? 0.0811 0.1159 0.1053 -0.0026 -0.0032 0.0165  53  TYR A CD2  
993  C CE1  . TYR A 54  ? 0.1636 0.0951 0.1095 0.0003  -0.0230 0.0225  53  TYR A CE1  
994  C CE2  . TYR A 54  ? 0.0886 0.1212 0.1060 -0.0051 -0.0160 0.0246  53  TYR A CE2  
995  C CZ   . TYR A 54  ? 0.1134 0.1123 0.1114 -0.0029 -0.0099 0.0266  53  TYR A CZ   
996  O OH   . TYR A 54  ? 0.1379 0.1200 0.1201 -0.0094 -0.0205 0.0397  53  TYR A OH   
998  D D    B TYR A 54  ? 0.0697 0.0572 0.0772 0.0203  -0.0241 0.0511  53  TYR A D    
999  D DA   . TYR A 54  ? 0.0929 0.1233 0.1099 -0.0154 0.0070  0.0074  53  TYR A DA   
1000 D DB2  . TYR A 54  ? 0.1038 0.1353 0.1721 -0.0087 -0.0200 0.0473  53  TYR A DB2  
1001 D DB3  . TYR A 54  ? 0.1174 0.1584 0.1334 0.0390  0.0577  0.0338  53  TYR A DB3  
1002 D DD1  . TYR A 54  ? 0.2585 0.1139 0.1009 -0.0157 -0.0238 0.0139  53  TYR A DD1  
1003 D DD2  . TYR A 54  ? 0.1200 0.1293 0.1176 -0.0136 0.0108  0.0009  53  TYR A DD2  
1004 D DE1  . TYR A 54  ? 0.3173 0.1080 0.1493 -0.0439 -0.0311 0.0142  53  TYR A DE1  
1005 D DE2  . TYR A 54  ? 0.1332 0.1379 0.1097 -0.0214 -0.0189 0.0252  53  TYR A DE2  
1006 D DH   . TYR A 54  ? 0.1423 0.1684 0.1187 -0.0111 -0.0221 0.0515  53  TYR A DH   
1007 N N    . GLY A 55  ? 0.1161 0.0958 0.0901 -0.0066 -0.0124 0.0067  54  GLY A N    
1008 C CA   . GLY A 55  ? 0.1312 0.1149 0.0805 0.0185  -0.0102 0.0118  54  GLY A CA   
1009 C C    . GLY A 55  ? 0.0917 0.1085 0.0825 0.0091  -0.0003 0.0046  54  GLY A C    
1010 O O    . GLY A 55  ? 0.0796 0.1195 0.0998 0.0059  0.0089  0.0098  54  GLY A O    
1012 D DA2  . GLY A 55  ? 0.2097 0.1111 0.0929 0.0305  -0.0273 0.0030  54  GLY A DA2  
1013 D DA3  . GLY A 55  ? 0.1288 0.1369 0.1194 0.0244  0.0048  0.0429  54  GLY A DA3  
1014 N N    . ILE A 56  ? 0.0974 0.1167 0.0839 0.0117  0.0053  0.0081  55  ILE A N    
1015 C CA   . ILE A 56  ? 0.1001 0.1199 0.0939 -0.0004 -0.0071 0.0158  55  ILE A CA   
1016 C C    . ILE A 56  ? 0.1018 0.1049 0.0922 -0.0078 -0.0130 0.0270  55  ILE A C    
1017 O O    . ILE A 56  ? 0.1499 0.1110 0.1029 0.0130  -0.0297 0.0144  55  ILE A O    
1018 C CB   . ILE A 56  ? 0.1570 0.1708 0.0983 -0.0211 0.0205  0.0160  55  ILE A CB   
1019 C CG1  . ILE A 56  ? 0.2326 0.1955 0.1635 -0.0142 0.0265  0.0747  55  ILE A CG1  
1020 C CG2  . ILE A 56  ? 0.1352 0.2194 0.1528 -0.0236 0.0418  0.0040  55  ILE A CG2  
1021 C CD1  . ILE A 56  ? 0.2763 0.2476 0.1615 0.0272  0.0385  0.0921  55  ILE A CD1  
1023 D D    B ILE A 56  ? 0.0856 0.1181 0.1251 0.0049  0.0153  0.0018  55  ILE A D    
1024 D DA   . ILE A 56  ? 0.1171 0.1407 0.1057 0.0050  -0.0250 0.0121  55  ILE A DA   
1025 D DB   . ILE A 56  ? 0.1994 0.1737 0.1251 0.0024  0.0245  -0.0006 55  ILE A DB   
1026 D DG12 . ILE A 56  ? 0.2816 0.2000 0.2531 0.0104  0.0105  0.0350  55  ILE A DG12 
1027 D DG13 . ILE A 56  ? 0.2343 0.2783 0.1527 -0.0034 0.0021  0.0884  55  ILE A DG13 
1028 D DG21 . ILE A 56  ? 0.1700 0.2643 0.2532 -0.0650 0.0326  -0.0521 55  ILE A DG21 
1029 D DG22 . ILE A 56  ? 0.1987 0.3170 0.2306 0.0179  0.1089  0.0268  55  ILE A DG22 
1030 D DG23 . ILE A 56  ? 0.1589 0.2889 0.2207 -0.0153 -0.0027 0.0525  55  ILE A DG23 
1031 D DD11 . ILE A 56  ? 0.3805 0.2901 0.2188 -0.0205 0.0842  0.0370  55  ILE A DD11 
1032 D DD12 . ILE A 56  ? 0.2652 0.3288 0.2733 0.0674  0.0593  0.0484  55  ILE A DD12 
1033 D DD13 . ILE A 56  ? 0.2927 0.3006 0.1945 0.0315  0.0516  0.1336  55  ILE A DD13 
1034 N N    A LEU A 57  ? 0.0990 0.1039 0.0927 -0.0067 -0.0096 0.0185  56  LEU A N    
1035 N N    C LEU A 57  ? 0.1049 0.1047 0.0940 0.0051  -0.0105 0.0129  56  LEU A N    
1036 C CA   A LEU A 57  ? 0.1009 0.0889 0.0922 0.0019  -0.0192 0.0245  56  LEU A CA   
1037 C CA   C LEU A 57  ? 0.1192 0.0915 0.0921 -0.0055 -0.0119 0.0186  56  LEU A CA   
1038 C C    A LEU A 57  ? 0.1094 0.0892 0.0903 -0.0042 -0.0146 0.0142  56  LEU A C    
1039 C C    C LEU A 57  ? 0.1175 0.0858 0.0977 -0.0003 -0.0015 0.0129  56  LEU A C    
1040 O O    A LEU A 57  ? 0.0998 0.1277 0.1043 -0.0315 -0.0031 -0.0061 56  LEU A O    
1041 O O    C LEU A 57  ? 0.1103 0.1113 0.1201 -0.0246 0.0187  -0.0123 56  LEU A O    
1042 C CB   A LEU A 57  ? 0.1027 0.1251 0.1033 -0.0069 -0.0221 0.0214  56  LEU A CB   
1043 C CB   C LEU A 57  ? 0.1150 0.1181 0.1038 -0.0077 -0.0133 0.0257  56  LEU A CB   
1044 C CG   A LEU A 57  ? 0.1183 0.1379 0.1364 -0.0192 -0.0036 0.0328  56  LEU A CG   
1045 C CG   C LEU A 57  ? 0.1354 0.1370 0.1296 -0.0137 0.0087  0.0391  56  LEU A CG   
1046 C CD1  A LEU A 57  ? 0.1156 0.1626 0.1828 -0.0214 -0.0057 0.0205  56  LEU A CD1  
1047 C CD1  C LEU A 57  ? 0.1376 0.1490 0.1747 -0.0236 0.0063  0.0316  56  LEU A CD1  
1048 C CD2  A LEU A 57  ? 0.1534 0.1470 0.1314 -0.0006 0.0019  0.0443  56  LEU A CD2  
1049 C CD2  C LEU A 57  ? 0.1538 0.1247 0.1463 -0.0117 -0.0222 0.0304  56  LEU A CD2  
1052 D DA   A LEU A 57  ? 0.1155 0.0980 0.1144 0.0157  -0.0224 0.0317  56  LEU A DA   
1053 D DA   C LEU A 57  ? 0.1294 0.0870 0.1021 0.0022  -0.0171 0.0111  56  LEU A DA   
1054 D DB2  A LEU A 57  ? 0.0993 0.1410 0.1245 -0.0066 -0.0381 0.0360  56  LEU A DB2  
1055 D DB2  C LEU A 57  ? 0.1173 0.1464 0.1742 0.0069  -0.0016 0.0616  56  LEU A DB2  
1056 D DB3  A LEU A 57  ? 0.1348 0.1718 0.1178 -0.0169 -0.0340 -0.0038 56  LEU A DB3  
1057 D DB3  C LEU A 57  ? 0.1645 0.1757 0.1103 -0.0750 0.0047  0.0056  56  LEU A DB3  
1058 D DG   A LEU A 57  ? 0.1180 0.1592 0.1306 -0.0159 0.0057  0.0290  56  LEU A DG   
1059 D DG   C LEU A 57  ? 0.1331 0.1574 0.1273 0.0137  0.0062  0.0265  56  LEU A DG   
1060 D DD11 A LEU A 57  ? 0.1620 0.2105 0.2088 -0.0163 -0.0452 -0.0115 56  LEU A DD11 
1061 D DD11 C LEU A 57  ? 0.1894 0.2441 0.1935 -0.0342 -0.0269 0.0057  56  LEU A DD11 
1062 D DD12 A LEU A 57  ? 0.1031 0.2100 0.2222 -0.0042 0.0025  0.0624  56  LEU A DD12 
1063 D DD12 C LEU A 57  ? 0.1686 0.1951 0.2299 -0.0413 0.0126  0.0713  56  LEU A DD12 
1064 D DD13 A LEU A 57  ? 0.0986 0.1841 0.2194 -0.0158 0.0012  0.0474  56  LEU A DD13 
1065 D DD13 C LEU A 57  ? 0.1469 0.1793 0.2583 0.0036  0.0272  0.0499  56  LEU A DD13 
1066 D DD21 A LEU A 57  ? 0.2683 0.1975 0.1576 0.0554  -0.0277 0.0068  56  LEU A DD21 
1067 D DD21 C LEU A 57  ? 0.2519 0.1466 0.1723 -0.0221 -0.0413 0.0017  56  LEU A DD21 
1068 D DD22 A LEU A 57  ? 0.1515 0.2200 0.1025 -0.0082 0.0087  0.0781  56  LEU A DD22 
1069 D DD22 C LEU A 57  ? 0.1460 0.1939 0.2046 -0.0051 -0.0143 0.0157  56  LEU A DD22 
1070 D DD23 A LEU A 57  ? 0.1562 0.2007 0.2155 0.0078  0.0160  0.1078  56  LEU A DD23 
1071 D DD23 C LEU A 57  ? 0.1775 0.1822 0.1864 0.0089  -0.0074 0.0790  56  LEU A DD23 
1072 N N    . GLN A 58  ? 0.0960 0.0930 0.0828 -0.0006 -0.0108 0.0060  57  GLN A N    
1073 C CA   . GLN A 58  ? 0.0959 0.0891 0.0875 0.0086  -0.0086 0.0183  57  GLN A CA   
1074 C C    . GLN A 58  ? 0.0947 0.0972 0.0903 0.0043  -0.0062 0.0134  57  GLN A C    
1075 O O    . GLN A 58  ? 0.1247 0.1542 0.0899 0.0227  -0.0029 -0.0042 57  GLN A O    
1076 C CB   . GLN A 58  ? 0.1021 0.0923 0.1022 0.0202  -0.0070 0.0113  57  GLN A CB   
1077 C CG   . GLN A 58  ? 0.1092 0.1093 0.1062 0.0108  -0.0168 0.0357  57  GLN A CG   
1078 C CD   . GLN A 58  ? 0.1026 0.1150 0.1150 0.0003  -0.0061 0.0211  57  GLN A CD   
1079 O OE1  . GLN A 58  ? 0.1001 0.1562 0.1567 -0.0172 0.0093  0.0090  57  GLN A OE1  
1080 N NE2  . GLN A 58  ? 0.1189 0.1193 0.1253 -0.0090 -0.0045 0.0029  57  GLN A NE2  
1082 D DA   . GLN A 58  ? 0.0974 0.0886 0.1095 0.0052  -0.0006 0.0070  57  GLN A DA   
1083 D DB2  . GLN A 58  ? 0.1304 0.0874 0.1572 0.0145  -0.0276 0.0213  57  GLN A DB2  
1084 D DB3  . GLN A 58  ? 0.1247 0.1222 0.0972 0.0087  -0.0033 -0.0086 57  GLN A DB3  
1085 D DG2  . GLN A 58  ? 0.1555 0.1400 0.1144 -0.0100 0.0015  0.0309  57  GLN A DG2  
1086 D DG3  . GLN A 58  ? 0.1267 0.1270 0.1553 0.0249  -0.0398 0.0312  57  GLN A DG3  
1087 D DE21 . GLN A 58  ? 0.1456 0.1191 0.2056 -0.0117 0.0264  -0.0080 57  GLN A DE21 
1088 D DE22 . GLN A 58  ? 0.1370 0.1402 0.1192 -0.0154 0.0058  -0.0126 57  GLN A DE22 
1089 N N    . ILE A 59  ? 0.0969 0.1080 0.0782 0.0046  -0.0154 0.0118  58  ILE A N    
1090 C CA   . ILE A 59  ? 0.0922 0.1083 0.0894 -0.0080 -0.0139 0.0155  58  ILE A CA   
1091 C C    . ILE A 59  ? 0.1051 0.1053 0.0822 -0.0170 -0.0141 0.0118  58  ILE A C    
1092 O O    . ILE A 59  ? 0.1213 0.1127 0.0976 -0.0330 -0.0087 0.0094  58  ILE A O    
1093 C CB   . ILE A 59  ? 0.0923 0.1347 0.0918 -0.0013 -0.0146 0.0302  58  ILE A CB   
1094 C CG1  . ILE A 59  ? 0.1025 0.1650 0.1233 -0.0122 -0.0014 0.0503  58  ILE A CG1  
1095 C CG2  . ILE A 59  ? 0.1023 0.1769 0.1179 -0.0226 -0.0371 0.0458  58  ILE A CG2  
1096 C CD1  . ILE A 59  ? 0.1039 0.2028 0.1514 -0.0090 0.0040  0.0468  58  ILE A CD1  
1098 D DA   . ILE A 59  ? 0.1249 0.1079 0.0993 -0.0135 -0.0268 0.0030  58  ILE A DA   
1099 D DB   . ILE A 59  ? 0.1027 0.1622 0.1187 0.0077  -0.0042 -0.0029 58  ILE A DB   
1100 D DG12 . ILE A 59  ? 0.2026 0.1611 0.1784 -0.0391 0.0408  0.0256  58  ILE A DG12 
1101 D DG13 . ILE A 59  ? 0.1091 0.2373 0.1748 -0.0167 0.0024  0.1228  58  ILE A DG13 
1102 D DG21 . ILE A 59  ? 0.1782 0.2004 0.1309 -0.0227 -0.0726 0.0288  58  ILE A DG21 
1103 D DG22 . ILE A 59  ? 0.0916 0.2405 0.1886 -0.0117 -0.0351 0.0688  58  ILE A DG22 
1104 D DG23 . ILE A 59  ? 0.1301 0.1898 0.1459 -0.0163 -0.0445 0.0723  58  ILE A DG23 
1105 D DD11 . ILE A 59  ? 0.1743 0.2723 0.2473 -0.0007 0.0301  -0.0377 58  ILE A DD11 
1106 D DD12 . ILE A 59  ? 0.1053 0.3588 0.2020 -0.0075 -0.0118 0.0911  58  ILE A DD12 
1107 D DD13 . ILE A 59  ? 0.1490 0.2483 0.2313 -0.0181 0.0510  0.0880  58  ILE A DD13 
1108 N N    . ASN A 60  ? 0.1126 0.1138 0.0848 -0.0208 -0.0135 0.0103  59  ASN A N    
1109 C CA   . ASN A 60  ? 0.1141 0.1209 0.0801 -0.0154 -0.0152 0.0098  59  ASN A CA   
1110 C C    . ASN A 60  ? 0.0975 0.1140 0.0920 -0.0228 -0.0102 0.0144  59  ASN A C    
1111 O O    . ASN A 60  ? 0.1114 0.1503 0.1152 -0.0406 -0.0284 0.0308  59  ASN A O    
1112 C CB   . ASN A 60  ? 0.1243 0.1291 0.1076 -0.0083 0.0082  0.0035  59  ASN A CB   
1113 C CG   . ASN A 60  ? 0.1358 0.1370 0.1057 -0.0096 0.0017  0.0152  59  ASN A CG   
1114 O OD1  . ASN A 60  ? 0.1527 0.1569 0.0960 0.0249  0.0091  0.0034  59  ASN A OD1  
1115 N ND2  . ASN A 60  ? 0.1317 0.1800 0.1283 -0.0272 0.0061  0.0200  59  ASN A ND2  
1117 D D    B ASN A 60  ? 0.0943 0.1153 0.0961 -0.0147 -0.0108 0.0017  59  ASN A D    
1118 D DA   . ASN A 60  ? 0.1188 0.1393 0.0945 -0.0297 -0.0266 0.0188  59  ASN A DA   
1119 D DB2  . ASN A 60  ? 0.1605 0.1374 0.1364 0.0042  0.0004  0.0192  59  ASN A DB2  
1120 D DB3  . ASN A 60  ? 0.1432 0.1738 0.1138 -0.0251 0.0133  -0.0231 59  ASN A DB3  
1121 D DD21 . ASN A 60  ? 0.1519 0.2139 0.1648 -0.0219 0.0291  0.0552  59  ASN A DD21 
1122 D DD22 . ASN A 60  ? 0.1595 0.2455 0.1445 -0.0329 -0.0087 0.0556  59  ASN A DD22 
1123 N N    . SER A 61  ? 0.1005 0.1209 0.0871 -0.0247 -0.0137 0.0176  60  SER A N    
1124 C CA   . SER A 61  ? 0.0955 0.1244 0.0803 -0.0112 0.0019  0.0143  60  SER A CA   
1125 C C    . SER A 61  ? 0.0914 0.1530 0.0824 -0.0002 -0.0024 0.0106  60  SER A C    
1126 O O    . SER A 61  ? 0.1326 0.1783 0.0957 0.0253  -0.0333 -0.0008 60  SER A O    
1127 C CB   . SER A 61  ? 0.1001 0.1222 0.1014 -0.0083 -0.0212 0.0215  60  SER A CB   
1128 O OG   . SER A 61  ? 0.0974 0.1285 0.1357 -0.0188 -0.0176 0.0368  60  SER A OG   
1130 D DA   . SER A 61  ? 0.0946 0.1742 0.0944 -0.0169 0.0065  -0.0068 60  SER A DA   
1131 D DB2  . SER A 61  ? 0.1312 0.1288 0.1496 0.0099  -0.0261 0.0256  60  SER A DB2  
1132 D DB3  . SER A 61  ? 0.1406 0.1543 0.1020 -0.0336 -0.0293 0.0131  60  SER A DB3  
1133 D DG   . SER A 61  ? 0.1179 0.1190 0.1436 -0.0160 0.0028  0.0317  60  SER A DG   
1134 N N    . ARG A 62  ? 0.1092 0.1319 0.0836 -0.0196 -0.0040 0.0109  61  ARG A N    
1135 C CA   . ARG A 62  ? 0.1243 0.1346 0.0805 -0.0088 -0.0021 0.0228  61  ARG A CA   
1136 C C    . ARG A 62  ? 0.1243 0.1205 0.0740 -0.0088 -0.0103 0.0120  61  ARG A C    
1137 O O    . ARG A 62  ? 0.1425 0.1343 0.1454 -0.0070 -0.0333 0.0441  61  ARG A O    
1138 C CB   . ARG A 62  ? 0.1377 0.1760 0.0906 -0.0031 0.0169  0.0121  61  ARG A CB   
1139 C CG   . ARG A 62  ? 0.2254 0.2500 0.0904 -0.0108 0.0062  -0.0055 61  ARG A CG   
1140 C CD   . ARG A 62  ? 0.3069 0.3275 0.1289 0.0072  0.0307  -0.0781 61  ARG A CD   
1141 N NE   . ARG A 62  ? 0.2767 0.3998 0.2299 0.0414  0.0481  -0.0708 61  ARG A NE   
1142 C CZ   . ARG A 62  ? 0.3108 0.4136 0.3231 0.0022  0.0657  -0.0803 61  ARG A CZ   
1143 N NH1  . ARG A 62  ? 0.3708 0.4146 0.3818 -0.0056 0.0889  -0.0218 61  ARG A NH1  
1144 N NH2  . ARG A 62  ? 0.3067 0.3976 0.3765 0.0079  0.0613  -0.1486 61  ARG A NH2  
1146 D DA   . ARG A 62  ? 0.1547 0.1298 0.1059 -0.0151 -0.0003 0.0290  61  ARG A DA   
1147 D DB2  . ARG A 62  ? 0.1481 0.2496 0.1151 -0.0200 0.0135  -0.0327 61  ARG A DB2  
1148 D DB3  . ARG A 62  ? 0.1722 0.1683 0.1142 0.0146  0.0249  0.0030  61  ARG A DB3  
1149 D DG2  . ARG A 62  ? 0.2400 0.4101 0.1183 -0.0497 0.0046  -0.0535 61  ARG A DG2  
1150 D DG3  . ARG A 62  ? 0.2785 0.2832 0.1277 0.0205  0.0277  0.0598  61  ARG A DG3  
1151 D DD2  . ARG A 62  ? 0.3662 0.3152 0.3174 0.0131  0.0789  -0.0827 61  ARG A DD2  
1152 D DD3  . ARG A 62  ? 0.3972 0.5617 0.1311 0.0331  0.0329  -0.0654 61  ARG A DD3  
1153 D DE   . ARG A 62  ? 0.2982 0.5379 0.2125 0.0792  0.0523  -0.0246 61  ARG A DE   
1154 D DH11 . ARG A 62  ? 0.3248 0.5336 0.3590 -0.0216 0.1314  0.1154  61  ARG A DH11 
1155 D DH12 . ARG A 62  ? 0.4405 0.5775 0.4705 -0.1535 0.0078  0.0390  61  ARG A DH12 
1156 D DH21 . ARG A 62  ? 0.4701 0.4327 0.8969 -0.0395 -0.1268 -0.1898 61  ARG A DH21 
1157 D DH22 . ARG A 62  ? 0.4477 0.4436 0.9584 0.0126  -0.1300 -0.0758 61  ARG A DH22 
1158 N N    . TRP A 63  ? 0.1134 0.1242 0.1071 0.0056  -0.0035 0.0251  62  TRP A N    
1159 C CA   . TRP A 63  ? 0.1153 0.1390 0.1126 -0.0071 0.0103  0.0085  62  TRP A CA   
1160 C C    . TRP A 63  ? 0.1034 0.1257 0.0987 0.0002  -0.0126 0.0070  62  TRP A C    
1161 O O    . TRP A 63  ? 0.1074 0.1594 0.0841 -0.0012 -0.0143 -0.0008 62  TRP A O    
1162 C CB   . TRP A 63  ? 0.1414 0.1445 0.1368 -0.0050 -0.0095 -0.0098 62  TRP A CB   
1163 C CG   . TRP A 63  ? 0.1984 0.1787 0.1345 -0.0077 -0.0052 -0.0227 62  TRP A CG   
1164 C CD1  . TRP A 63  ? 0.1714 0.2133 0.1254 -0.0107 -0.0115 -0.0244 62  TRP A CD1  
1165 C CD2  . TRP A 63  ? 0.2201 0.1865 0.1522 0.0006  -0.0142 -0.0377 62  TRP A CD2  
1166 N NE1  . TRP A 63  ? 0.1976 0.2450 0.1590 0.0113  0.0157  -0.0416 62  TRP A NE1  
1167 C CE2  . TRP A 63  ? 0.2360 0.2271 0.1743 0.0067  0.0079  -0.0627 62  TRP A CE2  
1168 C CE3  . TRP A 63  ? 0.2754 0.1813 0.2116 -0.0161 0.0120  -0.0422 62  TRP A CE3  
1169 C CZ2  . TRP A 63  ? 0.3431 0.2258 0.2142 0.0601  0.0242  -0.0679 62  TRP A CZ2  
1170 C CZ3  . TRP A 63  ? 0.3652 0.1886 0.2565 -0.0105 0.0142  -0.0606 62  TRP A CZ3  
1171 C CH2  . TRP A 63  ? 0.3721 0.2191 0.2497 0.0178  0.0053  -0.0878 62  TRP A CH2  
1172 D D    . TRP A 63  ? 0.1135 0.1870 0.2106 0.0136  0.0082  0.1128  62  TRP A D    
1173 D DA   . TRP A 63  ? 0.1443 0.1699 0.1037 -0.0156 -0.0076 -0.0016 62  TRP A DA   
1174 D DB2  . TRP A 63  ? 0.1921 0.1443 0.1320 0.0270  0.0015  -0.0034 62  TRP A DB2  
1175 D DB3  . TRP A 63  ? 0.1491 0.1671 0.2403 -0.0262 -0.0064 -0.0112 62  TRP A DB3  
1176 D DD1  . TRP A 63  ? 0.2798 0.2212 0.1814 -0.0495 0.0507  -0.0256 62  TRP A DD1  
1177 D DE1  . TRP A 63  ? 0.2941 0.3305 0.1877 -0.0037 0.0784  -0.0400 62  TRP A DE1  
1178 D DE3  . TRP A 63  ? 0.4149 0.2090 0.2652 -0.0548 0.1002  -0.0524 62  TRP A DE3  
1179 D DZ2  . TRP A 63  ? 0.4294 0.2961 0.2316 0.0129  0.0620  -0.1202 62  TRP A DZ2  
1180 D DZ3  . TRP A 63  ? 0.5872 0.2300 0.2653 -0.1390 -0.0028 -0.0854 62  TRP A DZ3  
1181 D DH2  . TRP A 63  ? 0.9222 0.1974 0.2759 0.0071  0.1182  -0.0759 62  TRP A DH2  
1182 N N    . TRP A 64  ? 0.0811 0.1140 0.1015 0.0024  -0.0150 0.0117  63  TRP A N    
1183 C CA   . TRP A 64  ? 0.0876 0.1072 0.1018 0.0028  -0.0097 0.0081  63  TRP A CA   
1184 C C    . TRP A 64  ? 0.0898 0.1055 0.0946 -0.0016 -0.0214 0.0150  63  TRP A C    
1185 O O    . TRP A 64  ? 0.0939 0.1188 0.1549 -0.0043 -0.0016 -0.0168 63  TRP A O    
1186 C CB   . TRP A 64  ? 0.0956 0.1115 0.1033 -0.0060 -0.0059 0.0195  63  TRP A CB   
1187 C CG   . TRP A 64  ? 0.1227 0.1096 0.1228 0.0056  -0.0018 0.0194  63  TRP A CG   
1188 C CD1  . TRP A 64  ? 0.1341 0.1169 0.1818 0.0160  0.0092  0.0211  63  TRP A CD1  
1189 C CD2  . TRP A 64  ? 0.1453 0.1110 0.1168 -0.0010 -0.0008 0.0107  63  TRP A CD2  
1190 N NE1  . TRP A 64  ? 0.1679 0.1088 0.2113 0.0203  0.0390  0.0157  63  TRP A NE1  
1191 C CE2  . TRP A 64  ? 0.1778 0.1005 0.1351 -0.0023 0.0297  0.0207  63  TRP A CE2  
1192 C CE3  . TRP A 64  ? 0.1463 0.1116 0.1271 -0.0188 -0.0183 0.0173  63  TRP A CE3  
1193 C CZ2  . TRP A 64  ? 0.2456 0.1228 0.1498 -0.0243 0.0419  -0.0084 63  TRP A CZ2  
1194 C CZ3  . TRP A 64  ? 0.1974 0.1383 0.1181 -0.0388 -0.0290 0.0103  63  TRP A CZ3  
1195 C CH2  . TRP A 64  ? 0.2503 0.1347 0.1509 -0.0513 0.0077  -0.0117 63  TRP A CH2  
1197 D DA   . TRP A 64  ? 0.0997 0.1194 0.1072 -0.0218 -0.0110 0.0126  63  TRP A DA   
1198 D DB2  . TRP A 64  ? 0.1181 0.1405 0.1482 -0.0084 -0.0402 0.0218  63  TRP A DB2  
1199 D DB3  . TRP A 64  ? 0.1347 0.1388 0.1150 -0.0043 0.0221  0.0153  63  TRP A DB3  
1200 D DD1  . TRP A 64  ? 0.1391 0.1414 0.3081 0.0132  -0.0216 0.0184  63  TRP A DD1  
1201 D DE1  . TRP A 64  ? 0.1902 0.1634 0.3275 0.0442  0.0586  -0.0339 63  TRP A DE1  
1202 D DE3  . TRP A 64  ? 0.1277 0.1367 0.1543 -0.0108 -0.0212 0.0082  63  TRP A DE3  
1203 D DZ2  . TRP A 64  ? 0.3113 0.1345 0.2096 -0.0017 0.0479  -0.0273 63  TRP A DZ2  
1204 D DZ3  . TRP A 64  ? 0.2037 0.1578 0.2066 -0.0616 -0.0471 0.0093  63  TRP A DZ3  
1205 D DH2  . TRP A 64  ? 0.3321 0.1541 0.2445 -0.0767 -0.0321 -0.0357 63  TRP A DH2  
1206 N N    . CYS A 65  ? 0.0807 0.1299 0.1473 -0.0066 -0.0034 -0.0321 64  CYS A N    
1207 C CA   . CYS A 65  ? 0.0900 0.1227 0.1361 0.0051  0.0085  -0.0156 64  CYS A CA   
1208 C C    . CYS A 65  ? 0.0963 0.1338 0.1245 -0.0001 -0.0012 -0.0076 64  CYS A C    
1209 O O    . CYS A 65  ? 0.1135 0.1260 0.1389 -0.0058 0.0141  -0.0108 64  CYS A O    
1210 C CB   . CYS A 65  ? 0.1165 0.1159 0.1247 -0.0040 0.0167  -0.0126 64  CYS A CB   
1211 S SG   . CYS A 65  ? 0.1189 0.1221 0.1302 0.0046  -0.0041 -0.0056 64  CYS A SG   
1213 D DA   . CYS A 65  ? 0.0880 0.1508 0.1530 -0.0008 0.0193  -0.0263 64  CYS A DA   
1214 D DB2  . CYS A 65  ? 0.1131 0.1349 0.1236 0.0015  0.0113  -0.0127 64  CYS A DB2  
1215 D DB3  . CYS A 65  ? 0.1422 0.1443 0.1524 -0.0179 0.0211  0.0046  64  CYS A DB3  
1216 N N    . ASN A 66  ? 0.0920 0.1362 0.1250 0.0042  -0.0113 -0.0086 65  ASN A N    
1217 C CA   . ASN A 66  ? 0.1189 0.1408 0.1307 0.0023  -0.0158 0.0058  65  ASN A CA   
1218 C C    . ASN A 66  ? 0.1085 0.1227 0.1154 0.0112  -0.0086 0.0104  65  ASN A C    
1219 O O    . ASN A 66  ? 0.1270 0.1235 0.1297 0.0085  0.0025  0.0039  65  ASN A O    
1220 C CB   . ASN A 66  ? 0.1175 0.1780 0.2031 0.0063  -0.0405 0.0294  65  ASN A CB   
1221 C CG   . ASN A 66  ? 0.1936 0.2203 0.2789 0.0399  -0.0116 0.1009  65  ASN A CG   
1222 O OD1  . ASN A 66  ? 0.1915 0.2597 0.2392 0.0151  -0.0252 0.1028  65  ASN A OD1  
1223 N ND2  . ASN A 66  ? 0.4315 0.2513 0.3998 0.1406  0.1184  0.1307  65  ASN A ND2  
1225 D DA   . ASN A 66  ? 0.1275 0.1862 0.1306 -0.0120 -0.0153 -0.0248 65  ASN A DA   
1226 D DB2  . ASN A 66  ? 0.1571 0.2478 0.2743 -0.0123 -0.1003 0.0228  65  ASN A DB2  
1227 D DB3  . ASN A 66  ? 0.1385 0.2429 0.2317 0.0542  -0.0095 0.0372  65  ASN A DB3  
1228 D DD21 . ASN A 66  ? 0.6716 0.2699 0.5129 0.1826  0.2438  0.1853  65  ASN A DD21 
1229 D DD22 . ASN A 66  ? 0.5851 0.2860 0.5102 0.1856  0.2766  0.1090  65  ASN A DD22 
1230 N N    . ASP A 67  ? 0.1087 0.1215 0.1243 0.0117  -0.0085 -0.0047 66  ASP A N    
1231 C CA   . ASP A 67  ? 0.1132 0.1225 0.1409 0.0027  -0.0140 0.0058  66  ASP A CA   
1232 C C    . ASP A 67  ? 0.1493 0.1312 0.1538 -0.0112 -0.0291 0.0157  66  ASP A C    
1233 O O    . ASP A 67  ? 0.1624 0.1324 0.1803 -0.0219 -0.0344 0.0226  66  ASP A O    
1234 C CB   . ASP A 67  ? 0.1040 0.1360 0.1275 -0.0011 -0.0101 0.0029  66  ASP A CB   
1235 C CG   . ASP A 67  ? 0.1121 0.1068 0.1136 -0.0009 -0.0106 0.0247  66  ASP A CG   
1236 O OD1  . ASP A 67  ? 0.1405 0.1542 0.1171 0.0017  -0.0104 0.0448  66  ASP A OD1  
1237 O OD2  . ASP A 67  ? 0.1141 0.1462 0.1149 0.0175  0.0058  0.0422  66  ASP A OD2  
1238 D D    . ASP A 67  ? 0.1477 0.1267 0.1437 0.0033  0.0235  -0.0044 66  ASP A D    
1239 D DA   . ASP A 67  ? 0.1244 0.1595 0.1456 -0.0040 -0.0157 -0.0181 66  ASP A DA   
1240 D DB2  . ASP A 67  ? 0.1437 0.1622 0.1297 0.0036  -0.0281 -0.0161 66  ASP A DB2  
1241 D DB3  . ASP A 67  ? 0.1224 0.1635 0.1294 0.0141  0.0029  0.0262  66  ASP A DB3  
1242 N N    . GLY A 68  ? 0.1667 0.1267 0.1625 0.0151  -0.0382 0.0223  67  GLY A N    
1243 C CA   . GLY A 68  ? 0.2667 0.1316 0.1696 0.0234  -0.0358 0.0335  67  GLY A CA   
1244 C C    . GLY A 68  ? 0.3076 0.1457 0.1536 0.0078  -0.0048 0.0476  67  GLY A C    
1245 O O    . GLY A 68  ? 0.4627 0.1758 0.2568 0.0603  0.0725  0.1142  67  GLY A O    
1246 D D    . GLY A 68  ? 0.1914 0.1541 0.1639 -0.0058 -0.0528 0.0207  67  GLY A D    
1247 D DA2  . GLY A 68  ? 0.3148 0.2111 0.2027 0.0202  -0.0765 0.0485  67  GLY A DA2  
1248 D DA3  . GLY A 68  ? 0.3052 0.1353 0.2108 0.0382  -0.0183 0.0223  67  GLY A DA3  
1249 N N    A ARG A 69  ? 0.2645 0.1371 0.1539 -0.0140 0.0053  0.0404  68  ARG A N    
1250 N N    B ARG A 69  ? 0.2451 0.1285 0.1478 -0.0317 -0.0123 0.0388  68  ARG A N    
1251 C CA   A ARG A 69  ? 0.2688 0.1476 0.1747 -0.0514 0.0151  0.0175  68  ARG A CA   
1252 C CA   B ARG A 69  ? 0.2663 0.1425 0.1644 -0.0553 0.0096  0.0255  68  ARG A CA   
1253 C C    A ARG A 69  ? 0.2418 0.1403 0.1565 -0.0485 0.0139  0.0310  68  ARG A C    
1254 C C    B ARG A 69  ? 0.2376 0.1458 0.1568 -0.0532 0.0035  0.0267  68  ARG A C    
1255 O O    A ARG A 69  ? 0.2619 0.1370 0.1622 -0.0545 0.0276  0.0412  68  ARG A O    
1256 O O    B ARG A 69  ? 0.2366 0.1471 0.1562 -0.0666 0.0049  0.0214  68  ARG A O    
1257 C CB   A ARG A 69  ? 0.2689 0.2021 0.1999 -0.0641 -0.0005 -0.0080 68  ARG A CB   
1258 C CB   B ARG A 69  ? 0.2665 0.1744 0.1886 -0.0840 0.0092  0.0083  68  ARG A CB   
1259 C CG   A ARG A 69  ? 0.3104 0.2125 0.2285 -0.0851 0.0021  -0.0272 68  ARG A CG   
1260 C CG   B ARG A 69  ? 0.3076 0.1882 0.2257 -0.0803 0.0017  -0.0151 68  ARG A CG   
1261 C CD   A ARG A 69  ? 0.3084 0.2488 0.2360 -0.0941 0.0010  -0.0397 68  ARG A CD   
1262 C CD   B ARG A 69  ? 0.3250 0.2232 0.2406 -0.0953 0.0009  -0.0408 68  ARG A CD   
1263 N NE   A ARG A 69  ? 0.2887 0.2640 0.2367 -0.0857 -0.0098 -0.0314 68  ARG A NE   
1264 N NE   B ARG A 69  ? 0.2885 0.2505 0.2286 -0.0983 -0.0096 -0.0368 68  ARG A NE   
1265 C CZ   A ARG A 69  ? 0.2740 0.2602 0.2533 -0.0949 -0.0023 -0.0226 68  ARG A CZ   
1266 C CZ   B ARG A 69  ? 0.2888 0.2628 0.2351 -0.0917 -0.0075 -0.0268 68  ARG A CZ   
1267 N NH1  A ARG A 69  ? 0.3126 0.2597 0.2683 -0.0805 0.0385  0.0197  68  ARG A NH1  
1268 N NH1  B ARG A 69  ? 0.3363 0.2677 0.2298 -0.0647 0.0108  -0.0236 68  ARG A NH1  
1269 N NH2  A ARG A 69  ? 0.3352 0.2814 0.2611 -0.0471 0.0236  -0.0091 68  ARG A NH2  
1270 N NH2  B ARG A 69  ? 0.3104 0.2744 0.2531 -0.0683 0.0176  -0.0132 68  ARG A NH2  
1271 D D    A ARG A 69  ? 0.2028 0.1929 0.1328 -0.0305 -0.0455 0.0646  68  ARG A D    
1272 D D    B ARG A 69  ? 0.2973 0.1184 0.1468 0.0016  0.0420  0.0315  68  ARG A D    
1273 D DA   A ARG A 69  ? 0.3340 0.1428 0.1914 -0.0507 0.0462  0.0125  68  ARG A DA   
1274 D DA   B ARG A 69  ? 0.3184 0.1255 0.1790 -0.0731 0.0086  0.0241  68  ARG A DA   
1275 D DB2  A ARG A 69  ? 0.2346 0.2119 0.2124 -0.0822 -0.0529 0.0106  68  ARG A DB2  
1276 D DB2  B ARG A 69  ? 0.2502 0.2015 0.1843 -0.0910 -0.0051 0.0186  68  ARG A DB2  
1277 D DB3  A ARG A 69  ? 0.2690 0.2551 0.2345 -0.0583 0.0071  -0.0037 68  ARG A DB3  
1278 D DB3  B ARG A 69  ? 0.2613 0.1937 0.2113 -0.0639 0.0073  0.0613  68  ARG A DB3  
1279 D DG2  A ARG A 69  ? 0.3948 0.2193 0.2315 -0.0660 0.0157  -0.0184 68  ARG A DG2  
1280 D DG2  B ARG A 69  ? 0.3452 0.2090 0.2492 -0.0212 0.0294  0.0101  68  ARG A DG2  
1281 D DG3  A ARG A 69  ? 0.3199 0.2840 0.1486 -0.0608 -0.0137 -0.0504 68  ARG A DG3  
1282 D DG3  B ARG A 69  ? 0.3113 0.1883 0.2438 -0.0758 0.0110  -0.0330 68  ARG A DG3  
1283 D DD2  A ARG A 69  ? 0.3059 0.2548 0.2825 -0.1133 0.0132  -0.0442 68  ARG A DD2  
1284 D DD2  B ARG A 69  ? 0.3256 0.2597 0.2165 -0.1180 -0.0098 -0.0468 68  ARG A DD2  
1285 D DD3  A ARG A 69  ? 0.4019 0.2563 0.1951 -0.0894 0.0010  -0.0390 68  ARG A DD3  
1286 D DD3  B ARG A 69  ? 0.4174 0.2435 0.2516 -0.0694 -0.0112 -0.0644 68  ARG A DD3  
1287 D DE   A ARG A 69  ? 0.3311 0.2802 0.3612 -0.0576 0.0854  0.0390  68  ARG A DE   
1288 D DE   B ARG A 69  ? 0.3151 0.3317 0.2472 -0.0621 0.0116  -0.0262 68  ARG A DE   
1289 D DH11 A ARG A 69  ? 0.3340 0.1659 0.4483 -0.0091 0.1048  0.1318  68  ARG A DH11 
1290 D DH11 B ARG A 69  ? 0.4688 0.3819 0.2508 0.0584  0.0645  0.0393  68  ARG A DH11 
1291 D DH12 A ARG A 69  ? 0.3362 0.2203 0.2200 -0.0765 0.1132  -0.0332 68  ARG A DH12 
1292 D DH12 B ARG A 69  ? 0.2840 0.3536 0.3229 -0.0290 0.0430  0.0646  68  ARG A DH12 
1293 D DH21 A ARG A 69  ? 0.1829 0.3931 0.2574 -0.0386 -0.0050 -0.0001 68  ARG A DH21 
1294 D DH21 B ARG A 69  ? 0.2484 0.3793 0.2108 -0.0492 -0.0327 0.0234  68  ARG A DH21 
1295 D DH22 A ARG A 69  ? 0.4720 0.3155 0.3676 0.0193  0.1492  0.0420  68  ARG A DH22 
1296 D DH22 B ARG A 69  ? 0.3516 0.3174 0.3056 -0.0270 0.0648  0.0290  68  ARG A DH22 
1297 N N    . THR A 70  ? 0.2093 0.1360 0.1242 -0.0358 -0.0032 0.0353  69  THR A N    
1298 C CA   . THR A 70  ? 0.1645 0.1400 0.1277 -0.0311 -0.0055 0.0323  69  THR A CA   
1299 C C    . THR A 70  ? 0.1633 0.1305 0.1210 0.0026  0.0060  0.0351  69  THR A C    
1300 O O    . THR A 70  ? 0.1646 0.1923 0.1195 0.0195  0.0073  0.0357  69  THR A O    
1301 C CB   . THR A 70  ? 0.1386 0.1302 0.1186 -0.0127 -0.0036 0.0313  69  THR A CB   
1302 O OG1  . THR A 70  ? 0.1501 0.1011 0.1252 0.0053  -0.0105 0.0251  69  THR A OG1  
1303 C CG2  . THR A 70  ? 0.1734 0.1311 0.1091 -0.0120 -0.0049 0.0265  69  THR A CG2  
1304 D D    . THR A 70  ? 0.2282 0.1391 0.2218 -0.0381 0.0337  -0.0043 69  THR A D    
1305 D DA   . THR A 70  ? 0.1640 0.1473 0.1526 -0.0437 -0.0012 0.0337  69  THR A DA   
1306 D DB   . THR A 70  ? 0.1387 0.1732 0.1430 -0.0166 -0.0118 0.0424  69  THR A DB   
1307 D DG1  . THR A 70  ? 0.1682 0.1174 0.1445 0.0110  -0.0157 0.0113  69  THR A DG1  
1308 D DG21 . THR A 70  ? 0.1819 0.1517 0.1616 -0.0049 0.0193  0.0142  69  THR A DG21 
1309 D DG22 . THR A 70  ? 0.1866 0.1327 0.1522 -0.0157 0.0041  0.0371  69  THR A DG22 
1310 D DG23 . THR A 70  ? 0.2637 0.1527 0.1305 -0.0371 -0.0322 0.0040  69  THR A DG23 
1311 N N    . PRO A 71  ? 0.1652 0.1466 0.1300 -0.0104 0.0207  0.0339  70  PRO A N    
1312 C CA   . PRO A 71  ? 0.2090 0.1549 0.1317 -0.0229 0.0188  0.0165  70  PRO A CA   
1313 C C    . PRO A 71  ? 0.2327 0.1676 0.1391 -0.0404 0.0126  0.0181  70  PRO A C    
1314 O O    . PRO A 71  ? 0.2868 0.1364 0.1869 -0.0249 -0.0049 0.0106  70  PRO A O    
1315 C CB   . PRO A 71  ? 0.2461 0.2214 0.1579 -0.0214 0.0608  0.0104  70  PRO A CB   
1316 C CG   . PRO A 71  ? 0.2089 0.2602 0.1997 -0.0182 0.0669  0.0044  70  PRO A CG   
1317 C CD   . PRO A 71  ? 0.1682 0.2066 0.1823 -0.0025 0.0235  0.0138  70  PRO A CD   
1318 D DA   . PRO A 71  ? 0.2221 0.1858 0.1309 -0.0197 0.0133  0.0539  70  PRO A DA   
1319 D DB2  . PRO A 71  ? 0.2963 0.2309 0.2498 -0.0161 0.1242  -0.0250 70  PRO A DB2  
1320 D DB3  . PRO A 71  ? 0.2500 0.3415 0.1828 -0.0234 0.0681  0.0636  70  PRO A DB3  
1321 D DG2  . PRO A 71  ? 0.2503 0.3641 0.2085 0.0365  0.0555  -0.0618 70  PRO A DG2  
1322 D DG3  . PRO A 71  ? 0.2434 0.2740 0.2317 -0.0566 0.0584  0.0342  70  PRO A DG3  
1323 D DD2  . PRO A 71  ? 0.1772 0.2550 0.3016 0.0233  0.0160  0.0799  70  PRO A DD2  
1324 D DD3  . PRO A 71  ? 0.1818 0.2921 0.1973 -0.0268 0.0176  -0.0218 70  PRO A DD3  
1325 N N    . GLY A 72  ? 0.2222 0.2051 0.1191 -0.0468 0.0261  0.0074  71  GLY A N    
1326 C CA   . GLY A 72  ? 0.2393 0.2284 0.1305 -0.0584 0.0235  -0.0157 71  GLY A CA   
1327 C C    . GLY A 72  ? 0.2137 0.2051 0.1279 -0.0473 0.0092  0.0107  71  GLY A C    
1328 O O    . GLY A 72  ? 0.2138 0.1972 0.1794 -0.0416 0.0379  -0.0213 71  GLY A O    
1329 D D    . GLY A 72  ? 0.2063 0.2666 0.2489 -0.0747 -0.0497 0.0884  71  GLY A D    
1330 D DA2  . GLY A 72  ? 0.3157 0.3543 0.1339 -0.1278 -0.0088 0.0226  71  GLY A DA2  
1331 D DA3  . GLY A 72  ? 0.2544 0.2128 0.2691 -0.0713 0.0868  -0.0358 71  GLY A DA3  
1332 N N    . SER A 73  ? 0.1822 0.1781 0.1372 -0.0446 0.0199  0.0236  72  SER A N    
1333 C CA   . SER A 73  ? 0.1665 0.1661 0.1197 -0.0392 0.0009  0.0288  72  SER A CA   
1334 C C    . SER A 73  ? 0.1541 0.1578 0.0991 -0.0183 -0.0007 0.0259  72  SER A C    
1335 O O    . SER A 73  ? 0.1988 0.1635 0.1997 -0.0364 -0.0382 0.0853  72  SER A O    
1336 C CB   . SER A 73  ? 0.2518 0.2024 0.1456 -0.0637 0.0064  -0.0109 72  SER A CB   
1337 O OG   . SER A 73  ? 0.2585 0.2402 0.1547 -0.0661 0.0167  -0.0450 72  SER A OG   
1338 D D    . SER A 73  ? 0.2492 0.1976 0.2136 -0.0786 0.1112  -0.0079 72  SER A D    
1339 D DA   . SER A 73  ? 0.1582 0.2038 0.1725 -0.0383 -0.0203 0.0654  72  SER A DA   
1340 D DB2  . SER A 73  ? 0.2527 0.2670 0.1763 -0.0683 0.0106  -0.0370 72  SER A DB2  
1341 D DB3  . SER A 73  ? 0.2940 0.1793 0.1977 -0.0268 0.0269  -0.0055 72  SER A DB3  
1342 D DG   . SER A 73  ? 0.4551 0.6614 0.1816 0.1717  0.0634  0.0598  72  SER A DG   
1343 N N    . ARG A 74  ? 0.1246 0.1454 0.0774 -0.0054 -0.0051 0.0158  73  ARG A N    
1344 C CA   . ARG A 74  ? 0.1241 0.1545 0.0816 -0.0064 -0.0113 0.0109  73  ARG A CA   
1345 C C    . ARG A 74  ? 0.1131 0.1407 0.0822 -0.0026 -0.0163 0.0135  73  ARG A C    
1346 O O    . ARG A 74  ? 0.1176 0.1994 0.1058 0.0060  -0.0280 -0.0119 73  ARG A O    
1347 C CB   . ARG A 74  ? 0.1281 0.1581 0.0909 -0.0120 -0.0160 0.0036  73  ARG A CB   
1348 C CG   . ARG A 74  ? 0.1532 0.1690 0.0943 -0.0186 -0.0077 -0.0065 73  ARG A CG   
1349 C CD   . ARG A 74  ? 0.1593 0.1646 0.1612 -0.0124 -0.0301 -0.0221 73  ARG A CD   
1350 N NE   . ARG A 74  ? 0.1731 0.2069 0.1826 0.0056  -0.0264 -0.0453 73  ARG A NE   
1351 C CZ   . ARG A 74  ? 0.1954 0.2300 0.2389 0.0275  -0.0452 -0.0815 73  ARG A CZ   
1352 N NH1  . ARG A 74  ? 0.2111 0.2164 0.3265 -0.0031 -0.0315 -0.1102 73  ARG A NH1  
1353 N NH2  . ARG A 74  ? 0.2483 0.2899 0.2464 0.0398  -0.0280 -0.1095 73  ARG A NH2  
1354 D D    . ARG A 74  ? 0.1260 0.1628 0.1114 -0.0153 -0.0223 0.0301  73  ARG A D    
1355 D DA   . ARG A 74  ? 0.1596 0.1684 0.0949 0.0078  -0.0200 0.0147  73  ARG A DA   
1356 D DB2  . ARG A 74  ? 0.1776 0.1443 0.0922 -0.0052 -0.0126 0.0095  73  ARG A DB2  
1357 D DB3  . ARG A 74  ? 0.1340 0.1940 0.1454 -0.0178 -0.0077 -0.0486 73  ARG A DB3  
1358 D DG2  . ARG A 74  ? 0.2654 0.2113 0.0978 0.0366  0.0045  0.0047  73  ARG A DG2  
1359 D DG3  . ARG A 74  ? 0.1581 0.2087 0.1665 -0.0473 0.0219  -0.0218 73  ARG A DG3  
1360 D DD2  . ARG A 74  ? 0.1988 0.1823 0.1956 -0.0045 -0.0105 0.0188  73  ARG A DD2  
1361 D DD3  . ARG A 74  ? 0.1570 0.1971 0.2408 -0.0166 -0.0229 -0.0309 73  ARG A DD3  
1362 D DE   . ARG A 74  ? 0.1761 0.2184 0.2038 0.0116  0.0077  -0.0347 73  ARG A DE   
1363 D DH11 . ARG A 74  ? 0.2528 0.2411 0.4293 0.0108  -0.0490 -0.1617 73  ARG A DH11 
1364 D DH12 . ARG A 74  ? 0.3694 0.1697 0.3667 -0.0253 0.0577  -0.0771 73  ARG A DH12 
1365 D DH21 . ARG A 74  ? 0.3542 0.3337 0.3437 -0.0036 0.0151  -0.1732 73  ARG A DH21 
1366 D DH22 . ARG A 74  ? 0.3637 0.3138 0.3392 0.0028  0.0959  -0.1366 73  ARG A DH22 
1367 N N    . ASN A 75  ? 0.1075 0.1343 0.0828 -0.0044 -0.0147 0.0157  74  ASN A N    
1368 C CA   . ASN A 75  ? 0.1187 0.1256 0.0857 -0.0171 -0.0094 0.0046  74  ASN A CA   
1369 C C    . ASN A 75  ? 0.0998 0.1172 0.0908 -0.0036 -0.0101 -0.0020 74  ASN A C    
1370 O O    . ASN A 75  ? 0.1009 0.1147 0.1350 -0.0010 -0.0118 0.0044  74  ASN A O    
1371 C CB   . ASN A 75  ? 0.1542 0.1171 0.1232 -0.0086 0.0101  0.0169  74  ASN A CB   
1372 C CG   . ASN A 75  ? 0.1218 0.1263 0.1372 -0.0184 0.0091  0.0006  74  ASN A CG   
1373 O OD1  . ASN A 75  ? 0.1466 0.1583 0.1104 -0.0091 -0.0008 -0.0129 74  ASN A OD1  
1374 N ND2  . ASN A 75  ? 0.1727 0.1352 0.1836 0.0016  0.0108  -0.0160 74  ASN A ND2  
1375 D D    . ASN A 75  ? 0.1081 0.1985 0.0881 -0.0012 -0.0169 0.0108  74  ASN A D    
1376 D DA   . ASN A 75  ? 0.1122 0.1333 0.0878 -0.0163 -0.0140 0.0082  74  ASN A DA   
1377 D DB2  . ASN A 75  ? 0.1868 0.1282 0.1598 -0.0329 0.0301  0.0066  74  ASN A DB2  
1378 D DB3  . ASN A 75  ? 0.1831 0.1474 0.1459 0.0233  -0.0019 0.0208  74  ASN A DB3  
1379 D DD21 . ASN A 75  ? 0.2243 0.1873 0.2065 0.0044  0.0459  -0.0319 74  ASN A DD21 
1380 D DD22 . ASN A 75  ? 0.2820 0.2165 0.2224 0.0876  0.0525  0.0382  74  ASN A DD22 
1381 N N    . LEU A 76  ? 0.0998 0.1213 0.0813 0.0009  -0.0107 0.0073  75  LEU A N    
1382 C CA   . LEU A 76  ? 0.1086 0.1171 0.0831 -0.0004 -0.0118 0.0093  75  LEU A CA   
1383 C C    . LEU A 76  ? 0.0931 0.1197 0.0843 -0.0046 -0.0140 -0.0003 75  LEU A C    
1384 O O    . LEU A 76  ? 0.1095 0.1633 0.0927 -0.0359 -0.0078 -0.0204 75  LEU A O    
1385 C CB   . LEU A 76  ? 0.1098 0.1261 0.0962 -0.0055 -0.0026 -0.0046 75  LEU A CB   
1386 C CG   . LEU A 76  ? 0.1179 0.1347 0.0950 -0.0150 -0.0057 -0.0125 75  LEU A CG   
1387 C CD1  . LEU A 76  ? 0.1674 0.1558 0.1285 0.0156  0.0078  -0.0272 75  LEU A CD1  
1388 C CD2  . LEU A 76  ? 0.1502 0.1850 0.1032 0.0042  -0.0236 -0.0144 75  LEU A CD2  
1390 D DA   . LEU A 76  ? 0.1247 0.1335 0.0954 -0.0014 -0.0274 0.0119  75  LEU A DA   
1391 D DB2  . LEU A 76  ? 0.1394 0.1367 0.1126 0.0203  -0.0147 -0.0112 75  LEU A DB2  
1392 D DB3  . LEU A 76  ? 0.1442 0.1484 0.1107 -0.0325 0.0045  -0.0118 75  LEU A DB3  
1393 D DG   . LEU A 76  ? 0.1445 0.1828 0.1023 -0.0482 0.0035  -0.0134 75  LEU A DG   
1394 D DD11 . LEU A 76  ? 0.2043 0.1490 0.1957 -0.0037 0.0142  -0.0283 75  LEU A DD11 
1395 D DD12 . LEU A 76  ? 0.2179 0.2161 0.1362 0.0016  0.0278  -0.0518 75  LEU A DD12 
1396 D DD13 . LEU A 76  ? 0.1938 0.1956 0.1821 0.0619  -0.0132 -0.0184 75  LEU A DD13 
1397 D DD21 . LEU A 76  ? 0.1679 0.2577 0.1654 -0.0390 -0.0644 0.0428  75  LEU A DD21 
1398 D DD22 . LEU A 76  ? 0.2327 0.1878 0.1142 0.0347  -0.0216 0.0037  75  LEU A DD22 
1399 D DD23 . LEU A 76  ? 0.2066 0.2161 0.0951 -0.0100 -0.0243 -0.0203 75  LEU A DD23 
1400 N N    . CYS A 77  ? 0.0867 0.1045 0.0873 -0.0007 -0.0144 -0.0014 76  CYS A N    
1401 C CA   . CYS A 77  ? 0.0991 0.1077 0.0878 -0.0021 -0.0050 0.0038  76  CYS A CA   
1402 C C    . CYS A 77  ? 0.1095 0.1147 0.0786 0.0076  -0.0072 -0.0016 76  CYS A C    
1403 O O    . CYS A 77  ? 0.1306 0.1506 0.0855 0.0245  0.0077  0.0069  76  CYS A O    
1404 C CB   . CYS A 77  ? 0.1220 0.0934 0.0793 -0.0033 -0.0129 -0.0010 76  CYS A CB   
1405 S SG   . CYS A 77  ? 0.1035 0.1080 0.0838 0.0081  0.0004  0.0006  76  CYS A SG   
1407 D D    B CYS A 77  ? 0.0875 0.0850 0.0838 0.0023  -0.0116 -0.0013 76  CYS A D    
1408 D DA   . CYS A 77  ? 0.1118 0.1184 0.1122 -0.0142 -0.0018 -0.0042 76  CYS A DA   
1409 D DB2  . CYS A 77  ? 0.1281 0.1127 0.1068 -0.0137 -0.0318 0.0108  76  CYS A DB2  
1410 D DB3  . CYS A 77  ? 0.1488 0.1387 0.0851 0.0175  -0.0067 -0.0017 76  CYS A DB3  
1411 N N    A ASN A 78  ? 0.1086 0.1201 0.0823 0.0201  -0.0119 0.0036  77  ASN A N    
1412 N N    B ASN A 78  ? 0.0774 0.1085 0.0955 -0.0039 -0.0056 -0.0017 77  ASN A N    
1413 C CA   A ASN A 78  ? 0.0714 0.1121 0.1044 0.0009  0.0018  0.0073  77  ASN A CA   
1414 C CA   B ASN A 78  ? 0.0704 0.1151 0.0975 -0.0008 0.0036  0.0085  77  ASN A CA   
1415 C C    A ASN A 78  ? 0.0874 0.1030 0.1223 0.0066  -0.0108 -0.0008 77  ASN A C    
1416 C C    B ASN A 78  ? 0.0768 0.1086 0.1005 0.0095  0.0056  0.0024  77  ASN A C    
1417 O O    A ASN A 78  ? 0.0871 0.1047 0.1131 0.0112  -0.0161 0.0034  77  ASN A O    
1418 O O    B ASN A 78  ? 0.1122 0.0904 0.1211 0.0254  0.0345  0.0158  77  ASN A O    
1419 C CB   A ASN A 78  ? 0.0721 0.1369 0.1041 -0.0105 0.0052  0.0119  77  ASN A CB   
1420 C CB   B ASN A 78  ? 0.0708 0.1500 0.1174 -0.0036 -0.0021 0.0055  77  ASN A CB   
1421 C CG   A ASN A 78  ? 0.0819 0.1613 0.1237 0.0097  -0.0115 0.0203  77  ASN A CG   
1422 C CG   B ASN A 78  ? 0.0698 0.1592 0.1271 0.0023  -0.0073 0.0109  77  ASN A CG   
1423 O OD1  A ASN A 78  ? 0.0818 0.1493 0.1598 0.0058  -0.0122 0.0293  77  ASN A OD1  
1424 O OD1  B ASN A 78  ? 0.0911 0.1508 0.1098 -0.0085 -0.0240 -0.0053 77  ASN A OD1  
1425 N ND2  A ASN A 78  ? 0.0887 0.1770 0.1482 0.0130  0.0010  -0.0013 77  ASN A ND2  
1426 N ND2  B ASN A 78  ? 0.0669 0.1849 0.1408 0.0032  -0.0156 -0.0129 77  ASN A ND2  
1427 D D    A ASN A 78  ? 0.1148 0.0956 0.0892 0.0017  -0.0063 -0.0109 77  ASN A D    
1428 D D    B ASN A 78  ? 0.1485 0.1954 0.1412 0.0845  0.0507  0.0586  77  ASN A D    
1429 D DA   A ASN A 78  ? 0.0931 0.1204 0.1257 -0.0166 -0.0039 0.0253  77  ASN A DA   
1430 D DA   B ASN A 78  ? 0.0747 0.1352 0.1049 -0.0056 0.0003  0.0211  77  ASN A DA   
1431 D DB2  A ASN A 78  ? 0.1012 0.1780 0.1595 -0.0219 -0.0083 -0.0291 77  ASN A DB2  
1432 D DB2  B ASN A 78  ? 0.0720 0.1755 0.1232 -0.0109 0.0052  -0.0078 77  ASN A DB2  
1433 D DB3  A ASN A 78  ? 0.1164 0.1522 0.1347 0.0049  0.0413  0.0310  77  ASN A DB3  
1434 D DB3  B ASN A 78  ? 0.0692 0.1574 0.1186 -0.0181 -0.0088 0.0049  77  ASN A DB3  
1435 D DD21 A ASN A 78  ? 0.1128 0.1624 0.1678 0.0144  -0.0077 -0.0259 77  ASN A DD21 
1436 D DD21 B ASN A 78  ? 0.0856 0.1816 0.1487 0.0063  -0.0477 -0.0348 77  ASN A DD21 
1437 D DD22 A ASN A 78  ? 0.1077 0.1540 0.1521 -0.0068 0.0100  -0.0359 77  ASN A DD22 
1438 D DD22 B ASN A 78  ? 0.0733 0.1801 0.1418 0.0133  0.0450  -0.0327 77  ASN A DD22 
1439 N N    . ILE A 79  ? 0.0870 0.1081 0.1165 0.0035  -0.0086 -0.0109 78  ILE A N    
1440 C CA   . ILE A 79  ? 0.0897 0.1351 0.1158 0.0037  -0.0016 -0.0166 78  ILE A CA   
1441 C C    . ILE A 79  ? 0.0808 0.1314 0.1256 0.0097  -0.0178 -0.0203 78  ILE A C    
1442 O O    . ILE A 79  ? 0.0949 0.1360 0.1493 -0.0007 0.0021  -0.0290 78  ILE A O    
1443 C CB   . ILE A 79  ? 0.1515 0.1516 0.1112 0.0092  -0.0129 -0.0148 78  ILE A CB   
1444 C CG1  . ILE A 79  ? 0.1725 0.1338 0.1463 0.0101  -0.0033 0.0000  78  ILE A CG1  
1445 C CG2  . ILE A 79  ? 0.1973 0.1600 0.1379 0.0070  0.0278  0.0070  78  ILE A CG2  
1446 C CD1  . ILE A 79  ? 0.2165 0.1556 0.1865 0.0202  -0.0307 0.0189  78  ILE A CD1  
1448 D DA   . ILE A 79  ? 0.0936 0.1481 0.1434 0.0054  -0.0063 -0.0367 78  ILE A DA   
1449 D DB   . ILE A 79  ? 0.2051 0.1603 0.1397 0.0169  -0.0426 -0.0186 78  ILE A DB   
1450 D DG12 . ILE A 79  ? 0.3080 0.1339 0.2557 0.0324  -0.1066 -0.0381 78  ILE A DG12 
1451 D DG13 . ILE A 79  ? 0.2261 0.1990 0.2513 0.0744  0.0854  0.0638  78  ILE A DG13 
1452 D DG21 . ILE A 79  ? 0.2086 0.2603 0.1844 -0.0615 0.0038  0.0010  78  ILE A DG21 
1453 D DG22 . ILE A 79  ? 0.2874 0.2122 0.1679 -0.0057 0.0141  0.0489  78  ILE A DG22 
1454 D DG23 . ILE A 79  ? 0.2617 0.1887 0.2579 0.0448  0.1178  0.0338  78  ILE A DG23 
1455 D DD11 . ILE A 79  ? 0.2467 0.3118 0.2530 0.0540  0.0008  0.1335  78  ILE A DD11 
1456 D DD12 . ILE A 79  ? 0.3065 0.1944 0.2168 0.0753  -0.0087 0.0374  78  ILE A DD12 
1457 D DD13 . ILE A 79  ? 0.3651 0.2382 0.2498 -0.0068 -0.1296 -0.0098 78  ILE A DD13 
1458 N N    . PRO A 80  ? 0.0959 0.1190 0.1276 0.0083  -0.0128 -0.0121 79  PRO A N    
1459 C CA   . PRO A 80  ? 0.0943 0.1010 0.1407 0.0093  -0.0129 -0.0021 79  PRO A CA   
1460 C C    . PRO A 80  ? 0.0870 0.1067 0.1194 0.0088  -0.0090 -0.0087 79  PRO A C    
1461 O O    . PRO A 80  ? 0.0901 0.1211 0.1271 0.0046  -0.0028 -0.0021 79  PRO A O    
1462 C CB   . PRO A 80  ? 0.1092 0.1027 0.1978 0.0087  -0.0111 -0.0188 79  PRO A CB   
1463 C CG   . PRO A 80  ? 0.1368 0.1319 0.1810 0.0093  0.0025  -0.0438 79  PRO A CG   
1464 C CD   . PRO A 80  ? 0.1007 0.1209 0.1690 0.0113  0.0082  -0.0271 79  PRO A CD   
1465 D DA   . PRO A 80  ? 0.1048 0.1290 0.1478 -0.0012 -0.0035 0.0099  79  PRO A DA   
1466 D DB2  . PRO A 80  ? 0.1267 0.1638 0.2237 0.0044  -0.0171 -0.0677 79  PRO A DB2  
1467 D DB3  . PRO A 80  ? 0.1839 0.1036 0.2429 0.0091  -0.0056 0.0080  79  PRO A DB3  
1468 D DG2  . PRO A 80  ? 0.1974 0.1547 0.1870 -0.0107 -0.0226 -0.0264 79  PRO A DG2  
1469 D DG3  . PRO A 80  ? 0.1546 0.1331 0.2522 0.0075  0.0337  -0.0479 79  PRO A DG3  
1470 D DD2  . PRO A 80  ? 0.1438 0.1436 0.1883 -0.0080 0.0287  -0.0280 79  PRO A DD2  
1471 D DD3  . PRO A 80  ? 0.1220 0.1713 0.2061 0.0324  -0.0058 -0.0190 79  PRO A DD3  
1472 N N    . CYS A 81  ? 0.0925 0.1058 0.1002 0.0100  -0.0073 0.0018  80  CYS A N    
1473 C CA   . CYS A 81  ? 0.0830 0.1031 0.1173 0.0070  -0.0107 0.0068  80  CYS A CA   
1474 C C    . CYS A 81  ? 0.1115 0.1131 0.1145 0.0071  -0.0149 0.0109  80  CYS A C    
1475 O O    . CYS A 81  ? 0.1299 0.1217 0.1248 0.0106  -0.0125 0.0213  80  CYS A O    
1476 C CB   . CYS A 81  ? 0.0884 0.1126 0.1185 0.0045  -0.0096 0.0148  80  CYS A CB   
1477 S SG   . CYS A 81  ? 0.0977 0.1233 0.1219 0.0061  -0.0065 0.0024  80  CYS A SG   
1479 D D    B CYS A 81  ? 0.1050 0.0947 0.0696 -0.0265 -0.0274 -0.0242 80  CYS A D    
1480 D DA   . CYS A 81  ? 0.1036 0.1127 0.1295 -0.0073 0.0019  0.0035  80  CYS A DA   
1481 D DB2  . CYS A 81  ? 0.1213 0.1144 0.1412 -0.0081 0.0079  -0.0022 80  CYS A DB2  
1482 D DB3  . CYS A 81  ? 0.0865 0.1435 0.1272 0.0250  0.0000  0.0202  80  CYS A DB3  
1483 N N    . SER A 82  ? 0.0986 0.1120 0.1102 -0.0047 -0.0170 0.0105  81  SER A N    
1484 C CA   . SER A 82  ? 0.1314 0.1290 0.1155 -0.0219 -0.0291 0.0059  81  SER A CA   
1485 C C    . SER A 82  ? 0.1336 0.1016 0.1094 0.0048  -0.0099 -0.0091 81  SER A C    
1486 O O    . SER A 82  ? 0.1629 0.1278 0.1125 -0.0053 -0.0161 -0.0009 81  SER A O    
1487 C CB   . SER A 82  ? 0.1980 0.1214 0.1319 -0.0489 -0.0280 -0.0075 81  SER A CB   
1488 O OG   . SER A 82  ? 0.2119 0.1494 0.1675 0.0272  -0.0053 -0.0257 81  SER A OG   
1489 D D    . SER A 82  ? 0.1396 0.1118 0.1139 -0.0023 -0.0147 0.0115  81  SER A D    
1490 D DA   . SER A 82  ? 0.1261 0.2170 0.1371 -0.0264 -0.0370 0.0166  81  SER A DA   
1491 D DB2  . SER A 82  ? 0.3003 0.1915 0.1545 -0.0889 -0.0466 -0.0430 81  SER A DB2  
1492 D DB3  . SER A 82  ? 0.2011 0.1573 0.1865 -0.0536 -0.0177 0.0220  81  SER A DB3  
1493 D DG   . SER A 82  ? 0.2299 0.3218 0.3741 -0.0091 0.0657  -0.1702 81  SER A DG   
1494 N N    . ALA A 83  ? 0.1186 0.1113 0.1128 0.0119  -0.0051 0.0143  82  ALA A N    
1495 C CA   . ALA A 83  ? 0.1255 0.1060 0.1244 0.0133  0.0101  0.0036  82  ALA A CA   
1496 C C    . ALA A 83  ? 0.1070 0.1022 0.1149 0.0003  0.0027  0.0042  82  ALA A C    
1497 O O    . ALA A 83  ? 0.1851 0.1243 0.1486 0.0389  0.0594  0.0299  82  ALA A O    
1498 C CB   . ALA A 83  ? 0.1137 0.1560 0.1501 0.0137  0.0037  0.0282  82  ALA A CB   
1500 D D    B ALA A 83  ? 0.1091 0.1384 0.1169 -0.0044 -0.0052 0.0175  82  ALA A D    
1501 D DA   . ALA A 83  ? 0.1758 0.1194 0.1401 0.0181  0.0318  -0.0055 82  ALA A DA   
1502 D DB1  . ALA A 83  ? 0.1287 0.2035 0.1618 -0.0146 -0.0081 -0.0089 82  ALA A DB1  
1503 D DB2  . ALA A 83  ? 0.1297 0.2032 0.1807 0.0030  0.0130  0.0517  82  ALA A DB2  
1504 D DB3  . ALA A 83  ? 0.1479 0.1619 0.2247 0.0130  -0.0383 0.0394  82  ALA A DB3  
1505 N N    . LEU A 84  ? 0.1119 0.1065 0.1108 0.0084  0.0016  0.0124  83  LEU A N    
1506 C CA   . LEU A 84  ? 0.1120 0.1100 0.1202 0.0067  -0.0080 0.0161  83  LEU A CA   
1507 C C    . LEU A 84  ? 0.1294 0.1037 0.1348 0.0089  -0.0189 0.0121  83  LEU A C    
1508 O O    . LEU A 84  ? 0.1863 0.1241 0.1362 0.0392  -0.0452 0.0042  83  LEU A O    
1509 C CB   . LEU A 84  ? 0.1207 0.1135 0.1340 0.0143  -0.0033 0.0064  83  LEU A CB   
1510 C CG   . LEU A 84  ? 0.1593 0.1279 0.1375 0.0022  -0.0196 0.0050  83  LEU A CG   
1511 C CD1  . LEU A 84  ? 0.2142 0.1712 0.1249 0.0418  -0.0170 0.0082  83  LEU A CD1  
1512 C CD2  . LEU A 84  ? 0.1954 0.1728 0.1827 -0.0482 -0.0208 0.0075  83  LEU A CD2  
1514 D DA   . LEU A 84  ? 0.1181 0.1229 0.1405 0.0089  -0.0024 0.0247  83  LEU A DA   
1515 D DB2  . LEU A 84  ? 0.1216 0.1389 0.1832 0.0146  0.0237  0.0050  83  LEU A DB2  
1516 D DB3  . LEU A 84  ? 0.1908 0.1380 0.1579 0.0502  -0.0077 0.0132  83  LEU A DB3  
1517 D DG   . LEU A 84  ? 0.1719 0.1605 0.1536 0.0260  -0.0252 0.0177  83  LEU A DG   
1518 D DD11 . LEU A 84  ? 0.3296 0.2048 0.1813 0.1104  -0.0086 -0.0055 83  LEU A DD11 
1519 D DD12 . LEU A 84  ? 0.2834 0.2387 0.1274 -0.0093 -0.0336 0.0041  83  LEU A DD12 
1520 D DD13 . LEU A 84  ? 0.2555 0.2486 0.1598 -0.0076 0.0086  0.0175  83  LEU A DD13 
1521 D DD21 . LEU A 84  ? 0.2691 0.1745 0.2450 -0.0335 -0.0296 0.0308  83  LEU A DD21 
1522 D DD22 . LEU A 84  ? 0.1895 0.2519 0.2321 -0.0846 0.0125  -0.0335 83  LEU A DD22 
1523 D DD23 . LEU A 84  ? 0.2445 0.2456 0.2106 -0.0946 -0.0504 0.0105  83  LEU A DD23 
1524 N N    . LEU A 85  ? 0.1259 0.1137 0.1304 0.0060  -0.0094 -0.0010 84  LEU A N    
1525 C CA   . LEU A 85  ? 0.1407 0.1310 0.1148 0.0063  -0.0169 0.0082  84  LEU A CA   
1526 C C    . LEU A 85  ? 0.1955 0.1640 0.1335 -0.0152 0.0139  -0.0218 84  LEU A C    
1527 O O    . LEU A 85  ? 0.2523 0.2784 0.1449 -0.0653 0.0057  -0.0519 84  LEU A O    
1528 C CB   . LEU A 85  ? 0.1391 0.1403 0.1378 -0.0085 -0.0098 -0.0027 84  LEU A CB   
1529 C CG   . LEU A 85  ? 0.1486 0.1382 0.1291 -0.0040 -0.0112 0.0138  84  LEU A CG   
1530 C CD1  . LEU A 85  ? 0.2018 0.1542 0.1509 -0.0323 0.0193  0.0011  84  LEU A CD1  
1531 C CD2  . LEU A 85  ? 0.2198 0.1834 0.1414 0.0554  0.0156  0.0208  84  LEU A CD2  
1533 D D    B LEU A 85  ? 0.0887 0.0924 0.0942 -0.0222 0.0080  0.0017  84  LEU A D    
1534 D DA   . LEU A 85  ? 0.1662 0.1385 0.1285 0.0170  -0.0278 0.0005  84  LEU A DA   
1535 D DB2  . LEU A 85  ? 0.1762 0.1351 0.1506 0.0009  -0.0028 -0.0050 84  LEU A DB2  
1536 D DB3  . LEU A 85  ? 0.1665 0.1761 0.1427 -0.0373 -0.0161 -0.0054 84  LEU A DB3  
1537 D DG   . LEU A 85  ? 0.1723 0.1750 0.1302 -0.0221 -0.0093 -0.0043 84  LEU A DG   
1538 D DD11 . LEU A 85  ? 0.2597 0.2453 0.1675 -0.1132 0.0150  -0.0173 84  LEU A DD11 
1539 D DD12 . LEU A 85  ? 0.2353 0.2414 0.1545 -0.0316 0.0360  0.0098  84  LEU A DD12 
1540 D DD13 . LEU A 85  ? 0.2485 0.1800 0.3046 0.0000  0.0717  0.0661  84  LEU A DD13 
1541 D DD21 . LEU A 85  ? 0.2345 0.3080 0.1634 0.0803  -0.0210 0.0385  84  LEU A DD21 
1542 D DD22 . LEU A 85  ? 0.2383 0.1774 0.2901 0.0750  0.0743  0.0528  84  LEU A DD22 
1543 D DD23 . LEU A 85  ? 0.2443 0.2162 0.1720 0.0311  0.0416  -0.0101 84  LEU A DD23 
1544 N N    . SER A 86  ? 0.1969 0.1886 0.1691 -0.0155 0.0291  -0.0356 85  SER A N    
1545 C CA   . SER A 86  ? 0.2060 0.1896 0.1848 0.0136  0.0495  -0.0258 85  SER A CA   
1546 C C    . SER A 86  ? 0.1580 0.1808 0.1712 -0.0050 0.0237  -0.0431 85  SER A C    
1547 O O    . SER A 86  ? 0.1677 0.1931 0.1752 0.0213  0.0153  -0.0425 85  SER A O    
1548 C CB   . SER A 86  ? 0.2042 0.2033 0.2120 0.0353  0.0355  0.0189  85  SER A CB   
1549 O OG   . SER A 86  ? 0.1816 0.1891 0.2290 -0.0054 0.0396  -0.0050 85  SER A OG   
1550 D D    . SER A 86  ? 0.2172 0.1978 0.1840 -0.0080 -0.0045 -0.0276 85  SER A D    
1551 D DA   . SER A 86  ? 0.2613 0.1881 0.2052 0.0099  0.0320  -0.0269 85  SER A DA   
1552 D DB2  . SER A 86  ? 0.3105 0.3181 0.2517 0.0820  0.0425  0.0869  85  SER A DB2  
1553 D DB3  . SER A 86  ? 0.2236 0.2697 0.2073 0.0075  0.0166  -0.0328 85  SER A DB3  
1554 D DG   . SER A 86  ? 0.6699 0.1991 0.4466 0.0281  0.2960  -0.0146 85  SER A DG   
1555 N N    . SER A 87  ? 0.2050 0.1935 0.1749 -0.0083 0.0069  -0.0572 86  SER A N    
1556 C CA   . SER A 87  ? 0.1963 0.2459 0.1674 0.0012  -0.0270 -0.0444 86  SER A CA   
1557 C C    . SER A 87  ? 0.1875 0.2028 0.1366 0.0263  -0.0239 -0.0179 86  SER A C    
1558 O O    . SER A 87  ? 0.2146 0.2679 0.1748 0.0571  0.0240  0.0570  86  SER A O    
1559 C CB   . SER A 87  ? 0.2677 0.3013 0.1772 -0.0634 -0.0148 -0.0633 86  SER A CB   
1560 O OG   . SER A 87  ? 0.2896 0.2810 0.1688 -0.0703 0.0243  -0.0853 86  SER A OG   
1561 D D    . SER A 87  ? 0.3094 0.2083 0.2169 0.0339  -0.0049 -0.0752 86  SER A D    
1562 D DA   . SER A 87  ? 0.2088 0.2886 0.2411 0.0306  -0.0182 -0.0295 86  SER A DA   
1563 D DB2  . SER A 87  ? 0.3168 0.3650 0.1533 -0.0292 0.0000  -0.0481 86  SER A DB2  
1564 D DB3  . SER A 87  ? 0.2787 0.3622 0.2927 -0.0928 -0.0323 -0.0914 86  SER A DB3  
1565 D DG   . SER A 87  ? 0.2844 0.3254 0.5517 -0.0663 -0.0260 -0.0974 86  SER A DG   
1566 N N    A ASP A 88  ? 0.1751 0.1968 0.1294 0.0327  -0.0087 -0.0305 87  ASP A N    
1567 N N    B ASP A 88  ? 0.1773 0.2013 0.1170 0.0315  -0.0049 -0.0272 87  ASP A N    
1568 C CA   A ASP A 88  ? 0.1690 0.2238 0.1255 0.0278  0.0079  -0.0416 87  ASP A CA   
1569 C CA   B ASP A 88  ? 0.1738 0.2178 0.1286 0.0257  0.0095  -0.0389 87  ASP A CA   
1570 C C    A ASP A 88  ? 0.1669 0.2132 0.1150 0.0184  0.0021  -0.0300 87  ASP A C    
1571 C C    B ASP A 88  ? 0.1632 0.2140 0.1223 0.0185  0.0015  -0.0338 87  ASP A C    
1572 O O    A ASP A 88  ? 0.1289 0.2080 0.1198 0.0066  -0.0045 -0.0258 87  ASP A O    
1573 O O    B ASP A 88  ? 0.1677 0.2096 0.1169 -0.0243 -0.0123 -0.0487 87  ASP A O    
1574 C CB   A ASP A 88  ? 0.1849 0.2403 0.1629 0.0476  0.0071  -0.0417 87  ASP A CB   
1575 C CB   B ASP A 88  ? 0.1793 0.2218 0.1642 0.0304  0.0270  -0.0299 87  ASP A CB   
1576 C CG   A ASP A 88  ? 0.1730 0.2367 0.1957 0.0502  0.0322  -0.0170 87  ASP A CG   
1577 C CG   B ASP A 88  ? 0.1802 0.2333 0.1715 0.0553  0.0311  -0.0282 87  ASP A CG   
1578 O OD1  A ASP A 88  ? 0.2740 0.3496 0.2867 -0.0050 0.1278  -0.0755 87  ASP A OD1  
1579 O OD1  B ASP A 88  ? 0.2227 0.2377 0.1433 0.0418  0.0184  -0.0265 87  ASP A OD1  
1580 O OD2  A ASP A 88  ? 0.1592 0.2689 0.2344 0.0065  0.0366  -0.0508 87  ASP A OD2  
1581 O OD2  B ASP A 88  ? 0.2092 0.2072 0.1881 0.0733  0.0068  -0.0378 87  ASP A OD2  
1582 D D    A ASP A 88  ? 0.1685 0.2046 0.1076 0.0411  -0.0019 -0.0324 87  ASP A D    
1583 D D    B ASP A 88  ? 0.1796 0.2097 0.0975 0.0399  0.0332  -0.0102 87  ASP A D    
1584 D DA   A ASP A 88  ? 0.1953 0.2089 0.1287 0.0252  0.0179  -0.0469 87  ASP A DA   
1585 D DA   B ASP A 88  ? 0.1882 0.1799 0.1216 0.0220  0.0032  -0.0629 87  ASP A DA   
1586 D DB2  A ASP A 88  ? 0.2545 0.2716 0.1887 0.0875  -0.0058 -0.0723 87  ASP A DB2  
1587 D DB2  B ASP A 88  ? 0.1918 0.2275 0.1715 0.0186  0.0075  -0.0296 87  ASP A DB2  
1588 D DB3  A ASP A 88  ? 0.1715 0.2347 0.1941 0.0321  -0.0030 -0.0269 87  ASP A DB3  
1589 D DB3  B ASP A 88  ? 0.1517 0.2323 0.1742 0.0248  0.0300  -0.0400 87  ASP A DB3  
1590 N N    . ILE A 89  ? 0.1483 0.2143 0.1027 0.0145  0.0045  -0.0215 88  ILE A N    
1591 C CA   . ILE A 89  ? 0.1345 0.2182 0.0993 0.0052  0.0015  -0.0263 88  ILE A CA   
1592 C C    . ILE A 89  ? 0.1231 0.2068 0.0971 -0.0128 0.0121  -0.0145 88  ILE A C    
1593 O O    . ILE A 89  ? 0.1431 0.2102 0.1174 0.0177  -0.0179 -0.0307 88  ILE A O    
1594 C CB   . ILE A 89  ? 0.1765 0.2318 0.1201 0.0399  -0.0064 -0.0277 88  ILE A CB   
1595 C CG1  . ILE A 89  ? 0.2228 0.2428 0.1285 0.0303  -0.0039 0.0199  88  ILE A CG1  
1596 C CG2  . ILE A 89  ? 0.1992 0.3107 0.1617 0.0587  -0.0397 -0.0269 88  ILE A CG2  
1597 C CD1  . ILE A 89  ? 0.3523 0.2504 0.1656 0.0568  0.0137  0.0380  88  ILE A CD1  
1598 D D    . ILE A 89  ? 0.2022 0.2522 0.1114 0.0284  0.0333  -0.0080 88  ILE A D    
1599 D DA   . ILE A 89  ? 0.1427 0.2378 0.1204 -0.0195 0.0218  -0.0561 88  ILE A DA   
1600 D DB   . ILE A 89  ? 0.1544 0.2445 0.1470 0.0316  0.0142  -0.0444 88  ILE A DB   
1601 D DG12 . ILE A 89  ? 0.2746 0.2871 0.1582 -0.0259 0.0324  -0.0168 88  ILE A DG12 
1602 D DG13 . ILE A 89  ? 0.2247 0.2525 0.1845 -0.0104 -0.0249 0.0389  88  ILE A DG13 
1603 D DG21 . ILE A 89  ? 0.2646 0.3926 0.1585 0.0661  -0.0610 -0.0562 88  ILE A DG21 
1604 D DG22 . ILE A 89  ? 0.2262 0.3323 0.2343 0.0762  -0.0548 -0.0003 88  ILE A DG22 
1605 D DG23 . ILE A 89  ? 0.1887 0.3328 0.2097 0.0413  -0.0444 -0.0175 88  ILE A DG23 
1606 D DD11 . ILE A 89  ? 0.4847 0.2443 0.1804 0.0876  0.0395  0.0363  88  ILE A DD11 
1607 D DD12 . ILE A 89  ? 0.3697 0.2897 0.2294 0.1154  -0.0140 0.0385  88  ILE A DD12 
1608 D DD13 . ILE A 89  ? 0.3868 0.2802 0.2512 0.0476  0.0357  0.0908  88  ILE A DD13 
1609 N N    . THR A 90  ? 0.1173 0.2632 0.1233 -0.0013 0.0107  -0.0480 89  THR A N    
1610 C CA   . THR A 90  ? 0.1202 0.3028 0.1337 -0.0025 0.0026  -0.0517 89  THR A CA   
1611 C C    . THR A 90  ? 0.1131 0.1920 0.1328 0.0291  -0.0113 -0.0276 89  THR A C    
1612 O O    . THR A 90  ? 0.1127 0.1786 0.1223 0.0074  0.0061  -0.0113 89  THR A O    
1613 C CB   . THR A 90  ? 0.1454 0.4072 0.1762 0.0597  -0.0097 -0.0966 89  THR A CB   
1614 O OG1  . THR A 90  ? 0.1881 0.4580 0.1850 0.0765  0.0143  -0.1034 89  THR A OG1  
1615 C CG2  . THR A 90  ? 0.1341 0.5332 0.2074 0.0886  -0.0085 -0.1373 89  THR A CG2  
1616 D D    . THR A 90  ? 0.1361 0.2924 0.1573 -0.0066 -0.0028 -0.0800 89  THR A D    
1617 D DA   . THR A 90  ? 0.1411 0.3355 0.1214 -0.0355 0.0025  -0.0173 89  THR A DA   
1618 D DB   . THR A 90  ? 0.1819 0.3754 0.2486 0.0810  0.0056  -0.0920 89  THR A DB   
1619 D DG1  . THR A 90  ? 0.2252 0.4444 0.1737 0.0855  -0.0199 -0.0847 89  THR A DG1  
1620 D DG21 . THR A 90  ? 0.2035 0.5739 0.3430 0.0194  -0.0473 -0.1972 89  THR A DG21 
1621 D DG22 . THR A 90  ? 0.1684 0.6131 0.2803 0.1424  -0.0192 -0.1521 89  THR A DG22 
1622 D DG23 . THR A 90  ? 0.2305 0.7056 0.1870 0.1397  -0.0330 -0.1269 89  THR A DG23 
1623 N N    . ALA A 91  ? 0.1263 0.1663 0.1433 0.0318  -0.0196 -0.0484 90  ALA A N    
1624 C CA   . ALA A 91  ? 0.1227 0.1361 0.1446 0.0154  -0.0273 -0.0303 90  ALA A CA   
1625 C C    . ALA A 91  ? 0.1210 0.1239 0.1016 0.0122  -0.0190 -0.0012 90  ALA A C    
1626 O O    . ALA A 91  ? 0.1468 0.1333 0.0978 0.0240  -0.0252 -0.0008 90  ALA A O    
1627 C CB   . ALA A 91  ? 0.1744 0.1284 0.1864 0.0047  -0.0142 -0.0402 90  ALA A CB   
1628 D D    . ALA A 91  ? 0.1906 0.1846 0.1759 0.0169  -0.0308 -0.0679 90  ALA A D    
1629 D DA   . ALA A 91  ? 0.1218 0.1657 0.1585 0.0220  -0.0304 -0.0288 90  ALA A DA   
1630 D DB1  . ALA A 91  ? 0.1844 0.1445 0.2368 -0.0157 -0.0332 -0.0264 90  ALA A DB1  
1631 D DB2  . ALA A 91  ? 0.2601 0.1227 0.1906 0.0286  -0.0001 -0.0212 90  ALA A DB2  
1632 D DB3  . ALA A 91  ? 0.2074 0.1541 0.2196 0.0350  0.0057  -0.0272 90  ALA A DB3  
1633 N N    . SER A 92  ? 0.1075 0.1324 0.1001 0.0062  -0.0142 -0.0095 91  SER A N    
1634 C CA   . SER A 92  ? 0.1090 0.1280 0.0870 0.0083  -0.0046 -0.0050 91  SER A CA   
1635 C C    . SER A 92  ? 0.1106 0.1280 0.0857 0.0112  -0.0066 -0.0015 91  SER A C    
1636 O O    . SER A 92  ? 0.1570 0.1263 0.1014 -0.0090 0.0154  -0.0057 91  SER A O    
1637 C CB   . SER A 92  ? 0.1060 0.1454 0.1132 0.0073  -0.0134 0.0006  91  SER A CB   
1638 O OG   . SER A 92  ? 0.1127 0.1463 0.1451 0.0001  0.0064  -0.0231 91  SER A OG   
1639 D D    . SER A 92  ? 0.1192 0.2104 0.1191 0.0297  -0.0248 -0.0470 91  SER A D    
1640 D DA   . SER A 92  ? 0.1353 0.1444 0.0969 -0.0136 -0.0016 0.0004  91  SER A DA   
1641 D DB2  . SER A 92  ? 0.1140 0.2008 0.1069 -0.0095 -0.0226 0.0005  91  SER A DB2  
1642 D DB3  . SER A 92  ? 0.1378 0.1589 0.1756 0.0299  -0.0175 -0.0109 91  SER A DB3  
1643 D DG   . SER A 92  ? 0.1478 0.1657 0.1881 0.0156  -0.0159 -0.0578 91  SER A DG   
1644 N N    . VAL A 93  ? 0.1301 0.1206 0.0920 0.0046  -0.0009 0.0009  92  VAL A N    
1645 C CA   . VAL A 93  ? 0.1476 0.1143 0.1190 -0.0003 -0.0160 0.0199  92  VAL A CA   
1646 C C    . VAL A 93  ? 0.1159 0.1149 0.1135 -0.0064 0.0067  0.0049  92  VAL A C    
1647 O O    . VAL A 93  ? 0.1130 0.1215 0.1259 -0.0042 0.0078  -0.0032 92  VAL A O    
1648 C CB   . VAL A 93  ? 0.2252 0.1425 0.1230 -0.0237 0.0062  0.0297  92  VAL A CB   
1649 C CG1  . VAL A 93  ? 0.2294 0.1671 0.1805 -0.0453 0.0341  0.0216  92  VAL A CG1  
1650 C CG2  . VAL A 93  ? 0.2820 0.1536 0.1351 -0.0074 -0.0244 0.0331  92  VAL A CG2  
1652 D D    B VAL A 93  ? 0.0580 0.1410 0.0985 0.0139  0.0005  -0.0081 92  VAL A D    
1653 D DA   . VAL A 93  ? 0.1580 0.1223 0.1616 0.0063  -0.0225 0.0091  92  VAL A DA   
1654 D DB   . VAL A 93  ? 0.2222 0.1806 0.1533 -0.0041 0.0081  0.0051  92  VAL A DB   
1655 D DG11 . VAL A 93  ? 0.2513 0.1859 0.2452 -0.0229 0.0096  -0.0065 92  VAL A DG11 
1656 D DG12 . VAL A 93  ? 0.3387 0.2659 0.1996 -0.1407 0.0464  0.0281  92  VAL A DG12 
1657 D DG13 . VAL A 93  ? 0.2037 0.2328 0.2263 -0.0355 0.0309  0.0095  92  VAL A DG13 
1658 D DG21 . VAL A 93  ? 0.3044 0.1940 0.2307 0.0395  -0.0421 0.0258  92  VAL A DG21 
1659 D DG22 . VAL A 93  ? 0.3233 0.1999 0.1669 -0.0537 -0.0587 0.0332  92  VAL A DG22 
1660 D DG23 . VAL A 93  ? 0.3704 0.2174 0.1323 -0.0489 -0.0178 0.0335  92  VAL A DG23 
1661 N N    . ASN A 94  ? 0.1090 0.1206 0.1102 -0.0054 0.0026  0.0061  93  ASN A N    
1662 C CA   . ASN A 94  ? 0.0995 0.1356 0.1288 -0.0066 0.0004  0.0026  93  ASN A CA   
1663 C C    . ASN A 94  ? 0.0951 0.1228 0.1153 -0.0022 -0.0128 0.0037  93  ASN A C    
1664 O O    . ASN A 94  ? 0.0957 0.1484 0.1356 -0.0227 -0.0027 -0.0154 93  ASN A O    
1665 C CB   . ASN A 94  ? 0.0987 0.1548 0.1576 0.0114  -0.0040 -0.0163 93  ASN A CB   
1666 C CG   . ASN A 94  ? 0.1374 0.2100 0.1766 0.0211  0.0222  -0.0089 93  ASN A CG   
1667 O OD1  . ASN A 94  ? 0.2682 0.2396 0.2163 0.0187  0.0848  0.0329  93  ASN A OD1  
1668 N ND2  . ASN A 94  ? 0.1749 0.2360 0.1869 0.0641  0.0254  -0.0143 93  ASN A ND2  
1670 D D    B ASN A 94  ? 0.2005 0.1566 0.1653 0.0465  -0.0483 -0.0425 93  ASN A D    
1671 D DA   . ASN A 94  ? 0.1124 0.1583 0.1466 -0.0321 -0.0030 -0.0024 93  ASN A DA   
1672 D DB2  . ASN A 94  ? 0.1287 0.1562 0.2210 -0.0034 0.0000  -0.0004 93  ASN A DB2  
1673 D DB3  . ASN A 94  ? 0.1451 0.1996 0.1636 0.0262  -0.0192 -0.0030 93  ASN A DB3  
1674 D DD21 . ASN A 94  ? 0.2359 0.3031 0.2911 0.0018  0.1085  -0.0839 93  ASN A DD21 
1675 D DD22 . ASN A 94  ? 0.2098 0.2366 0.2750 0.0276  0.0206  0.0006  93  ASN A DD22 
1676 N N    . CYS A 95  ? 0.0989 0.1095 0.0951 -0.0004 -0.0090 -0.0023 94  CYS A N    
1677 C CA   . CYS A 95  ? 0.1126 0.1030 0.0917 0.0015  -0.0093 0.0086  94  CYS A CA   
1678 C C    . CYS A 95  ? 0.1074 0.0963 0.0989 -0.0040 -0.0101 0.0028  94  CYS A C    
1679 O O    . CYS A 95  ? 0.1443 0.0998 0.1064 -0.0097 -0.0180 -0.0002 94  CYS A O    
1680 C CB   . CYS A 95  ? 0.1269 0.0956 0.0869 -0.0044 -0.0092 0.0127  94  CYS A CB   
1681 S SG   . CYS A 95  ? 0.1205 0.1004 0.0922 -0.0073 -0.0117 0.0101  94  CYS A SG   
1683 D D    B CYS A 95  ? 0.0867 0.0963 0.1049 0.0059  -0.0034 -0.0076 94  CYS A D    
1684 D DA   . CYS A 95  ? 0.1264 0.1170 0.1006 0.0012  -0.0208 0.0082  94  CYS A DA   
1685 D DB2  . CYS A 95  ? 0.1454 0.1078 0.1280 -0.0003 -0.0044 -0.0028 94  CYS A DB2  
1686 D DB3  . CYS A 95  ? 0.1384 0.1378 0.1063 -0.0113 -0.0244 0.0122  94  CYS A DB3  
1687 N N    . ALA A 96  ? 0.0987 0.1023 0.1015 0.0018  -0.0057 0.0014  95  ALA A N    
1688 C CA   . ALA A 96  ? 0.1005 0.1017 0.1316 0.0088  -0.0088 0.0048  95  ALA A CA   
1689 C C    . ALA A 96  ? 0.1126 0.0959 0.1303 0.0107  -0.0041 0.0019  95  ALA A C    
1690 O O    . ALA A 96  ? 0.1359 0.1058 0.1257 0.0009  0.0111  -0.0051 95  ALA A O    
1691 C CB   . ALA A 96  ? 0.1486 0.1316 0.1389 0.0275  -0.0293 0.0036  95  ALA A CB   
1693 D DA   . ALA A 96  ? 0.1343 0.1111 0.1460 0.0049  0.0155  -0.0055 95  ALA A DA   
1694 D DB1  . ALA A 96  ? 0.1813 0.1550 0.1316 0.0482  -0.0165 0.0167  95  ALA A DB1  
1695 D DB2  . ALA A 96  ? 0.2218 0.1423 0.1659 0.0540  -0.0120 0.0082  95  ALA A DB2  
1696 D DB3  . ALA A 96  ? 0.1648 0.1655 0.1816 0.0121  -0.0647 0.0161  95  ALA A DB3  
1697 N N    . LYS A 97  ? 0.1075 0.1061 0.1238 -0.0024 -0.0047 0.0035  96  LYS A N    
1698 C CA   . LYS A 97  ? 0.1286 0.1176 0.1285 -0.0279 0.0038  0.0021  96  LYS A CA   
1699 C C    . LYS A 97  ? 0.1286 0.1491 0.1358 -0.0407 -0.0090 -0.0026 96  LYS A C    
1700 O O    . LYS A 97  ? 0.1464 0.1621 0.1474 -0.0486 -0.0195 -0.0133 96  LYS A O    
1701 C CB   . LYS A 97  ? 0.1229 0.1495 0.1562 -0.0190 0.0080  0.0048  96  LYS A CB   
1702 C CG   . LYS A 97  ? 0.1559 0.1631 0.1526 -0.0361 0.0216  0.0047  96  LYS A CG   
1703 C CD   . LYS A 97  ? 0.1888 0.2404 0.1830 -0.0154 0.0483  -0.0110 96  LYS A CD   
1704 C CE   . LYS A 97  ? 0.2438 0.3088 0.1845 -0.0383 0.0626  0.0019  96  LYS A CE   
1705 N NZ   . LYS A 97  ? 0.2576 0.3247 0.2280 -0.0677 0.0978  -0.0318 96  LYS A NZ   
1707 D DA   . LYS A 97  ? 0.1658 0.1131 0.1553 -0.0294 0.0066  -0.0009 96  LYS A DA   
1708 D DB2  . LYS A 97  ? 0.1374 0.1488 0.1937 0.0064  -0.0042 0.0162  96  LYS A DB2  
1709 D DB3  . LYS A 97  ? 0.1322 0.1982 0.1717 -0.0326 0.0161  -0.0084 96  LYS A DB3  
1710 D DG2  . LYS A 97  ? 0.1840 0.1597 0.1859 -0.0242 0.0144  0.0185  96  LYS A DG2  
1711 D DG3  . LYS A 97  ? 0.1765 0.1948 0.1417 -0.0452 0.0117  0.0039  96  LYS A DG3  
1712 D DD2  . LYS A 97  ? 0.2202 0.2387 0.2923 0.0090  0.1257  0.0103  96  LYS A DD2  
1713 D DD3  . LYS A 97  ? 0.1734 0.3748 0.2116 -0.0217 0.0471  -0.0434 96  LYS A DD3  
1714 D DE2  . LYS A 97  ? 0.2735 0.3011 0.2870 -0.0220 0.0810  0.0551  96  LYS A DE2  
1715 D DE3  . LYS A 97  ? 0.2582 0.4167 0.2188 -0.0527 0.0242  0.0299  96  LYS A DE3  
1716 D DZ1  . LYS A 97  ? 0.2490 0.4522 0.3117 -0.0533 0.0868  -0.1217 96  LYS A DZ1  
1717 D DZ2  . LYS A 97  ? 0.2601 0.4647 0.2466 -0.0345 0.1154  0.0127  96  LYS A DZ2  
1718 D DZ3  . LYS A 97  ? 0.3273 0.3265 0.3462 -0.0338 0.1787  -0.0084 96  LYS A DZ3  
1719 N N    . LYS A 98  ? 0.1222 0.1503 0.1259 -0.0280 -0.0259 0.0034  97  LYS A N    
1720 C CA   . LYS A 98  ? 0.1577 0.1668 0.1337 -0.0271 -0.0452 0.0026  97  LYS A CA   
1721 C C    . LYS A 98  ? 0.1857 0.1558 0.1197 -0.0407 -0.0362 -0.0089 97  LYS A C    
1722 O O    . LYS A 98  ? 0.2374 0.1916 0.1545 -0.0279 -0.0624 -0.0428 97  LYS A O    
1723 C CB   . LYS A 98  ? 0.2083 0.1655 0.1768 -0.0003 -0.0518 0.0243  97  LYS A CB   
1724 C CG   . LYS A 98  ? 0.3027 0.1977 0.1835 0.0033  -0.0742 0.0302  97  LYS A CG   
1725 C CD   . LYS A 98  ? 0.3714 0.3249 0.2657 -0.0031 -0.1790 -0.0709 97  LYS A CD   
1726 C CE   . LYS A 98  ? 0.4754 0.3882 0.3043 0.0696  -0.2188 -0.0346 97  LYS A CE   
1727 N NZ   . LYS A 98  ? 0.4661 0.4502 0.3622 0.0872  -0.2380 -0.0048 97  LYS A NZ   
1729 D DA   . LYS A 98  ? 0.1814 0.2053 0.1454 -0.0496 -0.0531 -0.0017 97  LYS A DA   
1730 D DB2  . LYS A 98  ? 0.2414 0.1858 0.2104 0.0038  -0.0309 0.0037  97  LYS A DB2  
1731 D DB3  . LYS A 98  ? 0.2280 0.1359 0.1797 -0.0065 -0.0455 0.0049  97  LYS A DB3  
1732 D DG2  . LYS A 98  ? 0.2970 0.1961 0.2391 0.0121  -0.0156 0.0680  97  LYS A DG2  
1733 D DG3  . LYS A 98  ? 0.4159 0.2762 0.1913 0.0584  -0.0508 0.0000  97  LYS A DG3  
1734 D DD2  . LYS A 98  ? 0.3988 0.3300 0.3573 -0.0471 -0.1816 -0.0552 97  LYS A DD2  
1735 D DD3  . LYS A 98  ? 0.2918 0.3715 0.3818 -0.0224 -0.1022 -0.0425 97  LYS A DD3  
1736 D DE2  . LYS A 98  ? 0.5060 0.3611 0.5106 0.0856  -0.1357 0.0146  97  LYS A DE2  
1737 D DE3  . LYS A 98  ? 0.5347 0.3334 0.3458 0.0775  -0.1001 0.0862  97  LYS A DE3  
1738 D DZ1  . LYS A 98  ? 0.4819 0.5481 0.4506 0.0424  -0.2536 0.0862  97  LYS A DZ1  
1739 D DZ2  . LYS A 98  ? 0.4756 0.4552 0.6093 0.0482  -0.1030 -0.0493 97  LYS A DZ2  
1740 D DZ3  . LYS A 98  ? 0.5408 0.5078 0.3763 0.0428  -0.2773 -0.0177 97  LYS A DZ3  
1741 N N    . ILE A 99  ? 0.1698 0.1285 0.1034 -0.0282 -0.0141 -0.0028 98  ILE A N    
1742 C CA   . ILE A 99  ? 0.2028 0.1223 0.1176 -0.0250 0.0221  0.0088  98  ILE A CA   
1743 C C    . ILE A 99  ? 0.2800 0.1277 0.1472 -0.0465 0.0683  -0.0146 98  ILE A C    
1744 O O    . ILE A 99  ? 0.3679 0.1581 0.1594 -0.0528 0.0969  -0.0375 98  ILE A O    
1745 C CB   . ILE A 99  ? 0.1867 0.1258 0.1173 0.0079  0.0280  0.0144  98  ILE A CB   
1746 C CG1  . ILE A 99  ? 0.1536 0.1334 0.1415 -0.0080 0.0060  0.0245  98  ILE A CG1  
1747 C CG2  . ILE A 99  ? 0.2233 0.1517 0.1771 0.0335  0.0687  0.0280  98  ILE A CG2  
1748 C CD1  . ILE A 99  ? 0.1760 0.1853 0.1910 -0.0155 -0.0230 0.0188  98  ILE A CD1  
1750 D DA   . ILE A 99  ? 0.2140 0.1268 0.1241 -0.0174 0.0086  0.0099  98  ILE A DA   
1751 D DB   . ILE A 99  ? 0.1754 0.1456 0.1259 0.0041  0.0210  0.0305  98  ILE A DB   
1752 D DG12 . ILE A 99  ? 0.2719 0.1527 0.1481 -0.0293 0.0167  0.0245  98  ILE A DG12 
1753 D DG13 . ILE A 99  ? 0.1663 0.1125 0.1975 -0.0057 -0.0109 -0.0015 98  ILE A DG13 
1754 D DG21 . ILE A 99  ? 0.2916 0.2457 0.1972 0.0734  0.1077  0.0607  98  ILE A DG21 
1755 D DG22 . ILE A 99  ? 0.2138 0.2686 0.2714 0.0392  0.0359  0.0592  98  ILE A DG22 
1756 D DG23 . ILE A 99  ? 0.2707 0.1428 0.3094 0.0525  0.0817  0.0416  98  ILE A DG23 
1757 D DD11 . ILE A 99  ? 0.1818 0.2976 0.3041 0.0373  -0.0557 -0.0036 98  ILE A DD11 
1758 D DD12 . ILE A 99  ? 0.2641 0.1931 0.1995 -0.0594 -0.0143 -0.0191 98  ILE A DD12 
1759 D DD13 . ILE A 99  ? 0.2361 0.3244 0.1847 -0.0814 -0.0531 0.0369  98  ILE A DD13 
1760 N N    A VAL A 100 ? 0.2659 0.1225 0.1619 -0.0439 0.0838  -0.0125 99  VAL A N    
1761 N N    B VAL A 100 ? 0.2821 0.1191 0.1651 -0.0410 0.0864  -0.0105 99  VAL A N    
1762 C CA   A VAL A 100 ? 0.3273 0.1228 0.1842 -0.0447 0.0947  -0.0124 99  VAL A CA   
1763 C CA   B VAL A 100 ? 0.3387 0.1232 0.1811 -0.0444 0.0934  -0.0121 99  VAL A CA   
1764 C C    A VAL A 100 ? 0.3823 0.1372 0.1924 -0.1043 0.0735  -0.0257 99  VAL A C    
1765 C C    B VAL A 100 ? 0.3853 0.1500 0.1915 -0.0873 0.0639  -0.0424 99  VAL A C    
1766 O O    A VAL A 100 ? 0.4664 0.1823 0.2029 -0.1235 0.0991  -0.0521 99  VAL A O    
1767 O O    B VAL A 100 ? 0.4674 0.1690 0.1937 -0.1155 0.0979  -0.0683 99  VAL A O    
1768 C CB   A VAL A 100 ? 0.3394 0.1278 0.1946 -0.0167 0.1094  0.0051  99  VAL A CB   
1769 C CB   B VAL A 100 ? 0.3540 0.1277 0.2005 -0.0093 0.1110  0.0062  99  VAL A CB   
1770 C CG1  A VAL A 100 ? 0.3552 0.1301 0.2350 -0.0196 0.1337  0.0109  99  VAL A CG1  
1771 C CG1  B VAL A 100 ? 0.3449 0.1423 0.2028 0.0160  0.1041  0.0298  99  VAL A CG1  
1772 C CG2  A VAL A 100 ? 0.3398 0.1381 0.1934 0.0076  0.1045  0.0099  99  VAL A CG2  
1773 C CG2  B VAL A 100 ? 0.3478 0.1355 0.1996 -0.0087 0.1121  0.0171  99  VAL A CG2  
1776 D DA   A VAL A 100 ? 0.3951 0.1384 0.2262 -0.0112 0.1466  -0.0109 99  VAL A DA   
1777 D DA   B VAL A 100 ? 0.4114 0.0987 0.1984 0.0130  0.1227  0.0089  99  VAL A DA   
1778 D DB   A VAL A 100 ? 0.3323 0.1603 0.2116 -0.0098 0.1056  -0.0148 99  VAL A DB   
1779 D DB   B VAL A 100 ? 0.3656 0.1227 0.2760 -0.0076 0.1420  0.0060  99  VAL A DB   
1780 D DG11 A VAL A 100 ? 0.4366 0.1594 0.2954 -0.0850 0.0743  0.0113  99  VAL A DG11 
1781 D DG11 B VAL A 100 ? 0.3334 0.1215 0.2305 0.0743  0.1158  0.0941  99  VAL A DG11 
1782 D DG12 A VAL A 100 ? 0.4220 0.1304 0.3848 0.0079  0.1940  0.0157  99  VAL A DG12 
1783 D DG12 B VAL A 100 ? 0.3054 0.1721 0.2503 0.0427  0.0490  -0.0074 99  VAL A DG12 
1784 D DG13 A VAL A 100 ? 0.3706 0.2091 0.2770 -0.0301 0.1513  0.0700  99  VAL A DG13 
1785 D DG13 B VAL A 100 ? 0.3594 0.1962 0.1723 0.0898  0.1637  0.0427  99  VAL A DG13 
1786 D DG21 A VAL A 100 ? 0.3635 0.1942 0.2629 0.0474  0.1440  0.0251  99  VAL A DG21 
1787 D DG21 B VAL A 100 ? 0.3712 0.1488 0.1981 -0.0108 0.1212  -0.0096 99  VAL A DG21 
1788 D DG22 A VAL A 100 ? 0.3540 0.1632 0.2830 -0.0234 0.0721  -0.0108 99  VAL A DG22 
1789 D DG22 B VAL A 100 ? 0.3636 0.1865 0.1937 -0.0309 0.1099  -0.0109 99  VAL A DG22 
1790 D DG23 A VAL A 100 ? 0.4029 0.2472 0.2009 0.0316  0.0986  0.0357  99  VAL A DG23 
1791 D DG23 B VAL A 100 ? 0.3620 0.2031 0.2107 -0.0118 0.1035  0.0408  99  VAL A DG23 
1792 N N    . SER A 101 ? 0.3596 0.1796 0.1781 -0.0964 -0.0047 -0.0409 100 SER A N    
1793 C CA   . SER A 101 ? 0.3767 0.2541 0.2056 -0.1480 -0.0299 -0.0614 100 SER A CA   
1794 C C    . SER A 101 ? 0.4157 0.2300 0.2081 -0.1379 -0.0569 -0.0460 100 SER A C    
1795 O O    . SER A 101 ? 0.3686 0.3342 0.2093 -0.1394 -0.0328 -0.0452 100 SER A O    
1796 C CB   . SER A 101 ? 0.3416 0.3988 0.2665 -0.0794 -0.0456 -0.0798 100 SER A CB   
1797 O OG   . SER A 101 ? 0.3832 0.4562 0.2811 -0.0855 -0.0790 -0.1259 100 SER A OG   
1798 D D    . SER A 101 ? 0.3667 0.1771 0.2349 -0.0394 -0.0738 -0.0638 100 SER A D    
1799 D DA   . SER A 101 ? 0.5333 0.2973 0.2268 -0.2262 -0.0607 -0.0124 100 SER A DA   
1803 N N    . ASP A 102 ? 0.3779 0.2030 0.1804 -0.0990 -0.0928 0.0018  101 ASP A N    
1804 C CA   . ASP A 102 ? 0.3628 0.2704 0.1832 -0.0478 -0.1008 0.0288  101 ASP A CA   
1805 C C    . ASP A 102 ? 0.4127 0.3363 0.1951 -0.0272 -0.0800 -0.0047 101 ASP A C    
1806 O O    . ASP A 102 ? 0.5012 0.4146 0.2677 -0.0067 0.0011  0.0288  101 ASP A O    
1807 C CB   . ASP A 102 ? 0.3220 0.2885 0.1865 -0.0542 -0.0690 0.0606  101 ASP A CB   
1808 C CG   . ASP A 102 ? 0.3039 0.2642 0.1236 -0.0760 -0.0675 0.0463  101 ASP A CG   
1809 O OD1  . ASP A 102 ? 0.2846 0.2654 0.2183 -0.0403 -0.0575 -0.0415 101 ASP A OD1  
1810 O OD2  . ASP A 102 ? 0.3109 0.2658 0.1434 -0.0857 -0.0365 0.0445  101 ASP A OD2  
1811 D D    . ASP A 102 ? 0.3120 0.3724 0.1434 -0.1003 -0.0493 -0.0049 101 ASP A D    
1812 D DA   . ASP A 102 ? 0.3839 0.2651 0.2551 -0.0583 -0.1453 0.0643  101 ASP A DA   
1813 D DB2  . ASP A 102 ? 0.4744 0.2184 0.2264 -0.0435 -0.1504 0.0637  101 ASP A DB2  
1814 D DB3  . ASP A 102 ? 0.3868 0.3946 0.2741 0.0195  0.0106  0.1268  101 ASP A DB3  
1815 D DD2  . ASP A 102 ? 0.3029 0.2486 0.1255 -0.0703 -0.0211 0.0245  101 ASP A DD2  
1816 N N    . GLY A 103 ? 0.4530 0.3131 0.2513 -0.0232 -0.0270 -0.0369 102 GLY A N    
1817 C CA   . GLY A 103 ? 0.4705 0.3613 0.2993 -0.0010 -0.0609 -0.0899 102 GLY A CA   
1818 C C    . GLY A 103 ? 0.5233 0.3737 0.2965 0.0438  -0.0719 -0.0933 102 GLY A C    
1819 O O    . GLY A 103 ? 0.5190 0.3734 0.3382 0.0364  -0.0585 -0.1059 102 GLY A O    
1820 D D    . GLY A 103 ? 0.4699 0.3691 0.3272 0.0530  0.0342  0.0527  102 GLY A D    
1821 D DA2  . GLY A 103 ? 0.5092 0.3500 0.6578 -0.0081 -0.0975 -0.1574 102 GLY A DA2  
1822 D DA3  . GLY A 103 ? 0.5534 0.5804 0.2770 0.1446  -0.0278 -0.0636 102 GLY A DA3  
1823 N N    . ASN A 104 ? 0.5284 0.3196 0.2728 0.0757  -0.1093 -0.0436 103 ASN A N    
1824 C CA   . ASN A 104 ? 0.5043 0.3193 0.2484 0.0777  -0.0716 -0.0343 103 ASN A CA   
1825 C C    . ASN A 104 ? 0.4126 0.3357 0.2311 0.0616  -0.0791 -0.0447 103 ASN A C    
1826 O O    . ASN A 104 ? 0.4413 0.3977 0.3353 0.0680  -0.0206 -0.0636 103 ASN A O    
1827 C CB   . ASN A 104 ? 0.4491 0.3426 0.3677 0.0486  -0.0465 -0.0407 103 ASN A CB   
1828 C CG   . ASN A 104 ? 0.4850 0.3434 0.4002 0.0558  -0.0267 -0.0184 103 ASN A CG   
1829 O OD1  . ASN A 104 ? 0.6055 0.3326 0.4252 0.0908  0.0407  -0.0086 103 ASN A OD1  
1830 N ND2  . ASN A 104 ? 0.5377 0.3723 0.4190 0.0959  -0.0360 -0.0206 103 ASN A ND2  
1831 D D    . ASN A 104 ? 0.6720 0.3714 0.7193 0.1503  -0.2646 -0.1862 103 ASN A D    
1832 D DA   . ASN A 104 ? 0.5403 0.4414 0.1683 0.1217  -0.1136 -0.0245 103 ASN A DA   
1833 D DB2  . ASN A 104 ? 0.5218 0.3064 0.3407 0.0819  -0.0746 -0.0540 103 ASN A DB2  
1834 D DB3  . ASN A 104 ? 0.4938 0.4197 0.3888 0.0774  -0.1018 -0.0960 103 ASN A DB3  
1835 D DD21 . ASN A 104 ? 0.4123 0.2446 0.3835 -0.0242 -0.1016 -0.0927 103 ASN A DD21 
1836 D DD22 . ASN A 104 ? 0.6287 0.2694 0.4437 0.1135  0.0150  -0.0253 103 ASN A DD22 
1837 N N    . GLY A 105 ? 0.3999 0.3264 0.1732 0.0360  -0.1113 -0.0612 104 GLY A N    
1838 C CA   . GLY A 105 ? 0.2920 0.2484 0.1865 -0.0426 -0.0880 -0.0580 104 GLY A CA   
1839 C C    . GLY A 105 ? 0.2482 0.1846 0.1473 -0.0413 -0.0592 -0.0035 104 GLY A C    
1840 O O    . GLY A 105 ? 0.3142 0.1881 0.1683 -0.0512 -0.0583 0.0083  104 GLY A O    
1841 D D    . GLY A 105 ? 0.4967 0.2735 0.1867 0.0759  -0.0647 -0.0377 104 GLY A D    
1842 D DA2  . GLY A 105 ? 0.2535 0.3782 0.2390 -0.0793 -0.1083 -0.0396 104 GLY A DA2  
1843 D DA3  . GLY A 105 ? 0.3863 0.2474 0.2815 -0.0234 -0.1297 -0.0678 104 GLY A DA3  
1844 N N    . MET A 106 ? 0.1731 0.1632 0.1270 -0.0458 -0.0177 -0.0129 105 MET A N    
1845 C CA   . MET A 106 ? 0.1483 0.1468 0.1317 -0.0256 -0.0192 -0.0065 105 MET A CA   
1846 C C    . MET A 106 ? 0.1617 0.1559 0.1370 -0.0266 -0.0045 -0.0080 105 MET A C    
1847 O O    . MET A 106 ? 0.1397 0.1564 0.1380 -0.0215 0.0009  0.0038  105 MET A O    
1848 C CB   . MET A 106 ? 0.1556 0.1316 0.1318 -0.0316 -0.0150 -0.0126 105 MET A CB   
1849 C CG   . MET A 106 ? 0.1479 0.1263 0.1282 -0.0227 -0.0184 0.0107  105 MET A CG   
1850 S SD   . MET A 106 ? 0.1763 0.1562 0.1251 -0.0024 -0.0297 -0.0042 105 MET A SD   
1851 C CE   . MET A 106 ? 0.1640 0.1764 0.2133 0.0200  -0.0605 -0.0723 105 MET A CE   
1852 D D    . MET A 106 ? 0.2007 0.1781 0.1663 -0.0712 -0.0450 0.0084  105 MET A D    
1853 D DA   . MET A 106 ? 0.1692 0.1529 0.1416 -0.0118 -0.0363 -0.0191 105 MET A DA   
1854 D DB2  . MET A 106 ? 0.1761 0.1293 0.1718 -0.0126 -0.0215 -0.0013 105 MET A DB2  
1855 D DB3  . MET A 106 ? 0.1485 0.1727 0.1652 -0.0408 -0.0250 0.0142  105 MET A DB3  
1856 D DG2  . MET A 106 ? 0.1414 0.1398 0.1667 0.0010  0.0080  0.0323  105 MET A DG2  
1857 D DG3  . MET A 106 ? 0.1443 0.1750 0.1462 -0.0209 -0.0247 -0.0055 105 MET A DG3  
1858 D DE1  . MET A 106 ? 0.2670 0.3069 0.2194 -0.0367 -0.0868 -0.0740 105 MET A DE1  
1859 D DE2  . MET A 106 ? 0.1682 0.2381 0.2755 -0.0048 -0.0335 -0.0959 105 MET A DE2  
1860 D DE3  . MET A 106 ? 0.2036 0.1644 0.3595 0.0107  -0.0283 -0.0435 105 MET A DE3  
1861 N N    A ASN A 107 ? 0.2205 0.1775 0.1576 -0.0202 0.0121  -0.0271 106 ASN A N    
1862 N N    B ASN A 107 ? 0.2128 0.1804 0.1581 -0.0320 0.0150  -0.0314 106 ASN A N    
1863 C CA   A ASN A 107 ? 0.2870 0.1959 0.1752 0.0344  0.0664  0.0049  106 ASN A CA   
1864 C CA   B ASN A 107 ? 0.2387 0.2128 0.1718 -0.0062 0.0456  -0.0106 106 ASN A CA   
1865 C C    A ASN A 107 ? 0.3092 0.1957 0.1450 0.0468  0.1164  0.0101  106 ASN A C    
1867 O O    A ASN A 107 ? 0.3347 0.1863 0.2250 0.0880  0.2000  0.0487  106 ASN A O    
1869 C CB   A ASN A 107 ? 0.3157 0.2302 0.1916 0.0079  0.0691  -0.0127 106 ASN A CB   
1870 C CB   B ASN A 107 ? 0.2874 0.2391 0.1994 -0.0025 0.0549  -0.0365 106 ASN A CB   
1872 C CG   B ASN A 107 ? 0.2916 0.2335 0.2458 -0.0124 0.0122  -0.0458 106 ASN A CG   
1877 D D    A ASN A 107 ? 0.2970 0.2442 0.1889 -0.0795 0.0140  -0.0684 106 ASN A D    
1878 D D    B ASN A 107 ? 0.2398 0.2829 0.1975 -0.0615 0.0253  -0.1117 106 ASN A D    
1879 D DA   A ASN A 107 ? 0.2572 0.1801 0.1915 0.0087  0.0717  0.0113  106 ASN A DA   
1880 D DA   B ASN A 107 ? 0.2230 0.1976 0.1857 0.0079  0.0566  -0.0051 106 ASN A DA   
1881 D DB2  A ASN A 107 ? 0.3733 0.2017 0.2767 0.0122  0.1054  -0.0320 106 ASN A DB2  
1882 D DB2  B ASN A 107 ? 0.3287 0.2415 0.2056 -0.0159 0.0182  -0.0404 106 ASN A DB2  
1883 D DB3  A ASN A 107 ? 0.4062 0.2280 0.1671 0.0660  0.0387  -0.0706 106 ASN A DB3  
1884 D DB3  B ASN A 107 ? 0.3398 0.2503 0.2136 0.0075  0.1099  -0.0653 106 ASN A DB3  
1889 N N    . ALA A 108 ? 0.2126 0.1845 0.1446 -0.0060 0.0061  -0.0048 107 ALA A N    
1890 C CA   . ALA A 108 ? 0.1859 0.1954 0.1367 -0.0068 -0.0169 0.0364  107 ALA A CA   
1891 C C    . ALA A 108 ? 0.1781 0.1713 0.1451 -0.0095 -0.0137 0.0358  107 ALA A C    
1892 O O    . ALA A 108 ? 0.2209 0.1950 0.1589 -0.0324 -0.0183 0.0594  107 ALA A O    
1893 C CB   . ALA A 108 ? 0.1775 0.1973 0.2115 -0.0077 -0.0260 0.0623  107 ALA A CB   
1894 D D    . ALA A 108 ? 0.2058 0.2191 0.1667 -0.0266 -0.0126 0.0125  107 ALA A D    
1895 D DA   . ALA A 108 ? 0.2660 0.2782 0.1260 -0.0315 -0.0164 0.0318  107 ALA A DA   
1896 D DB1  . ALA A 108 ? 0.1958 0.2739 0.2373 0.0571  0.0054  0.0891  107 ALA A DB1  
1897 D DB2  . ALA A 108 ? 0.2113 0.2012 0.3191 -0.0007 -0.0162 0.0869  107 ALA A DB2  
1898 D DB3  . ALA A 108 ? 0.2152 0.3189 0.2944 0.0143  -0.0689 -0.0223 107 ALA A DB3  
1899 N N    . TRP A 109 ? 0.1228 0.1414 0.1372 0.0049  0.0015  0.0199  108 TRP A N    
1900 C CA   . TRP A 109 ? 0.1181 0.1290 0.1391 0.0088  0.0065  0.0104  108 TRP A CA   
1901 C C    . TRP A 109 ? 0.1240 0.1204 0.1446 0.0079  0.0086  -0.0031 108 TRP A C    
1902 O O    . TRP A 109 ? 0.1054 0.1198 0.1700 -0.0017 0.0014  -0.0016 108 TRP A O    
1903 C CB   . TRP A 109 ? 0.1134 0.1367 0.1366 0.0156  0.0038  0.0055  108 TRP A CB   
1904 C CG   . TRP A 109 ? 0.1125 0.1318 0.1361 0.0053  -0.0082 -0.0193 108 TRP A CG   
1905 C CD1  . TRP A 109 ? 0.1305 0.1410 0.1559 -0.0007 -0.0144 -0.0324 108 TRP A CD1  
1906 C CD2  . TRP A 109 ? 0.1124 0.1109 0.1293 0.0044  0.0077  -0.0052 108 TRP A CD2  
1907 N NE1  . TRP A 109 ? 0.1445 0.1142 0.1727 -0.0031 0.0008  -0.0191 108 TRP A NE1  
1908 C CE2  . TRP A 109 ? 0.1256 0.1094 0.1215 0.0079  0.0056  -0.0031 108 TRP A CE2  
1909 C CE3  . TRP A 109 ? 0.1178 0.1153 0.1876 -0.0056 0.0185  -0.0202 108 TRP A CE3  
1910 C CZ2  . TRP A 109 ? 0.1310 0.1317 0.1648 0.0205  0.0069  -0.0102 108 TRP A CZ2  
1911 C CZ3  . TRP A 109 ? 0.1139 0.1301 0.2247 -0.0022 0.0272  -0.0065 108 TRP A CZ3  
1912 C CH2  . TRP A 109 ? 0.1142 0.1388 0.1987 0.0126  0.0142  -0.0024 108 TRP A CH2  
1914 D D    B TRP A 109 ? 0.1353 0.1552 0.1647 -0.0079 -0.0111 0.0367  108 TRP A D    
1915 D DA   . TRP A 109 ? 0.1363 0.1301 0.1852 0.0046  -0.0067 0.0265  108 TRP A DA   
1916 D DB2  . TRP A 109 ? 0.1431 0.1312 0.1392 0.0191  0.0077  0.0242  108 TRP A DB2  
1917 D DB3  . TRP A 109 ? 0.1508 0.1824 0.1523 0.0350  -0.0263 -0.0106 108 TRP A DB3  
1918 D DD1  . TRP A 109 ? 0.1533 0.1839 0.2428 -0.0164 -0.0453 -0.0720 108 TRP A DD1  
1919 D DE1  . TRP A 109 ? 0.2010 0.1113 0.1893 0.0001  -0.0082 -0.0156 108 TRP A DE1  
1920 D DE3  . TRP A 109 ? 0.1628 0.1277 0.2316 0.0172  -0.0132 -0.0379 108 TRP A DE3  
1921 D DZ2  . TRP A 109 ? 0.1567 0.1261 0.2750 0.0185  0.0830  0.0023  108 TRP A DZ2  
1922 D DZ3  . TRP A 109 ? 0.1419 0.1487 0.3806 -0.0125 -0.0105 -0.0304 108 TRP A DZ3  
1923 D DH2  . TRP A 109 ? 0.1246 0.1655 0.2356 0.0300  0.0076  -0.0077 108 TRP A DH2  
1924 N N    . VAL A 110 ? 0.1225 0.1126 0.1443 0.0104  0.0058  0.0007  109 VAL A N    
1925 C CA   . VAL A 110 ? 0.1352 0.1475 0.1615 0.0296  0.0347  0.0167  109 VAL A CA   
1926 C C    . VAL A 110 ? 0.1008 0.1150 0.1622 0.0049  0.0115  -0.0044 109 VAL A C    
1927 O O    . VAL A 110 ? 0.1216 0.1394 0.1723 0.0367  0.0199  -0.0021 109 VAL A O    
1928 C CB   . VAL A 110 ? 0.1680 0.1993 0.2577 0.0223  0.0781  0.0669  109 VAL A CB   
1929 C CG1  . VAL A 110 ? 0.2029 0.2094 0.3363 -0.0406 0.0738  0.0426  109 VAL A CG1  
1930 C CG2  . VAL A 110 ? 0.1493 0.2583 0.3590 0.0096  0.0897  0.0324  109 VAL A CG2  
1931 D D    . VAL A 110 ? 0.1543 0.1178 0.1793 0.0135  0.0249  0.0190  109 VAL A D    
1932 D DA   . VAL A 110 ? 0.1902 0.1647 0.1626 0.0469  0.0301  -0.0034 109 VAL A DA   
1933 D DB   . VAL A 110 ? 0.2493 0.2364 0.3203 -0.0254 0.0276  0.1216  109 VAL A DB   
1934 D DG11 . VAL A 110 ? 0.3183 0.2674 0.3442 -0.0154 0.0181  0.0303  109 VAL A DG11 
1935 D DG12 . VAL A 110 ? 0.2603 0.3032 0.4594 -0.0986 0.0929  0.0872  109 VAL A DG12 
1936 D DG13 . VAL A 110 ? 0.1883 0.2944 0.4075 -0.0366 0.0358  -0.0485 109 VAL A DG13 
1937 D DG21 . VAL A 110 ? 0.1771 0.3282 0.4200 0.0360  0.0662  0.0970  109 VAL A DG21 
1938 D DG22 . VAL A 110 ? 0.1992 0.3369 0.5641 0.0403  0.0607  -0.1090 109 VAL A DG22 
1939 D DG23 . VAL A 110 ? 0.1960 0.3358 0.4259 0.0368  0.1505  0.0924  109 VAL A DG23 
1940 N N    . ALA A 111 ? 0.1142 0.1007 0.1625 0.0073  -0.0071 0.0000  110 ALA A N    
1941 C CA   . ALA A 111 ? 0.1264 0.1329 0.1652 0.0069  -0.0171 0.0020  110 ALA A CA   
1942 C C    . ALA A 111 ? 0.1226 0.1229 0.1535 0.0224  -0.0031 0.0088  110 ALA A C    
1943 O O    . ALA A 111 ? 0.1204 0.1541 0.1744 0.0287  -0.0119 0.0271  110 ALA A O    
1944 C CB   . ALA A 111 ? 0.2201 0.1471 0.1654 -0.0061 -0.0322 -0.0047 110 ALA A CB   
1945 D D    . ALA A 111 ? 0.1459 0.1072 0.1728 0.0173  -0.0060 0.0010  110 ALA A D    
1946 D DA   . ALA A 111 ? 0.1161 0.1667 0.2313 0.0149  -0.0276 0.0146  110 ALA A DA   
1947 D DB1  . ALA A 111 ? 0.2593 0.1651 0.1646 0.0235  0.0027  -0.0068 110 ALA A DB1  
1948 D DB2  . ALA A 111 ? 0.3316 0.2285 0.1874 0.0194  -0.0805 0.0074  110 ALA A DB2  
1949 D DB3  . ALA A 111 ? 0.2443 0.1801 0.2372 -0.0610 -0.0909 0.0030  110 ALA A DB3  
1950 N N    . TRP A 112 ? 0.1155 0.1072 0.1541 0.0251  0.0090  0.0127  111 TRP A N    
1951 C CA   . TRP A 112 ? 0.1286 0.1194 0.1658 0.0122  0.0132  0.0144  111 TRP A CA   
1952 C C    . TRP A 112 ? 0.1203 0.1100 0.1742 0.0182  0.0126  0.0240  111 TRP A C    
1953 O O    . TRP A 112 ? 0.1379 0.1098 0.1894 0.0097  0.0141  0.0276  111 TRP A O    
1954 C CB   . TRP A 112 ? 0.1279 0.1193 0.1744 0.0110  0.0162  0.0090  111 TRP A CB   
1955 C CG   . TRP A 112 ? 0.1093 0.1216 0.1774 0.0242  0.0141  0.0226  111 TRP A CG   
1956 C CD1  . TRP A 112 ? 0.1078 0.1346 0.1808 0.0206  0.0170  0.0243  111 TRP A CD1  
1957 C CD2  . TRP A 112 ? 0.1186 0.1242 0.1782 0.0056  0.0048  0.0297  111 TRP A CD2  
1958 N NE1  . TRP A 112 ? 0.1275 0.1360 0.1781 0.0113  -0.0012 0.0396  111 TRP A NE1  
1959 C CE2  . TRP A 112 ? 0.1240 0.1288 0.1868 0.0059  0.0113  0.0296  111 TRP A CE2  
1960 C CE3  . TRP A 112 ? 0.1514 0.1561 0.1750 0.0028  -0.0055 0.0258  111 TRP A CE3  
1961 C CZ2  . TRP A 112 ? 0.1609 0.1380 0.2200 -0.0085 0.0128  0.0130  111 TRP A CZ2  
1962 C CZ3  . TRP A 112 ? 0.1680 0.1764 0.1860 0.0101  -0.0078 0.0013  111 TRP A CZ3  
1963 C CH2  . TRP A 112 ? 0.1837 0.1579 0.2235 -0.0139 0.0015  -0.0135 111 TRP A CH2  
1965 D D    B TRP A 112 ? 0.1396 0.1180 0.1933 0.0350  0.0007  0.0258  111 TRP A D    
1966 D DA   . TRP A 112 ? 0.1488 0.1590 0.1666 0.0050  0.0196  0.0314  111 TRP A DA   
1967 D DB2  . TRP A 112 ? 0.1624 0.1261 0.2078 0.0179  0.0454  -0.0026 111 TRP A DB2  
1968 D DB3  . TRP A 112 ? 0.1146 0.1714 0.1742 0.0280  0.0308  0.0255  111 TRP A DB3  
1969 D DD1  . TRP A 112 ? 0.1814 0.1582 0.1832 0.0165  0.0165  0.0145  111 TRP A DD1  
1970 D DE1  . TRP A 112 ? 0.2149 0.1586 0.2100 0.0246  0.0416  0.0569  111 TRP A DE1  
1971 D DE3  . TRP A 112 ? 0.1721 0.2021 0.1851 0.0027  0.0011  0.0548  111 TRP A DE3  
1972 D DZ2  . TRP A 112 ? 0.2184 0.1548 0.2592 -0.0418 0.0461  0.0082  111 TRP A DZ2  
1973 D DZ3  . TRP A 112 ? 0.2027 0.2400 0.1893 0.0208  -0.0103 -0.0121 111 TRP A DZ3  
1974 D DH2  . TRP A 112 ? 0.2310 0.1775 0.2822 -0.0149 -0.0440 -0.0365 111 TRP A DH2  
1975 N N    . ARG A 113 ? 0.1175 0.1134 0.1707 0.0102  0.0092  0.0142  112 ARG A N    
1976 C CA   . ARG A 113 ? 0.1386 0.1411 0.1996 0.0044  0.0006  -0.0234 112 ARG A CA   
1977 C C    . ARG A 113 ? 0.1454 0.1174 0.2314 0.0099  0.0020  -0.0241 112 ARG A C    
1978 O O    . ARG A 113 ? 0.2035 0.1203 0.3410 0.0215  -0.0353 -0.0411 112 ARG A O    
1979 C CB   . ARG A 113 ? 0.2069 0.3071 0.1844 0.0368  0.0029  -0.0045 112 ARG A CB   
1980 C CG   . ARG A 113 ? 0.3870 0.4079 0.2208 0.0431  0.0155  -0.0721 112 ARG A CG   
1981 C CD   . ARG A 113 ? 0.5627 0.4776 0.2198 0.0842  0.0741  -0.0590 112 ARG A CD   
1982 N NE   . ARG A 113 ? 0.6560 0.4902 0.2901 0.1182  0.0616  0.0016  112 ARG A NE   
1983 C CZ   . ARG A 113 ? 0.6913 0.4819 0.3896 0.0736  0.0876  -0.0165 112 ARG A CZ   
1984 N NH1  . ARG A 113 ? 0.6853 0.4740 0.4267 0.0735  0.0806  -0.0039 112 ARG A NH1  
1985 N NH2  . ARG A 113 ? 0.7079 0.4775 0.4232 0.0609  0.1107  -0.0189 112 ARG A NH2  
1987 D DA   . ARG A 113 ? 0.1506 0.1376 0.2668 -0.0004 -0.0085 -0.0353 112 ARG A DA   
1988 D DB2  . ARG A 113 ? 0.2319 0.5224 0.2315 0.1092  0.0082  0.0651  112 ARG A DB2  
1989 D DB3  . ARG A 113 ? 0.2474 0.3279 0.2310 0.0115  0.0957  0.0138  112 ARG A DB3  
1990 D DG2  . ARG A 113 ? 0.4265 0.3445 0.4157 0.0959  0.0830  -0.0060 112 ARG A DG2  
1991 D DG3  . ARG A 113 ? 0.4696 0.3851 0.4310 -0.0087 -0.0042 -0.1069 112 ARG A DG3  
1992 D DD2  . ARG A 113 ? 0.5677 0.6121 0.4153 0.0476  0.1062  0.0944  112 ARG A DD2  
1993 D DD3  . ARG A 113 ? 0.9908 0.5270 0.2398 0.0974  -0.0509 -0.0634 112 ARG A DD3  
1994 D DE   . ARG A 113 ? 0.7389 0.5531 0.5140 0.2640  0.2044  0.2188  112 ARG A DE   
1995 D DH11 . ARG A 113 ? 0.3750 0.5058 0.5063 -0.0550 0.0378  0.0661  112 ARG A DH11 
1996 D DH12 . ARG A 113 ? 0.5721 0.5444 0.4407 0.0974  0.0614  -0.0125 112 ARG A DH12 
1997 D DH21 . ARG A 113 ? 0.8211 0.4903 0.7174 0.0959  0.2849  0.0441  112 ARG A DH21 
1998 D DH22 . ARG A 113 ? 0.7970 0.4861 0.6384 0.0900  0.2276  0.0057  112 ARG A DH22 
1999 N N    . ASN A 114 ? 0.1336 0.1029 0.2383 0.0237  -0.0032 -0.0205 113 ASN A N    
2000 C CA   . ASN A 114 ? 0.1285 0.1412 0.2645 0.0248  0.0032  -0.0322 113 ASN A CA   
2001 C C    . ASN A 114 ? 0.1270 0.1383 0.2691 0.0197  -0.0273 -0.0302 113 ASN A C    
2002 O O    . ASN A 114 ? 0.1883 0.1686 0.3327 0.0821  -0.0447 -0.0474 113 ASN A O    
2003 C CB   . ASN A 114 ? 0.1451 0.1962 0.3113 -0.0039 0.0144  -0.0107 113 ASN A CB   
2004 C CG   . ASN A 114 ? 0.2339 0.2796 0.3147 0.0310  0.0739  0.0123  113 ASN A CG   
2005 O OD1  . ASN A 114 ? 0.3147 0.3452 0.2637 -0.0033 0.0853  0.0056  113 ASN A OD1  
2006 N ND2  . ASN A 114 ? 0.3275 0.2771 0.3646 0.0334  0.1364  0.0215  113 ASN A ND2  
2007 D D    . ASN A 114 ? 0.1689 0.1046 0.2214 0.0185  0.0433  -0.0168 113 ASN A D    
2008 D DA   . ASN A 114 ? 0.1861 0.1544 0.2577 0.0562  0.0033  -0.0329 113 ASN A DA   
2009 D DB2  . ASN A 114 ? 0.1860 0.1808 0.3329 -0.0372 0.0340  -0.0163 113 ASN A DB2  
2010 D DB3  . ASN A 114 ? 0.1389 0.2644 0.3929 -0.0134 0.0015  0.0311  113 ASN A DB3  
2011 D DD21 . ASN A 114 ? 1.0642 0.3603 0.4506 -0.1031 0.3911  -0.0053 113 ASN A DD21 
2012 D DD22 . ASN A 114 ? 0.8886 0.3483 0.4455 -0.1255 0.2199  -0.0576 113 ASN A DD22 
2013 N N    A ARG A 115 ? 0.1152 0.1577 0.2493 0.0192  -0.0274 0.0032  114 ARG A N    
2014 N N    B ARG A 115 ? 0.1165 0.1488 0.2546 0.0075  -0.0197 0.0051  114 ARG A N    
2015 C CA   A ARG A 115 ? 0.1195 0.1756 0.2548 0.0106  -0.0462 0.0129  114 ARG A CA   
2016 C CA   B ARG A 115 ? 0.1263 0.1826 0.2601 0.0141  -0.0330 0.0143  114 ARG A CA   
2017 C C    A ARG A 115 ? 0.1437 0.1712 0.2399 0.0027  -0.0394 0.0116  114 ARG A C    
2018 C C    B ARG A 115 ? 0.1364 0.1780 0.2370 0.0200  -0.0320 0.0169  114 ARG A C    
2019 O O    A ARG A 115 ? 0.1653 0.2050 0.2447 0.0111  -0.0498 0.0243  114 ARG A O    
2020 O O    B ARG A 115 ? 0.1549 0.1705 0.2153 0.0245  -0.0457 -0.0004 114 ARG A O    
2021 C CB   A ARG A 115 ? 0.1221 0.2029 0.2716 -0.0057 -0.0507 -0.0052 114 ARG A CB   
2022 C CB   B ARG A 115 ? 0.1406 0.2107 0.2632 -0.0015 -0.0442 -0.0082 114 ARG A CB   
2023 C CG   A ARG A 115 ? 0.1292 0.2641 0.2805 -0.0480 -0.0322 -0.0378 114 ARG A CG   
2024 C CG   B ARG A 115 ? 0.1427 0.2364 0.2764 -0.0293 -0.0448 -0.0322 114 ARG A CG   
2025 C CD   A ARG A 115 ? 0.1331 0.3174 0.3073 -0.0308 -0.0317 -0.0539 114 ARG A CD   
2026 C CD   B ARG A 115 ? 0.1355 0.3193 0.2913 -0.0281 -0.0515 -0.0531 114 ARG A CD   
2027 N NE   A ARG A 115 ? 0.0888 0.3765 0.3058 -0.0579 -0.0255 -0.0486 114 ARG A NE   
2028 N NE   B ARG A 115 ? 0.1099 0.3576 0.2852 -0.0304 -0.0429 -0.0423 114 ARG A NE   
2029 C CZ   A ARG A 115 ? 0.1082 0.3724 0.2963 -0.0498 -0.0307 -0.0535 114 ARG A CZ   
2030 C CZ   B ARG A 115 ? 0.1166 0.3844 0.2870 -0.0320 -0.0434 -0.0500 114 ARG A CZ   
2031 N NH1  A ARG A 115 ? 0.1337 0.3711 0.3038 -0.0439 -0.0227 -0.0502 114 ARG A NH1  
2032 N NH1  B ARG A 115 ? 0.1520 0.3976 0.2802 -0.0070 -0.0510 -0.0556 114 ARG A NH1  
2033 N NH2  A ARG A 115 ? 0.1539 0.3828 0.2858 -0.0261 -0.0455 -0.0678 114 ARG A NH2  
2034 N NH2  B ARG A 115 ? 0.1246 0.3853 0.3014 -0.0357 -0.0477 -0.0701 114 ARG A NH2  
2035 D D    A ARG A 115 ? 0.1203 0.1882 0.2496 0.0338  -0.0046 0.0372  114 ARG A D    
2036 D D    B ARG A 115 ? 0.1651 0.2831 0.2462 0.0885  -0.0177 0.0011  114 ARG A D    
2037 D DA   A ARG A 115 ? 0.1175 0.1680 0.3006 0.0072  -0.0663 0.0173  114 ARG A DA   
2038 D DA   B ARG A 115 ? 0.1480 0.2007 0.2855 0.0401  -0.0078 0.0629  114 ARG A DA   
2039 D DB2  A ARG A 115 ? 0.1078 0.1941 0.2783 -0.0193 -0.0545 -0.0090 114 ARG A DB2  
2040 D DB2  B ARG A 115 ? 0.1591 0.1622 0.2719 0.0165  0.0121  0.0764  114 ARG A DB2  
2041 D DB3  A ARG A 115 ? 0.1441 0.2084 0.2727 -0.0006 -0.0677 -0.0227 114 ARG A DB3  
2042 D DB3  B ARG A 115 ? 0.2133 0.2266 0.2631 0.0582  -0.0393 -0.0050 114 ARG A DB3  
2043 D DG2  A ARG A 115 ? 0.0885 0.3008 0.2621 -0.0671 -0.0125 -0.0625 114 ARG A DG2  
2044 D DG2  B ARG A 115 ? 0.1261 0.2870 0.2806 -0.0466 -0.0256 0.0068  114 ARG A DG2  
2045 D DG3  A ARG A 115 ? 0.2019 0.2131 0.2208 -0.0182 -0.1055 0.0224  114 ARG A DG3  
2046 D DG3  B ARG A 115 ? 0.2565 0.2044 0.2808 0.0040  -0.0228 -0.0176 114 ARG A DG3  
2047 D DD2  A ARG A 115 ? 0.1635 0.3082 0.4221 -0.0252 -0.0025 -0.1005 114 ARG A DD2  
2048 D DD2  B ARG A 115 ? 0.1062 0.2512 0.2818 -0.0234 -0.0634 -0.0242 114 ARG A DD2  
2049 D DD3  A ARG A 115 ? 0.1584 0.4283 0.3158 -0.0481 -0.0115 -0.0603 114 ARG A DD3  
2050 D DD3  B ARG A 115 ? 0.1436 0.3221 0.2085 -0.0492 -0.0684 -0.0911 114 ARG A DD3  
2051 D DE   A ARG A 115 ? 0.2738 0.4113 0.3199 -0.1415 -0.0730 -0.0290 114 ARG A DE   
2052 D DE   B ARG A 115 ? 0.1299 0.3537 0.2320 -0.0301 -0.0007 -0.0558 114 ARG A DE   
2053 D DH11 A ARG A 115 ? 0.1665 0.4069 0.2845 -0.0868 0.0165  -0.0744 114 ARG A DH11 
2054 D DH11 B ARG A 115 ? 0.2888 0.4450 0.3363 0.0126  -0.1384 -0.0747 114 ARG A DH11 
2055 D DH12 A ARG A 115 ? 0.1187 0.4607 0.3024 -0.0083 0.0245  0.0101  114 ARG A DH12 
2056 D DH12 B ARG A 115 ? 0.2663 0.3934 0.3587 -0.0240 -0.1085 -0.0299 114 ARG A DH12 
2057 D DH21 A ARG A 115 ? 0.1733 0.4036 0.2539 -0.0182 -0.0406 -0.1086 114 ARG A DH21 
2058 D DH21 B ARG A 115 ? 0.1937 0.3880 0.0967 -0.0146 0.0829  -0.0073 114 ARG A DH21 
2059 D DH22 A ARG A 115 ? 0.2062 0.4029 0.4027 -0.0311 -0.0701 -0.0136 114 ARG A DH22 
2060 D DH22 B ARG A 115 ? 0.1220 0.4280 0.2932 -0.0620 -0.0794 -0.1449 114 ARG A DH22 
2061 N N    . CYS A 116 ? 0.1308 0.1345 0.2096 0.0176  -0.0184 0.0093  115 CYS A N    
2062 C CA   . CYS A 116 ? 0.1370 0.1382 0.1688 0.0109  -0.0275 0.0007  115 CYS A CA   
2063 C C    . CYS A 116 ? 0.1636 0.1181 0.1588 0.0134  -0.0117 0.0103  115 CYS A C    
2064 O O    . CYS A 116 ? 0.1867 0.1325 0.1447 -0.0070 0.0289  -0.0173 115 CYS A O    
2065 C CB   . CYS A 116 ? 0.1445 0.1174 0.1443 0.0015  -0.0074 0.0113  115 CYS A CB   
2066 S SG   . CYS A 116 ? 0.1664 0.1309 0.1444 -0.0104 0.0033  0.0102  115 CYS A SG   
2067 D D    . CYS A 116 ? 0.1632 0.1811 0.2153 0.0591  0.0081  0.0312  115 CYS A D    
2068 D DA   . CYS A 116 ? 0.2165 0.1545 0.1760 0.0291  -0.0429 0.0058  115 CYS A DA   
2069 D DB2  . CYS A 116 ? 0.1336 0.1516 0.1447 0.0262  -0.0031 0.0079  115 CYS A DB2  
2070 D DB3  . CYS A 116 ? 0.1592 0.1367 0.1782 0.0024  0.0145  0.0103  115 CYS A DB3  
2071 N N    . LYS A 117 ? 0.1745 0.1199 0.1552 0.0076  -0.0046 0.0080  116 LYS A N    
2072 C CA   . LYS A 117 ? 0.1869 0.1214 0.1619 -0.0100 0.0332  -0.0101 116 LYS A CA   
2073 C C    . LYS A 117 ? 0.2417 0.1278 0.1392 0.0138  0.0337  -0.0178 116 LYS A C    
2074 O O    . LYS A 117 ? 0.2557 0.2127 0.2209 0.0640  0.0667  0.0413  116 LYS A O    
2075 C CB   . LYS A 117 ? 0.1881 0.1443 0.1623 0.0039  0.0073  0.0000  116 LYS A CB   
2076 C CG   . LYS A 117 ? 0.2419 0.1615 0.1744 0.0123  -0.0293 -0.0052 116 LYS A CG   
2077 C CD   . LYS A 117 ? 0.2866 0.2777 0.1618 0.0892  -0.0445 0.0197  116 LYS A CD   
2078 C CE   . LYS A 117 ? 0.3829 0.2944 0.1707 0.0936  -0.0395 -0.0025 116 LYS A CE   
2079 N NZ   . LYS A 117 ? 0.4228 0.3084 0.1819 0.1049  -0.0106 -0.0135 116 LYS A NZ   
2081 D D    B LYS A 117 ? 0.1391 0.1054 0.1711 0.0230  0.0056  0.0033  116 LYS A D    
2082 D DA   . LYS A 117 ? 0.1881 0.1459 0.2156 -0.0266 0.0337  -0.0227 116 LYS A DA   
2083 D DB2  . LYS A 117 ? 0.2295 0.1430 0.2057 0.0155  0.0158  0.0063  116 LYS A DB2  
2084 D DB3  . LYS A 117 ? 0.1914 0.1839 0.1629 0.0032  0.0270  0.0225  116 LYS A DB3  
2085 D DG2  . LYS A 117 ? 0.2863 0.1510 0.1800 0.0121  -0.0038 0.0005  116 LYS A DG2  
2086 D DG3  . LYS A 117 ? 0.2511 0.2113 0.2343 -0.0139 -0.0156 -0.0604 116 LYS A DG3  
2087 D DD2  . LYS A 117 ? 0.3405 0.3022 0.1453 0.1287  -0.0487 0.0102  116 LYS A DD2  
2088 D DD3  . LYS A 117 ? 0.2945 0.3573 0.1716 0.0905  0.0069  0.0252  116 LYS A DD3  
2089 D DE2  . LYS A 117 ? 0.4798 0.2666 0.2987 0.0881  -0.0133 0.0270  116 LYS A DE2  
2090 D DE3  . LYS A 117 ? 0.3804 0.3212 0.2672 0.0437  -0.0216 -0.0944 116 LYS A DE3  
2091 D DZ1  . LYS A 117 ? 0.4439 0.3183 0.2137 0.1233  0.0743  0.0334  116 LYS A DZ1  
2092 D DZ2  . LYS A 117 ? 0.4225 0.3311 0.2298 0.0859  0.0060  -0.0349 116 LYS A DZ2  
2093 D DZ3  . LYS A 117 ? 0.4194 0.3440 0.2118 0.0915  0.0136  -0.0456 116 LYS A DZ3  
2094 N N    . GLY A 118 ? 0.3102 0.1243 0.1681 -0.0088 0.0474  -0.0158 117 GLY A N    
2095 C CA   . GLY A 118 ? 0.3609 0.1218 0.2055 0.0102  0.0601  -0.0240 117 GLY A CA   
2096 C C    . GLY A 118 ? 0.2991 0.1098 0.2161 0.0152  0.0639  -0.0060 117 GLY A C    
2097 O O    . GLY A 118 ? 0.3317 0.1143 0.2620 0.0149  0.0390  -0.0042 117 GLY A O    
2098 D D    . GLY A 118 ? 0.2973 0.1510 0.3842 -0.0182 0.0616  0.0555  117 GLY A D    
2099 D DA2  . GLY A 118 ? 0.4508 0.1412 0.2921 -0.0295 -0.0206 -0.0175 117 GLY A DA2  
2100 D DA3  . GLY A 118 ? 0.4679 0.1989 0.2288 0.0916  0.1074  -0.0154 117 GLY A DA3  
2101 N N    . THR A 119 ? 0.2743 0.1402 0.1885 0.0566  0.0641  -0.0113 118 THR A N    
2102 C CA   . THR A 119 ? 0.2569 0.1810 0.1962 0.0694  0.0591  0.0003  118 THR A CA   
2103 C C    . THR A 119 ? 0.2273 0.2020 0.1677 0.0777  0.0278  0.0037  118 THR A C    
2104 O O    . THR A 119 ? 0.2353 0.1741 0.1826 0.0013  0.0030  -0.0050 118 THR A O    
2105 C CB   . THR A 119 ? 0.2441 0.2040 0.2074 0.0645  0.0389  -0.0100 118 THR A CB   
2106 O OG1  . THR A 119 ? 0.2595 0.1892 0.2083 0.0577  0.0290  -0.0232 118 THR A OG1  
2107 C CG2  . THR A 119 ? 0.2580 0.1985 0.2422 0.0501  0.0543  -0.0034 118 THR A CG2  
2108 D D    . THR A 119 ? 0.3420 0.1369 0.2165 0.0537  0.0268  -0.0108 118 THR A D    
2109 D DA   . THR A 119 ? 0.2475 0.1930 0.2641 0.0722  0.0602  0.0184  118 THR A DA   
2110 D DB   . THR A 119 ? 0.2061 0.3050 0.2325 0.0544  0.0313  0.0286  118 THR A DB   
2111 D DG1  . THR A 119 ? 0.2842 0.2034 0.2208 0.0642  0.0280  0.0024  118 THR A DG1  
2112 D DG21 . THR A 119 ? 0.2464 0.3123 0.2498 -0.0056 0.0557  0.0523  118 THR A DG21 
2113 D DG22 . THR A 119 ? 0.3173 0.2454 0.3295 -0.0059 0.0423  -0.0220 118 THR A DG22 
2114 D DG23 . THR A 119 ? 0.2956 0.2269 0.3574 0.0847  0.1260  0.0322  118 THR A DG23 
2115 N N    . ASP A 120 ? 0.2643 0.2023 0.1756 0.0701  0.0150  0.0209  119 ASP A N    
2116 C CA   . ASP A 120 ? 0.2798 0.1970 0.1743 0.0692  0.0207  0.0346  119 ASP A CA   
2117 C C    . ASP A 120 ? 0.2159 0.1903 0.1428 0.0452  0.0057  0.0360  119 ASP A C    
2118 O O    . ASP A 120 ? 0.2152 0.2493 0.1425 0.0616  -0.0006 0.0180  119 ASP A O    
2119 C CB   . ASP A 120 ? 0.3837 0.2161 0.2010 0.0956  0.0151  0.0605  119 ASP A CB   
2120 C CG   . ASP A 120 ? 0.4057 0.2999 0.2009 0.0833  0.0248  0.0914  119 ASP A CG   
2123 D D    . ASP A 120 ? 0.2671 0.2540 0.1945 0.0667  -0.0019 0.0366  119 ASP A D    
2124 D DA   . ASP A 120 ? 0.3057 0.2008 0.1967 0.0277  0.0350  0.0206  119 ASP A DA   
2125 D DB2  . ASP A 120 ? 0.4969 0.2184 0.2834 0.1131  0.0166  0.0511  119 ASP A DB2  
2126 D DB3  . ASP A 120 ? 0.3982 0.3200 0.1619 0.0587  0.0045  0.0905  119 ASP A DB3  
2127 N N    . VAL A 121 ? 0.2122 0.1851 0.1619 0.0381  -0.0120 0.0285  120 VAL A N    
2128 C CA   . VAL A 121 ? 0.2185 0.1789 0.1761 0.0360  -0.0068 0.0429  120 VAL A CA   
2129 C C    . VAL A 121 ? 0.2174 0.1722 0.1730 0.0503  -0.0082 0.0412  120 VAL A C    
2130 O O    . VAL A 121 ? 0.2640 0.1735 0.1919 0.0587  -0.0039 0.0378  120 VAL A O    
2131 C CB   . VAL A 121 ? 0.2666 0.2173 0.1815 0.0635  -0.0136 0.0572  120 VAL A CB   
2132 C CG1  . VAL A 121 ? 0.3011 0.2277 0.1920 0.0629  0.0060  0.0680  120 VAL A CG1  
2133 C CG2  . VAL A 121 ? 0.2551 0.2805 0.2053 0.0634  -0.0353 0.0456  120 VAL A CG2  
2134 D D    . VAL A 121 ? 0.3354 0.2086 0.2130 0.0362  -0.0811 0.0120  120 VAL A D    
2135 D DA   . VAL A 121 ? 0.2301 0.2079 0.1896 0.0172  0.0097  0.0027  120 VAL A DA   
2136 D DB   . VAL A 121 ? 0.2591 0.2231 0.2331 0.0830  -0.0076 0.0565  120 VAL A DB   
2137 D DG11 . VAL A 121 ? 0.3200 0.2371 0.2085 0.0796  0.0381  0.0709  120 VAL A DG11 
2138 D DG12 . VAL A 121 ? 0.3253 0.2567 0.1907 0.0989  0.0100  0.0577  120 VAL A DG12 
2139 D DG13 . VAL A 121 ? 0.3402 0.3059 0.1903 0.0137  0.0032  0.0525  120 VAL A DG13 
2140 D DG21 . VAL A 121 ? 0.3101 0.2909 0.2962 0.0477  -0.0598 0.0015  120 VAL A DG21 
2141 D DG22 . VAL A 121 ? 0.2467 0.3759 0.2605 0.0635  -0.0080 0.0647  120 VAL A DG22 
2142 D DG23 . VAL A 121 ? 0.2715 0.4258 0.2729 0.0646  -0.0580 0.1244  120 VAL A DG23 
2143 N N    . GLN A 122 ? 0.2520 0.1767 0.1860 0.0434  0.0157  0.0396  121 GLN A N    
2144 C CA   . GLN A 122 ? 0.2378 0.2191 0.2091 0.0262  0.0347  0.0361  121 GLN A CA   
2145 C C    . GLN A 122 ? 0.2471 0.1764 0.1895 0.0679  0.0303  0.0383  121 GLN A C    
2146 O O    . GLN A 122 ? 0.2904 0.1614 0.2159 0.0352  0.0659  0.0257  121 GLN A O    
2147 C CB   . GLN A 122 ? 0.2927 0.2682 0.2961 -0.0327 0.0517  0.0498  121 GLN A CB   
2152 D D    . GLN A 122 ? 0.2405 0.1869 0.2996 0.0228  0.0904  0.0117  121 GLN A D    
2153 D DA   . GLN A 122 ? 0.2455 0.2734 0.2184 0.0559  0.0177  0.0119  121 GLN A DA   
2154 D DB2  . GLN A 122 ? 0.3208 0.2204 0.2243 -0.0511 0.0059  0.0187  121 GLN A DB2  
2155 D DB3  . GLN A 122 ? 0.3260 0.3071 0.3705 -0.0990 0.1103  0.0042  121 GLN A DB3  
2160 N N    . ALA A 123 ? 0.2464 0.1712 0.1873 0.0677  0.0183  0.0468  122 ALA A N    
2161 C CA   . ALA A 123 ? 0.2694 0.2140 0.1801 0.0881  -0.0060 0.0526  122 ALA A CA   
2162 C C    . ALA A 123 ? 0.2402 0.2110 0.1595 0.0650  -0.0332 0.0474  122 ALA A C    
2163 O O    . ALA A 123 ? 0.2546 0.2368 0.1626 0.0695  -0.0534 0.0495  122 ALA A O    
2164 C CB   . ALA A 123 ? 0.2657 0.2758 0.1991 0.1031  -0.0209 0.0227  122 ALA A CB   
2165 D D    . ALA A 123 ? 0.2169 0.2052 0.2082 0.0650  0.0172  0.0221  122 ALA A D    
2166 D DA   . ALA A 123 ? 0.3250 0.2267 0.1964 0.0827  0.0044  0.0745  122 ALA A DA   
2167 D DB1  . ALA A 123 ? 0.2119 0.3736 0.2172 0.0812  -0.0244 0.0596  122 ALA A DB1  
2168 D DB2  . ALA A 123 ? 0.2866 0.3403 0.2227 0.1161  -0.0496 0.0102  122 ALA A DB2  
2169 D DB3  . ALA A 123 ? 0.2937 0.2769 0.3165 0.1201  -0.0125 0.0107  122 ALA A DB3  
2170 N N    A TRP A 124 ? 0.1958 0.1914 0.1482 0.0366  -0.0277 0.0430  123 TRP A N    
2171 N N    B TRP A 124 ? 0.2006 0.1939 0.1480 0.0407  -0.0277 0.0421  123 TRP A N    
2172 C CA   A TRP A 124 ? 0.2090 0.1904 0.1536 0.0286  -0.0109 0.0420  123 TRP A CA   
2173 C CA   B TRP A 124 ? 0.2063 0.1919 0.1518 0.0280  -0.0137 0.0415  123 TRP A CA   
2174 C C    A TRP A 124 ? 0.2015 0.1771 0.1418 0.0160  -0.0238 0.0233  123 TRP A C    
2175 C C    B TRP A 124 ? 0.2199 0.1805 0.1459 0.0206  -0.0124 0.0305  123 TRP A C    
2176 O O    A TRP A 124 ? 0.2063 0.1735 0.1269 0.0202  -0.0435 0.0304  123 TRP A O    
2177 O O    B TRP A 124 ? 0.1750 0.1844 0.1496 0.0391  -0.0630 0.0275  123 TRP A O    
2178 C CB   A TRP A 124 ? 0.2289 0.1893 0.1550 0.0249  -0.0118 0.0467  123 TRP A CB   
2179 C CB   B TRP A 124 ? 0.2218 0.1896 0.1503 0.0180  -0.0160 0.0447  123 TRP A CB   
2180 C CG   A TRP A 124 ? 0.2311 0.1882 0.1562 0.0127  -0.0060 0.0533  123 TRP A CG   
2181 C CG   B TRP A 124 ? 0.2237 0.1890 0.1550 0.0115  -0.0080 0.0542  123 TRP A CG   
2182 C CD1  A TRP A 124 ? 0.2325 0.1939 0.1549 0.0007  0.0043  0.0523  123 TRP A CD1  
2183 C CD1  B TRP A 124 ? 0.2189 0.1914 0.1516 -0.0032 0.0010  0.0525  123 TRP A CD1  
2184 C CD2  A TRP A 124 ? 0.2451 0.1877 0.1618 -0.0026 0.0057  0.0501  123 TRP A CD2  
2185 C CD2  B TRP A 124 ? 0.2378 0.1919 0.1594 -0.0013 -0.0003 0.0455  123 TRP A CD2  
2186 N NE1  A TRP A 124 ? 0.2299 0.2057 0.1595 0.0015  0.0001  0.0433  123 TRP A NE1  
2187 N NE1  B TRP A 124 ? 0.2216 0.1933 0.1600 -0.0127 0.0050  0.0414  123 TRP A NE1  
2188 C CE2  A TRP A 124 ? 0.2446 0.1982 0.1707 -0.0123 0.0120  0.0421  123 TRP A CE2  
2189 C CE2  B TRP A 124 ? 0.2293 0.1936 0.1616 -0.0124 0.0025  0.0417  123 TRP A CE2  
2190 C CE3  A TRP A 124 ? 0.2611 0.2150 0.1805 -0.0042 0.0034  0.0278  123 TRP A CE3  
2191 C CE3  B TRP A 124 ? 0.2525 0.2015 0.1599 -0.0002 -0.0051 0.0385  123 TRP A CE3  
2192 C CZ2  A TRP A 124 ? 0.2475 0.2199 0.1790 -0.0151 0.0073  0.0284  123 TRP A CZ2  
2193 C CZ2  B TRP A 124 ? 0.2357 0.2131 0.1856 -0.0245 0.0006  0.0188  123 TRP A CZ2  
2194 C CZ3  A TRP A 124 ? 0.2717 0.2131 0.1646 -0.0145 0.0014  0.0329  123 TRP A CZ3  
2195 C CZ3  B TRP A 124 ? 0.2621 0.2173 0.1810 -0.0162 0.0007  0.0204  123 TRP A CZ3  
2196 C CH2  A TRP A 124 ? 0.2572 0.2205 0.1857 -0.0171 0.0010  0.0261  123 TRP A CH2  
2197 C CH2  B TRP A 124 ? 0.2562 0.2147 0.1917 -0.0295 0.0083  0.0123  123 TRP A CH2  
2200 D DA   A TRP A 124 ? 0.2057 0.1830 0.1675 0.0520  -0.0211 0.0221  123 TRP A DA   
2201 D DA   B TRP A 124 ? 0.2185 0.2212 0.1660 0.0218  -0.0288 0.0252  123 TRP A DA   
2202 D DB2  A TRP A 124 ? 0.2175 0.2080 0.1686 0.0263  -0.0172 0.0493  123 TRP A DB2  
2203 D DB2  B TRP A 124 ? 0.2130 0.2006 0.1939 0.0272  -0.0394 0.0490  123 TRP A DB2  
2204 D DB3  A TRP A 124 ? 0.2702 0.1909 0.1759 0.0318  0.0059  0.0485  123 TRP A DB3  
2205 D DB3  B TRP A 124 ? 0.2530 0.1913 0.1674 0.0249  -0.0092 0.0457  123 TRP A DB3  
2206 D DD1  A TRP A 124 ? 0.2121 0.2422 0.2125 0.0131  0.0151  -0.0101 123 TRP A DD1  
2207 D DD1  B TRP A 124 ? 0.2193 0.2560 0.3036 -0.0231 0.0290  -0.0381 123 TRP A DD1  
2208 D DE1  A TRP A 124 ? 0.2767 0.2070 0.2417 -0.0452 0.0725  0.0035  123 TRP A DE1  
2209 D DE1  B TRP A 124 ? 0.2428 0.1734 0.1729 -0.0244 0.0322  0.0484  123 TRP A DE1  
2210 D DE3  A TRP A 124 ? 0.2811 0.2052 0.2024 -0.0193 0.0243  0.0112  123 TRP A DE3  
2211 D DE3  B TRP A 124 ? 0.2744 0.1510 0.1853 -0.0022 0.0224  0.0627  123 TRP A DE3  
2212 D DZ2  A TRP A 124 ? 0.2192 0.4682 0.2716 -0.0380 -0.0003 -0.1371 123 TRP A DZ2  
2213 D DZ2  B TRP A 124 ? 0.1978 0.2827 0.3265 -0.1027 0.0286  -0.1093 123 TRP A DZ2  
2214 D DZ3  A TRP A 124 ? 0.3263 0.2489 0.1711 -0.0426 0.0092  0.0132  123 TRP A DZ3  
2215 D DZ3  B TRP A 124 ? 0.3492 0.3428 0.2264 -0.1362 0.1062  -0.0680 123 TRP A DZ3  
2216 D DH2  A TRP A 124 ? 0.2722 0.4159 0.3667 -0.0697 0.0246  -0.1253 123 TRP A DH2  
2217 D DH2  B TRP A 124 ? 0.2750 0.3211 0.4204 -0.0764 0.0583  -0.1379 123 TRP A DH2  
2218 N N    A ILE A 125 ? 0.2357 0.1603 0.1266 0.0261  0.0050  0.0399  124 ILE A N    
2219 N N    B ILE A 125 ? 0.2421 0.1639 0.1356 0.0240  0.0099  0.0323  124 ILE A N    
2220 C CA   A ILE A 125 ? 0.2340 0.1601 0.1323 0.0177  0.0030  0.0142  124 ILE A CA   
2221 C CA   B ILE A 125 ? 0.2413 0.1605 0.1424 0.0209  0.0092  0.0177  124 ILE A CA   
2222 C C    A ILE A 125 ? 0.2316 0.1460 0.1321 -0.0057 0.0171  0.0148  124 ILE A C    
2223 C C    B ILE A 125 ? 0.2490 0.1562 0.1337 0.0074  0.0165  0.0090  124 ILE A C    
2224 O O    A ILE A 125 ? 0.2292 0.1360 0.1553 -0.0500 0.0381  -0.0019 124 ILE A O    
2225 O O    B ILE A 125 ? 0.2752 0.1765 0.1523 -0.0030 0.0397  -0.0023 124 ILE A O    
2226 C CB   A ILE A 125 ? 0.2400 0.1861 0.1662 0.0390  -0.0158 -0.0230 124 ILE A CB   
2227 C CB   B ILE A 125 ? 0.2531 0.1884 0.1450 0.0414  -0.0069 -0.0228 124 ILE A CB   
2228 C CG1  A ILE A 125 ? 0.2641 0.1944 0.2175 0.0347  -0.0277 -0.0451 124 ILE A CG1  
2229 C CG1  B ILE A 125 ? 0.2738 0.1961 0.1988 0.0435  -0.0226 -0.0480 124 ILE A CG1  
2230 C CG2  A ILE A 125 ? 0.2762 0.2061 0.1497 0.0578  -0.0319 -0.0303 124 ILE A CG2  
2231 C CG2  B ILE A 125 ? 0.2779 0.1997 0.1405 0.0713  -0.0066 -0.0184 124 ILE A CG2  
2232 C CD1  A ILE A 125 ? 0.2648 0.2031 0.2459 0.0407  -0.0363 -0.0736 124 ILE A CD1  
2233 C CD1  B ILE A 125 ? 0.2763 0.2192 0.2271 0.0423  -0.0364 -0.0663 124 ILE A CD1  
2236 D DA   A ILE A 125 ? 0.2835 0.1573 0.0913 0.0228  -0.0211 0.0261  124 ILE A DA   
2237 D DA   B ILE A 125 ? 0.2644 0.1522 0.1425 0.0322  -0.0217 0.0233  124 ILE A DA   
2238 D DB   A ILE A 125 ? 0.2400 0.1999 0.1625 0.0601  -0.0249 -0.0155 124 ILE A DB   
2239 D DB   B ILE A 125 ? 0.2361 0.2141 0.1352 0.0240  -0.0163 -0.0391 124 ILE A DB   
2240 D DG12 A ILE A 125 ? 0.3070 0.1820 0.2548 0.0376  0.0108  -0.0534 124 ILE A DG12 
2241 D DG12 B ILE A 125 ? 0.2895 0.2445 0.2138 0.0296  -0.0156 -0.0838 124 ILE A DG12 
2242 D DG13 A ILE A 125 ? 0.2668 0.1856 0.2649 0.0246  -0.0338 -0.0161 124 ILE A DG13 
2243 D DG13 B ILE A 125 ? 0.2953 0.1946 0.2254 0.0217  -0.0411 -0.0364 124 ILE A DG13 
2244 D DG21 A ILE A 125 ? 0.3541 0.2450 0.1439 0.1206  -0.0199 -0.0096 124 ILE A DG21 
2245 D DG21 B ILE A 125 ? 0.2834 0.2092 0.1284 0.0756  -0.0136 -0.0221 124 ILE A DG21 
2246 D DG22 A ILE A 125 ? 0.2924 0.2256 0.1953 0.0631  -0.0559 -0.0278 124 ILE A DG22 
2247 D DG22 B ILE A 125 ? 0.2799 0.2273 0.1946 0.0865  -0.0066 0.0004  124 ILE A DG22 
2248 D DG23 A ILE A 125 ? 0.3268 0.2107 0.1557 0.0314  -0.0370 -0.0082 124 ILE A DG23 
2249 D DG23 B ILE A 125 ? 0.3188 0.2018 0.1356 0.0455  0.0170  -0.0162 124 ILE A DG23 
2250 D DD11 A ILE A 125 ? 0.2756 0.3658 0.2563 0.1276  -0.0419 -0.0602 124 ILE A DD11 
2251 D DD11 B ILE A 125 ? 0.2957 0.2537 0.2277 0.0249  -0.0650 -0.0621 124 ILE A DD11 
2252 D DD12 A ILE A 125 ? 0.2672 0.2104 0.3897 0.0438  0.0257  -0.0499 124 ILE A DD12 
2253 D DD12 B ILE A 125 ? 0.2887 0.2296 0.2829 0.0313  -0.0224 -0.0739 124 ILE A DD12 
2254 D DD13 A ILE A 125 ? 0.2743 0.2253 0.3239 0.0239  -0.0156 -0.1242 124 ILE A DD13 
2255 D DD13 B ILE A 125 ? 0.2797 0.2603 0.2585 0.0388  -0.0296 -0.0988 124 ILE A DD13 
2256 N N    . ARG A 126 ? 0.2714 0.1612 0.1292 0.0191  0.0064  0.0205  125 ARG A N    
2257 C CA   . ARG A 126 ? 0.4248 0.1736 0.1497 0.0420  0.0166  0.0410  125 ARG A CA   
2258 C C    . ARG A 126 ? 0.4729 0.1825 0.1386 0.0463  -0.0323 0.0583  125 ARG A C    
2259 O O    . ARG A 126 ? 0.4771 0.2274 0.1770 0.0167  -0.0476 0.0494  125 ARG A O    
2260 C CB   . ARG A 126 ? 0.4762 0.2204 0.1988 0.1052  -0.0079 0.0562  125 ARG A CB   
2261 C CG   . ARG A 126 ? 0.5749 0.2550 0.2440 0.1147  0.0017  0.0956  125 ARG A CG   
2262 C CD   . ARG A 126 ? 0.6430 0.2843 0.3094 0.1838  -0.0248 0.1145  125 ARG A CD   
2263 N NE   . ARG A 126 ? 0.7553 0.2152 0.3131 0.1660  0.0224  0.1017  125 ARG A NE   
2264 C CZ   . ARG A 126 ? 0.7819 0.2535 0.3531 0.1242  0.0619  0.0818  125 ARG A CZ   
2265 N NH1  . ARG A 126 ? 0.7849 0.2909 0.4021 0.1111  0.0788  0.0704  125 ARG A NH1  
2266 N NH2  . ARG A 126 ? 0.8169 0.2576 0.3229 0.1501  0.0545  0.0957  125 ARG A NH2  
2268 D D    B ARG A 126 ? 0.2060 0.2862 0.1292 0.0595  -0.0157 0.0351  125 ARG A D    
2269 D DA   . ARG A 126 ? 0.4443 0.2172 0.1653 0.0080  0.0276  0.0484  125 ARG A DA   
2270 D DB2  . ARG A 126 ? 0.4843 0.2643 0.1994 0.1346  0.0237  0.0323  125 ARG A DB2  
2271 D DB3  . ARG A 126 ? 0.4469 0.2843 0.2377 0.1128  -0.0276 0.1064  125 ARG A DB3  
2272 D DG2  . ARG A 126 ? 0.7634 0.3248 0.2255 0.0636  -0.0163 0.1011  125 ARG A DG2  
2273 D DG3  . ARG A 126 ? 0.5752 0.2939 0.3934 0.1122  -0.0036 0.1892  125 ARG A DG3  
2274 D DD2  . ARG A 126 ? 0.6228 0.3692 0.4184 0.1907  -0.0195 0.1103  125 ARG A DD2  
2275 D DD3  . ARG A 126 ? 0.6140 0.4206 0.3436 0.2404  -0.0413 0.1994  125 ARG A DD3  
2276 D DE   . ARG A 126 ? 0.7792 0.5064 0.2478 0.0854  0.0391  -0.0041 125 ARG A DE   
2277 D DH11 . ARG A 126 ? 0.8041 0.4408 0.5768 0.0372  0.1584  -0.0777 125 ARG A DH11 
2278 D DH12 . ARG A 126 ? 0.7804 0.3550 0.4971 0.0903  0.0662  -0.0019 125 ARG A DH12 
2279 D DH21 . ARG A 126 ? 1.2064 0.8343 0.3684 -0.1235 0.1968  -0.0096 125 ARG A DH21 
2280 D DH22 . ARG A 126 ? 1.0394 0.7386 0.4146 -0.1181 0.0162  0.0563  125 ARG A DH22 
2281 N N    . GLY A 127 ? 0.5550 0.1472 0.1388 0.0209  -0.0037 0.0275  126 GLY A N    
2282 C CA   . GLY A 127 ? 0.5694 0.1956 0.1465 0.0135  -0.0126 0.0092  126 GLY A CA   
2283 C C    . GLY A 127 ? 0.5572 0.1696 0.1302 -0.0171 0.0174  0.0019  126 GLY A C    
2284 O O    . GLY A 127 ? 0.5977 0.2151 0.1867 -0.0334 -0.0286 -0.0559 126 GLY A O    
2285 D D    . GLY A 127 ? 0.6368 0.2468 0.1765 -0.0714 0.0473  -0.0274 126 GLY A D    
2286 D DA2  . GLY A 127 ? 0.6252 0.2180 0.1511 0.0940  0.0517  0.0181  126 GLY A DA2  
2287 D DA3  . GLY A 127 ? 0.5736 0.2998 0.1923 0.0114  -0.0455 -0.0022 126 GLY A DA3  
2288 N N    . CYS A 128 ? 0.4942 0.1621 0.1452 -0.0217 0.0340  0.0153  127 CYS A N    
2289 C CA   . CYS A 128 ? 0.4143 0.1430 0.2356 -0.0612 0.0663  0.0337  127 CYS A CA   
2290 C C    . CYS A 128 ? 0.4211 0.2013 0.2411 -0.0839 0.0760  0.0463  127 CYS A C    
2291 O O    . CYS A 128 ? 0.4476 0.2165 0.3558 -0.1103 0.0786  0.0431  127 CYS A O    
2292 C CB   . CYS A 128 ? 0.3425 0.0999 0.2373 -0.0719 0.0615  0.0245  127 CYS A CB   
2293 S SG   . CYS A 128 ? 0.3204 0.1416 0.2324 -0.0541 0.0528  -0.0056 127 CYS A SG   
2294 D D    . CYS A 128 ? 0.5371 0.1783 0.1419 -0.0527 0.0214  0.0100  127 CYS A D    
2295 D DA   . CYS A 128 ? 0.3705 0.1887 0.2320 -0.0339 0.1034  -0.0240 127 CYS A DA   
2296 D DB2  . CYS A 128 ? 0.3679 0.1495 0.2604 -0.0953 0.0644  -0.0026 127 CYS A DB2  
2297 D DB3  . CYS A 128 ? 0.3091 0.1411 0.2359 -0.0530 0.0488  0.0185  127 CYS A DB3  
2298 N N    . ARG A 129 ? 0.3911 0.2841 0.2485 -0.0576 0.0525  -0.0062 128 ARG A N    
2299 C CA   . ARG A 129 ? 0.3838 0.3264 0.3278 -0.0541 0.0502  0.0082  128 ARG A CA   
2300 C C    . ARG A 129 ? 0.4117 0.3662 0.3670 -0.0257 0.0259  0.0188  128 ARG A C    
2301 O O    . ARG A 129 ? 0.5934 0.4092 0.3984 -0.0191 0.0898  0.0980  128 ARG A O    
2309 D D    . ARG A 129 ? 0.3804 0.2730 0.3062 -0.0318 0.0579  -0.0585 128 ARG A D    
2310 D DA   . ARG A 129 ? 0.3722 0.3755 0.6069 -0.0363 0.0690  0.1569  128 ARG A DA   
2412 O O    . DOD K .   ? 0.2188 0.2038 0.3911 -0.0816 0.1167  -0.0565 320 DOD A O    
2413 D D1   . DOD K .   ? 0.1994 0.1923 0.3645 -0.0588 0.0510  -0.0354 320 DOD A D1   
2414 D D2   . DOD K .   ? 0.2560 0.2627 0.3904 -0.0311 0.1264  -0.0415 320 DOD A D2   
2420 O O    . DOD K .   ? 0.2710 0.2908 0.1437 0.0645  -0.0396 -0.0354 324 DOD A O    
2421 D D1   . DOD K .   ? 0.2023 0.2950 0.2152 0.0679  -0.0744 -0.0599 324 DOD A D1   
2422 D D2   . DOD K .   ? 0.2566 0.2713 0.1402 0.1075  -0.0381 -0.0470 324 DOD A D2   
2427 O O    . DOD K .   ? 0.1458 0.1624 0.1494 0.0239  -0.0114 -0.0107 327 DOD A O    
2428 D D1   . DOD K .   ? 0.1474 0.1586 0.1554 0.0160  -0.0212 0.0141  327 DOD A D1   
2429 D D2   . DOD K .   ? 0.1301 0.1694 0.1604 0.0098  -0.0049 0.0106  327 DOD A D2   
2443 O O    . DOD K .   ? 0.1518 0.3108 0.1143 0.0149  -0.0382 -0.0068 332 DOD A O    
2444 D D1   . DOD K .   ? 0.1883 0.3206 0.1147 -0.0027 -0.0379 -0.0035 332 DOD A D1   
2445 D D2   . DOD K .   ? 0.1724 0.2397 0.1395 0.0079  -0.0148 0.0118  332 DOD A D2   
2446 O O    . DOD K .   ? 0.2638 0.6697 0.4478 -0.0793 -0.0578 0.1913  333 DOD A O    
2447 D D1   . DOD K .   ? 0.2127 0.2624 0.2711 -0.0322 0.0321  -0.0074 333 DOD A D1   
2448 D D2   . DOD K .   ? 0.2711 0.3755 0.1403 -0.0370 -0.0263 -0.1072 333 DOD A D2   
2452 O O    . DOD K .   ? 0.1735 0.2304 0.2385 0.0223  -0.0822 0.0168  335 DOD A O    
2453 D D1   . DOD K .   ? 0.1768 0.2565 0.2381 0.0006  -0.0588 0.0186  335 DOD A D1   
2454 D D2   . DOD K .   ? 0.2289 0.2873 0.2965 0.0217  -0.0586 -0.0384 335 DOD A D2   
2455 O O    . DOD K .   ? 0.1351 0.1382 0.1654 -0.0136 -0.0135 0.0176  336 DOD A O    
2456 D D1   . DOD K .   ? 0.1881 0.1713 0.1623 0.0031  0.0004  0.0164  336 DOD A D1   
2457 D D2   . DOD K .   ? 0.1407 0.1851 0.1728 -0.0010 -0.0048 0.0382  336 DOD A D2   
2461 O O    . DOD K .   ? 0.3358 0.2163 0.1733 -0.0560 0.0298  0.0152  338 DOD A O    
2462 D D1   . DOD K .   ? 0.2979 0.2763 0.1798 -0.0037 0.0584  -0.0759 338 DOD A D1   
2463 D D2   . DOD K .   ? 0.2917 0.3170 0.1821 0.1230  0.0615  0.0400  338 DOD A D2   
2473 O O    . DOD K .   ? 0.1900 0.2346 0.0893 0.0116  -0.0170 -0.0191 342 DOD A O    
2474 D D1   . DOD K .   ? 0.2087 0.2625 0.1022 0.0269  -0.0330 -0.0407 342 DOD A D1   
2475 D D2   . DOD K .   ? 0.1942 0.2592 0.0989 0.0038  -0.0091 -0.0142 342 DOD A D2   
2481 O O    . DOD K .   ? 0.2599 0.7296 0.2845 -0.1237 0.2522  -0.1463 346 DOD A O    
2482 D D1   . DOD K .   ? 0.2237 0.6339 0.2508 -0.0938 0.0374  -0.0248 346 DOD A D1   
2483 D D2   . DOD K .   ? 0.1255 0.5968 0.2000 -0.0267 0.1024  -0.0544 346 DOD A D2   
2484 O O    . DOD K .   ? 0.3848 0.4543 0.1152 0.1657  -0.0992 -0.0408 347 DOD A O    
2485 D D1   . DOD K .   ? 0.3549 0.2237 0.1841 0.0560  -0.1274 -0.0328 347 DOD A D1   
2486 D D2   . DOD K .   ? 0.3985 0.4729 0.1750 0.1674  -0.0730 -0.0029 347 DOD A D2   
2487 O O    . DOD K .   ? 0.1936 0.3114 0.2153 -0.0763 0.0925  -0.1144 348 DOD A O    
2488 D D1   . DOD K .   ? 0.2350 0.3225 0.1981 -0.0357 0.0307  -0.1134 348 DOD A D1   
2489 D D2   . DOD K .   ? 0.1894 0.2550 0.2084 -0.0346 0.0794  -0.0123 348 DOD A D2   
2493 O O    . DOD K .   ? 0.4217 0.6765 0.4951 0.3148  -0.0731 -0.0572 350 DOD A O    
2494 D D1   . DOD K .   ? 0.1750 0.1952 0.3533 0.0021  0.0632  0.0134  350 DOD A D1   
2495 D D2   . DOD K .   ? 0.2443 0.2213 0.4235 0.0569  0.0295  0.1246  350 DOD A D2   
2496 O O    . DOD K .   ? 0.0892 0.1088 0.1468 0.0343  0.0164  0.0187  351 DOD A O    
2497 D D1   . DOD K .   ? 0.1354 0.1428 0.1358 0.0014  0.0037  0.0199  351 DOD A D1   
2498 D D2   . DOD K .   ? 0.1157 0.1309 0.1491 0.0047  -0.0162 0.0246  351 DOD A D2   
2520 O O    . DOD K .   ? 0.1960 0.1835 0.1122 -0.0280 0.0097  -0.0405 361 DOD A O    
2521 D D1   . DOD K .   ? 0.2491 0.1841 0.1270 -0.0227 -0.0569 -0.0218 361 DOD A D1   
2522 D D2   . DOD K .   ? 0.2185 0.2535 0.1196 0.0037  0.0320  -0.0169 361 DOD A D2   
2568 O O    A DOD K .   ? 0.1024 0.1528 0.4476 -0.0084 -0.0703 0.0990  382 DOD A O    
2569 O O    B DOD K .   ? 0.0604 0.2833 0.4291 -0.0434 0.0049  -0.0935 382 DOD A O    
2570 D D1   A DOD K .   ? 0.1435 0.1706 0.3511 0.0166  -0.0584 0.1144  382 DOD A D1   
2571 D D1   B DOD K .   ? 0.0602 0.2964 0.5878 -0.0352 -0.0309 -0.1369 382 DOD A D1   
2572 D D2   A DOD K .   ? 0.1135 0.1584 0.4010 -0.0341 -0.0660 0.0282  382 DOD A D2   
2573 D D2   B DOD K .   ? 0.0913 0.3082 0.3729 -0.0067 0.0235  -0.1042 382 DOD A D2   
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