data_8RLH
# 
_entry.id   8RLH 
# 
_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   8RLH         pdb_00008rlh 10.2210/pdb8rlh/pdb 
WWPDB D_1292133904 ?            ?                   
# 
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                        8RLH 
_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     nat 'Lysozyme C'  14331.160 1   3.2.1.17 ? ? ? 
2 non-polymer syn 'NITRATE ION' 62.005    9   ?        ? ? ? 
3 non-polymer syn 'ACETATE ION' 59.044    1   ?        ? ? ? 
4 water       nat water         18.015    105 ?        ? ? ? 
# 
_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       
;KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
;
_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   LYS n 
1 2   VAL n 
1 3   PHE n 
1 4   GLY n 
1 5   ARG n 
1 6   CYS n 
1 7   GLU n 
1 8   LEU n 
1 9   ALA n 
1 10  ALA n 
1 11  ALA n 
1 12  MET n 
1 13  LYS n 
1 14  ARG n 
1 15  HIS n 
1 16  GLY n 
1 17  LEU n 
1 18  ASP n 
1 19  ASN n 
1 20  TYR n 
1 21  ARG n 
1 22  GLY n 
1 23  TYR n 
1 24  SER n 
1 25  LEU n 
1 26  GLY n 
1 27  ASN n 
1 28  TRP n 
1 29  VAL n 
1 30  CYS n 
1 31  ALA n 
1 32  ALA n 
1 33  LYS n 
1 34  PHE n 
1 35  GLU n 
1 36  SER n 
1 37  ASN n 
1 38  PHE n 
1 39  ASN n 
1 40  THR n 
1 41  GLN n 
1 42  ALA n 
1 43  THR n 
1 44  ASN n 
1 45  ARG n 
1 46  ASN n 
1 47  THR n 
1 48  ASP n 
1 49  GLY n 
1 50  SER n 
1 51  THR n 
1 52  ASP n 
1 53  TYR n 
1 54  GLY n 
1 55  ILE n 
1 56  LEU n 
1 57  GLN n 
1 58  ILE n 
1 59  ASN n 
1 60  SER n 
1 61  ARG n 
1 62  TRP n 
1 63  TRP n 
1 64  CYS n 
1 65  ASN n 
1 66  ASP n 
1 67  GLY n 
1 68  ARG n 
1 69  THR n 
1 70  PRO n 
1 71  GLY n 
1 72  SER n 
1 73  ARG n 
1 74  ASN n 
1 75  LEU n 
1 76  CYS n 
1 77  ASN n 
1 78  ILE n 
1 79  PRO n 
1 80  CYS n 
1 81  SER n 
1 82  ALA n 
1 83  LEU n 
1 84  LEU n 
1 85  SER n 
1 86  SER n 
1 87  ASP n 
1 88  ILE n 
1 89  THR n 
1 90  ALA n 
1 91  SER n 
1 92  VAL n 
1 93  ASN n 
1 94  CYS n 
1 95  ALA n 
1 96  LYS n 
1 97  LYS n 
1 98  ILE n 
1 99  VAL n 
1 100 SER n 
1 101 ASP n 
1 102 GLY n 
1 103 ASN n 
1 104 GLY n 
1 105 MET n 
1 106 ASN n 
1 107 ALA n 
1 108 TRP n 
1 109 VAL n 
1 110 ALA n 
1 111 TRP n 
1 112 ARG n 
1 113 ASN n 
1 114 ARG n 
1 115 CYS n 
1 116 LYS n 
1 117 GLY n 
1 118 THR n 
1 119 ASP n 
1 120 VAL n 
1 121 GLN n 
1 122 ALA n 
1 123 TRP n 
1 124 ILE n 
1 125 ARG n 
1 126 GLY n 
1 127 CYS n 
1 128 ARG n 
1 129 LEU n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           129 
_entity_src_nat.common_name                chicken 
_entity_src_nat.pdbx_organism_scientific   'Gallus gallus' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9031 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
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   LYS 1   1   1   LYS LYS A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   GLY 4   4   4   GLY GLY A . n 
A 1 5   ARG 5   5   5   ARG ARG A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  TYR 20  20  20  TYR TYR A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  TRP 28  28  28  TRP TRP A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  CYS 30  30  30  CYS CYS A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  ASN 39  39  39  ASN ASN A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  TRP 62  62  62  TRP TRP A . n 
A 1 63  TRP 63  63  63  TRP TRP A . n 
A 1 64  CYS 64  64  64  CYS CYS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  CYS 76  76  76  CYS CYS A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  CYS 80  80  80  CYS CYS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  CYS 94  94  94  CYS CYS A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 MET 105 105 105 MET MET A . n 
A 1 106 ASN 106 106 106 ASN ASN A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 TRP 108 108 108 TRP TRP A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 TRP 111 111 111 TRP TRP A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 CYS 115 115 115 CYS CYS A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 ASP 119 119 119 ASP ASP A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 CYS 127 127 127 CYS CYS A . n 
A 1 128 ARG 128 128 128 ARG ARG A . n 
A 1 129 LEU 129 129 129 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   205 205 NO3 NO3 A . 
G 2 NO3 1   206 206 NO3 NO3 A . 
H 2 NO3 1   207 207 NO3 NO3 A . 
I 2 NO3 1   208 208 NO3 NO3 A . 
J 2 NO3 1   209 209 NO3 NO3 A . 
K 3 ACT 1   210 210 ACT ACT A . 
L 4 DOD 1   301 387 DOD DOD A . 
L 4 DOD 2   302 308 DOD DOD A . 
L 4 DOD 3   303 386 DOD DOD A . 
L 4 DOD 4   304 382 DOD DOD A . 
L 4 DOD 5   305 358 DOD DOD A . 
L 4 DOD 6   306 367 DOD DOD A . 
L 4 DOD 7   307 390 DOD DOD A . 
L 4 DOD 8   308 378 DOD DOD A . 
L 4 DOD 9   309 342 DOD DOD A . 
L 4 DOD 10  310 384 DOD DOD A . 
L 4 DOD 11  311 359 DOD DOD A . 
L 4 DOD 12  312 326 DOD DOD A . 
L 4 DOD 13  313 391 DOD DOD A . 
L 4 DOD 14  314 338 DOD DOD A . 
L 4 DOD 15  315 304 DOD DOD A . 
L 4 DOD 16  316 373 DOD DOD A . 
L 4 DOD 17  317 346 DOD DOD A . 
L 4 DOD 18  318 405 DOD DOD A . 
L 4 DOD 19  319 352 DOD DOD A . 
L 4 DOD 20  320 394 DOD DOD A . 
L 4 DOD 21  321 362 DOD DOD A . 
L 4 DOD 22  322 363 DOD DOD A . 
L 4 DOD 23  323 315 DOD DOD A . 
L 4 DOD 24  324 335 DOD DOD A . 
L 4 DOD 25  325 397 DOD DOD A . 
L 4 DOD 26  326 392 DOD DOD A . 
L 4 DOD 27  327 356 DOD DOD A . 
L 4 DOD 28  328 323 DOD DOD A . 
L 4 DOD 29  329 345 DOD DOD A . 
L 4 DOD 30  330 331 DOD DOD A . 
L 4 DOD 31  331 355 DOD DOD A . 
L 4 DOD 32  332 307 DOD DOD A . 
L 4 DOD 33  333 334 DOD DOD A . 
L 4 DOD 34  334 321 DOD DOD A . 
L 4 DOD 35  335 370 DOD DOD A . 
L 4 DOD 36  336 383 DOD DOD A . 
L 4 DOD 37  337 325 DOD DOD A . 
L 4 DOD 38  338 330 DOD DOD A . 
L 4 DOD 39  339 339 DOD DOD A . 
L 4 DOD 40  340 302 DOD DOD A . 
L 4 DOD 41  341 402 DOD DOD A . 
L 4 DOD 42  342 336 DOD DOD A . 
L 4 DOD 43  343 309 DOD DOD A . 
L 4 DOD 44  344 341 DOD DOD A . 
L 4 DOD 45  345 306 DOD DOD A . 
L 4 DOD 46  346 311 DOD DOD A . 
L 4 DOD 47  347 301 DOD DOD A . 
L 4 DOD 48  348 316 DOD DOD A . 
L 4 DOD 49  349 399 DOD DOD A . 
L 4 DOD 50  350 317 DOD DOD A . 
L 4 DOD 51  351 365 DOD DOD A . 
L 4 DOD 52  352 389 DOD DOD A . 
L 4 DOD 53  353 319 DOD DOD A . 
L 4 DOD 54  354 379 DOD DOD A . 
L 4 DOD 55  355 333 DOD DOD A . 
L 4 DOD 56  356 344 DOD DOD A . 
L 4 DOD 57  357 354 DOD DOD A . 
L 4 DOD 58  358 380 DOD DOD A . 
L 4 DOD 59  359 303 DOD DOD A . 
L 4 DOD 60  360 322 DOD DOD A . 
L 4 DOD 61  361 374 DOD DOD A . 
L 4 DOD 62  362 401 DOD DOD A . 
L 4 DOD 63  363 318 DOD DOD A . 
L 4 DOD 64  364 324 DOD DOD A . 
L 4 DOD 65  365 328 DOD DOD A . 
L 4 DOD 66  366 372 DOD DOD A . 
L 4 DOD 67  367 351 DOD DOD A . 
L 4 DOD 68  368 371 DOD DOD A . 
L 4 DOD 69  369 396 DOD DOD A . 
L 4 DOD 70  370 313 DOD DOD A . 
L 4 DOD 71  371 361 DOD DOD A . 
L 4 DOD 72  372 403 DOD DOD A . 
L 4 DOD 73  373 357 DOD DOD A . 
L 4 DOD 74  374 375 DOD DOD A . 
L 4 DOD 75  375 388 DOD DOD A . 
L 4 DOD 76  376 314 DOD DOD A . 
L 4 DOD 77  377 320 DOD DOD A . 
L 4 DOD 78  378 310 DOD DOD A . 
L 4 DOD 79  379 305 DOD DOD A . 
L 4 DOD 80  380 332 DOD DOD A . 
L 4 DOD 81  381 353 DOD DOD A . 
L 4 DOD 82  382 376 DOD DOD A . 
L 4 DOD 83  383 312 DOD DOD A . 
L 4 DOD 84  384 377 DOD DOD A . 
L 4 DOD 85  385 327 DOD DOD A . 
L 4 DOD 86  386 337 DOD DOD A . 
L 4 DOD 87  387 369 DOD DOD A . 
L 4 DOD 88  388 385 DOD DOD A . 
L 4 DOD 89  389 366 DOD DOD A . 
L 4 DOD 90  390 340 DOD DOD A . 
L 4 DOD 91  391 368 DOD DOD A . 
L 4 DOD 92  392 329 DOD DOD A . 
L 4 DOD 93  393 360 DOD DOD A . 
L 4 DOD 94  394 381 DOD DOD A . 
L 4 DOD 95  395 404 DOD DOD A . 
L 4 DOD 96  396 398 DOD DOD A . 
L 4 DOD 97  397 395 DOD DOD A . 
L 4 DOD 98  398 348 DOD DOD A . 
L 4 DOD 99  399 364 DOD DOD A . 
L 4 DOD 100 400 400 DOD DOD A . 
L 4 DOD 101 401 343 DOD DOD A . 
L 4 DOD 102 402 393 DOD DOD A . 
L 4 DOD 103 403 349 DOD DOD A . 
L 4 DOD 104 404 350 DOD DOD A . 
L 4 DOD 105 405 347 DOD DOD A . 
# 
_cell.angle_alpha                  88.64 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   71.51 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  68.17 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RLH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     27.290 
_cell.length_a_esd                 ? 
_cell.length_b                     31.940 
_cell.length_b_esd                 ? 
_cell.length_c                     34.350 
_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                         8RLH 
_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                   8RLH 
_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          'BATCH MODE' 
_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    '2 % NaNO3, 0.1 M Na 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         2020-09-10 
_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   1.458 
_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        1.458 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   D19 
_diffrn_source.pdbx_synchrotron_site       ILL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RLH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.10 
_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                                     38932 
_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                           94.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.7 
_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                                0.107 
_reflns.pdbx_Rpim_I_all                                0.056 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.089 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.10 
_reflns_shell.d_res_low                                     1.14 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3703 
_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                               1.6 
_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                               0.769 
_reflns_shell.pdbx_Rpim_I_all                               0.494 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.545 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          88.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.585 
_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                                 8RLH 
_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                            1.10 
_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                     36985 
_refine.ls_number_reflns_R_free                  1947 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.5 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2343 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1860 
_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                     8RLH 
_struct.title                        'Neutron structure of hydrogenated 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        8RLH 
_struct_keywords.text            'lysozyme, hydrogenated, 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 2 ? 
K N N 3 ? 
L 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   
;KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
;
_struct_ref.pdbx_align_begin           19 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8RLH 
_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                 129 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00698 
_struct_ref_seq.db_align_beg                  19 
_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       1 
_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)' 11360 ? 
1 MORE         40    ? 
1 'SSA (A^2)'  9130  ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_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 4   ? HIS A 15  ? GLY A 4   HIS A 15  1 ? 12 
HELX_P HELX_P2 AA2 ASN A 19  ? TYR A 23  ? ASN A 19  TYR A 23  5 ? 5  
HELX_P HELX_P3 AA3 SER A 24  ? ASN A 37  ? SER A 24  ASN A 37  1 ? 14 
HELX_P HELX_P4 AA4 PRO A 79  ? SER A 85  ? PRO A 79  SER A 85  5 ? 7  
HELX_P HELX_P5 AA5 ILE A 88  ? ASP A 101 ? ILE A 88  ASP A 101 1 ? 14 
HELX_P HELX_P6 AA6 GLY A 104 ? ALA A 107 ? GLY A 104 ALA A 107 5 ? 4  
HELX_P HELX_P7 AA7 TRP A 108 ? CYS A 115 ? TRP A 108 CYS A 115 1 ? 8  
HELX_P HELX_P8 AA8 ASP A 119 ? ILE A 124 ? 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 6  SG ? ? ? 1_555 A CYS 127 SG ? ? A CYS 6  A CYS 127 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf2 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 115 SG ? ? A CYS 30 A CYS 115 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 80  SG ? ? A CYS 64 A CYS 80  1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf4 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 94  SG ? ? A CYS 76 A CYS 94  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
# 
_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 6  ? CYS A 127 ? CYS A 6  ? 1_555 CYS A 127 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 30 ? CYS A 115 ? CYS A 30 ? 1_555 CYS A 115 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 64 ? CYS A 80  ? CYS A 64 ? 1_555 CYS A 80  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 76 ? CYS A 94  ? 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 43 ? ARG A 45 ? THR A 43 ARG A 45 
AA1 2 THR A 51 ? TYR A 53 ? THR A 51 TYR A 53 
AA1 3 ILE A 58 ? ASN A 59 ? 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 44 ? N ASN A 44 O ASP A 52 ? O ASP A 52 
AA1 2 3 N TYR A 53 ? N TYR A 53 O ILE A 58 ? O ILE A 58 
# 
_pdbx_entry_details.entry_id                   8RLH 
_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 D1 A DOD 360 ? ? D1 A DOD 377 ? ? 1.15 
2 1 O  A DOD 334 ? ? D2 A DOD 403 ? ? 1.46 
3 1 DG A SER 85  ? ? O  A ASP 87  ? B 1.53 
4 1 DG A SER 85  ? ? O  A ASP 87  ? A 1.57 
5 1 O  A ARG 128 ? ? D1 A DOD 306 ? ? 1.58 
# 
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 DD21 A ASN 113 ? A 1_555 DH21 A ARG 128 ? ? 1_654 1.28 
2 1 D2   A DOD 334 ? ? 1_555 O    A DOD 389 ? ? 1_456 1.46 
3 1 OE2  A GLU 7   ? ? 1_555 DD2  A ASP 101 ? ? 1_556 1.56 
# 
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 21  ? ? CZ A ARG 21  ? ? NH1 A ARG 21  ? ? 117.13 120.30 -3.17 0.50 N 
2 1 NE A ARG 61  ? ? CZ A ARG 61  ? ? NH2 A ARG 61  ? ? 114.29 120.30 -6.01 0.50 N 
3 1 NE A ARG 68  ? ? CZ A ARG 68  ? ? NH2 A ARG 68  ? ? 115.65 120.30 -4.65 0.50 N 
4 1 NE A ARG 112 ? ? CZ A ARG 112 ? ? NH1 A ARG 112 ? ? 125.02 120.30 4.72  0.50 N 
5 1 NE A ARG 125 ? ? CZ A ARG 125 ? ? NH1 A ARG 125 ? ? 116.94 120.30 -3.36 0.50 N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     101 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -87.26 
_pdbx_validate_torsion.psi             41.66 
# 
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 5   ? A 0.164 'SIDE CHAIN' 
2 1 ARG A 68  ? ? 0.101 'SIDE CHAIN' 
3 1 ARG A 112 ? ? 0.106 'SIDE CHAIN' 
4 1 ARG A 128 ? ? 0.102 '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                    8RLH 
_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]   0.036643 
_atom_sites.fract_transf_matrix[1][2]   -0.014680 
_atom_sites.fract_transf_matrix[1][3]   -0.013908 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.033728 
_atom_sites.fract_transf_matrix[2][3]   0.003632 
_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]   0.030875 
_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 LYS A 1 1   ? 29.351 23.362 26.709 0.718 15.21  ? 1   LYS A N    1 
ATOM   2    N N    B LYS A 1 1   ? 29.532 23.322 26.634 0.282 13.18  ? 1   LYS A N    1 
ATOM   3    C CA   A LYS A 1 1   ? 29.216 22.394 27.787 0.718 14.31  ? 1   LYS A CA   1 
ATOM   4    C CA   B LYS A 1 1   ? 29.353 22.385 27.750 0.282 13.45  ? 1   LYS A CA   1 
ATOM   5    C C    A LYS A 1 1   ? 29.967 21.126 27.401 0.718 12.53  ? 1   LYS A C    1 
ATOM   6    C C    B LYS A 1 1   ? 29.837 20.994 27.412 0.282 13.14  ? 1   LYS A C    1 
ATOM   7    O O    A LYS A 1 1   ? 29.896 20.750 26.219 0.718 12.63  ? 1   LYS A O    1 
ATOM   8    O O    B LYS A 1 1   ? 29.487 20.419 26.380 0.282 13.19  ? 1   LYS A O    1 
ATOM   9    C CB   A LYS A 1 1   ? 27.742 22.092 28.067 0.718 14.31  ? 1   LYS A CB   1 
ATOM   10   C CB   B LYS A 1 1   ? 27.880 22.347 28.157 0.282 13.64  ? 1   LYS A CB   1 
ATOM   11   C CG   A LYS A 1 1   ? 27.470 21.016 29.102 0.718 13.50  ? 1   LYS A CG   1 
ATOM   12   C CG   B LYS A 1 1   ? 27.426 21.134 28.951 0.282 13.50  ? 1   LYS A CG   1 
ATOM   13   C CD   A LYS A 1 1   ? 25.951 20.922 29.298 0.718 14.25  ? 1   LYS A CD   1 
ATOM   14   C CD   B LYS A 1 1   ? 26.089 21.341 29.633 0.282 14.45  ? 1   LYS A CD   1 
ATOM   15   C CE   A LYS A 1 1   ? 25.662 19.831 30.318 0.718 15.92  ? 1   LYS A CE   1 
ATOM   16   C CE   B LYS A 1 1   ? 25.568 20.056 30.267 0.282 15.18  ? 1   LYS A CE   1 
ATOM   17   N NZ   A LYS A 1 1   ? 24.315 19.991 30.937 0.718 17.17  ? 1   LYS A NZ   1 
ATOM   18   N NZ   B LYS A 1 1   ? 25.923 19.936 31.709 0.282 15.33  ? 1   LYS A NZ   1 
ATOM   19   D D1   A LYS A 1 1   ? 28.900 22.960 25.899 0.718 14.61  ? 1   LYS A D1   1 
ATOM   20   D D1   B LYS A 1 1   ? 29.039 22.875 25.858 0.282 20.99  ? 1   LYS A D1   1 
ATOM   21   D D2   A LYS A 1 1   ? 28.893 24.211 27.031 0.718 16.51  ? 1   LYS A D2   1 
ATOM   22   D D2   B LYS A 1 1   ? 29.077 24.186 26.977 0.282 20.99  ? 1   LYS A D2   1 
ATOM   23   D D3   A LYS A 1 1   ? 30.356 23.465 26.557 0.718 14.99  ? 1   LYS A D3   1 
ATOM   24   D D3   B LYS A 1 1   ? 30.517 23.411 26.501 0.282 20.99  ? 1   LYS A D3   1 
ATOM   25   H HA   A LYS A 1 1   ? 29.670 22.811 28.697 0.718 37.07  ? 1   LYS A HA   1 
ATOM   26   H HA   B LYS A 1 1   ? 29.937 22.754 28.606 0.282 0.08   ? 1   LYS A HA   1 
ATOM   27   H HB2  A LYS A 1 1   ? 27.260 23.013 28.395 0.718 20.95  ? 1   LYS A HB2  1 
ATOM   28   H HB2  B LYS A 1 1   ? 27.668 23.238 28.748 0.282 10.21  ? 1   LYS A HB2  1 
ATOM   29   H HB3  A LYS A 1 1   ? 27.270 21.794 27.131 0.718 10.58  ? 1   LYS A HB3  1 
ATOM   30   H HB3  B LYS A 1 1   ? 27.276 22.406 27.252 0.282 25.66  ? 1   LYS A HB3  1 
ATOM   31   H HG2  A LYS A 1 1   ? 27.864 20.059 28.760 0.718 14.60  ? 1   LYS A HG2  1 
ATOM   32   H HG2  B LYS A 1 1   ? 27.353 20.278 28.280 0.282 8.17   ? 1   LYS A HG2  1 
ATOM   33   H HG3  A LYS A 1 1   ? 27.955 21.271 30.044 0.718 12.80  ? 1   LYS A HG3  1 
ATOM   34   H HG3  B LYS A 1 1   ? 28.177 20.902 29.706 0.282 167.91 ? 1   LYS A HG3  1 
ATOM   35   H HD2  A LYS A 1 1   ? 25.562 21.876 29.653 0.718 20.99  ? 1   LYS A HD2  1 
ATOM   36   H HD2  B LYS A 1 1   ? 26.193 22.104 30.404 0.282 35.07  ? 1   LYS A HD2  1 
ATOM   37   H HD3  A LYS A 1 1   ? 25.467 20.685 28.351 0.718 18.48  ? 1   LYS A HD3  1 
ATOM   38   H HD3  B LYS A 1 1   ? 25.364 21.699 28.902 0.282 29.24  ? 1   LYS A HD3  1 
ATOM   39   H HE2  A LYS A 1 1   ? 25.719 18.858 29.829 0.718 24.71  ? 1   LYS A HE2  1 
ATOM   40   H HE2  B LYS A 1 1   ? 24.483 20.024 30.164 0.282 17.84  ? 1   LYS A HE2  1 
ATOM   41   H HE3  A LYS A 1 1   ? 26.422 19.859 31.099 0.718 23.55  ? 1   LYS A HE3  1 
ATOM   42   H HE3  B LYS A 1 1   ? 25.979 19.203 29.728 0.282 21.88  ? 1   LYS A HE3  1 
ATOM   43   D DZ1  A LYS A 1 1   ? 24.293 20.820 31.535 0.718 19.56  ? 1   LYS A DZ1  1 
ATOM   44   D DZ1  B LYS A 1 1   ? 26.891 19.583 31.796 0.282 15.63  ? 1   LYS A DZ1  1 
ATOM   45   D DZ2  A LYS A 1 1   ? 23.607 20.105 30.187 0.718 18.48  ? 1   LYS A DZ2  1 
ATOM   46   D DZ2  B LYS A 1 1   ? 25.817 20.840 32.179 0.282 16.33  ? 1   LYS A DZ2  1 
ATOM   47   D DZ3  A LYS A 1 1   ? 24.087 19.147 31.498 0.718 18.25  ? 1   LYS A DZ3  1 
ATOM   48   D DZ3  B LYS A 1 1   ? 25.314 19.247 32.170 0.282 15.50  ? 1   LYS A DZ3  1 
ATOM   49   N N    . VAL A 1 2   ? 30.641 20.457 28.330 1.000 12.05  ? 2   VAL A N    1 
ATOM   50   C CA   . VAL A 1 2   ? 31.132 19.113 28.108 1.000 11.13  ? 2   VAL A CA   1 
ATOM   51   C C    . VAL A 1 2   ? 30.304 18.180 28.968 1.000 11.34  ? 2   VAL A C    1 
ATOM   52   O O    . VAL A 1 2   ? 30.280 18.275 30.195 1.000 12.42  ? 2   VAL A O    1 
ATOM   53   C CB   . VAL A 1 2   ? 32.610 19.009 28.465 1.000 12.00  ? 2   VAL A CB   1 
ATOM   54   C CG1  . VAL A 1 2   ? 33.134 17.635 28.106 1.000 13.06  ? 2   VAL A CG1  1 
ATOM   55   C CG2  . VAL A 1 2   ? 33.455 20.051 27.785 1.000 14.37  ? 2   VAL A CG2  1 
ATOM   56   D D    . VAL A 1 2   ? 30.632 20.799 29.277 1.000 12.55  ? 2   VAL A D    1 
ATOM   57   H HA   . VAL A 1 2   ? 30.996 18.847 27.050 1.000 12.57  ? 2   VAL A HA   1 
ATOM   58   H HB   . VAL A 1 2   ? 32.711 19.141 29.553 1.000 14.14  ? 2   VAL A HB   1 
ATOM   59   H HG11 . VAL A 1 2   ? 33.047 17.486 27.060 1.000 27.79  ? 2   VAL A HG11 1 
ATOM   60   H HG12 . VAL A 1 2   ? 34.153 17.561 28.389 1.000 17.31  ? 2   VAL A HG12 1 
ATOM   61   H HG13 . VAL A 1 2   ? 32.571 16.897 28.616 1.000 18.67  ? 2   VAL A HG13 1 
ATOM   62   H HG21 . VAL A 1 2   ? 33.372 19.942 26.734 1.000 22.06  ? 2   VAL A HG21 1 
ATOM   63   H HG22 . VAL A 1 2   ? 33.120 21.017 28.068 1.000 20.86  ? 2   VAL A HG22 1 
ATOM   64   H HG23 . VAL A 1 2   ? 34.467 19.930 28.075 1.000 20.66  ? 2   VAL A HG23 1 
ATOM   65   N N    . PHE A 1 3   ? 29.589 17.276 28.331 1.000 10.73  ? 3   PHE A N    1 
ATOM   66   C CA   . PHE A 1 3   ? 28.676 16.365 28.999 1.000 10.44  ? 3   PHE A CA   1 
ATOM   67   C C    . PHE A 1 3   ? 29.480 15.212 29.625 1.000 10.01  ? 3   PHE A C    1 
ATOM   68   O O    . PHE A 1 3   ? 30.562 14.850 29.154 1.000 11.02  ? 3   PHE A O    1 
ATOM   69   C CB   . PHE A 1 3   ? 27.680 15.741 28.034 1.000 10.71  ? 3   PHE A CB   1 
ATOM   70   C CG   . PHE A 1 3   ? 26.422 16.536 27.807 1.000 10.88  ? 3   PHE A CG   1 
ATOM   71   C CD1  . PHE A 1 3   ? 26.345 17.571 26.880 1.000 11.63  ? 3   PHE A CD1  1 
ATOM   72   C CD2  . PHE A 1 3   ? 25.307 16.189 28.559 1.000 11.44  ? 3   PHE A CD2  1 
ATOM   73   C CE1  . PHE A 1 3   ? 25.168 18.270 26.654 1.000 12.68  ? 3   PHE A CE1  1 
ATOM   74   C CE2  . PHE A 1 3   ? 24.115 16.883 28.341 1.000 13.60  ? 3   PHE A CE2  1 
ATOM   75   C CZ   . PHE A 1 3   ? 24.070 17.913 27.420 1.000 13.23  ? 3   PHE A CZ   1 
ATOM   76   H H    . PHE A 1 3   ? 29.681 17.213 27.327 1.000 12.77  ? 3   PHE A H    1 
ATOM   77   H HA   . PHE A 1 3   ? 28.133 16.904 29.789 1.000 11.13  ? 3   PHE A HA   1 
ATOM   78   H HB2  . PHE A 1 3   ? 28.175 15.595 27.074 1.000 16.24  ? 3   PHE A HB2  1 
ATOM   79   H HB3  . PHE A 1 3   ? 27.403 14.757 28.413 1.000 13.43  ? 3   PHE A HB3  1 
ATOM   80   H HD1  . PHE A 1 3   ? 27.229 17.839 26.319 1.000 16.28  ? 3   PHE A HD1  1 
ATOM   81   H HD2  . PHE A 1 3   ? 25.361 15.401 29.295 1.000 13.40  ? 3   PHE A HD2  1 
ATOM   82   H HE1  . PHE A 1 3   ? 25.110 19.056 25.915 1.000 13.77  ? 3   PHE A HE1  1 
ATOM   83   H HE2  . PHE A 1 3   ? 23.226 16.614 28.893 1.000 14.48  ? 3   PHE A HE2  1 
ATOM   84   H HZ   . PHE A 1 3   ? 23.146 18.459 27.293 1.000 17.46  ? 3   PHE A HZ   1 
ATOM   85   N N    . GLY A 1 4   ? 28.903 14.640 30.683 1.000 9.89   ? 4   GLY A N    1 
ATOM   86   C CA   . GLY A 1 4   ? 29.248 13.313 31.132 1.000 10.97  ? 4   GLY A CA   1 
ATOM   87   C C    . GLY A 1 4   ? 28.507 12.282 30.287 1.000 10.76  ? 4   GLY A C    1 
ATOM   88   O O    . GLY A 1 4   ? 27.489 12.562 29.702 1.000 11.02  ? 4   GLY A O    1 
ATOM   89   H H    . GLY A 1 4   ? 28.198 15.156 31.190 1.000 14.17  ? 4   GLY A H    1 
ATOM   90   H HA2  . GLY A 1 4   ? 30.324 13.161 31.041 1.000 11.70  ? 4   GLY A HA2  1 
ATOM   91   H HA3  . GLY A 1 4   ? 28.975 13.196 32.181 1.000 13.52  ? 4   GLY A HA3  1 
ATOM   92   N N    A ARG A 1 5   ? 29.034 11.054 30.134 0.501 11.28  ? 5   ARG A N    1 
ATOM   93   N N    B ARG A 1 5   ? 29.071 11.093 30.357 0.499 11.32  ? 5   ARG A N    1 
ATOM   94   C CA   A ARG A 1 5   ? 28.370 10.011 29.337 0.501 10.46  ? 5   ARG A CA   1 
ATOM   95   C CA   B ARG A 1 5   ? 28.552 9.984  29.576 0.499 10.36  ? 5   ARG A CA   1 
ATOM   96   C C    A ARG A 1 5   ? 26.987 9.694  29.897 0.501 10.35  ? 5   ARG A C    1 
ATOM   97   C C    B ARG A 1 5   ? 27.107 9.641  29.907 0.499 10.29  ? 5   ARG A C    1 
ATOM   98   O O    A ARG A 1 5   ? 26.049 9.630  29.096 0.501 9.79   ? 5   ARG A O    1 
ATOM   99   O O    B ARG A 1 5   ? 26.283 9.518  29.005 0.499 10.02  ? 5   ARG A O    1 
ATOM   100  C CB   A ARG A 1 5   ? 29.156 8.703  29.168 0.501 12.25  ? 5   ARG A CB   1 
ATOM   101  C CB   B ARG A 1 5   ? 29.470 8.790  29.841 0.499 11.64  ? 5   ARG A CB   1 
ATOM   102  C CG   A ARG A 1 5   ? 29.406 7.878  30.394 0.501 13.29  ? 5   ARG A CG   1 
ATOM   103  C CG   B ARG A 1 5   ? 29.070 7.523  29.136 0.499 13.40  ? 5   ARG A CG   1 
ATOM   104  C CD   A ARG A 1 5   ? 30.341 6.694  30.110 0.501 16.61  ? 5   ARG A CD   1 
ATOM   105  C CD   B ARG A 1 5   ? 30.069 6.416  29.455 0.499 15.87  ? 5   ARG A CD   1 
ATOM   106  N NE   A ARG A 1 5   ? 30.486 5.910  31.335 0.501 18.56  ? 5   ARG A NE   1 
ATOM   107  N NE   B ARG A 1 5   ? 30.090 6.038  30.861 0.499 18.15  ? 5   ARG A NE   1 
ATOM   108  C CZ   A ARG A 1 5   ? 29.476 5.211  31.830 0.501 19.25  ? 5   ARG A CZ   1 
ATOM   109  C CZ   B ARG A 1 5   ? 29.598 4.918  31.376 0.499 19.17  ? 5   ARG A CZ   1 
ATOM   110  N NH1  A ARG A 1 5   ? 28.527 4.710  31.060 0.501 18.81  ? 5   ARG A NH1  1 
ATOM   111  N NH1  B ARG A 1 5   ? 28.605 4.302  30.751 0.499 18.66  ? 5   ARG A NH1  1 
ATOM   112  N NH2  A ARG A 1 5   ? 29.372 5.097  33.145 0.501 20.08  ? 5   ARG A NH2  1 
ATOM   113  N NH2  B ARG A 1 5   ? 30.024 4.402  32.520 0.499 19.59  ? 5   ARG A NH2  1 
ATOM   114  D D    A ARG A 1 5   ? 29.926 10.865 30.550 0.501 12.59  ? 5   ARG A D    1 
ATOM   115  D D    B ARG A 1 5   ? 29.873 11.005 30.968 0.499 13.26  ? 5   ARG A D    1 
ATOM   116  H HA   A ARG A 1 5   ? 28.220 10.425 28.329 0.501 13.01  ? 5   ARG A HA   1 
ATOM   117  H HA   B ARG A 1 5   ? 28.615 10.246 28.509 0.499 9.28   ? 5   ARG A HA   1 
ATOM   118  H HB2  A ARG A 1 5   ? 28.623 8.082  28.449 0.501 9.63   ? 5   ARG A HB2  1 
ATOM   119  H HB2  B ARG A 1 5   ? 30.482 9.054  29.534 0.499 13.30  ? 5   ARG A HB2  1 
ATOM   120  H HB3  A ARG A 1 5   ? 30.123 8.949  28.727 0.501 9.52   ? 5   ARG A HB3  1 
ATOM   121  H HB3  B ARG A 1 5   ? 29.491 8.599  30.914 0.499 21.63  ? 5   ARG A HB3  1 
ATOM   122  H HG2  A ARG A 1 5   ? 29.848 8.507  31.166 0.501 15.85  ? 5   ARG A HG2  1 
ATOM   123  H HG2  B ARG A 1 5   ? 28.073 7.222  29.458 0.499 14.29  ? 5   ARG A HG2  1 
ATOM   124  H HG3  A ARG A 1 5   ? 28.456 7.501  30.772 0.501 12.66  ? 5   ARG A HG3  1 
ATOM   125  H HG3  B ARG A 1 5   ? 29.042 7.694  28.060 0.499 12.27  ? 5   ARG A HG3  1 
ATOM   126  H HD2  A ARG A 1 5   ? 29.926 6.073  29.317 0.501 17.21  ? 5   ARG A HD2  1 
ATOM   127  H HD2  B ARG A 1 5   ? 29.823 5.537  28.858 0.499 14.76  ? 5   ARG A HD2  1 
ATOM   128  H HD3  A ARG A 1 5   ? 31.316 7.059  29.785 0.501 7.76   ? 5   ARG A HD3  1 
ATOM   129  H HD3  B ARG A 1 5   ? 31.066 6.746  29.163 0.499 13.38  ? 5   ARG A HD3  1 
ATOM   130  D DE   A ARG A 1 5   ? 31.377 6.033  31.774 0.501 18.94  ? 5   ARG A DE   1 
ATOM   131  D DE   B ARG A 1 5   ? 30.523 6.760  31.443 0.499 19.03  ? 5   ARG A DE   1 
ATOM   132  D DH11 A ARG A 1 5   ? 28.018 3.888  31.352 0.501 19.22  ? 5   ARG A DH11 1 
ATOM   133  D DH11 B ARG A 1 5   ? 28.130 3.535  31.216 0.499 19.18  ? 5   ARG A DH11 1 
ATOM   134  D DH12 A ARG A 1 5   ? 28.269 5.183  30.206 0.501 18.98  ? 5   ARG A DH12 1 
ATOM   135  D DH12 B ARG A 1 5   ? 28.323 4.606  29.832 0.499 18.85  ? 5   ARG A DH12 1 
ATOM   136  D DH21 A ARG A 1 5   ? 28.698 4.460  33.544 0.501 21.61  ? 5   ARG A DH21 1 
ATOM   137  D DH21 B ARG A 1 5   ? 29.473 3.698  32.984 0.499 19.49  ? 5   ARG A DH21 1 
ATOM   138  D DH22 A ARG A 1 5   ? 29.970 5.657  33.740 0.501 22.01  ? 5   ARG A DH22 1 
ATOM   139  D DH22 B ARG A 1 5   ? 30.906 4.713  32.914 0.499 20.48  ? 5   ARG A DH22 1 
ATOM   140  N N    . CYS A 1 6   ? 26.835 9.490  31.202 1.000 10.25  ? 6   CYS A N    1 
ATOM   141  C CA   . CYS A 1 6   ? 25.508 9.087  31.673 1.000 10.38  ? 6   CYS A CA   1 
ATOM   142  C C    . CYS A 1 6   ? 24.504 10.237 31.544 1.000 10.40  ? 6   CYS A C    1 
ATOM   143  O O    . CYS A 1 6   ? 23.331 10.011 31.232 1.000 9.95   ? 6   CYS A O    1 
ATOM   144  C CB   . CYS A 1 6   ? 25.535 8.583  33.119 1.000 11.13  ? 6   CYS A CB   1 
ATOM   145  S SG   . CYS A 1 6   ? 26.510 7.056  33.281 1.000 14.83  ? 6   CYS A SG   1 
ATOM   146  D D    . CYS A 1 6   ? 27.571 9.617  31.875 1.000 11.36  ? 6   CYS A D    1 
ATOM   147  H HA   . CYS A 1 6   ? 25.160 8.262  31.035 1.000 13.86  ? 6   CYS A HA   1 
ATOM   148  H HB2  . CYS A 1 6   ? 25.964 9.353  33.761 1.000 14.34  ? 6   CYS A HB2  1 
ATOM   149  H HB3  . CYS A 1 6   ? 24.515 8.396  33.455 1.000 14.55  ? 6   CYS A HB3  1 
ATOM   150  N N    . GLU A 1 7   ? 24.936 11.479 31.767 1.000 9.98   ? 7   GLU A N    1 
ATOM   151  C CA   . GLU A 1 7   ? 24.112 12.652 31.610 1.000 9.73   ? 7   GLU A CA   1 
ATOM   152  C C    . GLU A 1 7   ? 23.676 12.831 30.150 1.000 9.04   ? 7   GLU A C    1 
ATOM   153  O O    . GLU A 1 7   ? 22.504 13.170 29.878 1.000 10.15  ? 7   GLU A O    1 
ATOM   154  C CB   . GLU A 1 7   ? 24.875 13.880 32.099 1.000 10.47  ? 7   GLU A CB   1 
ATOM   155  C CG   . GLU A 1 7   ? 25.142 13.945 33.620 1.000 11.29  ? 7   GLU A CG   1 
ATOM   156  C CD   . GLU A 1 7   ? 26.208 13.034 34.168 1.000 11.60  ? 7   GLU A CD   1 
ATOM   157  O OE1  . GLU A 1 7   ? 26.976 12.351 33.444 1.000 12.37  ? 7   GLU A OE1  1 
ATOM   158  O OE2  . GLU A 1 7   ? 26.312 13.014 35.427 1.000 14.23  ? 7   GLU A OE2  1 
ATOM   159  D D    . GLU A 1 7   ? 25.888 11.617 32.094 1.000 10.49  ? 7   GLU A D    1 
ATOM   160  H HA   . GLU A 1 7   ? 23.212 12.531 32.230 1.000 11.96  ? 7   GLU A HA   1 
ATOM   161  H HB2  . GLU A 1 7   ? 25.833 13.917 31.582 1.000 10.97  ? 7   GLU A HB2  1 
ATOM   162  H HB3  . GLU A 1 7   ? 24.314 14.769 31.812 1.000 14.60  ? 7   GLU A HB3  1 
ATOM   163  H HG2  . GLU A 1 7   ? 25.412 14.971 33.871 1.000 13.91  ? 7   GLU A HG2  1 
ATOM   164  H HG3  . GLU A 1 7   ? 24.208 13.721 34.136 1.000 20.94  ? 7   GLU A HG3  1 
ATOM   165  N N    . LEU A 1 8   ? 24.599 12.589 29.235 1.000 9.10   ? 8   LEU A N    1 
ATOM   166  C CA   . LEU A 1 8   ? 24.238 12.656 27.826 1.000 9.08   ? 8   LEU A CA   1 
ATOM   167  C C    . LEU A 1 8   ? 23.305 11.532 27.416 1.000 9.65   ? 8   LEU A C    1 
ATOM   168  O O    . LEU A 1 8   ? 22.337 11.717 26.670 1.000 10.04  ? 8   LEU A O    1 
ATOM   169  C CB   . LEU A 1 8   ? 25.490 12.661 26.936 1.000 9.31   ? 8   LEU A CB   1 
ATOM   170  C CG   . LEU A 1 8   ? 25.199 12.783 25.444 1.000 9.99   ? 8   LEU A CG   1 
ATOM   171  C CD1  . LEU A 1 8   ? 24.560 14.132 25.107 1.000 10.53  ? 8   LEU A CD1  1 
ATOM   172  C CD2  . LEU A 1 8   ? 26.459 12.613 24.619 1.000 11.82  ? 8   LEU A CD2  1 
ATOM   173  H H    . LEU A 1 8   ? 25.543 12.360 29.510 1.000 9.65   ? 8   LEU A H    1 
ATOM   174  H HA   . LEU A 1 8   ? 23.708 13.606 27.663 1.000 11.18  ? 8   LEU A HA   1 
ATOM   175  H HB2  . LEU A 1 8   ? 26.129 13.491 27.236 1.000 11.79  ? 8   LEU A HB2  1 
ATOM   176  H HB3  . LEU A 1 8   ? 26.044 11.738 27.109 1.000 13.93  ? 8   LEU A HB3  1 
ATOM   177  H HG   . LEU A 1 8   ? 24.493 11.987 25.164 1.000 12.31  ? 8   LEU A HG   1 
ATOM   178  H HD11 . LEU A 1 8   ? 25.225 14.914 25.370 1.000 21.52  ? 8   LEU A HD11 1 
ATOM   179  H HD12 . LEU A 1 8   ? 24.356 14.176 24.067 1.000 13.32  ? 8   LEU A HD12 1 
ATOM   180  H HD13 . LEU A 1 8   ? 23.655 14.240 25.649 1.000 15.05  ? 8   LEU A HD13 1 
ATOM   181  H HD21 . LEU A 1 8   ? 27.154 13.372 24.875 1.000 24.03  ? 8   LEU A HD21 1 
ATOM   182  H HD22 . LEU A 1 8   ? 26.886 11.663 24.816 1.000 17.06  ? 8   LEU A HD22 1 
ATOM   183  H HD23 . LEU A 1 8   ? 26.220 12.686 23.589 1.000 16.60  ? 8   LEU A HD23 1 
ATOM   184  N N    . ALA A 1 9   ? 23.574 10.342 27.925 1.000 9.72   ? 9   ALA A N    1 
ATOM   185  C CA   . ALA A 1 9   ? 22.661 9.224  27.637 1.000 9.84   ? 9   ALA A CA   1 
ATOM   186  C C    . ALA A 1 9   ? 21.229 9.560  28.096 1.000 9.64   ? 9   ALA A C    1 
ATOM   187  O O    . ALA A 1 9   ? 20.288 9.286  27.369 1.000 11.33  ? 9   ALA A O    1 
ATOM   188  C CB   . ALA A 1 9   ? 23.164 7.973  28.325 1.000 11.47  ? 9   ALA A CB   1 
ATOM   189  H H    . ALA A 1 9   ? 24.391 10.202 28.501 1.000 10.41  ? 9   ALA A H    1 
ATOM   190  H HA   . ALA A 1 9   ? 22.651 9.049  26.551 1.000 11.67  ? 9   ALA A HA   1 
ATOM   191  H HB1  . ALA A 1 9   ? 23.179 8.128  29.374 1.000 13.21  ? 9   ALA A HB1  1 
ATOM   192  H HB2  . ALA A 1 9   ? 22.521 7.161  28.097 1.000 19.27  ? 9   ALA A HB2  1 
ATOM   193  H HB3  . ALA A 1 9   ? 24.144 7.753  27.987 1.000 12.34  ? 9   ALA A HB3  1 
ATOM   194  N N    . ALA A 1 10  ? 21.094 10.125 29.300 1.000 10.12  ? 10  ALA A N    1 
ATOM   195  C CA   . ALA A 1 10  ? 19.753 10.465 29.784 1.000 10.50  ? 10  ALA A CA   1 
ATOM   196  C C    . ALA A 1 10  ? 19.115 11.524 28.919 1.000 10.38  ? 10  ALA A C    1 
ATOM   197  O O    . ALA A 1 10  ? 17.929 11.412 28.619 1.000 10.34  ? 10  ALA A O    1 
ATOM   198  C CB   . ALA A 1 10  ? 19.833 10.877 31.254 1.000 12.75  ? 10  ALA A CB   1 
ATOM   199  H H    . ALA A 1 10  ? 21.906 10.315 29.869 1.000 10.50  ? 10  ALA A H    1 
ATOM   200  H HA   . ALA A 1 10  ? 19.132 9.559  29.721 1.000 11.84  ? 10  ALA A HA   1 
ATOM   201  H HB1  . ALA A 1 10  ? 20.427 11.750 31.344 1.000 16.26  ? 10  ALA A HB1  1 
ATOM   202  H HB2  . ALA A 1 10  ? 18.857 11.075 31.619 1.000 19.58  ? 10  ALA A HB2  1 
ATOM   203  H HB3  . ALA A 1 10  ? 20.269 10.093 31.818 1.000 14.02  ? 10  ALA A HB3  1 
ATOM   204  N N    . ALA A 1 11  ? 19.847 12.535 28.486 1.000 10.13  ? 11  ALA A N    1 
ATOM   205  C CA   . ALA A 1 11  ? 19.284 13.588 27.645 1.000 9.77   ? 11  ALA A CA   1 
ATOM   206  C C    . ALA A 1 11  ? 18.873 13.003 26.294 1.000 9.78   ? 11  ALA A C    1 
ATOM   207  O O    . ALA A 1 11  ? 17.794 13.317 25.786 1.000 11.28  ? 11  ALA A O    1 
ATOM   208  C CB   . ALA A 1 11  ? 20.308 14.701 27.478 1.000 11.38  ? 11  ALA A CB   1 
ATOM   209  H H    . ALA A 1 11  ? 20.823 12.581 28.742 1.000 12.36  ? 11  ALA A H    1 
ATOM   210  H HA   . ALA A 1 11  ? 18.392 13.998 28.141 1.000 14.26  ? 11  ALA A HA   1 
ATOM   211  H HB1  . ALA A 1 11  ? 21.173 14.317 27.001 1.000 15.73  ? 11  ALA A HB1  1 
ATOM   212  H HB2  . ALA A 1 11  ? 19.893 15.477 26.886 1.000 17.53  ? 11  ALA A HB2  1 
ATOM   213  H HB3  . ALA A 1 11  ? 20.571 15.085 28.431 1.000 15.51  ? 11  ALA A HB3  1 
ATOM   214  N N    . MET A 1 12  ? 19.719 12.140 25.718 1.000 9.93   ? 12  MET A N    1 
ATOM   215  C CA   . MET A 1 12  ? 19.355 11.559 24.436 1.000 10.10  ? 12  MET A CA   1 
ATOM   216  C C    . MET A 1 12  ? 18.132 10.648 24.565 1.000 10.95  ? 12  MET A C    1 
ATOM   217  O O    . MET A 1 12  ? 17.312 10.630 23.645 1.000 11.37  ? 12  MET A O    1 
ATOM   218  C CB   . MET A 1 12  ? 20.544 10.800 23.821 1.000 9.78   ? 12  MET A CB   1 
ATOM   219  C CG   . MET A 1 12  ? 21.645 11.749 23.330 1.000 9.56   ? 12  MET A CG   1 
ATOM   220  S SD   . MET A 1 12  ? 23.022 10.704 22.729 1.000 12.24  ? 12  MET A SD   1 
ATOM   221  C CE   . MET A 1 12  ? 23.760 11.833 21.563 1.000 14.34  ? 12  MET A CE   1 
ATOM   222  H H    . MET A 1 12  ? 20.592 11.897 26.165 1.000 11.97  ? 12  MET A H    1 
ATOM   223  H HA   . MET A 1 12  ? 19.092 12.383 23.756 1.000 11.46  ? 12  MET A HA   1 
ATOM   224  H HB2  . MET A 1 12  ? 20.960 10.123 24.567 1.000 12.57  ? 12  MET A HB2  1 
ATOM   225  H HB3  . MET A 1 12  ? 20.190 10.199 22.984 1.000 16.01  ? 12  MET A HB3  1 
ATOM   226  H HG2  . MET A 1 12  ? 21.270 12.381 22.525 1.000 13.19  ? 12  MET A HG2  1 
ATOM   227  H HG3  . MET A 1 12  ? 21.984 12.389 24.145 1.000 12.33  ? 12  MET A HG3  1 
ATOM   228  H HE1  . MET A 1 12  ? 24.599 11.373 21.108 1.000 19.67  ? 12  MET A HE1  1 
ATOM   229  H HE2  . MET A 1 12  ? 23.049 12.087 20.818 1.000 21.33  ? 12  MET A HE2  1 
ATOM   230  H HE3  . MET A 1 12  ? 24.070 12.711 22.069 1.000 25.16  ? 12  MET A HE3  1 
ATOM   231  N N    . LYS A 1 13  ? 17.996 9.940  25.679 1.000 10.51  ? 13  LYS A N    1 
ATOM   232  C CA   . LYS A 1 13  ? 16.819 9.106  25.896 1.000 11.99  ? 13  LYS A CA   1 
ATOM   233  C C    . LYS A 1 13  ? 15.565 9.963  26.009 1.000 11.70  ? 13  LYS A C    1 
ATOM   234  O O    . LYS A 1 13  ? 14.532 9.598  25.458 1.000 12.46  ? 13  LYS A O    1 
ATOM   235  C CB   . LYS A 1 13  ? 17.018 8.228  27.134 1.000 14.43  ? 13  LYS A CB   1 
ATOM   236  C CG   . LYS A 1 13  ? 15.887 7.259  27.326 1.000 19.91  ? 13  LYS A CG   1 
ATOM   237  C CD   . LYS A 1 13  ? 15.955 6.310  28.504 1.000 27.80  ? 13  LYS A CD   1 
ATOM   238  C CE   . LYS A 1 13  ? 14.683 6.291  29.336 1.000 41.53  ? 13  LYS A CE   1 
ATOM   239  N NZ   . LYS A 1 13  ? 14.348 4.962  29.912 1.000 73.08  ? 13  LYS A NZ   1 
ATOM   240  H H    . LYS A 1 13  ? 18.716 9.980  26.386 1.000 12.32  ? 13  LYS A H    1 
ATOM   241  H HA   . LYS A 1 13  ? 16.704 8.446  25.024 1.000 12.75  ? 13  LYS A HA   1 
ATOM   242  H HB2  . LYS A 1 13  ? 17.951 7.674  27.035 1.000 19.28  ? 13  LYS A HB2  1 
ATOM   243  H HB3  . LYS A 1 13  ? 17.099 8.864  28.016 1.000 15.37  ? 13  LYS A HB3  1 
ATOM   244  H HG2  . LYS A 1 13  ? 14.966 7.836  27.416 1.000 19.04  ? 13  LYS A HG2  1 
ATOM   245  H HG3  . LYS A 1 13  ? 15.803 6.660  26.419 1.000 50.47  ? 13  LYS A HG3  1 
ATOM   246  H HD2  . LYS A 1 13  ? 16.151 5.303  28.135 1.000 90.57  ? 13  LYS A HD2  1 
ATOM   247  H HD3  . LYS A 1 13  ? 16.791 6.598  29.142 1.000 37.14  ? 13  LYS A HD3  1 
ATOM   248  H HE2  . LYS A 1 13  ? 14.789 7.008  30.151 1.000 49.83  ? 13  LYS A HE2  1 
ATOM   249  H HE3  . LYS A 1 13  ? 13.853 6.621  28.712 1.000 49.83  ? 13  LYS A HE3  1 
ATOM   250  D DZ1  . LYS A 1 13  ? 14.657 4.912  30.895 1.000 109.62 ? 13  LYS A DZ1  1 
ATOM   251  D DZ2  . LYS A 1 13  ? 13.325 4.813  29.887 1.000 109.62 ? 13  LYS A DZ2  1 
ATOM   252  D DZ3  . LYS A 1 13  ? 14.806 4.214  29.374 1.000 109.62 ? 13  LYS A DZ3  1 
ATOM   253  N N    . ARG A 1 14  ? 15.633 11.087 26.703 1.000 12.15  ? 14  ARG A N    1 
ATOM   254  C CA   . ARG A 1 14  ? 14.493 11.980 26.817 1.000 13.44  ? 14  ARG A CA   1 
ATOM   255  C C    . ARG A 1 14  ? 14.040 12.528 25.482 1.000 13.53  ? 14  ARG A C    1 
ATOM   256  O O    . ARG A 1 14  ? 12.882 12.878 25.305 1.000 17.62  ? 14  ARG A O    1 
ATOM   257  C CB   . ARG A 1 14  ? 14.776 13.184 27.752 1.000 15.22  ? 14  ARG A CB   1 
ATOM   258  C CG   . ARG A 1 14  ? 14.743 12.744 29.205 1.000 20.09  ? 14  ARG A CG   1 
ATOM   259  C CD   . ARG A 1 14  ? 14.824 13.903 30.161 1.000 25.22  ? 14  ARG A CD   1 
ATOM   260  N NE   . ARG A 1 14  ? 15.993 14.771 30.060 1.000 28.36  ? 14  ARG A NE   1 
ATOM   261  C CZ   . ARG A 1 14  ? 17.116 14.608 30.764 1.000 30.96  ? 14  ARG A CZ   1 
ATOM   262  N NH1  . ARG A 1 14  ? 17.158 13.640 31.669 1.000 31.80  ? 14  ARG A NH1  1 
ATOM   263  N NH2  . ARG A 1 14  ? 18.127 15.433 30.533 1.000 32.23  ? 14  ARG A NH2  1 
ATOM   264  H H    A ARG A 1 14  ? 16.498 11.329 27.166 0.653 77.87  ? 14  ARG A H    1 
ATOM   265  D D    B ARG A 1 14  ? 16.483 11.256 27.235 0.347 13.31  ? 14  ARG A D    1 
ATOM   266  H HA   . ARG A 1 14  ? 13.658 11.407 27.248 1.000 13.91  ? 14  ARG A HA   1 
ATOM   267  H HB2  . ARG A 1 14  ? 15.755 13.605 27.520 1.000 14.47  ? 14  ARG A HB2  1 
ATOM   268  H HB3  . ARG A 1 14  ? 14.027 13.959 27.588 1.000 16.24  ? 14  ARG A HB3  1 
ATOM   269  H HG2  . ARG A 1 14  ? 13.821 12.194 29.389 1.000 18.39  ? 14  ARG A HG2  1 
ATOM   270  H HG3  . ARG A 1 14  ? 15.578 12.069 29.391 1.000 16.52  ? 14  ARG A HG3  1 
ATOM   271  H HD2  . ARG A 1 14  ? 13.934 14.517 30.022 1.000 28.02  ? 14  ARG A HD2  1 
ATOM   272  H HD3  . ARG A 1 14  ? 14.786 13.505 31.175 1.000 41.56  ? 14  ARG A HD3  1 
ATOM   273  D DE   . ARG A 1 14  ? 15.844 15.549 29.432 1.000 32.66  ? 14  ARG A DE   1 
ATOM   274  D DH11 . ARG A 1 14  ? 17.902 13.612 32.347 1.000 32.49  ? 14  ARG A DH11 1 
ATOM   275  D DH12 . ARG A 1 14  ? 16.421 12.942 31.691 1.000 31.73  ? 14  ARG A DH12 1 
ATOM   276  D DH21 . ARG A 1 14  ? 19.019 15.282 30.976 1.000 33.04  ? 14  ARG A DH21 1 
ATOM   277  D DH22 . ARG A 1 14  ? 17.988 16.232 29.921 1.000 31.80  ? 14  ARG A DH22 1 
ATOM   278  N N    A HIS A 1 15  ? 14.926 12.507 24.485 0.304 12.66  ? 15  HIS A N    1 
ATOM   279  N N    B HIS A 1 15  ? 14.995 12.708 24.573 0.696 12.99  ? 15  HIS A N    1 
ATOM   280  C CA   A HIS A 1 15  ? 14.740 13.188 23.214 0.304 13.44  ? 15  HIS A CA   1 
ATOM   281  C CA   B HIS A 1 15  ? 14.653 13.095 23.219 0.696 13.71  ? 15  HIS A CA   1 
ATOM   282  C C    A HIS A 1 15  ? 14.589 12.214 22.054 0.304 13.58  ? 15  HIS A C    1 
ATOM   283  C C    B HIS A 1 15  ? 14.335 11.944 22.275 0.696 13.67  ? 15  HIS A C    1 
ATOM   284  O O    A HIS A 1 15  ? 14.822 12.585 20.900 0.304 13.74  ? 15  HIS A O    1 
ATOM   285  O O    B HIS A 1 15  ? 14.196 12.240 21.077 0.696 15.14  ? 15  HIS A O    1 
ATOM   286  C CB   A HIS A 1 15  ? 15.900 14.163 22.951 0.304 14.86  ? 15  HIS A CB   1 
ATOM   287  C CB   B HIS A 1 15  ? 15.794 13.955 22.696 0.696 14.89  ? 15  HIS A CB   1 
ATOM   288  C CG   A HIS A 1 15  ? 15.652 15.427 23.723 0.304 15.97  ? 15  HIS A CG   1 
ATOM   289  C CG   B HIS A 1 15  ? 16.002 15.269 23.360 0.696 15.66  ? 15  HIS A CG   1 
ATOM   290  N ND1  A HIS A 1 15  ? 14.611 16.272 23.407 0.304 17.69  ? 15  HIS A ND1  1 
ATOM   291  N ND1  B HIS A 1 15  ? 15.526 16.434 22.778 0.696 17.52  ? 15  HIS A ND1  1 
ATOM   292  C CD2  A HIS A 1 15  ? 16.270 15.983 24.787 0.304 16.61  ? 15  HIS A CD2  1 
ATOM   293  C CD2  B HIS A 1 15  ? 16.593 15.667 24.504 0.696 16.18  ? 15  HIS A CD2  1 
ATOM   294  C CE1  A HIS A 1 15  ? 14.611 17.297 24.232 0.304 17.85  ? 15  HIS A CE1  1 
ATOM   295  C CE1  B HIS A 1 15  ? 15.817 17.481 23.517 0.696 18.36  ? 15  HIS A CE1  1 
ATOM   296  N NE2  A HIS A 1 15  ? 15.613 17.154 25.089 0.304 17.75  ? 15  HIS A NE2  1 
ATOM   297  N NE2  B HIS A 1 15  ? 16.464 17.041 24.577 0.696 17.79  ? 15  HIS A NE2  1 
ATOM   298  D D    A HIS A 1 15  ? 15.762 11.959 24.607 0.304 11.53  ? 15  HIS A D    1 
ATOM   299  D D    B HIS A 1 15  ? 15.942 12.601 24.867 0.696 13.80  ? 15  HIS A D    1 
ATOM   300  H HA   A HIS A 1 15  ? 13.814 13.778 23.281 0.304 13.17  ? 15  HIS A HA   1 
ATOM   301  H HA   B HIS A 1 15  ? 13.759 13.732 23.275 0.696 15.16  ? 15  HIS A HA   1 
ATOM   302  H HB2  A HIS A 1 15  ? 16.841 13.714 23.266 0.304 27.01  ? 15  HIS A HB2  1 
ATOM   303  H HB2  B HIS A 1 15  ? 16.717 13.382 22.782 0.696 13.90  ? 15  HIS A HB2  1 
ATOM   304  H HB3  A HIS A 1 15  ? 15.964 14.384 21.886 0.304 13.21  ? 15  HIS A HB3  1 
ATOM   305  H HB3  B HIS A 1 15  ? 15.623 14.135 21.635 0.696 13.25  ? 15  HIS A HB3  1 
ATOM   306  D DD1  A HIS A 1 15  ? 13.971 16.081 22.653 0.304 19.11  ? 15  HIS A DD1  1 
ATOM   307  D DD1  B HIS A 1 15  ? 14.997 16.409 21.919 0.696 21.10  ? 15  HIS A DD1  1 
ATOM   308  H HD2  A HIS A 1 15  ? 17.126 15.580 25.308 0.304 167.91 ? 15  HIS A HD2  1 
ATOM   309  H HD2  B HIS A 1 15  ? 17.078 15.030 25.228 0.696 167.91 ? 15  HIS A HD2  1 
ATOM   310  H HE1  A HIS A 1 15  ? 13.911 18.119 24.213 0.304 11.30  ? 15  HIS A HE1  1 
ATOM   311  H HE1  B HIS A 1 15  ? 15.572 18.510 23.297 0.696 25.98  ? 15  HIS A HE1  1 
ATOM   312  D DE2  A HIS A 1 15  ? 15.883 17.769 25.840 0.304 18.76  ? 15  HIS A DE2  1 
ATOM   313  D DE2  B HIS A 1 15  ? 16.824 17.581 25.358 0.696 20.86  ? 15  HIS A DE2  1 
ATOM   314  N N    A GLY A 1 16  ? 14.181 10.992 22.368 0.304 13.39  ? 16  GLY A N    1 
ATOM   315  N N    B GLY A 1 16  ? 14.174 10.719 22.762 0.696 12.79  ? 16  GLY A N    1 
ATOM   316  C CA   A GLY A 1 16  ? 13.737 10.030 21.384 0.304 12.84  ? 16  GLY A CA   1 
ATOM   317  C CA   B GLY A 1 16  ? 13.698 9.649  21.914 0.696 12.97  ? 16  GLY A CA   1 
ATOM   318  C C    A GLY A 1 16  ? 14.828 9.328  20.628 0.304 12.24  ? 16  GLY A C    1 
ATOM   319  C C    B GLY A 1 16  ? 14.699 8.938  21.039 0.696 12.10  ? 16  GLY A C    1 
ATOM   320  O O    A GLY A 1 16  ? 14.614 8.962  19.465 0.304 13.61  ? 16  GLY A O    1 
ATOM   321  O O    B GLY A 1 16  ? 14.267 8.182  20.153 0.696 12.95  ? 16  GLY A O    1 
ATOM   322  D D    A GLY A 1 16  ? 14.163 10.720 23.341 0.304 13.08  ? 16  GLY A D    1 
ATOM   323  D D    B GLY A 1 16  ? 14.362 10.589 23.742 0.696 13.99  ? 16  GLY A D    1 
ATOM   324  H HA2  A GLY A 1 16  ? 13.129 9.279  21.887 0.304 12.56  ? 16  GLY A HA2  1 
ATOM   325  H HA2  B GLY A 1 16  ? 13.224 8.904  22.553 0.696 14.31  ? 16  GLY A HA2  1 
ATOM   326  H HA3  A GLY A 1 16  ? 13.096 10.542 20.666 0.304 9.59   ? 16  GLY A HA3  1 
ATOM   327  H HA3  B GLY A 1 16  ? 12.921 10.058 21.267 0.696 15.57  ? 16  GLY A HA3  1 
ATOM   328  N N    . LEU A 1 17  ? 16.013 9.095  21.204 1.000 11.38  ? 17  LEU A N    1 
ATOM   329  C CA   . LEU A 1 17  ? 16.959 8.380  20.366 1.000 11.79  ? 17  LEU A CA   1 
ATOM   330  C C    . LEU A 1 17  ? 17.158 6.918  20.632 1.000 12.41  ? 17  LEU A C    1 
ATOM   331  O O    . LEU A 1 17  ? 17.785 6.270  19.785 1.000 13.64  ? 17  LEU A O    1 
ATOM   332  C CB   . LEU A 1 17  ? 18.334 9.087  20.423 1.000 11.83  ? 17  LEU A CB   1 
ATOM   333  C CG   . LEU A 1 17  ? 18.452 10.415 19.713 1.000 13.68  ? 17  LEU A CG   1 
ATOM   334  C CD1  . LEU A 1 17  ? 19.850 11.011 19.831 1.000 14.62  ? 17  LEU A CD1  1 
ATOM   335  C CD2  . LEU A 1 17  ? 18.215 10.284 18.206 1.000 14.30  ? 17  LEU A CD2  1 
ATOM   336  D D    . LEU A 1 17  ? 16.280 9.672  21.987 1.000 13.40  ? 17  LEU A D    1 
ATOM   337  H HA   . LEU A 1 17  ? 16.597 8.469  19.331 1.000 14.81  ? 17  LEU A HA   1 
ATOM   338  H HB2  . LEU A 1 17  ? 18.592 9.241  21.471 1.000 14.18  ? 17  LEU A HB2  1 
ATOM   339  H HB3  . LEU A 1 17  ? 19.079 8.412  20.002 1.000 14.61  ? 17  LEU A HB3  1 
ATOM   340  H HG   . LEU A 1 17  ? 17.721 11.119 20.135 1.000 15.41  ? 17  LEU A HG   1 
ATOM   341  H HD11 . LEU A 1 17  ? 20.558 10.335 19.425 1.000 31.61  ? 17  LEU A HD11 1 
ATOM   342  H HD12 . LEU A 1 17  ? 19.890 11.927 19.299 1.000 18.50  ? 17  LEU A HD12 1 
ATOM   343  H HD13 . LEU A 1 17  ? 20.074 11.185 20.853 1.000 21.23  ? 17  LEU A HD13 1 
ATOM   344  H HD21 . LEU A 1 17  ? 18.918 9.606  17.795 1.000 17.30  ? 17  LEU A HD21 1 
ATOM   345  H HD22 . LEU A 1 17  ? 17.233 9.922  18.033 1.000 23.18  ? 17  LEU A HD22 1 
ATOM   346  H HD23 . LEU A 1 17  ? 18.328 11.232 17.746 1.000 17.23  ? 17  LEU A HD23 1 
ATOM   347  N N    . ASP A 1 18  ? 16.681 6.399  21.749 1.000 12.68  ? 18  ASP A N    1 
ATOM   348  C CA   . ASP A 1 18  ? 16.925 4.975  21.999 1.000 12.20  ? 18  ASP A CA   1 
ATOM   349  C C    . ASP A 1 18  ? 16.055 4.202  20.994 1.000 12.45  ? 18  ASP A C    1 
ATOM   350  O O    . ASP A 1 18  ? 14.837 4.346  20.988 1.000 13.78  ? 18  ASP A O    1 
ATOM   351  C CB   . ASP A 1 18  ? 16.593 4.592  23.416 1.000 13.92  ? 18  ASP A CB   1 
ATOM   352  C CG   . ASP A 1 18  ? 16.903 3.150  23.781 1.000 17.02  ? 18  ASP A CG   1 
ATOM   353  O OD1  . ASP A 1 18  ? 17.763 2.552  23.097 1.000 15.31  ? 18  ASP A OD1  1 
ATOM   354  O OD2  . ASP A 1 18  ? 16.292 2.660  24.755 1.000 26.42  ? 18  ASP A OD2  1 
ATOM   355  D D    . ASP A 1 18  ? 16.131 6.915  22.400 1.000 12.76  ? 18  ASP A D    1 
ATOM   356  H HA   . ASP A 1 18  ? 17.985 4.751  21.804 1.000 12.81  ? 18  ASP A HA   1 
ATOM   357  H HB2  . ASP A 1 18  ? 17.145 5.246  24.090 1.000 14.20  ? 18  ASP A HB2  1 
ATOM   358  H HB3  . ASP A 1 18  ? 15.530 4.770  23.582 1.000 19.24  ? 18  ASP A HB3  1 
ATOM   359  N N    . ASN A 1 19  ? 16.709 3.432  20.145 1.000 10.40  ? 19  ASN A N    1 
ATOM   360  C CA   . ASN A 1 19  ? 16.044 2.610  19.164 1.000 11.31  ? 19  ASN A CA   1 
ATOM   361  C C    . ASN A 1 19  ? 15.408 3.430  18.040 1.000 11.09  ? 19  ASN A C    1 
ATOM   362  O O    . ASN A 1 19  ? 14.540 2.920  17.341 1.000 13.84  ? 19  ASN A O    1 
ATOM   363  C CB   . ASN A 1 19  ? 15.038 1.648  19.815 1.000 11.94  ? 19  ASN A CB   1 
ATOM   364  C CG   . ASN A 1 19  ? 14.737 0.471  18.935 1.000 13.16  ? 19  ASN A CG   1 
ATOM   365  O OD1  . ASN A 1 19  ? 15.590 -0.010 18.185 1.000 15.80  ? 19  ASN A OD1  1 
ATOM   366  N ND2  . ASN A 1 19  ? 13.499 -0.014 19.032 1.000 14.85  ? 19  ASN A ND2  1 
ATOM   367  D D    . ASN A 1 19  ? 17.715 3.442  20.092 1.000 12.11  ? 19  ASN A D    1 
ATOM   368  H HA   . ASN A 1 19  ? 16.820 1.986  18.697 1.000 14.15  ? 19  ASN A HA   1 
ATOM   369  H HB2  . ASN A 1 19  ? 15.442 1.294  20.763 1.000 15.80  ? 19  ASN A HB2  1 
ATOM   370  H HB3  . ASN A 1 19  ? 14.112 2.185  20.025 1.000 13.55  ? 19  ASN A HB3  1 
ATOM   371  D DD21 . ASN A 1 19  ? 13.263 -0.843 18.515 1.000 17.68  ? 19  ASN A DD21 1 
ATOM   372  D DD22 . ASN A 1 19  ? 12.848 0.445  19.648 1.000 18.61  ? 19  ASN A DD22 1 
ATOM   373  N N    . TYR A 1 20  ? 15.879 4.669  17.867 1.000 10.70  ? 20  TYR A N    1 
ATOM   374  C CA   . TYR A 1 20  ? 15.464 5.423  16.686 1.000 10.72  ? 20  TYR A CA   1 
ATOM   375  C C    . TYR A 1 20  ? 15.989 4.763  15.410 1.000 10.56  ? 20  TYR A C    1 
ATOM   376  O O    . TYR A 1 20  ? 17.207 4.645  15.257 1.000 11.31  ? 20  TYR A O    1 
ATOM   377  C CB   . TYR A 1 20  ? 15.900 6.887  16.821 1.000 11.13  ? 20  TYR A CB   1 
ATOM   378  C CG   . TYR A 1 20  ? 15.421 7.733  15.661 1.000 11.11  ? 20  TYR A CG   1 
ATOM   379  C CD1  . TYR A 1 20  ? 14.120 8.214  15.634 1.000 14.06  ? 20  TYR A CD1  1 
ATOM   380  C CD2  . TYR A 1 20  ? 16.263 8.006  14.600 1.000 13.24  ? 20  TYR A CD2  1 
ATOM   381  C CE1  . TYR A 1 20  ? 13.687 8.972  14.569 1.000 15.75  ? 20  TYR A CE1  1 
ATOM   382  C CE2  . TYR A 1 20  ? 15.831 8.771  13.535 1.000 15.08  ? 20  TYR A CE2  1 
ATOM   383  C CZ   . TYR A 1 20  ? 14.542 9.248  13.535 1.000 16.44  ? 20  TYR A CZ   1 
ATOM   384  O OH   . TYR A 1 20  ? 14.059 10.005 12.499 1.000 18.96  ? 20  TYR A OH   1 
ATOM   385  H H    . TYR A 1 20  ? 16.510 5.077  18.542 1.000 20.00  ? 20  TYR A H    1 
ATOM   386  H HA   . TYR A 1 20  ? 14.365 5.403  16.645 1.000 11.53  ? 20  TYR A HA   1 
ATOM   387  H HB2  . TYR A 1 20  ? 15.502 7.295  17.750 1.000 14.68  ? 20  TYR A HB2  1 
ATOM   388  H HB3  . TYR A 1 20  ? 16.987 6.933  16.874 1.000 12.23  ? 20  TYR A HB3  1 
ATOM   389  H HD1  . TYR A 1 20  ? 13.447 7.995  16.449 1.000 16.07  ? 20  TYR A HD1  1 
ATOM   390  H HD2  . TYR A 1 20  ? 17.270 7.618  14.605 1.000 14.15  ? 20  TYR A HD2  1 
ATOM   391  H HE1  . TYR A 1 20  ? 12.674 9.347  14.549 1.000 15.95  ? 20  TYR A HE1  1 
ATOM   392  H HE2  . TYR A 1 20  ? 16.496 8.991  12.713 1.000 17.85  ? 20  TYR A HE2  1 
ATOM   393  D DH   . TYR A 1 20  ? 14.804 9.997  11.831 1.000 24.19  ? 20  TYR A DH   1 
ATOM   394  N N    . ARG A 1 21  ? 15.064 4.358  14.548 1.000 10.39  ? 21  ARG A N    1 
ATOM   395  C CA   . ARG A 1 21  ? 15.440 3.638  13.311 1.000 11.67  ? 21  ARG A CA   1 
ATOM   396  C C    . ARG A 1 21  ? 16.370 2.475  13.538 1.000 11.49  ? 21  ARG A C    1 
ATOM   397  O O    . ARG A 1 21  ? 17.184 2.192  12.668 1.000 13.09  ? 21  ARG A O    1 
ATOM   398  C CB   . ARG A 1 21  ? 15.983 4.637  12.277 1.000 13.03  ? 21  ARG A CB   1 
ATOM   399  C CG   . ARG A 1 21  ? 14.945 5.644  11.818 1.000 16.85  ? 21  ARG A CG   1 
ATOM   400  C CD   . ARG A 1 21  ? 13.770 5.021  11.068 1.000 20.46  ? 21  ARG A CD   1 
ATOM   401  N NE   . ARG A 1 21  ? 14.232 4.275  9.887  1.000 23.02  ? 21  ARG A NE   1 
ATOM   402  C CZ   . ARG A 1 21  ? 14.478 4.850  8.724  1.000 24.85  ? 21  ARG A CZ   1 
ATOM   403  N NH1  . ARG A 1 21  ? 14.067 6.107  8.569  1.000 26.85  ? 21  ARG A NH1  1 
ATOM   404  N NH2  . ARG A 1 21  ? 15.054 4.156  7.746  1.000 29.58  ? 21  ARG A NH2  1 
ATOM   405  D D    . ARG A 1 21  ? 14.083 4.462  14.683 1.000 14.07  ? 21  ARG A D    1 
ATOM   406  H HA   . ARG A 1 21  ? 14.511 3.222  12.892 1.000 16.01  ? 21  ARG A HA   1 
ATOM   407  H HB2  . ARG A 1 21  ? 16.827 5.172  12.711 1.000 17.40  ? 21  ARG A HB2  1 
ATOM   408  H HB3  . ARG A 1 21  ? 16.348 4.086  11.410 1.000 19.44  ? 21  ARG A HB3  1 
ATOM   409  H HG2  . ARG A 1 21  ? 14.562 6.176  12.690 1.000 14.42  ? 21  ARG A HG2  1 
ATOM   410  H HG3  . ARG A 1 21  ? 15.427 6.376  11.170 1.000 23.25  ? 21  ARG A HG3  1 
ATOM   411  H HD2  . ARG A 1 21  ? 13.231 4.347  11.734 1.000 23.29  ? 21  ARG A HD2  1 
ATOM   412  H HD3  . ARG A 1 21  ? 13.082 5.806  10.754 1.000 167.91 ? 21  ARG A HD3  1 
ATOM   413  D DE   . ARG A 1 21  ? 14.316 3.283  10.065 1.000 22.28  ? 21  ARG A DE   1 
ATOM   414  D DH11 . ARG A 1 21  ? 14.084 6.507  7.628  1.000 26.94  ? 21  ARG A DH11 1 
ATOM   415  D DH12 . ARG A 1 21  ? 13.633 6.589  9.336  1.000 26.07  ? 21  ARG A DH12 1 
ATOM   416  D DH21 . ARG A 1 21  ? 15.471 4.628  6.964  1.000 30.34  ? 21  ARG A DH21 1 
ATOM   417  D DH22 . ARG A 1 21  ? 15.103 3.153  7.807  1.000 30.25  ? 21  ARG A DH22 1 
ATOM   418  N N    . GLY A 1 22  ? 16.189 1.793  14.664 1.000 11.13  ? 22  GLY A N    1 
ATOM   419  C CA   . GLY A 1 22  ? 16.891 0.588  15.012 1.000 12.37  ? 22  GLY A CA   1 
ATOM   420  C C    . GLY A 1 22  ? 18.285 0.764  15.578 1.000 12.27  ? 22  GLY A C    1 
ATOM   421  O O    . GLY A 1 22  ? 19.046 -0.196 15.665 1.000 14.41  ? 22  GLY A O    1 
ATOM   422  D D    . GLY A 1 22  ? 15.535 2.201  15.297 1.000 11.85  ? 22  GLY A D    1 
ATOM   423  H HA2  . GLY A 1 22  ? 16.293 0.043  15.742 1.000 15.29  ? 22  GLY A HA2  1 
ATOM   424  H HA3  . GLY A 1 22  ? 16.962 -0.034 14.120 1.000 15.33  ? 22  GLY A HA3  1 
ATOM   425  N N    . TYR A 1 23  ? 18.633 1.978  15.982 1.000 11.25  ? 23  TYR A N    1 
ATOM   426  C CA   . TYR A 1 23  ? 19.928 2.268  16.597 1.000 11.19  ? 23  TYR A CA   1 
ATOM   427  C C    . TYR A 1 23  ? 19.750 2.485  18.114 1.000 11.76  ? 23  TYR A C    1 
ATOM   428  O O    . TYR A 1 23  ? 19.167 3.487  18.553 1.000 11.06  ? 23  TYR A O    1 
ATOM   429  C CB   . TYR A 1 23  ? 20.588 3.466  15.948 1.000 11.35  ? 23  TYR A CB   1 
ATOM   430  C CG   . TYR A 1 23  ? 20.998 3.224  14.517 1.000 11.41  ? 23  TYR A CG   1 
ATOM   431  C CD1  . TYR A 1 23  ? 22.140 2.502  14.193 1.000 11.92  ? 23  TYR A CD1  1 
ATOM   432  C CD2  . TYR A 1 23  ? 20.231 3.736  13.485 1.000 12.73  ? 23  TYR A CD2  1 
ATOM   433  C CE1  . TYR A 1 23  ? 22.505 2.295  12.871 1.000 13.15  ? 23  TYR A CE1  1 
ATOM   434  C CE2  . TYR A 1 23  ? 20.561 3.539  12.154 1.000 14.09  ? 23  TYR A CE2  1 
ATOM   435  C CZ   . TYR A 1 23  ? 21.705 2.814  11.876 1.000 14.09  ? 23  TYR A CZ   1 
ATOM   436  O OH   . TYR A 1 23  ? 21.973 2.658  10.541 1.000 16.77  ? 23  TYR A OH   1 
ATOM   437  H H    . TYR A 1 23  ? 17.976 2.736  15.859 1.000 16.03  ? 23  TYR A H    1 
ATOM   438  H HA   . TYR A 1 23  ? 20.581 1.395  16.450 1.000 14.25  ? 23  TYR A HA   1 
ATOM   439  H HB2  . TYR A 1 23  ? 19.897 4.309  15.980 1.000 18.23  ? 23  TYR A HB2  1 
ATOM   440  H HB3  . TYR A 1 23  ? 21.470 3.739  16.527 1.000 13.98  ? 23  TYR A HB3  1 
ATOM   441  H HD1  . TYR A 1 23  ? 22.753 2.095  14.983 1.000 14.93  ? 23  TYR A HD1  1 
ATOM   442  H HD2  . TYR A 1 23  ? 19.348 4.309  13.725 1.000 15.39  ? 23  TYR A HD2  1 
ATOM   443  H HE1  . TYR A 1 23  ? 23.398 1.740  12.627 1.000 18.19  ? 23  TYR A HE1  1 
ATOM   444  H HE2  . TYR A 1 23  ? 19.946 3.937  11.361 1.000 17.38  ? 23  TYR A HE2  1 
ATOM   445  D DH   . TYR A 1 23  ? 22.650 1.992  10.387 1.000 21.50  ? 23  TYR A DH   1 
ATOM   446  N N    . SER A 1 24  ? 20.285 1.529  18.881 1.000 12.12  ? 24  SER A N    1 
ATOM   447  C CA   . SER A 1 24  ? 20.227 1.654  20.330 1.000 12.21  ? 24  SER A CA   1 
ATOM   448  C C    . SER A 1 24  ? 20.944 2.893  20.844 1.000 10.51  ? 24  SER A C    1 
ATOM   449  O O    . SER A 1 24  ? 21.838 3.438  20.219 1.000 12.68  ? 24  SER A O    1 
ATOM   450  C CB   . SER A 1 24  ? 20.843 0.409  20.970 1.000 13.83  ? 24  SER A CB   1 
ATOM   451  O OG   . SER A 1 24  ? 22.236 0.336  20.703 1.000 16.02  ? 24  SER A OG   1 
ATOM   452  D D    . SER A 1 24  ? 20.688 0.722  18.425 1.000 13.85  ? 24  SER A D    1 
ATOM   453  H HA   . SER A 1 24  ? 19.171 1.713  20.632 1.000 10.71  ? 24  SER A HA   1 
ATOM   454  H HB2  . SER A 1 24  ? 20.681 0.436  22.047 1.000 15.59  ? 24  SER A HB2  1 
ATOM   455  H HB3  . SER A 1 24  ? 20.352 -0.481 20.577 1.000 16.31  ? 24  SER A HB3  1 
ATOM   456  D DG   . SER A 1 24  ? 22.647 -0.245 21.374 1.000 21.96  ? 24  SER A DG   1 
ATOM   457  N N    . LEU A 1 25  ? 20.528 3.317  22.044 1.000 11.00  ? 25  LEU A N    1 
ATOM   458  C CA   . LEU A 1 25  ? 21.093 4.497  22.684 1.000 10.56  ? 25  LEU A CA   1 
ATOM   459  C C    . LEU A 1 25  ? 22.598 4.515  22.728 1.000 11.14  ? 25  LEU A C    1 
ATOM   460  O O    . LEU A 1 25  ? 23.220 5.558  22.511 1.000 12.82  ? 25  LEU A O    1 
ATOM   461  C CB   . LEU A 1 25  ? 20.533 4.543  24.106 1.000 11.04  ? 25  LEU A CB   1 
ATOM   462  C CG   . LEU A 1 25  ? 20.786 5.807  24.900 1.000 13.12  ? 25  LEU A CG   1 
ATOM   463  C CD1  . LEU A 1 25  ? 20.223 7.057  24.249 1.000 13.07  ? 25  LEU A CD1  1 
ATOM   464  C CD2  . LEU A 1 25  ? 20.183 5.735  26.291 1.000 12.45  ? 25  LEU A CD2  1 
ATOM   465  D D    . LEU A 1 25  ? 19.758 2.862  22.490 1.000 11.46  ? 25  LEU A D    1 
ATOM   466  H HA   . LEU A 1 25  ? 20.747 5.390  22.142 1.000 11.21  ? 25  LEU A HA   1 
ATOM   467  H HB2  . LEU A 1 25  ? 19.455 4.390  24.050 1.000 13.92  ? 25  LEU A HB2  1 
ATOM   468  H HB3  . LEU A 1 25  ? 20.951 3.704  24.662 1.000 13.04  ? 25  LEU A HB3  1 
ATOM   469  H HG   . LEU A 1 25  ? 21.874 5.935  25.004 1.000 12.05  ? 25  LEU A HG   1 
ATOM   470  H HD11 . LEU A 1 25  ? 19.174 6.956  24.139 1.000 36.48  ? 25  LEU A HD11 1 
ATOM   471  H HD12 . LEU A 1 25  ? 20.435 7.899  24.857 1.000 20.26  ? 25  LEU A HD12 1 
ATOM   472  H HD13 . LEU A 1 25  ? 20.667 7.189  23.295 1.000 27.55  ? 25  LEU A HD13 1 
ATOM   473  H HD21 . LEU A 1 25  ? 19.133 5.612  26.214 1.000 21.87  ? 25  LEU A HD21 1 
ATOM   474  H HD22 . LEU A 1 25  ? 20.598 4.912  26.814 1.000 18.07  ? 25  LEU A HD22 1 
ATOM   475  H HD23 . LEU A 1 25  ? 20.396 6.631  26.815 1.000 14.02  ? 25  LEU A HD23 1 
ATOM   476  N N    . GLY A 1 26  ? 23.236 3.389  23.036 1.000 10.47  ? 26  GLY A N    1 
ATOM   477  C CA   . GLY A 1 26  ? 24.686 3.351  23.089 1.000 11.31  ? 26  GLY A CA   1 
ATOM   478  C C    . GLY A 1 26  ? 25.400 3.763  21.829 1.000 10.36  ? 26  GLY A C    1 
ATOM   479  O O    . GLY A 1 26  ? 26.500 4.321  21.840 1.000 11.56  ? 26  GLY A O    1 
ATOM   480  D D    . GLY A 1 26  ? 22.707 2.567  23.275 1.000 12.34  ? 26  GLY A D    1 
ATOM   481  H HA2  . GLY A 1 26  ? 25.016 4.002  23.899 1.000 11.39  ? 26  GLY A HA2  1 
ATOM   482  H HA3  . GLY A 1 26  ? 24.993 2.336  23.340 1.000 14.33  ? 26  GLY A HA3  1 
ATOM   483  N N    . ASN A 1 27  ? 24.778 3.488  20.668 1.000 9.76   ? 27  ASN A N    1 
ATOM   484  C CA   . ASN A 1 27  ? 25.359 3.929  19.403 1.000 10.14  ? 27  ASN A CA   1 
ATOM   485  C C    . ASN A 1 27  ? 25.478 5.475  19.353 1.000 10.21  ? 27  ASN A C    1 
ATOM   486  O O    . ASN A 1 27  ? 26.482 5.965  18.827 1.000 9.92   ? 27  ASN A O    1 
ATOM   487  C CB   . ASN A 1 27  ? 24.524 3.479  18.210 1.000 11.03  ? 27  ASN A CB   1 
ATOM   488  C CG   . ASN A 1 27  ? 24.726 2.001  17.932 1.000 11.03  ? 27  ASN A CG   1 
ATOM   489  O OD1  . ASN A 1 27  ? 25.753 1.616  17.413 1.000 14.62  ? 27  ASN A OD1  1 
ATOM   490  N ND2  . ASN A 1 27  ? 23.738 1.168  18.221 1.000 14.55  ? 27  ASN A ND2  1 
ATOM   491  H H    . ASN A 1 27  ? 23.907 2.975  20.671 1.000 14.00  ? 27  ASN A H    1 
ATOM   492  H HA   . ASN A 1 27  ? 26.366 3.496  19.309 1.000 11.61  ? 27  ASN A HA   1 
ATOM   493  H HB2  . ASN A 1 27  ? 23.470 3.670  18.413 1.000 13.88  ? 27  ASN A HB2  1 
ATOM   494  H HB3  . ASN A 1 27  ? 24.808 4.056  17.330 1.000 11.79  ? 27  ASN A HB3  1 
ATOM   495  D DD21 . ASN A 1 27  ? 23.808 0.208  17.980 1.000 18.00  ? 27  ASN A DD21 1 
ATOM   496  D DD22 . ASN A 1 27  ? 22.926 1.497  18.691 1.000 15.78  ? 27  ASN A DD22 1 
ATOM   497  N N    . TRP A 1 28  ? 24.448 6.177  19.809 1.000 9.61   ? 28  TRP A N    1 
ATOM   498  C CA   . TRP A 1 28  ? 24.420 7.647  19.771 1.000 9.88   ? 28  TRP A CA   1 
ATOM   499  C C    . TRP A 1 28  ? 25.430 8.227  20.749 1.000 9.39   ? 28  TRP A C    1 
ATOM   500  O O    . TRP A 1 28  ? 26.128 9.197  20.448 1.000 10.22  ? 28  TRP A O    1 
ATOM   501  C CB   . TRP A 1 28  ? 22.995 8.086  20.066 1.000 9.85   ? 28  TRP A CB   1 
ATOM   502  C CG   . TRP A 1 28  ? 22.009 7.613  19.050 1.000 9.82   ? 28  TRP A CG   1 
ATOM   503  C CD1  . TRP A 1 28  ? 21.146 6.562  19.202 1.000 11.31  ? 28  TRP A CD1  1 
ATOM   504  C CD2  . TRP A 1 28  ? 21.777 8.148  17.742 1.000 10.51  ? 28  TRP A CD2  1 
ATOM   505  N NE1  . TRP A 1 28  ? 20.388 6.399  18.086 1.000 13.01  ? 28  TRP A NE1  1 
ATOM   506  C CE2  . TRP A 1 28  ? 20.749 7.351  17.176 1.000 12.74  ? 28  TRP A CE2  1 
ATOM   507  C CE3  . TRP A 1 28  ? 22.339 9.197  17.016 1.000 14.00  ? 28  TRP A CE3  1 
ATOM   508  C CZ2  . TRP A 1 28  ? 20.244 7.571  15.876 1.000 16.24  ? 28  TRP A CZ2  1 
ATOM   509  C CZ3  . TRP A 1 28  ? 21.850 9.447  15.730 1.000 17.58  ? 28  TRP A CZ3  1 
ATOM   510  C CH2  . TRP A 1 28  ? 20.827 8.640  15.210 1.000 19.08  ? 28  TRP A CH2  1 
ATOM   511  H H    . TRP A 1 28  ? 23.656 5.685  20.196 1.000 12.26  ? 28  TRP A H    1 
ATOM   512  H HA   . TRP A 1 28  ? 24.686 7.976  18.756 1.000 9.87   ? 28  TRP A HA   1 
ATOM   513  H HB2  . TRP A 1 28  ? 22.704 7.706  21.045 1.000 11.63  ? 28  TRP A HB2  1 
ATOM   514  H HB3  . TRP A 1 28  ? 22.963 9.175  20.110 1.000 15.09  ? 28  TRP A HB3  1 
ATOM   515  H HD1  . TRP A 1 28  ? 21.076 5.947  20.087 1.000 13.89  ? 28  TRP A HD1  1 
ATOM   516  H HE1  . TRP A 1 28  ? 19.678 5.693  17.952 1.000 22.95  ? 28  TRP A HE1  1 
ATOM   517  H HE3  . TRP A 1 28  ? 23.132 9.800  17.434 1.000 20.65  ? 28  TRP A HE3  1 
ATOM   518  H HZ2  . TRP A 1 28  ? 19.469 6.960  15.438 1.000 20.95  ? 28  TRP A HZ2  1 
ATOM   519  H HZ3  . TRP A 1 28  ? 22.255 10.257 15.142 1.000 21.26  ? 28  TRP A HZ3  1 
ATOM   520  H HH2  . TRP A 1 28  ? 20.468 8.866  14.217 1.000 22.04  ? 28  TRP A HH2  1 
ATOM   521  N N    . VAL A 1 29  ? 25.521 7.638  21.949 1.000 9.42   ? 29  VAL A N    1 
ATOM   522  C CA   . VAL A 1 29  ? 26.483 8.113  22.935 1.000 9.49   ? 29  VAL A CA   1 
ATOM   523  C C    . VAL A 1 29  ? 27.902 7.865  22.424 1.000 9.77   ? 29  VAL A C    1 
ATOM   524  O O    . VAL A 1 29  ? 28.746 8.748  22.505 1.000 9.98   ? 29  VAL A O    1 
ATOM   525  C CB   . VAL A 1 29  ? 26.247 7.467  24.299 1.000 10.50  ? 29  VAL A CB   1 
ATOM   526  C CG1  . VAL A 1 29  ? 27.307 7.877  25.309 1.000 11.60  ? 29  VAL A CG1  1 
ATOM   527  C CG2  . VAL A 1 29  ? 24.854 7.773  24.833 1.000 12.16  ? 29  VAL A CG2  1 
ATOM   528  H H    . VAL A 1 29  ? 24.919 6.858  22.171 1.000 10.59  ? 29  VAL A H    1 
ATOM   529  H HA   . VAL A 1 29  ? 26.347 9.199  23.046 1.000 10.02  ? 29  VAL A HA   1 
ATOM   530  H HB   . VAL A 1 29  ? 26.320 6.377  24.167 1.000 12.57  ? 29  VAL A HB   1 
ATOM   531  H HG11 . VAL A 1 29  ? 27.264 8.925  25.459 1.000 15.06  ? 29  VAL A HG11 1 
ATOM   532  H HG12 . VAL A 1 29  ? 27.130 7.380  26.228 1.000 13.50  ? 29  VAL A HG12 1 
ATOM   533  H HG13 . VAL A 1 29  ? 28.265 7.612  24.942 1.000 14.63  ? 29  VAL A HG13 1 
ATOM   534  H HG21 . VAL A 1 29  ? 24.751 8.819  24.972 1.000 15.65  ? 29  VAL A HG21 1 
ATOM   535  H HG22 . VAL A 1 29  ? 24.127 7.436  24.139 1.000 16.16  ? 29  VAL A HG22 1 
ATOM   536  H HG23 . VAL A 1 29  ? 24.714 7.278  25.760 1.000 16.79  ? 29  VAL A HG23 1 
ATOM   537  N N    . CYS A 1 30  ? 28.166 6.695  21.870 1.000 9.59   ? 30  CYS A N    1 
ATOM   538  C CA   . CYS A 1 30  ? 29.477 6.412  21.282 1.000 10.01  ? 30  CYS A CA   1 
ATOM   539  C C    . CYS A 1 30  ? 29.808 7.365  20.147 1.000 10.12  ? 30  CYS A C    1 
ATOM   540  O O    . CYS A 1 30  ? 30.953 7.831  20.021 1.000 9.77   ? 30  CYS A O    1 
ATOM   541  C CB   . CYS A 1 30  ? 29.468 4.961  20.796 1.000 10.79  ? 30  CYS A CB   1 
ATOM   542  S SG   . CYS A 1 30  ? 31.060 4.376  20.170 1.000 9.99   ? 30  CYS A SG   1 
ATOM   543  H H    . CYS A 1 30  ? 27.450 5.982  21.852 1.000 11.81  ? 30  CYS A H    1 
ATOM   544  H HA   . CYS A 1 30  ? 30.243 6.516  22.064 1.000 12.12  ? 30  CYS A HA   1 
ATOM   545  H HB2  . CYS A 1 30  ? 29.160 4.319  21.621 1.000 13.89  ? 30  CYS A HB2  1 
ATOM   546  H HB3  . CYS A 1 30  ? 28.724 4.862  20.006 1.000 13.32  ? 30  CYS A HB3  1 
ATOM   547  N N    . ALA A 1 31  ? 28.846 7.685  19.263 1.000 9.68   ? 31  ALA A N    1 
ATOM   548  C CA   . ALA A 1 31  ? 29.117 8.599  18.139 1.000 9.81   ? 31  ALA A CA   1 
ATOM   549  C C    . ALA A 1 31  ? 29.535 9.955  18.715 1.000 9.52   ? 31  ALA A C    1 
ATOM   550  O O    . ALA A 1 31  ? 30.473 10.589 18.241 1.000 10.39  ? 31  ALA A O    1 
ATOM   551  C CB   . ALA A 1 31  ? 27.900 8.693  17.254 1.000 10.00  ? 31  ALA A CB   1 
ATOM   552  H H    . ALA A 1 31  ? 27.922 7.291  19.371 1.000 14.15  ? 31  ALA A H    1 
ATOM   553  H HA   . ALA A 1 31  ? 29.952 8.195  17.548 1.000 11.67  ? 31  ALA A HA   1 
ATOM   554  H HB1  . ALA A 1 31  ? 27.087 9.082  17.812 1.000 12.43  ? 31  ALA A HB1  1 
ATOM   555  H HB2  . ALA A 1 31  ? 28.107 9.334  16.436 1.000 12.29  ? 31  ALA A HB2  1 
ATOM   556  H HB3  . ALA A 1 31  ? 27.651 7.728  16.892 1.000 14.60  ? 31  ALA A HB3  1 
ATOM   557  N N    . ALA A 1 32  ? 28.806 10.447 19.721 1.000 9.51   ? 32  ALA A N    1 
ATOM   558  C CA   . ALA A 1 32  ? 29.141 11.746 20.294 1.000 9.16   ? 32  ALA A CA   1 
ATOM   559  C C    . ALA A 1 32  ? 30.522 11.744 20.959 1.000 9.81   ? 32  ALA A C    1 
ATOM   560  O O    . ALA A 1 32  ? 31.291 12.703 20.831 1.000 9.83   ? 32  ALA A O    1 
ATOM   561  C CB   . ALA A 1 32  ? 28.076 12.195 21.288 1.000 9.56   ? 32  ALA A CB   1 
ATOM   562  H H    . ALA A 1 32  ? 28.025 9.920  20.085 1.000 11.60  ? 32  ALA A H    1 
ATOM   563  H HA   . ALA A 1 32  ? 29.165 12.479 19.474 1.000 12.33  ? 32  ALA A HA   1 
ATOM   564  H HB1  . ALA A 1 32  ? 28.031 11.505 22.092 1.000 11.40  ? 32  ALA A HB1  1 
ATOM   565  H HB2  . ALA A 1 32  ? 28.323 13.156 21.660 1.000 12.22  ? 32  ALA A HB2  1 
ATOM   566  H HB3  . ALA A 1 32  ? 27.135 12.234 20.803 1.000 14.37  ? 32  ALA A HB3  1 
ATOM   567  N N    . LYS A 1 33  ? 30.867 10.659 21.659 1.000 9.54   ? 33  LYS A N    1 
ATOM   568  C CA   . LYS A 1 33  ? 32.167 10.537 22.307 1.000 9.56   ? 33  LYS A CA   1 
ATOM   569  C C    . LYS A 1 33  ? 33.283 10.750 21.278 1.000 10.20  ? 33  LYS A C    1 
ATOM   570  O O    . LYS A 1 33  ? 34.216 11.505 21.521 1.000 9.91   ? 33  LYS A O    1 
ATOM   571  C CB   . LYS A 1 33  ? 32.319 9.180  22.982 1.000 10.62  ? 33  LYS A CB   1 
ATOM   572  C CG   . LYS A 1 33  ? 33.703 8.822  23.469 1.000 12.39  ? 33  LYS A CG   1 
ATOM   573  C CD   . LYS A 1 33  ? 34.201 9.738  24.546 1.000 14.97  ? 33  LYS A CD   1 
ATOM   574  C CE   . LYS A 1 33  ? 35.622 9.395  24.906 1.000 19.67  ? 33  LYS A CE   1 
ATOM   575  N NZ   . LYS A 1 33  ? 36.200 10.297 25.934 1.000 22.10  ? 33  LYS A NZ   1 
ATOM   576  H H    . LYS A 1 33  ? 30.207 9.899  21.741 1.000 11.74  ? 33  LYS A H    1 
ATOM   577  H HA   . LYS A 1 33  ? 32.248 11.319 23.076 1.000 9.97   ? 33  LYS A HA   1 
ATOM   578  H HB2  . LYS A 1 33  ? 31.640 9.145  23.833 1.000 12.51  ? 33  LYS A HB2  1 
ATOM   579  H HB3  . LYS A 1 33  ? 31.997 8.412  22.278 1.000 12.71  ? 33  LYS A HB3  1 
ATOM   580  H HG2  . LYS A 1 33  ? 33.692 7.800  23.850 1.000 15.21  ? 33  LYS A HG2  1 
ATOM   581  H HG3  . LYS A 1 33  ? 34.395 8.855  22.627 1.000 17.79  ? 33  LYS A HG3  1 
ATOM   582  H HD2  . LYS A 1 33  ? 34.151 10.771 24.200 1.000 18.89  ? 33  LYS A HD2  1 
ATOM   583  H HD3  . LYS A 1 33  ? 33.567 9.645  25.427 1.000 16.62  ? 33  LYS A HD3  1 
ATOM   584  H HE2  . LYS A 1 33  ? 35.655 8.370  25.275 1.000 22.01  ? 33  LYS A HE2  1 
ATOM   585  H HE3  . LYS A 1 33  ? 36.236 9.444  24.006 1.000 19.06  ? 33  LYS A HE3  1 
ATOM   586  D DZ1  . LYS A 1 33  ? 36.261 11.261 25.563 1.000 22.90  ? 33  LYS A DZ1  1 
ATOM   587  D DZ2  . LYS A 1 33  ? 35.608 10.290 26.780 1.000 23.66  ? 33  LYS A DZ2  1 
ATOM   588  D DZ3  . LYS A 1 33  ? 37.143 9.988  26.183 1.000 23.73  ? 33  LYS A DZ3  1 
ATOM   589  N N    . PHE A 1 34  ? 33.196 10.044 20.143 1.000 10.16  ? 34  PHE A N    1 
ATOM   590  C CA   . PHE A 1 34  ? 34.320 10.070 19.214 1.000 10.50  ? 34  PHE A CA   1 
ATOM   591  C C    . PHE A 1 34  ? 34.252 11.187 18.190 1.000 10.59  ? 34  PHE A C    1 
ATOM   592  O O    . PHE A 1 34  ? 35.275 11.538 17.591 1.000 13.83  ? 34  PHE A O    1 
ATOM   593  C CB   . PHE A 1 34  ? 34.509 8.694  18.576 1.000 10.97  ? 34  PHE A CB   1 
ATOM   594  C CG   . PHE A 1 34  ? 34.983 7.693  19.610 1.000 12.48  ? 34  PHE A CG   1 
ATOM   595  C CD1  . PHE A 1 34  ? 36.255 7.828  20.163 1.000 13.02  ? 34  PHE A CD1  1 
ATOM   596  C CD2  . PHE A 1 34  ? 34.206 6.651  20.058 1.000 13.23  ? 34  PHE A CD2  1 
ATOM   597  C CE1  . PHE A 1 34  ? 36.693 6.929  21.111 1.000 14.96  ? 34  PHE A CE1  1 
ATOM   598  C CE2  . PHE A 1 34  ? 34.647 5.754  21.007 1.000 15.72  ? 34  PHE A CE2  1 
ATOM   599  C CZ   . PHE A 1 34  ? 35.910 5.876  21.569 1.000 15.89  ? 34  PHE A CZ   1 
ATOM   600  H H    . PHE A 1 34  ? 32.368 9.504  19.935 1.000 10.55  ? 34  PHE A H    1 
ATOM   601  H HA   . PHE A 1 34  ? 35.219 10.257 19.819 1.000 11.02  ? 34  PHE A HA   1 
ATOM   602  H HB2  . PHE A 1 34  ? 33.564 8.357  18.147 1.000 14.44  ? 34  PHE A HB2  1 
ATOM   603  H HB3  . PHE A 1 34  ? 35.241 8.762  17.771 1.000 12.28  ? 34  PHE A HB3  1 
ATOM   604  H HD1  . PHE A 1 34  ? 36.897 8.638  19.849 1.000 15.76  ? 34  PHE A HD1  1 
ATOM   605  H HD2  . PHE A 1 34  ? 33.213 6.530  19.650 1.000 16.37  ? 34  PHE A HD2  1 
ATOM   606  H HE1  . PHE A 1 34  ? 37.688 7.047  21.515 1.000 17.41  ? 34  PHE A HE1  1 
ATOM   607  H HE2  . PHE A 1 34  ? 34.001 4.946  21.317 1.000 16.82  ? 34  PHE A HE2  1 
ATOM   608  H HZ   . PHE A 1 34  ? 36.266 5.189  22.323 1.000 25.23  ? 34  PHE A HZ   1 
ATOM   609  N N    . GLU A 1 35  ? 33.081 11.798 18.003 1.000 10.01  ? 35  GLU A N    1 
ATOM   610  C CA   . GLU A 1 35  ? 32.948 12.960 17.148 1.000 10.07  ? 35  GLU A CA   1 
ATOM   611  C C    . GLU A 1 35  ? 33.469 14.218 17.860 1.000 9.36   ? 35  GLU A C    1 
ATOM   612  O O    . GLU A 1 35  ? 34.213 15.004 17.276 1.000 11.30  ? 35  GLU A O    1 
ATOM   613  C CB   . GLU A 1 35  ? 31.491 13.185 16.640 1.000 9.23   ? 35  GLU A CB   1 
ATOM   614  C CG   . GLU A 1 35  ? 31.014 12.196 15.601 1.000 10.56  ? 35  GLU A CG   1 
ATOM   615  C CD   . GLU A 1 35  ? 31.703 12.304 14.250 1.000 10.98  ? 35  GLU A CD   1 
ATOM   616  O OE1  . GLU A 1 35  ? 31.638 11.345 13.458 1.000 13.63  ? 35  GLU A OE1  1 
ATOM   617  O OE2  . GLU A 1 35  ? 32.358 13.349 14.043 1.000 13.83  ? 35  GLU A OE2  1 
ATOM   618  D D    . GLU A 1 35  ? 32.258 11.442 18.421 1.000 12.39  ? 35  GLU A D    1 
ATOM   619  H HA   . GLU A 1 35  ? 33.583 12.794 16.265 1.000 9.94   ? 35  GLU A HA   1 
ATOM   620  H HB2  . GLU A 1 35  ? 30.817 13.140 17.495 1.000 10.74  ? 35  GLU A HB2  1 
ATOM   621  H HB3  . GLU A 1 35  ? 31.423 14.188 16.221 1.000 12.69  ? 35  GLU A HB3  1 
ATOM   622  H HG2  . GLU A 1 35  ? 31.165 11.188 15.986 1.000 12.88  ? 35  GLU A HG2  1 
ATOM   623  H HG3  . GLU A 1 35  ? 29.943 12.335 15.456 1.000 12.88  ? 35  GLU A HG3  1 
ATOM   624  D DE2  . GLU A 1 35  ? 32.920 13.391 13.191 1.000 17.25  ? 35  GLU A DE2  1 
ATOM   625  N N    . SER A 1 36  ? 33.071 14.430 19.113 1.000 10.08  ? 36  SER A N    1 
ATOM   626  C CA   . SER A 1 36  ? 33.261 15.714 19.765 1.000 11.08  ? 36  SER A CA   1 
ATOM   627  C C    . SER A 1 36  ? 33.817 15.601 21.186 1.000 10.62  ? 36  SER A C    1 
ATOM   628  O O    . SER A 1 36  ? 33.976 16.671 21.820 1.000 10.68  ? 36  SER A O    1 
ATOM   629  C CB   . SER A 1 36  ? 31.953 16.507 19.893 1.000 10.18  ? 36  SER A CB   1 
ATOM   630  O OG   . SER A 1 36  ? 31.105 15.811 20.788 1.000 9.02   ? 36  SER A OG   1 
ATOM   631  H H    A SER A 1 36  ? 32.627 13.679 19.622 0.755 8.91   ? 36  SER A H    1 
ATOM   632  D D    B SER A 1 36  ? 32.797 13.639 19.677 0.245 8.41   ? 36  SER A D    1 
ATOM   633  H HA   . SER A 1 36  ? 33.967 16.306 19.164 1.000 11.80  ? 36  SER A HA   1 
ATOM   634  H HB2  . SER A 1 36  ? 32.158 17.508 20.273 1.000 13.50  ? 36  SER A HB2  1 
ATOM   635  H HB3  . SER A 1 36  ? 31.474 16.599 18.918 1.000 14.63  ? 36  SER A HB3  1 
ATOM   636  D DG   . SER A 1 36  ? 30.380 15.419 20.270 1.000 11.21  ? 36  SER A DG   1 
ATOM   637  N N    A ASN A 1 37  ? 34.108 14.414 21.672 0.521 10.97  ? 37  ASN A N    1 
ATOM   638  N N    B ASN A 1 37  ? 34.013 14.412 21.708 0.479 11.39  ? 37  ASN A N    1 
ATOM   639  C CA   A ASN A 1 37  ? 34.382 14.194 23.093 0.521 12.19  ? 37  ASN A CA   1 
ATOM   640  C CA   B ASN A 1 37  ? 34.455 14.288 23.100 0.479 12.12  ? 37  ASN A CA   1 
ATOM   641  C C    A ASN A 1 37  ? 33.401 14.978 23.969 0.521 11.15  ? 37  ASN A C    1 
ATOM   642  C C    B ASN A 1 37  ? 33.390 14.869 24.036 0.479 11.03  ? 37  ASN A C    1 
ATOM   643  O O    A ASN A 1 37  ? 33.770 15.670 24.906 0.521 12.90  ? 37  ASN A O    1 
ATOM   644  O O    B ASN A 1 37  ? 33.689 15.322 25.135 0.479 10.96  ? 37  ASN A O    1 
ATOM   645  C CB   A ASN A 1 37  ? 35.844 14.487 23.455 0.521 13.56  ? 37  ASN A CB   1 
ATOM   646  C CB   B ASN A 1 37  ? 35.837 14.902 23.315 0.479 13.44  ? 37  ASN A CB   1 
ATOM   647  C CG   A ASN A 1 37  ? 36.231 13.736 24.725 0.521 15.09  ? 37  ASN A CG   1 
ATOM   648  C CG   B ASN A 1 37  ? 36.789 13.951 24.025 0.479 15.45  ? 37  ASN A CG   1 
ATOM   649  O OD1  A ASN A 1 37  ? 35.700 12.650 24.970 0.521 15.82  ? 37  ASN A OD1  1 
ATOM   650  O OD1  B ASN A 1 37  ? 36.454 12.778 24.237 0.479 16.21  ? 37  ASN A OD1  1 
ATOM   651  N ND2  A ASN A 1 37  ? 37.152 14.244 25.519 0.521 16.59  ? 37  ASN A ND2  1 
ATOM   652  N ND2  B ASN A 1 37  ? 37.979 14.408 24.390 0.479 15.47  ? 37  ASN A ND2  1 
ATOM   653  D D    A ASN A 1 37  ? 34.129 13.593 21.086 0.521 13.63  ? 37  ASN A D    1 
ATOM   654  D D    B ASN A 1 37  ? 33.829 13.548 21.222 0.479 12.05  ? 37  ASN A D    1 
ATOM   655  H HA   A ASN A 1 37  ? 34.209 13.126 23.292 0.521 9.82   ? 37  ASN A HA   1 
ATOM   656  H HA   B ASN A 1 37  ? 34.536 13.214 23.323 0.479 16.13  ? 37  ASN A HA   1 
ATOM   657  H HB2  A ASN A 1 37  ? 36.493 14.180 22.635 0.521 14.70  ? 37  ASN A HB2  1 
ATOM   658  H HB2  B ASN A 1 37  ? 36.261 15.175 22.349 0.479 15.73  ? 37  ASN A HB2  1 
ATOM   659  H HB3  A ASN A 1 37  ? 35.975 15.558 23.609 0.521 13.87  ? 37  ASN A HB3  1 
ATOM   660  H HB3  B ASN A 1 37  ? 35.736 15.812 23.905 0.479 24.60  ? 37  ASN A HB3  1 
ATOM   661  D DD21 A ASN A 1 37  ? 37.491 13.679 26.295 0.521 17.61  ? 37  ASN A DD21 1 
ATOM   662  D DD21 B ASN A 1 37  ? 38.499 13.911 25.094 0.479 17.87  ? 37  ASN A DD21 1 
ATOM   663  D DD22 A ASN A 1 37  ? 37.518 15.162 25.330 0.521 17.42  ? 37  ASN A DD22 1 
ATOM   664  D DD22 B ASN A 1 37  ? 38.341 15.237 23.963 0.479 16.86  ? 37  ASN A DD22 1 
ATOM   665  N N    . PHE A 1 38  ? 32.131 14.860 23.601 1.000 10.30  ? 38  PHE A N    1 
ATOM   666  C CA   . PHE A 1 38  ? 30.976 15.298 24.384 1.000 9.89   ? 38  PHE A CA   1 
ATOM   667  C C    . PHE A 1 38  ? 30.915 16.811 24.549 1.000 10.57  ? 38  PHE A C    1 
ATOM   668  O O    . PHE A 1 38  ? 30.214 17.294 25.428 1.000 12.81  ? 38  PHE A O    1 
ATOM   669  C CB   . PHE A 1 38  ? 30.906 14.593 25.740 1.000 11.44  ? 38  PHE A CB   1 
ATOM   670  C CG   . PHE A 1 38  ? 30.750 13.094 25.770 1.000 10.80  ? 38  PHE A CG   1 
ATOM   671  C CD1  . PHE A 1 38  ? 30.045 12.395 24.809 1.000 11.01  ? 38  PHE A CD1  1 
ATOM   672  C CD2  . PHE A 1 38  ? 31.342 12.429 26.817 1.000 11.69  ? 38  PHE A CD2  1 
ATOM   673  C CE1  . PHE A 1 38  ? 29.896 11.027 24.932 1.000 11.52  ? 38  PHE A CE1  1 
ATOM   674  C CE2  . PHE A 1 38  ? 31.195 11.053 26.949 1.000 12.63  ? 38  PHE A CE2  1 
ATOM   675  C CZ   . PHE A 1 38  ? 30.473 10.363 25.993 1.000 11.71  ? 38  PHE A CZ   1 
ATOM   676  H H    A PHE A 1 38  ? 31.948 14.432 22.705 1.000 12.36  ? 38  PHE A H    1 
ATOM   677  H HA   . PHE A 1 38  ? 30.078 15.001 23.822 1.000 12.88  ? 38  PHE A HA   1 
ATOM   678  H HB2  . PHE A 1 38  ? 31.814 14.842 26.289 1.000 15.12  ? 38  PHE A HB2  1 
ATOM   679  H HB3  . PHE A 1 38  ? 30.071 15.023 26.293 1.000 16.36  ? 38  PHE A HB3  1 
ATOM   680  H HD1  . PHE A 1 38  ? 29.612 12.915 23.967 1.000 15.63  ? 38  PHE A HD1  1 
ATOM   681  H HD2  . PHE A 1 38  ? 31.924 12.979 27.541 1.000 38.37  ? 38  PHE A HD2  1 
ATOM   682  H HE1  . PHE A 1 38  ? 29.329 10.477 24.195 1.000 17.28  ? 38  PHE A HE1  1 
ATOM   683  H HE2  . PHE A 1 38  ? 31.638 10.532 27.784 1.000 16.58  ? 38  PHE A HE2  1 
ATOM   684  H HZ   . PHE A 1 38  ? 30.359 9.293  26.079 1.000 16.30  ? 38  PHE A HZ   1 
ATOM   685  N N    A ASN A 1 39  ? 31.583 17.545 23.660 0.603 10.53  ? 39  ASN A N    1 
ATOM   686  N N    B ASN A 1 39  ? 31.686 17.551 23.749 0.397 10.44  ? 39  ASN A N    1 
ATOM   687  C CA   A ASN A 1 39  ? 31.714 18.998 23.741 0.603 10.61  ? 39  ASN A CA   1 
ATOM   688  C CA   B ASN A 1 39  ? 31.714 19.007 23.828 0.397 10.82  ? 39  ASN A CA   1 
ATOM   689  C C    A ASN A 1 39  ? 30.717 19.698 22.836 0.603 9.06   ? 39  ASN A C    1 
ATOM   690  C C    B ASN A 1 39  ? 30.651 19.580 22.894 0.397 9.61   ? 39  ASN A C    1 
ATOM   691  O O    A ASN A 1 39  ? 30.841 19.642 21.595 0.603 8.52   ? 39  ASN A O    1 
ATOM   692  O O    B ASN A 1 39  ? 30.674 19.272 21.694 0.397 10.43  ? 39  ASN A O    1 
ATOM   693  C CB   A ASN A 1 39  ? 33.160 19.340 23.358 0.603 12.02  ? 39  ASN A CB   1 
ATOM   694  C CB   B ASN A 1 39  ? 33.113 19.535 23.480 0.397 12.05  ? 39  ASN A CB   1 
ATOM   695  C CG   A ASN A 1 39  ? 33.410 20.831 23.339 0.603 13.91  ? 39  ASN A CG   1 
ATOM   696  C CG   B ASN A 1 39  ? 33.316 21.001 23.817 0.397 13.86  ? 39  ASN A CG   1 
ATOM   697  O OD1  A ASN A 1 39  ? 32.596 21.622 23.802 0.603 12.64  ? 39  ASN A OD1  1 
ATOM   698  O OD1  B ASN A 1 39  ? 32.345 21.763 23.844 0.397 12.93  ? 39  ASN A OD1  1 
ATOM   699  N ND2  A ASN A 1 39  ? 34.552 21.206 22.764 0.603 15.63  ? 39  ASN A ND2  1 
ATOM   700  N ND2  B ASN A 1 39  ? 34.551 21.416 24.058 0.397 15.37  ? 39  ASN A ND2  1 
ATOM   701  H H    A ASN A 1 39  ? 32.023 17.070 22.885 0.603 18.93  ? 39  ASN A H    1 
ATOM   702  H H    B ASN A 1 39  ? 32.269 17.087 23.067 0.397 6.75   ? 39  ASN A H    1 
ATOM   703  H HA   A ASN A 1 39  ? 31.537 19.315 24.780 0.603 116.52 ? 39  ASN A HA   1 
ATOM   704  H HA   B ASN A 1 39  ? 31.473 19.306 24.859 0.397 3.89   ? 39  ASN A HA   1 
ATOM   705  H HB2  A ASN A 1 39  ? 33.839 18.873 24.071 0.603 13.30  ? 39  ASN A HB2  1 
ATOM   706  H HB2  B ASN A 1 39  ? 33.855 18.945 24.017 0.397 23.86  ? 39  ASN A HB2  1 
ATOM   707  H HB3  A ASN A 1 39  ? 33.375 18.929 22.372 0.603 15.03  ? 39  ASN A HB3  1 
ATOM   708  H HB3  B ASN A 1 39  ? 33.286 19.393 22.413 0.397 9.29   ? 39  ASN A HB3  1 
ATOM   709  D DD21 A ASN A 1 39  ? 34.791 22.187 22.775 0.603 18.69  ? 39  ASN A DD21 1 
ATOM   710  D DD21 B ASN A 1 39  ? 34.758 22.396 24.054 0.397 16.59  ? 39  ASN A DD21 1 
ATOM   711  D DD22 A ASN A 1 39  ? 35.113 20.516 22.307 0.603 19.07  ? 39  ASN A DD22 1 
ATOM   712  D DD22 B ASN A 1 39  ? 35.286 20.748 24.196 0.397 17.05  ? 39  ASN A DD22 1 
ATOM   713  N N    . THR A 1 40  ? 29.722 20.392 23.395 1.000 9.55   ? 40  THR A N    1 
ATOM   714  C CA   . THR A 1 40  ? 28.693 21.007 22.569 1.000 10.09  ? 40  THR A CA   1 
ATOM   715  C C    . THR A 1 40  ? 29.198 22.155 21.703 1.000 9.40   ? 40  THR A C    1 
ATOM   716  O O    . THR A 1 40  ? 28.495 22.532 20.760 1.000 10.61  ? 40  THR A O    1 
ATOM   717  C CB   . THR A 1 40  ? 27.526 21.563 23.397 1.000 11.53  ? 40  THR A CB   1 
ATOM   718  O OG1  . THR A 1 40  ? 28.020 22.514 24.329 1.000 12.87  ? 40  THR A OG1  1 
ATOM   719  C CG2  . THR A 1 40  ? 26.841 20.462 24.207 1.000 12.48  ? 40  THR A CG2  1 
ATOM   720  H H    A THR A 1 40  ? 29.683 20.490 24.399 1.000 12.68  ? 40  THR A H    1 
ATOM   721  H HA   . THR A 1 40  ? 28.290 20.233 21.900 1.000 9.85   ? 40  THR A HA   1 
ATOM   722  H HB   . THR A 1 40  ? 26.795 22.043 22.731 1.000 14.23  ? 40  THR A HB   1 
ATOM   723  D DG1  . THR A 1 40  ? 27.685 23.419 24.096 1.000 13.94  ? 40  THR A DG1  1 
ATOM   724  H HG21 . THR A 1 40  ? 27.548 20.002 24.848 1.000 17.14  ? 40  THR A HG21 1 
ATOM   725  H HG22 . THR A 1 40  ? 26.060 20.884 24.787 1.000 15.03  ? 40  THR A HG22 1 
ATOM   726  H HG23 . THR A 1 40  ? 26.438 19.737 23.547 1.000 16.41  ? 40  THR A HG23 1 
ATOM   727  N N    A GLN A 1 41  ? 30.370 22.685 22.000 0.667 9.37   ? 41  GLN A N    1 
ATOM   728  N N    B GLN A 1 41  ? 30.378 22.664 22.007 0.333 9.59   ? 41  GLN A N    1 
ATOM   729  C CA   A GLN A 1 41  ? 30.949 23.765 21.240 0.667 10.38  ? 41  GLN A CA   1 
ATOM   730  C CA   B GLN A 1 41  ? 30.930 23.776 21.262 0.333 10.75  ? 41  GLN A CA   1 
ATOM   731  C C    A GLN A 1 41  ? 32.025 23.337 20.242 0.667 9.58   ? 41  GLN A C    1 
ATOM   732  C C    B GLN A 1 41  ? 31.852 23.333 20.129 0.333 9.85   ? 41  GLN A C    1 
ATOM   733  O O    A GLN A 1 41  ? 32.708 24.174 19.678 0.667 10.06  ? 41  GLN A O    1 
ATOM   734  O O    B GLN A 1 41  ? 32.250 24.193 19.353 0.333 8.09   ? 41  GLN A O    1 
ATOM   735  C CB   A GLN A 1 41  ? 31.589 24.787 22.179 0.667 12.92  ? 41  GLN A CB   1 
ATOM   736  C CB   B GLN A 1 41  ? 31.695 24.710 22.204 0.333 12.67  ? 41  GLN A CB   1 
ATOM   737  C CG   A GLN A 1 41  ? 30.568 25.583 22.973 0.667 15.84  ? 41  GLN A CG   1 
ATOM   738  C CG   B GLN A 1 41  ? 30.764 25.356 23.212 0.333 18.29  ? 41  GLN A CG   1 
ATOM   739  C CD   A GLN A 1 41  ? 31.295 26.495 23.949 0.667 20.92  ? 41  GLN A CD   1 
ATOM   740  C CD   B GLN A 1 41  ? 31.298 26.640 23.807 0.333 19.39  ? 41  GLN A CD   1 
ATOM   741  O OE1  A GLN A 1 41  ? 32.097 26.078 24.783 0.667 21.59  ? 41  GLN A OE1  1 
ATOM   742  O OE1  B GLN A 1 41  ? 32.379 27.109 23.452 0.333 23.45  ? 41  GLN A OE1  1 
ATOM   743  N NE2  A GLN A 1 41  ? 31.020 27.797 23.829 0.667 26.06  ? 41  GLN A NE2  1 
ATOM   744  N NE2  B GLN A 1 41  ? 30.519 27.216 24.721 0.333 24.95  ? 41  GLN A NE2  1 
ATOM   745  D D    A GLN A 1 41  ? 30.881 22.319 22.777 0.667 10.20  ? 41  GLN A D    1 
ATOM   746  D D    B GLN A 1 41  ? 30.904 22.268 22.764 0.333 10.21  ? 41  GLN A D    1 
ATOM   747  H HA   A GLN A 1 41  ? 30.143 24.266 20.684 0.667 8.54   ? 41  GLN A HA   1 
ATOM   748  H HA   B GLN A 1 41  ? 30.096 24.342 20.823 0.333 63.49  ? 41  GLN A HA   1 
ATOM   749  H HB2  A GLN A 1 41  ? 32.250 24.266 22.871 0.667 40.86  ? 41  GLN A HB2  1 
ATOM   750  H HB2  B GLN A 1 41  ? 32.462 24.142 22.732 0.333 5.13   ? 41  GLN A HB2  1 
ATOM   751  H HB3  A GLN A 1 41  ? 32.197 25.475 21.592 0.667 21.19  ? 41  GLN A HB3  1 
ATOM   752  H HB3  B GLN A 1 41  ? 32.192 25.485 21.621 0.333 12.49  ? 41  GLN A HB3  1 
ATOM   753  H HG2  A GLN A 1 41  ? 29.955 26.178 22.296 0.667 22.65  ? 41  GLN A HG2  1 
ATOM   754  H HG2  B GLN A 1 41  ? 29.811 25.566 22.724 0.333 25.80  ? 41  GLN A HG2  1 
ATOM   755  H HG3  A GLN A 1 41  ? 29.913 24.904 23.519 0.667 13.25  ? 41  GLN A HG3  1 
ATOM   756  H HG3  B GLN A 1 41  ? 30.573 24.648 24.018 0.333 19.96  ? 41  GLN A HG3  1 
ATOM   757  D DE21 A GLN A 1 41  ? 31.590 28.465 24.335 0.667 31.28  ? 41  GLN A DE21 1 
ATOM   758  D DE21 B GLN A 1 41  ? 30.819 27.247 25.686 0.333 27.44  ? 41  GLN A DE21 1 
ATOM   759  D DE22 A GLN A 1 41  ? 30.260 28.087 23.232 0.667 31.28  ? 41  GLN A DE22 1 
ATOM   760  D DE22 B GLN A 1 41  ? 29.631 27.607 24.443 0.333 28.07  ? 41  GLN A DE22 1 
ATOM   761  N N    . ALA A 1 42  ? 32.159 22.050 20.028 1.000 10.43  ? 42  ALA A N    1 
ATOM   762  C CA   . ALA A 1 42  ? 33.185 21.602 19.079 1.000 10.54  ? 42  ALA A CA   1 
ATOM   763  C C    . ALA A 1 42  ? 32.876 22.064 17.658 1.000 10.30  ? 42  ALA A C    1 
ATOM   764  O O    . ALA A 1 42  ? 31.732 21.996 17.202 1.000 10.70  ? 42  ALA A O    1 
ATOM   765  C CB   . ALA A 1 42  ? 33.266 20.081 19.081 1.000 12.07  ? 42  ALA A CB   1 
ATOM   766  H H    A ALA A 1 42  ? 31.570 21.382 20.505 1.000 13.99  ? 42  ALA A H    1 
ATOM   767  H HA   . ALA A 1 42  ? 34.158 22.013 19.385 1.000 16.67  ? 42  ALA A HA   1 
ATOM   768  H HB1  . ALA A 1 42  ? 32.331 19.676 18.787 1.000 18.87  ? 42  ALA A HB1  1 
ATOM   769  H HB2  . ALA A 1 42  ? 34.017 19.766 18.402 1.000 14.81  ? 42  ALA A HB2  1 
ATOM   770  H HB3  . ALA A 1 42  ? 33.507 19.741 20.056 1.000 14.63  ? 42  ALA A HB3  1 
ATOM   771  N N    . THR A 1 43  ? 33.903 22.542 16.961 1.000 11.05  ? 43  THR A N    1 
ATOM   772  C CA   . THR A 1 43  ? 33.880 22.934 15.570 1.000 11.90  ? 43  THR A CA   1 
ATOM   773  C C    . THR A 1 43  ? 35.128 22.414 14.853 1.000 12.41  ? 43  THR A C    1 
ATOM   774  O O    . THR A 1 43  ? 36.226 22.485 15.375 1.000 17.78  ? 43  THR A O    1 
ATOM   775  C CB   . THR A 1 43  ? 33.850 24.459 15.359 1.000 15.74  ? 43  THR A CB   1 
ATOM   776  O OG1  . THR A 1 43  ? 34.929 25.068 16.081 1.000 19.65  ? 43  THR A OG1  1 
ATOM   777  C CG2  . THR A 1 43  ? 32.553 25.053 15.854 1.000 18.69  ? 43  THR A CG2  1 
ATOM   778  D D    . THR A 1 43  ? 34.774 22.626 17.461 1.000 12.02  ? 43  THR A D    1 
ATOM   779  H HA   . THR A 1 43  ? 32.991 22.494 15.094 1.000 9.92   ? 43  THR A HA   1 
ATOM   780  H HB   . THR A 1 43  ? 33.963 24.679 14.287 1.000 167.91 ? 43  THR A HB   1 
ATOM   781  D DG1  . THR A 1 43  ? 35.722 25.203 15.523 1.000 24.81  ? 43  THR A DG1  1 
ATOM   782  H HG21 . THR A 1 43  ? 32.440 24.843 16.887 1.000 26.79  ? 43  THR A HG21 1 
ATOM   783  H HG22 . THR A 1 43  ? 32.565 26.102 15.706 1.000 21.55  ? 43  THR A HG22 1 
ATOM   784  H HG23 . THR A 1 43  ? 31.743 24.629 15.318 1.000 17.59  ? 43  THR A HG23 1 
ATOM   785  N N    . ASN A 1 44  ? 34.922 21.922 13.644 1.000 10.94  ? 44  ASN A N    1 
ATOM   786  C CA   . ASN A 1 44  ? 36.032 21.470 12.820 1.000 10.97  ? 44  ASN A CA   1 
ATOM   787  C C    . ASN A 1 44  ? 35.888 22.131 11.448 1.000 10.38  ? 44  ASN A C    1 
ATOM   788  O O    . ASN A 1 44  ? 34.931 21.879 10.716 1.000 10.44  ? 44  ASN A O    1 
ATOM   789  C CB   . ASN A 1 44  ? 36.052 19.934 12.695 1.000 14.41  ? 44  ASN A CB   1 
ATOM   790  C CG   . ASN A 1 44  ? 37.183 19.532 11.737 1.000 20.24  ? 44  ASN A CG   1 
ATOM   791  O OD1  . ASN A 1 44  ? 38.316 19.838 12.080 1.000 21.70  ? 44  ASN A OD1  1 
ATOM   792  N ND2  . ASN A 1 44  ? 36.819 18.919 10.616 1.000 25.69  ? 44  ASN A ND2  1 
ATOM   793  H H    . ASN A 1 44  ? 33.979 21.858 13.287 1.000 12.67  ? 44  ASN A H    1 
ATOM   794  H HA   . ASN A 1 44  ? 36.975 21.803 13.278 1.000 14.28  ? 44  ASN A HA   1 
ATOM   795  H HB2  . ASN A 1 44  ? 36.216 19.483 13.674 1.000 18.90  ? 44  ASN A HB2  1 
ATOM   796  H HB3  . ASN A 1 44  ? 35.095 19.579 12.311 1.000 16.84  ? 44  ASN A HB3  1 
ATOM   797  D DD21 . ASN A 1 44  ? 37.511 18.636 9.954  1.000 29.95  ? 44  ASN A DD21 1 
ATOM   798  D DD22 . ASN A 1 44  ? 35.832 18.752 10.458 1.000 27.63  ? 44  ASN A DD22 1 
ATOM   799  N N    A ARG A 1 45  ? 36.796 23.053 11.130 0.600 11.02  ? 45  ARG A N    1 
ATOM   800  N N    B ARG A 1 45  ? 36.867 22.971 11.145 0.400 11.04  ? 45  ARG A N    1 
ATOM   801  C CA   A ARG A 1 45  ? 36.709 23.845 9.902  0.600 11.67  ? 45  ARG A CA   1 
ATOM   802  C CA   B ARG A 1 45  ? 36.858 23.745 9.913  0.400 11.49  ? 45  ARG A CA   1 
ATOM   803  C C    A ARG A 1 45  ? 37.545 23.160 8.827  0.600 11.91  ? 45  ARG A C    1 
ATOM   804  C C    B ARG A 1 45  ? 37.620 23.016 8.826  0.400 11.52  ? 45  ARG A C    1 
ATOM   805  O O    A ARG A 1 45  ? 38.772 23.074 8.987  0.600 12.80  ? 45  ARG A O    1 
ATOM   806  O O    B ARG A 1 45  ? 38.828 22.782 8.954  0.400 12.73  ? 45  ARG A O    1 
ATOM   807  C CB   A ARG A 1 45  ? 37.163 25.287 10.186 0.600 13.49  ? 45  ARG A CB   1 
ATOM   808  C CB   B ARG A 1 45  ? 37.486 25.114 10.196 0.400 13.22  ? 45  ARG A CB   1 
ATOM   809  C CG   A ARG A 1 45  ? 36.435 25.975 11.316 0.600 16.26  ? 45  ARG A CG   1 
ATOM   810  C CG   B ARG A 1 45  ? 36.540 25.933 11.060 0.400 15.74  ? 45  ARG A CG   1 
ATOM   811  C CD   A ARG A 1 45  ? 35.960 27.389 11.098 0.600 20.47  ? 45  ARG A CD   1 
ATOM   812  C CD   B ARG A 1 45  ? 37.138 27.269 11.439 0.400 17.57  ? 45  ARG A CD   1 
ATOM   813  N NE   A ARG A 1 45  ? 35.122 27.931 12.171 0.600 21.24  ? 45  ARG A NE   1 
ATOM   814  N NE   B ARG A 1 45  ? 36.249 27.996 12.345 0.400 20.59  ? 45  ARG A NE   1 
ATOM   815  C CZ   A ARG A 1 45  ? 33.855 28.339 12.070 0.600 22.40  ? 45  ARG A CZ   1 
ATOM   816  C CZ   B ARG A 1 45  ? 36.433 28.057 13.656 0.400 20.97  ? 45  ARG A CZ   1 
ATOM   817  N NH1  A ARG A 1 45  ? 33.245 28.364 10.900 0.600 26.75  ? 45  ARG A NH1  1 
ATOM   818  N NH1  B ARG A 1 45  ? 37.606 27.690 14.159 0.400 20.72  ? 45  ARG A NH1  1 
ATOM   819  N NH2  A ARG A 1 45  ? 33.207 28.672 13.176 0.600 22.26  ? 45  ARG A NH2  1 
ATOM   820  N NH2  B ARG A 1 45  ? 35.478 28.483 14.471 0.400 20.34  ? 45  ARG A NH2  1 
ATOM   821  D D    A ARG A 1 45  ? 37.566 23.234 11.750 0.600 12.78  ? 45  ARG A D    1 
ATOM   822  D D    B ARG A 1 45  ? 37.642 23.078 11.784 0.400 12.53  ? 45  ARG A D    1 
ATOM   823  H HA   A ARG A 1 45  ? 35.660 23.866 9.571  0.600 9.97   ? 45  ARG A HA   1 
ATOM   824  H HA   B ARG A 1 45  ? 35.817 23.888 9.588  0.400 12.14  ? 45  ARG A HA   1 
ATOM   825  H HB2  A ARG A 1 45  ? 38.228 25.275 10.418 0.600 11.71  ? 45  ARG A HB2  1 
ATOM   826  H HB2  B ARG A 1 45  ? 38.437 24.985 10.712 0.400 21.35  ? 45  ARG A HB2  1 
ATOM   827  H HB3  A ARG A 1 45  ? 37.031 25.876 9.279  0.600 16.20  ? 45  ARG A HB3  1 
ATOM   828  H HB3  B ARG A 1 45  ? 37.674 25.636 9.258  0.400 12.14  ? 45  ARG A HB3  1 
ATOM   829  H HG2  A ARG A 1 45  ? 35.566 25.368 11.570 0.600 21.31  ? 45  ARG A HG2  1 
ATOM   830  H HG2  B ARG A 1 45  ? 35.609 26.097 10.518 0.400 16.25  ? 45  ARG A HG2  1 
ATOM   831  H HG3  A ARG A 1 45  ? 37.093 25.975 12.185 0.600 63.36  ? 45  ARG A HG3  1 
ATOM   832  H HG3  B ARG A 1 45  ? 36.306 25.374 11.966 0.400 14.66  ? 45  ARG A HG3  1 
ATOM   833  H HD2  A ARG A 1 45  ? 36.832 28.033 10.980 0.600 17.36  ? 45  ARG A HD2  1 
ATOM   834  H HD2  B ARG A 1 45  ? 38.102 27.112 11.923 0.400 20.10  ? 45  ARG A HD2  1 
ATOM   835  H HD3  A ARG A 1 45  ? 35.396 27.426 10.166 0.600 47.30  ? 45  ARG A HD3  1 
ATOM   836  H HD3  B ARG A 1 45  ? 37.304 27.862 10.539 0.400 23.53  ? 45  ARG A HD3  1 
ATOM   837  D DE   A ARG A 1 45  ? 35.626 27.957 13.057 0.600 19.40  ? 45  ARG A DE   1 
ATOM   838  D DE   B ARG A 1 45  ? 35.494 28.449 11.854 0.400 21.22  ? 45  ARG A DE   1 
ATOM   839  D DH11 A ARG A 1 45  ? 33.594 27.822 10.124 0.600 29.81  ? 45  ARG A DH11 1 
ATOM   840  D DH11 B ARG A 1 45  ? 37.849 27.981 15.102 0.400 20.89  ? 45  ARG A DH11 1 
ATOM   841  D DH12 A ARG A 1 45  ? 32.404 28.914 10.780 0.600 32.60  ? 45  ARG A DH12 1 
ATOM   842  D DH12 B ARG A 1 45  ? 38.259 27.181 13.595 0.400 21.02  ? 45  ARG A DH12 1 
ATOM   843  D DH21 A ARG A 1 45  ? 33.721 28.790 14.040 0.600 22.21  ? 45  ARG A DH21 1 
ATOM   844  D DH21 B ARG A 1 45  ? 35.664 28.600 15.453 0.400 21.82  ? 45  ARG A DH21 1 
ATOM   845  D DH22 A ARG A 1 45  ? 32.203 28.746 13.183 0.600 22.60  ? 45  ARG A DH22 1 
ATOM   846  D DH22 B ARG A 1 45  ? 34.551 28.661 14.103 0.400 21.20  ? 45  ARG A DH22 1 
ATOM   847  N N    . ASN A 1 46  ? 36.888 22.665 7.778  1.000 11.50  ? 46  ASN A N    1 
ATOM   848  C CA   . ASN A 1 46  ? 37.509 21.827 6.751  1.000 12.34  ? 46  ASN A CA   1 
ATOM   849  C C    . ASN A 1 46  ? 38.053 22.664 5.597  1.000 12.36  ? 46  ASN A C    1 
ATOM   850  O O    . ASN A 1 46  ? 37.635 23.787 5.371  1.000 14.06  ? 46  ASN A O    1 
ATOM   851  C CB   . ASN A 1 46  ? 36.467 20.856 6.182  1.000 13.33  ? 46  ASN A CB   1 
ATOM   852  C CG   . ASN A 1 46  ? 35.939 19.933 7.259  1.000 15.48  ? 46  ASN A CG   1 
ATOM   853  O OD1  . ASN A 1 46  ? 36.755 19.252 7.865  1.000 17.43  ? 46  ASN A OD1  1 
ATOM   854  N ND2  . ASN A 1 46  ? 34.638 19.981 7.464  1.000 16.19  ? 46  ASN A ND2  1 
ATOM   855  D D    . ASN A 1 46  ? 35.915 22.867 7.708  1.000 16.64  ? 46  ASN A D    1 
ATOM   856  H HA   . ASN A 1 46  ? 38.332 21.253 7.201  1.000 15.84  ? 46  ASN A HA   1 
ATOM   857  H HB2  . ASN A 1 46  ? 35.641 21.423 5.752  1.000 12.94  ? 46  ASN A HB2  1 
ATOM   858  H HB3  . ASN A 1 46  ? 36.920 20.264 5.387  1.000 18.75  ? 46  ASN A HB3  1 
ATOM   859  D DD21 . ASN A 1 46  ? 34.241 19.396 8.205  1.000 17.41  ? 46  ASN A DD21 1 
ATOM   860  D DD22 . ASN A 1 46  ? 34.082 20.604 6.872  1.000 16.61  ? 46  ASN A DD22 1 
ATOM   861  N N    . THR A 1 47  ? 38.974 22.123 4.796  1.000 14.15  ? 47  THR A N    1 
ATOM   862  C CA   . THR A 1 47  ? 39.547 22.865 3.704  1.000 13.55  ? 47  THR A CA   1 
ATOM   863  C C    . THR A 1 47  ? 38.640 22.968 2.484  1.000 13.69  ? 47  THR A C    1 
ATOM   864  O O    . THR A 1 47  ? 38.956 23.752 1.590  1.000 17.15  ? 47  THR A O    1 
ATOM   865  C CB   . THR A 1 47  ? 40.870 22.226 3.256  1.000 13.45  ? 47  THR A CB   1 
ATOM   866  O OG1  . THR A 1 47  ? 40.601 20.894 2.789  1.000 14.21  ? 47  THR A OG1  1 
ATOM   867  C CG2  . THR A 1 47  ? 41.861 22.159 4.412  1.000 14.42  ? 47  THR A CG2  1 
ATOM   868  D D    . THR A 1 47  ? 39.218 21.181 5.048  1.000 14.57  ? 47  THR A D    1 
ATOM   869  H HA   . THR A 1 47  ? 39.762 23.884 4.058  1.000 13.79  ? 47  THR A HA   1 
ATOM   870  H HB   . THR A 1 47  ? 41.304 22.820 2.438  1.000 14.51  ? 47  THR A HB   1 
ATOM   871  D DG1  . THR A 1 47  ? 41.173 20.292 3.322  1.000 16.36  ? 47  THR A DG1  1 
ATOM   872  H HG21 . THR A 1 47  ? 41.444 21.587 5.202  1.000 21.70  ? 47  THR A HG21 1 
ATOM   873  H HG22 . THR A 1 47  ? 42.759 21.703 4.082  1.000 20.35  ? 47  THR A HG22 1 
ATOM   874  H HG23 . THR A 1 47  ? 42.068 23.139 4.758  1.000 22.03  ? 47  THR A HG23 1 
ATOM   875  N N    . ASP A 1 48  ? 37.545 22.213 2.448  1.000 14.01  ? 48  ASP A N    1 
ATOM   876  C CA   . ASP A 1 48  ? 36.572 22.291 1.374  1.000 14.67  ? 48  ASP A CA   1 
ATOM   877  C C    . ASP A 1 48  ? 35.535 23.392 1.580  1.000 14.83  ? 48  ASP A C    1 
ATOM   878  O O    . ASP A 1 48  ? 34.575 23.460 0.791  1.000 18.66  ? 48  ASP A O    1 
ATOM   879  C CB   . ASP A 1 48  ? 35.879 20.921 1.226  1.000 16.16  ? 48  ASP A CB   1 
ATOM   880  C CG   . ASP A 1 48  ? 34.959 20.549 2.375  1.000 16.38  ? 48  ASP A CG   1 
ATOM   881  O OD1  . ASP A 1 48  ? 34.814 21.286 3.371  1.000 14.35  ? 48  ASP A OD1  1 
ATOM   882  O OD2  . ASP A 1 48  ? 34.339 19.467 2.259  1.000 21.66  ? 48  ASP A OD2  1 
ATOM   883  D D    . ASP A 1 48  ? 37.423 21.571 3.198  1.000 15.09  ? 48  ASP A D    1 
ATOM   884  H HA   . ASP A 1 48  ? 37.112 22.502 0.439  1.000 19.32  ? 48  ASP A HA   1 
ATOM   885  H HB2  . ASP A 1 48  ? 35.299 20.923 0.303  1.000 19.87  ? 48  ASP A HB2  1 
ATOM   886  H HB3  . ASP A 1 48  ? 36.645 20.152 1.132  1.000 21.05  ? 48  ASP A HB3  1 
ATOM   887  N N    . GLY A 1 49  ? 35.704 24.252 2.576  1.000 14.34  ? 49  GLY A N    1 
ATOM   888  C CA   . GLY A 1 49  ? 34.801 25.362 2.828  1.000 16.26  ? 49  GLY A CA   1 
ATOM   889  C C    . GLY A 1 49  ? 33.680 25.038 3.768  1.000 13.15  ? 49  GLY A C    1 
ATOM   890  O O    . GLY A 1 49  ? 32.920 25.946 4.104  1.000 14.06  ? 49  GLY A O    1 
ATOM   891  D D    . GLY A 1 49  ? 36.456 24.136 3.241  1.000 16.07  ? 49  GLY A D    1 
ATOM   892  H HA2  . GLY A 1 49  ? 35.374 26.192 3.239  1.000 16.30  ? 49  GLY A HA2  1 
ATOM   893  H HA3  . GLY A 1 49  ? 34.378 25.691 1.879  1.000 17.64  ? 49  GLY A HA3  1 
ATOM   894  N N    . SER A 1 50  ? 33.554 23.771 4.120  1.000 11.13  ? 50  SER A N    1 
ATOM   895  C CA   . SER A 1 50  ? 32.521 23.376 5.084  1.000 10.17  ? 50  SER A CA   1 
ATOM   896  C C    . SER A 1 50  ? 33.080 23.271 6.503  1.000 10.36  ? 50  SER A C    1 
ATOM   897  O O    . SER A 1 50  ? 34.303 23.270 6.728  1.000 11.66  ? 50  SER A O    1 
ATOM   898  C CB   . SER A 1 50  ? 31.919 22.030 4.692  1.000 10.22  ? 50  SER A CB   1 
ATOM   899  O OG   . SER A 1 50  ? 32.778 20.943 4.994  1.000 10.64  ? 50  SER A OG   1 
ATOM   900  H H    A SER A 1 50  ? 34.169 23.074 3.724  0.609 43.32  ? 50  SER A H    1 
ATOM   901  D D    B SER A 1 50  ? 34.250 23.099 3.862  0.391 10.51  ? 50  SER A D    1 
ATOM   902  H HA   . SER A 1 50  ? 31.724 24.134 5.075  1.000 12.18  ? 50  SER A HA   1 
ATOM   903  H HB2  . SER A 1 50  ? 30.974 21.895 5.218  1.000 11.83  ? 50  SER A HB2  1 
ATOM   904  H HB3  . SER A 1 50  ? 31.709 22.032 3.623  1.000 13.58  ? 50  SER A HB3  1 
ATOM   905  D DG   . SER A 1 50  ? 33.497 20.960 4.315  1.000 12.88  ? 50  SER A DG   1 
ATOM   906  N N    . THR A 1 51  ? 32.172 23.227 7.454  1.000 9.33   ? 51  THR A N    1 
ATOM   907  C CA   . THR A 1 51  ? 32.505 23.164 8.877  1.000 8.12   ? 51  THR A CA   1 
ATOM   908  C C    . THR A 1 51  ? 31.581 22.130 9.526  1.000 8.31   ? 51  THR A C    1 
ATOM   909  O O    . THR A 1 51  ? 30.426 22.086 9.157  1.000 9.32   ? 51  THR A O    1 
ATOM   910  C CB   . THR A 1 51  ? 32.354 24.526 9.551  1.000 9.23   ? 51  THR A CB   1 
ATOM   911  O OG1  . THR A 1 51  ? 33.297 25.415 8.943  1.000 11.32  ? 51  THR A OG1  1 
ATOM   912  C CG2  . THR A 1 51  ? 32.648 24.513 11.046 1.000 10.43  ? 51  THR A CG2  1 
ATOM   913  H H    A THR A 1 51  ? 31.198 23.237 7.189  0.772 31.05  ? 51  THR A H    1 
ATOM   914  D D    B THR A 1 51  ? 31.211 23.244 7.155  0.228 8.16   ? 51  THR A D    1 
ATOM   915  H HA   . THR A 1 51  ? 33.546 22.827 8.984  1.000 9.49   ? 51  THR A HA   1 
ATOM   916  H HB   . THR A 1 51  ? 31.335 24.905 9.384  1.000 10.65  ? 51  THR A HB   1 
ATOM   917  D DG1  . THR A 1 51  ? 32.864 25.831 8.154  1.000 12.03  ? 51  THR A DG1  1 
ATOM   918  H HG21 . THR A 1 51  ? 33.630 24.148 11.210 1.000 17.30  ? 51  THR A HG21 1 
ATOM   919  H HG22 . THR A 1 51  ? 32.568 25.498 11.430 1.000 13.76  ? 51  THR A HG22 1 
ATOM   920  H HG23 . THR A 1 51  ? 31.951 23.884 11.537 1.000 12.95  ? 51  THR A HG23 1 
ATOM   921  N N    . ASP A 1 52  ? 32.129 21.358 10.449 1.000 8.49   ? 52  ASP A N    1 
ATOM   922  C CA   . ASP A 1 52  ? 31.363 20.397 11.240 1.000 7.98   ? 52  ASP A CA   1 
ATOM   923  C C    . ASP A 1 52  ? 31.082 21.021 12.609 1.000 7.92   ? 52  ASP A C    1 
ATOM   924  O O    . ASP A 1 52  ? 31.991 21.535 13.265 1.000 10.08  ? 52  ASP A O    1 
ATOM   925  C CB   . ASP A 1 52  ? 32.163 19.127 11.429 1.000 9.89   ? 52  ASP A CB   1 
ATOM   926  C CG   . ASP A 1 52  ? 32.678 18.519 10.149 1.000 12.72  ? 52  ASP A CG   1 
ATOM   927  O OD1  . ASP A 1 52  ? 31.923 18.433 9.158  1.000 15.46  ? 52  ASP A OD1  1 
ATOM   928  O OD2  . ASP A 1 52  ? 33.862 18.108 10.147 1.000 17.49  ? 52  ASP A OD2  1 
ATOM   929  H H    . ASP A 1 52  ? 33.122 21.435 10.614 1.000 13.06  ? 52  ASP A H    1 
ATOM   930  H HA   . ASP A 1 52  ? 30.414 20.168 10.733 1.000 9.78   ? 52  ASP A HA   1 
ATOM   931  H HB2  . ASP A 1 52  ? 33.011 19.344 12.079 1.000 12.91  ? 52  ASP A HB2  1 
ATOM   932  H HB3  . ASP A 1 52  ? 31.538 18.393 11.937 1.000 12.33  ? 52  ASP A HB3  1 
ATOM   933  N N    . TYR A 1 53  ? 29.817 21.000 13.024 1.000 7.64   ? 53  TYR A N    1 
ATOM   934  C CA   . TYR A 1 53  ? 29.378 21.714 14.196 1.000 8.26   ? 53  TYR A CA   1 
ATOM   935  C C    . TYR A 1 53  ? 28.761 20.822 15.292 1.000 8.15   ? 53  TYR A C    1 
ATOM   936  O O    . TYR A 1 53  ? 27.864 20.037 15.033 1.000 8.49   ? 53  TYR A O    1 
ATOM   937  C CB   . TYR A 1 53  ? 28.279 22.704 13.784 1.000 9.83   ? 53  TYR A CB   1 
ATOM   938  C CG   . TYR A 1 53  ? 28.723 23.874 12.934 1.000 9.13   ? 53  TYR A CG   1 
ATOM   939  C CD1  . TYR A 1 53  ? 29.159 25.047 13.519 1.000 10.63  ? 53  TYR A CD1  1 
ATOM   940  C CD2  . TYR A 1 53  ? 28.704 23.807 11.526 1.000 8.18   ? 53  TYR A CD2  1 
ATOM   941  C CE1  . TYR A 1 53  ? 29.581 26.151 12.784 1.000 10.41  ? 53  TYR A CE1  1 
ATOM   942  C CE2  . TYR A 1 53  ? 29.123 24.900 10.802 1.000 8.76   ? 53  TYR A CE2  1 
ATOM   943  C CZ   . TYR A 1 53  ? 29.546 26.057 11.392 1.000 9.46   ? 53  TYR A CZ   1 
ATOM   944  O OH   . TYR A 1 53  ? 29.955 27.137 10.656 1.000 11.03  ? 53  TYR A OH   1 
ATOM   945  H H    . TYR A 1 53  ? 29.141 20.464 12.499 1.000 11.32  ? 53  TYR A H    1 
ATOM   946  H HA   . TYR A 1 53  ? 30.227 22.272 14.618 1.000 10.79  ? 53  TYR A HA   1 
ATOM   947  H HB2  . TYR A 1 53  ? 27.513 22.155 13.236 1.000 13.15  ? 53  TYR A HB2  1 
ATOM   948  H HB3  . TYR A 1 53  ? 27.815 23.096 14.689 1.000 12.76  ? 53  TYR A HB3  1 
ATOM   949  H HD1  . TYR A 1 53  ? 29.172 25.110 14.597 1.000 14.50  ? 53  TYR A HD1  1 
ATOM   950  H HD2  . TYR A 1 53  ? 28.367 22.912 11.023 1.000 13.58  ? 53  TYR A HD2  1 
ATOM   951  H HE1  . TYR A 1 53  ? 29.924 27.050 13.275 1.000 15.82  ? 53  TYR A HE1  1 
ATOM   952  H HE2  . TYR A 1 53  ? 29.117 24.841 9.724  1.000 11.65  ? 53  TYR A HE2  1 
ATOM   953  D DH   . TYR A 1 53  ? 29.757 27.004 9.692  1.000 11.94  ? 53  TYR A DH   1 
ATOM   954  N N    . GLY A 1 54  ? 29.215 21.086 16.514 1.000 8.67   ? 54  GLY A N    1 
ATOM   955  C CA   . GLY A 1 54  ? 28.546 20.622 17.716 1.000 9.45   ? 54  GLY A CA   1 
ATOM   956  C C    . GLY A 1 54  ? 28.857 19.197 18.119 1.000 9.34   ? 54  GLY A C    1 
ATOM   957  O O    . GLY A 1 54  ? 29.765 18.566 17.607 1.000 9.09   ? 54  GLY A O    1 
ATOM   958  H H    . GLY A 1 54  ? 30.060 21.630 16.610 1.000 9.74   ? 54  GLY A H    1 
ATOM   959  H HA2  . GLY A 1 54  ? 28.819 21.282 18.540 1.000 14.44  ? 54  GLY A HA2  1 
ATOM   960  H HA3  . GLY A 1 54  ? 27.469 20.712 17.568 1.000 8.75   ? 54  GLY A HA3  1 
ATOM   961  N N    . ILE A 1 55  ? 28.075 18.703 19.088 1.000 8.87   ? 55  ILE A N    1 
ATOM   962  C CA   . ILE A 1 55  ? 28.329 17.428 19.737 1.000 9.00   ? 55  ILE A CA   1 
ATOM   963  C C    . ILE A 1 55  ? 28.309 16.257 18.765 1.000 9.51   ? 55  ILE A C    1 
ATOM   964  O O    . ILE A 1 55  ? 28.960 15.228 18.996 1.000 10.49  ? 55  ILE A O    1 
ATOM   965  C CB   . ILE A 1 55  ? 27.318 17.326 20.904 1.000 10.77  ? 55  ILE A CB   1 
ATOM   966  C CG1  . ILE A 1 55  ? 27.823 16.282 21.907 1.000 13.62  ? 55  ILE A CG1  1 
ATOM   967  C CG2  . ILE A 1 55  ? 25.890 17.107 20.459 1.000 11.74  ? 55  ILE A CG2  1 
ATOM   968  C CD1  . ILE A 1 55  ? 27.209 16.314 23.267 1.000 15.66  ? 55  ILE A CD1  1 
ATOM   969  D D    A ILE A 1 55  ? 27.330 19.315 19.406 0.536 7.96   ? 55  ILE A D    1 
ATOM   970  H H    B ILE A 1 55  ? 27.168 19.141 19.198 0.464 57.48  ? 55  ILE A H    1 
ATOM   971  H HA   . ILE A 1 55  ? 29.337 17.476 20.177 1.000 10.59  ? 55  ILE A HA   1 
ATOM   972  H HB   . ILE A 1 55  ? 27.340 18.296 21.423 1.000 12.20  ? 55  ILE A HB   1 
ATOM   973  H HG12 . ILE A 1 55  ? 27.655 15.293 21.482 1.000 21.82  ? 55  ILE A HG12 1 
ATOM   974  H HG13 . ILE A 1 55  ? 28.900 16.410 22.017 1.000 13.63  ? 55  ILE A HG13 1 
ATOM   975  H HG21 . ILE A 1 55  ? 25.816 16.180 19.950 1.000 20.75  ? 55  ILE A HG21 1 
ATOM   976  H HG22 . ILE A 1 55  ? 25.253 17.097 21.306 1.000 25.97  ? 55  ILE A HG22 1 
ATOM   977  H HG23 . ILE A 1 55  ? 25.598 17.891 19.808 1.000 17.96  ? 55  ILE A HG23 1 
ATOM   978  H HD11 . ILE A 1 55  ? 27.361 17.270 23.701 1.000 28.62  ? 55  ILE A HD11 1 
ATOM   979  H HD12 . ILE A 1 55  ? 26.170 16.122 23.191 1.000 20.48  ? 55  ILE A HD12 1 
ATOM   980  H HD13 . ILE A 1 55  ? 27.662 15.574 23.877 1.000 19.27  ? 55  ILE A HD13 1 
ATOM   981  N N    A LEU A 1 56  ? 27.553 16.394 17.666 0.616 9.23   ? 56  LEU A N    1 
ATOM   982  N N    B LEU A 1 56  ? 27.593 16.358 17.644 0.384 9.18   ? 56  LEU A N    1 
ATOM   983  C CA   A LEU A 1 56  ? 27.492 15.344 16.651 0.616 9.42   ? 56  LEU A CA   1 
ATOM   984  C CA   B LEU A 1 56  ? 27.629 15.278 16.663 0.384 9.49   ? 56  LEU A CA   1 
ATOM   985  C C    A LEU A 1 56  ? 28.138 15.758 15.336 0.616 9.06   ? 56  LEU A C    1 
ATOM   986  C C    B LEU A 1 56  ? 28.322 15.663 15.368 0.384 8.99   ? 56  LEU A C    1 
ATOM   987  O O    A LEU A 1 56  ? 27.939 15.063 14.344 0.616 9.11   ? 56  LEU A O    1 
ATOM   988  O O    B LEU A 1 56  ? 28.336 14.911 14.396 0.384 7.81   ? 56  LEU A O    1 
ATOM   989  C CB   A LEU A 1 56  ? 26.027 14.861 16.461 0.616 10.60  ? 56  LEU A CB   1 
ATOM   990  C CB   B LEU A 1 56  ? 26.211 14.807 16.331 0.384 10.75  ? 56  LEU A CB   1 
ATOM   991  C CG   A LEU A 1 56  ? 25.629 13.826 17.516 0.616 11.33  ? 56  LEU A CG   1 
ATOM   992  C CG   B LEU A 1 56  ? 25.408 14.217 17.491 0.384 11.39  ? 56  LEU A CG   1 
ATOM   993  C CD1  A LEU A 1 56  ? 24.116 13.605 17.518 0.616 12.12  ? 56  LEU A CD1  1 
ATOM   994  C CD1  B LEU A 1 56  ? 23.967 14.001 17.064 0.384 12.14  ? 56  LEU A CD1  1 
ATOM   995  C CD2  A LEU A 1 56  ? 26.294 12.455 17.372 0.616 12.68  ? 56  LEU A CD2  1 
ATOM   996  C CD2  B LEU A 1 56  ? 26.068 12.936 17.982 0.384 12.65  ? 56  LEU A CD2  1 
ATOM   997  H H    A LEU A 1 56  ? 27.016 17.239 17.536 0.616 167.91 ? 56  LEU A H    1 
ATOM   998  H H    B LEU A 1 56  ? 27.029 17.179 17.475 0.384 167.91 ? 56  LEU A H    1 
ATOM   999  H HA   A LEU A 1 56  ? 28.066 14.488 17.037 0.616 11.75  ? 56  LEU A HA   1 
ATOM   1000 H HA   B LEU A 1 56  ? 28.176 14.432 17.106 0.384 7.65   ? 56  LEU A HA   1 
ATOM   1001 H HB2  A LEU A 1 56  ? 25.355 15.717 16.526 0.616 7.14   ? 56  LEU A HB2  1 
ATOM   1002 H HB2  B LEU A 1 56  ? 25.656 15.654 15.927 0.384 7.95   ? 56  LEU A HB2  1 
ATOM   1003 H HB3  A LEU A 1 56  ? 25.919 14.424 15.469 0.616 19.28  ? 56  LEU A HB3  1 
ATOM   1004 H HB3  B LEU A 1 56  ? 26.276 14.055 15.544 0.384 5.01   ? 56  LEU A HB3  1 
ATOM   1005 H HG   A LEU A 1 56  ? 25.907 14.229 18.501 0.616 12.94  ? 56  LEU A HG   1 
ATOM   1006 H HG   B LEU A 1 56  ? 25.416 14.944 18.317 0.384 17.10  ? 56  LEU A HG   1 
ATOM   1007 H HD11 A LEU A 1 56  ? 23.815 13.215 16.579 0.616 81.50  ? 56  LEU A HD11 1 
ATOM   1008 H HD11 B LEU A 1 56  ? 23.936 13.303 16.267 0.384 76.92  ? 56  LEU A HD11 1 
ATOM   1009 H HD12 A LEU A 1 56  ? 23.860 12.919 18.284 0.616 12.32  ? 56  LEU A HD12 1 
ATOM   1010 H HD12 B LEU A 1 56  ? 23.408 13.628 17.883 0.384 12.04  ? 56  LEU A HD12 1 
ATOM   1011 H HD13 A LEU A 1 56  ? 23.625 14.528 17.691 0.616 39.01  ? 56  LEU A HD13 1 
ATOM   1012 H HD13 B LEU A 1 56  ? 23.553 14.923 16.743 0.384 12.37  ? 56  LEU A HD13 1 
ATOM   1013 H HD21 A LEU A 1 56  ? 26.044 12.039 16.429 0.616 17.50  ? 56  LEU A HD21 1 
ATOM   1014 H HD21 B LEU A 1 56  ? 26.072 12.219 17.201 0.384 25.49  ? 56  LEU A HD21 1 
ATOM   1015 H HD22 A LEU A 1 56  ? 27.346 12.564 17.442 0.616 12.12  ? 56  LEU A HD22 1 
ATOM   1016 H HD22 B LEU A 1 56  ? 27.065 13.142 18.277 0.384 9.59   ? 56  LEU A HD22 1 
ATOM   1017 H HD23 A LEU A 1 56  ? 25.952 11.814 18.143 0.616 19.52  ? 56  LEU A HD23 1 
ATOM   1018 H HD23 B LEU A 1 56  ? 25.526 12.554 18.809 0.384 14.09  ? 56  LEU A HD23 1 
ATOM   1019 N N    . GLN A 1 57  ? 28.927 16.842 15.344 1.000 8.40   ? 57  GLN A N    1 
ATOM   1020 C CA   . GLN A 1 57  ? 29.775 17.233 14.209 1.000 8.50   ? 57  GLN A CA   1 
ATOM   1021 C C    . GLN A 1 57  ? 29.037 17.155 12.878 1.000 8.78   ? 57  GLN A C    1 
ATOM   1022 O O    . GLN A 1 57  ? 29.475 16.509 11.931 1.000 12.32  ? 57  GLN A O    1 
ATOM   1023 C CB   . GLN A 1 57  ? 31.089 16.431 14.190 1.000 9.04   ? 57  GLN A CB   1 
ATOM   1024 C CG   . GLN A 1 57  ? 32.007 16.774 15.382 1.000 9.28   ? 57  GLN A CG   1 
ATOM   1025 C CD   . GLN A 1 57  ? 32.644 18.128 15.171 1.000 10.02  ? 57  GLN A CD   1 
ATOM   1026 O OE1  . GLN A 1 57  ? 33.657 18.278 14.487 1.000 13.10  ? 57  GLN A OE1  1 
ATOM   1027 N NE2  . GLN A 1 57  ? 32.031 19.160 15.783 1.000 10.85  ? 57  GLN A NE2  1 
ATOM   1028 H H    A GLN A 1 57  ? 28.941 17.418 16.173 0.876 7.54   ? 57  GLN A H    1 
ATOM   1029 D D    B GLN A 1 57  ? 28.756 17.522 16.064 0.124 6.09   ? 57  GLN A D    1 
ATOM   1030 H HA   . GLN A 1 57  ? 30.046 18.288 14.362 1.000 9.96   ? 57  GLN A HA   1 
ATOM   1031 H HB2  . GLN A 1 57  ? 30.857 15.366 14.214 1.000 10.56  ? 57  GLN A HB2  1 
ATOM   1032 H HB3  . GLN A 1 57  ? 31.619 16.637 13.261 1.000 8.76   ? 57  GLN A HB3  1 
ATOM   1033 H HG2  . GLN A 1 57  ? 31.425 16.782 16.303 1.000 11.87  ? 57  GLN A HG2  1 
ATOM   1034 H HG3  . GLN A 1 57  ? 32.783 16.015 15.477 1.000 11.35  ? 57  GLN A HG3  1 
ATOM   1035 D DE21 . GLN A 1 57  ? 32.370 20.090 15.589 1.000 12.31  ? 57  GLN A DE21 1 
ATOM   1036 D DE22 . GLN A 1 57  ? 31.313 19.001 16.433 1.000 12.52  ? 57  GLN A DE22 1 
ATOM   1037 N N    . ILE A 1 58  ? 27.918 17.863 12.844 1.000 9.03   ? 58  ILE A N    1 
ATOM   1038 C CA   . ILE A 1 58  ? 27.064 17.899 11.664 1.000 8.68   ? 58  ILE A CA   1 
ATOM   1039 C C    . ILE A 1 58  ? 27.592 18.936 10.669 1.000 9.19   ? 58  ILE A C    1 
ATOM   1040 O O    . ILE A 1 58  ? 27.921 20.067 11.010 1.000 9.51   ? 58  ILE A O    1 
ATOM   1041 C CB   . ILE A 1 58  ? 25.623 18.173 12.121 1.000 9.79   ? 58  ILE A CB   1 
ATOM   1042 C CG1  . ILE A 1 58  ? 25.079 16.960 12.896 1.000 11.67  ? 58  ILE A CG1  1 
ATOM   1043 C CG2  . ILE A 1 58  ? 24.736 18.578 10.950 1.000 10.59  ? 58  ILE A CG2  1 
ATOM   1044 C CD1  . ILE A 1 58  ? 23.739 17.153 13.552 1.000 13.61  ? 58  ILE A CD1  1 
ATOM   1045 H H    . ILE A 1 58  ? 27.649 18.393 13.661 1.000 9.14   ? 58  ILE A H    1 
ATOM   1046 H HA   . ILE A 1 58  ? 27.094 16.910 11.183 1.000 9.97   ? 58  ILE A HA   1 
ATOM   1047 H HB   . ILE A 1 58  ? 25.655 19.023 12.819 1.000 11.86  ? 58  ILE A HB   1 
ATOM   1048 H HG12 . ILE A 1 58  ? 25.007 16.118 12.208 1.000 13.78  ? 58  ILE A HG12 1 
ATOM   1049 H HG13 . ILE A 1 58  ? 25.803 16.692 13.665 1.000 12.09  ? 58  ILE A HG13 1 
ATOM   1050 H HG21 . ILE A 1 58  ? 24.683 17.779 10.255 1.000 15.76  ? 58  ILE A HG21 1 
ATOM   1051 H HG22 . ILE A 1 58  ? 23.763 18.803 11.305 1.000 15.73  ? 58  ILE A HG22 1 
ATOM   1052 H HG23 . ILE A 1 58  ? 25.145 19.433 10.475 1.000 14.16  ? 58  ILE A HG23 1 
ATOM   1053 H HD11 . ILE A 1 58  ? 23.020 17.415 12.818 1.000 17.31  ? 58  ILE A HD11 1 
ATOM   1054 H HD12 . ILE A 1 58  ? 23.445 16.253 14.028 1.000 19.33  ? 58  ILE A HD12 1 
ATOM   1055 H HD13 . ILE A 1 58  ? 23.806 17.928 14.273 1.000 18.63  ? 58  ILE A HD13 1 
ATOM   1056 N N    . ASN A 1 59  ? 27.710 18.503 9.413  1.000 9.31   ? 59  ASN A N    1 
ATOM   1057 C CA   . ASN A 1 59  ? 28.376 19.284 8.391  1.000 9.46   ? 59  ASN A CA   1 
ATOM   1058 C C    . ASN A 1 59  ? 27.489 20.312 7.668  1.000 9.39   ? 59  ASN A C    1 
ATOM   1059 O O    . ASN A 1 59  ? 26.319 20.107 7.358  1.000 10.84  ? 59  ASN A O    1 
ATOM   1060 C CB   . ASN A 1 59  ? 28.991 18.279 7.375  1.000 10.62  ? 59  ASN A CB   1 
ATOM   1061 C CG   . ASN A 1 59  ? 29.843 18.968 6.306  1.000 11.15  ? 59  ASN A CG   1 
ATOM   1062 O OD1  . ASN A 1 59  ? 29.379 19.255 5.209  1.000 11.04  ? 59  ASN A OD1  1 
ATOM   1063 N ND2  . ASN A 1 59  ? 31.084 19.242 6.650  1.000 13.04  ? 59  ASN A ND2  1 
ATOM   1064 D D    . ASN A 1 59  ? 27.409 17.565 9.204  1.000 12.91  ? 59  ASN A D    1 
ATOM   1065 H HA   . ASN A 1 59  ? 29.203 19.829 8.869  1.000 11.17  ? 59  ASN A HA   1 
ATOM   1066 H HB2  . ASN A 1 59  ? 29.609 17.560 7.914  1.000 12.99  ? 59  ASN A HB2  1 
ATOM   1067 H HB3  . ASN A 1 59  ? 28.186 17.727 6.888  1.000 13.98  ? 59  ASN A HB3  1 
ATOM   1068 D DD21 . ASN A 1 59  ? 31.694 19.677 5.971  1.000 13.09  ? 59  ASN A DD21 1 
ATOM   1069 D DD22 . ASN A 1 59  ? 31.414 18.990 7.568  1.000 13.53  ? 59  ASN A DD22 1 
ATOM   1070 N N    . SER A 1 60  ? 28.108 21.471 7.372  1.000 9.21   ? 60  SER A N    1 
ATOM   1071 C CA   . SER A 1 60  ? 27.376 22.598 6.831  1.000 8.63   ? 60  SER A CA   1 
ATOM   1072 C C    . SER A 1 60  ? 27.155 22.529 5.323  1.000 10.71  ? 60  SER A C    1 
ATOM   1073 O O    . SER A 1 60  ? 26.544 23.489 4.838  1.000 14.02  ? 60  SER A O    1 
ATOM   1074 C CB   . SER A 1 60  ? 28.121 23.867 7.067  1.000 9.80   ? 60  SER A CB   1 
ATOM   1075 O OG   . SER A 1 60  ? 29.420 23.806 6.472  1.000 9.84   ? 60  SER A OG   1 
ATOM   1076 H H    . SER A 1 60  ? 29.102 21.556 7.530  1.000 13.84  ? 60  SER A H    1 
ATOM   1077 H HA   . SER A 1 60  ? 26.399 22.660 7.332  1.000 9.71   ? 60  SER A HA   1 
ATOM   1078 H HB2  . SER A 1 60  ? 27.563 24.701 6.641  1.000 12.66  ? 60  SER A HB2  1 
ATOM   1079 H HB3  . SER A 1 60  ? 28.219 24.038 8.139  1.000 11.93  ? 60  SER A HB3  1 
ATOM   1080 D DG   . SER A 1 60  ? 29.488 24.588 5.874  1.000 11.05  ? 60  SER A DG   1 
ATOM   1081 N N    . ARG A 1 61  ? 27.634 21.542 4.598  1.000 9.37   ? 61  ARG A N    1 
ATOM   1082 C CA   . ARG A 1 61  ? 27.283 21.496 3.181  1.000 9.70   ? 61  ARG A CA   1 
ATOM   1083 C C    . ARG A 1 61  ? 25.858 21.011 2.992  1.000 10.51  ? 61  ARG A C    1 
ATOM   1084 O O    . ARG A 1 61  ? 25.113 21.674 2.280  1.000 11.45  ? 61  ARG A O    1 
ATOM   1085 C CB   . ARG A 1 61  ? 28.299 20.688 2.381  1.000 10.95  ? 61  ARG A CB   1 
ATOM   1086 C CG   . ARG A 1 61  ? 28.083 20.834 0.897  1.000 15.26  ? 61  ARG A CG   1 
ATOM   1087 C CD   . ARG A 1 61  ? 29.012 20.027 0.032  1.000 21.84  ? 61  ARG A CD   1 
ATOM   1088 N NE   . ARG A 1 61  ? 30.417 20.134 0.384  1.000 25.00  ? 61  ARG A NE   1 
ATOM   1089 C CZ   . ARG A 1 61  ? 31.287 21.011 -0.109 1.000 30.79  ? 61  ARG A CZ   1 
ATOM   1090 N NH1  . ARG A 1 61  ? 30.957 21.899 -1.024 1.000 34.89  ? 61  ARG A NH1  1 
ATOM   1091 N NH2  . ARG A 1 61  ? 32.515 20.912 0.402  1.000 32.50  ? 61  ARG A NH2  1 
ATOM   1092 H H    . ARG A 1 61  ? 28.228 20.836 5.010  1.000 11.10  ? 61  ARG A H    1 
ATOM   1093 H HA   . ARG A 1 61  ? 27.324 22.529 2.805  1.000 14.56  ? 61  ARG A HA   1 
ATOM   1094 H HB2  . ARG A 1 61  ? 29.305 21.024 2.634  1.000 17.87  ? 61  ARG A HB2  1 
ATOM   1095 H HB3  . ARG A 1 61  ? 28.218 19.636 2.655  1.000 18.10  ? 61  ARG A HB3  1 
ATOM   1096 H HG2  . ARG A 1 61  ? 27.058 20.544 0.667  1.000 17.62  ? 61  ARG A HG2  1 
ATOM   1097 H HG3  . ARG A 1 61  ? 28.193 21.886 0.634  1.000 18.97  ? 61  ARG A HG3  1 
ATOM   1098 H HD2  . ARG A 1 61  ? 28.718 18.979 0.090  1.000 25.94  ? 61  ARG A HD2  1 
ATOM   1099 H HD3  . ARG A 1 61  ? 28.888 20.346 -1.003 1.000 29.10  ? 61  ARG A HD3  1 
ATOM   1100 D DE   . ARG A 1 61  ? 30.691 19.452 1.102  1.000 26.85  ? 61  ARG A DE   1 
ATOM   1101 D DH11 . ARG A 1 61  ? 31.681 22.350 -1.572 1.000 39.48  ? 61  ARG A DH11 1 
ATOM   1102 D DH12 . ARG A 1 61  ? 29.986 22.135 -1.184 1.000 37.12  ? 61  ARG A DH12 1 
ATOM   1103 D DH21 . ARG A 1 61  ? 33.253 21.488 0.037  1.000 34.76  ? 61  ARG A DH21 1 
ATOM   1104 D DH22 . ARG A 1 61  ? 32.664 20.260 1.171  1.000 31.00  ? 61  ARG A DH22 1 
ATOM   1105 N N    . TRP A 1 62  ? 25.483 19.899 3.609  1.000 10.48  ? 62  TRP A N    1 
ATOM   1106 C CA   . TRP A 1 62  ? 24.139 19.376 3.415  1.000 11.59  ? 62  TRP A CA   1 
ATOM   1107 C C    . TRP A 1 62  ? 23.143 19.823 4.504  1.000 10.11  ? 62  TRP A C    1 
ATOM   1108 O O    . TRP A 1 62  ? 21.980 19.932 4.136  1.000 10.65  ? 62  TRP A O    1 
ATOM   1109 C CB   . TRP A 1 62  ? 24.034 17.848 3.241  1.000 14.05  ? 62  TRP A CB   1 
ATOM   1110 C CG   . TRP A 1 62  ? 24.595 17.362 1.942  1.000 16.21  ? 62  TRP A CG   1 
ATOM   1111 C CD1  . TRP A 1 62  ? 25.314 18.030 1.001  1.000 17.36  ? 62  TRP A CD1  1 
ATOM   1112 C CD2  . TRP A 1 62  ? 24.439 16.024 1.457  1.000 18.17  ? 62  TRP A CD2  1 
ATOM   1113 N NE1  . TRP A 1 62  ? 25.618 17.175 -0.036 1.000 20.47  ? 62  TRP A NE1  1 
ATOM   1114 C CE2  . TRP A 1 62  ? 25.092 15.938 0.222  1.000 20.47  ? 62  TRP A CE2  1 
ATOM   1115 C CE3  . TRP A 1 62  ? 23.808 14.878 1.963  1.000 22.32  ? 62  TRP A CE3  1 
ATOM   1116 C CZ2  . TRP A 1 62  ? 25.123 14.768 -0.499 1.000 20.46  ? 62  TRP A CZ2  1 
ATOM   1117 C CZ3  . TRP A 1 62  ? 23.824 13.694 1.259  1.000 22.80  ? 62  TRP A CZ3  1 
ATOM   1118 C CH2  . TRP A 1 62  ? 24.490 13.666 0.030  1.000 23.18  ? 62  TRP A CH2  1 
ATOM   1119 D D    . TRP A 1 62  ? 26.183 19.455 4.155  1.000 14.90  ? 62  TRP A D    1 
ATOM   1120 H HA   . TRP A 1 62  ? 23.776 19.814 2.474  1.000 10.83  ? 62  TRP A HA   1 
ATOM   1121 H HB2  . TRP A 1 62  ? 24.565 17.362 4.059  1.000 19.76  ? 62  TRP A HB2  1 
ATOM   1122 H HB3  . TRP A 1 62  ? 22.986 17.556 3.305  1.000 16.10  ? 62  TRP A HB3  1 
ATOM   1123 H HD1  . TRP A 1 62  ? 25.603 19.069 1.058  1.000 18.52  ? 62  TRP A HD1  1 
ATOM   1124 D DE1  . TRP A 1 62  ? 26.142 17.424 -0.852 1.000 25.57  ? 62  TRP A DE1  1 
ATOM   1125 H HE3  . TRP A 1 62  ? 23.303 14.925 2.916  1.000 27.47  ? 62  TRP A HE3  1 
ATOM   1126 H HZ2  . TRP A 1 62  ? 25.629 14.715 -1.452 1.000 48.82  ? 62  TRP A HZ2  1 
ATOM   1127 H HZ3  . TRP A 1 62  ? 23.336 12.811 1.646  1.000 47.34  ? 62  TRP A HZ3  1 
ATOM   1128 H HH2  . TRP A 1 62  ? 24.509 12.741 -0.527 1.000 52.53  ? 62  TRP A HH2  1 
ATOM   1129 N N    . TRP A 1 63  ? 23.564 20.025 5.754  1.000 8.30   ? 63  TRP A N    1 
ATOM   1130 C CA   . TRP A 1 63  ? 22.578 19.901 6.822  1.000 8.04   ? 63  TRP A CA   1 
ATOM   1131 C C    . TRP A 1 63  ? 22.151 21.196 7.498  1.000 9.02   ? 63  TRP A C    1 
ATOM   1132 O O    . TRP A 1 63  ? 20.987 21.345 7.857  1.000 11.31  ? 63  TRP A O    1 
ATOM   1133 C CB   . TRP A 1 63  ? 23.088 18.919 7.898  1.000 9.54   ? 63  TRP A CB   1 
ATOM   1134 C CG   . TRP A 1 63  ? 23.349 17.604 7.233  1.000 10.19  ? 63  TRP A CG   1 
ATOM   1135 C CD1  . TRP A 1 63  ? 24.573 17.042 7.038  1.000 12.04  ? 63  TRP A CD1  1 
ATOM   1136 C CD2  . TRP A 1 63  ? 22.397 16.677 6.667  1.000 9.86   ? 63  TRP A CD2  1 
ATOM   1137 N NE1  . TRP A 1 63  ? 24.462 15.842 6.409  1.000 13.26  ? 63  TRP A NE1  1 
ATOM   1138 C CE2  . TRP A 1 63  ? 23.140 15.584 6.155  1.000 12.07  ? 63  TRP A CE2  1 
ATOM   1139 C CE3  . TRP A 1 63  ? 21.019 16.659 6.552  1.000 10.90  ? 63  TRP A CE3  1 
ATOM   1140 C CZ2  . TRP A 1 63  ? 22.492 14.521 5.540  1.000 13.63  ? 63  TRP A CZ2  1 
ATOM   1141 C CZ3  . TRP A 1 63  ? 20.383 15.602 5.935  1.000 11.88  ? 63  TRP A CZ3  1 
ATOM   1142 C CH2  . TRP A 1 63  ? 21.124 14.535 5.429  1.000 13.79  ? 63  TRP A CH2  1 
ATOM   1143 H H    . TRP A 1 63  ? 24.528 20.255 5.953  1.000 17.54  ? 63  TRP A H    1 
ATOM   1144 H HA   . TRP A 1 63  ? 21.676 19.455 6.378  1.000 8.11   ? 63  TRP A HA   1 
ATOM   1145 H HB2  . TRP A 1 63  ? 24.004 19.300 8.350  1.000 13.91  ? 63  TRP A HB2  1 
ATOM   1146 H HB3  . TRP A 1 63  ? 22.339 18.801 8.682  1.000 10.03  ? 63  TRP A HB3  1 
ATOM   1147 H HD1  . TRP A 1 63  ? 25.507 17.490 7.342  1.000 13.14  ? 63  TRP A HD1  1 
ATOM   1148 D DE1  . TRP A 1 63  ? 25.224 15.198 6.240  1.000 18.25  ? 63  TRP A DE1  1 
ATOM   1149 H HE3  . TRP A 1 63  ? 20.437 17.478 6.949  1.000 12.02  ? 63  TRP A HE3  1 
ATOM   1150 H HZ2  . TRP A 1 63  ? 23.060 13.689 5.151  1.000 20.10  ? 63  TRP A HZ2  1 
ATOM   1151 H HZ3  . TRP A 1 63  ? 19.307 15.601 5.843  1.000 14.82  ? 63  TRP A HZ3  1 
ATOM   1152 H HH2  . TRP A 1 63  ? 20.617 13.713 4.946  1.000 13.59  ? 63  TRP A HH2  1 
ATOM   1153 N N    . CYS A 1 64  ? 23.066 22.152 7.696  1.000 10.37  ? 64  CYS A N    1 
ATOM   1154 C CA   . CYS A 1 64  ? 22.712 23.395 8.346  1.000 10.12  ? 64  CYS A CA   1 
ATOM   1155 C C    . CYS A 1 64  ? 23.289 24.554 7.539  1.000 10.12  ? 64  CYS A C    1 
ATOM   1156 O O    . CYS A 1 64  ? 24.240 24.379 6.767  1.000 11.96  ? 64  CYS A O    1 
ATOM   1157 C CB   . CYS A 1 64  ? 23.194 23.424 9.796  1.000 9.13   ? 64  CYS A CB   1 
ATOM   1158 S SG   . CYS A 1 64  ? 24.992 23.293 9.997  1.000 9.65   ? 64  CYS A SG   1 
ATOM   1159 H H    . CYS A 1 64  ? 24.016 22.003 7.388  1.000 15.41  ? 64  CYS A H    1 
ATOM   1160 H HA   . CYS A 1 64  ? 21.615 23.485 8.345  1.000 9.91   ? 64  CYS A HA   1 
ATOM   1161 H HB2  . CYS A 1 64  ? 22.859 24.355 10.255 1.000 11.56  ? 64  CYS A HB2  1 
ATOM   1162 H HB3  . CYS A 1 64  ? 22.723 22.603 10.336 1.000 12.45  ? 64  CYS A HB3  1 
ATOM   1163 N N    A ASN A 1 65  ? 22.725 25.740 7.720  0.401 10.37  ? 65  ASN A N    1 
ATOM   1164 N N    B ASN A 1 65  ? 22.769 25.755 7.724  0.599 10.06  ? 65  ASN A N    1 
ATOM   1165 C CA   A ASN A 1 65  ? 23.235 26.933 7.056  0.401 10.83  ? 65  ASN A CA   1 
ATOM   1166 C CA   B ASN A 1 65  ? 23.267 26.896 6.963  0.599 10.81  ? 65  ASN A CA   1 
ATOM   1167 C C    A ASN A 1 65  ? 24.230 27.705 7.912  0.401 9.97   ? 65  ASN A C    1 
ATOM   1168 C C    B ASN A 1 65  ? 24.164 27.813 7.784  0.599 10.04  ? 65  ASN A C    1 
ATOM   1169 O O    A ASN A 1 65  ? 23.937 28.111 9.039  0.401 9.63   ? 65  ASN A O    1 
ATOM   1170 O O    B ASN A 1 65  ? 23.715 28.416 8.761  0.599 8.98   ? 65  ASN A O    1 
ATOM   1171 C CB   A ASN A 1 65  ? 22.068 27.862 6.709  0.401 12.54  ? 65  ASN A CB   1 
ATOM   1172 C CB   B ASN A 1 65  ? 22.070 27.697 6.462  0.599 12.48  ? 65  ASN A CB   1 
ATOM   1173 C CG   A ASN A 1 65  ? 22.516 29.016 5.826  0.401 15.05  ? 65  ASN A CG   1 
ATOM   1174 C CG   B ASN A 1 65  ? 22.429 28.925 5.652  0.599 15.16  ? 65  ASN A CG   1 
ATOM   1175 O OD1  A ASN A 1 65  ? 22.955 28.801 4.693  0.401 16.17  ? 65  ASN A OD1  1 
ATOM   1176 O OD1  B ASN A 1 65  ? 23.502 29.070 5.075  0.599 14.26  ? 65  ASN A OD1  1 
ATOM   1177 N ND2  A ASN A 1 65  ? 22.425 30.238 6.304  0.401 16.36  ? 65  ASN A ND2  1 
ATOM   1178 N ND2  B ASN A 1 65  ? 21.485 29.856 5.557  0.599 17.76  ? 65  ASN A ND2  1 
ATOM   1179 H H    A ASN A 1 65  ? 21.924 25.818 8.331  0.401 9.72   ? 65  ASN A H    1 
ATOM   1180 H H    B ASN A 1 65  ? 22.024 25.884 8.394  0.599 15.51  ? 65  ASN A H    1 
ATOM   1181 H HA   A ASN A 1 65  ? 23.734 26.630 6.123  0.401 13.30  ? 65  ASN A HA   1 
ATOM   1182 H HA   B ASN A 1 65  ? 23.835 26.525 6.097  0.599 13.09  ? 65  ASN A HA   1 
ATOM   1183 H HB2  A ASN A 1 65  ? 21.295 27.292 6.194  0.401 20.32  ? 65  ASN A HB2  1 
ATOM   1184 H HB2  B ASN A 1 65  ? 21.447 27.045 5.849  0.599 14.83  ? 65  ASN A HB2  1 
ATOM   1185 H HB3  A ASN A 1 65  ? 21.637 28.258 7.629  0.401 14.24  ? 65  ASN A HB3  1 
ATOM   1186 H HB3  B ASN A 1 65  ? 21.475 28.008 7.321  0.599 15.53  ? 65  ASN A HB3  1 
ATOM   1187 D DD21 A ASN A 1 65  ? 21.561 30.558 6.709  0.401 18.45  ? 65  ASN A DD21 1 
ATOM   1188 D DD21 B ASN A 1 65  ? 20.647 29.738 6.120  0.599 19.84  ? 65  ASN A DD21 1 
ATOM   1189 D DD22 A ASN A 1 65  ? 23.228 30.857 6.240  0.401 19.91  ? 65  ASN A DD22 1 
ATOM   1190 D DD22 B ASN A 1 65  ? 21.632 30.633 4.947  0.599 20.49  ? 65  ASN A DD22 1 
ATOM   1191 N N    . ASP A 1 66  ? 25.424 27.950 7.375  1.000 9.96   ? 66  ASP A N    1 
ATOM   1192 C CA   . ASP A 1 66  ? 26.326 28.903 8.006  1.000 10.17  ? 66  ASP A CA   1 
ATOM   1193 C C    . ASP A 1 66  ? 26.668 30.063 7.081  1.000 10.51  ? 66  ASP A C    1 
ATOM   1194 O O    . ASP A 1 66  ? 27.503 30.882 7.458  1.000 12.03  ? 66  ASP A O    1 
ATOM   1195 C CB   . ASP A 1 66  ? 27.606 28.235 8.536  1.000 9.56   ? 66  ASP A CB   1 
ATOM   1196 C CG   . ASP A 1 66  ? 28.573 27.665 7.526  1.000 10.01  ? 66  ASP A CG   1 
ATOM   1197 O OD1  . ASP A 1 66  ? 28.355 27.886 6.304  1.000 10.50  ? 66  ASP A OD1  1 
ATOM   1198 O OD2  . ASP A 1 66  ? 29.565 27.033 7.943  1.000 10.71  ? 66  ASP A OD2  1 
ATOM   1199 D D    . ASP A 1 66  ? 25.702 27.420 6.565  1.000 11.55  ? 66  ASP A D    1 
ATOM   1200 H HA   . ASP A 1 66  ? 25.797 29.325 8.873  1.000 9.65   ? 66  ASP A HA   1 
ATOM   1201 H HB2  . ASP A 1 66  ? 28.144 28.971 9.135  1.000 15.99  ? 66  ASP A HB2  1 
ATOM   1202 H HB3  . ASP A 1 66  ? 27.309 27.429 9.207  1.000 12.27  ? 66  ASP A HB3  1 
ATOM   1203 N N    . GLY A 1 67  ? 26.030 30.130 5.919  1.000 11.71  ? 67  GLY A N    1 
ATOM   1204 C CA   . GLY A 1 67  ? 26.254 31.270 5.033  1.000 13.75  ? 67  GLY A CA   1 
ATOM   1205 C C    . GLY A 1 67  ? 27.567 31.313 4.298  1.000 15.87  ? 67  GLY A C    1 
ATOM   1206 O O    . GLY A 1 67  ? 27.753 32.224 3.477  1.000 22.97  ? 67  GLY A O    1 
ATOM   1207 D D    . GLY A 1 67  ? 25.388 29.414 5.613  1.000 13.00  ? 67  GLY A D    1 
ATOM   1208 H HA2  . GLY A 1 67  ? 25.453 31.287 4.295  1.000 24.17  ? 67  GLY A HA2  1 
ATOM   1209 H HA3  . GLY A 1 67  ? 26.169 32.181 5.625  1.000 13.86  ? 67  GLY A HA3  1 
ATOM   1210 N N    . ARG A 1 68  ? 28.498 30.419 4.570  1.000 13.69  ? 68  ARG A N    1 
ATOM   1211 C CA   . ARG A 1 68  ? 29.822 30.492 3.957  1.000 15.22  ? 68  ARG A CA   1 
ATOM   1212 C C    . ARG A 1 68  ? 30.215 29.242 3.187  1.000 14.53  ? 68  ARG A C    1 
ATOM   1213 O O    . ARG A 1 68  ? 31.342 29.160 2.658  1.000 20.07  ? 68  ARG A O    1 
ATOM   1214 C CB   . ARG A 1 68  ? 30.853 30.777 5.058  1.000 19.99  ? 68  ARG A CB   1 
ATOM   1215 C CG   . ARG A 1 68  ? 30.506 32.042 5.834  1.000 26.94  ? 68  ARG A CG   1 
ATOM   1216 C CD   . ARG A 1 68  ? 31.593 32.445 6.798  1.000 31.81  ? 68  ARG A CD   1 
ATOM   1217 N NE   . ARG A 1 68  ? 31.551 31.710 8.048  1.000 33.68  ? 68  ARG A NE   1 
ATOM   1218 C CZ   . ARG A 1 68  ? 32.144 30.548 8.263  1.000 37.36  ? 68  ARG A CZ   1 
ATOM   1219 N NH1  . ARG A 1 68  ? 33.156 30.117 7.532  1.000 39.97  ? 68  ARG A NH1  1 
ATOM   1220 N NH2  . ARG A 1 68  ? 31.655 29.830 9.269  1.000 37.09  ? 68  ARG A NH2  1 
ATOM   1221 D D    . ARG A 1 68  ? 28.314 29.683 5.249  1.000 13.88  ? 68  ARG A D    1 
ATOM   1222 H HA   . ARG A 1 68  ? 29.828 31.340 3.256  1.000 23.35  ? 68  ARG A HA   1 
ATOM   1223 H HB2  . ARG A 1 68  ? 30.890 29.931 5.745  1.000 35.34  ? 68  ARG A HB2  1 
ATOM   1224 H HB3  . ARG A 1 68  ? 31.840 30.889 4.609  1.000 49.19  ? 68  ARG A HB3  1 
ATOM   1225 H HG2  . ARG A 1 68  ? 30.334 32.856 5.130  1.000 22.91  ? 68  ARG A HG2  1 
ATOM   1226 H HG3  . ARG A 1 68  ? 29.581 31.878 6.387  1.000 23.58  ? 68  ARG A HG3  1 
ATOM   1227 H HD2  . ARG A 1 68  ? 32.562 32.285 6.326  1.000 59.39  ? 68  ARG A HD2  1 
ATOM   1228 H HD3  . ARG A 1 68  ? 31.499 33.510 7.011  1.000 167.91 ? 68  ARG A HD3  1 
ATOM   1229 D DE   . ARG A 1 68  ? 31.040 32.225 8.780  1.000 37.06  ? 68  ARG A DE   1 
ATOM   1230 D DH11 . ARG A 1 68  ? 33.411 29.134 7.539  1.000 43.68  ? 68  ARG A DH11 1 
ATOM   1231 D DH12 . ARG A 1 68  ? 33.677 30.768 6.957  1.000 41.70  ? 68  ARG A DH12 1 
ATOM   1232 D DH21 . ARG A 1 68  ? 31.911 28.857 9.353  1.000 38.09  ? 68  ARG A DH21 1 
ATOM   1233 D DH22 . ARG A 1 68  ? 31.007 30.289 9.912  1.000 31.68  ? 68  ARG A DH22 1 
ATOM   1234 N N    . THR A 1 69  ? 29.351 28.256 3.141  1.000 12.49  ? 69  THR A N    1 
ATOM   1235 C CA   . THR A 1 69  ? 29.705 26.961 2.595  1.000 11.61  ? 69  THR A CA   1 
ATOM   1236 C C    . THR A 1 69  ? 29.176 26.829 1.156  1.000 10.80  ? 69  THR A C    1 
ATOM   1237 O O    . THR A 1 69  ? 27.982 26.990 0.896  1.000 13.38  ? 69  THR A O    1 
ATOM   1238 C CB   . THR A 1 69  ? 29.114 25.837 3.437  1.000 10.80  ? 69  THR A CB   1 
ATOM   1239 O OG1  . THR A 1 69  ? 29.617 25.957 4.766  1.000 12.81  ? 69  THR A OG1  1 
ATOM   1240 C CG2  . THR A 1 69  ? 29.540 24.449 2.900  1.000 10.97  ? 69  THR A CG2  1 
ATOM   1241 D D    . THR A 1 69  ? 28.406 28.401 3.483  1.000 17.27  ? 69  THR A D    1 
ATOM   1242 H HA   . THR A 1 69  ? 30.800 26.864 2.584  1.000 15.90  ? 69  THR A HA   1 
ATOM   1243 H HB   . THR A 1 69  ? 28.017 25.914 3.445  1.000 13.47  ? 69  THR A HB   1 
ATOM   1244 D DG1  . THR A 1 69  ? 29.210 26.690 5.256  1.000 11.09  ? 69  THR A DG1  1 
ATOM   1245 H HG21 . THR A 1 69  ? 30.598 24.382 2.894  1.000 18.45  ? 69  THR A HG21 1 
ATOM   1246 H HG22 . THR A 1 69  ? 29.141 23.691 3.524  1.000 13.73  ? 69  THR A HG22 1 
ATOM   1247 H HG23 . THR A 1 69  ? 29.173 24.325 1.913  1.000 17.31  ? 69  THR A HG23 1 
ATOM   1248 N N    . PRO A 1 70  ? 29.994 26.525 0.165  1.000 12.54  ? 70  PRO A N    1 
ATOM   1249 C CA   . PRO A 1 70  ? 29.437 26.316 -1.171 1.000 13.47  ? 70  PRO A CA   1 
ATOM   1250 C C    . PRO A 1 70  ? 28.537 25.098 -1.250 1.000 13.58  ? 70  PRO A C    1 
ATOM   1251 O O    . PRO A 1 70  ? 28.717 24.059 -0.628 1.000 16.00  ? 70  PRO A O    1 
ATOM   1252 C CB   . PRO A 1 70  ? 30.670 26.126 -2.055 1.000 14.65  ? 70  PRO A CB   1 
ATOM   1253 C CG   . PRO A 1 70  ? 31.799 26.673 -1.251 1.000 16.42  ? 70  PRO A CG   1 
ATOM   1254 C CD   . PRO A 1 70  ? 31.457 26.336 0.172  1.000 14.34  ? 70  PRO A CD   1 
ATOM   1255 H HA   . PRO A 1 70  ? 28.883 27.212 -1.490 1.000 17.23  ? 70  PRO A HA   1 
ATOM   1256 H HB2  . PRO A 1 70  ? 30.829 25.071 -2.277 1.000 19.58  ? 70  PRO A HB2  1 
ATOM   1257 H HB3  . PRO A 1 70  ? 30.563 26.672 -2.992 1.000 25.89  ? 70  PRO A HB3  1 
ATOM   1258 H HG2  . PRO A 1 70  ? 32.742 26.209 -1.543 1.000 18.38  ? 70  PRO A HG2  1 
ATOM   1259 H HG3  . PRO A 1 70  ? 31.882 27.752 -1.384 1.000 20.56  ? 70  PRO A HG3  1 
ATOM   1260 H HD2  . PRO A 1 70  ? 31.727 25.309 0.416  1.000 24.93  ? 70  PRO A HD2  1 
ATOM   1261 H HD3  . PRO A 1 70  ? 31.945 27.014 0.872  1.000 38.20  ? 70  PRO A HD3  1 
ATOM   1262 N N    . GLY A 1 71  ? 27.521 25.165 -2.105 1.000 15.22  ? 71  GLY A N    1 
ATOM   1263 C CA   . GLY A 1 71  ? 26.626 24.056 -2.342 1.000 16.17  ? 71  GLY A CA   1 
ATOM   1264 C C    . GLY A 1 71  ? 25.667 23.756 -1.204 1.000 14.10  ? 71  GLY A C    1 
ATOM   1265 O O    . GLY A 1 71  ? 25.169 22.631 -1.081 1.000 17.56  ? 71  GLY A O    1 
ATOM   1266 D D    . GLY A 1 71  ? 27.385 26.028 -2.611 1.000 16.77  ? 71  GLY A D    1 
ATOM   1267 H HA2  . GLY A 1 71  ? 26.044 24.265 -3.240 1.000 22.36  ? 71  GLY A HA2  1 
ATOM   1268 H HA3  . GLY A 1 71  ? 27.222 23.165 -2.538 1.000 19.75  ? 71  GLY A HA3  1 
ATOM   1269 N N    . SER A 1 72  ? 25.381 24.730 -0.367 1.000 13.14  ? 72  SER A N    1 
ATOM   1270 C CA   . SER A 1 72  ? 24.574 24.458 0.818  1.000 13.55  ? 72  SER A CA   1 
ATOM   1271 C C    . SER A 1 72  ? 23.164 24.012 0.436  1.000 11.86  ? 72  SER A C    1 
ATOM   1272 O O    . SER A 1 72  ? 22.533 24.589 -0.418 1.000 14.65  ? 72  SER A O    1 
ATOM   1273 C CB   . SER A 1 72  ? 24.495 25.723 1.664  1.000 16.28  ? 72  SER A CB   1 
ATOM   1274 O OG   . SER A 1 72  ? 23.807 25.433 2.884  1.000 21.67  ? 72  SER A OG   1 
ATOM   1275 D D    . SER A 1 72  ? 25.740 25.634 -0.557 1.000 17.24  ? 72  SER A D    1 
ATOM   1276 H HA   . SER A 1 72  ? 25.056 23.662 1.406  1.000 15.47  ? 72  SER A HA   1 
ATOM   1277 H HB2  . SER A 1 72  ? 25.499 26.085 1.883  1.000 104.78 ? 72  SER A HB2  1 
ATOM   1278 H HB3  . SER A 1 72  ? 23.963 26.501 1.116  1.000 106.63 ? 72  SER A HB3  1 
ATOM   1279 D DG   . SER A 1 72  ? 23.305 26.233 3.157  1.000 28.99  ? 72  SER A DG   1 
ATOM   1280 N N    . ARG A 1 73  ? 22.723 22.936 1.106  1.000 9.56   ? 73  ARG A N    1 
ATOM   1281 C CA   . ARG A 1 73  ? 21.373 22.423 0.968  1.000 10.05  ? 73  ARG A CA   1 
ATOM   1282 C C    . ARG A 1 73  ? 20.460 22.734 2.170  1.000 9.54   ? 73  ARG A C    1 
ATOM   1283 O O    . ARG A 1 73  ? 19.235 22.746 2.045  1.000 10.52  ? 73  ARG A O    1 
ATOM   1284 C CB   . ARG A 1 73  ? 21.394 20.891 0.756  1.000 10.14  ? 73  ARG A CB   1 
ATOM   1285 C CG   . ARG A 1 73  ? 22.284 20.459 -0.409 1.000 12.12  ? 73  ARG A CG   1 
ATOM   1286 C CD   . ARG A 1 73  ? 22.125 19.005 -0.719 1.000 15.11  ? 73  ARG A CD   1 
ATOM   1287 N NE   . ARG A 1 73  ? 23.056 18.543 -1.746 1.000 16.92  ? 73  ARG A NE   1 
ATOM   1288 C CZ   . ARG A 1 73  ? 23.044 17.364 -2.353 1.000 22.11  ? 73  ARG A CZ   1 
ATOM   1289 N NH1  . ARG A 1 73  ? 22.241 16.408 -1.921 1.000 24.73  ? 73  ARG A NH1  1 
ATOM   1290 N NH2  . ARG A 1 73  ? 23.892 17.172 -3.347 1.000 25.36  ? 73  ARG A NH2  1 
ATOM   1291 D D    . ARG A 1 73  ? 23.373 22.427 1.644  1.000 12.05  ? 73  ARG A D    1 
ATOM   1292 H HA   . ARG A 1 73  ? 20.925 22.883 0.075  1.000 12.13  ? 73  ARG A HA   1 
ATOM   1293 H HB2  . ARG A 1 73  ? 21.747 20.411 1.669  1.000 16.93  ? 73  ARG A HB2  1 
ATOM   1294 H HB3  . ARG A 1 73  ? 20.376 20.545 0.572  1.000 12.19  ? 73  ARG A HB3  1 
ATOM   1295 H HG2  . ARG A 1 73  ? 22.030 21.045 -1.292 1.000 13.11  ? 73  ARG A HG2  1 
ATOM   1296 H HG3  . ARG A 1 73  ? 23.326 20.662 -0.160 1.000 16.50  ? 73  ARG A HG3  1 
ATOM   1297 H HD2  . ARG A 1 73  ? 22.283 18.428 0.192  1.000 17.32  ? 73  ARG A HD2  1 
ATOM   1298 H HD3  . ARG A 1 73  ? 21.104 18.823 -1.056 1.000 14.39  ? 73  ARG A HD3  1 
ATOM   1299 D DE   . ARG A 1 73  ? 23.779 19.240 -1.924 1.000 17.85  ? 73  ARG A DE   1 
ATOM   1300 D DH11 . ARG A 1 73  ? 22.172 15.532 -2.387 1.000 24.78  ? 73  ARG A DH11 1 
ATOM   1301 D DH12 . ARG A 1 73  ? 21.743 16.586 -1.026 1.000 20.91  ? 73  ARG A DH12 1 
ATOM   1302 D DH21 . ARG A 1 73  ? 23.861 16.311 -3.879 1.000 27.17  ? 73  ARG A DH21 1 
ATOM   1303 D DH22 . ARG A 1 73  ? 24.613 17.885 -3.516 1.000 27.68  ? 73  ARG A DH22 1 
ATOM   1304 N N    . ASN A 1 74  ? 21.032 22.952 3.346  1.000 9.07   ? 74  ASN A N    1 
ATOM   1305 C CA   . ASN A 1 74  ? 20.319 23.218 4.587  1.000 9.02   ? 74  ASN A CA   1 
ATOM   1306 C C    . ASN A 1 74  ? 19.132 22.296 4.806  1.000 8.80   ? 74  ASN A C    1 
ATOM   1307 O O    . ASN A 1 74  ? 17.985 22.750 4.990  1.000 8.49   ? 74  ASN A O    1 
ATOM   1308 C CB   . ASN A 1 74  ? 19.936 24.694 4.670  1.000 10.71  ? 74  ASN A CB   1 
ATOM   1309 C CG   . ASN A 1 74  ? 19.456 25.056 6.067  1.000 10.01  ? 74  ASN A CG   1 
ATOM   1310 O OD1  . ASN A 1 74  ? 19.641 24.322 7.049  1.000 10.09  ? 74  ASN A OD1  1 
ATOM   1311 N ND2  . ASN A 1 74  ? 18.834 26.229 6.161  1.000 13.80  ? 74  ASN A ND2  1 
ATOM   1312 D D    . ASN A 1 74  ? 22.029 22.941 3.392  1.000 10.04  ? 74  ASN A D    1 
ATOM   1313 H HA   . ASN A 1 74  ? 21.026 23.026 5.408  1.000 10.90  ? 74  ASN A HA   1 
ATOM   1314 H HB2  . ASN A 1 74  ? 20.800 25.307 4.414  1.000 10.95  ? 74  ASN A HB2  1 
ATOM   1315 H HB3  . ASN A 1 74  ? 19.146 24.905 3.949  1.000 13.37  ? 74  ASN A HB3  1 
ATOM   1316 D DD21 . ASN A 1 74  ? 18.544 26.538 7.078  1.000 13.40  ? 74  ASN A DD21 1 
ATOM   1317 D DD22 . ASN A 1 74  ? 18.686 26.762 5.328  1.000 16.45  ? 74  ASN A DD22 1 
ATOM   1318 N N    . LEU A 1 75  ? 19.363 20.975 4.813  1.000 8.35   ? 75  LEU A N    1 
ATOM   1319 C CA   . LEU A 1 75  ? 18.248 20.040 4.859  1.000 8.38   ? 75  LEU A CA   1 
ATOM   1320 C C    . LEU A 1 75  ? 17.633 19.975 6.245  1.000 8.57   ? 75  LEU A C    1 
ATOM   1321 O O    . LEU A 1 75  ? 16.484 19.527 6.381  1.000 9.01   ? 75  LEU A O    1 
ATOM   1322 C CB   . LEU A 1 75  ? 18.718 18.649 4.375  1.000 9.13   ? 75  LEU A CB   1 
ATOM   1323 C CG   . LEU A 1 75  ? 19.198 18.601 2.893  1.000 10.19  ? 75  LEU A CG   1 
ATOM   1324 C CD1  . LEU A 1 75  ? 19.659 17.189 2.559  1.000 11.80  ? 75  LEU A CD1  1 
ATOM   1325 C CD2  . LEU A 1 75  ? 18.114 19.030 1.918  1.000 12.31  ? 75  LEU A CD2  1 
ATOM   1326 H H    . LEU A 1 75  ? 20.311 20.629 4.786  1.000 12.59  ? 75  LEU A H    1 
ATOM   1327 H HA   . LEU A 1 75  ? 17.476 20.398 4.162  1.000 8.96   ? 75  LEU A HA   1 
ATOM   1328 H HB2  . LEU A 1 75  ? 19.536 18.317 5.016  1.000 11.82  ? 75  LEU A HB2  1 
ATOM   1329 H HB3  . LEU A 1 75  ? 17.897 17.942 4.498  1.000 10.16  ? 75  LEU A HB3  1 
ATOM   1330 H HG   . LEU A 1 75  ? 20.055 19.282 2.782  1.000 11.92  ? 75  LEU A HG   1 
ATOM   1331 H HD11 . LEU A 1 75  ? 18.845 16.518 2.661  1.000 16.11  ? 75  LEU A HD11 1 
ATOM   1332 H HD12 . LEU A 1 75  ? 20.018 17.160 1.562  1.000 18.31  ? 75  LEU A HD12 1 
ATOM   1333 H HD13 . LEU A 1 75  ? 20.436 16.904 3.222  1.000 17.56  ? 75  LEU A HD13 1 
ATOM   1334 H HD21 . LEU A 1 75  ? 17.279 18.383 2.011  1.000 17.28  ? 75  LEU A HD21 1 
ATOM   1335 H HD22 . LEU A 1 75  ? 17.817 20.024 2.135  1.000 20.97  ? 75  LEU A HD22 1 
ATOM   1336 H HD23 . LEU A 1 75  ? 18.490 18.982 0.928  1.000 19.14  ? 75  LEU A HD23 1 
ATOM   1337 N N    . CYS A 1 76  ? 18.348 20.360 7.308  1.000 8.77   ? 76  CYS A N    1 
ATOM   1338 C CA   . CYS A 1 76  ? 17.717 20.423 8.633  1.000 8.33   ? 76  CYS A CA   1 
ATOM   1339 C C    . CYS A 1 76  ? 17.005 21.757 8.839  1.000 8.93   ? 76  CYS A C    1 
ATOM   1340 O O    . CYS A 1 76  ? 16.339 21.914 9.880  1.000 10.16  ? 76  CYS A O    1 
ATOM   1341 C CB   . CYS A 1 76  ? 18.767 20.219 9.745  1.000 7.97   ? 76  CYS A CB   1 
ATOM   1342 S SG   . CYS A 1 76  ? 19.287 18.483 9.768  1.000 8.59   ? 76  CYS A SG   1 
ATOM   1343 H H    . CYS A 1 76  ? 19.322 20.606 7.199  1.000 10.18  ? 76  CYS A H    1 
ATOM   1344 H HA   . CYS A 1 76  ? 16.973 19.616 8.703  1.000 12.52  ? 76  CYS A HA   1 
ATOM   1345 H HB2  . CYS A 1 76  ? 19.629 20.860 9.561  1.000 9.53   ? 76  CYS A HB2  1 
ATOM   1346 H HB3  . CYS A 1 76  ? 18.340 20.490 10.710 1.000 10.50  ? 76  CYS A HB3  1 
ATOM   1347 N N    . ASN A 1 77  ? 17.114 22.704 7.912  1.000 8.57   ? 77  ASN A N    1 
ATOM   1348 C CA   . ASN A 1 77  ? 16.441 23.996 7.999  1.000 8.67   ? 77  ASN A CA   1 
ATOM   1349 C C    . ASN A 1 77  ? 16.765 24.756 9.268  1.000 9.39   ? 77  ASN A C    1 
ATOM   1350 O O    . ASN A 1 77  ? 15.868 25.238 9.943  1.000 10.84  ? 77  ASN A O    1 
ATOM   1351 C CB   . ASN A 1 77  ? 14.926 23.799 7.838  1.000 9.89   ? 77  ASN A CB   1 
ATOM   1352 C CG   . ASN A 1 77  ? 14.243 25.128 7.532  1.000 12.18  ? 77  ASN A CG   1 
ATOM   1353 O OD1  . ASN A 1 77  ? 14.899 26.039 7.048  1.000 14.03  ? 77  ASN A OD1  1 
ATOM   1354 N ND2  . ASN A 1 77  ? 12.954 25.167 7.813  1.000 15.21  ? 77  ASN A ND2  1 
ATOM   1355 D D    . ASN A 1 77  ? 17.644 22.534 7.072  1.000 13.19  ? 77  ASN A D    1 
ATOM   1356 H HA   . ASN A 1 77  ? 16.787 24.606 7.152  1.000 7.84   ? 77  ASN A HA   1 
ATOM   1357 H HB2  . ASN A 1 77  ? 14.734 23.095 7.028  1.000 11.61  ? 77  ASN A HB2  1 
ATOM   1358 H HB3  . ASN A 1 77  ? 14.513 23.380 8.756  1.000 12.66  ? 77  ASN A HB3  1 
ATOM   1359 D DD21 . ASN A 1 77  ? 12.443 26.026 7.629  1.000 19.75  ? 77  ASN A DD21 1 
ATOM   1360 D DD22 . ASN A 1 77  ? 12.508 24.380 8.234  1.000 16.48  ? 77  ASN A DD22 1 
ATOM   1361 N N    . ILE A 1 78  ? 18.060 24.864 9.552  1.000 9.01   ? 78  ILE A N    1 
ATOM   1362 C CA   . ILE A 1 78  ? 18.488 25.578 10.743 1.000 9.90   ? 78  ILE A CA   1 
ATOM   1363 C C    . ILE A 1 78  ? 19.799 26.277 10.492 1.000 9.98   ? 78  ILE A C    1 
ATOM   1364 O O    . ILE A 1 78  ? 20.590 25.798 9.674  1.000 9.87   ? 78  ILE A O    1 
ATOM   1365 C CB   . ILE A 1 78  ? 18.711 24.622 11.934 1.000 11.00  ? 78  ILE A CB   1 
ATOM   1366 C CG1  . ILE A 1 78  ? 19.562 23.406 11.572 1.000 11.90  ? 78  ILE A CG1  1 
ATOM   1367 C CG2  . ILE A 1 78  ? 17.384 24.264 12.566 1.000 14.09  ? 78  ILE A CG2  1 
ATOM   1368 C CD1  . ILE A 1 78  ? 20.257 22.724 12.696 1.000 14.96  ? 78  ILE A CD1  1 
ATOM   1369 H H    . ILE A 1 78  ? 18.746 24.449 8.939  1.000 10.67  ? 78  ILE A H    1 
ATOM   1370 H HA   . ILE A 1 78  ? 17.725 26.323 11.013 1.000 11.03  ? 78  ILE A HA   1 
ATOM   1371 H HB   . ILE A 1 78  ? 19.277 25.188 12.689 1.000 16.81  ? 78  ILE A HB   1 
ATOM   1372 H HG12 . ILE A 1 78  ? 18.920 22.677 11.078 1.000 18.27  ? 78  ILE A HG12 1 
ATOM   1373 H HG13 . ILE A 1 78  ? 20.314 23.720 10.848 1.000 24.60  ? 78  ILE A HG13 1 
ATOM   1374 H HG21 . ILE A 1 78  ? 16.800 23.714 11.873 1.000 17.24  ? 78  ILE A HG21 1 
ATOM   1375 H HG22 . ILE A 1 78  ? 17.552 23.675 13.431 1.000 15.46  ? 78  ILE A HG22 1 
ATOM   1376 H HG23 . ILE A 1 78  ? 16.870 25.151 12.836 1.000 20.02  ? 78  ILE A HG23 1 
ATOM   1377 H HD11 . ILE A 1 78  ? 20.889 23.416 13.192 1.000 26.23  ? 78  ILE A HD11 1 
ATOM   1378 H HD12 . ILE A 1 78  ? 19.539 22.348 13.379 1.000 39.40  ? 78  ILE A HD12 1 
ATOM   1379 H HD13 . ILE A 1 78  ? 20.839 21.923 12.317 1.000 20.42  ? 78  ILE A HD13 1 
ATOM   1380 N N    . PRO A 1 79  ? 20.062 27.351 11.215 1.000 10.55  ? 79  PRO A N    1 
ATOM   1381 C CA   . PRO A 1 79  ? 21.407 27.921 11.221 1.000 9.71   ? 79  PRO A CA   1 
ATOM   1382 C C    . PRO A 1 79  ? 22.340 26.985 11.958 1.000 9.15   ? 79  PRO A C    1 
ATOM   1383 O O    . PRO A 1 79  ? 22.004 26.340 12.939 1.000 10.10  ? 79  PRO A O    1 
ATOM   1384 C CB   . PRO A 1 79  ? 21.190 29.263 11.903 1.000 11.99  ? 79  PRO A CB   1 
ATOM   1385 C CG   . PRO A 1 79  ? 20.014 29.061 12.798 1.000 13.91  ? 79  PRO A CG   1 
ATOM   1386 C CD   . PRO A 1 79  ? 19.123 28.089 12.077 1.000 12.45  ? 79  PRO A CD   1 
ATOM   1387 H HA   . PRO A 1 79  ? 21.759 28.072 10.190 1.000 11.76  ? 79  PRO A HA   1 
ATOM   1388 H HB2  . PRO A 1 79  ? 22.069 29.549 12.481 1.000 15.68  ? 79  PRO A HB2  1 
ATOM   1389 H HB3  . PRO A 1 79  ? 20.985 30.041 11.167 1.000 16.78  ? 79  PRO A HB3  1 
ATOM   1390 H HG2  . PRO A 1 79  ? 20.327 28.655 13.759 1.000 19.76  ? 79  PRO A HG2  1 
ATOM   1391 H HG3  . PRO A 1 79  ? 19.494 30.004 12.969 1.000 16.23  ? 79  PRO A HG3  1 
ATOM   1392 H HD2  . PRO A 1 79  ? 18.624 27.420 12.777 1.000 16.26  ? 79  PRO A HD2  1 
ATOM   1393 H HD3  . PRO A 1 79  ? 18.372 28.610 11.484 1.000 13.61  ? 79  PRO A HD3  1 
ATOM   1394 N N    . CYS A 1 80  ? 23.585 26.864 11.473 1.000 8.98   ? 80  CYS A N    1 
ATOM   1395 C CA   . CYS A 1 80  ? 24.521 25.980 12.153 1.000 8.77   ? 80  CYS A CA   1 
ATOM   1396 C C    . CYS A 1 80  ? 24.789 26.420 13.598 1.000 8.30   ? 80  CYS A C    1 
ATOM   1397 O O    . CYS A 1 80  ? 25.128 25.538 14.393 1.000 9.11   ? 80  CYS A O    1 
ATOM   1398 C CB   . CYS A 1 80  ? 25.834 25.899 11.367 1.000 9.04   ? 80  CYS A CB   1 
ATOM   1399 S SG   . CYS A 1 80  ? 25.684 25.188 9.714  1.000 8.93   ? 80  CYS A SG   1 
ATOM   1400 H H    . CYS A 1 80  ? 23.868 27.377 10.650 1.000 10.92  ? 80  CYS A H    1 
ATOM   1401 H HA   . CYS A 1 80  ? 24.079 24.973 12.181 1.000 8.09   ? 80  CYS A HA   1 
ATOM   1402 H HB2  . CYS A 1 80  ? 26.246 26.904 11.276 1.000 11.45  ? 80  CYS A HB2  1 
ATOM   1403 H HB3  . CYS A 1 80  ? 26.545 25.303 11.938 1.000 9.36   ? 80  CYS A HB3  1 
ATOM   1404 N N    . SER A 1 81  ? 24.694 27.717 13.865 1.000 7.80   ? 81  SER A N    1 
ATOM   1405 C CA   . SER A 1 81  ? 24.899 28.119 15.252 1.000 10.14  ? 81  SER A CA   1 
ATOM   1406 C C    . SER A 1 81  ? 23.936 27.479 16.232 1.000 9.42   ? 81  SER A C    1 
ATOM   1407 O O    . SER A 1 81  ? 24.253 27.345 17.416 1.000 10.83  ? 81  SER A O    1 
ATOM   1408 C CB   . SER A 1 81  ? 24.812 29.644 15.342 1.000 12.12  ? 81  SER A CB   1 
ATOM   1409 O OG   . SER A 1 81  ? 23.575 30.089 14.817 1.000 15.45  ? 81  SER A OG   1 
ATOM   1410 D D    . SER A 1 81  ? 24.559 28.392 13.165 1.000 10.44  ? 81  SER A D    1 
ATOM   1411 H HA   . SER A 1 81  ? 25.918 27.823 15.540 1.000 13.06  ? 81  SER A HA   1 
ATOM   1412 H HB2  . SER A 1 81  ? 24.902 29.955 16.383 1.000 17.45  ? 81  SER A HB2  1 
ATOM   1413 H HB3  . SER A 1 81  ? 25.632 30.092 14.781 1.000 16.85  ? 81  SER A HB3  1 
ATOM   1414 D DG   . SER A 1 81  ? 22.977 30.284 15.553 1.000 19.78  ? 81  SER A DG   1 
ATOM   1415 N N    . ALA A 1 82  ? 22.761 27.025 15.791 1.000 8.99   ? 82  ALA A N    1 
ATOM   1416 C CA   . ALA A 1 82  ? 21.836 26.351 16.692 1.000 9.77   ? 82  ALA A CA   1 
ATOM   1417 C C    . ALA A 1 82  ? 22.398 25.018 17.171 1.000 8.79   ? 82  ALA A C    1 
ATOM   1418 O O    . ALA A 1 82  ? 21.966 24.534 18.216 1.000 10.70  ? 82  ALA A O    1 
ATOM   1419 C CB   . ALA A 1 82  ? 20.507 26.125 16.016 1.000 10.50  ? 82  ALA A CB   1 
ATOM   1420 H H    . ALA A 1 82  ? 22.510 27.150 14.820 1.000 10.83  ? 82  ALA A H    1 
ATOM   1421 H HA   . ALA A 1 82  ? 21.674 26.995 17.569 1.000 14.08  ? 82  ALA A HA   1 
ATOM   1422 H HB1  . ALA A 1 82  ? 20.644 25.505 15.167 1.000 13.83  ? 82  ALA A HB1  1 
ATOM   1423 H HB2  . ALA A 1 82  ? 19.841 25.655 16.693 1.000 11.69  ? 82  ALA A HB2  1 
ATOM   1424 H HB3  . ALA A 1 82  ? 20.103 27.057 15.712 1.000 18.95  ? 82  ALA A HB3  1 
ATOM   1425 N N    . LEU A 1 83  ? 23.361 24.453 16.461 1.000 9.34   ? 83  LEU A N    1 
ATOM   1426 C CA   . LEU A 1 83  ? 24.018 23.200 16.843 1.000 9.81   ? 83  LEU A CA   1 
ATOM   1427 C C    . LEU A 1 83  ? 25.113 23.373 17.865 1.000 10.35  ? 83  LEU A C    1 
ATOM   1428 O O    . LEU A 1 83  ? 25.690 22.387 18.303 1.000 14.01  ? 83  LEU A O    1 
ATOM   1429 C CB   . LEU A 1 83  ? 24.586 22.502 15.579 1.000 10.49  ? 83  LEU A CB   1 
ATOM   1430 C CG   . LEU A 1 83  ? 23.547 22.190 14.486 1.000 11.21  ? 83  LEU A CG   1 
ATOM   1431 C CD1  . LEU A 1 83  ? 24.272 21.680 13.272 1.000 13.85  ? 83  LEU A CD1  1 
ATOM   1432 C CD2  . LEU A 1 83  ? 22.489 21.226 15.012 1.000 12.87  ? 83  LEU A CD2  1 
ATOM   1433 H H    . LEU A 1 83  ? 23.660 24.910 15.611 1.000 9.82   ? 83  LEU A H    1 
ATOM   1434 H HA   . LEU A 1 83  ? 23.253 22.539 17.278 1.000 12.38  ? 83  LEU A HA   1 
ATOM   1435 H HB2  . LEU A 1 83  ? 25.359 23.139 15.150 1.000 17.26  ? 83  LEU A HB2  1 
ATOM   1436 H HB3  . LEU A 1 83  ? 25.060 21.569 15.883 1.000 12.24  ? 83  LEU A HB3  1 
ATOM   1437 H HG   . LEU A 1 83  ? 23.047 23.130 14.213 1.000 14.16  ? 83  LEU A HG   1 
ATOM   1438 H HD11 . LEU A 1 83  ? 24.764 20.771 13.510 1.000 27.53  ? 83  LEU A HD11 1 
ATOM   1439 H HD12 . LEU A 1 83  ? 23.577 21.510 12.490 1.000 25.11  ? 83  LEU A HD12 1 
ATOM   1440 H HD13 . LEU A 1 83  ? 24.987 22.397 12.960 1.000 20.24  ? 83  LEU A HD13 1 
ATOM   1441 H HD21 . LEU A 1 83  ? 22.948 20.310 15.283 1.000 24.09  ? 83  LEU A HD21 1 
ATOM   1442 H HD22 . LEU A 1 83  ? 22.017 21.649 15.862 1.000 23.24  ? 83  LEU A HD22 1 
ATOM   1443 H HD23 . LEU A 1 83  ? 21.765 21.050 14.258 1.000 25.50  ? 83  LEU A HD23 1 
ATOM   1444 N N    . LEU A 1 84  ? 25.427 24.595 18.250 1.000 10.68  ? 84  LEU A N    1 
ATOM   1445 C CA   . LEU A 1 84  ? 26.438 24.905 19.242 1.000 11.03  ? 84  LEU A CA   1 
ATOM   1446 C C    . LEU A 1 84  ? 25.865 25.348 20.573 1.000 13.56  ? 84  LEU A C    1 
ATOM   1447 O O    . LEU A 1 84  ? 26.598 25.913 21.382 1.000 17.94  ? 84  LEU A O    1 
ATOM   1448 C CB   . LEU A 1 84  ? 27.388 26.005 18.734 1.000 10.91  ? 84  LEU A CB   1 
ATOM   1449 C CG   . LEU A 1 84  ? 28.113 25.676 17.431 1.000 10.73  ? 84  LEU A CG   1 
ATOM   1450 C CD1  . LEU A 1 84  ? 28.936 26.843 16.945 1.000 13.09  ? 84  LEU A CD1  1 
ATOM   1451 C CD2  . LEU A 1 84  ? 29.031 24.483 17.613 1.000 12.27  ? 84  LEU A CD2  1 
ATOM   1452 H H    . LEU A 1 84  ? 24.931 25.366 17.826 1.000 14.98  ? 84  LEU A H    1 
ATOM   1453 H HA   . LEU A 1 84  ? 27.033 23.996 19.414 1.000 13.85  ? 84  LEU A HA   1 
ATOM   1454 H HB2  . LEU A 1 84  ? 26.814 26.920 18.589 1.000 12.24  ? 84  LEU A HB2  1 
ATOM   1455 H HB3  . LEU A 1 84  ? 28.133 26.203 19.504 1.000 13.51  ? 84  LEU A HB3  1 
ATOM   1456 H HG   . LEU A 1 84  ? 27.364 25.430 16.664 1.000 13.78  ? 84  LEU A HG   1 
ATOM   1457 H HD11 . LEU A 1 84  ? 29.663 27.090 17.676 1.000 23.24  ? 84  LEU A HD11 1 
ATOM   1458 H HD12 . LEU A 1 84  ? 29.421 26.580 16.040 1.000 15.68  ? 84  LEU A HD12 1 
ATOM   1459 H HD13 . LEU A 1 84  ? 28.304 27.677 16.779 1.000 18.51  ? 84  LEU A HD13 1 
ATOM   1460 H HD21 . LEU A 1 84  ? 29.758 24.706 18.351 1.000 20.78  ? 84  LEU A HD21 1 
ATOM   1461 H HD22 . LEU A 1 84  ? 28.462 23.643 17.921 1.000 19.10  ? 84  LEU A HD22 1 
ATOM   1462 H HD23 . LEU A 1 84  ? 29.513 24.265 16.695 1.000 20.48  ? 84  LEU A HD23 1 
ATOM   1463 N N    . SER A 1 85  ? 24.610 25.037 20.817 1.000 16.42  ? 85  SER A N    1 
ATOM   1464 C CA   . SER A 1 85  ? 23.946 25.257 22.097 1.000 15.89  ? 85  SER A CA   1 
ATOM   1465 C C    . SER A 1 85  ? 24.287 24.238 23.178 1.000 14.10  ? 85  SER A C    1 
ATOM   1466 O O    . SER A 1 85  ? 24.668 23.089 22.917 1.000 15.13  ? 85  SER A O    1 
ATOM   1467 C CB   . SER A 1 85  ? 22.424 25.200 21.823 1.000 16.47  ? 85  SER A CB   1 
ATOM   1468 O OG   . SER A 1 85  ? 21.946 23.920 21.417 1.000 21.47  ? 85  SER A OG   1 
ATOM   1469 D D    . SER A 1 85  ? 24.061 24.632 20.071 1.000 16.73  ? 85  SER A D    1 
ATOM   1470 H HA   . SER A 1 85  ? 24.204 26.262 22.462 1.000 15.14  ? 85  SER A HA   1 
ATOM   1471 H HB2  . SER A 1 85  ? 21.895 25.498 22.728 1.000 167.91 ? 85  SER A HB2  1 
ATOM   1472 H HB3  . SER A 1 85  ? 22.182 25.925 21.046 1.000 25.86  ? 85  SER A HB3  1 
ATOM   1473 D DG   . SER A 1 85  ? 21.579 23.390 22.173 1.000 23.35  ? 85  SER A DG   1 
ATOM   1474 N N    . SER A 1 86  ? 24.095 24.640 24.437 1.000 14.92  ? 86  SER A N    1 
ATOM   1475 C CA   . SER A 1 86  ? 24.312 23.703 25.537 1.000 16.53  ? 86  SER A CA   1 
ATOM   1476 C C    . SER A 1 86  ? 23.196 22.677 25.677 1.000 14.52  ? 86  SER A C    1 
ATOM   1477 O O    . SER A 1 86  ? 23.420 21.606 26.237 1.000 16.83  ? 86  SER A O    1 
ATOM   1478 C CB   . SER A 1 86  ? 24.473 24.472 26.844 1.000 20.96  ? 86  SER A CB   1 
ATOM   1479 O OG   . SER A 1 86  ? 25.672 25.235 26.856 1.000 24.49  ? 86  SER A OG   1 
ATOM   1480 D D    . SER A 1 86  ? 23.775 25.570 24.619 1.000 19.44  ? 86  SER A D    1 
ATOM   1481 H HA   . SER A 1 86  ? 25.249 23.162 25.343 1.000 25.89  ? 86  SER A HA   1 
ATOM   1482 H HB2  . SER A 1 86  ? 23.621 25.139 26.977 1.000 167.91 ? 86  SER A HB2  1 
ATOM   1483 H HB3  . SER A 1 86  ? 24.484 23.769 27.676 1.000 19.80  ? 86  SER A HB3  1 
ATOM   1484 D DG   . SER A 1 86  ? 25.488 26.149 27.158 1.000 28.70  ? 86  SER A DG   1 
ATOM   1485 N N    A ASP A 1 87  ? 22.083 22.983 25.018 0.570 13.75  ? 87  ASP A N    1 
ATOM   1486 N N    B ASP A 1 87  ? 21.982 23.007 25.251 0.430 13.77  ? 87  ASP A N    1 
ATOM   1487 C CA   A ASP A 1 87  ? 20.860 22.193 24.935 0.570 13.80  ? 87  ASP A CA   1 
ATOM   1488 C CA   B ASP A 1 87  ? 20.958 21.968 25.138 0.430 13.51  ? 87  ASP A CA   1 
ATOM   1489 C C    A ASP A 1 87  ? 20.974 21.346 23.656 0.570 12.58  ? 87  ASP A C    1 
ATOM   1490 C C    B ASP A 1 87  ? 21.029 21.340 23.741 0.430 12.94  ? 87  ASP A C    1 
ATOM   1491 O O    A ASP A 1 87  ? 21.274 21.906 22.603 0.570 14.58  ? 87  ASP A O    1 
ATOM   1492 O O    B ASP A 1 87  ? 21.308 22.004 22.754 0.430 14.08  ? 87  ASP A O    1 
ATOM   1493 C CB   A ASP A 1 87  ? 19.601 23.058 24.916 0.570 15.39  ? 87  ASP A CB   1 
ATOM   1494 C CB   B ASP A 1 87  ? 19.577 22.529 25.461 0.430 14.57  ? 87  ASP A CB   1 
ATOM   1495 C CG   A ASP A 1 87  ? 18.336 22.272 24.630 0.570 15.49  ? 87  ASP A CG   1 
ATOM   1496 C CG   B ASP A 1 87  ? 18.944 23.318 24.342 0.430 14.86  ? 87  ASP A CG   1 
ATOM   1497 O OD1  A ASP A 1 87  ? 17.668 21.803 25.574 0.570 20.12  ? 87  ASP A OD1  1 
ATOM   1498 O OD1  B ASP A 1 87  ? 17.849 22.936 23.875 0.430 16.08  ? 87  ASP A OD1  1 
ATOM   1499 O OD2  A ASP A 1 87  ? 17.994 22.105 23.441 0.570 17.73  ? 87  ASP A OD2  1 
ATOM   1500 O OD2  B ASP A 1 87  ? 19.549 24.333 23.937 0.430 15.65  ? 87  ASP A OD2  1 
ATOM   1501 D D    A ASP A 1 87  ? 22.162 23.830 24.461 0.570 14.21  ? 87  ASP A D    1 
ATOM   1502 D D    B ASP A 1 87  ? 21.796 23.964 25.010 0.430 13.37  ? 87  ASP A D    1 
ATOM   1503 H HA   A ASP A 1 87  ? 20.814 21.519 25.803 0.570 20.35  ? 87  ASP A HA   1 
ATOM   1504 H HA   B ASP A 1 87  ? 21.187 21.184 25.875 0.430 17.89  ? 87  ASP A HA   1 
ATOM   1505 H HB2  A ASP A 1 87  ? 19.498 23.553 25.881 0.570 13.94  ? 87  ASP A HB2  1 
ATOM   1506 H HB2  B ASP A 1 87  ? 18.917 21.701 25.720 0.430 15.45  ? 87  ASP A HB2  1 
ATOM   1507 H HB3  A ASP A 1 87  ? 19.715 23.831 24.157 0.570 27.23  ? 87  ASP A HB3  1 
ATOM   1508 H HB3  B ASP A 1 87  ? 19.659 23.171 26.337 0.430 27.83  ? 87  ASP A HB3  1 
ATOM   1509 N N    . ILE A 1 88  ? 20.798 20.027 23.736 1.000 12.00  ? 88  ILE A N    1 
ATOM   1510 C CA   . ILE A 1 88  ? 21.109 19.195 22.590 1.000 12.23  ? 88  ILE A CA   1 
ATOM   1511 C C    . ILE A 1 88  ? 19.956 19.067 21.593 1.000 11.09  ? 88  ILE A C    1 
ATOM   1512 O O    . ILE A 1 88  ? 20.129 18.387 20.578 1.000 11.35  ? 88  ILE A O    1 
ATOM   1513 C CB   . ILE A 1 88  ? 21.564 17.780 22.964 1.000 12.88  ? 88  ILE A CB   1 
ATOM   1514 C CG1  . ILE A 1 88  ? 20.475 16.954 23.653 1.000 14.01  ? 88  ILE A CG1  1 
ATOM   1515 C CG2  . ILE A 1 88  ? 22.809 17.897 23.824 1.000 15.84  ? 88  ILE A CG2  1 
ATOM   1516 C CD1  . ILE A 1 88  ? 20.887 15.500 23.862 1.000 15.12  ? 88  ILE A CD1  1 
ATOM   1517 D D    . ILE A 1 88  ? 20.496 19.649 24.609 1.000 14.59  ? 88  ILE A D    1 
ATOM   1518 H HA   . ILE A 1 88  ? 21.945 19.675 22.059 1.000 11.40  ? 88  ILE A HA   1 
ATOM   1519 H HB   . ILE A 1 88  ? 21.845 17.260 22.036 1.000 13.46  ? 88  ILE A HB   1 
ATOM   1520 H HG12 . ILE A 1 88  ? 20.247 17.402 24.620 1.000 21.65  ? 88  ILE A HG12 1 
ATOM   1521 H HG13 . ILE A 1 88  ? 19.569 16.984 23.049 1.000 20.50  ? 88  ILE A HG13 1 
ATOM   1522 H HG21 . ILE A 1 88  ? 22.567 18.396 24.728 1.000 26.97  ? 88  ILE A HG21 1 
ATOM   1523 H HG22 . ILE A 1 88  ? 23.180 16.929 24.043 1.000 22.40  ? 88  ILE A HG22 1 
ATOM   1524 H HG23 . ILE A 1 88  ? 23.548 18.449 23.303 1.000 21.16  ? 88  ILE A HG23 1 
ATOM   1525 H HD11 . ILE A 1 88  ? 21.111 15.058 22.925 1.000 22.79  ? 88  ILE A HD11 1 
ATOM   1526 H HD12 . ILE A 1 88  ? 21.745 15.462 24.484 1.000 31.34  ? 88  ILE A HD12 1 
ATOM   1527 H HD13 . ILE A 1 88  ? 20.093 14.970 24.322 1.000 21.00  ? 88  ILE A HD13 1 
ATOM   1528 N N    . THR A 1 89  ? 18.842 19.706 21.835 1.000 11.52  ? 89  THR A N    1 
ATOM   1529 C CA   . THR A 1 89  ? 17.678 19.481 21.013 1.000 12.66  ? 89  THR A CA   1 
ATOM   1530 C C    . THR A 1 89  ? 17.892 19.715 19.514 1.000 11.88  ? 89  THR A C    1 
ATOM   1531 O O    . THR A 1 89  ? 17.459 18.881 18.729 1.000 11.38  ? 89  THR A O    1 
ATOM   1532 C CB   . THR A 1 89  ? 16.545 20.399 21.522 1.000 16.28  ? 89  THR A CB   1 
ATOM   1533 O OG1  . THR A 1 89  ? 16.312 20.172 22.923 1.000 18.78  ? 89  THR A OG1  1 
ATOM   1534 C CG2  . THR A 1 89  ? 15.264 20.069 20.786 1.000 18.91  ? 89  THR A CG2  1 
ATOM   1535 D D    . THR A 1 89  ? 18.791 20.320 22.618 1.000 13.90  ? 89  THR A D    1 
ATOM   1536 H HA   . THR A 1 89  ? 17.360 18.437 21.153 1.000 14.39  ? 89  THR A HA   1 
ATOM   1537 H HB   . THR A 1 89  ? 16.813 21.453 21.354 1.000 23.59  ? 89  THR A HB   1 
ATOM   1538 D DG1  . THR A 1 89  ? 16.746 20.891 23.428 1.000 21.01  ? 89  THR A DG1  1 
ATOM   1539 H HG21 . THR A 1 89  ? 15.012 19.053 20.953 1.000 22.87  ? 89  THR A HG21 1 
ATOM   1540 H HG22 . THR A 1 89  ? 14.482 20.690 21.141 1.000 20.37  ? 89  THR A HG22 1 
ATOM   1541 H HG23 . THR A 1 89  ? 15.401 20.233 19.747 1.000 26.70  ? 89  THR A HG23 1 
ATOM   1542 N N    . ALA A 1 90  ? 18.476 20.823 19.093 1.000 11.21  ? 90  ALA A N    1 
ATOM   1543 C CA   . ALA A 1 90  ? 18.636 21.040 17.662 1.000 9.94   ? 90  ALA A CA   1 
ATOM   1544 C C    . ALA A 1 90  ? 19.547 19.979 17.037 1.000 8.89   ? 90  ALA A C    1 
ATOM   1545 O O    . ALA A 1 90  ? 19.305 19.519 15.909 1.000 9.94   ? 90  ALA A O    1 
ATOM   1546 C CB   . ALA A 1 90  ? 19.193 22.417 17.354 1.000 11.78  ? 90  ALA A CB   1 
ATOM   1547 D D    . ALA A 1 90  ? 18.785 21.513 19.764 1.000 12.30  ? 90  ALA A D    1 
ATOM   1548 H HA   . ALA A 1 90  ? 17.645 20.959 17.191 1.000 13.74  ? 90  ALA A HA   1 
ATOM   1549 H HB1  . ALA A 1 90  ? 20.150 22.518 17.798 1.000 14.95  ? 90  ALA A HB1  1 
ATOM   1550 H HB2  . ALA A 1 90  ? 19.277 22.538 16.304 1.000 18.57  ? 90  ALA A HB2  1 
ATOM   1551 H HB3  . ALA A 1 90  ? 18.542 23.157 17.744 1.000 24.99  ? 90  ALA A HB3  1 
ATOM   1552 N N    . SER A 1 91  ? 20.612 19.560 17.744 1.000 9.31   ? 91  SER A N    1 
ATOM   1553 C CA   . SER A 1 91  ? 21.470 18.512 17.223 1.000 9.42   ? 91  SER A CA   1 
ATOM   1554 C C    . SER A 1 91  ? 20.734 17.182 17.132 1.000 9.51   ? 91  SER A C    1 
ATOM   1555 O O    . SER A 1 91  ? 20.955 16.493 16.134 1.000 10.48  ? 91  SER A O    1 
ATOM   1556 C CB   . SER A 1 91  ? 22.709 18.357 18.119 1.000 10.72  ? 91  SER A CB   1 
ATOM   1557 O OG   . SER A 1 91  ? 23.600 19.454 17.933 1.000 12.68  ? 91  SER A OG   1 
ATOM   1558 D D    . SER A 1 91  ? 20.739 19.991 18.618 1.000 11.88  ? 91  SER A D    1 
ATOM   1559 H HA   . SER A 1 91  ? 21.801 18.799 16.214 1.000 8.94   ? 91  SER A HA   1 
ATOM   1560 H HB2  . SER A 1 91  ? 22.401 18.311 19.163 1.000 11.88  ? 91  SER A HB2  1 
ATOM   1561 H HB3  . SER A 1 91  ? 23.222 17.426 17.875 1.000 13.39  ? 91  SER A HB3  1 
ATOM   1562 D DG   . SER A 1 91  ? 23.353 20.224 18.443 1.000 13.50  ? 91  SER A DG   1 
ATOM   1563 N N    . VAL A 1 92  ? 19.896 16.855 18.107 1.000 9.65   ? 92  VAL A N    1 
ATOM   1564 C CA   . VAL A 1 92  ? 19.145 15.607 18.017 1.000 10.20  ? 92  VAL A CA   1 
ATOM   1565 C C    . VAL A 1 92  ? 18.120 15.645 16.876 1.000 9.87   ? 92  VAL A C    1 
ATOM   1566 O O    . VAL A 1 92  ? 17.999 14.656 16.172 1.000 9.64   ? 92  VAL A O    1 
ATOM   1567 C CB   . VAL A 1 92  ? 18.421 15.306 19.334 1.000 12.91  ? 92  VAL A CB   1 
ATOM   1568 C CG1  . VAL A 1 92  ? 17.468 14.138 19.177 1.000 14.98  ? 92  VAL A CG1  1 
ATOM   1569 C CG2  . VAL A 1 92  ? 19.382 14.963 20.446 1.000 14.15  ? 92  VAL A CG2  1 
ATOM   1570 H H    . VAL A 1 92  ? 19.779 17.464 18.904 1.000 10.17  ? 92  VAL A H    1 
ATOM   1571 H HA   . VAL A 1 92  ? 19.855 14.791 17.818 1.000 12.57  ? 92  VAL A HA   1 
ATOM   1572 H HB   . VAL A 1 92  ? 17.844 16.194 19.629 1.000 13.49  ? 92  VAL A HB   1 
ATOM   1573 H HG11 . VAL A 1 92  ? 18.012 13.274 18.892 1.000 17.76  ? 92  VAL A HG11 1 
ATOM   1574 H HG12 . VAL A 1 92  ? 16.975 13.958 20.098 1.000 25.36  ? 92  VAL A HG12 1 
ATOM   1575 H HG13 . VAL A 1 92  ? 16.750 14.366 18.431 1.000 18.08  ? 92  VAL A HG13 1 
ATOM   1576 H HG21 . VAL A 1 92  ? 19.946 14.107 20.175 1.000 19.08  ? 92  VAL A HG21 1 
ATOM   1577 H HG22 . VAL A 1 92  ? 20.037 15.779 20.612 1.000 14.89  ? 92  VAL A HG22 1 
ATOM   1578 H HG23 . VAL A 1 92  ? 18.839 14.760 21.333 1.000 15.42  ? 92  VAL A HG23 1 
ATOM   1579 N N    . ASN A 1 93  ? 17.422 16.760 16.759 1.000 9.86   ? 93  ASN A N    1 
ATOM   1580 C CA   . ASN A 1 93  ? 16.441 16.861 15.677 1.000 10.39  ? 93  ASN A CA   1 
ATOM   1581 C C    . ASN A 1 93  ? 17.092 16.751 14.317 1.000 9.52   ? 93  ASN A C    1 
ATOM   1582 O O    . ASN A 1 93  ? 16.560 16.114 13.397 1.000 10.38  ? 93  ASN A O    1 
ATOM   1583 C CB   . ASN A 1 93  ? 15.667 18.171 15.767 1.000 12.62  ? 93  ASN A CB   1 
ATOM   1584 C CG   . ASN A 1 93  ? 14.703 18.201 16.935 1.000 17.07  ? 93  ASN A CG   1 
ATOM   1585 O OD1  . ASN A 1 93  ? 14.360 17.156 17.488 1.000 19.15  ? 93  ASN A OD1  1 
ATOM   1586 N ND2  . ASN A 1 93  ? 14.304 19.409 17.318 1.000 19.97  ? 93  ASN A ND2  1 
ATOM   1587 H H    . ASN A 1 93  ? 17.561 17.526 17.403 1.000 16.39  ? 93  ASN A H    1 
ATOM   1588 H HA   . ASN A 1 93  ? 15.726 16.031 15.784 1.000 13.05  ? 93  ASN A HA   1 
ATOM   1589 H HB2  . ASN A 1 93  ? 16.373 18.995 15.867 1.000 15.08  ? 93  ASN A HB2  1 
ATOM   1590 H HB3  . ASN A 1 93  ? 15.109 18.319 14.843 1.000 16.53  ? 93  ASN A HB3  1 
ATOM   1591 D DD21 . ASN A 1 93  ? 13.608 19.472 18.048 1.000 23.86  ? 93  ASN A DD21 1 
ATOM   1592 D DD22 . ASN A 1 93  ? 14.739 20.216 16.898 1.000 21.10  ? 93  ASN A DD22 1 
ATOM   1593 N N    . CYS A 1 94  ? 18.257 17.352 14.142 1.000 9.61   ? 94  CYS A N    1 
ATOM   1594 C CA   . CYS A 1 94  ? 18.934 17.246 12.852 1.000 9.48   ? 94  CYS A CA   1 
ATOM   1595 C C    . CYS A 1 94  ? 19.514 15.839 12.645 1.000 9.49   ? 94  CYS A C    1 
ATOM   1596 O O    . CYS A 1 94  ? 19.464 15.321 11.517 1.000 10.28  ? 94  CYS A O    1 
ATOM   1597 C CB   . CYS A 1 94  ? 19.972 18.365 12.756 1.000 8.73   ? 94  CYS A CB   1 
ATOM   1598 S SG   . CYS A 1 94  ? 20.784 18.486 11.141 1.000 9.64   ? 94  CYS A SG   1 
ATOM   1599 H H    . CYS A 1 94  ? 18.675 17.881 14.894 1.000 16.34  ? 94  CYS A H    1 
ATOM   1600 H HA   . CYS A 1 94  ? 18.184 17.418 12.066 1.000 9.09   ? 94  CYS A HA   1 
ATOM   1601 H HB2  . CYS A 1 94  ? 19.484 19.315 12.974 1.000 13.53  ? 94  CYS A HB2  1 
ATOM   1602 H HB3  . CYS A 1 94  ? 20.733 18.203 13.519 1.000 13.34  ? 94  CYS A HB3  1 
ATOM   1603 N N    . ALA A 1 95  ? 20.046 15.227 13.697 1.000 8.35   ? 95  ALA A N    1 
ATOM   1604 C CA   . ALA A 1 95  ? 20.514 13.862 13.528 1.000 9.06   ? 95  ALA A CA   1 
ATOM   1605 C C    . ALA A 1 95  ? 19.383 12.949 13.111 1.000 9.87   ? 95  ALA A C    1 
ATOM   1606 O O    . ALA A 1 95  ? 19.586 12.068 12.298 1.000 10.59  ? 95  ALA A O    1 
ATOM   1607 C CB   . ALA A 1 95  ? 21.125 13.406 14.839 1.000 9.61   ? 95  ALA A CB   1 
ATOM   1608 H H    . ALA A 1 95  ? 20.123 15.696 14.588 1.000 9.34   ? 95  ALA A H    1 
ATOM   1609 H HA   . ALA A 1 95  ? 21.291 13.846 12.749 1.000 12.22  ? 95  ALA A HA   1 
ATOM   1610 H HB1  . ALA A 1 95  ? 20.385 13.418 15.597 1.000 16.70  ? 95  ALA A HB1  1 
ATOM   1611 H HB2  . ALA A 1 95  ? 21.502 12.421 14.729 1.000 14.02  ? 95  ALA A HB2  1 
ATOM   1612 H HB3  . ALA A 1 95  ? 21.916 14.059 15.107 1.000 16.49  ? 95  ALA A HB3  1 
ATOM   1613 N N    . LYS A 1 96  ? 18.176 13.141 13.659 1.000 10.71  ? 96  LYS A N    1 
ATOM   1614 C CA   . LYS A 1 96  ? 17.050 12.318 13.221 1.000 11.01  ? 96  LYS A CA   1 
ATOM   1615 C C    . LYS A 1 96  ? 16.763 12.523 11.736 1.000 10.99  ? 96  LYS A C    1 
ATOM   1616 O O    . LYS A 1 96  ? 16.394 11.594 11.037 1.000 12.54  ? 96  LYS A O    1 
ATOM   1617 C CB   . LYS A 1 96  ? 15.781 12.615 14.034 1.000 11.15  ? 96  LYS A CB   1 
ATOM   1618 C CG   . LYS A 1 96  ? 15.861 12.170 15.484 1.000 12.62  ? 96  LYS A CG   1 
ATOM   1619 C CD   . LYS A 1 96  ? 14.593 12.588 16.210 1.000 14.08  ? 96  LYS A CD   1 
ATOM   1620 C CE   . LYS A 1 96  ? 14.493 12.071 17.626 1.000 18.76  ? 96  LYS A CE   1 
ATOM   1621 N NZ   . LYS A 1 96  ? 13.320 12.685 18.321 1.000 23.12  ? 96  LYS A NZ   1 
ATOM   1622 H H    . LYS A 1 96  ? 18.045 13.847 14.370 1.000 10.06  ? 96  LYS A H    1 
ATOM   1623 H HA   . LYS A 1 96  ? 17.316 11.263 13.375 1.000 14.24  ? 96  LYS A HA   1 
ATOM   1624 H HB2  . LYS A 1 96  ? 15.589 13.687 14.006 1.000 16.69  ? 96  LYS A HB2  1 
ATOM   1625 H HB3  . LYS A 1 96  ? 14.936 12.115 13.560 1.000 17.78  ? 96  LYS A HB3  1 
ATOM   1626 H HG2  . LYS A 1 96  ? 15.974 11.087 15.532 1.000 13.49  ? 96  LYS A HG2  1 
ATOM   1627 H HG3  . LYS A 1 96  ? 16.728 12.626 15.962 1.000 13.33  ? 96  LYS A HG3  1 
ATOM   1628 H HD2  . LYS A 1 96  ? 14.544 13.677 16.232 1.000 17.35  ? 96  LYS A HD2  1 
ATOM   1629 H HD3  . LYS A 1 96  ? 13.732 12.231 15.646 1.000 35.07  ? 96  LYS A HD3  1 
ATOM   1630 H HE2  . LYS A 1 96  ? 14.384 10.986 17.611 1.000 20.46  ? 96  LYS A HE2  1 
ATOM   1631 H HE3  . LYS A 1 96  ? 15.407 12.312 18.168 1.000 16.18  ? 96  LYS A HE3  1 
ATOM   1632 D DZ1  . LYS A 1 96  ? 12.448 12.299 17.934 1.000 24.30  ? 96  LYS A DZ1  1 
ATOM   1633 D DZ2  . LYS A 1 96  ? 13.382 12.502 19.334 1.000 24.64  ? 96  LYS A DZ2  1 
ATOM   1634 D DZ3  . LYS A 1 96  ? 13.296 13.698 18.108 1.000 26.02  ? 96  LYS A DZ3  1 
ATOM   1635 N N    . LYS A 1 97  ? 16.893 13.759 11.258 1.000 10.61  ? 97  LYS A N    1 
ATOM   1636 C CA   . LYS A 1 97  ? 16.653 14.053 9.849  1.000 11.61  ? 97  LYS A CA   1 
ATOM   1637 C C    . LYS A 1 97  ? 17.708 13.414 8.978  1.000 12.37  ? 97  LYS A C    1 
ATOM   1638 O O    . LYS A 1 97  ? 17.417 12.917 7.882  1.000 14.31  ? 97  LYS A O    1 
ATOM   1639 C CB   . LYS A 1 97  ? 16.676 15.565 9.642  1.000 13.74  ? 97  LYS A CB   1 
ATOM   1640 C CG   . LYS A 1 97  ? 16.548 16.079 8.218  1.000 17.09  ? 97  LYS A CG   1 
ATOM   1641 C CD   . LYS A 1 97  ? 15.168 15.757 7.653  1.000 24.00  ? 97  LYS A CD   1 
ATOM   1642 C CE   . LYS A 1 97  ? 14.924 16.366 6.294  1.000 30.71  ? 97  LYS A CE   1 
ATOM   1643 N NZ   . LYS A 1 97  ? 13.621 15.888 5.722  1.000 34.56  ? 97  LYS A NZ   1 
ATOM   1644 H H    . LYS A 1 97  ? 17.164 14.506 11.881 1.000 12.58  ? 97  LYS A H    1 
ATOM   1645 H HA   . LYS A 1 97  ? 15.665 13.665 9.563  1.000 15.66  ? 97  LYS A HA   1 
ATOM   1646 H HB2  . LYS A 1 97  ? 15.866 15.997 10.229 1.000 20.26  ? 97  LYS A HB2  1 
ATOM   1647 H HB3  . LYS A 1 97  ? 17.611 15.946 10.053 1.000 14.09  ? 97  LYS A HB3  1 
ATOM   1648 H HG2  . LYS A 1 97  ? 16.704 17.158 8.204  1.000 17.84  ? 97  LYS A HG2  1 
ATOM   1649 H HG3  . LYS A 1 97  ? 17.313 15.618 7.594  1.000 21.45  ? 97  LYS A HG3  1 
ATOM   1650 H HD2  . LYS A 1 97  ? 15.059 14.675 7.580  1.000 24.35  ? 97  LYS A HD2  1 
ATOM   1651 H HD3  . LYS A 1 97  ? 14.409 16.121 8.345  1.000 35.57  ? 97  LYS A HD3  1 
ATOM   1652 H HE2  . LYS A 1 97  ? 14.906 17.453 6.381  1.000 21.06  ? 97  LYS A HE2  1 
ATOM   1653 H HE3  . LYS A 1 97  ? 15.738 16.094 5.622  1.000 28.58  ? 97  LYS A HE3  1 
ATOM   1654 D DZ1  . LYS A 1 97  ? 13.692 14.869 5.536  1.000 35.98  ? 97  LYS A DZ1  1 
ATOM   1655 D DZ2  . LYS A 1 97  ? 12.872 16.082 6.416  1.000 36.15  ? 97  LYS A DZ2  1 
ATOM   1656 D DZ3  . LYS A 1 97  ? 13.437 16.370 4.832  1.000 37.24  ? 97  LYS A DZ3  1 
ATOM   1657 N N    . ILE A 1 98  ? 18.965 13.411 9.430  1.000 10.87  ? 98  ILE A N    1 
ATOM   1658 C CA   . ILE A 1 98  ? 20.016 12.766 8.647  1.000 12.40  ? 98  ILE A CA   1 
ATOM   1659 C C    . ILE A 1 98  ? 19.676 11.304 8.429  1.000 13.84  ? 98  ILE A C    1 
ATOM   1660 O O    . ILE A 1 98  ? 19.760 10.803 7.304  1.000 16.60  ? 98  ILE A O    1 
ATOM   1661 C CB   . ILE A 1 98  ? 21.361 12.962 9.377  1.000 11.24  ? 98  ILE A CB   1 
ATOM   1662 C CG1  . ILE A 1 98  ? 21.777 14.417 9.289  1.000 11.24  ? 98  ILE A CG1  1 
ATOM   1663 C CG2  . ILE A 1 98  ? 22.450 12.064 8.818  1.000 14.64  ? 98  ILE A CG2  1 
ATOM   1664 C CD1  . ILE A 1 98  ? 22.919 14.858 10.169 1.000 12.60  ? 98  ILE A CD1  1 
ATOM   1665 H H    . ILE A 1 98  ? 19.187 13.853 10.311 1.000 11.85  ? 98  ILE A H    1 
ATOM   1666 H HA   . ILE A 1 98  ? 20.075 13.261 7.666  1.000 13.37  ? 98  ILE A HA   1 
ATOM   1667 H HB   . ILE A 1 98  ? 21.217 12.709 10.438 1.000 11.48  ? 98  ILE A HB   1 
ATOM   1668 H HG12 . ILE A 1 98  ? 22.048 14.629 8.254  1.000 14.40  ? 98  ILE A HG12 1 
ATOM   1669 H HG13 . ILE A 1 98  ? 20.910 15.031 9.528  1.000 17.02  ? 98  ILE A HG13 1 
ATOM   1670 H HG21 . ILE A 1 98  ? 22.606 12.292 7.795  1.000 23.81  ? 98  ILE A HG21 1 
ATOM   1671 H HG22 . ILE A 1 98  ? 23.350 12.223 9.356  1.000 17.40  ? 98  ILE A HG22 1 
ATOM   1672 H HG23 . ILE A 1 98  ? 22.156 11.050 8.914  1.000 21.49  ? 98  ILE A HG23 1 
ATOM   1673 H HD11 . ILE A 1 98  ? 22.679 14.662 11.183 1.000 19.59  ? 98  ILE A HD11 1 
ATOM   1674 H HD12 . ILE A 1 98  ? 23.796 14.325 9.904  1.000 20.40  ? 98  ILE A HD12 1 
ATOM   1675 H HD13 . ILE A 1 98  ? 23.084 15.897 10.039 1.000 17.18  ? 98  ILE A HD13 1 
ATOM   1676 N N    A VAL A 1 99  ? 19.290 10.569 9.466  0.055 14.39  ? 99  VAL A N    1 
ATOM   1677 N N    B VAL A 1 99  ? 19.269 10.599 9.467  0.945 13.35  ? 99  VAL A N    1 
ATOM   1678 C CA   A VAL A 1 99  ? 18.864 9.190  9.236  0.055 15.52  ? 99  VAL A CA   1 
ATOM   1679 C CA   B VAL A 1 99  ? 18.868 9.181  9.272  0.945 15.30  ? 99  VAL A CA   1 
ATOM   1680 C C    A VAL A 1 99  ? 17.684 9.149  8.267  0.055 17.01  ? 99  VAL A C    1 
ATOM   1681 C C    B VAL A 1 99  ? 17.617 9.018  8.441  0.945 16.51  ? 99  VAL A C    1 
ATOM   1682 O O    A VAL A 1 99  ? 17.728 8.462  7.247  0.055 18.34  ? 99  VAL A O    1 
ATOM   1683 O O    B VAL A 1 99  ? 17.502 8.125  7.595  0.945 19.67  ? 99  VAL A O    1 
ATOM   1684 C CB   A VAL A 1 99  ? 18.477 8.466  10.536 0.055 16.26  ? 99  VAL A CB   1 
ATOM   1685 C CB   B VAL A 1 99  ? 18.741 8.557  10.667 0.945 16.82  ? 99  VAL A CB   1 
ATOM   1686 C CG1  A VAL A 1 99  ? 18.995 7.034  10.503 0.055 17.04  ? 99  VAL A CG1  1 
ATOM   1687 C CG1  B VAL A 1 99  ? 18.099 7.184  10.610 0.945 17.37  ? 99  VAL A CG1  1 
ATOM   1688 C CG2  A VAL A 1 99  ? 19.003 9.215  11.751 0.055 16.52  ? 99  VAL A CG2  1 
ATOM   1689 C CG2  B VAL A 1 99  ? 20.102 8.519  11.346 0.945 16.30  ? 99  VAL A CG2  1 
ATOM   1690 H H    A VAL A 1 99  ? 19.291 10.956 10.398 0.055 167.91 ? 99  VAL A H    1 
ATOM   1691 H H    B VAL A 1 99  ? 19.231 11.018 10.386 0.945 13.50  ? 99  VAL A H    1 
ATOM   1692 H HA   A VAL A 1 99  ? 19.702 8.645  8.777  0.055 167.91 ? 99  VAL A HA   1 
ATOM   1693 H HA   B VAL A 1 99  ? 19.688 8.668  8.748  0.945 16.38  ? 99  VAL A HA   1 
ATOM   1694 H HB   A VAL A 1 99  ? 17.380 8.435  10.599 0.055 167.91 ? 99  VAL A HB   1 
ATOM   1695 H HB   B VAL A 1 99  ? 18.087 9.207  11.266 0.945 20.89  ? 99  VAL A HB   1 
ATOM   1696 H HG11 A VAL A 1 99  ? 20.053 7.042  10.442 0.055 7.69   ? 99  VAL A HG11 1 
ATOM   1697 H HG11 B VAL A 1 99  ? 18.708 6.532  10.038 0.945 40.23  ? 99  VAL A HG11 1 
ATOM   1698 H HG12 A VAL A 1 99  ? 18.696 6.530  11.386 0.055 0.08   ? 99  VAL A HG12 1 
ATOM   1699 H HG12 B VAL A 1 99  ? 17.997 6.800  11.593 0.945 23.55  ? 99  VAL A HG12 1 
ATOM   1700 H HG13 A VAL A 1 99  ? 18.596 6.534  9.658  0.055 5.31   ? 99  VAL A HG13 1 
ATOM   1701 H HG13 B VAL A 1 99  ? 17.142 7.259  10.159 0.945 28.00  ? 99  VAL A HG13 1 
ATOM   1702 H HG21 A VAL A 1 99  ? 20.061 9.257  11.710 0.055 20.40  ? 99  VAL A HG21 1 
ATOM   1703 H HG21 B VAL A 1 99  ? 20.757 7.898  10.791 0.945 41.18  ? 99  VAL A HG21 1 
ATOM   1704 H HG22 A VAL A 1 99  ? 18.610 10.199 11.757 0.055 0.08   ? 99  VAL A HG22 1 
ATOM   1705 H HG22 B VAL A 1 99  ? 20.500 9.500  11.394 0.945 23.89  ? 99  VAL A HG22 1 
ATOM   1706 H HG23 A VAL A 1 99  ? 18.704 8.710  12.634 0.055 0.08   ? 99  VAL A HG23 1 
ATOM   1707 H HG23 B VAL A 1 99  ? 19.996 8.133  12.328 0.945 22.93  ? 99  VAL A HG23 1 
ATOM   1708 N N    . SER A 1 100 ? 16.636 9.896  8.595  1.000 18.14  ? 100 SER A N    1 
ATOM   1709 C CA   . SER A 1 100 ? 15.401 9.871  7.816  1.000 19.13  ? 100 SER A CA   1 
ATOM   1710 C C    . SER A 1 100 ? 15.651 10.150 6.328  1.000 19.89  ? 100 SER A C    1 
ATOM   1711 O O    . SER A 1 100 ? 14.903 9.631  5.504  1.000 23.35  ? 100 SER A O    1 
ATOM   1712 C CB   . SER A 1 100 ? 14.386 10.913 8.285  1.000 20.65  ? 100 SER A CB   1 
ATOM   1713 O OG   . SER A 1 100 ? 14.047 10.759 9.632  1.000 23.96  ? 100 SER A OG   1 
ATOM   1714 D D    . SER A 1 100 ? 16.769 10.616 9.308  1.000 21.29  ? 100 SER A D    1 
ATOM   1715 H HA   . SER A 1 100 ? 14.947 8.874  7.913  1.000 18.40  ? 100 SER A HA   1 
ATOM   1716 H HB2  . SER A 1 100 ? 14.802 11.909 8.133  1.000 167.91 ? 100 SER A HB2  1 
ATOM   1717 H HB3  . SER A 1 100 ? 13.485 10.832 7.678  1.000 82.38  ? 100 SER A HB3  1 
ATOM   1718 D DG   . SER A 1 100 ? 14.780 11.079 10.218 1.000 24.68  ? 100 SER A DG   1 
ATOM   1719 N N    . ASP A 1 101 ? 16.646 10.949 5.984  1.000 18.21  ? 101 ASP A N    1 
ATOM   1720 C CA   . ASP A 1 101 ? 16.991 11.260 4.614  1.000 17.72  ? 101 ASP A CA   1 
ATOM   1721 C C    . ASP A 1 101 ? 17.954 10.212 4.066  1.000 20.60  ? 101 ASP A C    1 
ATOM   1722 O O    . ASP A 1 101 ? 18.941 10.502 3.380  1.000 29.00  ? 101 ASP A O    1 
ATOM   1723 C CB   . ASP A 1 101 ? 17.644 12.635 4.454  1.000 16.96  ? 101 ASP A CB   1 
ATOM   1724 C CG   . ASP A 1 101 ? 16.610 13.701 4.127  1.000 16.84  ? 101 ASP A CG   1 
ATOM   1725 O OD1  . ASP A 1 101 ? 15.447 13.368 3.882  1.000 19.19  ? 101 ASP A OD1  1 
ATOM   1726 O OD2  . ASP A 1 101 ? 17.023 14.887 4.120  1.000 17.25  ? 101 ASP A OD2  1 
ATOM   1727 D D    . ASP A 1 101 ? 17.187 11.374 6.744  1.000 17.17  ? 101 ASP A D    1 
ATOM   1728 H HA   . ASP A 1 101 ? 16.072 11.239 4.009  1.000 20.68  ? 101 ASP A HA   1 
ATOM   1729 H HB2  . ASP A 1 101 ? 18.157 12.901 5.378  1.000 20.21  ? 101 ASP A HB2  1 
ATOM   1730 H HB3  . ASP A 1 101 ? 18.385 12.593 3.657  1.000 24.24  ? 101 ASP A HB3  1 
ATOM   1731 D DD2  . ASP A 1 101 ? 16.414 15.431 3.582  1.000 16.38  ? 101 ASP A DD2  1 
ATOM   1732 N N    . GLY A 1 102 ? 17.673 8.958  4.394  1.000 21.73  ? 102 GLY A N    1 
ATOM   1733 C CA   . GLY A 1 102 ? 18.207 7.841  3.667  1.000 23.02  ? 102 GLY A CA   1 
ATOM   1734 C C    . GLY A 1 102 ? 19.626 7.441  4.022  1.000 24.65  ? 102 GLY A C    1 
ATOM   1735 O O    . GLY A 1 102 ? 20.306 6.793  3.223  1.000 29.42  ? 102 GLY A O    1 
ATOM   1736 D D    . GLY A 1 102 ? 17.058 8.788  5.200  1.000 30.90  ? 102 GLY A D    1 
ATOM   1737 H HA2  . GLY A 1 102 ? 17.557 6.982  3.832  1.000 167.91 ? 102 GLY A HA2  1 
ATOM   1738 H HA3  . GLY A 1 102 ? 18.173 8.077  2.603  1.000 60.42  ? 102 GLY A HA3  1 
ATOM   1739 N N    . ASN A 1 103 ? 20.053 7.803  5.210  1.000 22.75  ? 103 ASN A N    1 
ATOM   1740 C CA   . ASN A 1 103 ? 21.384 7.574  5.726  1.000 21.71  ? 103 ASN A CA   1 
ATOM   1741 C C    . ASN A 1 103 ? 21.192 6.708  6.980  1.000 21.87  ? 103 ASN A C    1 
ATOM   1742 O O    . ASN A 1 103 ? 20.229 6.937  7.713  1.000 24.02  ? 103 ASN A O    1 
ATOM   1743 C CB   . ASN A 1 103 ? 22.101 8.863  6.097  1.000 22.01  ? 103 ASN A CB   1 
ATOM   1744 C CG   . ASN A 1 103 ? 22.263 9.781  4.889  1.000 25.56  ? 103 ASN A CG   1 
ATOM   1745 O OD1  . ASN A 1 103 ? 23.083 9.513  4.004  1.000 33.43  ? 103 ASN A OD1  1 
ATOM   1746 N ND2  . ASN A 1 103 ? 21.466 10.844 4.878  1.000 25.11  ? 103 ASN A ND2  1 
ATOM   1747 D D    . ASN A 1 103 ? 19.375 8.267  5.836  1.000 26.65  ? 103 ASN A D    1 
ATOM   1748 H HA   . ASN A 1 103 ? 21.978 7.022  4.982  1.000 50.47  ? 103 ASN A HA   1 
ATOM   1749 H HB2  . ASN A 1 103 ? 21.535 9.381  6.871  1.000 33.01  ? 103 ASN A HB2  1 
ATOM   1750 H HB3  . ASN A 1 103 ? 23.084 8.624  6.503  1.000 35.87  ? 103 ASN A HB3  1 
ATOM   1751 D DD21 . ASN A 1 103 ? 21.513 11.481 4.108  1.000 25.62  ? 103 ASN A DD21 1 
ATOM   1752 D DD22 . ASN A 1 103 ? 20.824 10.971 5.654  1.000 21.39  ? 103 ASN A DD22 1 
ATOM   1753 N N    . GLY A 1 104 ? 22.100 5.792  7.179  1.000 21.09  ? 104 GLY A N    1 
ATOM   1754 C CA   . GLY A 1 104 ? 22.244 5.144  8.474  1.000 17.73  ? 104 GLY A CA   1 
ATOM   1755 C C    . GLY A 1 104 ? 23.232 5.974  9.285  1.000 15.42  ? 104 GLY A C    1 
ATOM   1756 O O    . GLY A 1 104 ? 23.582 7.099  8.938  1.000 17.76  ? 104 GLY A O    1 
ATOM   1757 D D    . GLY A 1 104 ? 22.761 5.532  6.452  1.000 22.58  ? 104 GLY A D    1 
ATOM   1758 H HA2  . GLY A 1 104 ? 21.281 5.099  8.982  1.000 28.51  ? 104 GLY A HA2  1 
ATOM   1759 H HA3  . GLY A 1 104 ? 22.618 4.128  8.348  1.000 19.11  ? 104 GLY A HA3  1 
ATOM   1760 N N    . MET A 1 105 ? 23.696 5.355  10.353 1.000 12.88  ? 105 MET A N    1 
ATOM   1761 C CA   . MET A 1 105 ? 24.703 5.994  11.182 1.000 12.27  ? 105 MET A CA   1 
ATOM   1762 C C    . MET A 1 105 ? 26.084 6.006  10.551 1.000 13.44  ? 105 MET A C    1 
ATOM   1763 O O    . MET A 1 105 ? 26.962 6.689  11.094 1.000 12.18  ? 105 MET A O    1 
ATOM   1764 C CB   . MET A 1 105 ? 24.771 5.405  12.601 1.000 12.90  ? 105 MET A CB   1 
ATOM   1765 C CG   . MET A 1 105 ? 23.532 5.755  13.420 1.000 12.97  ? 105 MET A CG   1 
ATOM   1766 S SD   . MET A 1 105 ? 23.709 5.428  15.176 1.000 12.49  ? 105 MET A SD   1 
ATOM   1767 C CE   . MET A 1 105 ? 24.818 6.792  15.598 1.000 12.59  ? 105 MET A CE   1 
ATOM   1768 D D    . MET A 1 105 ? 23.360 4.437  10.543 1.000 14.26  ? 105 MET A D    1 
ATOM   1769 H HA   . MET A 1 105 ? 24.398 7.046  11.292 1.000 15.05  ? 105 MET A HA   1 
ATOM   1770 H HB2  . MET A 1 105 ? 24.864 4.321  12.536 1.000 13.38  ? 105 MET A HB2  1 
ATOM   1771 H HB3  . MET A 1 105 ? 25.656 5.789  13.108 1.000 14.06  ? 105 MET A HB3  1 
ATOM   1772 H HG2  . MET A 1 105 ? 23.306 6.812  13.280 1.000 12.70  ? 105 MET A HG2  1 
ATOM   1773 H HG3  . MET A 1 105 ? 22.687 5.182  13.040 1.000 18.11  ? 105 MET A HG3  1 
ATOM   1774 H HE1  . MET A 1 105 ? 25.040 6.759  16.634 1.000 20.92  ? 105 MET A HE1  1 
ATOM   1775 H HE2  . MET A 1 105 ? 25.715 6.703  15.042 1.000 24.35  ? 105 MET A HE2  1 
ATOM   1776 H HE3  . MET A 1 105 ? 24.348 7.714  15.367 1.000 14.97  ? 105 MET A HE3  1 
ATOM   1777 N N    . ASN A 1 106 ? 26.254 5.311  9.420  1.000 15.70  ? 106 ASN A N    1 
ATOM   1778 C CA   . ASN A 1 106 ? 27.460 5.509  8.630  1.000 18.74  ? 106 ASN A CA   1 
ATOM   1779 C C    . ASN A 1 106 ? 27.688 6.948  8.192  1.000 16.95  ? 106 ASN A C    1 
ATOM   1780 O O    . ASN A 1 106 ? 28.790 7.283  7.732  1.000 21.05  ? 106 ASN A O    1 
ATOM   1781 C CB   . ASN A 1 106 ? 27.384 4.626  7.367  1.000 24.30  ? 106 ASN A CB   1 
ATOM   1782 C CG   . ASN A 1 106 ? 26.009 4.534  6.748  1.000 30.17  ? 106 ASN A CG   1 
ATOM   1783 O OD1  . ASN A 1 106 ? 25.079 3.925  7.301  1.000 30.91  ? 106 ASN A OD1  1 
ATOM   1784 N ND2  . ASN A 1 106 ? 25.763 5.127  5.576  1.000 47.45  ? 106 ASN A ND2  1 
ATOM   1785 D D    . ASN A 1 106 ? 25.572 4.644  9.109  1.000 21.07  ? 106 ASN A D    1 
ATOM   1786 H HA   . ASN A 1 106 ? 28.325 5.186  9.229  1.000 18.44  ? 106 ASN A HA   1 
ATOM   1787 H HB2  . ASN A 1 106 ? 28.075 5.022  6.623  1.000 33.71  ? 106 ASN A HB2  1 
ATOM   1788 H HB3  . ASN A 1 106 ? 27.718 3.621  7.624  1.000 167.91 ? 106 ASN A HB3  1 
ATOM   1789 D DD21 . ASN A 1 106 ? 24.817 5.440  5.396  1.000 56.94  ? 106 ASN A DD21 1 
ATOM   1790 D DD22 . ASN A 1 106 ? 26.524 5.223  4.921  1.000 56.94  ? 106 ASN A DD22 1 
ATOM   1791 N N    . ALA A 1 107 ? 26.707 7.842  8.253  1.000 16.59  ? 107 ALA A N    1 
ATOM   1792 C CA   . ALA A 1 107 ? 26.964 9.262  7.968  1.000 17.25  ? 107 ALA A CA   1 
ATOM   1793 C C    . ALA A 1 107 ? 27.956 9.872  8.942  1.000 14.25  ? 107 ALA A C    1 
ATOM   1794 O O    . ALA A 1 107 ? 28.562 10.911 8.631  1.000 18.66  ? 107 ALA A O    1 
ATOM   1795 C CB   . ALA A 1 107 ? 25.622 9.975  7.958  1.000 19.04  ? 107 ALA A CB   1 
ATOM   1796 D D    . ALA A 1 107 ? 25.798 7.552  8.500  1.000 18.04  ? 107 ALA A D    1 
ATOM   1797 H HA   . ALA A 1 107 ? 27.394 9.333  6.958  1.000 14.56  ? 107 ALA A HA   1 
ATOM   1798 H HB1  . ALA A 1 107 ? 25.186 9.921  8.922  1.000 167.91 ? 107 ALA A HB1  1 
ATOM   1799 H HB2  . ALA A 1 107 ? 25.764 10.991 7.690  1.000 17.15  ? 107 ALA A HB2  1 
ATOM   1800 H HB3  . ALA A 1 107 ? 24.980 9.510  7.253  1.000 167.91 ? 107 ALA A HB3  1 
ATOM   1801 N N    . TRP A 1 108 ? 28.174 9.298  10.114 1.000 11.75  ? 108 TRP A N    1 
ATOM   1802 C CA   . TRP A 1 108 ? 29.179 9.759  11.050 1.000 11.64  ? 108 TRP A CA   1 
ATOM   1803 C C    . TRP A 1 108 ? 30.423 8.873  10.938 1.000 10.66  ? 108 TRP A C    1 
ATOM   1804 O O    . TRP A 1 108 ? 30.366 7.686  11.269 1.000 11.35  ? 108 TRP A O    1 
ATOM   1805 C CB   . TRP A 1 108 ? 28.601 9.706  12.483 1.000 10.70  ? 108 TRP A CB   1 
ATOM   1806 C CG   . TRP A 1 108 ? 27.607 10.791 12.716 1.000 10.59  ? 108 TRP A CG   1 
ATOM   1807 C CD1  . TRP A 1 108 ? 27.894 12.077 13.076 1.000 13.01  ? 108 TRP A CD1  1 
ATOM   1808 C CD2  . TRP A 1 108 ? 26.170 10.739 12.591 1.000 11.18  ? 108 TRP A CD2  1 
ATOM   1809 N NE1  . TRP A 1 108 ? 26.745 12.833 13.197 1.000 12.80  ? 108 TRP A NE1  1 
ATOM   1810 C CE2  . TRP A 1 108 ? 25.674 12.026 12.904 1.000 11.09  ? 108 TRP A CE2  1 
ATOM   1811 C CE3  . TRP A 1 108 ? 25.295 9.702  12.238 1.000 13.05  ? 108 TRP A CE3  1 
ATOM   1812 C CZ2  . TRP A 1 108 ? 24.315 12.312 12.883 1.000 11.74  ? 108 TRP A CZ2  1 
ATOM   1813 C CZ3  . TRP A 1 108 ? 23.951 10.009 12.225 1.000 13.96  ? 108 TRP A CZ3  1 
ATOM   1814 C CH2  . TRP A 1 108 ? 23.472 11.290 12.539 1.000 13.13  ? 108 TRP A CH2  1 
ATOM   1815 H H    . TRP A 1 108 ? 27.611 8.499  10.370 1.000 18.45  ? 108 TRP A H    1 
ATOM   1816 H HA   . TRP A 1 108 ? 29.451 10.796 10.807 1.000 14.44  ? 108 TRP A HA   1 
ATOM   1817 H HB2  . TRP A 1 108 ? 28.124 8.740  12.643 1.000 12.34  ? 108 TRP A HB2  1 
ATOM   1818 H HB3  . TRP A 1 108 ? 29.415 9.803  13.202 1.000 14.44  ? 108 TRP A HB3  1 
ATOM   1819 H HD1  . TRP A 1 108 ? 28.892 12.455 13.244 1.000 16.23  ? 108 TRP A HD1  1 
ATOM   1820 D DE1  . TRP A 1 108 ? 26.724 13.796 13.427 1.000 14.97  ? 108 TRP A DE1  1 
ATOM   1821 H HE3  . TRP A 1 108 ? 25.654 8.714  11.990 1.000 14.38  ? 108 TRP A HE3  1 
ATOM   1822 H HZ2  . TRP A 1 108 ? 23.941 13.296 13.127 1.000 16.08  ? 108 TRP A HZ2  1 
ATOM   1823 H HZ3  . TRP A 1 108 ? 23.242 9.237  11.964 1.000 12.89  ? 108 TRP A HZ3  1 
ATOM   1824 H HH2  . TRP A 1 108 ? 22.409 11.475 12.508 1.000 12.84  ? 108 TRP A HH2  1 
ATOM   1825 N N    . VAL A 1 109 ? 31.503 9.473  10.451 1.000 11.27  ? 109 VAL A N    1 
ATOM   1826 C CA   . VAL A 1 109 ? 32.729 8.690  10.243 1.000 13.48  ? 109 VAL A CA   1 
ATOM   1827 C C    . VAL A 1 109 ? 33.256 8.090  11.525 1.000 12.58  ? 109 VAL A C    1 
ATOM   1828 O O    . VAL A 1 109 ? 33.797 6.983  11.607 1.000 13.55  ? 109 VAL A O    1 
ATOM   1829 C CB   . VAL A 1 109 ? 33.794 9.562  9.528  1.000 16.26  ? 109 VAL A CB   1 
ATOM   1830 C CG1  . VAL A 1 109 ? 34.284 10.742 10.360 1.000 20.79  ? 109 VAL A CG1  1 
ATOM   1831 C CG2  . VAL A 1 109 ? 34.996 8.742  9.117  1.000 19.40  ? 109 VAL A CG2  1 
ATOM   1832 D D    . VAL A 1 109 ? 31.453 10.462 10.194 1.000 13.18  ? 109 VAL A D    1 
ATOM   1833 H HA   . VAL A 1 109 ? 32.478 7.858  9.569  1.000 14.62  ? 109 VAL A HA   1 
ATOM   1834 H HB   . VAL A 1 109 ? 33.336 9.965  8.613  1.000 98.43  ? 109 VAL A HB   1 
ATOM   1835 H HG11 . VAL A 1 109 ? 34.732 10.385 11.252 1.000 27.94  ? 109 VAL A HG11 1 
ATOM   1836 H HG12 . VAL A 1 109 ? 34.997 11.295 9.803  1.000 31.26  ? 109 VAL A HG12 1 
ATOM   1837 H HG13 . VAL A 1 109 ? 33.464 11.368 10.603 1.000 22.77  ? 109 VAL A HG13 1 
ATOM   1838 H HG21 . VAL A 1 109 ? 35.461 8.339  9.980  1.000 22.68  ? 109 VAL A HG21 1 
ATOM   1839 H HG22 . VAL A 1 109 ? 34.685 7.953  8.481  1.000 24.52  ? 109 VAL A HG22 1 
ATOM   1840 H HG23 . VAL A 1 109 ? 35.685 9.361  8.601  1.000 25.35  ? 109 VAL A HG23 1 
ATOM   1841 N N    . ALA A 1 110 ? 33.114 8.814  12.653 1.000 12.70  ? 110 ALA A N    1 
ATOM   1842 C CA   . ALA A 1 110 ? 33.589 8.277  13.900 1.000 12.82  ? 110 ALA A CA   1 
ATOM   1843 C C    . ALA A 1 110 ? 32.744 7.106  14.378 1.000 12.64  ? 110 ALA A C    1 
ATOM   1844 O O    . ALA A 1 110 ? 33.266 6.191  15.011 1.000 13.57  ? 110 ALA A O    1 
ATOM   1845 C CB   . ALA A 1 110 ? 33.596 9.375  14.952 1.000 14.80  ? 110 ALA A CB   1 
ATOM   1846 D D    . ALA A 1 110 ? 32.671 9.736  12.636 1.000 11.70  ? 110 ALA A D    1 
ATOM   1847 H HA   . ALA A 1 110 ? 34.622 7.926  13.756 1.000 13.77  ? 110 ALA A HA   1 
ATOM   1848 H HB1  . ALA A 1 110 ? 32.608 9.726  15.103 1.000 17.67  ? 110 ALA A HB1  1 
ATOM   1849 H HB2  . ALA A 1 110 ? 33.977 8.990  15.863 1.000 20.70  ? 110 ALA A HB2  1 
ATOM   1850 H HB3  . ALA A 1 110 ? 34.209 10.176 14.624 1.000 24.70  ? 110 ALA A HB3  1 
ATOM   1851 N N    . TRP A 1 111 ? 31.451 7.093  14.075 1.000 12.07  ? 111 TRP A N    1 
ATOM   1852 C CA   . TRP A 1 111 ? 30.645 5.927  14.395 1.000 12.46  ? 111 TRP A CA   1 
ATOM   1853 C C    . TRP A 1 111 ? 31.138 4.706  13.617 1.000 12.07  ? 111 TRP A C    1 
ATOM   1854 O O    . TRP A 1 111 ? 31.332 3.623  14.147 1.000 12.57  ? 111 TRP A O    1 
ATOM   1855 C CB   . TRP A 1 111 ? 29.125 6.180  14.169 1.000 12.65  ? 111 TRP A CB   1 
ATOM   1856 C CG   . TRP A 1 111 ? 28.337 4.943  14.499 1.000 12.76  ? 111 TRP A CG   1 
ATOM   1857 C CD1  . TRP A 1 111 ? 27.852 4.572  15.737 1.000 13.26  ? 111 TRP A CD1  1 
ATOM   1858 C CD2  . TRP A 1 111 ? 27.936 3.905  13.580 1.000 12.77  ? 111 TRP A CD2  1 
ATOM   1859 N NE1  . TRP A 1 111 ? 27.199 3.373  15.625 1.000 14.08  ? 111 TRP A NE1  1 
ATOM   1860 C CE2  . TRP A 1 111 ? 27.223 2.930  14.314 1.000 13.41  ? 111 TRP A CE2  1 
ATOM   1861 C CE3  . TRP A 1 111 ? 28.106 3.695  12.213 1.000 14.10  ? 111 TRP A CE3  1 
ATOM   1862 C CZ2  . TRP A 1 111 ? 26.679 1.770  13.769 1.000 15.42  ? 111 TRP A CZ2  1 
ATOM   1863 C CZ3  . TRP A 1 111 ? 27.573 2.544  11.640 1.000 15.92  ? 111 TRP A CZ3  1 
ATOM   1864 C CH2  . TRP A 1 111 ? 26.873 1.612  12.406 1.000 16.40  ? 111 TRP A CH2  1 
ATOM   1865 H H    . TRP A 1 111 ? 31.029 7.891  13.624 1.000 24.36  ? 111 TRP A H    1 
ATOM   1866 H HA   . TRP A 1 111 ? 30.787 5.713  15.464 1.000 11.76  ? 111 TRP A HA   1 
ATOM   1867 H HB2  . TRP A 1 111 ? 28.793 7.004  14.802 1.000 13.72  ? 111 TRP A HB2  1 
ATOM   1868 H HB3  . TRP A 1 111 ? 28.950 6.459  13.130 1.000 14.92  ? 111 TRP A HB3  1 
ATOM   1869 H HD1  . TRP A 1 111 ? 27.970 5.137  16.650 1.000 15.60  ? 111 TRP A HD1  1 
ATOM   1870 D DE1  . TRP A 1 111 ? 26.767 2.868  16.375 1.000 18.59  ? 111 TRP A DE1  1 
ATOM   1871 H HE3  . TRP A 1 111 ? 28.643 4.412  11.609 1.000 19.44  ? 111 TRP A HE3  1 
ATOM   1872 H HZ2  . TRP A 1 111 ? 26.143 1.047  14.365 1.000 16.55  ? 111 TRP A HZ2  1 
ATOM   1873 H HZ3  . TRP A 1 111 ? 27.703 2.370  10.583 1.000 20.39  ? 111 TRP A HZ3  1 
ATOM   1874 H HH2  . TRP A 1 111 ? 26.469 0.736  11.920 1.000 23.42  ? 111 TRP A HH2  1 
ATOM   1875 N N    . ARG A 1 112 ? 31.316 4.889  12.306 1.000 12.43  ? 112 ARG A N    1 
ATOM   1876 C CA   . ARG A 1 112 ? 31.710 3.807  11.407 1.000 15.00  ? 112 ARG A CA   1 
ATOM   1877 C C    . ARG A 1 112 ? 33.053 3.219  11.798 1.000 15.70  ? 112 ARG A C    1 
ATOM   1878 O O    . ARG A 1 112 ? 33.279 2.017  11.681 1.000 16.71  ? 112 ARG A O    1 
ATOM   1879 C CB   . ARG A 1 112 ? 31.796 4.412  10.016 1.000 20.02  ? 112 ARG A CB   1 
ATOM   1880 C CG   . ARG A 1 112 ? 31.837 3.625  8.738  1.000 28.29  ? 112 ARG A CG   1 
ATOM   1881 C CD   . ARG A 1 112 ? 31.311 4.450  7.562  1.000 33.66  ? 112 ARG A CD   1 
ATOM   1882 N NE   . ARG A 1 112 ? 32.288 5.353  6.957  1.000 39.60  ? 112 ARG A NE   1 
ATOM   1883 C CZ   . ARG A 1 112 ? 32.068 6.533  6.379  1.000 43.99  ? 112 ARG A CZ   1 
ATOM   1884 N NH1  . ARG A 1 112 ? 31.025 7.315  6.619  1.000 44.89  ? 112 ARG A NH1  1 
ATOM   1885 N NH2  . ARG A 1 112 ? 32.941 7.015  5.493  1.000 45.52  ? 112 ARG A NH2  1 
ATOM   1886 H H    A ARG A 1 112 ? 31.174 5.812  11.921 0.608 13.41  ? 112 ARG A H    1 
ATOM   1887 D D    B ARG A 1 112 ? 31.150 5.797  11.914 0.392 13.50  ? 112 ARG A D    1 
ATOM   1888 H HA   . ARG A 1 112 ? 30.943 3.018  11.421 1.000 15.71  ? 112 ARG A HA   1 
ATOM   1889 H HB2  . ARG A 1 112 ? 30.946 5.088  9.927  1.000 24.68  ? 112 ARG A HB2  1 
ATOM   1890 H HB3  . ARG A 1 112 ? 32.688 5.038  10.014 1.000 17.09  ? 112 ARG A HB3  1 
ATOM   1891 H HG2  . ARG A 1 112 ? 32.864 3.319  8.534  1.000 146.25 ? 112 ARG A HG2  1 
ATOM   1892 H HG3  . ARG A 1 112 ? 31.233 2.724  8.847  1.000 31.22  ? 112 ARG A HG3  1 
ATOM   1893 H HD2  . ARG A 1 112 ? 30.948 3.767  6.793  1.000 23.95  ? 112 ARG A HD2  1 
ATOM   1894 H HD3  . ARG A 1 112 ? 30.461 5.040  7.905  1.000 167.91 ? 112 ARG A HD3  1 
ATOM   1895 D DE   . ARG A 1 112 ? 33.232 4.942  6.991  1.000 41.77  ? 112 ARG A DE   1 
ATOM   1896 D DH11 . ARG A 1 112 ? 30.768 8.021  5.931  1.000 44.17  ? 112 ARG A DH11 1 
ATOM   1897 D DH12 . ARG A 1 112 ? 30.516 7.234  7.484  1.000 39.54  ? 112 ARG A DH12 1 
ATOM   1898 D DH21 . ARG A 1 112 ? 32.672 7.086  4.521  1.000 46.15  ? 112 ARG A DH21 1 
ATOM   1899 D DH22 . ARG A 1 112 ? 33.844 7.327  5.810  1.000 46.51  ? 112 ARG A DH22 1 
ATOM   1900 N N    A ASN A 1 113 ? 33.971 4.059  12.286 0.607 15.04  ? 113 ASN A N    1 
ATOM   1901 N N    B ASN A 1 113 ? 33.973 4.079  12.238 0.393 15.17  ? 113 ASN A N    1 
ATOM   1902 C CA   A ASN A 1 113 ? 35.336 3.581  12.514 0.607 15.84  ? 113 ASN A CA   1 
ATOM   1903 C CA   B ASN A 1 113 ? 35.339 3.643  12.529 0.393 15.85  ? 113 ASN A CA   1 
ATOM   1904 C C    A ASN A 1 113 ? 35.561 3.187  13.971 0.607 14.66  ? 113 ASN A C    1 
ATOM   1905 C C    B ASN A 1 113 ? 35.500 3.136  13.955 0.393 15.10  ? 113 ASN A C    1 
ATOM   1906 O O    A ASN A 1 113 ? 36.473 2.407  14.259 0.607 16.16  ? 113 ASN A O    1 
ATOM   1907 O O    B ASN A 1 113 ? 36.283 2.216  14.203 0.393 15.00  ? 113 ASN A O    1 
ATOM   1908 C CB   A ASN A 1 113 ? 36.358 4.627  12.124 0.607 17.05  ? 113 ASN A CB   1 
ATOM   1909 C CB   B ASN A 1 113 ? 36.319 4.787  12.268 0.393 17.31  ? 113 ASN A CB   1 
ATOM   1910 C CG   A ASN A 1 113 ? 36.430 4.975  10.651 0.607 19.47  ? 113 ASN A CG   1 
ATOM   1911 C CG   B ASN A 1 113 ? 36.663 4.859  10.786 0.393 19.57  ? 113 ASN A CG   1 
ATOM   1912 O OD1  A ASN A 1 113 ? 35.929 4.266  9.776  0.607 20.32  ? 113 ASN A OD1  1 
ATOM   1913 O OD1  B ASN A 1 113 ? 37.484 4.055  10.332 0.393 20.59  ? 113 ASN A OD1  1 
ATOM   1914 N ND2  A ASN A 1 113 ? 37.086 6.089  10.365 0.607 20.42  ? 113 ASN A ND2  1 
ATOM   1915 N ND2  B ASN A 1 113 ? 36.060 5.754  10.027 0.393 20.52  ? 113 ASN A ND2  1 
ATOM   1916 H H    A ASN A 1 113 ? 33.726 5.016  12.495 0.607 102.08 ? 113 ASN A H    1 
ATOM   1917 H H    B ASN A 1 113 ? 33.722 5.048  12.373 0.393 10.92  ? 113 ASN A H    1 
ATOM   1918 H HA   A ASN A 1 113 ? 35.498 2.691  11.888 0.607 26.86  ? 113 ASN A HA   1 
ATOM   1919 H HA   B ASN A 1 113 ? 35.587 2.819  11.844 0.393 12.51  ? 113 ASN A HA   1 
ATOM   1920 H HB2  A ASN A 1 113 ? 36.142 5.539  12.680 0.607 59.04  ? 113 ASN A HB2  1 
ATOM   1921 H HB2  B ASN A 1 113 ? 35.874 5.730  12.586 0.393 9.68   ? 113 ASN A HB2  1 
ATOM   1922 H HB3  A ASN A 1 113 ? 37.341 4.278  12.440 0.607 19.18  ? 113 ASN A HB3  1 
ATOM   1923 H HB3  B ASN A 1 113 ? 37.229 4.629  12.848 0.393 9.33   ? 113 ASN A HB3  1 
ATOM   1924 D DD21 A ASN A 1 113 ? 37.496 6.195  9.451  0.607 22.37  ? 113 ASN A DD21 1 
ATOM   1925 D DD21 B ASN A 1 113 ? 35.840 5.520  9.069  0.393 20.57  ? 113 ASN A DD21 1 
ATOM   1926 D DD22 A ASN A 1 113 ? 37.146 6.818  11.053 0.607 22.27  ? 113 ASN A DD22 1 
ATOM   1927 D DD22 B ASN A 1 113 ? 35.821 6.656  10.406 0.393 21.79  ? 113 ASN A DD22 1 
ATOM   1928 N N    . ARG A 1 114 ? 34.773 3.722  14.900 1.000 15.34  ? 114 ARG A N    1 
ATOM   1929 C CA   . ARG A 1 114 ? 35.087 3.531  16.307 1.000 14.86  ? 114 ARG A CA   1 
ATOM   1930 C C    . ARG A 1 114 ? 33.951 2.932  17.120 1.000 15.12  ? 114 ARG A C    1 
ATOM   1931 O O    . ARG A 1 114 ? 34.198 2.534  18.270 1.000 18.61  ? 114 ARG A O    1 
ATOM   1932 C CB   . ARG A 1 114 ? 35.547 4.854  16.956 1.000 16.22  ? 114 ARG A CB   1 
ATOM   1933 C CG   . ARG A 1 114 ? 36.657 5.465  16.090 1.000 17.80  ? 114 ARG A CG   1 
ATOM   1934 C CD   . ARG A 1 114 ? 37.522 6.411  16.879 1.000 19.38  ? 114 ARG A CD   1 
ATOM   1935 N NE   . ARG A 1 114 ? 38.398 5.685  17.807 1.000 20.25  ? 114 ARG A NE   1 
ATOM   1936 C CZ   . ARG A 1 114 ? 39.260 6.304  18.591 1.000 20.48  ? 114 ARG A CZ   1 
ATOM   1937 N NH1  . ARG A 1 114 ? 39.345 7.618  18.500 1.000 20.49  ? 114 ARG A NH1  1 
ATOM   1938 N NH2  . ARG A 1 114 ? 39.985 5.599  19.444 1.000 23.85  ? 114 ARG A NH2  1 
ATOM   1939 H H    A ARG A 1 114 ? 33.961 4.259  14.629 1.000 24.51  ? 114 ARG A H    1 
ATOM   1940 H HA   . ARG A 1 114 ? 35.932 2.830  16.361 1.000 17.14  ? 114 ARG A HA   1 
ATOM   1941 H HB2  . ARG A 1 114 ? 34.708 5.546  17.027 1.000 18.62  ? 114 ARG A HB2  1 
ATOM   1942 H HB3  . ARG A 1 114 ? 35.922 4.665  17.962 1.000 25.30  ? 114 ARG A HB3  1 
ATOM   1943 H HG2  . ARG A 1 114 ? 37.277 4.665  15.683 1.000 18.23  ? 114 ARG A HG2  1 
ATOM   1944 H HG3  . ARG A 1 114 ? 36.208 6.000  15.254 1.000 20.36  ? 114 ARG A HG3  1 
ATOM   1945 H HD2  . ARG A 1 114 ? 38.130 7.001  16.193 1.000 21.85  ? 114 ARG A HD2  1 
ATOM   1946 H HD3  . ARG A 1 114 ? 36.888 7.096  17.441 1.000 16.54  ? 114 ARG A HD3  1 
ATOM   1947 D DE   . ARG A 1 114 ? 38.265 4.691  17.778 1.000 22.41  ? 114 ARG A DE   1 
ATOM   1948 D DH11 . ARG A 1 114 ? 40.030 8.116  19.050 1.000 24.21  ? 114 ARG A DH11 1 
ATOM   1949 D DH12 . ARG A 1 114 ? 38.729 8.130  17.889 1.000 21.43  ? 114 ARG A DH12 1 
ATOM   1950 D DH21 . ARG A 1 114 ? 40.638 6.072  20.056 1.000 25.86  ? 114 ARG A DH21 1 
ATOM   1951 D DH22 . ARG A 1 114 ? 39.839 4.587  19.491 1.000 24.87  ? 114 ARG A DH22 1 
ATOM   1952 N N    . CYS A 1 115 ? 32.757 2.831  16.556 1.000 13.19  ? 115 CYS A N    1 
ATOM   1953 C CA   . CYS A 1 115 ? 31.641 2.299  17.340 1.000 12.62  ? 115 CYS A CA   1 
ATOM   1954 C C    . CYS A 1 115 ? 31.084 1.039  16.705 1.000 12.73  ? 115 CYS A C    1 
ATOM   1955 O O    . CYS A 1 115 ? 30.766 0.096  17.406 1.000 14.47  ? 115 CYS A O    1 
ATOM   1956 C CB   . CYS A 1 115 ? 30.517 3.328  17.391 1.000 12.06  ? 115 CYS A CB   1 
ATOM   1957 S SG   . CYS A 1 115 ? 30.995 4.880  18.196 1.000 11.75  ? 115 CYS A SG   1 
ATOM   1958 D D    A CYS A 1 115 ? 32.560 3.332  15.707 0.376 11.53  ? 115 CYS A D    1 
ATOM   1959 H H    B CYS A 1 115 ? 32.574 3.338  15.701 0.624 11.13  ? 115 CYS A H    1 
ATOM   1960 H HA   . CYS A 1 115 ? 31.983 2.076  18.361 1.000 17.41  ? 115 CYS A HA   1 
ATOM   1961 H HB2  . CYS A 1 115 ? 30.190 3.545  16.374 1.000 13.12  ? 115 CYS A HB2  1 
ATOM   1962 H HB3  . CYS A 1 115 ? 29.670 2.899  17.927 1.000 14.23  ? 115 CYS A HB3  1 
ATOM   1963 N N    . LYS A 1 116 ? 30.931 1.053  15.370 1.000 14.02  ? 116 LYS A N    1 
ATOM   1964 C CA   . LYS A 1 116 ? 30.440 -0.115 14.638 1.000 15.12  ? 116 LYS A CA   1 
ATOM   1965 C C    . LYS A 1 116 ? 31.224 -1.368 14.978 1.000 17.51  ? 116 LYS A C    1 
ATOM   1966 O O    . LYS A 1 116 ? 32.447 -1.372 14.944 1.000 20.13  ? 116 LYS A O    1 
ATOM   1967 C CB   . LYS A 1 116 ? 30.562 0.222  13.146 1.000 15.78  ? 116 LYS A CB   1 
ATOM   1968 C CG   . LYS A 1 116 ? 30.122 -0.882 12.206 1.000 15.41  ? 116 LYS A CG   1 
ATOM   1969 C CD   . LYS A 1 116 ? 30.405 -0.456 10.750 1.000 15.97  ? 116 LYS A CD   1 
ATOM   1970 C CE   . LYS A 1 116 ? 29.923 -1.504 9.786  1.000 19.55  ? 116 LYS A CE   1 
ATOM   1971 N NZ   . LYS A 1 116 ? 30.313 -1.200 8.385  1.000 20.07  ? 116 LYS A NZ   1 
ATOM   1972 H H    . LYS A 1 116 ? 31.161 1.893  14.857 1.000 16.57  ? 116 LYS A H    1 
ATOM   1973 H HA   . LYS A 1 116 ? 29.380 -0.276 14.885 1.000 24.63  ? 116 LYS A HA   1 
ATOM   1974 H HB2  . LYS A 1 116 ? 29.965 1.111  12.941 1.000 15.16  ? 116 LYS A HB2  1 
ATOM   1975 H HB3  . LYS A 1 116 ? 31.602 0.468  12.930 1.000 15.32  ? 116 LYS A HB3  1 
ATOM   1976 H HG2  . LYS A 1 116 ? 30.664 -1.799 12.434 1.000 16.64  ? 116 LYS A HG2  1 
ATOM   1977 H HG3  . LYS A 1 116 ? 29.057 -1.074 12.335 1.000 88.36  ? 116 LYS A HG3  1 
ATOM   1978 H HD2  . LYS A 1 116 ? 29.900 0.488  10.543 1.000 24.62  ? 116 LYS A HD2  1 
ATOM   1979 H HD3  . LYS A 1 116 ? 31.476 -0.303 10.617 1.000 15.48  ? 116 LYS A HD3  1 
ATOM   1980 H HE2  . LYS A 1 116 ? 30.338 -2.471 10.072 1.000 20.63  ? 116 LYS A HE2  1 
ATOM   1981 H HE3  . LYS A 1 116 ? 28.837 -1.575 9.848  1.000 24.35  ? 116 LYS A HE3  1 
ATOM   1982 D DZ1  . LYS A 1 116 ? 31.285 -0.881 8.342  1.000 21.45  ? 116 LYS A DZ1  1 
ATOM   1983 D DZ2  . LYS A 1 116 ? 30.159 -2.032 7.789  1.000 22.51  ? 116 LYS A DZ2  1 
ATOM   1984 D DZ3  . LYS A 1 116 ? 29.725 -0.423 8.021  1.000 20.56  ? 116 LYS A DZ3  1 
ATOM   1985 N N    . GLY A 1 117 ? 30.524 -2.453 15.310 1.000 20.09  ? 117 GLY A N    1 
ATOM   1986 C CA   . GLY A 1 117 ? 31.220 -3.662 15.627 1.000 23.14  ? 117 GLY A CA   1 
ATOM   1987 C C    . GLY A 1 117 ? 31.454 -3.902 17.109 1.000 23.71  ? 117 GLY A C    1 
ATOM   1988 O O    . GLY A 1 117 ? 31.654 -5.034 17.533 1.000 25.73  ? 117 GLY A O    1 
ATOM   1989 D D    . GLY A 1 117 ? 29.510 -2.353 15.340 1.000 19.72  ? 117 GLY A D    1 
ATOM   1990 H HA2  . GLY A 1 117 ? 30.654 -4.503 15.225 1.000 31.55  ? 117 GLY A HA2  1 
ATOM   1991 H HA3  . GLY A 1 117 ? 32.186 -3.647 15.122 1.000 24.28  ? 117 GLY A HA3  1 
ATOM   1992 N N    . THR A 1 118 ? 31.420 -2.829 17.881 1.000 20.78  ? 118 THR A N    1 
ATOM   1993 C CA   . THR A 1 118 ? 31.895 -2.852 19.254 1.000 20.20  ? 118 THR A CA   1 
ATOM   1994 C C    . THR A 1 118 ? 30.710 -3.050 20.192 1.000 20.20  ? 118 THR A C    1 
ATOM   1995 O O    . THR A 1 118 ? 29.554 -3.027 19.766 1.000 19.67  ? 118 THR A O    1 
ATOM   1996 C CB   . THR A 1 118 ? 32.678 -1.598 19.689 1.000 20.53  ? 118 THR A CB   1 
ATOM   1997 O OG1  . THR A 1 118 ? 31.755 -0.525 19.914 1.000 21.01  ? 118 THR A OG1  1 
ATOM   1998 C CG2  . THR A 1 118 ? 33.660 -1.177 18.616 1.000 23.58  ? 118 THR A CG2  1 
ATOM   1999 H H    A THR A 1 118 ? 31.053 -1.967 17.504 0.101 4.60   ? 118 THR A H    1 
ATOM   2000 D D    B THR A 1 118 ? 30.999 -1.989 17.520 0.899 18.87  ? 118 THR A D    1 
ATOM   2001 H HA   . THR A 1 118 ? 32.562 -3.720 19.365 1.000 21.35  ? 118 THR A HA   1 
ATOM   2002 H HB   . THR A 1 118 ? 33.223 -1.812 20.619 1.000 22.59  ? 118 THR A HB   1 
ATOM   2003 D DG1  . THR A 1 118 ? 31.386 -0.240 19.057 1.000 19.37  ? 118 THR A DG1  1 
ATOM   2004 H HG21 . THR A 1 118 ? 33.136 -0.970 17.719 1.000 23.57  ? 118 THR A HG21 1 
ATOM   2005 H HG22 . THR A 1 118 ? 34.177 -0.307 18.932 1.000 32.35  ? 118 THR A HG22 1 
ATOM   2006 H HG23 . THR A 1 118 ? 34.355 -1.959 18.447 1.000 24.41  ? 118 THR A HG23 1 
ATOM   2007 N N    . ASP A 1 119 ? 31.021 -3.261 21.464 1.000 22.94  ? 119 ASP A N    1 
ATOM   2008 C CA   . ASP A 1 119 ? 30.026 -3.316 22.526 1.000 24.28  ? 119 ASP A CA   1 
ATOM   2009 C C    . ASP A 1 119 ? 29.537 -1.949 22.961 1.000 21.35  ? 119 ASP A C    1 
ATOM   2010 O O    . ASP A 1 119 ? 29.957 -1.398 23.979 1.000 21.71  ? 119 ASP A O    1 
ATOM   2011 C CB   . ASP A 1 119 ? 30.642 -4.027 23.731 1.000 29.82  ? 119 ASP A CB   1 
ATOM   2012 C CG   . ASP A 1 119 ? 29.679 -4.234 24.885 1.000 35.22  ? 119 ASP A CG   1 
ATOM   2013 O OD1  . ASP A 1 119 ? 28.505 -3.825 24.753 1.000 37.63  ? 119 ASP A OD1  1 
ATOM   2014 O OD2  . ASP A 1 119 ? 30.092 -4.810 25.915 1.000 35.75  ? 119 ASP A OD2  1 
ATOM   2015 D D    . ASP A 1 119 ? 31.984 -3.410 21.723 1.000 22.93  ? 119 ASP A D    1 
ATOM   2016 H HA   . ASP A 1 119 ? 29.165 -3.903 22.173 1.000 28.58  ? 119 ASP A HA   1 
ATOM   2017 H HB2  . ASP A 1 119 ? 31.017 -4.999 23.410 1.000 45.19  ? 119 ASP A HB2  1 
ATOM   2018 H HB3  . ASP A 1 119 ? 31.493 -3.445 24.084 1.000 52.83  ? 119 ASP A HB3  1 
ATOM   2019 N N    . VAL A 1 120 ? 28.616 -1.405 22.167 1.000 19.80  ? 120 VAL A N    1 
ATOM   2020 C CA   . VAL A 1 120 ? 28.211 -0.037 22.419 1.000 19.03  ? 120 VAL A CA   1 
ATOM   2021 C C    . VAL A 1 120 ? 27.337 0.143  23.658 1.000 17.82  ? 120 VAL A C    1 
ATOM   2022 O O    . VAL A 1 120 ? 27.160 1.258  24.164 1.000 16.76  ? 120 VAL A O    1 
ATOM   2023 C CB   . VAL A 1 120 ? 27.487 0.623  21.232 1.000 15.93  ? 120 VAL A CB   1 
ATOM   2024 C CG1  . VAL A 1 120 ? 28.430 0.781  20.056 1.000 17.81  ? 120 VAL A CG1  1 
ATOM   2025 C CG2  . VAL A 1 120 ? 26.249 -0.163 20.835 1.000 16.72  ? 120 VAL A CG2  1 
ATOM   2026 D D    . VAL A 1 120 ? 28.243 -1.940 21.409 1.000 22.45  ? 120 VAL A D    1 
ATOM   2027 H HA   . VAL A 1 120 ? 29.131 0.541  22.592 1.000 19.49  ? 120 VAL A HA   1 
ATOM   2028 H HB   . VAL A 1 120 ? 27.165 1.627  21.546 1.000 16.07  ? 120 VAL A HB   1 
ATOM   2029 H HG11 . VAL A 1 120 ? 28.755 -0.175 19.734 1.000 22.79  ? 120 VAL A HG11 1 
ATOM   2030 H HG12 . VAL A 1 120 ? 27.926 1.269  19.262 1.000 18.74  ? 120 VAL A HG12 1 
ATOM   2031 H HG13 . VAL A 1 120 ? 29.268 1.358  20.351 1.000 25.08  ? 120 VAL A HG13 1 
ATOM   2032 H HG21 . VAL A 1 120 ? 26.533 -1.137 20.527 1.000 27.13  ? 120 VAL A HG21 1 
ATOM   2033 H HG22 . VAL A 1 120 ? 25.593 -0.232 21.664 1.000 41.15  ? 120 VAL A HG22 1 
ATOM   2034 H HG23 . VAL A 1 120 ? 25.758 0.331  20.036 1.000 18.11  ? 120 VAL A HG23 1 
ATOM   2035 N N    . GLN A 1 121 ? 26.796 -0.937 24.211 1.000 18.84  ? 121 GLN A N    1 
ATOM   2036 C CA   . GLN A 1 121 ? 26.148 -0.898 25.523 1.000 19.54  ? 121 GLN A CA   1 
ATOM   2037 C C    . GLN A 1 121 ? 27.127 -0.506 26.607 1.000 18.78  ? 121 GLN A C    1 
ATOM   2038 O O    . GLN A 1 121 ? 26.694 -0.020 27.665 1.000 17.69  ? 121 GLN A O    1 
ATOM   2039 C CB   . GLN A 1 121 ? 25.515 -2.236 25.870 1.000 24.07  ? 121 GLN A CB   1 
ATOM   2040 C CG   . GLN A 1 121 ? 24.641 -2.258 27.114 1.000 29.63  ? 121 GLN A CG   1 
ATOM   2041 C CD   . GLN A 1 121 ? 24.962 -3.400 28.066 1.000 49.53  ? 121 GLN A CD   1 
ATOM   2042 O OE1  . GLN A 1 121 ? 24.054 -4.162 28.426 1.000 58.62  ? 121 GLN A OE1  1 
ATOM   2043 N NE2  . GLN A 1 121 ? 26.211 -3.560 28.493 1.000 63.12  ? 121 GLN A NE2  1 
ATOM   2044 D D    . GLN A 1 121 ? 26.834 -1.793 23.710 1.000 20.10  ? 121 GLN A D    1 
ATOM   2045 H HA   . GLN A 1 121 ? 25.352 -0.140 25.489 1.000 27.66  ? 121 GLN A HA   1 
ATOM   2046 H HB2  . GLN A 1 121 ? 24.911 -2.558 25.021 1.000 163.03 ? 121 GLN A HB2  1 
ATOM   2047 H HB3  . GLN A 1 121 ? 26.312 -2.968 25.999 1.000 25.77  ? 121 GLN A HB3  1 
ATOM   2048 H HG2  . GLN A 1 121 ? 24.761 -1.313 27.644 1.000 35.55  ? 121 GLN A HG2  1 
ATOM   2049 H HG3  . GLN A 1 121 ? 23.597 -2.336 26.809 1.000 35.55  ? 121 GLN A HG3  1 
ATOM   2050 D DE21 . GLN A 1 121 ? 26.821 -2.760 28.588 1.000 75.74  ? 121 GLN A DE21 1 
ATOM   2051 D DE22 . GLN A 1 121 ? 26.549 -4.488 28.722 1.000 75.74  ? 121 GLN A DE22 1 
ATOM   2052 N N    . ALA A 1 122 ? 28.434 -0.667 26.446 1.000 18.09  ? 122 ALA A N    1 
ATOM   2053 C CA   . ALA A 1 122 ? 29.357 -0.147 27.445 1.000 19.43  ? 122 ALA A CA   1 
ATOM   2054 C C    . ALA A 1 122 ? 29.138 1.334  27.702 1.000 17.19  ? 122 ALA A C    1 
ATOM   2055 O O    . ALA A 1 122 ? 29.348 1.837  28.814 1.000 21.87  ? 122 ALA A O    1 
ATOM   2056 C CB   . ALA A 1 122 ? 30.775 -0.387 26.974 1.000 20.08  ? 122 ALA A CB   1 
ATOM   2057 D D    . ALA A 1 122 ? 28.833 -1.119 25.623 1.000 21.14  ? 122 ALA A D    1 
ATOM   2058 H HA   . ALA A 1 122 ? 29.202 -0.695 28.386 1.000 24.84  ? 122 ALA A HA   1 
ATOM   2059 H HB1  . ALA A 1 122 ? 30.939 0.135  26.067 1.000 167.91 ? 122 ALA A HB1  1 
ATOM   2060 H HB2  . ALA A 1 122 ? 31.455 -0.040 27.710 1.000 131.77 ? 122 ALA A HB2  1 
ATOM   2061 H HB3  . ALA A 1 122 ? 30.925 -1.424 26.817 1.000 25.96  ? 122 ALA A HB3  1 
ATOM   2062 N N    A TRP A 1 123 ? 28.679 2.054  26.675 0.512 15.77  ? 123 TRP A N    1 
ATOM   2063 N N    B TRP A 1 123 ? 28.691 2.086  26.698 0.488 15.88  ? 123 TRP A N    1 
ATOM   2064 C CA   A TRP A 1 123 ? 28.537 3.504  26.755 0.512 16.49  ? 123 TRP A CA   1 
ATOM   2065 C CA   B TRP A 1 123 ? 28.634 3.530  26.925 0.488 16.59  ? 123 TRP A CA   1 
ATOM   2066 C C    A TRP A 1 123 ? 27.382 3.968  27.618 0.512 16.05  ? 123 TRP A C    1 
ATOM   2067 C C    B TRP A 1 123 ? 27.500 3.904  27.859 0.488 15.86  ? 123 TRP A C    1 
ATOM   2068 O O    A TRP A 1 123 ? 27.337 5.145  27.978 0.512 15.49  ? 123 TRP A O    1 
ATOM   2069 O O    B TRP A 1 123 ? 27.581 4.955  28.502 0.488 16.58  ? 123 TRP A O    1 
ATOM   2070 C CB   A TRP A 1 123 ? 28.407 4.109  25.329 0.512 16.97  ? 123 TRP A CB   1 
ATOM   2071 C CB   B TRP A 1 123 ? 28.530 4.302  25.597 0.488 16.79  ? 123 TRP A CB   1 
ATOM   2072 C CG   A TRP A 1 123 ? 29.802 4.039  24.764 0.512 17.57  ? 123 TRP A CG   1 
ATOM   2073 C CG   B TRP A 1 123 ? 29.762 3.987  24.796 0.488 17.81  ? 123 TRP A CG   1 
ATOM   2074 C CD1  A TRP A 1 123 ? 30.296 3.184  23.833 0.512 18.20  ? 123 TRP A CD1  1 
ATOM   2075 C CD1  B TRP A 1 123 ? 29.884 3.093  23.781 0.488 18.13  ? 123 TRP A CD1  1 
ATOM   2076 C CD2  A TRP A 1 123 ? 30.886 4.899  25.146 0.512 17.80  ? 123 TRP A CD2  1 
ATOM   2077 C CD2  B TRP A 1 123 ? 31.055 4.584  24.977 0.488 18.32  ? 123 TRP A CD2  1 
ATOM   2078 N NE1  A TRP A 1 123 ? 31.626 3.456  23.611 0.512 18.83  ? 123 TRP A NE1  1 
ATOM   2079 N NE1  B TRP A 1 123 ? 31.176 3.093  23.317 0.488 19.20  ? 123 TRP A NE1  1 
ATOM   2080 C CE2  A TRP A 1 123 ? 32.010 4.500  24.399 0.512 18.48  ? 123 TRP A CE2  1 
ATOM   2081 C CE2  B TRP A 1 123 ? 31.915 3.994  24.026 0.488 18.72  ? 123 TRP A CE2  1 
ATOM   2082 C CE3  A TRP A 1 123 ? 30.987 5.951  26.051 0.512 18.82  ? 123 TRP A CE3  1 
ATOM   2083 C CE3  B TRP A 1 123 ? 31.525 5.555  25.869 0.488 18.84  ? 123 TRP A CE3  1 
ATOM   2084 C CZ2  A TRP A 1 123 ? 33.240 5.138  24.534 0.512 19.00  ? 123 TRP A CZ2  1 
ATOM   2085 C CZ2  B TRP A 1 123 ? 33.253 4.373  23.953 0.488 18.72  ? 123 TRP A CZ2  1 
ATOM   2086 C CZ3  A TRP A 1 123 ? 32.201 6.589  26.192 0.512 18.91  ? 123 TRP A CZ3  1 
ATOM   2087 C CZ3  B TRP A 1 123 ? 32.858 5.919  25.785 0.488 18.58  ? 123 TRP A CZ3  1 
ATOM   2088 C CH2  A TRP A 1 123 ? 33.298 6.170  25.433 0.512 19.59  ? 123 TRP A CH2  1 
ATOM   2089 C CH2  B TRP A 1 123 ? 33.691 5.320  24.831 0.488 18.77  ? 123 TRP A CH2  1 
ATOM   2090 H H    A TRP A 1 123 ? 28.423 1.582  25.819 0.512 17.43  ? 123 TRP A H    1 
ATOM   2091 H H    B TRP A 1 123 ? 28.405 1.678  25.819 0.488 21.08  ? 123 TRP A H    1 
ATOM   2092 H HA   A TRP A 1 123 ? 29.461 3.902  27.200 0.512 16.30  ? 123 TRP A HA   1 
ATOM   2093 H HA   B TRP A 1 123 ? 29.575 3.828  27.410 0.488 16.80  ? 123 TRP A HA   1 
ATOM   2094 H HB2  A TRP A 1 123 ? 27.712 3.529  24.723 0.512 10.97  ? 123 TRP A HB2  1 
ATOM   2095 H HB2  B TRP A 1 123 ? 27.638 3.995  25.051 0.488 21.15  ? 123 TRP A HB2  1 
ATOM   2096 H HB3  A TRP A 1 123 ? 28.058 5.141  25.376 0.512 16.82  ? 123 TRP A HB3  1 
ATOM   2097 H HB3  B TRP A 1 123 ? 28.468 5.373  25.787 0.488 9.12   ? 123 TRP A HB3  1 
ATOM   2098 H HD1  A TRP A 1 123 ? 29.730 2.407  23.340 0.512 30.02  ? 123 TRP A HD1  1 
ATOM   2099 H HD1  B TRP A 1 123 ? 29.086 2.476  23.396 0.488 27.73  ? 123 TRP A HD1  1 
ATOM   2100 D DE1  A TRP A 1 123 ? 32.224 2.916  23.007 0.512 19.39  ? 123 TRP A DE1  1 
ATOM   2101 D DE1  B TRP A 1 123 ? 31.524 2.473  22.599 0.488 20.70  ? 123 TRP A DE1  1 
ATOM   2102 H HE3  A TRP A 1 123 ? 30.131 6.262  26.632 0.512 18.50  ? 123 TRP A HE3  1 
ATOM   2103 H HE3  B TRP A 1 123 ? 30.868 6.005  26.598 0.488 167.91 ? 123 TRP A HE3  1 
ATOM   2104 H HZ2  A TRP A 1 123 ? 34.103 4.836  23.960 0.512 42.23  ? 123 TRP A HZ2  1 
ATOM   2105 H HZ2  B TRP A 1 123 ? 33.920 3.932  23.226 0.488 22.96  ? 123 TRP A HZ2  1 
ATOM   2106 H HZ3  A TRP A 1 123 ? 32.305 7.410  26.887 0.512 38.58  ? 123 TRP A HZ3  1 
ATOM   2107 H HZ3  B TRP A 1 123 ? 33.256 6.666  26.456 0.488 42.03  ? 123 TRP A HZ3  1 
ATOM   2108 H HH2  A TRP A 1 123 ? 34.238 6.685  25.563 0.512 12.83  ? 123 TRP A HH2  1 
ATOM   2109 H HH2  B TRP A 1 123 ? 34.727 5.622  24.789 0.488 12.96  ? 123 TRP A HH2  1 
ATOM   2110 N N    . ILE A 1 124 ? 26.466 3.075  27.955 1.000 15.37  ? 124 ILE A N    1 
ATOM   2111 C CA   . ILE A 1 124 ? 25.401 3.398  28.902 1.000 17.23  ? 124 ILE A CA   1 
ATOM   2112 C C    . ILE A 1 124 ? 25.386 2.523  30.152 1.000 16.72  ? 124 ILE A C    1 
ATOM   2113 O O    . ILE A 1 124 ? 24.564 2.671  31.043 1.000 16.90  ? 124 ILE A O    1 
ATOM   2114 C CB   . ILE A 1 124 ? 24.033 3.331  28.198 1.000 18.14  ? 124 ILE A CB   1 
ATOM   2115 C CG1  . ILE A 1 124 ? 23.677 1.898  27.786 1.000 20.72  ? 124 ILE A CG1  1 
ATOM   2116 C CG2  . ILE A 1 124 ? 23.968 4.279  27.022 1.000 19.38  ? 124 ILE A CG2  1 
ATOM   2117 C CD1  . ILE A 1 124 ? 22.179 1.770  27.604 1.000 23.31  ? 124 ILE A CD1  1 
ATOM   2118 H H    A ILE A 1 124 ? 26.504 2.151  27.550 1.000 20.43  ? 124 ILE A H    1 
ATOM   2119 H HA   . ILE A 1 124 ? 25.553 4.438  29.228 1.000 14.31  ? 124 ILE A HA   1 
ATOM   2120 H HB   . ILE A 1 124 ? 23.275 3.660  28.925 1.000 17.98  ? 124 ILE A HB   1 
ATOM   2121 H HG12 . ILE A 1 124 ? 24.182 1.649  26.853 1.000 23.43  ? 124 ILE A HG12 1 
ATOM   2122 H HG13 . ILE A 1 124 ? 24.014 1.201  28.553 1.000 24.41  ? 124 ILE A HG13 1 
ATOM   2123 H HG21 . ILE A 1 124 ? 24.687 3.992  26.298 1.000 21.68  ? 124 ILE A HG21 1 
ATOM   2124 H HG22 . ILE A 1 124 ? 23.000 4.242  26.592 1.000 34.15  ? 124 ILE A HG22 1 
ATOM   2125 H HG23 . ILE A 1 124 ? 24.172 5.265  27.351 1.000 22.84  ? 124 ILE A HG23 1 
ATOM   2126 H HD11 . ILE A 1 124 ? 21.854 2.450  26.857 1.000 45.90  ? 124 ILE A HD11 1 
ATOM   2127 H HD12 . ILE A 1 124 ? 21.942 0.781  27.308 1.000 27.20  ? 124 ILE A HD12 1 
ATOM   2128 H HD13 . ILE A 1 124 ? 21.692 1.992  28.519 1.000 35.85  ? 124 ILE A HD13 1 
ATOM   2129 N N    . ARG A 1 125 ? 26.334 1.606  30.238 1.000 18.25  ? 125 ARG A N    1 
ATOM   2130 C CA   . ARG A 1 125 ? 26.361 0.693  31.374 1.000 20.32  ? 125 ARG A CA   1 
ATOM   2131 C C    . ARG A 1 125 ? 26.678 1.446  32.659 1.000 19.71  ? 125 ARG A C    1 
ATOM   2132 O O    . ARG A 1 125 ? 27.595 2.264  32.770 1.000 20.39  ? 125 ARG A O    1 
ATOM   2133 C CB   . ARG A 1 125 ? 27.387 -0.391 31.050 1.000 35.87  ? 125 ARG A CB   1 
ATOM   2134 C CG   . ARG A 1 125 ? 27.476 -1.490 32.096 1.000 60.15  ? 125 ARG A CG   1 
ATOM   2135 C CD   . ARG A 1 125 ? 28.610 -2.436 31.750 1.000 83.22  ? 125 ARG A CD   1 
ATOM   2136 N NE   . ARG A 1 125 ? 28.315 -3.091 30.469 1.000 87.00  ? 125 ARG A NE   1 
ATOM   2137 C CZ   . ARG A 1 125 ? 29.226 -3.301 29.542 1.000 91.94  ? 125 ARG A CZ   1 
ATOM   2138 N NH1  . ARG A 1 125 ? 30.462 -2.911 29.816 1.000 92.87  ? 125 ARG A NH1  1 
ATOM   2139 N NH2  . ARG A 1 125 ? 28.891 -3.862 28.395 1.000 91.73  ? 125 ARG A NH2  1 
ATOM   2140 H H    . ARG A 1 125 ? 27.038 1.538  29.518 1.000 24.39  ? 125 ARG A H    1 
ATOM   2141 H HA   . ARG A 1 125 ? 25.371 0.224  31.474 1.000 28.16  ? 125 ARG A HA   1 
ATOM   2142 H HB2  . ARG A 1 125 ? 27.131 -0.840 30.090 1.000 17.14  ? 125 ARG A HB2  1 
ATOM   2143 H HB3  . ARG A 1 125 ? 28.367 0.074  30.946 1.000 26.40  ? 125 ARG A HB3  1 
ATOM   2144 H HG2  . ARG A 1 125 ? 27.649 -1.050 33.078 1.000 22.74  ? 125 ARG A HG2  1 
ATOM   2145 H HG3  . ARG A 1 125 ? 26.535 -2.041 32.131 1.000 26.52  ? 125 ARG A HG3  1 
ATOM   2146 H HD2  . ARG A 1 125 ? 29.545 -1.881 31.676 1.000 167.91 ? 125 ARG A HD2  1 
ATOM   2147 H HD3  . ARG A 1 125 ? 28.718 -3.186 32.534 1.000 88.51  ? 125 ARG A HD3  1 
ATOM   2148 D DE   . ARG A 1 125 ? 27.339 -3.322 30.383 1.000 88.62  ? 125 ARG A DE   1 
ATOM   2149 D DH11 . ARG A 1 125 ? 31.229 -3.239 29.253 1.000 94.67  ? 125 ARG A DH11 1 
ATOM   2150 D DH12 . ARG A 1 125 ? 30.613 -2.277 30.598 1.000 96.65  ? 125 ARG A DH12 1 
ATOM   2151 D DH21 . ARG A 1 125 ? 29.567 -3.951 27.654 1.000 86.38  ? 125 ARG A DH21 1 
ATOM   2152 D DH22 . ARG A 1 125 ? 27.945 -4.200 28.261 1.000 91.51  ? 125 ARG A DH22 1 
ATOM   2153 N N    . GLY A 1 126 ? 25.886 1.177  33.683 1.000 20.71  ? 126 GLY A N    1 
ATOM   2154 C CA   . GLY A 1 126 ? 26.100 1.791  34.978 1.000 22.07  ? 126 GLY A CA   1 
ATOM   2155 C C    . GLY A 1 126 ? 25.395 3.115  35.159 1.000 23.84  ? 126 GLY A C    1 
ATOM   2156 O O    . GLY A 1 126 ? 25.483 3.740  36.209 1.000 26.92  ? 126 GLY A O    1 
ATOM   2157 D D    . GLY A 1 126 ? 25.121 0.535  33.562 1.000 23.62  ? 126 GLY A D    1 
ATOM   2158 H HA2  . GLY A 1 126 ? 25.757 1.104  35.752 1.000 20.68  ? 126 GLY A HA2  1 
ATOM   2159 H HA3  . GLY A 1 126 ? 27.169 1.943  35.121 1.000 32.31  ? 126 GLY A HA3  1 
ATOM   2160 N N    . CYS A 1 127 ? 24.712 3.591  34.113 1.000 22.20  ? 127 CYS A N    1 
ATOM   2161 C CA   . CYS A 1 127 ? 24.000 4.861  34.172 1.000 21.53  ? 127 CYS A CA   1 
ATOM   2162 C C    . CYS A 1 127 ? 22.559 4.755  34.682 1.000 25.63  ? 127 CYS A C    1 
ATOM   2163 O O    . CYS A 1 127 ? 21.895 3.744  34.437 1.000 29.54  ? 127 CYS A O    1 
ATOM   2164 C CB   . CYS A 1 127 ? 23.989 5.460  32.769 1.000 19.13  ? 127 CYS A CB   1 
ATOM   2165 S SG   . CYS A 1 127 ? 25.609 5.746  32.017 1.000 18.35  ? 127 CYS A SG   1 
ATOM   2166 D D    . CYS A 1 127 ? 24.704 3.060  33.255 1.000 20.17  ? 127 CYS A D    1 
ATOM   2167 H HA   . CYS A 1 127 ? 24.554 5.540  34.836 1.000 19.17  ? 127 CYS A HA   1 
ATOM   2168 H HB2  . CYS A 1 127 ? 23.422 4.796  32.117 1.000 18.57  ? 127 CYS A HB2  1 
ATOM   2169 H HB3  . CYS A 1 127 ? 23.457 6.411  32.807 1.000 21.37  ? 127 CYS A HB3  1 
ATOM   2170 N N    . ARG A 1 128 ? 22.071 5.799  35.349 1.000 26.19  ? 128 ARG A N    1 
ATOM   2171 C CA   . ARG A 1 128 ? 20.659 5.905  35.704 1.000 31.15  ? 128 ARG A CA   1 
ATOM   2172 C C    . ARG A 1 128 ? 19.828 6.314  34.492 1.000 33.33  ? 128 ARG A C    1 
ATOM   2173 O O    . ARG A 1 128 ? 19.945 7.440  34.014 1.000 32.13  ? 128 ARG A O    1 
ATOM   2174 C CB   . ARG A 1 128 ? 20.426 6.912  36.834 1.000 40.12  ? 128 ARG A CB   1 
ATOM   2175 C CG   . ARG A 1 128 ? 20.416 6.294  38.226 1.000 72.85  ? 128 ARG A CG   1 
ATOM   2176 C CD   . ARG A 1 128 ? 21.743 5.634  38.553 1.000 105.26 ? 128 ARG A CD   1 
ATOM   2177 N NE   . ARG A 1 128 ? 21.717 4.853  39.786 1.000 137.37 ? 128 ARG A NE   1 
ATOM   2178 C CZ   . ARG A 1 128 ? 22.080 5.328  40.973 1.000 162.95 ? 128 ARG A CZ   1 
ATOM   2179 N NH1  . ARG A 1 128 ? 22.094 6.641  41.167 1.000 167.91 ? 128 ARG A NH1  1 
ATOM   2180 N NH2  . ARG A 1 128 ? 22.423 4.512  41.958 1.000 167.91 ? 128 ARG A NH2  1 
ATOM   2181 D D    . ARG A 1 128 ? 22.691 6.549  35.623 1.000 24.78  ? 128 ARG A D    1 
ATOM   2182 H HA   . ARG A 1 128 ? 20.313 4.918  36.044 1.000 35.90  ? 128 ARG A HA   1 
ATOM   2183 H HB2  . ARG A 1 128 ? 21.207 7.671  36.794 1.000 48.14  ? 128 ARG A HB2  1 
ATOM   2184 H HB3  . ARG A 1 128 ? 19.471 7.411  36.666 1.000 48.14  ? 128 ARG A HB3  1 
ATOM   2185 H HG2  . ARG A 1 128 ? 20.207 7.069  38.964 1.000 87.42  ? 128 ARG A HG2  1 
ATOM   2186 H HG3  . ARG A 1 128 ? 19.620 5.551  38.285 1.000 87.42  ? 128 ARG A HG3  1 
ATOM   2187 H HD2  . ARG A 1 128 ? 22.025 4.980  37.728 1.000 126.32 ? 128 ARG A HD2  1 
ATOM   2188 H HD3  . ARG A 1 128 ? 22.508 6.406  38.641 1.000 126.32 ? 128 ARG A HD3  1 
ATOM   2189 D DE   . ARG A 1 128 ? 21.392 3.908  39.637 1.000 164.85 ? 128 ARG A DE   1 
ATOM   2190 D DH11 . ARG A 1 128 ? 22.246 7.260  40.384 1.000 201.50 ? 128 ARG A DH11 1 
ATOM   2191 D DH12 . ARG A 1 128 ? 21.948 7.011  42.094 1.000 201.50 ? 128 ARG A DH12 1 
ATOM   2192 D DH21 . ARG A 1 128 ? 21.868 3.690  42.148 1.000 201.50 ? 128 ARG A DH21 1 
ATOM   2193 D DH22 . ARG A 1 128 ? 23.234 4.715  42.523 1.000 201.50 ? 128 ARG A DH22 1 
ATOM   2194 N N    . LEU A 1 129 ? 19.013 5.387  34.003 1.000 36.67  ? 129 LEU A N    1 
ATOM   2195 C CA   . LEU A 1 129 ? 18.126 5.657  32.879 1.000 43.08  ? 129 LEU A CA   1 
ATOM   2196 C C    . LEU A 1 129 ? 16.703 5.181  33.125 1.000 49.96  ? 129 LEU A C    1 
ATOM   2197 O O    . LEU A 1 129 ? 15.843 5.452  32.262 1.000 79.14  ? 129 LEU A O    1 
ATOM   2198 C CB   . LEU A 1 129 ? 18.691 4.988  31.623 1.000 42.31  ? 129 LEU A CB   1 
ATOM   2199 C CG   . LEU A 1 129 ? 20.096 5.440  31.219 1.000 39.63  ? 129 LEU A CG   1 
ATOM   2200 C CD1  . LEU A 1 129 ? 20.614 4.562  30.094 1.000 41.48  ? 129 LEU A CD1  1 
ATOM   2201 C CD2  . LEU A 1 129 ? 20.098 6.904  30.811 1.000 40.23  ? 129 LEU A CD2  1 
ATOM   2202 O OXT  . LEU A 1 129 ? 16.462 4.548  34.173 1.000 54.71  ? 129 LEU A OXT  1 
ATOM   2203 D D    . LEU A 1 129 ? 19.019 4.460  34.415 1.000 44.00  ? 129 LEU A D    1 
ATOM   2204 H HA   . LEU A 1 129 ? 18.103 6.744  32.711 1.000 51.70  ? 129 LEU A HA   1 
ATOM   2205 H HB2  . LEU A 1 129 ? 18.709 3.910  31.785 1.000 50.78  ? 129 LEU A HB2  1 
ATOM   2206 H HB3  . LEU A 1 129 ? 18.013 5.184  30.793 1.000 50.78  ? 129 LEU A HB3  1 
ATOM   2207 H HG   . LEU A 1 129 ? 20.761 5.321  32.087 1.000 47.56  ? 129 LEU A HG   1 
ATOM   2208 H HD11 . LEU A 1 129 ? 19.984 4.664  29.248 1.000 62.21  ? 129 LEU A HD11 1 
ATOM   2209 H HD12 . LEU A 1 129 ? 21.599 4.860  29.840 1.000 62.21  ? 129 LEU A HD12 1 
ATOM   2210 H HD13 . LEU A 1 129 ? 20.621 3.551  30.410 1.000 62.21  ? 129 LEU A HD13 1 
ATOM   2211 H HD21 . LEU A 1 129 ? 19.461 7.039  29.975 1.000 60.35  ? 129 LEU A HD21 1 
ATOM   2212 H HD22 . LEU A 1 129 ? 19.751 7.497  31.619 1.000 60.35  ? 129 LEU A HD22 1 
ATOM   2213 H HD23 . LEU A 1 129 ? 21.084 7.198  30.555 1.000 60.35  ? 129 LEU A HD23 1 
HETATM 2214 N N    . NO3 B 2 .   ? 34.108 9.739  28.770 1.000 23.69  ? 201 NO3 A N    1 
HETATM 2215 O O1   . NO3 B 2 .   ? 34.589 10.867 28.334 1.000 22.83  ? 201 NO3 A O1   1 
HETATM 2216 O O2   . NO3 B 2 .   ? 33.163 9.725  29.688 1.000 29.45  ? 201 NO3 A O2   1 
HETATM 2217 O O3   . NO3 B 2 .   ? 34.559 8.602  28.310 1.000 30.57  ? 201 NO3 A O3   1 
HETATM 2218 N N    . NO3 C 2 .   ? 24.958 1.129  9.415  1.000 31.06  ? 202 NO3 A N    1 
HETATM 2219 O O1   . NO3 C 2 .   ? 24.801 2.335  8.937  1.000 32.17  ? 202 NO3 A O1   1 
HETATM 2220 O O2   . NO3 C 2 .   ? 24.071 0.611  10.232 1.000 28.31  ? 202 NO3 A O2   1 
HETATM 2221 O O3   . NO3 C 2 .   ? 26.008 0.413  9.088  1.000 44.03  ? 202 NO3 A O3   1 
HETATM 2222 N N    . NO3 D 2 .   ? 37.722 12.648 28.525 1.000 45.07  ? 203 NO3 A N    1 
HETATM 2223 O O1   . NO3 D 2 .   ? 38.357 12.869 27.410 1.000 26.51  ? 203 NO3 A O1   1 
HETATM 2224 O O2   . NO3 D 2 .   ? 38.144 13.200 29.638 1.000 38.10  ? 203 NO3 A O2   1 
HETATM 2225 O O3   . NO3 D 2 .   ? 36.664 11.878 28.522 1.000 52.69  ? 203 NO3 A O3   1 
HETATM 2226 N N    . NO3 E 2 .   ? 26.009 30.022 11.538 1.000 15.20  ? 204 NO3 A N    1 
HETATM 2227 O O1   . NO3 E 2 .   ? 26.337 30.978 10.704 1.000 22.39  ? 204 NO3 A O1   1 
HETATM 2228 O O2   . NO3 E 2 .   ? 24.806 29.933 11.987 1.000 17.85  ? 204 NO3 A O2   1 
HETATM 2229 O O3   . NO3 E 2 .   ? 26.970 29.220 11.881 1.000 16.87  ? 204 NO3 A O3   1 
HETATM 2230 N N    . NO3 F 2 .   ? 27.288 15.399 8.842  1.000 22.98  ? 205 NO3 A N    1 
HETATM 2231 O O1   . NO3 F 2 .   ? 26.030 15.680 9.000  1.000 31.87  ? 205 NO3 A O1   1 
HETATM 2232 O O2   . NO3 F 2 .   ? 27.747 15.043 7.673  1.000 32.71  ? 205 NO3 A O2   1 
HETATM 2233 O O3   . NO3 F 2 .   ? 28.092 15.479 9.874  1.000 36.82  ? 205 NO3 A O3   1 
HETATM 2234 N N    . NO3 G 2 .   ? 22.389 0.157  24.245 1.000 26.20  ? 206 NO3 A N    1 
HETATM 2235 O O1   . NO3 G 2 .   ? 21.635 1.215  24.386 1.000 28.42  ? 206 NO3 A O1   1 
HETATM 2236 O O2   . NO3 G 2 .   ? 22.057 -0.922 24.925 1.000 34.02  ? 206 NO3 A O2   1 
HETATM 2237 O O3   . NO3 G 2 .   ? 23.417 0.161  23.463 1.000 24.87  ? 206 NO3 A O3   1 
HETATM 2238 N N    . NO3 H 2 .   ? 18.355 29.029 8.253  1.000 22.69  ? 207 NO3 A N    1 
HETATM 2239 O O1   . NO3 H 2 .   ? 19.608 28.986 7.878  1.000 33.75  ? 207 NO3 A O1   1 
HETATM 2240 O O2   . NO3 H 2 .   ? 17.729 27.919 8.536  1.000 20.89  ? 207 NO3 A O2   1 
HETATM 2241 O O3   . NO3 H 2 .   ? 17.744 30.183 8.336  1.000 35.29  ? 207 NO3 A O3   1 
HETATM 2242 N N    . NO3 I 2 .   ? 19.187 18.795 26.657 1.000 35.03  ? 208 NO3 A N    1 
HETATM 2243 O O1   . NO3 I 2 .   ? 20.414 19.150 26.942 1.000 24.71  ? 208 NO3 A O1   1 
HETATM 2244 O O2   . NO3 I 2 .   ? 18.540 19.358 25.666 1.000 42.22  ? 208 NO3 A O2   1 
HETATM 2245 O O3   . NO3 I 2 .   ? 18.575 17.870 27.362 1.000 38.27  ? 208 NO3 A O3   1 
HETATM 2246 N N    . NO3 J 2 .   ? 37.723 8.152  13.137 1.000 43.84  ? 209 NO3 A N    1 
HETATM 2247 O O1   . NO3 J 2 .   ? 37.407 8.022  14.401 1.000 47.58  ? 209 NO3 A O1   1 
HETATM 2248 O O2   . NO3 J 2 .   ? 37.408 9.252  12.505 1.000 44.22  ? 209 NO3 A O2   1 
HETATM 2249 O O3   . NO3 J 2 .   ? 38.358 7.188  12.508 1.000 29.22  ? 209 NO3 A O3   1 
HETATM 2250 C C    . ACT K 3 .   ? 38.676 18.525 4.844  1.000 44.65  ? 210 ACT A C    1 
HETATM 2251 O O    . ACT K 3 .   ? 38.286 18.734 3.665  1.000 41.61  ? 210 ACT A O    1 
HETATM 2252 O OXT  . ACT K 3 .   ? 39.381 19.266 5.575  1.000 23.84  ? 210 ACT A OXT  1 
HETATM 2253 C CH3  . ACT K 3 .   ? 38.213 17.169 5.446  1.000 47.12  ? 210 ACT A CH3  1 
HETATM 2254 H H1   . ACT K 3 .   ? 37.631 16.645 4.731  1.000 70.68  ? 210 ACT A H1   1 
HETATM 2255 H H2   . ACT K 3 .   ? 39.062 16.588 5.703  1.000 70.68  ? 210 ACT A H2   1 
HETATM 2256 H H3   . ACT K 3 .   ? 37.631 17.347 6.314  1.000 70.68  ? 210 ACT A H3   1 
HETATM 2257 O O    . DOD L 4 .   ? 19.780 30.911 9.114  1.000 33.10  ? 301 DOD A O    1 
HETATM 2258 O O    . DOD L 4 .   ? 23.786 23.476 4.085  1.000 15.42  ? 302 DOD A O    1 
HETATM 2259 D D1   . DOD L 4 .   ? 23.899 23.775 4.982  1.000 15.18  ? 302 DOD A D1   1 
HETATM 2260 D D2   . DOD L 4 .   ? 24.636 23.104 3.885  1.000 18.14  ? 302 DOD A D2   1 
HETATM 2261 O O    . DOD L 4 .   ? 24.458 3.817  38.265 1.000 34.83  ? 303 DOD A O    1 
HETATM 2262 O O    . DOD L 4 .   ? 26.606 -0.429 16.798 1.000 35.84  ? 304 DOD A O    1 
HETATM 2263 O O    . DOD L 4 .   ? 11.567 11.236 24.375 1.000 24.69  ? 305 DOD A O    1 
HETATM 2264 O O    . DOD L 4 .   ? 21.658 9.114  33.974 1.000 34.21  ? 306 DOD A O    1 
HETATM 2265 D D1   . DOD L 4 .   ? 21.235 8.297  33.686 1.000 30.45  ? 306 DOD A D1   1 
HETATM 2266 D D2   . DOD L 4 .   ? 22.060 9.462  33.170 1.000 35.81  ? 306 DOD A D2   1 
HETATM 2267 O O    . DOD L 4 .   ? 31.010 1.323  30.473 1.000 32.19  ? 307 DOD A O    1 
HETATM 2268 O O    . DOD L 4 .   ? 30.512 15.346 9.937  1.000 46.47  ? 308 DOD A O    1 
HETATM 2269 D D1   . DOD L 4 .   ? 31.106 15.953 9.487  1.000 43.60  ? 308 DOD A D1   1 
HETATM 2270 D D2   . DOD L 4 .   ? 30.538 15.551 10.876 1.000 29.85  ? 308 DOD A D2   1 
HETATM 2271 O O    . DOD L 4 .   ? 26.972 12.529 9.551  1.000 26.77  ? 309 DOD A O    1 
HETATM 2272 O O    . DOD L 4 .   ? 17.354 22.185 27.980 1.000 31.64  ? 310 DOD A O    1 
HETATM 2273 O O    . DOD L 4 .   ? 17.524 0.142  22.575 1.000 39.63  ? 311 DOD A O    1 
HETATM 2274 D D1   . DOD L 4 .   ? 17.955 0.985  22.729 1.000 37.20  ? 311 DOD A D1   1 
HETATM 2275 D D2   . DOD L 4 .   ? 17.249 0.151  21.656 1.000 41.37  ? 311 DOD A D2   1 
HETATM 2276 O O    . DOD L 4 .   ? 17.207 2.089  10.179 1.000 22.82  ? 312 DOD A O    1 
HETATM 2277 D D1   . DOD L 4 .   ? 16.703 1.672  9.461  1.000 25.74  ? 312 DOD A D1   1 
HETATM 2278 D D2   . DOD L 4 .   ? 16.745 1.751  10.959 1.000 30.23  ? 312 DOD A D2   1 
HETATM 2279 O O    . DOD L 4 .   ? 19.274 0.892  25.216 1.000 28.21  ? 313 DOD A O    1 
HETATM 2280 O O    . DOD L 4 .   ? 19.032 26.617 22.989 1.000 39.37  ? 314 DOD A O    1 
HETATM 2281 D D1   . DOD L 4 .   ? 18.766 25.803 22.560 1.000 28.09  ? 314 DOD A D1   1 
HETATM 2282 D D2   . DOD L 4 .   ? 19.629 27.086 22.395 1.000 35.75  ? 314 DOD A D2   1 
HETATM 2283 O O    . DOD L 4 .   ? 26.327 20.869 20.243 1.000 14.72  ? 315 DOD A O    1 
HETATM 2284 D D1   . DOD L 4 .   ? 27.074 21.435 20.497 1.000 14.75  ? 315 DOD A D1   1 
HETATM 2285 D D2   . DOD L 4 .   ? 25.923 21.275 19.483 1.000 15.48  ? 315 DOD A D2   1 
HETATM 2286 O O    . DOD L 4 .   ? 21.603 20.537 28.714 1.000 39.23  ? 316 DOD A O    1 
HETATM 2287 D D1   . DOD L 4 .   ? 22.464 20.793 28.377 1.000 28.94  ? 316 DOD A D1   1 
HETATM 2288 D D2   . DOD L 4 .   ? 21.740 19.745 29.240 1.000 37.76  ? 316 DOD A D2   1 
HETATM 2289 O O    . DOD L 4 .   ? 16.429 9.880  30.049 1.000 30.31  ? 317 DOD A O    1 
HETATM 2290 O O    . DOD L 4 .   ? 31.276 -6.059 19.885 1.000 24.63  ? 318 DOD A O    1 
HETATM 2291 O O    . DOD L 4 .   ? 27.764 25.432 23.657 1.000 23.78  ? 319 DOD A O    1 
HETATM 2292 D D1   . DOD L 4 .   ? 27.097 25.494 22.959 1.000 23.89  ? 319 DOD A D1   1 
HETATM 2293 D D2   . DOD L 4 .   ? 27.204 25.386 24.433 1.000 20.43  ? 319 DOD A D2   1 
HETATM 2294 O O    . DOD L 4 .   ? 36.571 15.049 18.399 1.000 34.88  ? 320 DOD A O    1 
HETATM 2295 O O    . DOD L 4 .   ? 21.657 26.879 2.552  1.000 32.07  ? 321 DOD A O    1 
HETATM 2296 D D1   . DOD L 4 .   ? 22.061 27.699 2.861  1.000 32.84  ? 321 DOD A D1   1 
HETATM 2297 D D2   . DOD L 4 .   ? 20.758 27.110 2.311  1.000 37.58  ? 321 DOD A D2   1 
HETATM 2298 O O    . DOD L 4 .   ? 27.104 2.756  38.046 1.000 23.61  ? 322 DOD A O    1 
HETATM 2299 O O    . DOD L 4 .   ? 21.027 -0.906 17.313 1.000 20.58  ? 323 DOD A O    1 
HETATM 2300 D D1   . DOD L 4 .   ? 20.258 -0.801 16.737 1.000 19.53  ? 323 DOD A D1   1 
HETATM 2301 D D2   . DOD L 4 .   ? 20.660 -1.484 18.000 1.000 25.97  ? 323 DOD A D2   1 
HETATM 2302 O O    . DOD L 4 .   ? 23.404 32.156 12.489 1.000 28.31  ? 324 DOD A O    1 
HETATM 2303 D D1   . DOD L 4 .   ? 24.000 31.444 12.275 1.000 25.87  ? 324 DOD A D1   1 
HETATM 2304 D D2   . DOD L 4 .   ? 23.015 31.897 13.326 1.000 30.65  ? 324 DOD A D2   1 
HETATM 2305 O O    . DOD L 4 .   ? 16.421 16.317 27.910 1.000 38.00  ? 325 DOD A O    1 
HETATM 2306 D D1   . DOD L 4 .   ? 17.139 16.917 28.137 1.000 40.74  ? 325 DOD A D1   1 
HETATM 2307 D D2   . DOD L 4 .   ? 15.627 16.690 28.311 1.000 37.48  ? 325 DOD A D2   1 
HETATM 2308 O O    . DOD L 4 .   ? 37.995 24.502 15.572 1.000 33.53  ? 326 DOD A O    1 
HETATM 2309 O O    . DOD L 4 .   ? 40.579 21.403 10.469 1.000 39.47  ? 327 DOD A O    1 
HETATM 2310 D D1   . DOD L 4 .   ? 39.900 21.963 10.073 1.000 26.61  ? 327 DOD A D1   1 
HETATM 2311 D D2   . DOD L 4 .   ? 40.274 20.498 10.342 1.000 35.78  ? 327 DOD A D2   1 
HETATM 2312 O O    . DOD L 4 .   ? 32.165 23.576 25.835 1.000 21.43  ? 328 DOD A O    1 
HETATM 2313 D D1   . DOD L 4 .   ? 32.859 23.482 26.498 1.000 27.14  ? 328 DOD A D1   1 
HETATM 2314 D D2   . DOD L 4 .   ? 32.297 22.790 25.287 1.000 19.12  ? 328 DOD A D2   1 
HETATM 2315 O O    . DOD L 4 .   ? 32.112 26.897 19.437 1.000 29.19  ? 329 DOD A O    1 
HETATM 2316 O O    . DOD L 4 .   ? 13.908 15.778 19.779 1.000 44.68  ? 330 DOD A O    1 
HETATM 2317 D D1   . DOD L 4 .   ? 14.392 16.569 20.023 1.000 45.21  ? 330 DOD A D1   1 
HETATM 2318 D D2   . DOD L 4 .   ? 14.397 15.420 19.034 1.000 45.71  ? 330 DOD A D2   1 
HETATM 2319 O O    . DOD L 4 .   ? 34.319 23.203 -1.898 1.000 34.54  ? 331 DOD A O    1 
HETATM 2320 D D1   . DOD L 4 .   ? 33.494 23.477 -2.301 1.000 30.00  ? 331 DOD A D1   1 
HETATM 2321 D D2   . DOD L 4 .   ? 34.382 23.655 -1.056 1.000 27.71  ? 331 DOD A D2   1 
HETATM 2322 O O    . DOD L 4 .   ? 28.469 10.091 33.613 1.000 18.01  ? 332 DOD A O    1 
HETATM 2323 D D1   . DOD L 4 .   ? 29.410 10.092 33.475 1.000 18.90  ? 332 DOD A D1   1 
HETATM 2324 D D2   . DOD L 4 .   ? 28.220 11.025 33.648 1.000 14.68  ? 332 DOD A D2   1 
HETATM 2325 O O    . DOD L 4 .   ? 19.703 25.424 19.436 1.000 23.81  ? 333 DOD A O    1 
HETATM 2326 D D1   . DOD L 4 .   ? 20.603 25.155 19.249 1.000 19.12  ? 333 DOD A D1   1 
HETATM 2327 D D2   . DOD L 4 .   ? 19.854 25.958 20.234 1.000 29.38  ? 333 DOD A D2   1 
HETATM 2328 O O    . DOD L 4 .   ? 21.166 14.842 31.563 1.000 23.86  ? 334 DOD A O    1 
HETATM 2329 D D1   . DOD L 4 .   ? 21.375 14.145 30.930 1.000 22.87  ? 334 DOD A D1   1 
HETATM 2330 D D2   . DOD L 4 .   ? 20.897 14.311 32.319 1.000 23.59  ? 334 DOD A D2   1 
HETATM 2331 O O    . DOD L 4 .   ? 13.881 24.268 11.558 1.000 34.05  ? 335 DOD A O    1 
HETATM 2332 D D1   . DOD L 4 .   ? 14.408 24.945 11.107 1.000 22.74  ? 335 DOD A D1   1 
HETATM 2333 D D2   . DOD L 4 .   ? 13.498 24.775 12.284 1.000 36.66  ? 335 DOD A D2   1 
HETATM 2334 O O    . DOD L 4 .   ? 24.241 29.758 2.457  1.000 28.82  ? 336 DOD A O    1 
HETATM 2335 O O    . DOD L 4 .   ? 30.700 29.442 11.976 1.000 28.52  ? 337 DOD A O    1 
HETATM 2336 D D1   . DOD L 4 .   ? 30.244 30.283 12.030 1.000 23.63  ? 337 DOD A D1   1 
HETATM 2337 D D2   . DOD L 4 .   ? 30.067 28.920 11.473 1.000 26.56  ? 337 DOD A D2   1 
HETATM 2338 O O    . DOD L 4 .   ? 19.277 23.080 21.091 1.000 26.70  ? 338 DOD A O    1 
HETATM 2339 D D1   . DOD L 4 .   ? 20.116 22.603 21.206 1.000 25.39  ? 338 DOD A D1   1 
HETATM 2340 D D2   . DOD L 4 .   ? 19.530 23.827 20.539 1.000 26.13  ? 338 DOD A D2   1 
HETATM 2341 O O    . DOD L 4 .   ? 32.807 1.321  21.707 1.000 26.07  ? 339 DOD A O    1 
HETATM 2342 D D1   . DOD L 4 .   ? 32.727 1.139  20.771 1.000 30.90  ? 339 DOD A D1   1 
HETATM 2343 D D2   . DOD L 4 .   ? 32.217 0.683  22.145 1.000 29.49  ? 339 DOD A D2   1 
HETATM 2344 O O    . DOD L 4 .   ? 32.059 26.677 6.753  1.000 11.15  ? 340 DOD A O    1 
HETATM 2345 D D1   . DOD L 4 .   ? 31.151 26.790 7.058  1.000 12.35  ? 340 DOD A D1   1 
HETATM 2346 D D2   . DOD L 4 .   ? 31.958 26.460 5.842  1.000 13.04  ? 340 DOD A D2   1 
HETATM 2347 O O    . DOD L 4 .   ? 12.001 15.760 16.988 1.000 35.08  ? 341 DOD A O    1 
HETATM 2348 O O    . DOD L 4 .   ? 39.033 1.835  9.661  1.000 50.35  ? 342 DOD A O    1 
HETATM 2349 D D1   . DOD L 4 .   ? 38.536 2.376  10.280 1.000 45.75  ? 342 DOD A D1   1 
HETATM 2350 D D2   . DOD L 4 .   ? 38.407 1.188  9.331  1.000 48.15  ? 342 DOD A D2   1 
HETATM 2351 O O    . DOD L 4 .   ? 24.057 20.618 21.770 1.000 15.96  ? 343 DOD A O    1 
HETATM 2352 D D1   . DOD L 4 .   ? 24.878 20.601 21.262 1.000 15.01  ? 343 DOD A D1   1 
HETATM 2353 D D2   . DOD L 4 .   ? 24.052 21.505 22.117 1.000 18.30  ? 343 DOD A D2   1 
HETATM 2354 O O    . DOD L 4 .   ? 31.745 18.576 2.825  1.000 32.98  ? 344 DOD A O    1 
HETATM 2355 O O    . DOD L 4 .   ? 17.527 22.285 -0.140 1.000 13.05  ? 345 DOD A O    1 
HETATM 2356 D D1   . DOD L 4 .   ? 18.108 22.402 0.611  1.000 13.97  ? 345 DOD A D1   1 
HETATM 2357 D D2   . DOD L 4 .   ? 18.177 22.128 -0.847 1.000 14.07  ? 345 DOD A D2   1 
HETATM 2358 O O    . DOD L 4 .   ? 22.448 21.359 19.656 1.000 18.19  ? 346 DOD A O    1 
HETATM 2359 D D1   . DOD L 4 .   ? 22.845 21.178 20.505 1.000 21.92  ? 346 DOD A D1   1 
HETATM 2360 D D2   . DOD L 4 .   ? 21.736 21.966 19.812 1.000 23.32  ? 346 DOD A D2   1 
HETATM 2361 O O    . DOD L 4 .   ? 25.978 18.457 16.567 1.000 12.73  ? 347 DOD A O    1 
HETATM 2362 D D1   . DOD L 4 .   ? 26.423 19.082 16.003 1.000 11.75  ? 347 DOD A D1   1 
HETATM 2363 D D2   . DOD L 4 .   ? 25.218 18.954 16.846 1.000 11.28  ? 347 DOD A D2   1 
HETATM 2364 O O    . DOD L 4 .   ? 42.124 18.976 4.190  1.000 15.46  ? 348 DOD A O    1 
HETATM 2365 D D1   . DOD L 4 .   ? 42.271 18.070 3.876  1.000 17.95  ? 348 DOD A D1   1 
HETATM 2366 D D2   . DOD L 4 .   ? 42.656 19.009 4.993  1.000 15.25  ? 348 DOD A D2   1 
HETATM 2367 O O    . DOD L 4 .   ? 13.828 15.924 12.690 1.000 37.31  ? 349 DOD A O    1 
HETATM 2368 D D1   . DOD L 4 .   ? 14.729 15.853 13.022 1.000 28.49  ? 349 DOD A D1   1 
HETATM 2369 D D2   . DOD L 4 .   ? 13.754 16.828 12.377 1.000 38.07  ? 349 DOD A D2   1 
HETATM 2370 O O    . DOD L 4 .   ? 25.939 20.135 -2.171 1.000 24.72  ? 350 DOD A O    1 
HETATM 2371 D D1   . DOD L 4 .   ? 25.391 20.784 -1.726 1.000 21.44  ? 350 DOD A D1   1 
HETATM 2372 D D2   . DOD L 4 .   ? 25.418 19.891 -2.940 1.000 27.05  ? 350 DOD A D2   1 
HETATM 2373 O O    . DOD L 4 .   ? 23.924 7.757  36.288 1.000 24.04  ? 351 DOD A O    1 
HETATM 2374 D D1   . DOD L 4 .   ? 23.404 8.447  35.863 1.000 36.85  ? 351 DOD A D1   1 
HETATM 2375 D D2   . DOD L 4 .   ? 24.797 8.152  36.342 1.000 33.52  ? 351 DOD A D2   1 
HETATM 2376 O O    . DOD L 4 .   ? 12.453 4.682  22.538 1.000 38.63  ? 352 DOD A O    1 
HETATM 2377 O O    . DOD L 4 .   ? 34.672 16.522 12.463 1.000 23.25  ? 353 DOD A O    1 
HETATM 2378 D D1   . DOD L 4 .   ? 34.393 17.017 13.240 1.000 16.32  ? 353 DOD A D1   1 
HETATM 2379 D D2   . DOD L 4 .   ? 34.316 17.006 11.715 1.000 21.68  ? 353 DOD A D2   1 
HETATM 2380 O O    . DOD L 4 .   ? 20.091 18.470 29.719 1.000 24.90  ? 354 DOD A O    1 
HETATM 2381 O O    . DOD L 4 .   ? 24.251 17.502 32.363 1.000 19.27  ? 355 DOD A O    1 
HETATM 2382 D D1   . DOD L 4 .   ? 23.389 17.398 31.957 1.000 21.00  ? 355 DOD A D1   1 
HETATM 2383 D D2   . DOD L 4 .   ? 24.133 17.434 33.318 1.000 20.54  ? 355 DOD A D2   1 
HETATM 2384 O O    . DOD L 4 .   ? 13.982 20.046 7.699  1.000 28.45  ? 356 DOD A O    1 
HETATM 2385 O O    . DOD L 4 .   ? 11.722 9.046  25.054 1.000 32.08  ? 357 DOD A O    1 
HETATM 2386 O O    . DOD L 4 .   ? 34.186 28.554 4.153  1.000 29.79  ? 358 DOD A O    1 
HETATM 2387 O O    . DOD L 4 .   ? 26.133 26.354 5.012  1.000 14.61  ? 359 DOD A O    1 
HETATM 2388 D D1   . DOD L 4 .   ? 25.573 26.607 4.293  1.000 22.96  ? 359 DOD A D1   1 
HETATM 2389 D D2   . DOD L 4 .   ? 26.030 25.418 5.133  1.000 14.05  ? 359 DOD A D2   1 
HETATM 2390 O O    . DOD L 4 .   ? 15.936 19.981 12.005 1.000 24.40  ? 360 DOD A O    1 
HETATM 2391 D D1   . DOD L 4 .   ? 16.259 20.388 12.820 1.000 27.02  ? 360 DOD A D1   1 
HETATM 2392 D D2   . DOD L 4 .   ? 16.041 20.743 11.418 1.000 20.49  ? 360 DOD A D2   1 
HETATM 2393 O O    . DOD L 4 .   ? 28.121 26.042 28.200 1.000 36.52  ? 361 DOD A O    1 
HETATM 2394 D D1   . DOD L 4 .   ? 28.831 26.279 27.595 1.000 29.49  ? 361 DOD A D1   1 
HETATM 2395 D D2   . DOD L 4 .   ? 27.330 25.991 27.657 1.000 29.40  ? 361 DOD A D2   1 
HETATM 2396 O O    . DOD L 4 .   ? 35.999 16.635 26.746 1.000 45.77  ? 362 DOD A O    1 
HETATM 2397 D D1   . DOD L 4 .   ? 35.811 17.072 25.911 1.000 45.41  ? 362 DOD A D1   1 
HETATM 2398 D D2   . DOD L 4 .   ? 35.588 15.770 26.676 1.000 44.70  ? 362 DOD A D2   1 
HETATM 2399 O O    . DOD L 4 .   ? 19.901 25.446 -1.364 1.000 17.88  ? 363 DOD A O    1 
HETATM 2400 D D1   . DOD L 4 .   ? 19.263 24.978 -0.831 1.000 23.63  ? 363 DOD A D1   1 
HETATM 2401 D D2   . DOD L 4 .   ? 20.753 25.090 -1.102 1.000 16.13  ? 363 DOD A D2   1 
HETATM 2402 O O    . DOD L 4 .   ? 20.768 14.484 -0.275 1.000 32.58  ? 364 DOD A O    1 
HETATM 2403 D D1   . DOD L 4 .   ? 21.042 13.696 -0.752 1.000 35.97  ? 364 DOD A D1   1 
HETATM 2404 D D2   . DOD L 4 .   ? 20.678 14.235 0.647  1.000 36.54  ? 364 DOD A D2   1 
HETATM 2405 O O    . DOD L 4 .   ? 37.785 10.235 16.284 1.000 37.63  ? 365 DOD A O    1 
HETATM 2406 D D1   . DOD L 4 .   ? 36.883 10.412 16.554 1.000 39.39  ? 365 DOD A D1   1 
HETATM 2407 D D2   . DOD L 4 .   ? 37.894 9.284  16.349 1.000 33.43  ? 365 DOD A D2   1 
HETATM 2408 O O    . DOD L 4 .   ? 37.136 11.201 21.857 1.000 33.90  ? 366 DOD A O    1 
HETATM 2409 D D1   . DOD L 4 .   ? 36.795 11.740 21.138 1.000 35.69  ? 366 DOD A D1   1 
HETATM 2410 D D2   . DOD L 4 .   ? 36.794 10.322 21.663 1.000 42.15  ? 366 DOD A D2   1 
HETATM 2411 O O    . DOD L 4 .   ? 33.296 14.151 11.364 1.000 26.64  ? 367 DOD A O    1 
HETATM 2412 D D1   . DOD L 4 .   ? 33.760 14.903 11.753 1.000 27.38  ? 367 DOD A D1   1 
HETATM 2413 D D2   . DOD L 4 .   ? 33.903 13.423 11.552 1.000 26.00  ? 367 DOD A D2   1 
HETATM 2414 O O    . DOD L 4 .   ? 27.083 17.544 4.480  1.000 23.70  ? 368 DOD A O    1 
HETATM 2415 D D1   . DOD L 4 .   ? 27.014 17.280 3.558  1.000 32.03  ? 368 DOD A D1   1 
HETATM 2416 D D2   . DOD L 4 .   ? 27.914 18.030 4.522  1.000 19.04  ? 368 DOD A D2   1 
HETATM 2417 O O    . DOD L 4 .   ? 27.232 28.780 21.801 1.000 44.65  ? 369 DOD A O    1 
HETATM 2418 D D1   . DOD L 4 .   ? 27.583 29.022 20.941 1.000 42.64  ? 369 DOD A D1   1 
HETATM 2419 D D2   . DOD L 4 .   ? 26.978 27.855 21.743 1.000 31.66  ? 369 DOD A D2   1 
HETATM 2420 O O    . DOD L 4 .   ? 26.338 28.112 3.097  1.000 24.32  ? 370 DOD A O    1 
HETATM 2421 D D1   . DOD L 4 .   ? 26.840 28.082 2.266  1.000 20.03  ? 370 DOD A D1   1 
HETATM 2422 D D2   . DOD L 4 .   ? 25.653 28.736 2.857  1.000 23.98  ? 370 DOD A D2   1 
HETATM 2423 O O    . DOD L 4 .   ? 12.175 4.233  13.860 1.000 24.54  ? 371 DOD A O    1 
HETATM 2424 D D1   . DOD L 4 .   ? 12.251 3.692  14.653 1.000 23.69  ? 371 DOD A D1   1 
HETATM 2425 D D2   . DOD L 4 .   ? 12.244 5.153  14.161 1.000 25.85  ? 371 DOD A D2   1 
HETATM 2426 O O    . DOD L 4 .   ? 24.864 22.529 32.721 1.000 25.91  ? 372 DOD A O    1 
HETATM 2427 O O    . DOD L 4 .   ? 20.292 12.618 1.776  1.000 39.56  ? 373 DOD A O    1 
HETATM 2428 D D1   . DOD L 4 .   ? 20.246 11.662 1.842  1.000 32.21  ? 373 DOD A D1   1 
HETATM 2429 D D2   . DOD L 4 .   ? 21.160 12.874 2.093  1.000 37.64  ? 373 DOD A D2   1 
HETATM 2430 O O    . DOD L 4 .   ? 38.970 24.004 12.994 1.000 32.76  ? 374 DOD A O    1 
HETATM 2431 D D1   . DOD L 4 .   ? 39.277 23.103 13.121 1.000 29.96  ? 374 DOD A D1   1 
HETATM 2432 D D2   . DOD L 4 .   ? 38.470 24.227 13.783 1.000 31.67  ? 374 DOD A D2   1 
HETATM 2433 O O    . DOD L 4 .   ? 26.369 13.497 5.521  1.000 30.38  ? 375 DOD A O    1 
HETATM 2434 O O    . DOD L 4 .   ? 35.044 0.148  15.976 1.000 27.46  ? 376 DOD A O    1 
HETATM 2435 D D1   . DOD L 4 .   ? 34.213 -0.062 15.544 1.000 28.14  ? 376 DOD A D1   1 
HETATM 2436 D D2   . DOD L 4 .   ? 35.528 0.667  15.328 1.000 24.27  ? 376 DOD A D2   1 
HETATM 2437 O O    . DOD L 4 .   ? 17.224 20.974 14.324 1.000 25.58  ? 377 DOD A O    1 
HETATM 2438 D D1   . DOD L 4 .   ? 17.202 20.601 13.439 1.000 25.98  ? 377 DOD A D1   1 
HETATM 2439 D D2   . DOD L 4 .   ? 17.944 20.496 14.750 1.000 19.71  ? 377 DOD A D2   1 
HETATM 2440 O O    . DOD L 4 .   ? 14.468 7.023  23.916 1.000 21.90  ? 378 DOD A O    1 
HETATM 2441 D D1   . DOD L 4 .   ? 14.515 7.974  24.104 1.000 21.50  ? 378 DOD A D1   1 
HETATM 2442 D D2   . DOD L 4 .   ? 13.771 6.969  23.271 1.000 26.89  ? 378 DOD A D2   1 
HETATM 2443 O O    . DOD L 4 .   ? 26.900 16.530 31.879 1.000 13.06  ? 379 DOD A O    1 
HETATM 2444 D D1   . DOD L 4 .   ? 27.387 17.292 32.199 1.000 13.78  ? 379 DOD A D1   1 
HETATM 2445 D D2   . DOD L 4 .   ? 25.975 16.784 31.964 1.000 12.78  ? 379 DOD A D2   1 
HETATM 2446 O O    . DOD L 4 .   ? 36.320 18.823 22.106 1.000 40.24  ? 380 DOD A O    1 
HETATM 2447 D D1   . DOD L 4 .   ? 35.913 18.108 21.621 1.000 33.40  ? 380 DOD A D1   1 
HETATM 2448 D D2   . DOD L 4 .   ? 36.510 18.526 22.999 1.000 37.05  ? 380 DOD A D2   1 
HETATM 2449 O O    . DOD L 4 .   ? 26.778 -1.858 7.209  1.000 29.81  ? 381 DOD A O    1 
HETATM 2450 O O    . DOD L 4 .   ? 16.541 24.614 3.049  1.000 33.62  ? 382 DOD A O    1 
HETATM 2451 D D1   . DOD L 4 .   ? 17.090 24.137 3.680  1.000 28.81  ? 382 DOD A D1   1 
HETATM 2452 D D2   . DOD L 4 .   ? 16.655 24.130 2.228  1.000 27.05  ? 382 DOD A D2   1 
HETATM 2453 O O    . DOD L 4 .   ? 35.768 25.963 6.662  1.000 27.29  ? 383 DOD A O    1 
HETATM 2454 D D1   . DOD L 4 .   ? 35.071 25.357 6.939  1.000 26.39  ? 383 DOD A D1   1 
HETATM 2455 D D2   . DOD L 4 .   ? 36.432 25.357 6.314  1.000 24.27  ? 383 DOD A D2   1 
HETATM 2456 O O    . DOD L 4 .   ? 36.870 22.663 18.379 1.000 32.83  ? 384 DOD A O    1 
HETATM 2457 D D1   . DOD L 4 .   ? 36.658 21.835 18.821 1.000 35.76  ? 384 DOD A D1   1 
HETATM 2458 D D2   . DOD L 4 .   ? 36.536 23.351 18.957 1.000 31.68  ? 384 DOD A D2   1 
HETATM 2459 O O    . DOD L 4 .   ? 31.644 12.401 9.443  1.000 40.89  ? 385 DOD A O    1 
HETATM 2460 D D1   . DOD L 4 .   ? 30.980 12.005 8.873  1.000 39.58  ? 385 DOD A D1   1 
HETATM 2461 D D2   . DOD L 4 .   ? 31.137 12.732 10.190 1.000 30.14  ? 385 DOD A D2   1 
HETATM 2462 O O    . DOD L 4 .   ? 36.017 13.837 15.015 1.000 46.70  ? 386 DOD A O    1 
HETATM 2463 D D1   . DOD L 4 .   ? 35.639 14.609 15.440 1.000 41.78  ? 386 DOD A D1   1 
HETATM 2464 D D2   . DOD L 4 .   ? 35.956 13.121 15.653 1.000 45.60  ? 386 DOD A D2   1 
HETATM 2465 O O    . DOD L 4 .   ? 11.461 2.383  17.768 1.000 35.93  ? 387 DOD A O    1 
HETATM 2466 D D1   . DOD L 4 .   ? 12.275 2.768  17.421 1.000 27.40  ? 387 DOD A D1   1 
HETATM 2467 D D2   . DOD L 4 .   ? 11.307 2.784  18.627 1.000 36.53  ? 387 DOD A D2   1 
HETATM 2468 O O    . DOD L 4 .   ? 23.358 27.670 24.945 1.000 32.26  ? 388 DOD A O    1 
HETATM 2469 O O    . DOD L 4 .   ? 36.884 17.210 1.206  1.000 27.90  ? 389 DOD A O    1 
HETATM 2470 D D1   . DOD L 4 .   ? 37.575 17.318 1.869  1.000 35.60  ? 389 DOD A D1   1 
HETATM 2471 D D2   . DOD L 4 .   ? 36.058 17.523 1.596  1.000 34.82  ? 389 DOD A D2   1 
HETATM 2472 O O    . DOD L 4 .   ? 25.499 28.196 -0.791 1.000 27.73  ? 390 DOD A O    1 
HETATM 2473 O O    . DOD L 4 .   ? 19.103 4.110  1.856  1.000 38.43  ? 391 DOD A O    1 
HETATM 2474 O O    . DOD L 4 .   ? 31.081 -7.687 15.695 1.000 24.91  ? 392 DOD A O    1 
HETATM 2475 D D1   . DOD L 4 .   ? 31.201 -6.772 15.957 1.000 30.76  ? 392 DOD A D1   1 
HETATM 2476 D D2   . DOD L 4 .   ? 30.509 -7.656 14.929 1.000 33.96  ? 392 DOD A D2   1 
HETATM 2477 O O    . DOD L 4 .   ? 18.334 -1.115 19.617 1.000 40.25  ? 393 DOD A O    1 
HETATM 2478 D D1   . DOD L 4 .   ? 17.556 -0.574 19.462 1.000 38.39  ? 393 DOD A D1   1 
HETATM 2479 D D2   . DOD L 4 .   ? 18.123 -1.630 20.400 1.000 37.77  ? 393 DOD A D2   1 
HETATM 2480 O O    . DOD L 4 .   ? 27.736 15.990 2.213  1.000 42.44  ? 394 DOD A O    1 
HETATM 2481 D D1   . DOD L 4 .   ? 28.451 16.536 1.878  1.000 39.09  ? 394 DOD A D1   1 
HETATM 2482 D D2   . DOD L 4 .   ? 26.975 16.166 1.657  1.000 45.70  ? 394 DOD A D2   1 
HETATM 2483 O O    . DOD L 4 .   ? 22.168 28.319 19.799 1.000 30.96  ? 395 DOD A O    1 
HETATM 2484 O O    . DOD L 4 .   ? 14.610 26.456 3.771  1.000 71.87  ? 396 DOD A O    1 
HETATM 2485 D D1   . DOD L 4 .   ? 14.776 27.294 4.205  1.000 70.44  ? 396 DOD A D1   1 
HETATM 2486 D D2   . DOD L 4 .   ? 15.330 25.885 4.042  1.000 69.42  ? 396 DOD A D2   1 
HETATM 2487 O O    . DOD L 4 .   ? 17.495 25.305 0.758  1.000 40.06  ? 397 DOD A O    1 
HETATM 2488 D D1   . DOD L 4 .   ? 18.243 25.896 0.654  1.000 38.97  ? 397 DOD A D1   1 
HETATM 2489 D D2   . DOD L 4 .   ? 17.495 24.776 -0.042 1.000 40.10  ? 397 DOD A D2   1 
HETATM 2490 O O    . DOD L 4 .   ? 21.830 29.899 17.725 1.000 27.48  ? 398 DOD A O    1 
HETATM 2491 D D1   . DOD L 4 .   ? 21.597 30.611 18.331 1.000 34.04  ? 398 DOD A D1   1 
HETATM 2492 D D2   . DOD L 4 .   ? 21.292 30.046 16.950 1.000 24.27  ? 398 DOD A D2   1 
HETATM 2493 O O    . DOD L 4 .   ? 12.202 14.830 2.769  1.000 56.68  ? 399 DOD A O    1 
HETATM 2494 D D1   . DOD L 4 .   ? 11.378 15.266 2.537  1.000 53.44  ? 399 DOD A D1   1 
HETATM 2495 D D2   . DOD L 4 .   ? 12.033 13.889 2.679  1.000 55.36  ? 399 DOD A D2   1 
HETATM 2496 O O    . DOD L 4 .   ? 23.632 -1.408 33.289 1.000 45.56  ? 400 DOD A O    1 
HETATM 2497 D D1   . DOD L 4 .   ? 23.330 -0.495 33.312 1.000 43.98  ? 400 DOD A D1   1 
HETATM 2498 D D2   . DOD L 4 .   ? 24.004 -1.580 34.156 1.000 42.16  ? 400 DOD A D2   1 
HETATM 2499 O O    . DOD L 4 .   ? 22.370 33.199 4.412  1.000 31.87  ? 401 DOD A O    1 
HETATM 2500 O O    . DOD L 4 .   ? 11.602 -1.120 21.811 1.000 28.59  ? 402 DOD A O    1 
HETATM 2501 O O    . DOD L 4 .   ? 21.915 17.105 31.137 1.000 23.51  ? 403 DOD A O    1 
HETATM 2502 D D1   . DOD L 4 .   ? 21.292 17.592 30.587 1.000 26.05  ? 403 DOD A D1   1 
HETATM 2503 D D2   . DOD L 4 .   ? 21.514 16.237 31.297 1.000 23.72  ? 403 DOD A D2   1 
HETATM 2504 O O    A DOD L 4 .   ? 33.342 -3.067 27.233 0.536 37.37  ? 404 DOD A O    1 
HETATM 2505 O O    B DOD L 4 .   ? 31.401 -5.823 27.103 0.464 28.34  ? 404 DOD A O    1 
HETATM 2506 D D1   A DOD L 4 .   ? 32.783 -3.729 26.820 0.536 31.86  ? 404 DOD A D1   1 
HETATM 2507 D D1   B DOD L 4 .   ? 31.689 -4.909 27.135 0.464 27.02  ? 404 DOD A D1   1 
HETATM 2508 D D2   A DOD L 4 .   ? 34.238 -3.330 27.011 0.536 37.67  ? 404 DOD A D2   1 
HETATM 2509 D D2   B DOD L 4 .   ? 30.505 -5.781 26.755 0.464 28.29  ? 404 DOD A D2   1 
HETATM 2510 O O    . DOD L 4 .   ? 36.826 14.115 12.025 1.000 36.67  ? 405 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 
1    N N    A LYS A 1   ? 0.2116 0.1500 0.1819 0.0034  0.0034  0.0191  1   LYS A N    
2    N N    B LYS A 1   ? 0.1570 0.1570 0.1570 0.0000  0.0000  0.0000  1   LYS A N    
3    C CA   A LYS A 1   ? 0.2028 0.1579 0.1506 0.0029  0.0025  0.0042  1   LYS A CA   
4    C CA   B LYS A 1   ? 0.1602 0.1602 0.1602 0.0000  0.0000  0.0000  1   LYS A CA   
5    C C    A LYS A 1   ? 0.1877 0.1428 0.1174 -0.0145 0.0067  0.0150  1   LYS A C    
6    C C    B LYS A 1   ? 0.1871 0.1606 0.1220 0.0033  -0.0024 0.0057  1   LYS A C    
7    O O    A LYS A 1   ? 0.2068 0.1373 0.1073 -0.0055 0.0146  0.0314  1   LYS A O    
8    O O    B LYS A 1   ? 0.1921 0.1641 0.1153 0.0169  -0.0098 0.0115  1   LYS A O    
9    C CB   A LYS A 1   ? 0.2013 0.1507 0.1592 0.0151  -0.0022 0.0235  1   LYS A CB   
10   C CB   B LYS A 1   ? 0.1673 0.1572 0.1630 -0.0012 -0.0017 0.0160  1   LYS A CB   
11   C CG   A LYS A 1   ? 0.1841 0.1479 0.1503 0.0041  -0.0218 0.0216  1   LYS A CG   
12   C CG   B LYS A 1   ? 0.1700 0.1548 0.1575 -0.0112 -0.0168 0.0144  1   LYS A CG   
13   C CD   A LYS A 1   ? 0.1852 0.1661 0.1577 0.0013  -0.0245 0.0222  1   LYS A CD   
14   C CD   B LYS A 1   ? 0.1811 0.1600 0.1754 -0.0158 -0.0010 0.0161  1   LYS A CD   
15   C CE   A LYS A 1   ? 0.2253 0.1633 0.1803 -0.0071 0.0067  0.0247  1   LYS A CE   
16   C CE   B LYS A 1   ? 0.1954 0.1640 0.1828 -0.0146 0.0013  0.0251  1   LYS A CE   
17   N NZ   A LYS A 1   ? 0.2374 0.1740 0.2020 0.0082  0.0218  0.0269  1   LYS A NZ   
18   N NZ   B LYS A 1   ? 0.1978 0.1675 0.1824 -0.0192 -0.0032 0.0200  1   LYS A NZ   
19   D D1   A LYS A 1   ? 0.2016 0.1499 0.1705 0.0112  -0.0022 0.0343  1   LYS A D1   
20   D D1   B LYS A 1   ? 0.2500 0.2500 0.2500 0.0000  0.0000  0.0000  1   LYS A D1   
21   D D2   A LYS A 1   ? 0.2293 0.1733 0.1873 0.0311  -0.0078 0.0140  1   LYS A D2   
22   D D2   B LYS A 1   ? 0.2500 0.2500 0.2500 0.0000  0.0000  0.0000  1   LYS A D2   
23   D D3   A LYS A 1   ? 0.2084 0.1460 0.1813 0.0036  -0.0039 0.0256  1   LYS A D3   
24   D D3   B LYS A 1   ? 0.2500 0.2500 0.2500 0.0000  0.0000  0.0000  1   LYS A D3   
43   D DZ1  A LYS A 1   ? 0.2665 0.1965 0.2358 0.0018  0.0363  -0.0007 1   LYS A DZ1  
44   D DZ1  B LYS A 1   ? 0.1946 0.1729 0.1909 -0.0243 -0.0123 0.0105  1   LYS A DZ1  
45   D DZ2  A LYS A 1   ? 0.2369 0.1973 0.2261 0.0275  0.0113  0.0284  1   LYS A DZ2  
46   D DZ2  B LYS A 1   ? 0.2075 0.1764 0.1996 -0.0185 -0.0095 0.0076  1   LYS A DZ2  
47   D DZ3  A LYS A 1   ? 0.2368 0.1881 0.2274 0.0272  0.0452  0.0440  1   LYS A DZ3  
48   D DZ3  B LYS A 1   ? 0.1978 0.1715 0.1846 -0.0106 0.0024  0.0279  1   LYS A DZ3  
49   N N    . VAL A 2   ? 0.1684 0.1483 0.1139 -0.0219 -0.0005 0.0073  2   VAL A N    
50   C CA   . VAL A 2   ? 0.1543 0.1447 0.0986 -0.0325 -0.0282 0.0066  2   VAL A CA   
51   C C    . VAL A 2   ? 0.1593 0.1495 0.0965 -0.0339 -0.0195 -0.0007 2   VAL A C    
52   O O    . VAL A 2   ? 0.1726 0.1780 0.0932 -0.0365 -0.0216 0.0023  2   VAL A O    
53   C CB   . VAL A 2   ? 0.1545 0.1437 0.1307 -0.0409 -0.0345 0.0089  2   VAL A CB   
54   C CG1  . VAL A 2   ? 0.1787 0.1550 0.1330 -0.0134 -0.0143 0.0255  2   VAL A CG1  
55   C CG2  . VAL A 2   ? 0.1655 0.1625 0.1853 -0.0509 -0.0218 0.0226  2   VAL A CG2  
56   D D    . VAL A 2   ? 0.1583 0.1682 0.1218 -0.0083 -0.0028 -0.0009 2   VAL A D    
65   N N    . PHE A 3   ? 0.1454 0.1391 0.0989 -0.0263 -0.0187 0.0005  3   PHE A N    
66   C CA   . PHE A 3   ? 0.1329 0.1350 0.1052 -0.0137 -0.0213 0.0071  3   PHE A CA   
67   C C    . PHE A 3   ? 0.1282 0.1300 0.0995 -0.0099 -0.0113 -0.0008 3   PHE A C    
68   O O    . PHE A 3   ? 0.1428 0.1309 0.1201 -0.0074 0.0070  -0.0001 3   PHE A O    
69   C CB   . PHE A 3   ? 0.1421 0.1300 0.1106 -0.0190 -0.0239 0.0005  3   PHE A CB   
70   C CG   . PHE A 3   ? 0.1361 0.1351 0.1177 -0.0250 -0.0236 0.0029  3   PHE A CG   
71   C CD1  . PHE A 3   ? 0.1461 0.1530 0.1164 -0.0116 -0.0200 0.0128  3   PHE A CD1  
72   C CD2  . PHE A 3   ? 0.1494 0.1389 0.1204 -0.0177 -0.0082 0.0012  3   PHE A CD2  
73   C CE1  . PHE A 3   ? 0.1547 0.1706 0.1277 -0.0001 -0.0360 0.0066  3   PHE A CE1  
74   C CE2  . PHE A 3   ? 0.1629 0.1805 0.1427 0.0108  0.0007  -0.0016 3   PHE A CE2  
75   C CZ   . PHE A 3   ? 0.1402 0.1831 0.1493 -0.0014 -0.0378 0.0031  3   PHE A CZ   
85   N N    . GLY A 4   ? 0.1215 0.1301 0.1018 -0.0091 -0.0148 0.0026  4   GLY A N    
86   C CA   . GLY A 4   ? 0.1412 0.1353 0.1156 -0.0210 -0.0437 0.0148  4   GLY A CA   
87   C C    . GLY A 4   ? 0.1405 0.1235 0.1205 -0.0151 -0.0345 0.0123  4   GLY A C    
88   O O    . GLY A 4   ? 0.1357 0.1036 0.1543 -0.0064 -0.0444 -0.0279 4   GLY A O    
92   N N    A ARG A 5   ? 0.1385 0.1281 0.1364 -0.0060 -0.0400 0.0158  5   ARG A N    
93   N N    B ARG A 5   ? 0.1435 0.1270 0.1339 -0.0066 -0.0347 0.0173  5   ARG A N    
94   C CA   A ARG A 5   ? 0.1248 0.1215 0.1276 0.0017  -0.0333 0.0169  5   ARG A CA   
95   C CA   B ARG A 5   ? 0.1252 0.1158 0.1293 0.0058  -0.0352 0.0262  5   ARG A CA   
96   C C    A ARG A 5   ? 0.1297 0.1217 0.1184 -0.0015 -0.0301 0.0127  5   ARG A C    
97   C C    B ARG A 5   ? 0.1287 0.1204 0.1186 0.0030  -0.0287 0.0130  5   ARG A C    
98   O O    A ARG A 5   ? 0.1229 0.1156 0.1113 0.0061  -0.0227 -0.0055 5   ARG A O    
99   O O    B ARG A 5   ? 0.1250 0.1225 0.1105 -0.0089 -0.0187 0.0048  5   ARG A O    
100  C CB   A ARG A 5   ? 0.1371 0.1380 0.1625 0.0200  -0.0434 0.0019  5   ARG A CB   
101  C CB   B ARG A 5   ? 0.1376 0.1311 0.1472 0.0216  -0.0535 0.0110  5   ARG A CB   
102  C CG   A ARG A 5   ? 0.1779 0.1166 0.1806 0.0162  -0.0503 0.0084  5   ARG A CG   
103  C CG   B ARG A 5   ? 0.1647 0.1263 0.1879 0.0077  -0.0452 0.0007  5   ARG A CG   
104  C CD   A ARG A 5   ? 0.2606 0.1372 0.1958 0.0600  -0.0547 0.0003  5   ARG A CD   
105  C CD   B ARG A 5   ? 0.2279 0.1349 0.2042 0.0380  -0.0586 -0.0017 5   ARG A CD   
106  N NE   A ARG A 5   ? 0.3154 0.1414 0.2063 0.0637  -0.0565 0.0151  5   ARG A NE   
107  N NE   B ARG A 5   ? 0.3037 0.1422 0.2027 0.0508  -0.0636 -0.0015 5   ARG A NE   
108  C CZ   A ARG A 5   ? 0.3422 0.1485 0.1970 0.0409  -0.0449 -0.0030 5   ARG A CZ   
109  C CZ   B ARG A 5   ? 0.3464 0.1439 0.1948 0.0423  -0.0437 -0.0057 5   ARG A CZ   
110  N NH1  A ARG A 5   ? 0.3466 0.1352 0.1903 0.0413  -0.0448 0.0014  5   ARG A NH1  
111  N NH1  B ARG A 5   ? 0.3463 0.1334 0.1871 0.0385  -0.0440 0.0067  5   ARG A NH1  
112  N NH2  A ARG A 5   ? 0.3572 0.1664 0.1938 0.0358  -0.0420 -0.0142 5   ARG A NH2  
113  N NH2  B ARG A 5   ? 0.3569 0.1597 0.1833 0.0329  -0.0438 -0.0109 5   ARG A NH2  
114  D D    A ARG A 5   ? 0.1475 0.1494 0.1531 -0.0001 -0.0528 0.0041  5   ARG A D    
115  D D    B ARG A 5   ? 0.1653 0.1479 0.1605 0.0088  -0.0577 -0.0003 5   ARG A D    
130  D DE   A ARG A 5   ? 0.3207 0.1477 0.2083 0.0646  -0.0644 0.0225  5   ARG A DE   
131  D DE   B ARG A 5   ? 0.3199 0.1539 0.2061 0.0425  -0.0663 -0.0067 5   ARG A DE   
132  D DH11 A ARG A 5   ? 0.3616 0.1419 0.1834 0.0319  -0.0447 -0.0018 5   ARG A DH11 
133  D DH11 B ARG A 5   ? 0.3675 0.1326 0.1853 0.0336  -0.0327 -0.0012 5   ARG A DH11 
134  D DH12 A ARG A 5   ? 0.3447 0.1456 0.1880 0.0428  -0.0397 0.0040  5   ARG A DH12 
135  D DH12 B ARG A 5   ? 0.3416 0.1437 0.1881 0.0481  -0.0411 0.0084  5   ARG A DH12 
136  D DH21 A ARG A 5   ? 0.3924 0.1803 0.1995 0.0168  -0.0119 -0.0327 5   ARG A DH21 
137  D DH21 B ARG A 5   ? 0.3712 0.1580 0.1673 0.0301  -0.0357 -0.0213 5   ARG A DH21 
138  D DH22 A ARG A 5   ? 0.3800 0.1977 0.2089 0.0216  -0.0422 -0.0351 5   ARG A DH22 
139  D DH22 B ARG A 5   ? 0.3591 0.2020 0.1707 0.0237  -0.0383 -0.0217 5   ARG A DH22 
140  N N    . CYS A 6   ? 0.1337 0.1167 0.1159 0.0063  -0.0310 0.0080  6   CYS A N    
141  C CA   . CYS A 6   ? 0.1446 0.1103 0.1162 -0.0097 -0.0211 -0.0065 6   CYS A CA   
142  C C    . CYS A 6   ? 0.1374 0.1212 0.1130 -0.0056 -0.0016 0.0060  6   CYS A C    
143  O O    . CYS A 6   ? 0.1375 0.1170 0.1011 -0.0010 0.0027  0.0035  6   CYS A O    
144  C CB   . CYS A 6   ? 0.1776 0.1030 0.1173 -0.0217 -0.0229 -0.0011 6   CYS A CB   
145  S SG   . CYS A 6   ? 0.2815 0.1144 0.1341 0.0218  0.0268  0.0278  6   CYS A SG   
146  D D    . CYS A 6   ? 0.1357 0.1569 0.1135 -0.0037 -0.0239 0.0011  6   CYS A D    
150  N N    . GLU A 7   ? 0.1460 0.1155 0.0951 0.0033  -0.0124 0.0043  7   GLU A N    
151  C CA   . GLU A 7   ? 0.1355 0.1127 0.0994 -0.0077 -0.0164 0.0084  7   GLU A CA   
152  C C    . GLU A 7   ? 0.1198 0.1024 0.1008 -0.0016 -0.0117 0.0072  7   GLU A C    
153  O O    . GLU A 7   ? 0.1252 0.1360 0.1016 0.0132  -0.0103 0.0024  7   GLU A O    
154  C CB   . GLU A 7   ? 0.1606 0.1147 0.0987 -0.0172 -0.0090 0.0008  7   GLU A CB   
155  C CG   . GLU A 7   ? 0.1669 0.1327 0.1039 0.0045  -0.0222 -0.0114 7   GLU A CG   
156  C CD   . GLU A 7   ? 0.1499 0.1348 0.1297 -0.0074 -0.0255 0.0014  7   GLU A CD   
157  O OE1  . GLU A 7   ? 0.1462 0.1249 0.1709 -0.0211 -0.0085 -0.0137 7   GLU A OE1  
158  O OE2  . GLU A 7   ? 0.2084 0.1692 0.1308 0.0252  -0.0301 0.0188  7   GLU A OE2  
159  D D    . GLU A 7   ? 0.1406 0.1126 0.1217 0.0063  -0.0097 0.0010  7   GLU A D    
165  N N    . LEU A 8   ? 0.1140 0.1095 0.1018 0.0037  -0.0192 -0.0070 8   LEU A N    
166  C CA   . LEU A 8   ? 0.1031 0.1199 0.1013 0.0039  -0.0175 0.0095  8   LEU A CA   
167  C C    . LEU A 8   ? 0.1059 0.1305 0.1084 -0.0053 -0.0254 0.0059  8   LEU A C    
168  O O    . LEU A 8   ? 0.0965 0.1717 0.0904 -0.0085 -0.0136 0.0177  8   LEU A O    
169  C CB   . LEU A 8   ? 0.0889 0.1368 0.1067 0.0073  -0.0228 0.0033  8   LEU A CB   
170  C CG   . LEU A 8   ? 0.1023 0.1521 0.1026 -0.0047 -0.0132 -0.0066 8   LEU A CG   
171  C CD1  . LEU A 8   ? 0.1380 0.1452 0.0932 -0.0014 -0.0241 -0.0011 8   LEU A CD1  
172  C CD2  . LEU A 8   ? 0.1192 0.1781 0.1251 -0.0005 0.0103  0.0119  8   LEU A CD2  
184  N N    . ALA A 9   ? 0.1177 0.1260 0.1037 0.0040  -0.0215 -0.0025 9   ALA A N    
185  C CA   . ALA A 9   ? 0.1170 0.1172 0.1172 0.0107  -0.0175 -0.0097 9   ALA A CA   
186  C C    . ALA A 9   ? 0.1178 0.1195 0.1072 0.0074  -0.0166 0.0036  9   ALA A C    
187  O O    . ALA A 9   ? 0.1201 0.1680 0.1168 -0.0068 -0.0216 0.0031  9   ALA A O    
188  C CB   . ALA A 9   ? 0.1491 0.1101 0.1506 0.0212  -0.0256 -0.0161 9   ALA A CB   
194  N N    . ALA A 10  ? 0.1290 0.1375 0.0952 0.0090  -0.0098 0.0115  10  ALA A N    
195  C CA   . ALA A 10  ? 0.1203 0.1464 0.1085 -0.0102 -0.0095 -0.0063 10  ALA A CA   
196  C C    . ALA A 10  ? 0.1075 0.1454 0.1179 0.0079  0.0104  -0.0080 10  ALA A C    
197  O O    . ALA A 10  ? 0.1156 0.1166 0.1373 -0.0027 -0.0003 0.0090  10  ALA A O    
198  C CB   . ALA A 10  ? 0.1471 0.2012 0.1072 -0.0197 0.0038  -0.0216 10  ALA A CB   
204  N N    . ALA A 11  ? 0.1074 0.1384 0.1164 0.0059  -0.0069 -0.0081 11  ALA A N    
205  C CA   . ALA A 11  ? 0.0976 0.1246 0.1267 0.0155  0.0019  -0.0167 11  ALA A CA   
206  C C    . ALA A 11  ? 0.1050 0.1215 0.1229 -0.0034 -0.0092 -0.0001 11  ALA A C    
207  O O    . ALA A 11  ? 0.1126 0.1532 0.1372 0.0248  -0.0130 -0.0321 11  ALA A O    
208  C CB   . ALA A 11  ? 0.1249 0.1208 0.1608 0.0002  -0.0095 -0.0189 11  ALA A CB   
214  N N    . MET A 12  ? 0.1062 0.1421 0.1066 0.0043  -0.0085 -0.0085 12  MET A N    
215  C CA   . MET A 12  ? 0.0958 0.1568 0.1085 0.0124  -0.0256 -0.0013 12  MET A CA   
216  C C    . MET A 12  ? 0.1131 0.1641 0.1140 -0.0008 -0.0162 -0.0272 12  MET A C    
217  O O    . MET A 12  ? 0.1149 0.1605 0.1311 0.0002  -0.0285 -0.0150 12  MET A O    
218  C CB   . MET A 12  ? 0.1251 0.1271 0.0971 -0.0049 -0.0020 0.0051  12  MET A CB   
219  C CG   . MET A 12  ? 0.1068 0.1402 0.0946 -0.0113 -0.0199 0.0105  12  MET A CG   
220  S SD   . MET A 12  ? 0.1495 0.1688 0.1190 0.0050  0.0237  0.0099  12  MET A SD   
221  C CE   . MET A 12  ? 0.1702 0.1736 0.1686 -0.0435 0.0445  0.0013  12  MET A CE   
231  N N    . LYS A 13  ? 0.1061 0.1524 0.1169 -0.0070 -0.0195 -0.0256 13  LYS A N    
232  C CA   . LYS A 13  ? 0.1137 0.1668 0.1478 -0.0166 -0.0305 -0.0159 13  LYS A CA   
233  C C    . LYS A 13  ? 0.1067 0.1660 0.1453 -0.0238 -0.0240 -0.0058 13  LYS A C    
234  O O    . LYS A 13  ? 0.1156 0.1670 0.1625 -0.0164 -0.0375 -0.0156 13  LYS A O    
235  C CB   . LYS A 13  ? 0.1272 0.1803 0.2083 -0.0299 -0.0390 0.0315  13  LYS A CB   
236  C CG   . LYS A 13  ? 0.1994 0.2272 0.2846 -0.0918 -0.0174 0.0329  13  LYS A CG   
237  C CD   . LYS A 13  ? 0.3494 0.2953 0.3485 -0.0890 0.0491  0.1013  13  LYS A CD   
253  N N    . ARG A 14  ? 0.1034 0.1888 0.1419 -0.0217 -0.0171 -0.0250 14  ARG A N    
254  C CA   . ARG A 14  ? 0.1171 0.2033 0.1599 -0.0068 -0.0019 -0.0163 14  ARG A CA   
255  C C    . ARG A 14  ? 0.1279 0.1982 0.1576 0.0044  -0.0055 -0.0222 14  ARG A C    
256  O O    . ARG A 14  ? 0.1492 0.3307 0.1497 0.0620  0.0061  -0.0179 14  ARG A O    
257  C CB   . ARG A 14  ? 0.1294 0.2363 0.1781 0.0129  -0.0172 -0.0469 14  ARG A CB   
258  C CG   . ARG A 14  ? 0.2033 0.3447 0.1699 0.0602  -0.0172 -0.0475 14  ARG A CG   
259  C CD   . ARG A 14  ? 0.3036 0.4004 0.1973 0.0569  0.0141  -0.0958 14  ARG A CD   
260  N NE   . ARG A 14  ? 0.3364 0.4107 0.2664 0.0205  -0.0023 -0.1430 14  ARG A NE   
261  C CZ   . ARG A 14  ? 0.3371 0.4651 0.3040 0.0415  -0.0175 -0.1762 14  ARG A CZ   
262  N NH1  . ARG A 14  ? 0.3406 0.4917 0.3039 0.0783  -0.0329 -0.1627 14  ARG A NH1  
263  N NH2  . ARG A 14  ? 0.3420 0.4829 0.3266 0.0230  -0.0161 -0.2128 14  ARG A NH2  
265  D D    B ARG A 14  ? 0.1143 0.1978 0.1635 -0.0248 -0.0310 -0.0291 14  ARG A D    
273  D DE   . ARG A 14  ? 0.3584 0.4412 0.3673 -0.0111 -0.0094 -0.0720 14  ARG A DE   
274  D DH11 . ARG A 14  ? 0.3344 0.5018 0.3246 0.1206  -0.0387 -0.2009 14  ARG A DH11 
275  D DH12 . ARG A 14  ? 0.3411 0.4835 0.3092 0.0835  -0.0413 -0.1196 14  ARG A DH12 
276  D DH21 . ARG A 14  ? 0.3470 0.4910 0.3424 0.0312  -0.0240 -0.2222 14  ARG A DH21 
277  D DH22 . ARG A 14  ? 0.3280 0.4701 0.3383 -0.0113 -0.0318 -0.2115 14  ARG A DH22 
278  N N    A HIS A 15  ? 0.1110 0.1938 0.1477 -0.0006 -0.0190 -0.0246 15  HIS A N    
279  N N    B HIS A 15  ? 0.1347 0.1788 0.1506 0.0088  -0.0046 -0.0232 15  HIS A N    
280  C CA   A HIS A 15  ? 0.1332 0.1960 0.1512 -0.0003 -0.0210 -0.0199 15  HIS A CA   
281  C CA   B HIS A 15  ? 0.1451 0.1876 0.1570 0.0013  -0.0129 -0.0158 15  HIS A CA   
282  C C    A HIS A 15  ? 0.1499 0.1884 0.1470 0.0122  -0.0271 -0.0166 15  HIS A C    
283  C C    B HIS A 15  ? 0.1566 0.1833 0.1486 0.0133  -0.0226 -0.0115 15  HIS A C    
284  O O    A HIS A 15  ? 0.1486 0.1957 0.1466 0.0008  -0.0338 -0.0143 15  HIS A O    
285  O O    B HIS A 15  ? 0.1950 0.1923 0.1536 -0.0032 -0.0352 -0.0039 15  HIS A O    
286  C CB   A HIS A 15  ? 0.1538 0.2145 0.1628 -0.0187 -0.0137 -0.0129 15  HIS A CB   
287  C CB   B HIS A 15  ? 0.1589 0.2096 0.1637 -0.0088 -0.0015 -0.0094 15  HIS A CB   
288  C CG   A HIS A 15  ? 0.1990 0.1997 0.1718 -0.0262 0.0000  -0.0067 15  HIS A CG   
289  C CG   B HIS A 15  ? 0.1885 0.2005 0.1706 -0.0218 0.0049  -0.0027 15  HIS A CG   
290  N ND1  A HIS A 15  ? 0.2295 0.2217 0.1810 0.0029  -0.0132 -0.0176 15  HIS A ND1  
291  N ND1  B HIS A 15  ? 0.2441 0.2131 0.1687 0.0008  0.0015  0.0022  15  HIS A ND1  
292  C CD2  A HIS A 15  ? 0.2070 0.2081 0.1786 -0.0235 -0.0048 -0.0168 15  HIS A CD2  
293  C CD2  B HIS A 15  ? 0.1851 0.2142 0.1788 -0.0212 -0.0056 -0.0090 15  HIS A CD2  
294  C CE1  A HIS A 15  ? 0.2343 0.2190 0.1845 -0.0015 -0.0059 -0.0163 15  HIS A CE1  
295  C CE1  B HIS A 15  ? 0.2606 0.2076 0.1879 -0.0034 0.0164  -0.0043 15  HIS A CE1  
296  N NE2  A HIS A 15  ? 0.2278 0.2186 0.1878 -0.0106 -0.0062 -0.0228 15  HIS A NE2  
297  N NE2  B HIS A 15  ? 0.2337 0.2156 0.1865 -0.0219 0.0090  -0.0186 15  HIS A NE2  
298  D D    A HIS A 15  ? 0.0907 0.1690 0.1523 -0.0253 -0.0286 -0.0314 15  HIS A D    
299  D D    B HIS A 15  ? 0.1333 0.2140 0.1458 0.0146  0.0043  -0.0128 15  HIS A D    
306  D DD1  A HIS A 15  ? 0.2393 0.2537 0.1899 0.0107  -0.0245 -0.0261 15  HIS A DD1  
307  D DD1  B HIS A 15  ? 0.2970 0.2647 0.1923 0.0270  -0.0354 -0.0063 15  HIS A DD1  
312  D DE2  A HIS A 15  ? 0.2462 0.2268 0.1975 -0.0048 -0.0124 -0.0326 15  HIS A DE2  
313  D DE2  B HIS A 15  ? 0.2938 0.2445 0.2070 -0.0023 -0.0059 -0.0501 15  HIS A DE2  
314  N N    A GLY A 16  ? 0.1536 0.1838 0.1412 0.0207  -0.0241 -0.0181 16  GLY A N    
315  N N    B GLY A 16  ? 0.1392 0.1789 0.1389 0.0188  -0.0291 -0.0180 16  GLY A N    
316  C CA   A GLY A 16  ? 0.1471 0.1761 0.1355 0.0138  -0.0264 -0.0059 16  GLY A CA   
317  C CA   B GLY A 16  ? 0.1304 0.1866 0.1464 0.0116  -0.0341 -0.0189 16  GLY A CA   
318  C C    A GLY A 16  ? 0.1347 0.1653 0.1374 -0.0095 -0.0272 -0.0211 16  GLY A C    
319  C C    B GLY A 16  ? 0.1307 0.1612 0.1404 -0.0095 -0.0289 -0.0201 16  GLY A C    
320  O O    A GLY A 16  ? 0.1616 0.1855 0.1392 0.0090  -0.0404 -0.0265 16  GLY A O    
321  O O    B GLY A 16  ? 0.1269 0.1733 0.1627 -0.0222 -0.0322 -0.0314 16  GLY A O    
322  D D    A GLY A 16  ? 0.1525 0.1741 0.1409 0.0369  -0.0255 -0.0190 16  GLY A D    
323  D D    B GLY A 16  ? 0.1930 0.1697 0.1371 0.0447  -0.0272 -0.0251 16  GLY A D    
328  N N    . LEU A 17  ? 0.1302 0.1410 0.1353 -0.0197 -0.0254 -0.0242 17  LEU A N    
329  C CA   . LEU A 17  ? 0.1295 0.1710 0.1207 -0.0103 -0.0290 -0.0181 17  LEU A CA   
330  C C    . LEU A 17  ? 0.1496 0.1628 0.1309 -0.0093 0.0050  -0.0268 17  LEU A C    
331  O O    . LEU A 17  ? 0.1487 0.1726 0.1662 -0.0423 0.0341  -0.0476 17  LEU A O    
332  C CB   . LEU A 17  ? 0.1174 0.1500 0.1552 0.0102  -0.0358 -0.0001 17  LEU A CB   
333  C CG   . LEU A 17  ? 0.1594 0.1536 0.1758 -0.0040 -0.0325 0.0091  17  LEU A CG   
334  C CD1  . LEU A 17  ? 0.1565 0.1581 0.2077 -0.0060 -0.0311 0.0045  17  LEU A CD1  
335  C CD2  . LEU A 17  ? 0.1840 0.1527 0.1741 -0.0111 -0.0350 0.0219  17  LEU A CD2  
336  D D    . LEU A 17  ? 0.1523 0.1826 0.1440 -0.0156 -0.0328 -0.0430 17  LEU A D    
347  N N    . ASP A 18  ? 0.1598 0.1746 0.1186 -0.0019 -0.0095 -0.0223 18  ASP A N    
348  C CA   . ASP A 18  ? 0.1347 0.1670 0.1343 -0.0154 -0.0064 -0.0199 18  ASP A CA   
349  C C    . ASP A 18  ? 0.1260 0.1745 0.1446 0.0059  -0.0142 -0.0274 18  ASP A C    
350  O O    . ASP A 18  ? 0.1232 0.2101 0.1590 0.0013  -0.0070 -0.0399 18  ASP A O    
351  C CB   . ASP A 18  ? 0.1652 0.1916 0.1405 -0.0341 -0.0115 -0.0049 18  ASP A CB   
352  C CG   . ASP A 18  ? 0.2176 0.2119 0.1785 -0.0136 -0.0177 0.0268  18  ASP A CG   
353  O OD1  . ASP A 18  ? 0.1930 0.1854 0.1686 -0.0165 -0.0334 0.0429  18  ASP A OD1  
354  O OD2  . ASP A 18  ? 0.4093 0.2136 0.3211 0.0120  0.1440  0.0631  18  ASP A OD2  
355  D D    . ASP A 18  ? 0.1730 0.1667 0.1164 -0.0135 -0.0007 -0.0223 18  ASP A D    
359  N N    . ASN A 19  ? 0.1198 0.1242 0.1276 0.0096  -0.0173 0.0040  19  ASN A N    
360  C CA   . ASN A 19  ? 0.1469 0.1398 0.1175 -0.0063 -0.0096 0.0050  19  ASN A CA   
361  C C    . ASN A 19  ? 0.1437 0.1248 0.1278 -0.0140 -0.0254 -0.0030 19  ASN A C    
362  O O    . ASN A 19  ? 0.1819 0.1519 0.1608 -0.0507 -0.0559 0.0229  19  ASN A O    
363  C CB   . ASN A 19  ? 0.1589 0.1634 0.1045 -0.0294 -0.0195 0.0021  19  ASN A CB   
364  C CG   . ASN A 19  ? 0.1649 0.1598 0.1455 -0.0172 -0.0008 -0.0171 19  ASN A CG   
365  O OD1  . ASN A 19  ? 0.1838 0.1780 0.2026 -0.0211 0.0283  -0.0400 19  ASN A OD1  
366  N ND2  . ASN A 19  ? 0.1757 0.1677 0.1873 -0.0358 0.0144  -0.0637 19  ASN A ND2  
367  D D    . ASN A 19  ? 0.1218 0.1353 0.1756 0.0148  -0.0157 -0.0098 19  ASN A D    
371  D DD21 . ASN A 19  ? 0.2411 0.1835 0.2070 -0.0589 0.0137  -0.0731 19  ASN A DD21 
372  D DD22 . ASN A 19  ? 0.1990 0.2080 0.2581 -0.0386 0.0620  -0.0797 19  ASN A DD22 
373  N N    . TYR A 20  ? 0.1210 0.1212 0.1400 -0.0055 -0.0243 -0.0050 20  TYR A N    
374  C CA   . TYR A 20  ? 0.1319 0.1189 0.1324 -0.0118 -0.0220 -0.0079 20  TYR A CA   
375  C C    . TYR A 20  ? 0.1194 0.1171 0.1408 -0.0178 -0.0185 -0.0133 20  TYR A C    
376  O O    . TYR A 20  ? 0.1184 0.1641 0.1217 -0.0289 -0.0178 -0.0085 20  TYR A O    
377  C CB   . TYR A 20  ? 0.1544 0.1252 0.1179 -0.0282 -0.0264 -0.0121 20  TYR A CB   
378  C CG   . TYR A 20  ? 0.1434 0.1251 0.1287 -0.0289 -0.0160 -0.0022 20  TYR A CG   
379  C CD1  . TYR A 20  ? 0.1374 0.1775 0.1873 -0.0230 -0.0235 0.0225  20  TYR A CD1  
380  C CD2  . TYR A 20  ? 0.1992 0.1071 0.1668 -0.0254 0.0292  0.0132  20  TYR A CD2  
381  C CE1  . TYR A 20  ? 0.1789 0.1862 0.1979 -0.0161 -0.0511 0.0196  20  TYR A CE1  
382  C CE2  . TYR A 20  ? 0.2590 0.1194 0.1604 -0.0289 0.0212  0.0172  20  TYR A CE2  
383  C CZ   . TYR A 20  ? 0.2498 0.1652 0.1725 -0.0297 -0.0406 0.0098  20  TYR A CZ   
384  O OH   . TYR A 20  ? 0.3425 0.1491 0.1859 -0.0099 -0.0536 0.0088  20  TYR A OH   
393  D DH   . TYR A 20  ? 0.4014 0.2770 0.1859 0.1034  -0.0243 0.0636  20  TYR A DH   
394  N N    . ARG A 21  ? 0.1239 0.1163 0.1310 0.0052  -0.0383 0.0056  21  ARG A N    
395  C CA   . ARG A 21  ? 0.1607 0.1342 0.1221 -0.0035 -0.0311 0.0067  21  ARG A CA   
396  C C    . ARG A 21  ? 0.1502 0.1215 0.1388 -0.0070 -0.0026 0.0094  21  ARG A C    
397  O O    . ARG A 21  ? 0.1677 0.1610 0.1389 -0.0185 0.0040  -0.0238 21  ARG A O    
398  C CB   . ARG A 21  ? 0.2101 0.1193 0.1360 -0.0228 -0.0279 0.0078  21  ARG A CB   
399  C CG   . ARG A 21  ? 0.2760 0.1687 0.1573 0.0119  -0.0547 0.0390  21  ARG A CG   
400  C CD   . ARG A 21  ? 0.3188 0.2016 0.2109 0.0139  -0.1193 0.0443  21  ARG A CD   
401  N NE   . ARG A 21  ? 0.4176 0.1807 0.2241 -0.0065 -0.1175 0.0188  21  ARG A NE   
402  C CZ   . ARG A 21  ? 0.4888 0.1903 0.2089 0.0062  -0.1158 0.0149  21  ARG A CZ   
403  N NH1  . ARG A 21  ? 0.5474 0.1760 0.2361 -0.0024 -0.0878 0.0223  21  ARG A NH1  
404  N NH2  . ARG A 21  ? 0.6227 0.1950 0.2393 0.0068  -0.0683 -0.0041 21  ARG A NH2  
405  D D    . ARG A 21  ? 0.1252 0.2076 0.1698 0.0069  -0.0375 -0.0271 21  ARG A D    
413  D DE   . ARG A 21  ? 0.3381 0.1909 0.2672 0.0183  -0.1175 0.0420  21  ARG A DE   
414  D DH11 . ARG A 21  ? 0.5425 0.1719 0.2481 -0.0240 -0.0895 0.0368  21  ARG A DH11 
415  D DH12 . ARG A 21  ? 0.5262 0.1606 0.2447 -0.0319 -0.1033 -0.0043 21  ARG A DH12 
416  D DH21 . ARG A 21  ? 0.6539 0.2268 0.2032 -0.0281 -0.0804 -0.0267 21  ARG A DH21 
417  D DH22 . ARG A 21  ? 0.6202 0.1869 0.2738 -0.0297 -0.1084 -0.0357 21  ARG A DH22 
418  N N    . GLY A 22  ? 0.1173 0.1337 0.1468 -0.0257 -0.0145 0.0223  22  GLY A N    
419  C CA   . GLY A 22  ? 0.1418 0.1298 0.1703 -0.0286 -0.0431 0.0223  22  GLY A CA   
420  C C    . GLY A 22  ? 0.1419 0.1346 0.1618 -0.0268 -0.0445 0.0112  22  GLY A C    
421  O O    . GLY A 22  ? 0.1540 0.1296 0.2312 -0.0268 -0.0682 0.0110  22  GLY A O    
422  D D    . GLY A 22  ? 0.0992 0.1770 0.1470 -0.0301 -0.0167 0.0128  22  GLY A D    
425  N N    . TYR A 23  ? 0.1412 0.1292 0.1318 -0.0353 -0.0083 0.0159  23  TYR A N    
426  C CA   . TYR A 23  ? 0.1371 0.1216 0.1413 -0.0279 -0.0141 0.0105  23  TYR A CA   
427  C C    . TYR A 23  ? 0.1314 0.1468 0.1420 -0.0168 -0.0155 0.0094  23  TYR A C    
428  O O    . TYR A 23  ? 0.1109 0.1438 0.1405 -0.0295 -0.0080 0.0136  23  TYR A O    
429  C CB   . TYR A 23  ? 0.1396 0.1152 0.1509 -0.0303 0.0027  -0.0052 23  TYR A CB   
430  C CG   . TYR A 23  ? 0.1484 0.1092 0.1500 -0.0272 0.0029  -0.0020 23  TYR A CG   
431  C CD1  . TYR A 23  ? 0.1704 0.0949 0.1606 -0.0158 0.0227  0.0144  23  TYR A CD1  
432  C CD2  . TYR A 23  ? 0.1248 0.1746 0.1554 -0.0406 -0.0037 0.0047  23  TYR A CD2  
433  C CE1  . TYR A 23  ? 0.1933 0.1103 0.1664 -0.0127 0.0272  0.0057  23  TYR A CE1  
434  C CE2  . TYR A 23  ? 0.1515 0.2004 0.1516 -0.0387 -0.0112 -0.0005 23  TYR A CE2  
435  C CZ   . TYR A 23  ? 0.1886 0.1582 0.1568 -0.0346 0.0140  0.0029  23  TYR A CZ   
436  O OH   . TYR A 23  ? 0.2503 0.1874 0.1616 -0.0181 0.0347  0.0076  23  TYR A OH   
445  D DH   . TYR A 23  ? 0.3182 0.2269 0.2229 0.0255  0.0558  -0.0233 23  TYR A DH   
446  N N    . SER A 24  ? 0.1383 0.1546 0.1402 -0.0157 -0.0208 0.0101  24  SER A N    
447  C CA   . SER A 24  ? 0.1469 0.1475 0.1419 -0.0235 -0.0149 0.0135  24  SER A CA   
448  C C    . SER A 24  ? 0.1107 0.1517 0.1133 -0.0239 -0.0106 0.0257  24  SER A C    
449  O O    . SER A 24  ? 0.1271 0.2176 0.1082 -0.0522 -0.0169 0.0418  24  SER A O    
450  C CB   . SER A 24  ? 0.1913 0.1497 0.1533 -0.0217 -0.0430 0.0130  24  SER A CB   
451  O OG   . SER A 24  ? 0.1861 0.2101 0.1763 0.0135  -0.0595 0.0323  24  SER A OG   
452  D D    . SER A 24  ? 0.1944 0.1699 0.1307 0.0229  -0.0204 0.0261  24  SER A D    
456  D DG   . SER A 24  ? 0.2746 0.2569 0.2531 0.0926  -0.0514 0.0740  24  SER A DG   
457  N N    . LEU A 25  ? 0.1362 0.1304 0.1265 -0.0161 0.0053  0.0251  25  LEU A N    
458  C CA   . LEU A 25  ? 0.1261 0.1322 0.1191 -0.0119 -0.0039 0.0284  25  LEU A CA   
459  C C    . LEU A 25  ? 0.1291 0.1315 0.1375 -0.0069 -0.0003 0.0130  25  LEU A C    
460  O O    . LEU A 25  ? 0.1289 0.1371 0.1921 -0.0145 0.0114  0.0264  25  LEU A O    
461  C CB   . LEU A 25  ? 0.1364 0.1369 0.1211 -0.0028 -0.0005 0.0293  25  LEU A CB   
462  C CG   . LEU A 25  ? 0.1560 0.1534 0.1594 0.0135  0.0033  -0.0017 25  LEU A CG   
463  C CD1  . LEU A 25  ? 0.1526 0.1388 0.1757 0.0049  -0.0126 -0.0026 25  LEU A CD1  
464  C CD2  . LEU A 25  ? 0.1189 0.1654 0.1604 0.0124  0.0005  -0.0084 25  LEU A CD2  
465  D D    . LEU A 25  ? 0.1490 0.1285 0.1318 -0.0164 0.0153  0.0240  25  LEU A D    
476  N N    . GLY A 26  ? 0.1336 0.1356 0.1048 -0.0013 -0.0100 0.0127  26  GLY A N    
477  C CA   . GLY A 26  ? 0.1299 0.1457 0.1286 -0.0129 -0.0261 0.0370  26  GLY A CA   
478  C C    . GLY A 26  ? 0.1117 0.1277 0.1308 -0.0041 -0.0223 0.0260  26  GLY A C    
479  O O    . GLY A 26  ? 0.1136 0.1660 0.1336 -0.0151 -0.0369 0.0410  26  GLY A O    
480  D D    . GLY A 26  ? 0.1216 0.1466 0.1726 -0.0016 -0.0118 0.0293  26  GLY A D    
483  N N    . ASN A 27  ? 0.0987 0.1204 0.1297 -0.0070 -0.0063 -0.0007 27  ASN A N    
484  C CA   . ASN A 27  ? 0.1128 0.1232 0.1263 0.0214  -0.0008 0.0021  27  ASN A CA   
485  C C    . ASN A 27  ? 0.1275 0.1200 0.1172 0.0160  -0.0160 0.0101  27  ASN A C    
486  O O    . ASN A 27  ? 0.1337 0.1138 0.1068 0.0192  -0.0040 -0.0077 27  ASN A O    
487  C CB   . ASN A 27  ? 0.1268 0.1397 0.1276 -0.0127 0.0014  0.0085  27  ASN A CB   
488  C CG   . ASN A 27  ? 0.1279 0.1355 0.1308 -0.0156 -0.0179 0.0145  27  ASN A CG   
489  O OD1  . ASN A 27  ? 0.1733 0.1168 0.2324 -0.0095 0.0528  0.0309  27  ASN A OD1  
490  N ND2  . ASN A 27  ? 0.1694 0.1628 0.1878 -0.0488 0.0292  -0.0206 27  ASN A ND2  
495  D DD21 . ASN A 27  ? 0.2494 0.1683 0.2257 -0.0749 0.0520  -0.0466 27  ASN A DD21 
496  D DD22 . ASN A 27  ? 0.1539 0.2099 0.2001 -0.0453 0.0277  -0.0219 27  ASN A DD22 
497  N N    . TRP A 28  ? 0.1205 0.1140 0.1089 -0.0007 -0.0132 -0.0004 28  TRP A N    
498  C CA   . TRP A 28  ? 0.1210 0.1185 0.1138 0.0085  -0.0170 0.0070  28  TRP A CA   
499  C C    . TRP A 28  ? 0.1130 0.1099 0.1127 -0.0019 -0.0058 0.0083  28  TRP A C    
500  O O    . TRP A 28  ? 0.1350 0.1011 0.1292 -0.0001 -0.0039 0.0166  28  TRP A O    
501  C CB   . TRP A 28  ? 0.1198 0.1027 0.1295 -0.0025 -0.0143 -0.0034 28  TRP A CB   
502  C CG   . TRP A 28  ? 0.1214 0.0984 0.1311 0.0002  -0.0200 0.0041  28  TRP A CG   
503  C CD1  . TRP A 28  ? 0.1459 0.1160 0.1423 -0.0225 -0.0101 -0.0037 28  TRP A CD1  
504  C CD2  . TRP A 28  ? 0.1230 0.1168 0.1356 0.0198  -0.0169 0.0135  28  TRP A CD2  
505  N NE1  . TRP A 28  ? 0.1382 0.1577 0.1690 -0.0252 -0.0262 -0.0169 28  TRP A NE1  
506  C CE2  . TRP A 28  ? 0.1428 0.1610 0.1513 0.0168  -0.0418 -0.0039 28  TRP A CE2  
507  C CE3  . TRP A 28  ? 0.2049 0.1462 0.1492 0.0105  0.0278  0.0247  28  TRP A CE3  
508  C CZ2  . TRP A 28  ? 0.2103 0.2078 0.1622 0.0572  -0.0697 -0.0166 28  TRP A CZ2  
509  C CZ3  . TRP A 28  ? 0.2792 0.1818 0.1673 0.0584  0.0083  0.0532  28  TRP A CZ3  
510  C CH2  . TRP A 28  ? 0.2976 0.2280 0.1559 0.0773  -0.0351 0.0184  28  TRP A CH2  
521  N N    . VAL A 29  ? 0.1096 0.1138 0.1132 0.0018  -0.0086 0.0167  29  VAL A N    
522  C CA   . VAL A 29  ? 0.1191 0.1118 0.1083 -0.0038 -0.0020 0.0125  29  VAL A CA   
523  C C    . VAL A 29  ? 0.1163 0.1068 0.1259 -0.0042 -0.0057 0.0021  29  VAL A C    
524  O O    . VAL A 29  ? 0.1087 0.1133 0.1346 -0.0046 -0.0069 -0.0041 29  VAL A O    
525  C CB   . VAL A 29  ? 0.1260 0.1394 0.1099 -0.0204 -0.0147 0.0228  29  VAL A CB   
526  C CG1  . VAL A 29  ? 0.1481 0.1534 0.1129 -0.0113 -0.0231 -0.0045 29  VAL A CG1  
527  C CG2  . VAL A 29  ? 0.1403 0.1995 0.0948 0.0108  -0.0070 0.0437  29  VAL A CG2  
537  N N    . CYS A 30  ? 0.1184 0.1048 0.1196 0.0000  -0.0056 0.0059  30  CYS A N    
538  C CA   . CYS A 30  ? 0.1196 0.1111 0.1270 0.0004  -0.0012 0.0109  30  CYS A CA   
539  C C    . CYS A 30  ? 0.1259 0.1142 0.1214 0.0094  0.0021  0.0090  30  CYS A C    
540  O O    . CYS A 30  ? 0.1178 0.1373 0.0941 0.0189  -0.0024 0.0372  30  CYS A O    
541  C CB   . CYS A 30  ? 0.1004 0.1102 0.1750 0.0098  0.0096  0.0076  30  CYS A CB   
542  S SG   . CYS A 30  ? 0.0875 0.1021 0.1672 0.0128  0.0016  0.0413  30  CYS A SG   
547  N N    . ALA A 31  ? 0.1273 0.1007 0.1179 -0.0155 -0.0101 0.0001  31  ALA A N    
548  C CA   . ALA A 31  ? 0.1192 0.1068 0.1246 0.0051  -0.0003 0.0109  31  ALA A CA   
549  C C    . ALA A 31  ? 0.1210 0.1074 0.1117 -0.0017 -0.0118 0.0153  31  ALA A C    
550  O O    . ALA A 31  ? 0.1270 0.1249 0.1194 -0.0077 0.0040  0.0002  31  ALA A O    
551  C CB   . ALA A 31  ? 0.1288 0.1007 0.1277 -0.0031 -0.0125 -0.0033 31  ALA A CB   
557  N N    . ALA A 32  ? 0.1181 0.1097 0.1120 -0.0016 -0.0081 0.0139  32  ALA A N    
558  C CA   . ALA A 32  ? 0.1049 0.1024 0.1202 -0.0088 -0.0002 0.0204  32  ALA A CA   
559  C C    . ALA A 32  ? 0.1096 0.1115 0.1292 -0.0050 -0.0052 0.0087  32  ALA A C    
560  O O    . ALA A 32  ? 0.1026 0.1098 0.1390 -0.0024 0.0016  0.0033  32  ALA A O    
561  C CB   . ALA A 32  ? 0.1126 0.1180 0.1109 0.0200  -0.0168 0.0100  32  ALA A CB   
567  N N    . LYS A 33  ? 0.1002 0.1114 0.1294 -0.0043 -0.0051 0.0098  33  LYS A N    
568  C CA   . LYS A 33  ? 0.0997 0.1098 0.1321 -0.0079 -0.0095 0.0028  33  LYS A CA   
569  C C    . LYS A 33  ? 0.1061 0.1099 0.1485 0.0030  0.0053  0.0033  33  LYS A C    
570  O O    . LYS A 33  ? 0.0800 0.1162 0.1580 0.0162  0.0053  -0.0022 33  LYS A O    
571  C CB   . LYS A 33  ? 0.1328 0.1156 0.1311 0.0107  0.0021  0.0096  33  LYS A CB   
572  C CG   . LYS A 33  ? 0.1430 0.1488 0.1509 0.0060  -0.0046 0.0541  33  LYS A CG   
573  C CD   . LYS A 33  ? 0.1785 0.1728 0.1838 0.0385  -0.0592 0.0363  33  LYS A CD   
574  C CE   . LYS A 33  ? 0.1939 0.2482 0.2607 0.0622  -0.0894 0.0025  33  LYS A CE   
575  N NZ   . LYS A 33  ? 0.2088 0.2964 0.2843 0.0450  -0.1050 -0.0187 33  LYS A NZ   
586  D DZ1  . LYS A 33  ? 0.2297 0.2792 0.3093 0.0474  -0.0989 -0.0338 33  LYS A DZ1  
587  D DZ2  . LYS A 33  ? 0.2355 0.3167 0.2930 0.0267  -0.0883 -0.0477 33  LYS A DZ2  
588  D DZ3  . LYS A 33  ? 0.2156 0.3164 0.3158 0.0544  -0.1151 -0.0245 33  LYS A DZ3  
589  N N    . PHE A 34  ? 0.1176 0.1062 0.1392 0.0113  -0.0048 0.0119  34  PHE A N    
590  C CA   . PHE A 34  ? 0.1082 0.1325 0.1345 0.0143  -0.0076 0.0080  34  PHE A CA   
591  C C    . PHE A 34  ? 0.1149 0.1208 0.1426 0.0059  -0.0031 0.0077  34  PHE A C    
592  O O    . PHE A 34  ? 0.1090 0.1835 0.2017 0.0375  0.0148  0.0659  34  PHE A O    
593  C CB   . PHE A 34  ? 0.1147 0.1317 0.1455 0.0338  -0.0071 0.0158  34  PHE A CB   
594  C CG   . PHE A 34  ? 0.1189 0.1512 0.1758 0.0415  -0.0042 0.0372  34  PHE A CG   
595  C CD1  . PHE A 34  ? 0.1293 0.1377 0.1981 0.0510  -0.0216 0.0400  34  PHE A CD1  
596  C CD2  . PHE A 34  ? 0.1317 0.1655 0.1754 0.0368  -0.0124 0.0530  34  PHE A CD2  
597  C CE1  . PHE A 34  ? 0.1469 0.1858 0.2016 0.0746  -0.0119 0.0619  34  PHE A CE1  
598  C CE2  . PHE A 34  ? 0.1673 0.1958 0.1986 0.0518  -0.0115 0.0776  34  PHE A CE2  
599  C CZ   . PHE A 34  ? 0.1724 0.1795 0.2158 0.0706  -0.0251 0.0781  34  PHE A CZ   
609  N N    . GLU A 35  ? 0.1045 0.1327 0.1205 0.0026  0.0036  0.0166  35  GLU A N    
610  C CA   . GLU A 35  ? 0.1144 0.1335 0.1117 0.0060  -0.0014 0.0088  35  GLU A CA   
611  C C    . GLU A 35  ? 0.0897 0.1271 0.1176 0.0017  -0.0016 0.0189  35  GLU A C    
612  O O    . GLU A 35  ? 0.1018 0.1595 0.1424 -0.0125 0.0037  0.0378  35  GLU A O    
613  C CB   . GLU A 35  ? 0.1068 0.1048 0.1182 -0.0022 0.0008  0.0060  35  GLU A CB   
614  C CG   . GLU A 35  ? 0.1470 0.1142 0.1160 -0.0016 -0.0171 0.0066  35  GLU A CG   
615  C CD   . GLU A 35  ? 0.1447 0.1289 0.1187 0.0118  -0.0183 0.0016  35  GLU A CD   
616  O OE1  . GLU A 35  ? 0.1935 0.1558 0.1378 0.0084  0.0058  -0.0209 35  GLU A OE1  
617  O OE2  . GLU A 35  ? 0.2131 0.1493 0.1316 -0.0124 0.0181  0.0195  35  GLU A OE2  
618  D D    . GLU A 35  ? 0.1222 0.1731 0.1475 -0.0239 0.0141  0.0127  35  GLU A D    
624  D DE2  . GLU A 35  ? 0.2705 0.1981 0.1478 -0.0326 0.0497  -0.0003 35  GLU A DE2  
625  N N    . SER A 36  ? 0.1129 0.1212 0.1260 0.0033  0.0105  0.0017  36  SER A N    
626  C CA   . SER A 36  ? 0.1214 0.1298 0.1448 -0.0020 -0.0144 -0.0080 36  SER A CA   
627  C C    . SER A 36  ? 0.1022 0.1294 0.1480 -0.0024 -0.0124 -0.0043 36  SER A C    
628  O O    . SER A 36  ? 0.1010 0.1263 0.1541 -0.0095 -0.0396 0.0018  36  SER A O    
629  C CB   . SER A 36  ? 0.1452 0.0983 0.1204 0.0105  -0.0085 0.0201  36  SER A CB   
630  O OG   . SER A 36  ? 0.1224 0.0937 0.1063 0.0011  -0.0268 0.0094  36  SER A OG   
632  D D    B SER A 36  ? 0.0691 0.1278 0.1034 0.0046  -0.0164 0.0042  36  SER A D    
636  D DG   . SER A 36  ? 0.1228 0.1512 0.1264 -0.0057 -0.0289 -0.0145 36  SER A DG   
637  N N    A ASN A 37  ? 0.1141 0.1274 0.1506 0.0018  -0.0124 -0.0082 37  ASN A N    
638  N N    B ASN A 37  ? 0.1284 0.1294 0.1491 0.0096  -0.0127 -0.0075 37  ASN A N    
639  C CA   A ASN A 37  ? 0.1369 0.1372 0.1615 0.0277  -0.0385 -0.0076 37  ASN A CA   
640  C CA   B ASN A 37  ? 0.1371 0.1337 0.1623 0.0214  -0.0339 -0.0046 37  ASN A CA   
641  C C    A ASN A 37  ? 0.1373 0.1293 0.1319 0.0094  -0.0388 -0.0041 37  ASN A C    
642  C C    B ASN A 37  ? 0.1382 0.1271 0.1289 0.0119  -0.0410 0.0053  37  ASN A C    
643  O O    A ASN A 37  ? 0.1844 0.1422 0.1344 0.0137  -0.0537 -0.0099 37  ASN A O    
644  O O    B ASN A 37  ? 0.1673 0.1021 0.1222 0.0062  -0.0477 0.0217  37  ASN A O    
645  C CB   A ASN A 37  ? 0.1346 0.1471 0.2027 0.0315  -0.0486 0.0038  37  ASN A CB   
646  C CB   B ASN A 37  ? 0.1313 0.1522 0.1968 0.0215  -0.0412 0.0024  37  ASN A CB   
647  C CG   A ASN A 37  ? 0.1476 0.1751 0.2166 0.0474  -0.0557 0.0189  37  ASN A CG   
648  C CG   B ASN A 37  ? 0.1579 0.1720 0.2220 0.0327  -0.0578 0.0125  37  ASN A CG   
649  O OD1  A ASN A 37  ? 0.1459 0.1769 0.2425 0.0517  -0.0662 0.0404  37  ASN A OD1  
650  O OD1  B ASN A 37  ? 0.1695 0.1685 0.2413 0.0356  -0.0554 0.0177  37  ASN A OD1  
651  N ND2  A ASN A 37  ? 0.1838 0.1883 0.2208 0.0421  -0.0705 0.0088  37  ASN A ND2  
652  N ND2  B ASN A 37  ? 0.1541 0.1753 0.2233 0.0372  -0.0626 0.0217  37  ASN A ND2  
653  D D    A ASN A 37  ? 0.1809 0.1392 0.1669 0.0232  -0.0276 -0.0203 37  ASN A D    
654  D D    B ASN A 37  ? 0.1466 0.1315 0.1525 0.0115  -0.0092 -0.0097 37  ASN A D    
661  D DD21 A ASN A 37  ? 0.1899 0.2085 0.2309 0.0482  -0.0786 0.0178  37  ASN A DD21 
662  D DD21 B ASN A 37  ? 0.1965 0.2088 0.2333 0.0567  -0.0862 0.0169  37  ASN A DD21 
663  D DD22 A ASN A 37  ? 0.2044 0.1884 0.2296 0.0318  -0.0766 0.0030  37  ASN A DD22 
664  D DD22 B ASN A 37  ? 0.1948 0.1697 0.2380 0.0137  -0.0535 0.0052  37  ASN A DD22 
665  N N    . PHE A 38  ? 0.1334 0.1276 0.1071 0.0143  -0.0284 0.0237  38  PHE A N    
666  C CA   . PHE A 38  ? 0.1363 0.1355 0.0815 -0.0025 -0.0325 0.0090  38  PHE A CA   
667  C C    . PHE A 38  ? 0.1187 0.1348 0.1243 0.0147  -0.0228 0.0208  38  PHE A C    
668  O O    . PHE A 38  ? 0.1819 0.1255 0.1505 0.0157  0.0219  0.0289  38  PHE A O    
669  C CB   . PHE A 38  ? 0.2138 0.1197 0.0752 0.0271  -0.0259 -0.0023 38  PHE A CB   
670  C CG   . PHE A 38  ? 0.1698 0.1184 0.0979 0.0208  -0.0161 0.0039  38  PHE A CG   
671  C CD1  . PHE A 38  ? 0.1637 0.1215 0.1083 0.0182  -0.0169 0.0025  38  PHE A CD1  
672  C CD2  . PHE A 38  ? 0.1829 0.1219 0.1130 0.0056  -0.0302 0.0135  38  PHE A CD2  
673  C CE1  . PHE A 38  ? 0.1423 0.1251 0.1442 0.0056  -0.0051 -0.0013 38  PHE A CE1  
674  C CE2  . PHE A 38  ? 0.1833 0.1199 0.1480 0.0117  -0.0175 0.0237  38  PHE A CE2  
675  C CZ   . PHE A 38  ? 0.1612 0.1063 0.1511 0.0007  0.0067  0.0181  38  PHE A CZ   
685  N N    A ASN A 39  ? 0.1282 0.1203 0.1276 0.0324  -0.0090 0.0192  39  ASN A N    
686  N N    B ASN A 39  ? 0.1232 0.1239 0.1261 0.0230  -0.0139 0.0166  39  ASN A N    
687  C CA   A ASN A 39  ? 0.1345 0.1241 0.1206 0.0165  -0.0213 0.0092  39  ASN A CA   
688  C CA   B ASN A 39  ? 0.1335 0.1249 0.1282 0.0151  -0.0140 0.0094  39  ASN A CA   
689  C C    A ASN A 39  ? 0.1192 0.0961 0.1085 -0.0021 -0.0124 0.0156  39  ASN A C    
690  C C    B ASN A 39  ? 0.1234 0.0970 0.1231 -0.0007 -0.0075 0.0160  39  ASN A C    
691  O O    A ASN A 39  ? 0.1077 0.0862 0.1106 -0.0153 -0.0001 0.0183  39  ASN A O    
692  O O    B ASN A 39  ? 0.1476 0.0941 0.1309 0.0373  -0.0170 0.0032  39  ASN A O    
693  C CB   A ASN A 39  ? 0.1299 0.1445 0.1553 0.0131  -0.0219 0.0119  39  ASN A CB   
694  C CB   B ASN A 39  ? 0.1323 0.1420 0.1561 0.0042  -0.0197 0.0058  39  ASN A CB   
695  C CG   A ASN A 39  ? 0.1582 0.1517 0.1871 -0.0109 -0.0187 -0.0062 39  ASN A CG   
696  C CG   B ASN A 39  ? 0.1597 0.1470 0.1884 -0.0071 -0.0085 -0.0065 39  ASN A CG   
697  O OD1  A ASN A 39  ? 0.1453 0.1386 0.1678 -0.0189 -0.0352 -0.0089 39  ASN A OD1  
698  O OD1  B ASN A 39  ? 0.1631 0.1323 0.1665 -0.0098 0.0014  0.0146  39  ASN A OD1  
699  N ND2  A ASN A 39  ? 0.1681 0.1577 0.2328 -0.0216 0.0034  -0.0184 39  ASN A ND2  
700  N ND2  B ASN A 39  ? 0.1623 0.1577 0.2291 -0.0119 -0.0091 -0.0269 39  ASN A ND2  
709  D DD21 A ASN A 39  ? 0.2081 0.1688 0.2910 -0.0490 0.0266  -0.0456 39  ASN A DD21 
710  D DD21 B ASN A 39  ? 0.1866 0.1603 0.2458 -0.0234 -0.0002 -0.0352 39  ASN A DD21 
711  D DD22 A ASN A 39  ? 0.1940 0.1804 0.3071 -0.0236 0.0405  -0.0449 39  ASN A DD22 
712  D DD22 B ASN A 39  ? 0.1649 0.1752 0.2693 -0.0063 -0.0315 -0.0313 39  ASN A DD22 
713  N N    . THR A 40  ? 0.1241 0.1121 0.1049 0.0050  -0.0028 0.0225  40  THR A N    
714  C CA   . THR A 40  ? 0.1087 0.1348 0.1170 -0.0014 -0.0100 0.0256  40  THR A CA   
715  C C    . THR A 40  ? 0.1148 0.1146 0.1064 0.0096  -0.0065 0.0171  40  THR A C    
716  O O    . THR A 40  ? 0.1387 0.1229 0.1174 0.0033  -0.0260 0.0169  40  THR A O    
717  C CB   . THR A 40  ? 0.1242 0.1588 0.1289 0.0176  0.0046  0.0342  40  THR A CB   
718  O OG1  . THR A 40  ? 0.1496 0.1606 0.1497 0.0197  0.0048  0.0148  40  THR A OG1  
719  C CG2  . THR A 40  ? 0.1191 0.1673 0.1597 0.0167  0.0223  0.0321  40  THR A CG2  
723  D DG1  . THR A 40  ? 0.1857 0.1677 0.1448 0.0331  0.0008  0.0153  40  THR A DG1  
727  N N    A GLN A 41  ? 0.1252 0.0965 0.1131 0.0065  -0.0119 0.0173  41  GLN A N    
728  N N    B GLN A 41  ? 0.1225 0.1048 0.1153 0.0057  -0.0118 0.0215  41  GLN A N    
729  C CA   A GLN A 41  ? 0.1426 0.1056 0.1228 -0.0060 -0.0106 0.0193  41  GLN A CA   
730  C CA   B GLN A 41  ? 0.1430 0.1078 0.1332 -0.0016 -0.0029 0.0247  41  GLN A CA   
731  C C    A GLN A 41  ? 0.1321 0.0994 0.1110 0.0025  -0.0179 0.0359  41  GLN A C    
732  C C    B GLN A 41  ? 0.1275 0.1031 0.1214 -0.0105 -0.0124 0.0238  41  GLN A C    
733  O O    A GLN A 41  ? 0.1173 0.1091 0.1332 0.0084  -0.0235 0.0549  41  GLN A O    
734  O O    B GLN A 41  ? 0.0822 0.1038 0.1031 -0.0306 -0.0494 0.0176  41  GLN A O    
735  C CB   A GLN A 41  ? 0.1769 0.1261 0.1586 -0.0278 -0.0077 -0.0068 41  GLN A CB   
736  C CB   B GLN A 41  ? 0.1754 0.1247 0.1526 -0.0202 0.0102  -0.0037 41  GLN A CB   
737  C CG   A GLN A 41  ? 0.2210 0.1715 0.1734 -0.0059 -0.0003 -0.0280 41  GLN A CG   
738  C CG   B GLN A 41  ? 0.3227 0.1606 0.1702 0.0483  0.0599  0.0032  41  GLN A CG   
745  D D    A GLN A 41  ? 0.1354 0.1010 0.1280 0.0073  -0.0282 0.0182  41  GLN A D    
746  D D    B GLN A 41  ? 0.1334 0.1055 0.1259 0.0041  -0.0264 0.0192  41  GLN A D    
761  N N    . ALA A 42  ? 0.1502 0.1048 0.1176 -0.0068 -0.0065 0.0161  42  ALA A N    
762  C CA   . ALA A 42  ? 0.1398 0.1250 0.1119 -0.0108 -0.0174 -0.0020 42  ALA A CA   
763  C C    . ALA A 42  ? 0.1293 0.1271 0.1115 -0.0272 -0.0169 -0.0008 42  ALA A C    
764  O O    . ALA A 42  ? 0.1243 0.1348 0.1232 -0.0200 -0.0125 0.0144  42  ALA A O    
765  C CB   . ALA A 42  ? 0.1535 0.1243 0.1537 0.0100  -0.0116 0.0043  42  ALA A CB   
771  N N    . THR A 43  ? 0.1290 0.1431 0.1228 -0.0303 -0.0121 -0.0018 43  THR A N    
772  C CA   . THR A 43  ? 0.1214 0.1797 0.1242 -0.0033 -0.0103 0.0182  43  THR A CA   
773  C C    . THR A 43  ? 0.1015 0.2085 0.1334 -0.0112 -0.0165 0.0070  43  THR A C    
774  O O    . THR A 43  ? 0.1144 0.3387 0.1821 -0.0059 -0.0403 -0.0503 43  THR A O    
775  C CB   . THR A 43  ? 0.2331 0.1774 0.1521 0.0063  0.0137  0.0209  43  THR A CB   
776  O OG1  . THR A 43  ? 0.2561 0.2071 0.2388 -0.0465 0.0216  -0.0184 43  THR A OG1  
777  C CG2  . THR A 43  ? 0.2565 0.1892 0.2221 0.0362  0.0228  0.0149  43  THR A CG2  
778  D D    . THR A 43  ? 0.1303 0.1804 0.1189 -0.0361 -0.0117 0.0086  43  THR A D    
781  D DG1  . THR A 43  ? 0.2629 0.3494 0.2742 -0.0586 0.0328  0.0049  43  THR A DG1  
785  N N    . ASN A 44  ? 0.0861 0.1854 0.1195 -0.0108 -0.0068 0.0257  44  ASN A N    
786  C CA   . ASN A 44  ? 0.0827 0.1764 0.1327 0.0016  -0.0045 0.0388  44  ASN A CA   
787  C C    . ASN A 44  ? 0.1081 0.1468 0.1161 -0.0165 -0.0013 0.0162  44  ASN A C    
788  O O    . ASN A 44  ? 0.1128 0.1326 0.1277 -0.0187 -0.0101 0.0252  44  ASN A O    
789  C CB   . ASN A 44  ? 0.1371 0.1723 0.2056 0.0264  0.0110  0.0596  44  ASN A CB   
790  C CG   . ASN A 44  ? 0.1854 0.2654 0.2725 0.0870  0.0244  -0.0025 44  ASN A CG   
791  O OD1  . ASN A 44  ? 0.1629 0.2734 0.3390 0.0870  0.0461  -0.0216 44  ASN A OD1  
792  N ND2  . ASN A 44  ? 0.2489 0.3740 0.2952 0.1215  0.0105  -0.0622 44  ASN A ND2  
797  D DD21 . ASN A 44  ? 0.3288 0.4225 0.3189 0.1370  0.0535  -0.0734 44  ASN A DD21 
798  D DD22 . ASN A 44  ? 0.2684 0.4024 0.3164 0.0985  -0.0327 -0.0599 44  ASN A DD22 
799  N N    A ARG A 45  ? 0.1083 0.1572 0.1284 -0.0237 -0.0093 0.0226  45  ARG A N    
800  N N    B ARG A 45  ? 0.1086 0.1550 0.1307 -0.0233 -0.0111 0.0223  45  ARG A N    
801  C CA   A ARG A 45  ? 0.1376 0.1431 0.1362 -0.0185 -0.0040 0.0256  45  ARG A CA   
802  C CA   B ARG A 45  ? 0.1294 0.1420 0.1392 -0.0253 -0.0052 0.0252  45  ARG A CA   
803  C C    A ARG A 45  ? 0.1244 0.1599 0.1412 -0.0181 0.0087  0.0332  45  ARG A C    
804  C C    B ARG A 45  ? 0.1182 0.1491 0.1443 -0.0208 0.0076  0.0347  45  ARG A C    
805  O O    A ARG A 45  ? 0.1228 0.1922 0.1422 -0.0347 0.0043  0.0432  45  ARG A O    
806  O O    B ARG A 45  ? 0.1164 0.1815 0.1570 -0.0242 -0.0011 0.0403  45  ARG A O    
807  C CB   A ARG A 45  ? 0.1569 0.1558 0.1695 -0.0437 -0.0030 0.0187  45  ARG A CB   
808  C CB   B ARG A 45  ? 0.1518 0.1568 0.1636 -0.0475 -0.0054 0.0158  45  ARG A CB   
809  C CG   A ARG A 45  ? 0.2180 0.1552 0.2079 -0.0659 0.0274  -0.0129 45  ARG A CG   
810  C CG   B ARG A 45  ? 0.2053 0.1502 0.2069 -0.0622 0.0296  -0.0067 45  ARG A CG   
811  C CD   A ARG A 45  ? 0.3093 0.1568 0.2655 -0.0410 0.0564  -0.0154 45  ARG A CD   
812  C CD   B ARG A 45  ? 0.2278 0.1542 0.2458 -0.0703 0.0267  -0.0142 45  ARG A CD   
813  N NE   A ARG A 45  ? 0.2955 0.1597 0.3036 -0.0605 0.0619  -0.0475 45  ARG A NE   
814  N NE   B ARG A 45  ? 0.2831 0.1617 0.2910 -0.0636 0.0553  -0.0390 45  ARG A NE   
815  C CZ   A ARG A 45  ? 0.2960 0.1659 0.3384 -0.0538 0.0521  -0.0452 45  ARG A CZ   
816  C CZ   B ARG A 45  ? 0.3001 0.1539 0.2953 -0.0628 0.0475  -0.0704 45  ARG A CZ   
817  N NH1  A ARG A 45  ? 0.3601 0.2565 0.3394 0.0196  0.0355  -0.0265 45  ARG A NH1  
818  N NH1  B ARG A 45  ? 0.2982 0.1517 0.2907 -0.0709 0.0457  -0.0642 45  ARG A NH1  
819  N NH2  A ARG A 45  ? 0.2881 0.1581 0.3492 -0.0358 0.0379  -0.0706 45  ARG A NH2  
820  N NH2  B ARG A 45  ? 0.2975 0.1226 0.3067 -0.0837 0.0456  -0.0987 45  ARG A NH2  
821  D D    A ARG A 45  ? 0.1334 0.1824 0.1407 -0.0428 -0.0229 0.0209  45  ARG A D    
822  D D    B ARG A 45  ? 0.1227 0.1825 0.1425 -0.0325 -0.0218 0.0178  45  ARG A D    
837  D DE   A ARG A 45  ? 0.2669 0.1305 0.2959 -0.0884 0.0764  -0.0606 45  ARG A DE   
838  D DE   B ARG A 45  ? 0.3011 0.1534 0.3036 -0.0385 0.0568  -0.0448 45  ARG A DE   
839  D DH11 A ARG A 45  ? 0.4266 0.3095 0.3290 0.0794  0.0041  -0.0395 45  ARG A DH11 
840  D DH11 B ARG A 45  ? 0.3049 0.1641 0.2776 -0.0754 0.0550  -0.0498 45  ARG A DH11 
841  D DH12 A ARG A 45  ? 0.4144 0.3619 0.3886 0.0927  0.0019  -0.0661 45  ARG A DH12 
842  D DH12 B ARG A 45  ? 0.3068 0.1600 0.2844 -0.0554 0.0419  -0.0575 45  ARG A DH12 
843  D DH21 A ARG A 45  ? 0.3120 0.1263 0.3555 -0.0572 0.0302  -0.0829 45  ARG A DH21 
844  D DH21 B ARG A 45  ? 0.3497 0.1181 0.3120 -0.0526 0.0357  -0.1195 45  ARG A DH21 
845  D DH22 A ARG A 45  ? 0.2867 0.1541 0.3669 -0.0358 0.0458  -0.0501 45  ARG A DH22 
846  D DH22 B ARG A 45  ? 0.3018 0.1256 0.3301 -0.0646 0.0450  -0.0944 45  ARG A DH22 
847  N N    . ASN A 46  ? 0.1007 0.1658 0.1443 0.0191  0.0109  0.0144  46  ASN A N    
848  C CA   . ASN A 46  ? 0.1268 0.1511 0.1631 0.0132  0.0259  0.0129  46  ASN A CA   
849  C C    . ASN A 46  ? 0.1293 0.1655 0.1470 0.0025  0.0235  0.0041  46  ASN A C    
850  O O    . ASN A 46  ? 0.1852 0.1808 0.1363 0.0309  0.0718  0.0262  46  ASN A O    
851  C CB   . ASN A 46  ? 0.1489 0.1540 0.1734 -0.0003 0.0336  0.0055  46  ASN A CB   
852  C CG   . ASN A 46  ? 0.1740 0.1573 0.2218 0.0049  0.0471  0.0375  46  ASN A CG   
853  O OD1  . ASN A 46  ? 0.1879 0.1954 0.2396 0.0148  0.0371  0.0562  46  ASN A OD1  
854  N ND2  . ASN A 46  ? 0.1751 0.1773 0.2261 0.0050  0.0506  0.0525  46  ASN A ND2  
855  D D    . ASN A 46  ? 0.1129 0.2911 0.1907 0.0508  -0.0069 -0.0333 46  ASN A D    
859  D DD21 . ASN A 46  ? 0.1918 0.1945 0.2359 -0.0162 0.0534  0.0542  46  ASN A DD21 
860  D DD22 . ASN A 46  ? 0.1833 0.1940 0.2164 0.0161  0.0409  0.0395  46  ASN A DD22 
861  N N    . THR A 47  ? 0.1499 0.1900 0.1657 0.0343  0.0380  0.0191  47  THR A N    
862  C CA   . THR A 47  ? 0.1289 0.1914 0.1638 -0.0128 0.0276  0.0019  47  THR A CA   
863  C C    . THR A 47  ? 0.1221 0.2079 0.1593 -0.0026 0.0324  0.0114  47  THR A C    
864  O O    . THR A 47  ? 0.1535 0.2702 0.1892 -0.0434 0.0129  0.0514  47  THR A O    
865  C CB   . THR A 47  ? 0.1140 0.2043 0.1623 -0.0238 0.0164  -0.0025 47  THR A CB   
866  O OG1  . THR A 47  ? 0.1497 0.1910 0.1669 -0.0003 0.0047  0.0001  47  THR A OG1  
867  C CG2  . THR A 47  ? 0.1170 0.2354 0.1630 -0.0383 0.0161  0.0124  47  THR A CG2  
868  D D    . THR A 47  ? 0.1426 0.1951 0.1829 0.0386  0.0156  0.0240  47  THR A D    
871  D DG1  . THR A 47  ? 0.1985 0.2222 0.1637 0.0387  -0.0090 -0.0157 47  THR A DG1  
875  N N    . ASP A 48  ? 0.1336 0.2213 0.1458 -0.0176 0.0344  0.0006  48  ASP A N    
876  C CA   . ASP A 48  ? 0.1512 0.2350 0.1379 -0.0065 0.0289  -0.0310 48  ASP A CA   
877  C C    . ASP A 48  ? 0.1395 0.2202 0.1703 -0.0099 0.0392  0.0043  48  ASP A C    
878  O O    . ASP A 48  ? 0.1894 0.2774 0.1998 0.0064  0.0001  0.0336  48  ASP A O    
879  C CB   . ASP A 48  ? 0.1901 0.2403 0.1470 -0.0168 0.0445  -0.0672 48  ASP A CB   
880  C CG   . ASP A 48  ? 0.1487 0.2745 0.1622 -0.0312 0.0269  -0.0398 48  ASP A CG   
881  O OD1  . ASP A 48  ? 0.1690 0.2103 0.1336 0.0202  0.0392  0.0105  48  ASP A OD1  
882  O OD2  . ASP A 48  ? 0.2348 0.3187 0.2204 -0.0881 0.0601  -0.0700 48  ASP A OD2  
883  D D    . ASP A 48  ? 0.2148 0.2063 0.1182 -0.0582 0.0262  -0.0251 48  ASP A D    
887  N N    . GLY A 49  ? 0.1648 0.1715 0.1761 -0.0067 0.0566  0.0195  49  GLY A N    
888  C CA   . GLY A 49  ? 0.2063 0.1666 0.2080 0.0052  0.0897  0.0419  49  GLY A CA   
889  C C    . GLY A 49  ? 0.1690 0.1467 0.1543 -0.0030 0.0470  0.0246  49  GLY A C    
890  O O    . GLY A 49  ? 0.1623 0.1368 0.2035 -0.0118 0.0586  0.0246  49  GLY A O    
891  D D    . GLY A 49  ? 0.1603 0.2406 0.1732 0.0086  0.0530  -0.0388 49  GLY A D    
894  N N    . SER A 50  ? 0.1267 0.1448 0.1261 -0.0081 0.0112  0.0151  50  SER A N    
895  C CA   . SER A 50  ? 0.1128 0.1306 0.1198 0.0015  0.0043  0.0219  50  SER A CA   
896  C C    . SER A 50  ? 0.1006 0.1507 0.1189 -0.0126 0.0061  -0.0015 50  SER A C    
897  O O    . SER A 50  ? 0.0978 0.1915 0.1272 -0.0236 0.0074  0.0269  50  SER A O    
898  C CB   . SER A 50  ? 0.1145 0.1453 0.1055 -0.0059 -0.0031 0.0107  50  SER A CB   
899  O OG   . SER A 50  ? 0.1236 0.1287 0.1278 -0.0049 0.0106  -0.0060 50  SER A OG   
901  D D    B SER A 50  ? 0.1214 0.1523 0.1018 -0.0027 0.0022  0.0202  50  SER A D    
905  D DG   . SER A 50  ? 0.1581 0.1386 0.1636 0.0039  0.0447  -0.0115 50  SER A DG   
906  N N    . THR A 51  ? 0.0880 0.1327 0.1127 -0.0079 -0.0055 0.0138  51  THR A N    
907  C CA   . THR A 51  ? 0.0735 0.1025 0.1142 0.0054  -0.0102 0.0219  51  THR A CA   
908  C C    . THR A 51  ? 0.0772 0.1072 0.1124 -0.0012 -0.0180 0.0173  51  THR A C    
909  O O    . THR A 51  ? 0.0806 0.1362 0.1164 -0.0106 -0.0208 0.0210  51  THR A O    
910  C CB   . THR A 51  ? 0.0936 0.1082 0.1278 -0.0033 -0.0098 0.0120  51  THR A CB   
911  O OG1  . THR A 51  ? 0.1280 0.1202 0.1564 -0.0250 -0.0079 0.0199  51  THR A OG1  
912  C CG2  . THR A 51  ? 0.0945 0.1508 0.1274 -0.0021 -0.0099 -0.0068 51  THR A CG2  
914  D D    B THR A 51  ? 0.0897 0.0956 0.1063 -0.0113 -0.0093 0.0185  51  THR A D    
917  D DG1  . THR A 51  ? 0.1178 0.1533 0.1586 -0.0051 0.0163  0.0453  51  THR A DG1  
921  N N    . ASP A 52  ? 0.0894 0.1144 0.0996 0.0034  -0.0122 0.0197  52  ASP A N    
922  C CA   . ASP A 52  ? 0.0731 0.1075 0.1046 -0.0008 -0.0211 0.0134  52  ASP A CA   
923  C C    . ASP A 52  ? 0.0757 0.1063 0.1009 0.0012  -0.0208 0.0189  52  ASP A C    
924  O O    . ASP A 52  ? 0.0763 0.1747 0.1093 -0.0120 -0.0120 -0.0116 52  ASP A O    
925  C CB   . ASP A 52  ? 0.1249 0.1118 0.1168 0.0202  -0.0092 0.0220  52  ASP A CB   
926  C CG   . ASP A 52  ? 0.1858 0.1348 0.1338 0.0368  0.0165  0.0152  52  ASP A CG   
927  O OD1  . ASP A 52  ? 0.2338 0.1910 0.1277 0.0265  0.0095  -0.0230 52  ASP A OD1  
928  O OD2  . ASP A 52  ? 0.1869 0.2107 0.2272 0.0521  0.0367  -0.0283 52  ASP A OD2  
933  N N    . TYR A 53  ? 0.0755 0.0908 0.1066 -0.0009 -0.0200 0.0087  53  TYR A N    
934  C CA   . TYR A 53  ? 0.0921 0.0942 0.1088 -0.0047 -0.0063 0.0097  53  TYR A CA   
935  C C    . TYR A 53  ? 0.0842 0.0995 0.1074 0.0016  -0.0145 0.0161  53  TYR A C    
936  O O    . TYR A 53  ? 0.1076 0.1088 0.0868 -0.0127 -0.0075 0.0095  53  TYR A O    
937  C CB   . TYR A 53  ? 0.1148 0.1018 0.1346 0.0166  0.0199  0.0253  53  TYR A CB   
938  C CG   . TYR A 53  ? 0.1102 0.0963 0.1196 0.0072  -0.0001 0.0172  53  TYR A CG   
939  C CD1  . TYR A 53  ? 0.1567 0.1074 0.1159 -0.0017 -0.0049 0.0103  53  TYR A CD1  
940  C CD2  . TYR A 53  ? 0.0822 0.0913 0.1188 0.0088  -0.0020 0.0067  53  TYR A CD2  
941  C CE1  . TYR A 53  ? 0.1548 0.0913 0.1260 0.0009  -0.0111 0.0091  53  TYR A CE1  
942  C CE2  . TYR A 53  ? 0.0979 0.0983 0.1168 0.0166  -0.0039 0.0169  53  TYR A CE2  
943  C CZ   . TYR A 53  ? 0.1236 0.0876 0.1270 0.0164  -0.0221 0.0221  53  TYR A CZ   
944  O OH   . TYR A 53  ? 0.1454 0.1107 0.1383 -0.0056 -0.0178 0.0300  53  TYR A OH   
953  D DH   . TYR A 53  ? 0.1474 0.1443 0.1350 0.0129  -0.0166 0.0350  53  TYR A DH   
954  N N    . GLY A 54  ? 0.1022 0.0997 0.1078 -0.0080 -0.0147 0.0124  54  GLY A N    
955  C CA   . GLY A 54  ? 0.1521 0.0804 0.1050 0.0157  0.0087  0.0026  54  GLY A CA   
956  C C    . GLY A 54  ? 0.1204 0.0894 0.1239 0.0109  0.0041  0.0180  54  GLY A C    
957  O O    . GLY A 54  ? 0.1203 0.0949 0.1095 0.0144  -0.0064 0.0089  54  GLY A O    
961  N N    . ILE A 55  ? 0.1245 0.0912 0.1011 0.0127  -0.0027 0.0060  55  ILE A N    
962  C CA   . ILE A 55  ? 0.1111 0.0985 0.1119 0.0050  -0.0056 0.0158  55  ILE A CA   
963  C C    . ILE A 55  ? 0.1279 0.0978 0.1142 0.0095  -0.0126 0.0122  55  ILE A C    
964  O O    . ILE A 55  ? 0.1238 0.1062 0.1448 0.0141  -0.0159 0.0091  55  ILE A O    
965  C CB   . ILE A 55  ? 0.1422 0.1194 0.1233 0.0047  0.0143  0.0198  55  ILE A CB   
966  C CG1  . ILE A 55  ? 0.2206 0.1468 0.1193 0.0238  0.0101  0.0301  55  ILE A CG1  
967  C CG2  . ILE A 55  ? 0.1317 0.1470 0.1408 -0.0011 0.0319  -0.0024 55  ILE A CG2  
968  C CD1  . ILE A 55  ? 0.2434 0.1944 0.1218 0.0236  0.0171  0.0332  55  ILE A CD1  
969  D D    A ILE A 55  ? 0.0974 0.0994 0.0877 0.0050  -0.0226 0.0001  55  ILE A D    
981  N N    A LEU A 56  ? 0.1059 0.1091 0.1148 -0.0192 -0.0099 0.0198  56  LEU A N    
982  N N    B LEU A 56  ? 0.1051 0.1072 0.1156 -0.0183 -0.0095 0.0197  56  LEU A N    
983  C CA   A LEU A 56  ? 0.1088 0.1020 0.1258 -0.0089 -0.0236 0.0186  56  LEU A CA   
984  C CA   B LEU A 56  ? 0.1084 0.1041 0.1266 -0.0126 -0.0237 0.0164  56  LEU A CA   
985  C C    A LEU A 56  ? 0.1072 0.0900 0.1265 -0.0003 -0.0143 0.0053  56  LEU A C    
986  C C    B LEU A 56  ? 0.1097 0.0885 0.1230 -0.0017 -0.0190 0.0049  56  LEU A C    
987  O O    A LEU A 56  ? 0.0958 0.0944 0.1352 -0.0134 -0.0075 0.0013  56  LEU A O    
988  O O    B LEU A 56  ? 0.0547 0.0938 0.1306 0.0147  -0.0407 -0.0022 56  LEU A O    
989  C CB   A LEU A 56  ? 0.1153 0.1373 0.1260 -0.0248 -0.0307 0.0221  56  LEU A CB   
990  C CB   B LEU A 56  ? 0.1160 0.1296 0.1384 -0.0254 -0.0310 0.0200  56  LEU A CB   
991  C CG   A LEU A 56  ? 0.1202 0.1300 0.1546 -0.0227 -0.0351 0.0389  56  LEU A CG   
992  C CG   B LEU A 56  ? 0.1197 0.1347 0.1528 -0.0353 -0.0345 0.0356  56  LEU A CG   
993  C CD1  A LEU A 56  ? 0.1184 0.1540 0.1609 -0.0264 -0.0434 0.0559  56  LEU A CD1  
994  C CD1  B LEU A 56  ? 0.1201 0.1516 0.1621 -0.0381 -0.0365 0.0341  56  LEU A CD1  
995  C CD2  A LEU A 56  ? 0.1390 0.1328 0.1812 -0.0183 -0.0248 0.0195  56  LEU A CD2  
996  C CD2  B LEU A 56  ? 0.1382 0.1514 0.1626 -0.0112 -0.0188 0.0423  56  LEU A CD2  
1019 N N    . GLN A 57  ? 0.0982 0.0876 0.1142 0.0035  -0.0177 0.0074  57  GLN A N    
1020 C CA   . GLN A 57  ? 0.1080 0.0796 0.1162 -0.0009 -0.0119 -0.0021 57  GLN A CA   
1021 C C    . GLN A 57  ? 0.1051 0.0902 0.1185 -0.0165 -0.0123 -0.0054 57  GLN A C    
1022 O O    . GLN A 57  ? 0.1538 0.1597 0.1266 0.0428  -0.0261 -0.0262 57  GLN A O    
1023 C CB   . GLN A 57  ? 0.1192 0.1051 0.0988 0.0146  -0.0059 0.0024  57  GLN A CB   
1024 C CG   . GLN A 57  ? 0.1085 0.1194 0.1038 0.0055  -0.0098 0.0234  57  GLN A CG   
1025 C CD   . GLN A 57  ? 0.1037 0.1282 0.1260 -0.0046 -0.0125 0.0116  57  GLN A CD   
1026 O OE1  . GLN A 57  ? 0.1232 0.1461 0.1987 -0.0060 0.0281  0.0200  57  GLN A OE1  
1027 N NE2  . GLN A 57  ? 0.1441 0.1207 0.1228 -0.0065 0.0014  0.0107  57  GLN A NE2  
1029 D D    B GLN A 57  ? 0.0676 0.0650 0.0849 0.0268  -0.0464 0.0337  57  GLN A D    
1035 D DE21 . GLN A 57  ? 0.1522 0.1243 0.1635 -0.0154 -0.0063 0.0117  57  GLN A DE21 
1036 D DE22 . GLN A 57  ? 0.1782 0.1348 0.1344 -0.0350 0.0260  -0.0285 57  GLN A DE22 
1037 N N    . ILE A 58  ? 0.1036 0.1139 0.1053 -0.0085 -0.0018 0.0066  58  ILE A N    
1038 C CA   . ILE A 58  ? 0.1115 0.0915 0.1073 -0.0143 -0.0064 0.0151  58  ILE A CA   
1039 C C    . ILE A 58  ? 0.1185 0.1053 0.1047 -0.0251 -0.0128 0.0192  58  ILE A C    
1040 O O    . ILE A 58  ? 0.1118 0.1079 0.1203 -0.0271 -0.0059 0.0144  58  ILE A O    
1041 C CB   . ILE A 58  ? 0.1117 0.1331 0.1049 -0.0067 -0.0104 0.0196  58  ILE A CB   
1042 C CG1  . ILE A 58  ? 0.1253 0.1602 0.1317 -0.0064 0.0187  0.0351  58  ILE A CG1  
1043 C CG2  . ILE A 58  ? 0.1058 0.1699 0.1026 -0.0321 -0.0255 0.0090  58  ILE A CG2  
1044 C CD1  . ILE A 58  ? 0.1377 0.1965 0.1521 0.0034  0.0312  0.0331  58  ILE A CD1  
1056 N N    . ASN A 59  ? 0.1043 0.1304 0.0979 -0.0307 -0.0313 0.0163  59  ASN A N    
1057 C CA   . ASN A 59  ? 0.1147 0.1332 0.0903 -0.0158 -0.0240 0.0137  59  ASN A CA   
1058 C C    . ASN A 59  ? 0.1129 0.1322 0.0904 -0.0107 -0.0237 0.0144  59  ASN A C    
1059 O O    . ASN A 59  ? 0.1112 0.1457 0.1303 -0.0201 -0.0252 0.0413  59  ASN A O    
1060 C CB   . ASN A 59  ? 0.1491 0.1171 0.1133 -0.0083 -0.0010 0.0173  59  ASN A CB   
1061 C CG   . ASN A 59  ? 0.1448 0.1471 0.1065 -0.0087 -0.0029 0.0231  59  ASN A CG   
1062 O OD1  . ASN A 59  ? 0.1545 0.1370 0.1032 0.0359  0.0036  0.0131  59  ASN A OD1  
1063 N ND2  . ASN A 59  ? 0.1356 0.1999 0.1306 -0.0078 0.0035  0.0273  59  ASN A ND2  
1064 D D    . ASN A 59  ? 0.1621 0.1580 0.1411 -0.0672 0.0060  -0.0192 59  ASN A D    
1068 D DD21 . ASN A 59  ? 0.1448 0.1894 0.1337 -0.0114 0.0147  0.0090  59  ASN A DD21 
1069 D DD22 . ASN A 59  ? 0.1352 0.2079 0.1403 -0.0090 -0.0064 0.0316  59  ASN A DD22 
1070 N N    . SER A 60  ? 0.1059 0.1175 0.1058 -0.0038 -0.0245 -0.0027 60  SER A N    
1071 C CA   . SER A 60  ? 0.0815 0.1209 0.1060 0.0016  0.0032  0.0097  60  SER A CA   
1072 C C    . SER A 60  ? 0.1180 0.1572 0.1075 0.0184  -0.0063 0.0067  60  SER A C    
1073 O O    . SER A 60  ? 0.1939 0.2076 0.0994 0.0822  0.0197  0.0233  60  SER A O    
1074 C CB   . SER A 60  ? 0.0965 0.1190 0.1347 0.0030  0.0065  0.0064  60  SER A CB   
1075 O OG   . SER A 60  ? 0.0996 0.1008 0.1514 -0.0007 0.0138  0.0170  60  SER A OG   
1080 D DG   . SER A 60  ? 0.1031 0.1219 0.1699 -0.0067 0.0047  0.0366  60  SER A DG   
1081 N N    . ARG A 61  ? 0.1036 0.1338 0.0975 0.0031  -0.0130 0.0184  61  ARG A N    
1082 C CA   . ARG A 61  ? 0.1151 0.1308 0.1007 0.0033  -0.0117 0.0138  61  ARG A CA   
1083 C C    . ARG A 61  ? 0.1184 0.1453 0.1119 -0.0061 -0.0185 0.0128  61  ARG A C    
1084 O O    . ARG A 61  ? 0.1101 0.1637 0.1352 -0.0140 -0.0143 0.0428  61  ARG A O    
1085 C CB   . ARG A 61  ? 0.1347 0.1423 0.1144 0.0222  -0.0065 0.0079  61  ARG A CB   
1086 C CG   . ARG A 61  ? 0.2286 0.2069 0.1095 0.0432  0.0020  0.0040  61  ARG A CG   
1087 C CD   . ARG A 61  ? 0.3358 0.2916 0.1531 0.0786  0.0364  -0.0531 61  ARG A CD   
1088 N NE   . ARG A 61  ? 0.2980 0.3423 0.2530 0.1111  0.0793  -0.0137 61  ARG A NE   
1089 C CZ   . ARG A 61  ? 0.3291 0.3988 0.3724 0.0899  0.1242  0.0209  61  ARG A CZ   
1090 N NH1  . ARG A 61  ? 0.3730 0.4446 0.4292 0.1221  0.1820  0.0912  61  ARG A NH1  
1091 N NH2  . ARG A 61  ? 0.3272 0.4129 0.4214 0.0620  0.1060  -0.0173 61  ARG A NH2  
1100 D DE   . ARG A 61  ? 0.3087 0.3709 0.2796 0.1206  0.0538  0.0029  61  ARG A DE   
1101 D DH11 . ARG A 61  ? 0.4120 0.5061 0.4926 0.0997  0.2127  0.1164  61  ARG A DH11 
1102 D DH12 . ARG A 61  ? 0.3825 0.4922 0.4518 0.1256  0.1572  0.1353  61  ARG A DH12 
1103 D DH21 . ARG A 61  ? 0.3499 0.4288 0.4631 0.0473  0.1364  -0.0311 61  ARG A DH21 
1104 D DH22 . ARG A 61  ? 0.3308 0.3971 0.3800 0.0311  0.0474  -0.0557 61  ARG A DH22 
1105 N N    . TRP A 62  ? 0.1099 0.1563 0.1083 0.0031  -0.0010 0.0236  62  TRP A N    
1106 C CA   . TRP A 62  ? 0.1243 0.1597 0.1302 -0.0157 0.0086  -0.0078 62  TRP A CA   
1107 C C    . TRP A 62  ? 0.1044 0.1475 0.1095 -0.0082 -0.0116 0.0022  62  TRP A C    
1108 O O    . TRP A 62  ? 0.1078 0.1885 0.0842 -0.0217 -0.0139 -0.0197 62  TRP A O    
1109 C CB   . TRP A 62  ? 0.1751 0.1525 0.1745 -0.0139 0.0350  -0.0056 62  TRP A CB   
1110 C CG   . TRP A 62  ? 0.1913 0.2044 0.1837 0.0042  0.0349  -0.0315 62  TRP A CG   
1111 C CD1  . TRP A 62  ? 0.2228 0.2271 0.1704 0.0141  0.0462  -0.0231 62  TRP A CD1  
1112 C CD2  . TRP A 62  ? 0.2162 0.2142 0.2189 0.0103  0.0370  -0.0475 62  TRP A CD2  
1113 N NE1  . TRP A 62  ? 0.2828 0.2557 0.1931 0.0378  0.0656  -0.0358 62  TRP A NE1  
1114 C CE2  . TRP A 62  ? 0.2732 0.2444 0.2139 0.0401  0.0438  -0.0571 62  TRP A CE2  
1115 C CE3  . TRP A 62  ? 0.2969 0.2020 0.2989 -0.0010 0.0630  -0.0413 62  TRP A CE3  
1116 C CZ2  . TRP A 62  ? 0.2659 0.2381 0.2273 0.0938  -0.0052 -0.0534 62  TRP A CZ2  
1117 C CZ3  . TRP A 62  ? 0.3096 0.2070 0.2980 0.0231  0.0057  -0.0445 62  TRP A CZ3  
1118 C CH2  . TRP A 62  ? 0.3149 0.2239 0.2896 0.0803  0.0000  -0.0496 62  TRP A CH2  
1119 D D    . TRP A 62  ? 0.1156 0.2201 0.1965 0.0079  -0.0055 0.0914  62  TRP A D    
1124 D DE1  . TRP A 62  ? 0.3937 0.3148 0.2054 0.0196  0.1149  -0.0439 62  TRP A DE1  
1129 N N    . TRP A 63  ? 0.0850 0.0984 0.1131 0.0114  -0.0213 0.0073  63  TRP A N    
1130 C CA   . TRP A 63  ? 0.0900 0.0943 0.1029 -0.0085 -0.0255 0.0093  63  TRP A CA   
1131 C C    . TRP A 63  ? 0.0977 0.0985 0.1261 -0.0098 0.0001  0.0062  63  TRP A C    
1132 O O    . TRP A 63  ? 0.1064 0.1232 0.1747 -0.0203 0.0164  -0.0332 63  TRP A O    
1133 C CB   . TRP A 63  ? 0.1182 0.1072 0.1156 -0.0010 -0.0325 0.0223  63  TRP A CB   
1134 C CG   . TRP A 63  ? 0.1222 0.1080 0.1339 0.0034  -0.0200 0.0239  63  TRP A CG   
1135 C CD1  . TRP A 63  ? 0.1290 0.1203 0.1808 0.0173  -0.0178 0.0296  63  TRP A CD1  
1136 C CD2  . TRP A 63  ? 0.1387 0.0992 0.1144 0.0019  -0.0178 0.0202  63  TRP A CD2  
1137 N NE1  . TRP A 63  ? 0.1542 0.1239 0.1958 0.0153  0.0167  0.0171  63  TRP A NE1  
1138 C CE2  . TRP A 63  ? 0.1641 0.1001 0.1671 -0.0012 0.0185  0.0151  63  TRP A CE2  
1139 C CE3  . TRP A 63  ? 0.1423 0.1122 0.1350 -0.0028 -0.0344 0.0038  63  TRP A CE3  
1140 C CZ2  . TRP A 63  ? 0.2078 0.1287 0.1506 -0.0183 0.0315  -0.0114 63  TRP A CZ2  
1141 C CZ3  . TRP A 63  ? 0.1736 0.1306 0.1202 -0.0254 -0.0317 0.0062  63  TRP A CZ3  
1142 C CH2  . TRP A 63  ? 0.2150 0.1282 0.1496 -0.0331 -0.0074 -0.0147 63  TRP A CH2  
1148 D DE1  . TRP A 63  ? 0.1723 0.1656 0.3141 0.0363  0.0194  -0.0230 63  TRP A DE1  
1153 N N    . CYS A 64  ? 0.1054 0.1260 0.1391 -0.0207 0.0075  -0.0310 64  CYS A N    
1154 C CA   . CYS A 64  ? 0.1058 0.1190 0.1367 -0.0100 -0.0006 -0.0248 64  CYS A CA   
1155 C C    . CYS A 64  ? 0.1050 0.1284 0.1280 -0.0050 -0.0018 -0.0146 64  CYS A C    
1156 O O    . CYS A 64  ? 0.1413 0.1704 0.1155 0.0063  0.0160  -0.0203 64  CYS A O    
1157 C CB   . CYS A 64  ? 0.0982 0.0985 0.1296 -0.0165 0.0157  -0.0227 64  CYS A CB   
1158 S SG   . CYS A 64  ? 0.1009 0.1106 0.1332 -0.0127 0.0082  -0.0159 64  CYS A SG   
1163 N N    A ASN A 65  ? 0.1096 0.1264 0.1344 -0.0054 -0.0014 -0.0096 65  ASN A N    
1164 N N    B ASN A 65  ? 0.1008 0.1237 0.1348 -0.0102 -0.0036 -0.0112 65  ASN A N    
1165 C CA   A ASN A 65  ? 0.1169 0.1331 0.1368 -0.0063 -0.0100 -0.0009 65  ASN A CA   
1166 C CA   B ASN A 65  ? 0.1189 0.1337 0.1334 -0.0111 -0.0072 -0.0030 65  ASN A CA   
1167 C C    A ASN A 65  ? 0.1203 0.1100 0.1261 0.0021  -0.0121 0.0042  65  ASN A C    
1168 C C    B ASN A 65  ? 0.1214 0.1055 0.1320 -0.0021 -0.0076 0.0006  65  ASN A C    
1169 O O    A ASN A 65  ? 0.1429 0.0822 0.1192 0.0263  -0.0127 0.0202  65  ASN A O    
1170 O O    B ASN A 65  ? 0.1263 0.0805 0.1141 0.0326  -0.0209 0.0264  65  ASN A O    
1171 C CB   A ASN A 65  ? 0.1287 0.1601 0.1593 0.0047  -0.0295 0.0127  65  ASN A CB   
1172 C CB   B ASN A 65  ? 0.1306 0.1517 0.1637 -0.0040 -0.0273 0.0059  65  ASN A CB   
1173 C CG   A ASN A 65  ? 0.1739 0.1782 0.1858 0.0136  -0.0191 0.0383  65  ASN A CG   
1174 C CG   B ASN A 65  ? 0.1812 0.1735 0.1870 0.0047  -0.0150 0.0326  65  ASN A CG   
1175 O OD1  A ASN A 65  ? 0.1956 0.1916 0.1905 0.0039  -0.0039 0.0434  65  ASN A OD1  
1176 O OD1  B ASN A 65  ? 0.1593 0.1846 0.1656 -0.0162 -0.0456 0.0437  65  ASN A OD1  
1177 N ND2  A ASN A 65  ? 0.1968 0.1708 0.2168 0.0127  0.0052  0.0429  65  ASN A ND2  
1178 N ND2  B ASN A 65  ? 0.2244 0.1821 0.2282 0.0326  0.0200  0.0459  65  ASN A ND2  
1187 D DD21 A ASN A 65  ? 0.2079 0.1931 0.2585 0.0143  0.0224  0.0233  65  ASN A DD21 
1188 D DD21 B ASN A 65  ? 0.2207 0.2190 0.2692 0.0401  0.0331  0.0604  65  ASN A DD21 
1189 D DD22 A ASN A 65  ? 0.2269 0.2016 0.2829 -0.0187 0.0452  -0.0065 65  ASN A DD22 
1190 D DD22 B ASN A 65  ? 0.2675 0.2032 0.2614 0.0545  0.0399  0.0747  65  ASN A DD22 
1191 N N    . ASP A 66  ? 0.1173 0.1073 0.1315 0.0021  -0.0119 -0.0012 66  ASP A N    
1192 C CA   . ASP A 66  ? 0.1221 0.1067 0.1346 0.0073  -0.0206 -0.0026 66  ASP A CA   
1193 C C    . ASP A 66  ? 0.1302 0.0996 0.1458 0.0043  -0.0345 0.0042  66  ASP A C    
1194 O O    . ASP A 66  ? 0.1648 0.1241 0.1408 -0.0190 -0.0430 -0.0021 66  ASP A O    
1195 C CB   . ASP A 66  ? 0.1153 0.1132 0.1131 -0.0040 -0.0145 0.0124  66  ASP A CB   
1196 C CG   . ASP A 66  ? 0.1263 0.1147 0.1167 0.0103  0.0026  0.0448  66  ASP A CG   
1197 O OD1  . ASP A 66  ? 0.1200 0.1412 0.1141 -0.0016 0.0032  0.0447  66  ASP A OD1  
1198 O OD2  . ASP A 66  ? 0.1363 0.1256 0.1208 0.0195  0.0015  0.0400  66  ASP A OD2  
1199 D D    . ASP A 66  ? 0.1140 0.1462 0.1526 0.0003  -0.0103 -0.0291 66  ASP A D    
1203 N N    . GLY A 67  ? 0.1573 0.1154 0.1459 -0.0139 -0.0430 0.0046  67  GLY A N    
1204 C CA   . GLY A 67  ? 0.2096 0.1306 0.1513 0.0147  -0.0344 0.0254  67  GLY A CA   
1205 C C    . GLY A 67  ? 0.2642 0.1427 0.1601 0.0176  0.0153  0.0362  67  GLY A C    
1206 O O    . GLY A 67  ? 0.3861 0.1716 0.2629 0.0739  0.1043  0.0976  67  GLY A O    
1207 D D    . GLY A 67  ? 0.1530 0.1350 0.1765 -0.0136 -0.0487 -0.0111 67  GLY A D    
1210 N N    . ARG A 68  ? 0.2114 0.1374 0.1403 -0.0148 0.0089  0.0271  68  ARG A N    
1211 C CA   . ARG A 68  ? 0.2280 0.1311 0.1846 -0.0460 0.0329  0.0082  68  ARG A CA   
1212 C C    . ARG A 68  ? 0.2206 0.1372 0.1615 -0.0405 0.0385  0.0142  68  ARG A C    
1213 O O    . ARG A 68  ? 0.2592 0.1618 0.2960 -0.0564 0.1102  -0.0025 68  ARG A O    
1214 C CB   . ARG A 68  ? 0.2276 0.2390 0.2475 -0.1080 0.0233  -0.0487 68  ARG A CB   
1215 C CG   . ARG A 68  ? 0.3083 0.3006 0.3537 -0.1298 0.0260  -0.1382 68  ARG A CG   
1216 C CD   . ARG A 68  ? 0.3683 0.3944 0.3740 -0.1233 -0.0083 -0.1830 68  ARG A CD   
1217 N NE   . ARG A 68  ? 0.4175 0.4157 0.3702 -0.1223 -0.0279 -0.1776 68  ARG A NE   
1218 C CZ   . ARG A 68  ? 0.4838 0.4580 0.3931 -0.0653 -0.0142 -0.1571 68  ARG A CZ   
1219 N NH1  . ARG A 68  ? 0.5322 0.4729 0.4230 -0.0488 0.0242  -0.1556 68  ARG A NH1  
1220 N NH2  . ARG A 68  ? 0.4801 0.4512 0.3940 -0.0313 -0.0117 -0.1479 68  ARG A NH2  
1221 D D    . ARG A 68  ? 0.2148 0.1348 0.1465 0.0008  0.0195  0.0303  68  ARG A D    
1229 D DE   . ARG A 68  ? 0.4884 0.4891 0.3466 -0.0464 -0.0412 -0.1722 68  ARG A DE   
1230 D DH11 . ARG A 68  ? 0.6125 0.4821 0.4661 -0.0202 0.0677  -0.1439 68  ARG A DH11 
1231 D DH12 . ARG A 68  ? 0.5764 0.4858 0.4277 -0.0617 0.0531  -0.1640 68  ARG A DH12 
1232 D DH21 . ARG A 68  ? 0.4820 0.4620 0.4172 -0.0112 0.0097  -0.1371 68  ARG A DH21 
1233 D DH22 . ARG A 68  ? 0.3437 0.4160 0.3723 -0.0839 -0.0771 -0.1683 68  ARG A DH22 
1234 N N    . THR A 69  ? 0.1818 0.1283 0.1360 -0.0143 -0.0122 0.0274  69  THR A N    
1235 C CA   . THR A 69  ? 0.1490 0.1277 0.1381 -0.0218 -0.0089 0.0318  69  THR A CA   
1236 C C    . THR A 69  ? 0.1473 0.1125 0.1260 -0.0076 0.0033  0.0414  69  THR A C    
1237 O O    . THR A 69  ? 0.1575 0.2001 0.1205 0.0266  -0.0022 0.0681  69  THR A O    
1238 C CB   . THR A 69  ? 0.1289 0.1263 0.1305 0.0066  -0.0185 0.0494  69  THR A CB   
1239 O OG1  . THR A 69  ? 0.1862 0.1365 0.1350 0.0229  -0.0330 0.0322  69  THR A OG1  
1240 C CG2  . THR A 69  ? 0.1278 0.1246 0.1396 -0.0140 -0.0118 0.0319  69  THR A CG2  
1241 D D    . THR A 69  ? 0.2045 0.1186 0.2940 -0.0247 0.0475  0.0031  69  THR A D    
1244 D DG1  . THR A 69  ? 0.1390 0.1085 0.1487 -0.0290 -0.0036 0.0366  69  THR A DG1  
1248 N N    . PRO A 70  ? 0.1655 0.1411 0.1415 -0.0191 0.0252  0.0319  70  PRO A N    
1249 C CA   . PRO A 70  ? 0.1906 0.1612 0.1294 -0.0204 0.0234  0.0470  70  PRO A CA   
1250 C C    . PRO A 70  ? 0.2060 0.1564 0.1230 -0.0229 0.0370  0.0094  70  PRO A C    
1251 O O    . PRO A 70  ? 0.2300 0.1668 0.1750 -0.0228 0.0455  0.0388  70  PRO A O    
1252 C CB   . PRO A 70  ? 0.2140 0.1567 0.1528 -0.0238 0.0463  0.0243  70  PRO A CB   
1253 C CG   . PRO A 70  ? 0.1984 0.2094 0.1790 -0.0412 0.0627  0.0056  70  PRO A CG   
1254 C CD   . PRO A 70  ? 0.1636 0.1782 0.1708 -0.0205 0.0285  0.0231  70  PRO A CD   
1262 N N    . GLY A 71  ? 0.2150 0.1796 0.1494 -0.0303 0.0212  0.0085  71  GLY A N    
1263 C CA   . GLY A 71  ? 0.2563 0.1773 0.1440 -0.0392 0.0140  -0.0141 71  GLY A CA   
1264 C C    . GLY A 71  ? 0.2030 0.1467 0.1543 -0.0272 -0.0034 0.0063  71  GLY A C    
1265 O O    . GLY A 71  ? 0.2850 0.1502 0.1921 -0.0515 0.0234  -0.0183 71  GLY A O    
1266 D D    . GLY A 71  ? 0.1924 0.2019 0.2050 -0.0392 -0.0054 0.0443  71  GLY A D    
1269 N N    . SER A 72  ? 0.1820 0.1343 0.1533 -0.0432 0.0055  0.0130  72  SER A N    
1270 C CA   . SER A 72  ? 0.1731 0.1622 0.1488 -0.0325 -0.0005 0.0252  72  SER A CA   
1271 C C    . SER A 72  ? 0.1652 0.1412 0.1174 -0.0181 0.0005  0.0196  72  SER A C    
1272 O O    . SER A 72  ? 0.1924 0.1506 0.1804 -0.0212 -0.0210 0.0624  72  SER A O    
1273 C CB   . SER A 72  ? 0.1938 0.2132 0.1749 -0.0805 0.0184  -0.0199 72  SER A CB   
1274 O OG   . SER A 72  ? 0.2798 0.3031 0.1916 -0.0590 0.0671  -0.0316 72  SER A OG   
1275 D D    . SER A 72  ? 0.2944 0.1469 0.1746 -0.0769 0.0452  0.0049  72  SER A D    
1279 D DG   . SER A 72  ? 0.3835 0.3559 0.2963 0.0071  0.1461  -0.0114 72  SER A DG   
1280 N N    . ARG A 73  ? 0.1332 0.1246 0.0837 0.0006  -0.0046 0.0047  73  ARG A N    
1281 C CA   . ARG A 73  ? 0.1289 0.1358 0.0944 0.0017  -0.0053 0.0157  73  ARG A CA   
1282 C C    . ARG A 73  ? 0.1173 0.1291 0.0944 0.0048  -0.0185 0.0123  73  ARG A C    
1283 O O    . ARG A 73  ? 0.1185 0.1775 0.0799 0.0213  -0.0210 -0.0148 73  ARG A O    
1284 C CB   . ARG A 73  ? 0.1436 0.1377 0.0810 -0.0132 -0.0085 0.0114  73  ARG A CB   
1285 C CG   . ARG A 73  ? 0.1646 0.1737 0.0949 0.0044  -0.0095 -0.0127 73  ARG A CG   
1286 C CD   . ARG A 73  ? 0.2033 0.1770 0.1596 0.0089  -0.0102 -0.0302 73  ARG A CD   
1287 N NE   . ARG A 73  ? 0.2130 0.2204 0.1711 0.0532  -0.0088 -0.0393 73  ARG A NE   
1288 C CZ   . ARG A 73  ? 0.2525 0.2682 0.2692 0.0539  -0.0078 -0.1083 73  ARG A CZ   
1289 N NH1  . ARG A 73  ? 0.2678 0.2679 0.3481 0.0121  0.0018  -0.1618 73  ARG A NH1  
1290 N NH2  . ARG A 73  ? 0.3258 0.3115 0.2688 0.0747  0.0155  -0.1310 73  ARG A NH2  
1291 D D    . ARG A 73  ? 0.1280 0.1586 0.1440 -0.0098 -0.0129 0.0436  73  ARG A D    
1299 D DE   . ARG A 73  ? 0.2272 0.2492 0.1613 0.0376  0.0035  -0.0241 73  ARG A DE   
1300 D DH11 . ARG A 73  ? 0.2680 0.2486 0.3690 0.0750  -0.0802 -0.1512 73  ARG A DH11 
1301 D DH12 . ARG A 73  ? 0.2234 0.1913 0.3324 0.0994  -0.0084 -0.0615 73  ARG A DH12 
1302 D DH21 . ARG A 73  ? 0.3144 0.3478 0.3086 0.0923  -0.0345 -0.1713 73  ARG A DH21 
1303 D DH22 . ARG A 73  ? 0.3836 0.3274 0.2779 0.0546  0.0956  -0.1435 73  ARG A DH22 
1304 N N    . ASN A 74  ? 0.0975 0.1334 0.0934 -0.0014 -0.0115 0.0100  74  ASN A N    
1305 C CA   . ASN A 74  ? 0.0888 0.1350 0.0985 -0.0041 -0.0153 -0.0001 74  ASN A CA   
1306 C C    . ASN A 74  ? 0.0900 0.1200 0.1045 0.0063  -0.0059 0.0048  74  ASN A C    
1307 O O    . ASN A 74  ? 0.0968 0.0995 0.1070 0.0068  0.0028  0.0055  74  ASN A O    
1308 C CB   . ASN A 74  ? 0.1410 0.1307 0.1109 -0.0097 0.0084  0.0037  74  ASN A CB   
1309 C CG   . ASN A 74  ? 0.1185 0.1223 0.1167 -0.0135 -0.0077 -0.0126 74  ASN A CG   
1310 O OD1  . ASN A 74  ? 0.1229 0.1415 0.0961 0.0136  0.0067  -0.0228 74  ASN A OD1  
1311 N ND2  . ASN A 74  ? 0.1778 0.1418 0.1735 0.0214  0.0437  0.0045  74  ASN A ND2  
1312 D D    . ASN A 74  ? 0.1009 0.1484 0.1092 0.0087  -0.0115 -0.0031 74  ASN A D    
1316 D DD21 . ASN A 74  ? 0.1333 0.1640 0.1816 0.0152  0.0301  -0.0221 74  ASN A DD21 
1317 D DD22 . ASN A 74  ? 0.2604 0.1341 0.1934 0.0538  0.0595  0.0180  74  ASN A DD22 
1318 N N    . LEU A 75  ? 0.0898 0.1176 0.0909 0.0084  0.0016  -0.0019 75  LEU A N    
1319 C CA   . LEU A 75  ? 0.0843 0.1199 0.0952 0.0058  -0.0102 -0.0030 75  LEU A CA   
1320 C C    . LEU A 75  ? 0.0837 0.1273 0.0953 0.0078  -0.0092 0.0001  75  LEU A C    
1321 O O    . LEU A 75  ? 0.0896 0.1280 0.1043 0.0031  -0.0136 0.0204  75  LEU A O    
1322 C CB   . LEU A 75  ? 0.1222 0.1094 0.0946 -0.0049 0.0009  0.0038  75  LEU A CB   
1323 C CG   . LEU A 75  ? 0.1450 0.1270 0.0919 -0.0102 -0.0062 -0.0150 75  LEU A CG   
1324 C CD1  . LEU A 75  ? 0.1735 0.1340 0.1142 -0.0011 -0.0078 -0.0271 75  LEU A CD1  
1325 C CD2  . LEU A 75  ? 0.1746 0.1647 0.1005 0.0103  -0.0332 -0.0399 75  LEU A CD2  
1337 N N    . CYS A 76  ? 0.1010 0.1154 0.0968 -0.0078 -0.0141 0.0086  76  CYS A N    
1338 C CA   . CYS A 76  ? 0.0913 0.1077 0.0988 -0.0172 -0.0182 -0.0018 76  CYS A CA   
1339 C C    . CYS A 76  ? 0.1075 0.1214 0.0902 0.0000  -0.0192 0.0031  76  CYS A C    
1340 O O    . CYS A 76  ? 0.1338 0.1223 0.1069 0.0119  0.0029  0.0162  76  CYS A O    
1341 C CB   . CYS A 76  ? 0.0964 0.0904 0.0982 -0.0225 -0.0162 0.0075  76  CYS A CB   
1342 S SG   . CYS A 76  ? 0.1196 0.0948 0.0927 -0.0066 -0.0083 -0.0027 76  CYS A SG   
1347 N N    . ASN A 77  ? 0.1043 0.1143 0.0878 -0.0084 -0.0116 -0.0063 77  ASN A N    
1348 C CA   . ASN A 77  ? 0.0893 0.1115 0.1092 -0.0167 -0.0049 0.0071  77  ASN A CA   
1349 C C    . ASN A 77  ? 0.1006 0.1038 0.1312 -0.0054 -0.0070 -0.0123 77  ASN A C    
1350 O O    . ASN A 77  ? 0.0857 0.1415 0.1602 -0.0165 -0.0040 -0.0370 77  ASN A O    
1351 C CB   . ASN A 77  ? 0.0905 0.1283 0.1346 -0.0162 -0.0117 0.0198  77  ASN A CB   
1352 C CG   . ASN A 77  ? 0.0978 0.1531 0.1844 -0.0027 -0.0262 0.0409  77  ASN A CG   
1353 O OD1  . ASN A 77  ? 0.1113 0.1536 0.2365 0.0038  -0.0218 0.0663  77  ASN A OD1  
1354 N ND2  . ASN A 77  ? 0.1052 0.1949 0.2435 0.0209  -0.0008 0.0632  77  ASN A ND2  
1355 D D    . ASN A 77  ? 0.1976 0.1630 0.1107 0.0358  0.0327  0.0156  77  ASN A D    
1359 D DD21 . ASN A 77  ? 0.1671 0.2442 0.2943 0.0811  0.0495  0.1019  77  ASN A DD21 
1360 D DD22 . ASN A 77  ? 0.1264 0.1972 0.2652 0.0062  0.0357  0.0427  77  ASN A DD22 
1361 N N    . ILE A 78  ? 0.0918 0.1077 0.1223 -0.0014 -0.0067 -0.0064 78  ILE A N    
1362 C CA   . ILE A 78  ? 0.0952 0.1435 0.1149 -0.0035 -0.0040 -0.0145 78  ILE A CA   
1363 C C    . ILE A 78  ? 0.1023 0.1426 0.1117 -0.0104 -0.0084 -0.0130 78  ILE A C    
1364 O O    . ILE A 78  ? 0.0906 0.1579 0.1042 -0.0060 -0.0178 -0.0169 78  ILE A O    
1365 C CB   . ILE A 78  ? 0.1313 0.1381 0.1238 -0.0205 -0.0142 -0.0068 78  ILE A CB   
1366 C CG1  . ILE A 78  ? 0.1600 0.1352 0.1301 -0.0119 -0.0332 -0.0295 78  ILE A CG1  
1367 C CG2  . ILE A 78  ? 0.1596 0.1960 0.1478 -0.0242 0.0167  0.0070  78  ILE A CG2  
1368 C CD1  . ILE A 78  ? 0.1569 0.1859 0.1920 0.0085  -0.0412 0.0110  78  ILE A CD1  
1380 N N    . PRO A 79  ? 0.1000 0.1409 0.1362 0.0001  -0.0229 -0.0235 79  PRO A N    
1381 C CA   . PRO A 79  ? 0.1043 0.1033 0.1393 0.0040  -0.0167 -0.0013 79  PRO A CA   
1382 C C    . PRO A 79  ? 0.0998 0.0984 0.1289 0.0018  -0.0129 -0.0049 79  PRO A C    
1383 O O    . PRO A 79  ? 0.1107 0.1090 0.1412 0.0364  0.0132  0.0047  79  PRO A O    
1384 C CB   . PRO A 79  ? 0.1133 0.1063 0.2089 0.0091  -0.0173 -0.0295 79  PRO A CB   
1385 C CG   . PRO A 79  ? 0.1327 0.1307 0.2337 -0.0026 0.0077  -0.0632 79  PRO A CG   
1386 C CD   . PRO A 79  ? 0.1188 0.1462 0.1799 -0.0044 0.0029  -0.0389 79  PRO A CD   
1394 N N    . CYS A 80  ? 0.1025 0.1029 0.1156 0.0021  -0.0124 -0.0043 80  CYS A N    
1395 C CA   . CYS A 80  ? 0.1030 0.0845 0.1259 0.0033  0.0027  0.0025  80  CYS A CA   
1396 C C    . CYS A 80  ? 0.0894 0.0832 0.1239 0.0090  -0.0127 0.0090  80  CYS A C    
1397 O O    . CYS A 80  ? 0.1253 0.0676 0.1328 0.0194  0.0053  0.0107  80  CYS A O    
1398 C CB   . CYS A 80  ? 0.0929 0.0986 0.1315 -0.0027 -0.0013 -0.0016 80  CYS A CB   
1399 S SG   . CYS A 80  ? 0.0778 0.1026 0.1385 -0.0013 0.0042  -0.0139 80  CYS A SG   
1404 N N    . SER A 81  ? 0.0874 0.0781 0.1131 0.0012  -0.0248 0.0193  81  SER A N    
1405 C CA   . SER A 81  ? 0.1290 0.1105 0.1229 -0.0307 -0.0266 -0.0036 81  SER A CA   
1406 C C    . SER A 81  ? 0.1327 0.0904 0.1136 -0.0127 -0.0116 -0.0173 81  SER A C    
1407 O O    . SER A 81  ? 0.1484 0.1235 0.1152 -0.0047 -0.0117 -0.0163 81  SER A O    
1408 C CB   . SER A 81  ? 0.2021 0.1076 0.1235 -0.0302 -0.0043 -0.0029 81  SER A CB   
1409 O OG   . SER A 81  ? 0.2217 0.1347 0.1957 0.0258  -0.0118 -0.0284 81  SER A OG   
1410 D D    . SER A 81  ? 0.1459 0.0956 0.1316 0.0275  -0.0193 0.0361  81  SER A D    
1414 D DG   . SER A 81  ? 0.2587 0.2317 0.2165 0.0608  0.0075  -0.0266 81  SER A DG   
1415 N N    . ALA A 82  ? 0.1063 0.0853 0.1295 0.0078  -0.0031 -0.0065 82  ALA A N    
1416 C CA   . ALA A 82  ? 0.1122 0.1116 0.1253 0.0054  -0.0038 0.0022  82  ALA A CA   
1417 C C    . ALA A 82  ? 0.0964 0.1107 0.1069 -0.0048 -0.0036 0.0029  82  ALA A C    
1418 O O    . ALA A 82  ? 0.1356 0.1242 0.1226 0.0087  0.0178  0.0144  82  ALA A O    
1419 C CB   . ALA A 82  ? 0.0880 0.1444 0.1428 0.0168  0.0057  0.0112  82  ALA A CB   
1425 N N    . LEU A 83  ? 0.1104 0.0979 0.1255 0.0000  0.0131  0.0223  83  LEU A N    
1426 C CA   . LEU A 83  ? 0.1169 0.0962 0.1373 -0.0007 0.0027  0.0248  83  LEU A CA   
1427 C C    . LEU A 83  ? 0.1247 0.1031 0.1420 -0.0050 -0.0024 0.0337  83  LEU A C    
1428 O O    . LEU A 83  ? 0.2114 0.1190 0.1703 0.0218  -0.0528 0.0292  83  LEU A O    
1429 C CB   . LEU A 83  ? 0.1279 0.0993 0.1476 0.0104  0.0016  0.0191  83  LEU A CB   
1430 C CG   . LEU A 83  ? 0.1582 0.0959 0.1464 0.0159  -0.0114 0.0198  83  LEU A CG   
1431 C CD1  . LEU A 83  ? 0.1827 0.1562 0.1561 0.0169  -0.0031 -0.0020 83  LEU A CD1  
1432 C CD2  . LEU A 83  ? 0.1794 0.1365 0.1441 -0.0281 -0.0276 0.0192  83  LEU A CD2  
1444 N N    . LEU A 84  ? 0.1369 0.1052 0.1395 -0.0018 -0.0102 0.0273  84  LEU A N    
1445 C CA   . LEU A 84  ? 0.1465 0.1138 0.1338 0.0084  -0.0105 0.0218  84  LEU A CA   
1446 C C    . LEU A 84  ? 0.1944 0.1402 0.1498 -0.0069 0.0150  -0.0072 84  LEU A C    
1447 O O    . LEU A 84  ? 0.2613 0.2141 0.1656 -0.0339 -0.0193 -0.0198 84  LEU A O    
1448 C CB   . LEU A 84  ? 0.1575 0.1004 0.1320 -0.0071 -0.0155 -0.0024 84  LEU A CB   
1449 C CG   . LEU A 84  ? 0.1483 0.1156 0.1195 0.0033  -0.0206 0.0199  84  LEU A CG   
1450 C CD1  . LEU A 84  ? 0.1981 0.1082 0.1613 0.0034  0.0083  0.0297  84  LEU A CD1  
1451 C CD2  . LEU A 84  ? 0.1913 0.1265 0.1207 0.0298  0.0161  0.0477  84  LEU A CD2  
1463 N N    . SER A 85  ? 0.2107 0.1708 0.2050 -0.0179 0.0505  -0.0476 85  SER A N    
1464 C CA   . SER A 85  ? 0.1838 0.1820 0.2021 -0.0039 0.0402  -0.0392 85  SER A CA   
1465 C C    . SER A 85  ? 0.1465 0.1696 0.1877 0.0031  0.0292  -0.0633 85  SER A C    
1466 O O    . SER A 85  ? 0.1838 0.1634 0.1935 -0.0036 0.0353  -0.0672 85  SER A O    
1467 C CB   . SER A 85  ? 0.1866 0.2000 0.2020 -0.0111 0.0165  -0.0143 85  SER A CB   
1468 O OG   . SER A 85  ? 0.2441 0.2429 0.2802 -0.0769 0.0524  -0.0389 85  SER A OG   
1469 D D    . SER A 85  ? 0.2039 0.2022 0.1917 -0.0543 0.0531  -0.0207 85  SER A D    
1473 D DG   . SER A 85  ? 0.2848 0.2409 0.3088 -0.0736 0.0825  -0.0297 85  SER A DG   
1474 N N    . SER A 86  ? 0.1780 0.1668 0.1884 -0.0066 0.0196  -0.0732 86  SER A N    
1475 C CA   . SER A 86  ? 0.1745 0.2289 0.1874 0.0031  0.0024  -0.0553 86  SER A CA   
1476 C C    . SER A 86  ? 0.1637 0.1994 0.1557 0.0258  0.0116  -0.0309 86  SER A C    
1477 O O    . SER A 86  ? 0.2231 0.2143 0.1639 0.0541  0.0186  -0.0170 86  SER A O    
1478 C CB   . SER A 86  ? 0.2442 0.2927 0.2121 0.0171  -0.0610 -0.0830 86  SER A CB   
1479 O OG   . SER A 86  ? 0.2900 0.3065 0.2785 -0.0223 -0.0521 -0.1114 86  SER A OG   
1480 D D    . SER A 86  ? 0.3008 0.1707 0.2230 0.0072  0.0511  -0.0822 86  SER A D    
1484 D DG   . SER A 86  ? 0.3702 0.3104 0.3450 -0.0334 -0.0006 -0.1272 86  SER A DG   
1485 N N    A ASP A 87  ? 0.1726 0.1662 0.1524 0.0192  0.0033  -0.0456 87  ASP A N    
1486 N N    B ASP A 87  ? 0.1678 0.1782 0.1459 0.0208  0.0048  -0.0490 87  ASP A N    
1487 C CA   A ASP A 87  ? 0.1663 0.1801 0.1468 0.0205  0.0073  -0.0411 87  ASP A CA   
1488 C CA   B ASP A 87  ? 0.1653 0.1780 0.1393 0.0209  0.0107  -0.0351 87  ASP A CA   
1489 C C    A ASP A 87  ? 0.1628 0.1577 0.1292 0.0050  0.0081  -0.0221 87  ASP A C    
1490 C C    B ASP A 87  ? 0.1680 0.1595 0.1348 0.0015  0.0122  -0.0267 87  ASP A C    
1491 O O    A ASP A 87  ? 0.2005 0.1798 0.1406 -0.0556 0.0071  -0.0183 87  ASP A O    
1492 O O    B ASP A 87  ? 0.2020 0.1634 0.1379 -0.0439 0.0063  -0.0310 87  ASP A O    
1493 C CB   A ASP A 87  ? 0.1765 0.1994 0.1742 0.0355  0.0187  -0.0308 87  ASP A CB   
1494 C CB   B ASP A 87  ? 0.1701 0.1892 0.1615 0.0276  0.0206  -0.0258 87  ASP A CB   
1495 C CG   A ASP A 87  ? 0.1601 0.2157 0.1778 0.0392  0.0272  -0.0216 87  ASP A CG   
1496 C CG   B ASP A 87  ? 0.1665 0.1992 0.1651 0.0355  0.0156  -0.0286 87  ASP A CG   
1497 O OD1  A ASP A 87  ? 0.2231 0.2685 0.2272 0.0092  0.0679  -0.0049 87  ASP A OD1  
1498 O OD1  B ASP A 87  ? 0.1857 0.2163 0.1726 0.0341  0.0024  -0.0620 87  ASP A OD1  
1499 O OD2  A ASP A 87  ? 0.1850 0.2542 0.1943 0.0363  0.0150  -0.0622 87  ASP A OD2  
1500 O OD2  B ASP A 87  ? 0.1706 0.2043 0.1842 0.0453  0.0277  -0.0091 87  ASP A OD2  
1501 D D    A ASP A 87  ? 0.1634 0.1746 0.1697 0.0338  0.0210  -0.0330 87  ASP A D    
1502 D D    B ASP A 87  ? 0.1513 0.1831 0.1433 0.0183  0.0150  -0.0414 87  ASP A D    
1509 N N    . ILE A 88  ? 0.1477 0.1594 0.1218 0.0045  0.0086  -0.0172 88  ILE A N    
1510 C CA   . ILE A 88  ? 0.1543 0.1608 0.1217 0.0159  -0.0049 -0.0230 88  ILE A CA   
1511 C C    . ILE A 88  ? 0.1511 0.1239 0.1210 0.0094  -0.0060 0.0014  88  ILE A C    
1512 O O    . ILE A 88  ? 0.1418 0.1391 0.1246 -0.0037 -0.0057 -0.0111 88  ILE A O    
1513 C CB   . ILE A 88  ? 0.1888 0.1728 0.0984 0.0335  -0.0324 -0.0243 88  ILE A CB   
1514 C CG1  . ILE A 88  ? 0.2117 0.1754 0.1135 0.0370  -0.0205 0.0020  88  ILE A CG1  
1515 C CG2  . ILE A 88  ? 0.1912 0.2361 0.1386 0.0521  -0.0444 -0.0447 88  ILE A CG2  
1516 C CD1  . ILE A 88  ? 0.2424 0.1828 0.1151 0.0466  -0.0450 0.0059  88  ILE A CD1  
1517 D D    . ILE A 88  ? 0.2281 0.1674 0.1260 0.0201  0.0259  -0.0097 88  ILE A D    
1528 N N    . THR A 89  ? 0.1518 0.1208 0.1390 -0.0006 -0.0123 -0.0248 89  THR A N    
1529 C CA   . THR A 89  ? 0.1285 0.1853 0.1387 -0.0189 0.0053  -0.0151 89  THR A CA   
1530 C C    . THR A 89  ? 0.1420 0.1464 0.1360 0.0149  -0.0061 -0.0032 89  THR A C    
1531 O O    . THR A 89  ? 0.1200 0.1481 0.1386 0.0037  0.0237  -0.0101 89  THR A O    
1532 C CB   . THR A 89  ? 0.1526 0.2685 0.1607 0.0210  -0.0115 -0.0641 89  THR A CB   
1533 O OG1  . THR A 89  ? 0.2101 0.3056 0.1556 0.0383  -0.0006 -0.0829 89  THR A OG1  
1534 C CG2  . THR A 89  ? 0.1476 0.3384 0.1895 0.0332  -0.0206 -0.0793 89  THR A CG2  
1535 D D    . THR A 89  ? 0.1778 0.1540 0.1650 0.0051  -0.0048 -0.0537 89  THR A D    
1538 D DG1  . THR A 89  ? 0.2434 0.3241 0.1834 0.0462  -0.0166 -0.1112 89  THR A DG1  
1542 N N    . ALA A 90  ? 0.1432 0.1352 0.1221 0.0144  -0.0182 -0.0142 90  ALA A N    
1543 C CA   . ALA A 90  ? 0.1199 0.1097 0.1255 0.0134  -0.0335 -0.0107 90  ALA A CA   
1544 C C    . ALA A 90  ? 0.1112 0.0976 0.1090 0.0028  -0.0199 0.0063  90  ALA A C    
1545 O O    . ALA A 90  ? 0.1322 0.1178 0.1053 0.0232  -0.0291 0.0078  90  ALA A O    
1546 C CB   . ALA A 90  ? 0.1678 0.1068 0.1462 0.0144  -0.0076 -0.0104 90  ALA A CB   
1547 D D    . ALA A 90  ? 0.1550 0.1549 0.1294 0.0029  0.0090  -0.0290 90  ALA A D    
1552 N N    . SER A 91  ? 0.1066 0.1185 0.1074 0.0047  -0.0163 0.0108  91  SER A N    
1553 C CA   . SER A 91  ? 0.1085 0.1278 0.1003 0.0073  -0.0159 0.0091  91  SER A CA   
1554 C C    . SER A 91  ? 0.1000 0.1214 0.1184 0.0130  -0.0154 0.0030  91  SER A C    
1555 O O    . SER A 91  ? 0.1357 0.1177 0.1211 0.0205  -0.0087 0.0034  91  SER A O    
1556 C CB   . SER A 91  ? 0.0993 0.1631 0.1205 0.0032  -0.0199 0.0141  91  SER A CB   
1557 O OG   . SER A 91  ? 0.1042 0.1765 0.1724 -0.0109 -0.0097 0.0072  91  SER A OG   
1558 D D    . SER A 91  ? 0.1565 0.1521 0.1159 0.0526  -0.0430 -0.0062 91  SER A D    
1562 D DG   . SER A 91  ? 0.1235 0.1812 0.1776 -0.0105 -0.0327 -0.0045 91  SER A DG   
1563 N N    . VAL A 92  ? 0.1182 0.1237 0.1031 0.0018  -0.0223 0.0066  92  VAL A N    
1564 C CA   . VAL A 92  ? 0.1446 0.1198 0.1000 -0.0028 -0.0146 0.0021  92  VAL A CA   
1565 C C    . VAL A 92  ? 0.1236 0.1188 0.1104 -0.0034 -0.0089 -0.0036 92  VAL A C    
1566 O O    . VAL A 92  ? 0.1032 0.1297 0.1118 -0.0003 -0.0115 -0.0100 92  VAL A O    
1567 C CB   . VAL A 92  ? 0.2145 0.1405 0.1062 -0.0368 0.0007  0.0032  92  VAL A CB   
1568 C CG1  . VAL A 92  ? 0.2241 0.1719 0.1391 -0.0600 0.0177  -0.0036 92  VAL A CG1  
1569 C CG2  . VAL A 92  ? 0.2603 0.1432 0.1020 -0.0330 -0.0130 0.0079  92  VAL A CG2  
1579 N N    . ASN A 93  ? 0.1124 0.1291 0.1109 0.0052  0.0006  0.0041  93  ASN A N    
1580 C CA   . ASN A 93  ? 0.1088 0.1379 0.1244 -0.0122 -0.0120 0.0006  93  ASN A CA   
1581 C C    . ASN A 93  ? 0.1116 0.1106 0.1179 -0.0030 -0.0200 0.0057  93  ASN A C    
1582 O O    . ASN A 93  ? 0.1330 0.1179 0.1199 -0.0115 -0.0273 0.0092  93  ASN A O    
1583 C CB   . ASN A 93  ? 0.1158 0.1911 0.1438 0.0318  -0.0265 -0.0056 93  ASN A CB   
1584 C CG   . ASN A 93  ? 0.1341 0.2892 0.1867 0.0467  0.0078  -0.0201 93  ASN A CG   
1585 O OD1  . ASN A 93  ? 0.1992 0.3176 0.1676 0.0557  0.0470  0.0042  93  ASN A OD1  
1586 N ND2  . ASN A 93  ? 0.1974 0.3051 0.2112 0.0580  0.0194  -0.0465 93  ASN A ND2  
1591 D DD21 . ASN A 93  ? 0.2404 0.3630 0.2492 0.1170  0.0563  -0.0185 93  ASN A DD21 
1592 D DD22 . ASN A 93  ? 0.2006 0.2962 0.2571 0.0453  -0.0030 -0.0380 93  ASN A DD22 
1593 N N    . CYS A 94  ? 0.1157 0.1189 0.1089 -0.0032 -0.0117 0.0053  94  CYS A N    
1594 C CA   . CYS A 94  ? 0.1163 0.1178 0.1047 -0.0054 -0.0180 0.0031  94  CYS A CA   
1595 C C    . CYS A 94  ? 0.1130 0.1156 0.1106 -0.0064 -0.0253 0.0019  94  CYS A C    
1596 O O    . CYS A 94  ? 0.1398 0.1124 0.1152 -0.0182 -0.0317 -0.0019 94  CYS A O    
1597 C CB   . CYS A 94  ? 0.0988 0.1093 0.1037 0.0021  -0.0275 0.0065  94  CYS A CB   
1598 S SG   . CYS A 94  ? 0.1145 0.1150 0.1148 -0.0045 -0.0165 0.0144  94  CYS A SG   
1603 N N    . ALA A 95  ? 0.0857 0.1069 0.1056 -0.0098 -0.0117 -0.0019 95  ALA A N    
1604 C CA   . ALA A 95  ? 0.1045 0.1132 0.1062 0.0033  -0.0138 -0.0063 95  ALA A CA   
1605 C C    . ALA A 95  ? 0.1212 0.1081 0.1235 -0.0063 -0.0209 -0.0050 95  ALA A C    
1606 O O    . ALA A 95  ? 0.1387 0.1072 0.1326 -0.0094 -0.0188 -0.0086 95  ALA A O    
1607 C CB   . ALA A 95  ? 0.1118 0.1276 0.1040 0.0119  -0.0112 -0.0042 95  ALA A CB   
1613 N N    . LYS A 96  ? 0.1236 0.1244 0.1349 -0.0222 -0.0096 -0.0122 96  LYS A N    
1614 C CA   . LYS A 96  ? 0.1341 0.1187 0.1404 -0.0296 -0.0134 0.0051  96  LYS A CA   
1615 C C    . LYS A 96  ? 0.0998 0.1503 0.1427 -0.0332 -0.0160 0.0116  96  LYS A C    
1616 O O    . LYS A 96  ? 0.1572 0.1597 0.1313 -0.0618 -0.0155 0.0201  96  LYS A O    
1617 C CB   . LYS A 96  ? 0.1251 0.1290 0.1443 -0.0354 -0.0171 0.0105  96  LYS A CB   
1618 C CG   . LYS A 96  ? 0.1403 0.1695 0.1413 -0.0460 -0.0147 0.0090  96  LYS A CG   
1619 C CD   . LYS A 96  ? 0.1271 0.2241 0.1520 -0.0405 -0.0194 0.0202  96  LYS A CD   
1620 C CE   . LYS A 96  ? 0.2793 0.2357 0.1552 -0.0036 0.0378  0.0167  96  LYS A CE   
1621 N NZ   . LYS A 96  ? 0.3456 0.2581 0.2226 0.0056  0.0934  -0.0231 96  LYS A NZ   
1632 D DZ1  . LYS A 96  ? 0.3111 0.3070 0.2501 0.0210  0.1089  -0.0506 96  LYS A DZ1  
1633 D DZ2  . LYS A 96  ? 0.3774 0.2779 0.2250 0.0459  0.0965  -0.0242 96  LYS A DZ2  
1634 D DZ3  . LYS A 96  ? 0.4079 0.2593 0.2625 0.0213  0.1336  -0.0119 96  LYS A DZ3  
1635 N N    . LYS A 97  ? 0.1064 0.1448 0.1279 -0.0230 -0.0184 0.0005  97  LYS A N    
1636 C CA   . LYS A 97  ? 0.1407 0.1475 0.1266 -0.0370 -0.0369 -0.0033 97  LYS A CA   
1637 C C    . LYS A 97  ? 0.1691 0.1584 0.1144 -0.0293 -0.0267 0.0016  97  LYS A C    
1638 O O    . LYS A 97  ? 0.2032 0.1904 0.1178 0.0085  -0.0523 -0.0064 97  LYS A O    
1639 C CB   . LYS A 97  ? 0.2223 0.1437 0.1250 -0.0426 -0.0096 -0.0042 97  LYS A CB   
1640 C CG   . LYS A 97  ? 0.2441 0.2120 0.1546 -0.0401 -0.0159 0.0449  97  LYS A CG   
1641 C CD   . LYS A 97  ? 0.2956 0.3411 0.2210 -0.0345 -0.0902 -0.0129 97  LYS A CD   
1642 C CE   . LYS A 97  ? 0.4045 0.4556 0.2375 0.0399  -0.1299 -0.0017 97  LYS A CE   
1643 N NZ   . LYS A 97  ? 0.4166 0.5129 0.3054 0.0591  -0.1789 -0.0190 97  LYS A NZ   
1654 D DZ1  . LYS A 97  ? 0.4288 0.5138 0.3430 0.0423  -0.2043 -0.0351 97  LYS A DZ1  
1655 D DZ2  . LYS A 97  ? 0.4073 0.5064 0.3783 0.0272  -0.1331 -0.0009 97  LYS A DZ2  
1656 D DZ3  . LYS A 97  ? 0.4470 0.5613 0.3223 0.0868  -0.1928 -0.0013 97  LYS A DZ3  
1657 N N    . ILE A 98  ? 0.1585 0.1326 0.0973 -0.0253 -0.0119 0.0066  98  ILE A N    
1658 C CA   . ILE A 98  ? 0.1865 0.1358 0.1208 -0.0234 0.0142  -0.0010 98  ILE A CA   
1659 C C    . ILE A 98  ? 0.2224 0.1391 0.1329 -0.0285 0.0226  -0.0115 98  ILE A C    
1660 O O    . ILE A 98  ? 0.2926 0.1595 0.1412 -0.0191 0.0338  -0.0256 98  ILE A O    
1661 C CB   . ILE A 98  ? 0.1687 0.1293 0.1035 -0.0084 0.0305  0.0082  98  ILE A CB   
1662 C CG1  . ILE A 98  ? 0.1448 0.1294 0.1274 -0.0081 0.0237  0.0180  98  ILE A CG1  
1663 C CG2  . ILE A 98  ? 0.2143 0.1495 0.1592 0.0291  0.0540  0.0131  98  ILE A CG2  
1664 C CD1  . ILE A 98  ? 0.1420 0.1489 0.1593 -0.0275 0.0181  0.0284  98  ILE A CD1  
1676 N N    A VAL A 99  ? 0.2324 0.1368 0.1449 -0.0336 0.0226  -0.0046 99  VAL A N    
1677 N N    B VAL A 99  ? 0.2048 0.1324 0.1397 -0.0308 0.0154  -0.0070 99  VAL A N    
1678 C CA   A VAL A 99  ? 0.2505 0.1379 0.1662 -0.0363 0.0155  -0.0047 99  VAL A CA   
1679 C CA   B VAL A 99  ? 0.2461 0.1409 0.1598 -0.0429 0.0153  -0.0138 99  VAL A CA   
1680 C C    A VAL A 99  ? 0.2740 0.1585 0.1752 -0.0476 0.0004  -0.0174 99  VAL A C    
1681 C C    B VAL A 99  ? 0.2648 0.1455 0.1795 -0.0585 0.0031  -0.0221 99  VAL A C    
1682 O O    A VAL A 99  ? 0.3042 0.1656 0.1856 -0.0632 0.0031  -0.0274 99  VAL A O    
1683 O O    B VAL A 99  ? 0.3075 0.1690 0.2262 -0.0710 -0.0166 -0.0520 99  VAL A O    
1684 C CB   A VAL A 99  ? 0.2717 0.1327 0.1765 -0.0307 0.0242  0.0031  99  VAL A CB   
1685 C CB   B VAL A 99  ? 0.2854 0.1378 0.1778 -0.0174 0.0213  0.0060  99  VAL A CB   
1686 C CG1  A VAL A 99  ? 0.2871 0.1391 0.1829 -0.0204 0.0272  0.0015  99  VAL A CG1  
1687 C CG1  B VAL A 99  ? 0.2926 0.1414 0.1866 -0.0214 0.0341  0.0059  99  VAL A CG1  
1688 C CG2  A VAL A 99  ? 0.2851 0.1377 0.1674 -0.0149 0.0158  0.0068  99  VAL A CG2  
1689 C CG2  B VAL A 99  ? 0.2917 0.1150 0.1756 -0.0045 0.0176  0.0198  99  VAL A CG2  
1708 N N    . SER A 100 ? 0.2670 0.2068 0.1744 -0.0264 -0.0253 -0.0232 100 SER A N    
1709 C CA   . SER A 100 ? 0.2706 0.2253 0.1875 -0.0688 -0.0400 -0.0425 100 SER A CA   
1710 C C    . SER A 100 ? 0.3022 0.2245 0.1839 -0.0580 -0.0500 -0.0333 100 SER A C    
1711 O O    . SER A 100 ? 0.3502 0.2991 0.1850 -0.1156 -0.0387 -0.0486 100 SER A O    
1712 C CB   . SER A 100 ? 0.2463 0.2908 0.2008 -0.0410 -0.0737 -0.0662 100 SER A CB   
1713 O OG   . SER A 100 ? 0.3296 0.3283 0.1983 -0.0071 -0.0564 -0.0815 100 SER A OG   
1718 D DG   . SER A 100 ? 0.3513 0.3290 0.2015 -0.0149 -0.0707 -0.0743 100 SER A DG   
1719 N N    . ASP A 101 ? 0.2705 0.2175 0.1627 -0.0293 -0.0554 -0.0199 101 ASP A N    
1720 C CA   . ASP A 101 ? 0.2739 0.2039 0.1554 0.0036  -0.0625 -0.0151 101 ASP A CA   
1721 C C    . ASP A 101 ? 0.3077 0.2334 0.1949 0.0412  -0.0246 0.0155  101 ASP A C    
1722 O O    . ASP A 101 ? 0.3873 0.2938 0.3551 0.0665  0.0918  0.0600  101 ASP A O    
1723 C CB   . ASP A 101 ? 0.2271 0.2215 0.1574 0.0026  -0.0745 0.0049  101 ASP A CB   
1724 C CG   . ASP A 101 ? 0.2230 0.2094 0.1692 -0.0051 -0.0678 0.0102  101 ASP A CG   
1725 O OD1  . ASP A 101 ? 0.2323 0.1888 0.2646 -0.0011 -0.0967 0.0151  101 ASP A OD1  
1726 O OD2  . ASP A 101 ? 0.2155 0.2123 0.1886 -0.0109 -0.0241 0.0108  101 ASP A OD2  
1727 D D    . ASP A 101 ? 0.2324 0.2284 0.1528 -0.0214 -0.0391 -0.0287 101 ASP A D    
1731 D DD2  . ASP A 101 ? 0.1910 0.2033 0.1912 -0.0305 -0.0174 0.0201  101 ASP A DD2  
1732 N N    . GLY A 102 ? 0.3160 0.2182 0.2423 0.0272  -0.0212 -0.0197 102 GLY A N    
1733 C CA   . GLY A 102 ? 0.3183 0.2594 0.2448 0.0279  -0.0803 -0.0795 102 GLY A CA   
1734 C C    . GLY A 102 ? 0.3329 0.2936 0.2542 0.0702  -0.0674 -0.0760 102 GLY A C    
1735 O O    . GLY A 102 ? 0.4350 0.3264 0.2900 0.1456  -0.0577 -0.0897 102 GLY A O    
1736 D D    . GLY A 102 ? 0.5169 0.1975 0.3897 0.0711  0.1466  0.0356  102 GLY A D    
1739 N N    . ASN A 103 ? 0.3064 0.2608 0.2458 0.0674  -0.0720 -0.0438 103 ASN A N    
1740 C CA   . ASN A 103 ? 0.2923 0.2594 0.2241 0.0658  -0.0387 -0.0066 103 ASN A CA   
1741 C C    . ASN A 103 ? 0.3186 0.2568 0.2060 0.0509  -0.0318 -0.0195 103 ASN A C    
1742 O O    . ASN A 103 ? 0.3184 0.2561 0.2839 0.0162  0.0114  -0.0176 103 ASN A O    
1743 C CB   . ASN A 103 ? 0.2580 0.2882 0.2405 0.0412  -0.0271 0.0017  103 ASN A CB   
1744 C CG   . ASN A 103 ? 0.3457 0.3002 0.2673 0.0504  0.0499  0.0149  103 ASN A CG   
1745 O OD1  . ASN A 103 ? 0.4723 0.3801 0.3422 0.0838  0.1437  0.0175  103 ASN A OD1  
1746 N ND2  . ASN A 103 ? 0.3631 0.2847 0.2493 0.0448  0.0335  0.0263  103 ASN A ND2  
1747 D D    . ASN A 103 ? 0.3187 0.3930 0.2404 0.1269  -0.1019 -0.0819 103 ASN A D    
1751 D DD21 . ASN A 103 ? 0.3954 0.3002 0.2199 0.0287  0.0070  0.0146  103 ASN A DD21 
1752 D DD22 . ASN A 103 ? 0.3790 0.1774 0.2080 0.0115  0.0069  -0.0330 103 ASN A DD22 
1753 N N    . GLY A 104 ? 0.3202 0.2697 0.1636 0.0519  -0.0657 -0.0309 104 GLY A N    
1754 C CA   . GLY A 104 ? 0.2430 0.2184 0.1721 -0.0367 -0.0491 -0.0216 104 GLY A CA   
1755 C C    . GLY A 104 ? 0.2026 0.1954 0.1531 -0.0434 -0.0205 0.0019  104 GLY A C    
1756 O O    . GLY A 104 ? 0.3068 0.1991 0.1287 -0.0604 -0.0176 0.0042  104 GLY A O    
1757 D D    . GLY A 104 ? 0.3502 0.3044 0.1522 0.0967  -0.0620 -0.0108 104 GLY A D    
1760 N N    . MET A 105 ? 0.1633 0.1635 0.1336 -0.0575 -0.0002 -0.0098 105 MET A N    
1761 C CA   . MET A 105 ? 0.1620 0.1231 0.1532 -0.0499 -0.0079 -0.0118 105 MET A CA   
1762 C C    . MET A 105 ? 0.1642 0.1573 0.1587 -0.0402 -0.0044 -0.0066 105 MET A C    
1763 O O    . MET A 105 ? 0.1340 0.1269 0.1742 -0.0105 0.0086  -0.0222 105 MET A O    
1764 C CB   . MET A 105 ? 0.1437 0.1691 0.1481 -0.0205 -0.0100 -0.0099 105 MET A CB   
1765 C CG   . MET A 105 ? 0.1226 0.1999 0.1409 -0.0251 -0.0262 -0.0159 105 MET A CG   
1766 S SD   . MET A 105 ? 0.1400 0.1693 0.1369 -0.0319 -0.0251 -0.0281 105 MET A SD   
1767 C CE   . MET A 105 ? 0.1512 0.1570 0.1415 -0.0317 -0.0226 -0.0271 105 MET A CE   
1768 D D    . MET A 105 ? 0.1690 0.1767 0.1637 -0.0778 -0.0312 -0.0030 105 MET A D    
1777 N N    . ASN A 106 ? 0.1904 0.1945 0.1759 -0.0546 0.0093  -0.0323 106 ASN A N    
1778 C CA   . ASN A 106 ? 0.2227 0.2460 0.2007 -0.0445 0.0445  -0.0270 106 ASN A CA   
1779 C C    . ASN A 106 ? 0.1785 0.2598 0.1675 -0.0318 0.0338  0.0008  106 ASN A C    
1780 O O    . ASN A 106 ? 0.1898 0.3141 0.2482 -0.0543 0.0600  -0.0043 106 ASN A O    
1781 C CB   . ASN A 106 ? 0.3232 0.3028 0.2424 -0.0251 0.0713  -0.0773 106 ASN A CB   
1785 D D    . ASN A 106 ? 0.2618 0.2917 0.1993 -0.1250 0.0282  -0.0790 106 ASN A D    
1791 N N    . ALA A 107 ? 0.1604 0.2797 0.1526 -0.0268 -0.0401 -0.0133 107 ALA A N    
1792 C CA   . ALA A 107 ? 0.1934 0.2843 0.1387 -0.0034 -0.0399 0.0288  107 ALA A CA   
1793 C C    . ALA A 107 ? 0.1654 0.2023 0.1415 -0.0101 -0.0198 0.0540  107 ALA A C    
1794 O O    . ALA A 107 ? 0.2735 0.2336 0.1599 -0.0554 0.0070  0.0679  107 ALA A O    
1795 C CB   . ALA A 107 ? 0.1990 0.3167 0.1646 0.0097  -0.0554 0.0176  107 ALA A CB   
1796 D D    . ALA A 107 ? 0.1562 0.2990 0.1895 -0.0232 -0.0376 -0.0058 107 ALA A D    
1801 N N    . TRP A 108 ? 0.1348 0.1609 0.1240 0.0091  -0.0064 0.0273  108 TRP A N    
1802 C CA   . TRP A 108 ? 0.1441 0.1321 0.1396 0.0110  -0.0125 0.0226  108 TRP A CA   
1803 C C    . TRP A 108 ? 0.1324 0.1179 0.1304 -0.0043 -0.0159 0.0053  108 TRP A C    
1804 O O    . TRP A 108 ? 0.1077 0.1166 0.1814 -0.0054 -0.0302 0.0078  108 TRP A O    
1805 C CB   . TRP A 108 ? 0.1357 0.1114 0.1352 -0.0009 -0.0161 0.0106  108 TRP A CB   
1806 C CG   . TRP A 108 ? 0.1445 0.1098 0.1239 0.0094  -0.0301 0.0163  108 TRP A CG   
1807 C CD1  . TRP A 108 ? 0.1569 0.1338 0.1740 0.0075  -0.0299 -0.0312 108 TRP A CD1  
1808 C CD2  . TRP A 108 ? 0.1443 0.1149 0.1404 0.0100  -0.0115 -0.0183 108 TRP A CD2  
1809 N NE1  . TRP A 108 ? 0.1688 0.1235 0.1649 0.0089  -0.0138 -0.0316 108 TRP A NE1  
1810 C CE2  . TRP A 108 ? 0.1538 0.1143 0.1282 0.0145  -0.0004 -0.0081 108 TRP A CE2  
1811 C CE3  . TRP A 108 ? 0.1457 0.1172 0.2035 -0.0078 0.0049  -0.0060 108 TRP A CE3  
1812 C CZ2  . TRP A 108 ? 0.1570 0.1141 0.1483 0.0209  0.0059  0.0138  108 TRP A CZ2  
1813 C CZ3  . TRP A 108 ? 0.1454 0.1360 0.2174 -0.0070 0.0126  -0.0143 108 TRP A CZ3  
1814 C CH2  . TRP A 108 ? 0.1519 0.1419 0.1755 0.0057  0.0234  -0.0038 108 TRP A CH2  
1820 D DE1  . TRP A 108 ? 0.2017 0.1215 0.2117 0.0187  -0.0411 -0.0336 108 TRP A DE1  
1825 N N    . VAL A 109 ? 0.1482 0.1142 0.1403 0.0086  0.0055  0.0177  109 VAL A N    
1826 C CA   . VAL A 109 ? 0.1542 0.1562 0.1711 0.0259  0.0185  0.0204  109 VAL A CA   
1827 C C    . VAL A 109 ? 0.0961 0.1739 0.1795 0.0258  0.0101  0.0117  109 VAL A C    
1828 O O    . VAL A 109 ? 0.1338 0.1853 0.1650 0.0458  0.0171  0.0153  109 VAL A O    
1829 C CB   . VAL A 109 ? 0.1760 0.1878 0.2171 0.0047  0.0459  0.0196  109 VAL A CB   
1830 C CG1  . VAL A 109 ? 0.2207 0.2270 0.2951 -0.0377 0.0494  -0.0200 109 VAL A CG1  
1831 C CG2  . VAL A 109 ? 0.1666 0.2575 0.2690 0.0218  0.0479  0.0007  109 VAL A CG2  
1832 D D    . VAL A 109 ? 0.1669 0.1169 0.1871 0.0059  0.0205  0.0232  109 VAL A D    
1841 N N    . ALA A 110 ? 0.1332 0.1505 0.1702 0.0273  0.0063  0.0291  110 ALA A N    
1842 C CA   . ALA A 110 ? 0.1407 0.1423 0.1753 0.0337  -0.0045 0.0217  110 ALA A CA   
1843 C C    . ALA A 110 ? 0.1633 0.1458 0.1425 0.0115  -0.0156 0.0113  110 ALA A C    
1844 O O    . ALA A 110 ? 0.1443 0.1729 0.1676 0.0075  -0.0216 0.0352  110 ALA A O    
1845 C CB   . ALA A 110 ? 0.1852 0.1499 0.1938 0.0009  -0.0169 0.0051  110 ALA A CB   
1846 D D    . ALA A 110 ? 0.1071 0.1489 0.1622 0.0157  -0.0329 0.0096  110 ALA A D    
1851 N N    . TRP A 111 ? 0.1560 0.1428 0.1325 0.0237  -0.0026 0.0390  111 TRP A N    
1852 C CA   . TRP A 111 ? 0.1436 0.1340 0.1677 0.0369  0.0086  0.0496  111 TRP A CA   
1853 C C    . TRP A 111 ? 0.1355 0.1286 0.1673 0.0409  -0.0016 0.0557  111 TRP A C    
1854 O O    . TRP A 111 ? 0.1182 0.1256 0.2053 0.0347  -0.0044 0.0578  111 TRP A O    
1855 C CB   . TRP A 111 ? 0.1473 0.1281 0.1768 0.0410  0.0089  0.0372  111 TRP A CB   
1856 C CG   . TRP A 111 ? 0.1447 0.1441 0.1673 0.0256  0.0106  0.0270  111 TRP A CG   
1857 C CD1  . TRP A 111 ? 0.1402 0.1669 0.1668 0.0208  0.0156  0.0223  111 TRP A CD1  
1858 C CD2  . TRP A 111 ? 0.1315 0.1540 0.1709 0.0256  0.0219  0.0176  111 TRP A CD2  
1859 N NE1  . TRP A 111 ? 0.1617 0.1625 0.1790 0.0189  0.0275  0.0300  111 TRP A NE1  
1860 C CE2  . TRP A 111 ? 0.1393 0.1510 0.1889 0.0192  0.0180  0.0200  111 TRP A CE2  
1861 C CE3  . TRP A 111 ? 0.1888 0.1425 0.1725 0.0506  0.0203  0.0159  111 TRP A CE3  
1862 C CZ2  . TRP A 111 ? 0.1980 0.1369 0.2161 0.0213  0.0143  0.0164  111 TRP A CZ2  
1863 C CZ3  . TRP A 111 ? 0.2270 0.1540 0.1879 0.0495  0.0079  0.0009  111 TRP A CZ3  
1864 C CH2  . TRP A 111 ? 0.2102 0.1553 0.2207 0.0263  0.0106  -0.0097 111 TRP A CH2  
1870 D DE1  . TRP A 111 ? 0.2505 0.2042 0.2097 -0.0168 0.0594  0.0384  111 TRP A DE1  
1875 N N    . ARG A 112 ? 0.1170 0.1596 0.1677 0.0184  0.0049  0.0386  112 ARG A N    
1876 C CA   . ARG A 112 ? 0.1458 0.1914 0.1988 0.0270  0.0075  0.0097  112 ARG A CA   
1877 C C    . ARG A 112 ? 0.1546 0.1709 0.2355 0.0349  -0.0050 -0.0097 112 ARG A C    
1878 O O    . ARG A 112 ? 0.1803 0.1672 0.2496 0.0299  0.0061  -0.0172 112 ARG A O    
1879 C CB   . ARG A 112 ? 0.2309 0.2963 0.1883 0.0764  0.0289  0.0226  112 ARG A CB   
1880 C CG   . ARG A 112 ? 0.3629 0.4400 0.2080 0.1318  -0.0310 -0.0357 112 ARG A CG   
1881 C CD   . ARG A 112 ? 0.4952 0.5010 0.2065 0.1473  -0.0243 0.0019  112 ARG A CD   
1882 N NE   . ARG A 112 ? 0.5576 0.5366 0.3209 0.1498  0.0415  0.0544  112 ARG A NE   
1883 C CZ   . ARG A 112 ? 0.6405 0.5510 0.3805 0.1843  0.1061  0.0859  112 ARG A CZ   
1884 N NH1  . ARG A 112 ? 0.6524 0.5495 0.4021 0.1933  0.1036  0.0826  112 ARG A NH1  
1885 N NH2  . ARG A 112 ? 0.6546 0.5705 0.4014 0.1717  0.1138  0.0976  112 ARG A NH2  
1887 D D    B ARG A 112 ? 0.1907 0.1670 0.1247 0.0186  -0.0275 0.0320  112 ARG A D    
1895 D DE   . ARG A 112 ? 0.5305 0.5256 0.4365 0.1172  0.0276  0.0555  112 ARG A DE   
1896 D DH11 . ARG A 112 ? 0.6410 0.5351 0.4023 0.1690  0.0658  0.0700  112 ARG A DH11 
1897 D DH12 . ARG A 112 ? 0.5444 0.4871 0.3815 0.1052  0.0569  0.0283  112 ARG A DH12 
1898 D DH21 . ARG A 112 ? 0.6535 0.5953 0.4002 0.1656  0.1180  0.1097  112 ARG A DH21 
1899 D DH22 . ARG A 112 ? 0.6648 0.5848 0.4124 0.1548  0.1083  0.1065  112 ARG A DH22 
1900 N N    A ASN A 113 ? 0.1495 0.1549 0.2330 0.0511  -0.0154 -0.0082 113 ASN A N    
1901 N N    B ASN A 113 ? 0.1515 0.1570 0.2335 0.0485  -0.0147 -0.0085 113 ASN A N    
1902 C CA   A ASN A 113 ? 0.1492 0.1734 0.2434 0.0558  -0.0103 -0.0082 113 ASN A CA   
1903 C CA   B ASN A 113 ? 0.1493 0.1743 0.2428 0.0503  -0.0095 -0.0083 113 ASN A CA   
1904 C C    A ASN A 113 ? 0.1189 0.1631 0.2420 0.0214  -0.0342 -0.0231 113 ASN A C    
1905 C C    B ASN A 113 ? 0.1295 0.1674 0.2425 0.0283  -0.0313 -0.0174 113 ASN A C    
1906 O O    A ASN A 113 ? 0.1573 0.1791 0.2409 0.0535  -0.0402 -0.0361 113 ASN A O    
1907 O O    B ASN A 113 ? 0.1553 0.1537 0.2268 0.0340  -0.0572 -0.0495 113 ASN A O    
1908 C CB   A ASN A 113 ? 0.1525 0.1976 0.2590 0.0431  -0.0091 -0.0003 113 ASN A CB   
1909 C CB   B ASN A 113 ? 0.1566 0.1993 0.2626 0.0351  -0.0005 -0.0020 113 ASN A CB   
1910 C CG   A ASN A 113 ? 0.2022 0.2318 0.2616 0.0364  0.0117  0.0062  113 ASN A CG   
1911 C CG   B ASN A 113 ? 0.2015 0.2302 0.2675 0.0229  0.0181  -0.0015 113 ASN A CG   
1912 O OD1  A ASN A 113 ? 0.2310 0.2503 0.2447 0.0137  0.0182  0.0123  113 ASN A OD1  
1913 O OD1  B ASN A 113 ? 0.2185 0.2444 0.2729 0.0316  0.0299  -0.0024 113 ASN A OD1  
1914 N ND2  A ASN A 113 ? 0.2193 0.2431 0.2673 0.0230  0.0235  0.0040  113 ASN A ND2  
1915 N ND2  B ASN A 113 ? 0.2305 0.2418 0.2609 0.0297  0.0227  0.0083  113 ASN A ND2  
1924 D DD21 A ASN A 113 ? 0.2641 0.2581 0.2771 0.0106  0.0449  -0.0019 113 ASN A DD21 
1925 D DD21 B ASN A 113 ? 0.2294 0.2461 0.2595 0.0107  0.0255  0.0122  113 ASN A DD21 
1926 D DD22 A ASN A 113 ? 0.2522 0.2642 0.2794 -0.0091 0.0396  -0.0117 113 ASN A DD22 
1927 D DD22 B ASN A 113 ? 0.2705 0.2452 0.2630 0.0478  0.0220  0.0112  113 ASN A DD22 
1928 N N    . ARG A 114 ? 0.1413 0.1750 0.2318 0.0557  -0.0199 0.0204  114 ARG A N    
1929 C CA   . ARG A 114 ? 0.1265 0.1712 0.2335 0.0461  -0.0273 0.0242  114 ARG A CA   
1930 C C    . ARG A 114 ? 0.1403 0.1727 0.2272 0.0429  -0.0356 0.0418  114 ARG A C    
1931 O O    . ARG A 114 ? 0.1776 0.2668 0.2205 0.0571  -0.0351 0.0524  114 ARG A O    
1932 C CB   . ARG A 114 ? 0.1231 0.2010 0.2556 0.0266  -0.0391 0.0133  114 ARG A CB   
1933 C CG   . ARG A 114 ? 0.1237 0.2412 0.2711 -0.0070 -0.0334 -0.0162 114 ARG A CG   
1934 C CD   . ARG A 114 ? 0.1262 0.2768 0.2897 -0.0058 -0.0346 -0.0497 114 ARG A CD   
1935 N NE   . ARG A 114 ? 0.1469 0.3063 0.2705 0.0179  -0.0370 -0.0677 114 ARG A NE   
1936 C CZ   . ARG A 114 ? 0.1257 0.3629 0.2431 -0.0090 -0.0142 -0.0584 114 ARG A CZ   
1937 N NH1  . ARG A 114 ? 0.1244 0.3651 0.2428 -0.0437 -0.0014 -0.0667 114 ARG A NH1  
1938 N NH2  . ARG A 114 ? 0.1766 0.4217 0.2538 0.0443  -0.0344 -0.0681 114 ARG A NH2  
1947 D DE   . ARG A 114 ? 0.2321 0.3003 0.2685 0.0216  -0.0527 -0.0499 114 ARG A DE   
1948 D DH11 . ARG A 114 ? 0.1824 0.4286 0.2540 -0.0758 -0.0119 -0.0957 114 ARG A DH11 
1949 D DH12 . ARG A 114 ? 0.1260 0.3589 0.2808 -0.0560 0.0071  -0.0212 114 ARG A DH12 
1950 D DH21 . ARG A 114 ? 0.2082 0.4348 0.2809 0.0390  -0.0663 -0.0606 114 ARG A DH21 
1951 D DH22 . ARG A 114 ? 0.2264 0.4201 0.2419 0.0474  -0.0665 -0.0490 114 ARG A DH22 
1952 N N    . CYS A 115 ? 0.1322 0.1382 0.2011 0.0463  -0.0154 0.0232  115 CYS A N    
1953 C CA   . CYS A 115 ? 0.1429 0.1363 0.1716 0.0396  -0.0202 0.0130  115 CYS A CA   
1954 C C    . CYS A 115 ? 0.1839 0.1229 0.1481 0.0315  0.0144  0.0181  115 CYS A C    
1955 O O    . CYS A 115 ? 0.2021 0.1439 0.1709 0.0271  0.0428  0.0330  115 CYS A O    
1956 C CB   . CYS A 115 ? 0.1337 0.1132 0.1839 0.0222  -0.0073 0.0163  115 CYS A CB   
1957 S SG   . CYS A 115 ? 0.1439 0.1190 0.1570 0.0101  0.0043  0.0211  115 CYS A SG   
1958 D D    A CYS A 115 ? 0.1123 0.1099 0.1896 0.0418  -0.0117 0.0061  115 CYS A D    
1963 N N    . LYS A 116 ? 0.2044 0.1451 0.1514 0.0121  0.0009  0.0180  116 LYS A N    
1964 C CA   . LYS A 116 ? 0.2288 0.1458 0.1656 0.0081  0.0106  0.0069  116 LYS A CA   
1965 C C    . LYS A 116 ? 0.3094 0.1592 0.1572 0.0466  0.0166  0.0023  116 LYS A C    
1966 O O    . LYS A 116 ? 0.3100 0.1840 0.2253 0.0846  0.0278  0.0293  116 LYS A O    
1967 C CB   . LYS A 116 ? 0.2400 0.1645 0.1594 0.0508  0.0096  -0.0031 116 LYS A CB   
1968 C CG   . LYS A 116 ? 0.2362 0.1458 0.1687 0.0659  0.0125  -0.0019 116 LYS A CG   
1969 C CD   . LYS A 116 ? 0.2345 0.1745 0.1615 0.0421  -0.0133 0.0054  116 LYS A CD   
1970 C CE   . LYS A 116 ? 0.2979 0.2135 0.1870 0.0296  -0.0020 -0.0305 116 LYS A CE   
1971 N NZ   . LYS A 116 ? 0.2870 0.2449 0.1854 0.0433  0.0091  -0.0442 116 LYS A NZ   
1982 D DZ1  . LYS A 116 ? 0.2872 0.2677 0.2116 0.0413  0.0167  -0.0363 116 LYS A DZ1  
1983 D DZ2  . LYS A 116 ? 0.3348 0.2600 0.2096 0.0257  0.0400  -0.0660 116 LYS A DZ2  
1984 D DZ3  . LYS A 116 ? 0.2927 0.2577 0.1843 0.0458  0.0212  -0.0196 116 LYS A DZ3  
1985 N N    . GLY A 117 ? 0.3624 0.1519 0.2037 0.0541  0.0516  0.0196  117 GLY A N    
1986 C CA   . GLY A 117 ? 0.4555 0.1614 0.2100 0.1079  0.0732  0.0073  117 GLY A CA   
1987 C C    . GLY A 117 ? 0.4473 0.1861 0.2138 0.1479  0.0904  0.0277  117 GLY A C    
1988 O O    . GLY A 117 ? 0.4759 0.1961 0.2473 0.1750  0.0783  0.0337  117 GLY A O    
1989 D D    . GLY A 117 ? 0.3561 0.1428 0.2056 0.0218  0.0326  0.0398  117 GLY A D    
1992 N N    . THR A 118 ? 0.3453 0.1957 0.2017 0.1343  0.0458  0.0211  118 THR A N    
1993 C CA   . THR A 118 ? 0.2875 0.2197 0.2147 0.1331  0.0346  0.0561  118 THR A CA   
1994 C C    . THR A 118 ? 0.2912 0.2187 0.2119 0.1169  0.0339  0.0574  118 THR A C    
1995 O O    . THR A 118 ? 0.2911 0.1742 0.2375 0.0927  0.0289  0.0714  118 THR A O    
1996 C CB   . THR A 118 ? 0.2565 0.2590 0.2181 0.1177  0.0283  0.0500  118 THR A CB   
1997 O OG1  . THR A 118 ? 0.2749 0.2416 0.2344 0.1070  0.0279  0.0175  118 THR A OG1  
1998 C CG2  . THR A 118 ? 0.2737 0.3119 0.2569 0.1012  0.0553  0.0521  118 THR A CG2  
2000 D D    B THR A 118 ? 0.3214 0.1762 0.1767 0.0987  0.0061  0.0048  118 THR A D    
2003 D DG1  . THR A 118 ? 0.2510 0.2070 0.2340 0.1136  0.0392  0.0152  118 THR A DG1  
2007 N N    . ASP A 119 ? 0.3312 0.2789 0.2096 0.1530  0.0353  0.0619  119 ASP A N    
2008 C CA   . ASP A 119 ? 0.3650 0.2729 0.2295 0.1368  0.0600  0.0735  119 ASP A CA   
2009 C C    . ASP A 119 ? 0.2937 0.2650 0.2042 0.1065  0.0547  0.0658  119 ASP A C    
2010 O O    . ASP A 119 ? 0.2764 0.2940 0.2052 0.1315  0.0316  0.0683  119 ASP A O    
2011 C CB   . ASP A 119 ? 0.4963 0.3272 0.2420 0.2009  0.0795  0.1106  119 ASP A CB   
2012 C CG   . ASP A 119 ? 0.6007 0.3787 0.2790 0.1965  0.1480  0.1242  119 ASP A CG   
2013 O OD1  . ASP A 119 ? 0.6040 0.4318 0.3087 0.2261  0.2018  0.1687  119 ASP A OD1  
2014 O OD2  . ASP A 119 ? 0.6178 0.3720 0.2875 0.1700  0.1455  0.1321  119 ASP A OD2  
2015 D D    . ASP A 119 ? 0.3390 0.2634 0.2169 0.1613  0.0283  0.0845  119 ASP A D    
2019 N N    . VAL A 120 ? 0.3074 0.2071 0.1930 0.0750  0.0280  0.0375  120 VAL A N    
2020 C CA   . VAL A 120 ? 0.2923 0.2028 0.1849 0.0697  0.0121  0.0367  120 VAL A CA   
2021 C C    . VAL A 120 ? 0.2638 0.1909 0.1821 0.0601  -0.0002 0.0277  120 VAL A C    
2022 O O    . VAL A 120 ? 0.2283 0.1870 0.1837 0.0944  -0.0383 0.0342  120 VAL A O    
2023 C CB   . VAL A 120 ? 0.2311 0.1570 0.1813 0.0187  0.0105  0.0243  120 VAL A CB   
2024 C CG1  . VAL A 120 ? 0.2475 0.1915 0.1975 0.0261  0.0259  0.0500  120 VAL A CG1  
2025 C CG2  . VAL A 120 ? 0.2669 0.1103 0.2203 -0.0001 0.0171  0.0191  120 VAL A CG2  
2026 D D    . VAL A 120 ? 0.3379 0.2291 0.2352 0.0718  0.0180  0.0003  120 VAL A D    
2035 N N    . GLN A 121 ? 0.2720 0.2000 0.2012 0.0527  0.0045  0.0320  121 GLN A N    
2036 C CA   . GLN A 121 ? 0.2799 0.2147 0.2038 0.0712  0.0129  0.0508  121 GLN A CA   
2037 C C    . GLN A 121 ? 0.2853 0.1916 0.1940 0.0896  0.0133  0.0465  121 GLN A C    
2038 O O    . GLN A 121 ? 0.2796 0.1587 0.1937 0.0426  0.0398  0.0609  121 GLN A O    
2039 C CB   . GLN A 121 ? 0.3391 0.2655 0.2555 0.0077  0.0444  0.0424  121 GLN A CB   
2044 D D    . GLN A 121 ? 0.2871 0.1998 0.2314 0.0439  0.0201  0.0218  121 GLN A D    
2052 N N    . ALA A 122 ? 0.2866 0.1688 0.1909 0.0998  0.0049  0.0305  122 ALA A N    
2053 C CA   . ALA A 122 ? 0.3033 0.2149 0.1762 0.1165  -0.0164 0.0378  122 ALA A CA   
2054 C C    . ALA A 122 ? 0.2516 0.2108 0.1518 0.0892  -0.0316 0.0331  122 ALA A C    
2055 O O    . ALA A 122 ? 0.3842 0.2501 0.1474 0.1377  -0.0461 0.0223  122 ALA A O    
2056 C CB   . ALA A 122 ? 0.2934 0.2437 0.1803 0.1520  -0.0432 0.0692  122 ALA A CB   
2057 D D    . ALA A 122 ? 0.2988 0.2616 0.1951 0.1257  -0.0100 0.0018  122 ALA A D    
2062 N N    A TRP A 123 ? 0.2230 0.1956 0.1449 0.0589  -0.0214 0.0390  123 TRP A N    
2063 N N    B TRP A 123 ? 0.2256 0.1969 0.1451 0.0629  -0.0214 0.0379  123 TRP A N    
2064 C CA   A TRP A 123 ? 0.2505 0.1945 0.1443 0.0564  -0.0101 0.0406  123 TRP A CA   
2065 C CA   B TRP A 123 ? 0.2520 0.1951 0.1456 0.0537  -0.0091 0.0422  123 TRP A CA   
2066 C C    A TRP A 123 ? 0.2525 0.1764 0.1446 0.0488  -0.0074 0.0417  123 TRP A C    
2067 C C    B TRP A 123 ? 0.2491 0.1740 0.1436 0.0472  -0.0129 0.0366  123 TRP A C    
2068 O O    A TRP A 123 ? 0.2709 0.1678 0.1149 0.0404  0.0122  0.0618  123 TRP A O    
2069 O O    B TRP A 123 ? 0.2487 0.1834 0.1604 0.0437  -0.0241 0.0246  123 TRP A O    
2070 C CB   A TRP A 123 ? 0.2581 0.2012 0.1470 0.0612  -0.0061 0.0463  123 TRP A CB   
2071 C CB   B TRP A 123 ? 0.2536 0.2014 0.1449 0.0593  -0.0125 0.0439  123 TRP A CB   
2072 C CG   A TRP A 123 ? 0.2631 0.2076 0.1573 0.0638  0.0022  0.0574  123 TRP A CG   
2073 C CG   B TRP A 123 ? 0.2692 0.2082 0.1591 0.0637  0.0062  0.0581  123 TRP A CG   
2074 C CD1  A TRP A 123 ? 0.2750 0.2118 0.1637 0.0557  0.0196  0.0556  123 TRP A CD1  
2075 C CD1  B TRP A 123 ? 0.2751 0.2140 0.1587 0.0644  0.0150  0.0568  123 TRP A CD1  
2076 C CD2  A TRP A 123 ? 0.2690 0.2022 0.1647 0.0517  0.0176  0.0634  123 TRP A CD2  
2077 C CD2  B TRP A 123 ? 0.2737 0.2093 0.1716 0.0527  0.0223  0.0599  123 TRP A CD2  
2078 N NE1  A TRP A 123 ? 0.2797 0.2167 0.1763 0.0506  0.0280  0.0522  123 TRP A NE1  
2079 N NE1  B TRP A 123 ? 0.2810 0.2253 0.1799 0.0540  0.0256  0.0498  123 TRP A NE1  
2080 C CE2  A TRP A 123 ? 0.2774 0.2048 0.1782 0.0496  0.0291  0.0608  123 TRP A CE2  
2081 C CE2  B TRP A 123 ? 0.2815 0.2121 0.1753 0.0529  0.0276  0.0582  123 TRP A CE2  
2082 C CE3  A TRP A 123 ? 0.2761 0.2020 0.1945 0.0315  0.0434  0.0496  123 TRP A CE3  
2083 C CE3  B TRP A 123 ? 0.2775 0.2023 0.1933 0.0337  0.0431  0.0515  123 TRP A CE3  
2084 C CZ2  A TRP A 123 ? 0.2792 0.2073 0.1925 0.0457  0.0387  0.0528  123 TRP A CZ2  
2085 C CZ2  B TRP A 123 ? 0.2767 0.2070 0.1852 0.0602  0.0262  0.0600  123 TRP A CZ2  
2086 C CZ3  A TRP A 123 ? 0.2790 0.1994 0.1974 0.0253  0.0553  0.0522  123 TRP A CZ3  
2087 C CZ3  B TRP A 123 ? 0.2797 0.1953 0.1887 0.0317  0.0515  0.0643  123 TRP A CZ3  
2088 C CH2  A TRP A 123 ? 0.2818 0.2153 0.2030 0.0327  0.0533  0.0438  123 TRP A CH2  
2089 C CH2  B TRP A 123 ? 0.2751 0.2063 0.1894 0.0528  0.0352  0.0582  123 TRP A CH2  
2100 D DE1  A TRP A 123 ? 0.2825 0.2270 0.1835 0.0564  0.0308  0.0496  123 TRP A DE1  
2101 D DE1  B TRP A 123 ? 0.2787 0.2435 0.2176 0.0293  0.0472  0.0218  123 TRP A DE1  
2110 N N    . ILE A 124 ? 0.2473 0.1647 0.1374 0.0525  -0.0178 0.0396  124 ILE A N    
2111 C CA   . ILE A 124 ? 0.2612 0.1920 0.1624 0.0454  0.0052  0.0391  124 ILE A CA   
2112 C C    . ILE A 124 ? 0.2769 0.1631 0.1573 -0.0002 -0.0075 0.0300  124 ILE A C    
2113 O O    . ILE A 124 ? 0.2774 0.1401 0.1863 -0.0429 0.0141  0.0259  124 ILE A O    
2114 C CB   . ILE A 124 ? 0.2575 0.2314 0.1594 0.0692  0.0082  0.0211  124 ILE A CB   
2115 C CG1  . ILE A 124 ? 0.2566 0.2634 0.2204 0.0469  0.0049  -0.0230 124 ILE A CG1  
2116 C CG2  . ILE A 124 ? 0.2730 0.2858 0.1336 0.1175  0.0293  0.0222  124 ILE A CG2  
2117 C CD1  . ILE A 124 ? 0.2583 0.3263 0.2483 0.0412  0.0007  -0.0261 124 ILE A CD1  
2129 N N    . ARG A 125 ? 0.3333 0.1571 0.1616 0.0256  -0.0203 0.0167  125 ARG A N    
2130 C CA   . ARG A 125 ? 0.4194 0.1294 0.1772 0.0245  -0.0197 0.0175  125 ARG A CA   
2131 C C    . ARG A 125 ? 0.4309 0.1039 0.1695 0.0038  -0.0311 0.0398  125 ARG A C    
2132 O O    . ARG A 125 ? 0.4180 0.1160 0.1947 0.0052  -0.0341 0.0423  125 ARG A O    
2133 C CB   . ARG A 125 ? 0.8182 0.1841 0.2795 0.2089  0.1876  0.0903  125 ARG A CB   
2134 C CG   . ARG A 125 ? 1.3280 0.3406 0.4806 0.4971  0.4671  0.2676  125 ARG A CG   
2135 C CD   . ARG A 125 ? 1.8855 0.4276 0.6604 0.7943  0.8137  0.4161  125 ARG A CD   
2136 N NE   . ARG A 125 ? 2.0014 0.4454 0.6617 0.8149  0.8406  0.3952  125 ARG A NE   
2137 C CZ   . ARG A 125 ? 2.0703 0.5125 0.7027 0.8419  0.9022  0.3984  125 ARG A CZ   
2138 N NH1  . ARG A 125 ? 2.0643 0.5466 0.7076 0.8163  0.9314  0.3451  125 ARG A NH1  
2139 N NH2  . ARG A 125 ? 2.0326 0.5497 0.6953 0.8273  0.9035  0.4002  125 ARG A NH2  
2148 D DE   . ARG A 125 ? 2.0084 0.5433 0.6150 0.8000  0.8142  0.3490  125 ARG A DE   
2149 D DH11 . ARG A 125 ? 2.0809 0.5636 0.7382 0.8314  0.9414  0.3394  125 ARG A DH11 
2150 D DH12 . ARG A 125 ? 2.0993 0.6028 0.7514 0.8378  0.9121  0.2960  125 ARG A DH12 
2151 D DH21 . ARG A 125 ? 1.8918 0.5397 0.6550 0.8129  0.8128  0.4057  125 ARG A DH21 
2152 D DH22 . ARG A 125 ? 1.9867 0.6147 0.6683 0.8528  0.9394  0.4155  125 ARG A DH22 
2153 N N    . GLY A 126 ? 0.4541 0.1115 0.1744 -0.0190 -0.0211 0.0188  126 GLY A N    
2154 C CA   . GLY A 126 ? 0.4857 0.1316 0.1714 -0.0173 -0.0200 0.0166  126 GLY A CA   
2155 C C    . GLY A 126 ? 0.5114 0.1565 0.1839 0.0070  -0.0057 0.0015  126 GLY A C    
2156 O O    . GLY A 126 ? 0.5887 0.1848 0.1882 0.0326  -0.0074 -0.0113 126 GLY A O    
2157 D D    . GLY A 126 ? 0.4755 0.1729 0.1955 -0.0570 0.0060  -0.0073 126 GLY A D    
2160 N N    . CYS A 127 ? 0.4658 0.1511 0.1765 0.0047  0.0288  0.0249  127 CYS A N    
2161 C CA   . CYS A 127 ? 0.4121 0.1336 0.2237 -0.0276 0.0494  0.0271  127 CYS A CA   
2162 C C    . CYS A 127 ? 0.4305 0.1939 0.2915 -0.0229 0.0838  0.0753  127 CYS A C    
2163 O O    . CYS A 127 ? 0.4010 0.2315 0.4231 -0.0323 0.1159  0.0226  127 CYS A O    
2164 C CB   . CYS A 127 ? 0.3562 0.1056 0.2219 -0.0344 0.0250  0.0171  127 CYS A CB   
2165 S SG   . CYS A 127 ? 0.3571 0.0863 0.2124 -0.0189 0.0312  0.0088  127 CYS A SG   
2166 D D    . CYS A 127 ? 0.3759 0.1736 0.1713 -0.0072 0.0375  0.0213  127 CYS A D    
2170 N N    . ARG A 128 ? 0.3885 0.2442 0.3033 -0.0150 0.0756  0.0435  128 ARG A N    
2171 C CA   . ARG A 128 ? 0.3700 0.3519 0.3913 -0.0157 0.0508  0.0115  128 ARG A CA   
2172 C C    . ARG A 128 ? 0.4034 0.3796 0.4081 0.0044  0.0269  -0.0005 128 ARG A C    
2173 O O    . ARG A 128 ? 0.3649 0.3864 0.3968 0.0346  0.0491  0.0088  128 ARG A O    
2181 D D    . ARG A 128 ? 0.3708 0.2340 0.2805 0.0045  0.0794  0.0370  128 ARG A D    
2258 O O    . DOD L .   ? 0.1129 0.2980 0.1401 -0.0022 -0.0872 -0.0621 302 DOD A O    
2259 D D1   . DOD L .   ? 0.1578 0.2546 0.1302 0.0367  -0.0848 -0.0431 302 DOD A D1   
2260 D D2   . DOD L .   ? 0.1662 0.3131 0.1689 0.0365  -0.0372 -0.0427 302 DOD A D2   
2283 O O    . DOD L .   ? 0.1504 0.2122 0.1633 0.0662  0.0051  0.0226  315 DOD A O    
2284 D D1   . DOD L .   ? 0.1557 0.2041 0.1672 0.0661  -0.0003 0.0268  315 DOD A D1   
2285 D D2   . DOD L .   ? 0.1316 0.2403 0.1814 0.0697  0.0031  0.0392  315 DOD A D2   
2322 O O    . DOD L .   ? 0.2483 0.1994 0.1959 0.0157  -0.0348 0.0235  332 DOD A O    
2323 D D1   . DOD L .   ? 0.2556 0.2168 0.2030 0.0443  -0.0126 0.0257  332 DOD A D1   
2324 D D2   . DOD L .   ? 0.1804 0.1913 0.1529 -0.0069 -0.0493 0.0344  332 DOD A D2   
2328 O O    . DOD L .   ? 0.3168 0.2743 0.2616 0.0164  0.0325  0.0166  334 DOD A O    
2329 D D1   . DOD L .   ? 0.3024 0.2692 0.2454 0.0502  -0.0018 0.0279  334 DOD A D1   
2330 D D2   . DOD L .   ? 0.3041 0.2773 0.2616 -0.0119 0.0205  0.0125  334 DOD A D2   
2344 O O    . DOD L .   ? 0.1425 0.1254 0.1304 -0.0112 -0.0052 0.0267  340 DOD A O    
2345 D D1   . DOD L .   ? 0.1474 0.1370 0.1567 -0.0051 0.0013  0.0138  340 DOD A D1   
2346 D D2   . DOD L .   ? 0.1899 0.1464 0.1296 0.0260  -0.0105 0.0228  340 DOD A D2   
2351 O O    . DOD L .   ? 0.1512 0.2194 0.1997 0.0067  0.0050  -0.0770 343 DOD A O    
2352 D D1   . DOD L .   ? 0.1401 0.1676 0.2286 0.0230  0.0069  -0.0274 343 DOD A D1   
2353 D D2   . DOD L .   ? 0.1837 0.2247 0.2456 0.0117  0.0110  -0.0920 343 DOD A D2   
2355 O O    . DOD L .   ? 0.1771 0.1847 0.1043 0.0431  -0.0200 -0.0017 345 DOD A O    
2356 D D1   . DOD L .   ? 0.1822 0.2117 0.1051 0.0186  -0.0170 -0.0027 345 DOD A D1   
2357 D D2   . DOD L .   ? 0.1484 0.2467 0.1076 0.0135  -0.0274 -0.0146 345 DOD A D2   
2358 O O    . DOD L .   ? 0.1510 0.2639 0.2350 -0.0343 0.0227  -0.0827 346 DOD A O    
2359 D D1   . DOD L .   ? 0.2308 0.3161 0.2365 0.0454  0.0032  -0.1185 346 DOD A D1   
2360 D D2   . DOD L .   ? 0.2245 0.3558 0.2529 0.0462  -0.0434 -0.1650 346 DOD A D2   
2361 O O    . DOD L .   ? 0.1840 0.1209 0.1500 0.0443  0.0018  0.0489  347 DOD A O    
2362 D D1   . DOD L .   ? 0.1825 0.1177 0.1195 0.0359  0.0004  0.0501  347 DOD A D1   
2363 D D2   . DOD L .   ? 0.1099 0.1449 0.1482 0.0040  -0.0338 0.0436  347 DOD A D2   
2364 O O    . DOD L .   ? 0.1807 0.2222 0.1494 0.0385  -0.0389 -0.0695 348 DOD A O    
2365 D D1   . DOD L .   ? 0.2345 0.2288 0.1779 0.0534  -0.0491 -0.0792 348 DOD A D1   
2366 D D2   . DOD L .   ? 0.1629 0.2316 0.1505 0.0126  -0.0342 -0.0527 348 DOD A D2   
2377 O O    . DOD L .   ? 0.2993 0.2856 0.2459 0.0534  0.0333  0.0054  353 DOD A O    
2378 D D1   . DOD L .   ? 0.1744 0.1792 0.2297 -0.0360 0.0408  0.0359  353 DOD A D1   
2379 D D2   . DOD L .   ? 0.2602 0.2852 0.2292 0.0706  0.0491  -0.0103 353 DOD A D2   
2381 O O    . DOD L .   ? 0.2652 0.1851 0.2381 0.0864  0.0376  -0.0302 355 DOD A O    
2382 D D1   . DOD L .   ? 0.2741 0.2567 0.2195 0.0549  0.0410  -0.0329 355 DOD A D1   
2383 D D2   . DOD L .   ? 0.2710 0.2278 0.2353 0.0514  0.0291  -0.0439 355 DOD A D2   
2443 O O    . DOD L .   ? 0.1714 0.1219 0.1733 0.0065  -0.0146 -0.0134 379 DOD A O    
2444 D D1   . DOD L .   ? 0.1782 0.1394 0.1745 -0.0037 -0.0295 -0.0112 379 DOD A D1   
2445 D D2   . DOD L .   ? 0.1693 0.1407 0.1466 0.0030  -0.0180 -0.0113 379 DOD A D2   
# 
