data_8RLF
# 
_entry.id   8RLF 
# 
_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   8RLF         pdb_00008rlf 10.2210/pdb8rlf/pdb 
WWPDB D_1292133897 ?            ?                   
# 
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                        8RLF 
_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    108 ?        ? ? ? 
# 
_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         HOH 
# 
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 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
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 HOH 1   301 366 HOH HOH A . 
L 4 HOH 2   302 356 HOH HOH A . 
L 4 HOH 3   303 352 HOH HOH A . 
L 4 HOH 4   304 400 HOH HOH A . 
L 4 HOH 5   305 340 HOH HOH A . 
L 4 HOH 6   306 399 HOH HOH A . 
L 4 HOH 7   307 398 HOH HOH A . 
L 4 HOH 8   308 327 HOH HOH A . 
L 4 HOH 9   309 320 HOH HOH A . 
L 4 HOH 10  310 370 HOH HOH A . 
L 4 HOH 11  311 334 HOH HOH A . 
L 4 HOH 12  312 335 HOH HOH A . 
L 4 HOH 13  313 303 HOH HOH A . 
L 4 HOH 14  314 393 HOH HOH A . 
L 4 HOH 15  315 379 HOH HOH A . 
L 4 HOH 16  316 329 HOH HOH A . 
L 4 HOH 17  317 338 HOH HOH A . 
L 4 HOH 18  318 351 HOH HOH A . 
L 4 HOH 19  319 365 HOH HOH A . 
L 4 HOH 20  320 394 HOH HOH A . 
L 4 HOH 21  321 310 HOH HOH A . 
L 4 HOH 22  322 336 HOH HOH A . 
L 4 HOH 23  323 361 HOH HOH A . 
L 4 HOH 24  324 337 HOH HOH A . 
L 4 HOH 25  325 328 HOH HOH A . 
L 4 HOH 26  326 317 HOH HOH A . 
L 4 HOH 27  327 385 HOH HOH A . 
L 4 HOH 28  328 316 HOH HOH A . 
L 4 HOH 29  329 368 HOH HOH A . 
L 4 HOH 30  330 354 HOH HOH A . 
L 4 HOH 31  331 383 HOH HOH A . 
L 4 HOH 32  332 308 HOH HOH A . 
L 4 HOH 33  333 306 HOH HOH A . 
L 4 HOH 34  334 348 HOH HOH A . 
L 4 HOH 35  335 312 HOH HOH A . 
L 4 HOH 36  336 377 HOH HOH A . 
L 4 HOH 37  337 373 HOH HOH A . 
L 4 HOH 38  338 397 HOH HOH A . 
L 4 HOH 39  339 362 HOH HOH A . 
L 4 HOH 40  340 382 HOH HOH A . 
L 4 HOH 41  341 357 HOH HOH A . 
L 4 HOH 42  342 305 HOH HOH A . 
L 4 HOH 43  343 359 HOH HOH A . 
L 4 HOH 44  344 372 HOH HOH A . 
L 4 HOH 45  345 347 HOH HOH A . 
L 4 HOH 46  346 324 HOH HOH A . 
L 4 HOH 47  347 315 HOH HOH A . 
L 4 HOH 48  348 314 HOH HOH A . 
L 4 HOH 49  349 355 HOH HOH A . 
L 4 HOH 50  350 323 HOH HOH A . 
L 4 HOH 51  351 402 HOH HOH A . 
L 4 HOH 52  352 371 HOH HOH A . 
L 4 HOH 53  353 391 HOH HOH A . 
L 4 HOH 54  354 313 HOH HOH A . 
L 4 HOH 55  355 326 HOH HOH A . 
L 4 HOH 56  356 380 HOH HOH A . 
L 4 HOH 57  357 309 HOH HOH A . 
L 4 HOH 58  358 325 HOH HOH A . 
L 4 HOH 59  359 330 HOH HOH A . 
L 4 HOH 60  360 301 HOH HOH A . 
L 4 HOH 61  361 376 HOH HOH A . 
L 4 HOH 62  362 367 HOH HOH A . 
L 4 HOH 63  363 353 HOH HOH A . 
L 4 HOH 64  364 346 HOH HOH A . 
L 4 HOH 65  365 307 HOH HOH A . 
L 4 HOH 66  366 389 HOH HOH A . 
L 4 HOH 67  367 378 HOH HOH A . 
L 4 HOH 68  368 304 HOH HOH A . 
L 4 HOH 69  369 319 HOH HOH A . 
L 4 HOH 70  370 343 HOH HOH A . 
L 4 HOH 71  371 322 HOH HOH A . 
L 4 HOH 72  372 390 HOH HOH A . 
L 4 HOH 73  373 318 HOH HOH A . 
L 4 HOH 74  374 381 HOH HOH A . 
L 4 HOH 75  375 302 HOH HOH A . 
L 4 HOH 76  376 349 HOH HOH A . 
L 4 HOH 77  377 332 HOH HOH A . 
L 4 HOH 78  378 350 HOH HOH A . 
L 4 HOH 79  379 384 HOH HOH A . 
L 4 HOH 80  380 358 HOH HOH A . 
L 4 HOH 81  381 392 HOH HOH A . 
L 4 HOH 82  382 344 HOH HOH A . 
L 4 HOH 83  383 401 HOH HOH A . 
L 4 HOH 84  384 374 HOH HOH A . 
L 4 HOH 85  385 375 HOH HOH A . 
L 4 HOH 86  386 386 HOH HOH A . 
L 4 HOH 87  387 345 HOH HOH A . 
L 4 HOH 88  388 321 HOH HOH A . 
L 4 HOH 89  389 388 HOH HOH A . 
L 4 HOH 90  390 341 HOH HOH A . 
L 4 HOH 91  391 408 HOH HOH A . 
L 4 HOH 92  392 395 HOH HOH A . 
L 4 HOH 93  393 311 HOH HOH A . 
L 4 HOH 94  394 333 HOH HOH A . 
L 4 HOH 95  395 406 HOH HOH A . 
L 4 HOH 96  396 396 HOH HOH A . 
L 4 HOH 97  397 339 HOH HOH A . 
L 4 HOH 98  398 404 HOH HOH A . 
L 4 HOH 99  399 403 HOH HOH A . 
L 4 HOH 100 400 405 HOH HOH A . 
L 4 HOH 101 401 363 HOH HOH A . 
L 4 HOH 102 402 387 HOH HOH A . 
L 4 HOH 103 403 342 HOH HOH A . 
L 4 HOH 104 404 369 HOH HOH A . 
L 4 HOH 105 405 331 HOH HOH A . 
L 4 HOH 106 406 360 HOH HOH A . 
L 4 HOH 107 407 364 HOH HOH A . 
L 4 HOH 108 408 407 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? SHELX  ? ? ? . 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? . 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? . 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? . 4 
# 
_cell.angle_alpha                  88.52 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   71.37 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  68.16 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RLF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     27.250 
_cell.length_a_esd                 ? 
_cell.length_b                     31.930 
_cell.length_b_esd                 ? 
_cell.length_c                     34.270 
_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                         8RLF 
_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                   8RLF 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.82 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          32.41 
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-09-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.688 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID29' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.688 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RLF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              0.96 
_reflns.d_resolution_low                               21.67 
_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                                     61660 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.131 
_reflns.pdbx_Rpim_I_all                                0.050 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.963 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.121 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    0.96 
_reflns_shell.d_res_low                                     0.99 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6128 
_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                               5.7 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.530 
_reflns_shell.pdbx_Rpim_I_all                               0.221 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.866 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.481 
_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                                 8RLF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            0.96 
_refine.ls_d_res_low                             21.67 
_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                     58579 
_refine.ls_number_reflns_R_free                  3081 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1236 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.0973 
_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                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1001 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             108 
_refine_hist.number_atoms_total               1149 
_refine_hist.d_res_high                       0.96 
_refine_hist.d_res_low                        21.67 
# 
_struct.entry_id                     8RLF 
_struct.title                        '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        8RLF 
_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              8RLF 
_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)' 1390 ? 
1 MORE         8    ? 
1 'SSA (A^2)'  6890 ? 
# 
_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_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_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 ? ? ? ? ? ? ? 2.026 ? ? 
disulf2 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 115 SG ? ? A CYS 30 A CYS 115 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 80  SG ? ? A CYS 64 A CYS 80  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf4 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 94  SG ? ? A CYS 76 A CYS 94  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
# 
_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                   8RLF 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 NE  A ARG 5   ? A CZ A ARG 5   ? A NH1 A ARG 5   ? A 123.98 120.30 3.68   0.50 N 
2  1 NH1 A ARG 14  ? ? CZ A ARG 14  ? ? NH2 A ARG 14  ? ? 126.39 119.40 6.99   1.10 N 
3  1 NE  A ARG 14  ? ? CZ A ARG 14  ? ? NH2 A ARG 14  ? ? 115.24 120.30 -5.06  0.50 N 
4  1 CB  A ASP 48  ? A CG A ASP 48  ? A OD1 A ASP 48  ? A 123.75 118.30 5.45   0.90 N 
5  1 CD  A ARG 61  ? ? NE A ARG 61  ? ? CZ  A ARG 61  ? ? 134.03 123.60 10.43  1.40 N 
6  1 NE  A ARG 61  ? ? CZ A ARG 61  ? ? NH1 A ARG 61  ? ? 126.29 120.30 5.99   0.50 N 
7  1 CD  A ARG 68  ? ? NE A ARG 68  ? ? CZ  A ARG 68  ? ? 140.27 123.60 16.67  1.40 N 
8  1 NE  A ARG 73  ? ? CZ A ARG 73  ? ? NH2 A ARG 73  ? ? 116.69 120.30 -3.61  0.50 N 
9  1 CB  A VAL 99  ? B CA A VAL 99  ? B C   A VAL 99  ? B 99.64  111.40 -11.76 1.90 N 
10 1 CB  A ASP 101 ? A CG A ASP 101 ? A OD1 A ASP 101 ? A 123.87 118.30 5.57   0.90 N 
11 1 CB  A ASP 101 ? A CG A ASP 101 ? A OD2 A ASP 101 ? A 112.11 118.30 -6.19  0.90 N 
12 1 NE  A ARG 112 ? ? CZ A ARG 112 ? ? NH1 A ARG 112 ? ? 114.62 120.30 -5.68  0.50 N 
13 1 O   A LYS 116 ? ? C  A LYS 116 ? ? N   A GLY 117 ? B 112.25 123.20 -10.95 1.70 Y 
14 1 NE  A ARG 125 ? ? CZ A ARG 125 ? ? NH2 A ARG 125 ? ? 115.03 120.30 -5.27  0.50 N 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ASP 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    101 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   B 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    102 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   B 
_pdbx_validate_peptide_omega.omega            132.40 
# 
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 68  ? ? 0.191 'SIDE CHAIN' 
2 1 ARG A 128 ? ? 0.085 'SIDE CHAIN' 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             LEU 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              84 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -11.84 
# 
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  
GLN N    N N N 95  
GLN CA   C N S 96  
GLN C    C N N 97  
GLN O    O N N 98  
GLN CB   C N N 99  
GLN CG   C N N 100 
GLN CD   C N N 101 
GLN OE1  O N N 102 
GLN NE2  N N N 103 
GLN OXT  O N N 104 
GLN H    H N N 105 
GLN H2   H N N 106 
GLN HA   H N N 107 
GLN HB2  H N N 108 
GLN HB3  H N N 109 
GLN HG2  H N N 110 
GLN HG3  H N N 111 
GLN HE21 H N N 112 
GLN HE22 H N N 113 
GLN HXT  H N N 114 
GLU N    N N N 115 
GLU CA   C N S 116 
GLU C    C N N 117 
GLU O    O N N 118 
GLU CB   C N N 119 
GLU CG   C N N 120 
GLU CD   C N N 121 
GLU OE1  O N N 122 
GLU OE2  O N N 123 
GLU OXT  O N N 124 
GLU H    H N N 125 
GLU H2   H N N 126 
GLU HA   H N N 127 
GLU HB2  H N N 128 
GLU HB3  H N N 129 
GLU HG2  H N N 130 
GLU HG3  H N N 131 
GLU HE2  H N N 132 
GLU HXT  H N N 133 
GLY N    N N N 134 
GLY CA   C N N 135 
GLY C    C N N 136 
GLY O    O N N 137 
GLY OXT  O N N 138 
GLY H    H N N 139 
GLY H2   H N N 140 
GLY HA2  H N N 141 
GLY HA3  H N N 142 
GLY HXT  H N N 143 
HIS N    N N N 144 
HIS CA   C N S 145 
HIS C    C N N 146 
HIS O    O N N 147 
HIS CB   C N N 148 
HIS CG   C Y N 149 
HIS ND1  N Y N 150 
HIS CD2  C Y N 151 
HIS CE1  C Y N 152 
HIS NE2  N Y N 153 
HIS OXT  O N N 154 
HIS H    H N N 155 
HIS H2   H N N 156 
HIS HA   H N N 157 
HIS HB2  H N N 158 
HIS HB3  H N N 159 
HIS HD1  H N N 160 
HIS HD2  H N N 161 
HIS HE1  H N N 162 
HIS HE2  H N N 163 
HIS HXT  H N N 164 
HOH O    O N N 165 
HOH H1   H N N 166 
HOH H2   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  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
HIS N   CA   sing N N 135 
HIS N   H    sing N N 136 
HIS N   H2   sing N N 137 
HIS CA  C    sing N N 138 
HIS CA  CB   sing N N 139 
HIS CA  HA   sing N N 140 
HIS C   O    doub N N 141 
HIS C   OXT  sing N N 142 
HIS CB  CG   sing N N 143 
HIS CB  HB2  sing N N 144 
HIS CB  HB3  sing N N 145 
HIS CG  ND1  sing Y N 146 
HIS CG  CD2  doub Y N 147 
HIS ND1 CE1  doub Y N 148 
HIS ND1 HD1  sing N N 149 
HIS CD2 NE2  sing Y N 150 
HIS CD2 HD2  sing N N 151 
HIS CE1 NE2  sing Y N 152 
HIS CE1 HE1  sing N N 153 
HIS NE2 HE2  sing N N 154 
HIS OXT HXT  sing N N 155 
HOH O   H1   sing N N 156 
HOH O   H2   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                    8RLF 
_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]   0.036697 
_atom_sites.fract_transf_matrix[1][2]   -0.014708 
_atom_sites.fract_transf_matrix[1][3]   -0.014005 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.033740 
_atom_sites.fract_transf_matrix[2][3]   0.003588 
_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]   0.030967 
_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 
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   ? 29.188 23.352 26.801 0.379 12.63  ? 1   LYS A N    1 
ATOM   2    N N    B LYS A 1 1   ? 29.358 23.265 26.566 0.621 14.16  ? 1   LYS A N    1 
ATOM   3    C CA   A LYS A 1 1   ? 29.021 22.331 27.848 0.379 12.57  ? 1   LYS A CA   1 
ATOM   4    C CA   B LYS A 1 1   ? 29.229 22.376 27.745 0.621 12.84  ? 1   LYS A CA   1 
ATOM   5    C C    A LYS A 1 1   ? 29.745 21.062 27.433 0.379 11.81  ? 1   LYS A C    1 
ATOM   6    C C    B LYS A 1 1   ? 29.887 21.075 27.354 0.621 10.98  ? 1   LYS A C    1 
ATOM   7    O O    A LYS A 1 1   ? 29.579 20.638 26.279 0.379 12.57  ? 1   LYS A O    1 
ATOM   8    O O    B LYS A 1 1   ? 29.764 20.701 26.179 0.621 15.10  ? 1   LYS A O    1 
ATOM   9    C CB   A LYS A 1 1   ? 27.544 22.044 28.067 0.379 11.65  ? 1   LYS A CB   1 
ATOM   10   C CB   B LYS A 1 1   ? 27.763 22.215 28.068 0.621 14.89  ? 1   LYS A CB   1 
ATOM   11   C CG   A LYS A 1 1   ? 27.221 20.847 28.925 0.379 11.81  ? 1   LYS A CG   1 
ATOM   12   C CG   B LYS A 1 1   ? 27.440 21.197 29.126 0.621 12.48  ? 1   LYS A CG   1 
ATOM   13   C CD   A LYS A 1 1   ? 25.754 20.838 29.320 0.379 11.87  ? 1   LYS A CD   1 
ATOM   14   C CD   B LYS A 1 1   ? 25.961 21.181 29.474 0.621 16.31  ? 1   LYS A CD   1 
ATOM   15   C CE   A LYS A 1 1   ? 25.388 19.688 30.219 0.379 12.41  ? 1   LYS A CE   1 
ATOM   16   C CE   B LYS A 1 1   ? 25.601 20.000 30.351 0.621 16.69  ? 1   LYS A CE   1 
ATOM   17   N NZ   A LYS A 1 1   ? 25.859 19.929 31.616 0.379 12.98  ? 1   LYS A NZ   1 
ATOM   18   N NZ   B LYS A 1 1   ? 24.225 20.091 30.925 0.621 18.36  ? 1   LYS A NZ   1 
ATOM   19   H H1   A LYS A 1 1   ? 28.764 24.096 27.042 0.379 18.94  ? 1   LYS A H1   1 
ATOM   20   H H1   B LYS A 1 1   ? 28.983 24.052 26.745 0.621 21.24  ? 1   LYS A H1   1 
ATOM   21   H H2   A LYS A 1 1   ? 30.053 23.525 26.691 0.379 18.94  ? 1   LYS A H2   1 
ATOM   22   H H2   B LYS A 1 1   ? 30.219 23.383 26.376 0.621 21.24  ? 1   LYS A H2   1 
ATOM   23   H H3   A LYS A 1 1   ? 28.846 23.051 26.036 0.379 18.94  ? 1   LYS A H3   1 
ATOM   24   H H3   B LYS A 1 1   ? 28.948 22.893 25.868 0.621 21.24  ? 1   LYS A H3   1 
ATOM   25   H HA   A LYS A 1 1   ? 29.410 22.663 28.683 0.379 15.08  ? 1   LYS A HA   1 
ATOM   26   H HA   B LYS A 1 1   ? 29.698 22.769 28.511 0.621 15.41  ? 1   LYS A HA   1 
ATOM   27   H HB2  A LYS A 1 1   ? 27.139 22.827 28.472 0.379 13.98  ? 1   LYS A HB2  1 
ATOM   28   H HB2  B LYS A 1 1   ? 27.416 23.074 28.353 0.621 17.87  ? 1   LYS A HB2  1 
ATOM   29   H HB3  A LYS A 1 1   ? 27.127 21.918 27.200 0.379 13.98  ? 1   LYS A HB3  1 
ATOM   30   H HB3  B LYS A 1 1   ? 27.296 21.968 27.254 0.621 17.87  ? 1   LYS A HB3  1 
ATOM   31   H HG2  A LYS A 1 1   ? 27.429 20.035 28.436 0.379 14.17  ? 1   LYS A HG2  1 
ATOM   32   H HG2  B LYS A 1 1   ? 27.703 20.317 28.814 0.621 14.98  ? 1   LYS A HG2  1 
ATOM   33   H HG3  A LYS A 1 1   ? 27.771 20.866 29.724 0.379 14.17  ? 1   LYS A HG3  1 
ATOM   34   H HG3  B LYS A 1 1   ? 27.953 21.395 29.926 0.621 14.98  ? 1   LYS A HG3  1 
ATOM   35   H HD2  A LYS A 1 1   ? 25.545 21.670 29.772 0.379 14.25  ? 1   LYS A HD2  1 
ATOM   36   H HD2  B LYS A 1 1   ? 25.731 22.003 29.935 0.621 19.58  ? 1   LYS A HD2  1 
ATOM   37   H HD3  A LYS A 1 1   ? 25.212 20.794 28.516 0.379 14.25  ? 1   LYS A HD3  1 
ATOM   38   H HD3  B LYS A 1 1   ? 25.440 21.142 28.656 0.621 19.58  ? 1   LYS A HD3  1 
ATOM   39   H HE2  A LYS A 1 1   ? 24.425 19.572 30.219 0.379 14.90  ? 1   LYS A HE2  1 
ATOM   40   H HE2  B LYS A 1 1   ? 25.671 19.186 29.827 0.621 20.03  ? 1   LYS A HE2  1 
ATOM   41   H HE3  A LYS A 1 1   ? 25.789 18.873 29.880 0.379 14.90  ? 1   LYS A HE3  1 
ATOM   42   H HE3  B LYS A 1 1   ? 26.242 19.940 31.076 0.621 20.03  ? 1   LYS A HE3  1 
ATOM   43   H HZ1  A LYS A 1 1   ? 25.632 19.237 32.128 0.379 19.47  ? 1   LYS A HZ1  1 
ATOM   44   H HZ1  B LYS A 1 1   ? 24.066 19.375 31.430 0.621 27.54  ? 1   LYS A HZ1  1 
ATOM   45   H HZ2  A LYS A 1 1   ? 26.744 20.022 31.618 0.379 19.47  ? 1   LYS A HZ2  1 
ATOM   46   H HZ2  B LYS A 1 1   ? 24.159 20.825 31.424 0.621 27.54  ? 1   LYS A HZ2  1 
ATOM   47   H HZ3  A LYS A 1 1   ? 25.481 20.670 31.933 0.379 19.47  ? 1   LYS A HZ3  1 
ATOM   48   H HZ3  B LYS A 1 1   ? 23.629 20.126 30.265 0.621 27.54  ? 1   LYS A HZ3  1 
ATOM   49   N N    . VAL A 1 2   ? 30.496 20.439 28.312 1.000 11.28  ? 2   VAL A N    1 
ATOM   50   C CA   . VAL A 1 2   ? 31.033 19.114 28.095 1.000 10.34  ? 2   VAL A CA   1 
ATOM   51   C C    . VAL A 1 2   ? 30.196 18.183 28.942 1.000 9.76   ? 2   VAL A C    1 
ATOM   52   O O    . VAL A 1 2   ? 30.176 18.284 30.183 1.000 11.61  ? 2   VAL A O    1 
ATOM   53   C CB   . VAL A 1 2   ? 32.511 18.987 28.449 1.000 12.09  ? 2   VAL A CB   1 
ATOM   54   C CG1  . VAL A 1 2   ? 32.986 17.593 28.127 1.000 13.66  ? 2   VAL A CG1  1 
ATOM   55   C CG2  . VAL A 1 2   ? 33.301 20.059 27.706 1.000 16.65  ? 2   VAL A CG2  1 
ATOM   56   H H    A VAL A 1 2   ? 30.678 20.838 29.051 1.000 13.53  ? 2   VAL A H    1 
ATOM   57   H HA   . VAL A 1 2   ? 30.913 18.876 27.152 1.000 12.41  ? 2   VAL A HA   1 
ATOM   58   H HB   . VAL A 1 2   ? 32.614 19.136 29.412 1.000 14.51  ? 2   VAL A HB   1 
ATOM   59   H HG11 . VAL A 1 2   ? 33.917 17.513 28.350 1.000 20.50  ? 2   VAL A HG11 1 
ATOM   60   H HG12 . VAL A 1 2   ? 32.480 16.956 28.637 1.000 20.50  ? 2   VAL A HG12 1 
ATOM   61   H HG13 . VAL A 1 2   ? 32.866 17.421 27.190 1.000 20.50  ? 2   VAL A HG13 1 
ATOM   62   H HG21 . VAL A 1 2   ? 32.963 20.927 27.941 1.000 24.97  ? 2   VAL A HG21 1 
ATOM   63   H HG22 . VAL A 1 2   ? 34.228 20.000 27.949 1.000 24.97  ? 2   VAL A HG22 1 
ATOM   64   H HG23 . VAL A 1 2   ? 33.209 19.927 26.759 1.000 24.97  ? 2   VAL A HG23 1 
ATOM   65   N N    . PHE A 1 3   ? 29.412 17.323 28.293 1.000 9.71   ? 3   PHE A N    1 
ATOM   66   C CA   . PHE A 1 3   ? 28.560 16.382 28.975 1.000 9.39   ? 3   PHE A CA   1 
ATOM   67   C C    . PHE A 1 3   ? 29.345 15.239 29.617 1.000 9.10   ? 3   PHE A C    1 
ATOM   68   O O    . PHE A 1 3   ? 30.369 14.829 29.117 1.000 11.30  ? 3   PHE A O    1 
ATOM   69   C CB   . PHE A 1 3   ? 27.531 15.751 28.011 1.000 10.52  ? 3   PHE A CB   1 
ATOM   70   C CG   . PHE A 1 3   ? 26.281 16.544 27.802 1.000 9.57   ? 3   PHE A CG   1 
ATOM   71   C CD1  . PHE A 1 3   ? 26.209 17.582 26.899 1.000 11.69  ? 3   PHE A CD1  1 
ATOM   72   C CD2  . PHE A 1 3   ? 25.140 16.246 28.506 1.000 11.13  ? 3   PHE A CD2  1 
ATOM   73   C CE1  . PHE A 1 3   ? 25.027 18.289 26.690 1.000 13.83  ? 3   PHE A CE1  1 
ATOM   74   C CE2  . PHE A 1 3   ? 23.965 16.918 28.289 1.000 12.86  ? 3   PHE A CE2  1 
ATOM   75   C CZ   . PHE A 1 3   ? 23.921 17.940 27.355 1.000 13.79  ? 3   PHE A CZ   1 
ATOM   76   H H    . PHE A 1 3   ? 29.415 17.330 27.433 1.000 11.65  ? 3   PHE A H    1 
ATOM   77   H HA   . PHE A 1 3   ? 28.074 16.858 29.680 1.000 11.27  ? 3   PHE A HA   1 
ATOM   78   H HB2  . PHE A 1 3   ? 27.958 15.619 27.150 1.000 12.62  ? 3   PHE A HB2  1 
ATOM   79   H HB3  . PHE A 1 3   ? 27.287 14.877 28.352 1.000 12.62  ? 3   PHE A HB3  1 
ATOM   80   H HD1  . PHE A 1 3   ? 26.969 17.817 26.417 1.000 14.03  ? 3   PHE A HD1  1 
ATOM   81   H HD2  . PHE A 1 3   ? 25.165 15.571 29.146 1.000 13.36  ? 3   PHE A HD2  1 
ATOM   82   H HE1  . PHE A 1 3   ? 25.006 19.000 26.090 1.000 16.60  ? 3   PHE A HE1  1 
ATOM   83   H HE2  . PHE A 1 3   ? 23.201 16.689 28.767 1.000 15.43  ? 3   PHE A HE2  1 
ATOM   84   H HZ   . PHE A 1 3   ? 23.121 18.384 27.191 1.000 16.55  ? 3   PHE A HZ   1 
ATOM   85   N N    . GLY A 1 4   ? 28.757 14.700 30.684 1.000 10.03  ? 4   GLY A N    1 
ATOM   86   C CA   . GLY A 1 4   ? 29.097 13.387 31.110 1.000 10.57  ? 4   GLY A CA   1 
ATOM   87   C C    . GLY A 1 4   ? 28.391 12.302 30.299 1.000 9.40   ? 4   GLY A C    1 
ATOM   88   O O    . GLY A 1 4   ? 27.338 12.550 29.713 1.000 10.14  ? 4   GLY A O    1 
ATOM   89   H H    . GLY A 1 4   ? 28.167 15.150 31.119 1.000 12.04  ? 4   GLY A H    1 
ATOM   90   H HA2  . GLY A 1 4   ? 30.056 13.267 31.032 1.000 12.68  ? 4   GLY A HA2  1 
ATOM   91   H HA3  . GLY A 1 4   ? 28.860 13.287 32.045 1.000 12.68  ? 4   GLY A HA3  1 
ATOM   92   N N    A ARG A 1 5   ? 28.940 11.137 30.328 0.610 11.01  ? 5   ARG A N    1 
ATOM   93   N N    B ARG A 1 5   ? 28.912 11.069 30.204 0.390 10.71  ? 5   ARG A N    1 
ATOM   94   C CA   A ARG A 1 5   ? 28.420 10.028 29.572 0.610 10.19  ? 5   ARG A CA   1 
ATOM   95   C CA   B ARG A 1 5   ? 28.283 10.032 29.382 0.390 11.22  ? 5   ARG A CA   1 
ATOM   96   C C    A ARG A 1 5   ? 26.989 9.663  29.919 0.610 9.68   ? 5   ARG A C    1 
ATOM   97   C C    B ARG A 1 5   ? 26.865 9.755  29.900 0.390 9.46   ? 5   ARG A C    1 
ATOM   98   O O    A ARG A 1 5   ? 26.109 9.500  29.076 0.610 9.07   ? 5   ARG A O    1 
ATOM   99   O O    B ARG A 1 5   ? 25.910 9.763  29.120 0.390 11.79  ? 5   ARG A O    1 
ATOM   100  C CB   A ARG A 1 5   ? 29.399 8.866  29.849 0.610 11.32  ? 5   ARG A CB   1 
ATOM   101  C CB   B ARG A 1 5   ? 29.041 8.696  29.243 0.390 11.19  ? 5   ARG A CB   1 
ATOM   102  C CG   A ARG A 1 5   ? 28.921 7.599  29.197 0.610 12.31  ? 5   ARG A CG   1 
ATOM   103  C CG   B ARG A 1 5   ? 29.285 7.790  30.415 0.390 13.42  ? 5   ARG A CG   1 
ATOM   104  C CD   A ARG A 1 5   ? 29.822 6.407  29.512 0.610 16.32  ? 5   ARG A CD   1 
ATOM   105  C CD   B ARG A 1 5   ? 30.212 6.636  30.062 0.390 15.83  ? 5   ARG A CD   1 
ATOM   106  N NE   A ARG A 1 5   ? 29.834 6.121  30.944 0.610 18.87  ? 5   ARG A NE   1 
ATOM   107  N NE   B ARG A 1 5   ? 30.512 5.865  31.256 0.390 18.12  ? 5   ARG A NE   1 
ATOM   108  C CZ   A ARG A 1 5   ? 29.112 5.173  31.555 0.610 18.36  ? 5   ARG A CZ   1 
ATOM   109  C CZ   B ARG A 1 5   ? 29.785 4.797  31.584 0.390 18.35  ? 5   ARG A CZ   1 
ATOM   110  N NH1  A ARG A 1 5   ? 28.239 4.409  30.944 0.610 19.31  ? 5   ARG A NH1  1 
ATOM   111  N NH1  B ARG A 1 5   ? 28.872 4.320  30.768 0.390 24.36  ? 5   ARG A NH1  1 
ATOM   112  N NH2  A ARG A 1 5   ? 29.205 4.996  32.841 0.610 23.34  ? 5   ARG A NH2  1 
ATOM   113  N NH2  B ARG A 1 5   ? 30.015 4.194  32.726 0.390 23.74  ? 5   ARG A NH2  1 
ATOM   114  H H    A ARG A 1 5   ? 29.638 11.018 30.815 0.610 13.21  ? 5   ARG A H    1 
ATOM   115  H H    B ARG A 1 5   ? 29.632 10.883 30.636 0.390 12.85  ? 5   ARG A H    1 
ATOM   116  H HA   A ARG A 1 5   ? 28.463 10.253 28.619 0.610 12.22  ? 5   ARG A HA   1 
ATOM   117  H HA   B ARG A 1 5   ? 28.189 10.401 28.479 0.390 13.47  ? 5   ARG A HA   1 
ATOM   118  H HB2  A ARG A 1 5   ? 30.278 9.094  29.507 0.610 13.58  ? 5   ARG A HB2  1 
ATOM   119  H HB2  B ARG A 1 5   ? 28.567 8.173  28.578 0.390 13.43  ? 5   ARG A HB2  1 
ATOM   120  H HB3  A ARG A 1 5   ? 29.475 8.728  30.806 0.610 13.58  ? 5   ARG A HB3  1 
ATOM   121  H HB3  B ARG A 1 5   ? 29.910 8.906  28.865 0.390 13.43  ? 5   ARG A HB3  1 
ATOM   122  H HG2  A ARG A 1 5   ? 28.021 7.406  29.501 0.610 14.77  ? 5   ARG A HG2  1 
ATOM   123  H HG2  B ARG A 1 5   ? 29.677 8.303  31.139 0.390 16.10  ? 5   ARG A HG2  1 
ATOM   124  H HG3  A ARG A 1 5   ? 28.890 7.729  28.236 0.610 14.77  ? 5   ARG A HG3  1 
ATOM   125  H HG3  B ARG A 1 5   ? 28.438 7.435  30.726 0.390 16.10  ? 5   ARG A HG3  1 
ATOM   126  H HD2  A ARG A 1 5   ? 29.506 5.627  29.030 0.610 19.58  ? 5   ARG A HD2  1 
ATOM   127  H HD2  B ARG A 1 5   ? 29.787 6.065  29.402 0.390 18.99  ? 5   ARG A HD2  1 
ATOM   128  H HD3  A ARG A 1 5   ? 30.726 6.598  29.215 0.610 19.58  ? 5   ARG A HD3  1 
ATOM   129  H HD3  B ARG A 1 5   ? 31.034 6.981  29.680 0.390 18.99  ? 5   ARG A HD3  1 
ATOM   130  H HE   A ARG A 1 5   ? 30.348 6.603  31.437 0.610 22.64  ? 5   ARG A HE   1 
ATOM   131  H HE   B ARG A 1 5   ? 31.168 6.102  31.759 0.390 21.74  ? 5   ARG A HE   1 
ATOM   132  H HH11 A ARG A 1 5   ? 27.776 3.841  31.393 0.610 23.18  ? 5   ARG A HH11 1 
ATOM   133  H HH11 B ARG A 1 5   ? 28.428 3.616  30.985 0.390 29.23  ? 5   ARG A HH11 1 
ATOM   134  H HH12 A ARG A 1 5   ? 28.129 4.477  30.093 0.610 23.18  ? 5   ARG A HH12 1 
ATOM   135  H HH12 B ARG A 1 5   ? 28.718 4.712  30.019 0.390 29.23  ? 5   ARG A HH12 1 
ATOM   136  H HH21 A ARG A 1 5   ? 28.712 4.410  33.231 0.610 28.00  ? 5   ARG A HH21 1 
ATOM   137  H HH21 B ARG A 1 5   ? 29.568 3.490  32.938 0.390 28.49  ? 5   ARG A HH21 1 
ATOM   138  H HH22 A ARG A 1 5   ? 29.760 5.466  33.301 0.610 28.00  ? 5   ARG A HH22 1 
ATOM   139  H HH22 B ARG A 1 5   ? 30.611 4.502  33.263 0.390 28.49  ? 5   ARG A HH22 1 
ATOM   140  N N    . CYS A 1 6   ? 26.690 9.509  31.203 1.000 10.27  ? 6   CYS A N    1 
ATOM   141  C CA   . CYS A 1 6   ? 25.381 9.135  31.654 1.000 10.28  ? 6   CYS A CA   1 
ATOM   142  C C    . CYS A 1 6   ? 24.375 10.283 31.542 1.000 9.45   ? 6   CYS A C    1 
ATOM   143  O O    . CYS A 1 6   ? 23.185 10.046 31.240 1.000 11.14  ? 6   CYS A O    1 
ATOM   144  C CB   . CYS A 1 6   ? 25.387 8.634  33.094 1.000 12.32  ? 6   CYS A CB   1 
ATOM   145  S SG   . CYS A 1 6   ? 26.273 7.072  33.309 1.000 16.23  ? 6   CYS A SG   1 
ATOM   146  H H    A CYS A 1 6   ? 27.306 9.639  31.789 1.000 12.32  ? 6   CYS A H    1 
ATOM   147  H HA   . CYS A 1 6   ? 25.065 8.403  31.084 1.000 12.33  ? 6   CYS A HA   1 
ATOM   148  H HB2  . CYS A 1 6   ? 25.797 9.308  33.659 1.000 14.78  ? 6   CYS A HB2  1 
ATOM   149  H HB3  . CYS A 1 6   ? 24.470 8.519  33.390 1.000 14.78  ? 6   CYS A HB3  1 
ATOM   150  N N    . GLU A 1 7   ? 24.818 11.500 31.746 1.000 9.35   ? 7   GLU A N    1 
ATOM   151  C CA   . GLU A 1 7   ? 24.013 12.666 31.587 1.000 9.44   ? 7   GLU A CA   1 
ATOM   152  C C    . GLU A 1 7   ? 23.555 12.813 30.129 1.000 8.64   ? 7   GLU A C    1 
ATOM   153  O O    . GLU A 1 7   ? 22.405 13.125 29.849 1.000 10.13  ? 7   GLU A O    1 
ATOM   154  C CB   . GLU A 1 7   ? 24.774 13.909 32.050 1.000 10.39  ? 7   GLU A CB   1 
ATOM   155  C CG   . GLU A 1 7   ? 24.980 13.918 33.551 1.000 12.69  ? 7   GLU A CG   1 
ATOM   156  C CD   . GLU A 1 7   ? 26.092 13.091 34.105 1.000 11.35  ? 7   GLU A CD   1 
ATOM   157  O OE1  . GLU A 1 7   ? 26.863 12.419 33.376 1.000 12.52  ? 7   GLU A OE1  1 
ATOM   158  O OE2  . GLU A 1 7   ? 26.202 13.105 35.383 1.000 15.08  ? 7   GLU A OE2  1 
ATOM   159  H H    . GLU A 1 7   ? 25.638 11.600 31.987 1.000 11.22  ? 7   GLU A H    1 
ATOM   160  H HA   . GLU A 1 7   ? 23.217 12.566 32.150 1.000 11.32  ? 7   GLU A HA   1 
ATOM   161  H HB2  . GLU A 1 7   ? 25.637 13.939 31.609 1.000 12.47  ? 7   GLU A HB2  1 
ATOM   162  H HB3  . GLU A 1 7   ? 24.278 14.702 31.791 1.000 12.47  ? 7   GLU A HB3  1 
ATOM   163  H HG2  . GLU A 1 7   ? 25.128 14.837 33.825 1.000 15.23  ? 7   GLU A HG2  1 
ATOM   164  H HG3  . GLU A 1 7   ? 24.155 13.624 33.967 1.000 15.23  ? 7   GLU A HG3  1 
ATOM   165  N N    . LEU A 1 8   ? 24.456 12.607 29.199 1.000 8.62   ? 8   LEU A N    1 
ATOM   166  C CA   . LEU A 1 8   ? 24.122 12.666 27.785 1.000 8.14   ? 8   LEU A CA   1 
ATOM   167  C C    . LEU A 1 8   ? 23.165 11.540 27.428 1.000 8.28   ? 8   LEU A C    1 
ATOM   168  O O    . LEU A 1 8   ? 22.210 11.749 26.686 1.000 9.07   ? 8   LEU A O    1 
ATOM   169  C CB   . LEU A 1 8   ? 25.360 12.618 26.907 1.000 8.92   ? 8   LEU A CB   1 
ATOM   170  C CG   . LEU A 1 8   ? 25.083 12.773 25.427 1.000 9.73   ? 8   LEU A CG   1 
ATOM   171  C CD1  . LEU A 1 8   ? 24.431 14.120 25.123 1.000 11.91  ? 8   LEU A CD1  1 
ATOM   172  C CD2  . LEU A 1 8   ? 26.318 12.542 24.646 1.000 13.96  ? 8   LEU A CD2  1 
ATOM   173  H H    . LEU A 1 8   ? 25.265 12.431 29.431 1.000 10.35  ? 8   LEU A H    1 
ATOM   174  H HA   . LEU A 1 8   ? 23.664 13.517 27.618 1.000 9.77   ? 8   LEU A HA   1 
ATOM   175  H HB2  . LEU A 1 8   ? 25.965 13.324 27.185 1.000 10.71  ? 8   LEU A HB2  1 
ATOM   176  H HB3  . LEU A 1 8   ? 25.811 11.772 27.051 1.000 10.71  ? 8   LEU A HB3  1 
ATOM   177  H HG   . LEU A 1 8   ? 24.443 12.075 25.175 1.000 11.67  ? 8   LEU A HG   1 
ATOM   178  H HD11 . LEU A 1 8   ? 23.637 14.218 25.654 1.000 17.87  ? 8   LEU A HD11 1 
ATOM   179  H HD12 . LEU A 1 8   ? 25.045 14.828 25.331 1.000 17.87  ? 8   LEU A HD12 1 
ATOM   180  H HD13 . LEU A 1 8   ? 24.199 14.160 24.192 1.000 17.87  ? 8   LEU A HD13 1 
ATOM   181  H HD21 . LEU A 1 8   ? 26.128 12.643 23.710 1.000 20.94  ? 8   LEU A HD21 1 
ATOM   182  H HD22 . LEU A 1 8   ? 26.986 13.179 24.907 1.000 20.94  ? 8   LEU A HD22 1 
ATOM   183  H HD23 . LEU A 1 8   ? 26.640 11.653 24.812 1.000 20.94  ? 8   LEU A HD23 1 
ATOM   184  N N    . ALA A 1 9   ? 23.429 10.340 27.932 1.000 8.93   ? 9   ALA A N    1 
ATOM   185  C CA   . ALA A 1 9   ? 22.535 9.222  27.662 1.000 9.45   ? 9   ALA A CA   1 
ATOM   186  C C    . ALA A 1 9   ? 21.122 9.556  28.096 1.000 9.32   ? 9   ALA A C    1 
ATOM   187  O O    . ALA A 1 9   ? 20.158 9.289  27.367 1.000 10.24  ? 9   ALA A O    1 
ATOM   188  C CB   . ALA A 1 9   ? 23.056 7.977  28.346 1.000 10.95  ? 9   ALA A CB   1 
ATOM   189  H H    . ALA A 1 9   ? 24.128 10.223 28.418 1.000 10.71  ? 9   ALA A H    1 
ATOM   190  H HA   . ALA A 1 9   ? 22.528 9.061  26.695 1.000 11.34  ? 9   ALA A HA   1 
ATOM   191  H HB1  . ALA A 1 9   ? 22.465 7.242  28.167 1.000 16.43  ? 9   ALA A HB1  1 
ATOM   192  H HB2  . ALA A 1 9   ? 23.932 7.771  28.012 1.000 16.43  ? 9   ALA A HB2  1 
ATOM   193  H HB3  . ALA A 1 9   ? 23.101 8.127  29.293 1.000 16.43  ? 9   ALA A HB3  1 
ATOM   194  N N    . ALA A 1 10  ? 20.958 10.116 29.286 1.000 9.83   ? 10  ALA A N    1 
ATOM   195  C CA   . ALA A 1 10  ? 19.630 10.444 29.783 1.000 10.31  ? 10  ALA A CA   1 
ATOM   196  C C    . ALA A 1 10  ? 18.970 11.496 28.916 1.000 9.72   ? 10  ALA A C    1 
ATOM   197  O O    . ALA A 1 10  ? 17.786 11.418 28.626 1.000 11.70  ? 10  ALA A O    1 
ATOM   198  C CB   . ALA A 1 10  ? 19.712 10.908 31.233 1.000 12.55  ? 10  ALA A CB   1 
ATOM   199  H H    . ALA A 1 10  ? 21.646 10.288 29.772 1.000 11.80  ? 10  ALA A H    1 
ATOM   200  H HA   . ALA A 1 10  ? 19.081 9.633  29.751 1.000 12.37  ? 10  ALA A HA   1 
ATOM   201  H HB1  . ALA A 1 10  ? 18.832 11.122 31.551 1.000 18.83  ? 10  ALA A HB1  1 
ATOM   202  H HB2  . ALA A 1 10  ? 20.086 10.207 31.772 1.000 18.83  ? 10  ALA A HB2  1 
ATOM   203  H HB3  . ALA A 1 10  ? 20.270 11.687 31.288 1.000 18.83  ? 10  ALA A HB3  1 
ATOM   204  N N    . ALA A 1 11  ? 19.718 12.528 28.503 1.000 9.47   ? 11  ALA A N    1 
ATOM   205  C CA   . ALA A 1 11  ? 19.163 13.571 27.665 1.000 9.98   ? 11  ALA A CA   1 
ATOM   206  C C    . ALA A 1 11  ? 18.752 13.013 26.298 1.000 9.39   ? 11  ALA A C    1 
ATOM   207  O O    . ALA A 1 11  ? 17.688 13.343 25.777 1.000 11.00  ? 11  ALA A O    1 
ATOM   208  C CB   . ALA A 1 11  ? 20.171 14.706 27.494 1.000 11.84  ? 11  ALA A CB   1 
ATOM   209  H H    . ALA A 1 11  ? 20.543 12.572 28.740 1.000 11.36  ? 11  ALA A H    1 
ATOM   210  H HA   . ALA A 1 11  ? 18.365 13.930 28.106 1.000 11.98  ? 11  ALA A HA   1 
ATOM   211  H HB1  . ALA A 1 11  ? 19.792 15.390 26.938 1.000 17.77  ? 11  ALA A HB1  1 
ATOM   212  H HB2  . ALA A 1 11  ? 20.386 15.075 28.354 1.000 17.77  ? 11  ALA A HB2  1 
ATOM   213  H HB3  . ALA A 1 11  ? 20.970 14.366 27.084 1.000 17.77  ? 11  ALA A HB3  1 
ATOM   214  N N    . MET A 1 12  ? 19.569 12.158 25.723 1.000 8.74   ? 12  MET A N    1 
ATOM   215  C CA   . MET A 1 12  ? 19.230 11.530 24.457 1.000 9.10   ? 12  MET A CA   1 
ATOM   216  C C    . MET A 1 12  ? 18.020 10.619 24.576 1.000 9.73   ? 12  MET A C    1 
ATOM   217  O O    . MET A 1 12  ? 17.187 10.591 23.658 1.000 11.71  ? 12  MET A O    1 
ATOM   218  C CB   . MET A 1 12  ? 20.438 10.772 23.898 1.000 8.98   ? 12  MET A CB   1 
ATOM   219  C CG   . MET A 1 12  ? 21.514 11.718 23.356 1.000 9.17   ? 12  MET A CG   1 
ATOM   220  S SD   . MET A 1 12  ? 22.912 10.743 22.734 1.000 11.12  ? 12  MET A SD   1 
ATOM   221  C CE   . MET A 1 12  ? 23.612 11.882 21.547 1.000 15.68  ? 12  MET A CE   1 
ATOM   222  H H    . MET A 1 12  ? 20.317 11.967 26.102 1.000 10.49  ? 12  MET A H    1 
ATOM   223  H HA   . MET A 1 12  ? 19.006 12.242 23.822 1.000 10.92  ? 12  MET A HA   1 
ATOM   224  H HB2  . MET A 1 12  ? 20.822 10.222 24.600 1.000 10.78  ? 12  MET A HB2  1 
ATOM   225  H HB3  . MET A 1 12  ? 20.143 10.183 23.186 1.000 10.78  ? 12  MET A HB3  1 
ATOM   226  H HG2  . MET A 1 12  ? 21.146 12.259 22.640 1.000 11.00  ? 12  MET A HG2  1 
ATOM   227  H HG3  . MET A 1 12  ? 21.816 12.312 24.061 1.000 11.00  ? 12  MET A HG3  1 
ATOM   228  H HE1  . MET A 1 12  ? 24.380 11.481 21.133 1.000 23.52  ? 12  MET A HE1  1 
ATOM   229  H HE2  . MET A 1 12  ? 22.957 12.087 20.876 1.000 23.52  ? 12  MET A HE2  1 
ATOM   230  H HE3  . MET A 1 12  ? 23.875 12.689 21.995 1.000 23.52  ? 12  MET A HE3  1 
ATOM   231  N N    . LYS A 1 13  ? 17.888 9.914  25.677 1.000 10.10  ? 13  LYS A N    1 
ATOM   232  C CA   . LYS A 1 13  ? 16.713 9.063  25.910 1.000 11.38  ? 13  LYS A CA   1 
ATOM   233  C C    . LYS A 1 13  ? 15.469 9.905  26.002 1.000 11.13  ? 13  LYS A C    1 
ATOM   234  O O    . LYS A 1 13  ? 14.427 9.542  25.442 1.000 12.76  ? 13  LYS A O    1 
ATOM   235  C CB   . LYS A 1 13  ? 16.911 8.230  27.181 1.000 14.04  ? 13  LYS A CB   1 
ATOM   236  C CG   . LYS A 1 13  ? 15.775 7.249  27.411 1.000 19.58  ? 13  LYS A CG   1 
ATOM   237  C CD   . LYS A 1 13  ? 16.121 6.322  28.514 1.000 30.45  ? 13  LYS A CD   1 
ATOM   238  C CE   . LYS A 1 13  ? 14.995 5.599  29.187 1.000 40.92  ? 13  LYS A CE   1 
ATOM   239  N NZ   . LYS A 1 13  ? 13.751 6.403  29.384 1.000 57.88  ? 13  LYS A NZ   1 
ATOM   240  H H    . LYS A 1 13  ? 18.504 9.951  26.276 1.000 12.12  ? 13  LYS A H    1 
ATOM   241  H HA   . LYS A 1 13  ? 16.618 8.451  25.150 1.000 13.66  ? 13  LYS A HA   1 
ATOM   242  H HB2  . LYS A 1 13  ? 17.746 7.740  27.113 1.000 16.85  ? 13  LYS A HB2  1 
ATOM   243  H HB3  . LYS A 1 13  ? 16.977 8.825  27.944 1.000 16.85  ? 13  LYS A HB3  1 
ATOM   244  H HG2  . LYS A 1 13  ? 14.965 7.734  27.634 1.000 23.49  ? 13  LYS A HG2  1 
ATOM   245  H HG3  . LYS A 1 13  ? 15.611 6.744  26.599 1.000 23.49  ? 13  LYS A HG3  1 
ATOM   246  H HD2  . LYS A 1 13  ? 16.735 5.657  28.164 1.000 36.54  ? 13  LYS A HD2  1 
ATOM   247  H HD3  . LYS A 1 13  ? 16.599 6.827  29.190 1.000 36.54  ? 13  LYS A HD3  1 
ATOM   248  H HE2  . LYS A 1 13  ? 14.774 4.815  28.660 1.000 49.11  ? 13  LYS A HE2  1 
ATOM   249  H HE3  . LYS A 1 13  ? 15.302 5.291  30.054 1.000 49.11  ? 13  LYS A HE3  1 
ATOM   250  H HZ1  . LYS A 1 13  ? 13.136 5.903  29.788 1.000 86.83  ? 13  LYS A HZ1  1 
ATOM   251  H HZ2  . LYS A 1 13  ? 13.934 7.114  29.888 1.000 86.83  ? 13  LYS A HZ2  1 
ATOM   252  H HZ3  . LYS A 1 13  ? 13.443 6.672  28.593 1.000 86.83  ? 13  LYS A HZ3  1 
ATOM   253  N N    . ARG A 1 14  ? 15.522 11.029 26.723 1.000 10.88  ? 14  ARG A N    1 
ATOM   254  C CA   . ARG A 1 14  ? 14.375 11.899 26.832 1.000 12.11  ? 14  ARG A CA   1 
ATOM   255  C C    . ARG A 1 14  ? 13.941 12.433 25.497 1.000 12.23  ? 14  ARG A C    1 
ATOM   256  O O    . ARG A 1 14  ? 12.739 12.697 25.290 1.000 16.62  ? 14  ARG A O    1 
ATOM   257  C CB   . ARG A 1 14  ? 14.660 13.071 27.778 1.000 14.07  ? 14  ARG A CB   1 
ATOM   258  C CG   . ARG A 1 14  ? 14.662 12.681 29.251 1.000 17.73  ? 14  ARG A CG   1 
ATOM   259  C CD   . ARG A 1 14  ? 14.606 13.982 30.109 1.000 21.84  ? 14  ARG A CD   1 
ATOM   260  N NE   . ARG A 1 14  ? 15.862 14.708 30.049 1.000 26.72  ? 14  ARG A NE   1 
ATOM   261  C CZ   . ARG A 1 14  ? 16.953 14.523 30.768 1.000 30.53  ? 14  ARG A CZ   1 
ATOM   262  N NH1  . ARG A 1 14  ? 16.940 13.582 31.699 1.000 39.87  ? 14  ARG A NH1  1 
ATOM   263  N NH2  . ARG A 1 14  ? 17.969 15.360 30.494 1.000 36.64  ? 14  ARG A NH2  1 
ATOM   264  H H    . ARG A 1 14  ? 16.252 11.238 27.129 1.000 13.06  ? 14  ARG A H    1 
ATOM   265  H HA   . ARG A 1 14  ? 13.633 11.378 27.207 1.000 14.53  ? 14  ARG A HA   1 
ATOM   266  H HB2  . ARG A 1 14  ? 15.523 13.451 27.553 1.000 16.88  ? 14  ARG A HB2  1 
ATOM   267  H HB3  . ARG A 1 14  ? 13.989 13.757 27.636 1.000 16.88  ? 14  ARG A HB3  1 
ATOM   268  H HG2  . ARG A 1 14  ? 13.894 12.122 29.447 1.000 21.27  ? 14  ARG A HG2  1 
ATOM   269  H HG3  . ARG A 1 14  ? 15.466 12.181 29.460 1.000 21.27  ? 14  ARG A HG3  1 
ATOM   270  H HD2  . ARG A 1 14  ? 13.890 14.551 29.785 1.000 26.20  ? 14  ARG A HD2  1 
ATOM   271  H HD3  . ARG A 1 14  ? 14.412 13.751 31.031 1.000 26.20  ? 14  ARG A HD3  1 
ATOM   272  H HE   . ARG A 1 14  ? 15.899 15.343 29.470 1.000 32.06  ? 14  ARG A HE   1 
ATOM   273  H HH11 . ARG A 1 14  ? 16.232 13.110 31.823 1.000 47.85  ? 14  ARG A HH11 1 
ATOM   274  H HH12 . ARG A 1 14  ? 17.640 13.442 32.180 1.000 47.85  ? 14  ARG A HH12 1 
ATOM   275  H HH21 . ARG A 1 14  ? 17.878 15.962 29.887 1.000 43.97  ? 14  ARG A HH21 1 
ATOM   276  H HH22 . ARG A 1 14  ? 18.710 15.293 30.926 1.000 43.97  ? 14  ARG A HH22 1 
ATOM   277  N N    A HIS A 1 15  ? 14.858 12.643 24.566 0.268 10.27  ? 15  HIS A N    1 
ATOM   278  N N    B HIS A 1 15  ? 14.858 12.547 24.538 0.732 12.43  ? 15  HIS A N    1 
ATOM   279  C CA   A HIS A 1 15  ? 14.484 13.132 23.251 0.268 13.19  ? 15  HIS A CA   1 
ATOM   280  C CA   B HIS A 1 15  ? 14.600 13.031 23.208 0.732 12.78  ? 15  HIS A CA   1 
ATOM   281  C C    A HIS A 1 15  ? 14.119 12.004 22.306 0.268 14.01  ? 15  HIS A C    1 
ATOM   282  C C    B HIS A 1 15  ? 14.329 11.924 22.205 0.732 14.08  ? 15  HIS A C    1 
ATOM   283  O O    A HIS A 1 15  ? 13.815 12.307 21.132 0.268 18.91  ? 15  HIS A O    1 
ATOM   284  O O    B HIS A 1 15  ? 14.311 12.199 20.969 0.732 18.77  ? 15  HIS A O    1 
ATOM   285  C CB   A HIS A 1 15  ? 15.633 14.005 22.713 0.268 14.49  ? 15  HIS A CB   1 
ATOM   286  C CB   B HIS A 1 15  ? 15.776 13.860 22.687 0.732 15.43  ? 15  HIS A CB   1 
ATOM   287  C CG   A HIS A 1 15  ? 15.616 15.382 23.309 0.268 16.61  ? 15  HIS A CG   1 
ATOM   288  C CG   B HIS A 1 15  ? 15.908 15.194 23.326 0.732 16.01  ? 15  HIS A CG   1 
ATOM   289  N ND1  A HIS A 1 15  ? 14.517 16.198 23.192 0.268 19.23  ? 15  HIS A ND1  1 
ATOM   290  N ND1  B HIS A 1 15  ? 15.544 16.377 22.752 0.732 19.38  ? 15  HIS A ND1  1 
ATOM   291  C CD2  A HIS A 1 15  ? 16.514 16.098 24.014 0.268 17.72  ? 15  HIS A CD2  1 
ATOM   292  C CD2  B HIS A 1 15  ? 16.418 15.490 24.545 0.732 17.24  ? 15  HIS A CD2  1 
ATOM   293  C CE1  A HIS A 1 15  ? 14.720 17.354 23.795 0.268 20.73  ? 15  HIS A CE1  1 
ATOM   294  C CE1  B HIS A 1 15  ? 15.833 17.346 23.594 0.732 20.87  ? 15  HIS A CE1  1 
ATOM   295  N NE2  A HIS A 1 15  ? 15.932 17.320 24.293 0.268 18.84  ? 15  HIS A NE2  1 
ATOM   296  N NE2  B HIS A 1 15  ? 16.334 16.827 24.705 0.732 21.69  ? 15  HIS A NE2  1 
ATOM   297  H H    A HIS A 1 15  ? 15.686 12.489 24.742 0.268 12.32  ? 15  HIS A H    1 
ATOM   298  H H    B HIS A 1 15  ? 15.664 12.314 24.728 0.732 14.92  ? 15  HIS A H    1 
ATOM   299  H HA   A HIS A 1 15  ? 13.695 13.704 23.356 0.268 15.83  ? 15  HIS A HA   1 
ATOM   300  H HA   B HIS A 1 15  ? 13.810 13.611 23.242 0.732 15.33  ? 15  HIS A HA   1 
ATOM   301  H HB2  A HIS A 1 15  ? 16.480 13.579 22.917 0.268 17.39  ? 15  HIS A HB2  1 
ATOM   302  H HB2  B HIS A 1 15  ? 16.596 13.363 22.832 0.732 18.51  ? 15  HIS A HB2  1 
ATOM   303  H HB3  A HIS A 1 15  ? 15.558 14.073 21.748 0.268 17.39  ? 15  HIS A HB3  1 
ATOM   304  H HB3  B HIS A 1 15  ? 15.672 13.982 21.730 0.732 18.51  ? 15  HIS A HB3  1 
ATOM   305  H HD1  A HIS A 1 15  ? 13.793 15.984 22.781 0.268 23.08  ? 15  HIS A HD1  1 
ATOM   306  H HD1  B HIS A 1 15  ? 15.187 16.473 21.976 0.732 23.25  ? 15  HIS A HD1  1 
ATOM   307  H HD2  A HIS A 1 15  ? 17.366 15.822 24.265 0.268 21.26  ? 15  HIS A HD2  1 
ATOM   308  H HD2  B HIS A 1 15  ? 16.764 14.882 25.159 0.732 20.69  ? 15  HIS A HD2  1 
ATOM   309  H HE1  A HIS A 1 15  ? 14.117 18.059 23.854 0.268 24.88  ? 15  HIS A HE1  1 
ATOM   310  H HE1  B HIS A 1 15  ? 15.706 18.253 23.433 0.732 25.05  ? 15  HIS A HE1  1 
ATOM   311  H HE2  A HIS A 1 15  ? 16.307 17.960 24.728 0.268 22.61  ? 15  HIS A HE2  1 
ATOM   312  H HE2  B HIS A 1 15  ? 16.565 17.267 25.407 0.732 26.03  ? 15  HIS A HE2  1 
ATOM   313  N N    . GLY A 1 16  ? 14.094 10.733 22.676 1.000 13.89  ? 16  GLY A N    1 
ATOM   314  C CA   . GLY A 1 16  ? 13.577 9.693  21.799 1.000 15.11  ? 16  GLY A CA   1 
ATOM   315  C C    . GLY A 1 16  ? 14.562 8.982  20.978 1.000 13.20  ? 16  GLY A C    1 
ATOM   316  O O    . GLY A 1 16  ? 14.170 8.291  20.025 1.000 17.15  ? 16  GLY A O    1 
ATOM   317  H H    A GLY A 1 16  ? 14.391 10.516 23.453 1.000 16.67  ? 16  GLY A H    1 
ATOM   318  H HA2  . GLY A 1 16  ? 13.111 9.041  22.346 1.000 18.13  ? 16  GLY A HA2  1 
ATOM   319  H HA3  . GLY A 1 16  ? 12.923 10.095 21.207 1.000 18.13  ? 16  GLY A HA3  1 
ATOM   320  N N    . LEU A 1 17  ? 15.864 9.039  21.274 1.000 11.78  ? 17  LEU A N    1 
ATOM   321  C CA   . LEU A 1 17  ? 16.835 8.359  20.410 1.000 10.97  ? 17  LEU A CA   1 
ATOM   322  C C    . LEU A 1 17  ? 16.992 6.905  20.659 1.000 11.21  ? 17  LEU A C    1 
ATOM   323  O O    . LEU A 1 17  ? 17.541 6.245  19.767 1.000 12.79  ? 17  LEU A O    1 
ATOM   324  C CB   . LEU A 1 17  ? 18.198 9.058  20.474 1.000 11.18  ? 17  LEU A CB   1 
ATOM   325  C CG   . LEU A 1 17  ? 18.322 10.351 19.733 1.000 12.59  ? 17  LEU A CG   1 
ATOM   326  C CD1  . LEU A 1 17  ? 19.743 10.928 19.886 1.000 14.65  ? 17  LEU A CD1  1 
ATOM   327  C CD2  . LEU A 1 17  ? 18.064 10.187 18.222 1.000 15.64  ? 17  LEU A CD2  1 
ATOM   328  H H    . LEU A 1 17  ? 16.131 9.472  21.968 1.000 14.13  ? 17  LEU A H    1 
ATOM   329  H HA   . LEU A 1 17  ? 16.511 8.455  19.490 1.000 13.16  ? 17  LEU A HA   1 
ATOM   330  H HB2  . LEU A 1 17  ? 18.410 9.223  21.406 1.000 13.42  ? 17  LEU A HB2  1 
ATOM   331  H HB3  . LEU A 1 17  ? 18.868 8.447  20.129 1.000 13.42  ? 17  LEU A HB3  1 
ATOM   332  H HG   . LEU A 1 17  ? 17.677 10.992 20.099 1.000 15.11  ? 17  LEU A HG   1 
ATOM   333  H HD11 . LEU A 1 17  ? 19.806 11.757 19.406 1.000 21.97  ? 17  LEU A HD11 1 
ATOM   334  H HD12 . LEU A 1 17  ? 19.927 11.083 20.816 1.000 21.97  ? 17  LEU A HD12 1 
ATOM   335  H HD13 . LEU A 1 17  ? 20.382 10.305 19.533 1.000 21.97  ? 17  LEU A HD13 1 
ATOM   336  H HD21 . LEU A 1 17  ? 18.154 11.039 17.787 1.000 23.47  ? 17  LEU A HD21 1 
ATOM   337  H HD22 . LEU A 1 17  ? 18.701 9.571  17.853 1.000 23.47  ? 17  LEU A HD22 1 
ATOM   338  H HD23 . LEU A 1 17  ? 17.176 9.850  18.084 1.000 23.47  ? 17  LEU A HD23 1 
ATOM   339  N N    . ASP A 1 18  ? 16.563 6.368  21.804 1.000 11.42  ? 18  ASP A N    1 
ATOM   340  C CA   . ASP A 1 18  ? 16.771 4.945  22.001 1.000 11.02  ? 18  ASP A CA   1 
ATOM   341  C C    . ASP A 1 18  ? 15.906 4.153  21.038 1.000 10.90  ? 18  ASP A C    1 
ATOM   342  O O    . ASP A 1 18  ? 14.674 4.279  21.038 1.000 13.88  ? 18  ASP A O    1 
ATOM   343  C CB   . ASP A 1 18  ? 16.423 4.508  23.424 1.000 13.96  ? 18  ASP A CB   1 
ATOM   344  C CG   . ASP A 1 18  ? 16.857 3.070  23.737 1.000 15.41  ? 18  ASP A CG   1 
ATOM   345  O OD1  . ASP A 1 18  ? 17.791 2.475  23.126 1.000 14.94  ? 18  ASP A OD1  1 
ATOM   346  O OD2  . ASP A 1 18  ? 16.200 2.493  24.605 1.000 26.42  ? 18  ASP A OD2  1 
ATOM   347  H H    . ASP A 1 18  ? 16.178 6.849  22.404 1.000 13.71  ? 18  ASP A H    1 
ATOM   348  H HA   . ASP A 1 18  ? 17.712 4.735  21.827 1.000 13.22  ? 18  ASP A HA   1 
ATOM   349  H HB2  . ASP A 1 18  ? 16.851 5.110  24.052 1.000 16.75  ? 18  ASP A HB2  1 
ATOM   350  H HB3  . ASP A 1 18  ? 15.464 4.582  23.550 1.000 16.75  ? 18  ASP A HB3  1 
ATOM   351  N N    . ASN A 1 19  ? 16.550 3.366  20.208 1.000 9.90   ? 19  ASN A N    1 
ATOM   352  C CA   . ASN A 1 19  ? 15.908 2.559  19.202 1.000 10.44  ? 19  ASN A CA   1 
ATOM   353  C C    . ASN A 1 19  ? 15.318 3.402  18.057 1.000 10.75  ? 19  ASN A C    1 
ATOM   354  O O    . ASN A 1 19  ? 14.484 2.871  17.298 1.000 13.21  ? 19  ASN A O    1 
ATOM   355  C CB   . ASN A 1 19  ? 14.862 1.638  19.805 1.000 11.37  ? 19  ASN A CB   1 
ATOM   356  C CG   . ASN A 1 19  ? 14.583 0.473  18.931 1.000 11.72  ? 19  ASN A CG   1 
ATOM   357  O OD1  . ASN A 1 19  ? 15.408 0.001  18.185 1.000 15.52  ? 19  ASN A OD1  1 
ATOM   358  N ND2  . ASN A 1 19  ? 13.374 -0.067 19.014 1.000 14.79  ? 19  ASN A ND2  1 
ATOM   359  H H    . ASN A 1 19  ? 17.407 3.329  20.269 1.000 11.88  ? 19  ASN A H    1 
ATOM   360  H HA   . ASN A 1 19  ? 16.601 1.988  18.810 1.000 12.53  ? 19  ASN A HA   1 
ATOM   361  H HB2  . ASN A 1 19  ? 15.172 1.323  20.668 1.000 13.64  ? 19  ASN A HB2  1 
ATOM   362  H HB3  . ASN A 1 19  ? 14.041 2.135  19.946 1.000 13.64  ? 19  ASN A HB3  1 
ATOM   363  H HD21 . ASN A 1 19  ? 13.177 -0.754 18.536 1.000 17.75  ? 19  ASN A HD21 1 
ATOM   364  H HD22 . ASN A 1 19  ? 12.788 0.271  19.545 1.000 17.75  ? 19  ASN A HD22 1 
ATOM   365  N N    . TYR A 1 20  ? 15.765 4.605  17.849 1.000 10.18  ? 20  TYR A N    1 
ATOM   366  C CA   . TYR A 1 20  ? 15.322 5.391  16.708 1.000 10.17  ? 20  TYR A CA   1 
ATOM   367  C C    . TYR A 1 20  ? 15.874 4.757  15.455 1.000 9.78   ? 20  TYR A C    1 
ATOM   368  O O    . TYR A 1 20  ? 17.105 4.606  15.299 1.000 10.73  ? 20  TYR A O    1 
ATOM   369  C CB   . TYR A 1 20  ? 15.785 6.844  16.860 1.000 10.87  ? 20  TYR A CB   1 
ATOM   370  C CG   . TYR A 1 20  ? 15.309 7.690  15.706 1.000 10.39  ? 20  TYR A CG   1 
ATOM   371  C CD1  . TYR A 1 20  ? 14.041 8.159  15.646 1.000 15.22  ? 20  TYR A CD1  1 
ATOM   372  C CD2  . TYR A 1 20  ? 16.101 7.950  14.621 1.000 12.49  ? 20  TYR A CD2  1 
ATOM   373  C CE1  . TYR A 1 20  ? 13.585 8.914  14.596 1.000 17.69  ? 20  TYR A CE1  1 
ATOM   374  C CE2  . TYR A 1 20  ? 15.651 8.673  13.582 1.000 15.01  ? 20  TYR A CE2  1 
ATOM   375  C CZ   . TYR A 1 20  ? 14.399 9.161  13.543 1.000 16.30  ? 20  TYR A CZ   1 
ATOM   376  O OH   . TYR A 1 20  ? 13.921 9.891  12.482 1.000 24.16  ? 20  TYR A OH   1 
ATOM   377  H H    . TYR A 1 20  ? 16.334 4.944  18.398 1.000 12.22  ? 20  TYR A H    1 
ATOM   378  H HA   . TYR A 1 20  ? 14.343 5.372  16.670 1.000 12.21  ? 20  TYR A HA   1 
ATOM   379  H HB2  . TYR A 1 20  ? 15.439 7.207  17.690 1.000 13.04  ? 20  TYR A HB2  1 
ATOM   380  H HB3  . TYR A 1 20  ? 16.754 6.871  16.901 1.000 13.04  ? 20  TYR A HB3  1 
ATOM   381  H HD1  . TYR A 1 20  ? 13.457 7.962  16.343 1.000 18.27  ? 20  TYR A HD1  1 
ATOM   382  H HD2  . TYR A 1 20  ? 16.970 7.619  14.602 1.000 14.98  ? 20  TYR A HD2  1 
ATOM   383  H HE1  . TYR A 1 20  ? 12.720 9.255  14.607 1.000 21.22  ? 20  TYR A HE1  1 
ATOM   384  H HE2  . TYR A 1 20  ? 16.223 8.841  12.868 1.000 18.02  ? 20  TYR A HE2  1 
ATOM   385  H HH   . TYR A 1 20  ? 14.518 9.993  11.929 1.000 36.23  ? 20  TYR A HH   1 
ATOM   386  N N    . ARG A 1 21  ? 15.002 4.332  14.561 1.000 10.69  ? 21  ARG A N    1 
ATOM   387  C CA   . ARG A 1 21  ? 15.334 3.661  13.352 1.000 11.53  ? 21  ARG A CA   1 
ATOM   388  C C    . ARG A 1 21  ? 16.244 2.467  13.614 1.000 11.15  ? 21  ARG A C    1 
ATOM   389  O O    . ARG A 1 21  ? 17.090 2.109  12.778 1.000 13.01  ? 21  ARG A O    1 
ATOM   390  C CB   . ARG A 1 21  ? 15.889 4.601  12.290 1.000 14.09  ? 21  ARG A CB   1 
ATOM   391  C CG   . ARG A 1 21  ? 14.841 5.597  11.871 1.000 16.66  ? 21  ARG A CG   1 
ATOM   392  C CD   . ARG A 1 21  ? 13.564 4.961  11.216 1.000 22.89  ? 21  ARG A CD   1 
ATOM   393  N NE   . ARG A 1 21  ? 13.897 4.233  9.993  1.000 33.76  ? 21  ARG A NE   1 
ATOM   394  C CZ   . ARG A 1 21  ? 14.174 4.775  8.807  1.000 38.35  ? 21  ARG A CZ   1 
ATOM   395  N NH1  . ARG A 1 21  ? 13.976 6.075  8.636  1.000 36.85  ? 21  ARG A NH1  1 
ATOM   396  N NH2  . ARG A 1 21  ? 14.632 4.046  7.799  1.000 48.94  ? 21  ARG A NH2  1 
ATOM   397  H H    . ARG A 1 21  ? 14.169 4.472  14.721 1.000 12.83  ? 21  ARG A H    1 
ATOM   398  H HA   . ARG A 1 21  ? 14.496 3.300  12.995 1.000 13.84  ? 21  ARG A HA   1 
ATOM   399  H HB2  . ARG A 1 21  ? 16.661 5.070  12.643 1.000 16.90  ? 21  ARG A HB2  1 
ATOM   400  H HB3  . ARG A 1 21  ? 16.176 4.086  11.519 1.000 16.90  ? 21  ARG A HB3  1 
ATOM   401  H HG2  . ARG A 1 21  ? 14.569 6.106  12.650 1.000 19.99  ? 21  ARG A HG2  1 
ATOM   402  H HG3  . ARG A 1 21  ? 15.238 6.216  11.239 1.000 19.99  ? 21  ARG A HG3  1 
ATOM   403  H HD2  . ARG A 1 21  ? 13.147 4.355  11.848 1.000 27.47  ? 21  ARG A HD2  1 
ATOM   404  H HD3  . ARG A 1 21  ? 12.927 5.663  11.009 1.000 27.47  ? 21  ARG A HD3  1 
ATOM   405  H HE   . ARG A 1 21  ? 13.916 3.375  10.043 1.000 40.51  ? 21  ARG A HE   1 
ATOM   406  H HH11 . ARG A 1 21  ? 14.146 6.440  7.876  1.000 44.23  ? 21  ARG A HH11 1 
ATOM   407  H HH12 . ARG A 1 21  ? 13.679 6.554  9.286  1.000 44.23  ? 21  ARG A HH12 1 
ATOM   408  H HH21 . ARG A 1 21  ? 14.799 4.417  7.041  1.000 58.73  ? 21  ARG A HH21 1 
ATOM   409  H HH22 . ARG A 1 21  ? 14.762 3.203  7.903  1.000 58.73  ? 21  ARG A HH22 1 
ATOM   410  N N    . GLY A 1 22  ? 16.053 1.798  14.760 1.000 10.85  ? 22  GLY A N    1 
ATOM   411  C CA   . GLY A 1 22  ? 16.747 0.602  15.071 1.000 11.41  ? 22  GLY A CA   1 
ATOM   412  C C    . GLY A 1 22  ? 18.138 0.752  15.653 1.000 10.94  ? 22  GLY A C    1 
ATOM   413  O O    . GLY A 1 22  ? 18.852 -0.240 15.755 1.000 15.07  ? 22  GLY A O    1 
ATOM   414  H H    . GLY A 1 22  ? 15.488 2.107  15.330 1.000 13.02  ? 22  GLY A H    1 
ATOM   415  H HA2  . GLY A 1 22  ? 16.210 0.096  15.701 1.000 13.69  ? 22  GLY A HA2  1 
ATOM   416  H HA3  . GLY A 1 22  ? 16.815 0.073  14.261 1.000 13.69  ? 22  GLY A HA3  1 
ATOM   417  N N    . TYR A 1 23  ? 18.511 1.974  16.031 1.000 9.94   ? 23  TYR A N    1 
ATOM   418  C CA   . TYR A 1 23  ? 19.780 2.227  16.658 1.000 10.13  ? 23  TYR A CA   1 
ATOM   419  C C    . TYR A 1 23  ? 19.626 2.450  18.151 1.000 9.69   ? 23  TYR A C    1 
ATOM   420  O O    . TYR A 1 23  ? 19.021 3.423  18.596 1.000 10.69  ? 23  TYR A O    1 
ATOM   421  C CB   . TYR A 1 23  ? 20.452 3.436  16.014 1.000 10.81  ? 23  TYR A CB   1 
ATOM   422  C CG   . TYR A 1 23  ? 20.878 3.166  14.584 1.000 11.18  ? 23  TYR A CG   1 
ATOM   423  C CD1  . TYR A 1 23  ? 21.999 2.443  14.266 1.000 12.50  ? 23  TYR A CD1  1 
ATOM   424  C CD2  . TYR A 1 23  ? 20.110 3.621  13.523 1.000 12.80  ? 23  TYR A CD2  1 
ATOM   425  C CE1  . TYR A 1 23  ? 22.384 2.220  12.955 1.000 14.15  ? 23  TYR A CE1  1 
ATOM   426  C CE2  . TYR A 1 23  ? 20.474 3.432  12.204 1.000 14.68  ? 23  TYR A CE2  1 
ATOM   427  C CZ   . TYR A 1 23  ? 21.594 2.700  11.945 1.000 14.00  ? 23  TYR A CZ   1 
ATOM   428  O OH   . TYR A 1 23  ? 21.997 2.513  10.651 1.000 18.81  ? 23  TYR A OH   1 
ATOM   429  H H    . TYR A 1 23  ? 17.975 2.633  15.895 1.000 11.93  ? 23  TYR A H    1 
ATOM   430  H HA   . TYR A 1 23  ? 20.354 1.445  16.520 1.000 12.15  ? 23  TYR A HA   1 
ATOM   431  H HB2  . TYR A 1 23  ? 19.836 4.186  16.026 1.000 12.97  ? 23  TYR A HB2  1 
ATOM   432  H HB3  . TYR A 1 23  ? 21.231 3.682  16.536 1.000 12.97  ? 23  TYR A HB3  1 
ATOM   433  H HD1  . TYR A 1 23  ? 22.517 2.091  14.953 1.000 15.00  ? 23  TYR A HD1  1 
ATOM   434  H HD2  . TYR A 1 23  ? 19.317 4.072  13.707 1.000 15.36  ? 23  TYR A HD2  1 
ATOM   435  H HE1  . TYR A 1 23  ? 23.165 1.753  12.763 1.000 16.98  ? 23  TYR A HE1  1 
ATOM   436  H HE2  . TYR A 1 23  ? 19.970 3.795  11.511 1.000 17.61  ? 23  TYR A HE2  1 
ATOM   437  H HH   . TYR A 1 23  ? 22.692 2.078  10.642 1.000 28.21  ? 23  TYR A HH   1 
ATOM   438  N N    A SER A 1 24  ? 20.152 1.530  18.947 0.200 10.67  ? 24  SER A N    1 
ATOM   439  N N    B SER A 1 24  ? 20.168 1.546  18.949 0.800 10.85  ? 24  SER A N    1 
ATOM   440  C CA   A SER A 1 24  ? 20.114 1.523  20.396 0.200 10.46  ? 24  SER A CA   1 
ATOM   441  C CA   B SER A 1 24  ? 20.075 1.628  20.383 0.800 10.66  ? 24  SER A CA   1 
ATOM   442  C C    A SER A 1 24  ? 20.878 2.707  20.997 0.200 9.83   ? 24  SER A C    1 
ATOM   443  C C    B SER A 1 24  ? 20.800 2.878  20.896 0.800 9.97   ? 24  SER A C    1 
ATOM   444  O O    A SER A 1 24  ? 21.913 3.044  20.408 0.200 9.33   ? 24  SER A O    1 
ATOM   445  O O    B SER A 1 24  ? 21.690 3.458  20.260 0.800 10.27  ? 24  SER A O    1 
ATOM   446  C CB   A SER A 1 24  ? 20.730 0.229  20.924 0.200 14.06  ? 24  SER A CB   1 
ATOM   447  C CB   B SER A 1 24  ? 20.658 0.395  21.058 0.800 12.85  ? 24  SER A CB   1 
ATOM   448  O OG   A SER A 1 24  ? 19.952 -0.909 20.657 0.200 20.85  ? 24  SER A OG   1 
ATOM   449  O OG   B SER A 1 24  ? 22.041 0.317  20.786 0.800 15.91  ? 24  SER A OG   1 
ATOM   450  H H    A SER A 1 24  ? 20.555 0.873  18.567 0.200 12.80  ? 24  SER A H    1 
ATOM   451  H H    B SER A 1 24  ? 20.592 0.885  18.599 0.800 13.02  ? 24  SER A H    1 
ATOM   452  H HA   A SER A 1 24  ? 19.180 1.570  20.687 0.200 12.55  ? 24  SER A HA   1 
ATOM   453  H HA   B SER A 1 24  ? 19.128 1.696  20.628 0.800 12.79  ? 24  SER A HA   1 
ATOM   454  H HB2  A SER A 1 24  ? 21.605 0.112  20.523 0.200 16.87  ? 24  SER A HB2  1 
ATOM   455  H HB2  B SER A 1 24  ? 20.515 0.447  22.016 0.800 15.42  ? 24  SER A HB2  1 
ATOM   456  H HB3  A SER A 1 24  ? 20.852 0.308  21.883 0.200 16.87  ? 24  SER A HB3  1 
ATOM   457  H HB3  B SER A 1 24  ? 20.214 -0.402 20.728 0.800 15.42  ? 24  SER A HB3  1 
ATOM   458  H HG   A SER A 1 24  ? 19.377 -0.724 20.103 0.200 31.27  ? 24  SER A HG   1 
ATOM   459  H HG   B SER A 1 24  ? 22.162 0.335  19.975 0.800 23.86  ? 24  SER A HG   1 
ATOM   460  N N    . LEU A 1 25  ? 20.424 3.271  22.107 1.000 10.39  ? 25  LEU A N    1 
ATOM   461  C CA   . LEU A 1 25  ? 20.960 4.448  22.734 1.000 10.11  ? 25  LEU A CA   1 
ATOM   462  C C    . LEU A 1 25  ? 22.472 4.463  22.754 1.000 9.46   ? 25  LEU A C    1 
ATOM   463  O O    . LEU A 1 25  ? 23.069 5.527  22.557 1.000 10.56  ? 25  LEU A O    1 
ATOM   464  C CB   . LEU A 1 25  ? 20.375 4.563  24.148 1.000 10.54  ? 25  LEU A CB   1 
ATOM   465  C CG   . LEU A 1 25  ? 20.664 5.834  24.909 1.000 11.92  ? 25  LEU A CG   1 
ATOM   466  C CD1  . LEU A 1 25  ? 20.052 7.031  24.195 1.000 16.74  ? 25  LEU A CD1  1 
ATOM   467  C CD2  . LEU A 1 25  ? 20.081 5.727  26.287 1.000 14.21  ? 25  LEU A CD2  1 
ATOM   468  H H    A LEU A 1 25  ? 19.747 2.900  22.486 1.000 12.47  ? 25  LEU A H    1 
ATOM   469  H HA   . LEU A 1 25  ? 20.658 5.226  22.220 1.000 12.13  ? 25  LEU A HA   1 
ATOM   470  H HB2  . LEU A 1 25  ? 19.413 4.463  24.084 1.000 12.65  ? 25  LEU A HB2  1 
ATOM   471  H HB3  . LEU A 1 25  ? 20.708 3.818  24.672 1.000 12.65  ? 25  LEU A HB3  1 
ATOM   472  H HG   . LEU A 1 25  ? 21.633 5.958  24.977 1.000 14.31  ? 25  LEU A HG   1 
ATOM   473  H HD11 . LEU A 1 25  ? 20.424 7.101  23.312 1.000 25.10  ? 25  LEU A HD11 1 
ATOM   474  H HD12 . LEU A 1 25  ? 19.101 6.915  24.133 1.000 25.10  ? 25  LEU A HD12 1 
ATOM   475  H HD13 . LEU A 1 25  ? 20.246 7.832  24.688 1.000 25.10  ? 25  LEU A HD13 1 
ATOM   476  H HD21 . LEU A 1 25  ? 20.262 6.534  26.775 1.000 21.31  ? 25  LEU A HD21 1 
ATOM   477  H HD22 . LEU A 1 25  ? 19.132 5.597  26.224 1.000 21.31  ? 25  LEU A HD22 1 
ATOM   478  H HD23 . LEU A 1 25  ? 20.475 4.981  26.744 1.000 21.31  ? 25  LEU A HD23 1 
ATOM   479  N N    . GLY A 1 26  ? 23.118 3.351  23.077 1.000 9.78   ? 26  GLY A N    1 
ATOM   480  C CA   . GLY A 1 26  ? 24.564 3.355  23.154 1.000 10.23  ? 26  GLY A CA   1 
ATOM   481  C C    . GLY A 1 26  ? 25.241 3.736  21.872 1.000 9.25   ? 26  GLY A C    1 
ATOM   482  O O    . GLY A 1 26  ? 26.344 4.292  21.906 1.000 10.15  ? 26  GLY A O    1 
ATOM   483  H H    . GLY A 1 26  ? 22.680 2.629  23.239 1.000 11.74  ? 26  GLY A H    1 
ATOM   484  H HA2  . GLY A 1 26  ? 24.837 3.975  23.848 1.000 12.28  ? 26  GLY A HA2  1 
ATOM   485  H HA3  . GLY A 1 26  ? 24.865 2.470  23.415 1.000 12.28  ? 26  GLY A HA3  1 
ATOM   486  N N    . ASN A 1 27  ? 24.639 3.455  20.723 1.000 9.27   ? 27  ASN A N    1 
ATOM   487  C CA   . ASN A 1 27  ? 25.212 3.924  19.461 1.000 8.90   ? 27  ASN A CA   1 
ATOM   488  C C    . ASN A 1 27  ? 25.343 5.424  19.401 1.000 8.54   ? 27  ASN A C    1 
ATOM   489  O O    . ASN A 1 27  ? 26.338 5.946  18.889 1.000 9.21   ? 27  ASN A O    1 
ATOM   490  C CB   . ASN A 1 27  ? 24.348 3.458  18.276 1.000 9.68   ? 27  ASN A CB   1 
ATOM   491  C CG   . ASN A 1 27  ? 24.538 2.005  17.956 1.000 11.00  ? 27  ASN A CG   1 
ATOM   492  O OD1  . ASN A 1 27  ? 25.606 1.627  17.469 1.000 12.82  ? 27  ASN A OD1  1 
ATOM   493  N ND2  . ASN A 1 27  ? 23.510 1.223  18.226 1.000 14.98  ? 27  ASN A ND2  1 
ATOM   494  H H    . ASN A 1 27  ? 23.912 2.996  20.720 1.000 11.12  ? 27  ASN A H    1 
ATOM   495  H HA   . ASN A 1 27  ? 26.106 3.532  19.363 1.000 10.68  ? 27  ASN A HA   1 
ATOM   496  H HB2  . ASN A 1 27  ? 23.414 3.617  18.484 1.000 11.62  ? 27  ASN A HB2  1 
ATOM   497  H HB3  . ASN A 1 27  ? 24.572 3.986  17.494 1.000 11.62  ? 27  ASN A HB3  1 
ATOM   498  H HD21 . ASN A 1 27  ? 23.556 0.380  18.061 1.000 17.97  ? 27  ASN A HD21 1 
ATOM   499  H HD22 . ASN A 1 27  ? 22.794 1.555  18.566 1.000 17.97  ? 27  ASN A HD22 1 
ATOM   500  N N    . TRP A 1 28  ? 24.307 6.126  19.859 1.000 8.61   ? 28  TRP A N    1 
ATOM   501  C CA   . TRP A 1 28  ? 24.280 7.568  19.818 1.000 8.56   ? 28  TRP A CA   1 
ATOM   502  C C    . TRP A 1 28  ? 25.267 8.199  20.775 1.000 8.38   ? 28  TRP A C    1 
ATOM   503  O O    . TRP A 1 28  ? 25.921 9.183  20.464 1.000 9.31   ? 28  TRP A O    1 
ATOM   504  C CB   . TRP A 1 28  ? 22.858 8.067  20.099 1.000 9.09   ? 28  TRP A CB   1 
ATOM   505  C CG   . TRP A 1 28  ? 21.865 7.586  19.114 1.000 8.76   ? 28  TRP A CG   1 
ATOM   506  C CD1  . TRP A 1 28  ? 21.013 6.548  19.255 1.000 10.66  ? 28  TRP A CD1  1 
ATOM   507  C CD2  . TRP A 1 28  ? 21.622 8.131  17.801 1.000 9.99   ? 28  TRP A CD2  1 
ATOM   508  N NE1  . TRP A 1 28  ? 20.258 6.376  18.133 1.000 12.59  ? 28  TRP A NE1  1 
ATOM   509  C CE2  . TRP A 1 28  ? 20.593 7.327  17.238 1.000 12.04  ? 28  TRP A CE2  1 
ATOM   510  C CE3  . TRP A 1 28  ? 22.168 9.175  17.107 1.000 13.80  ? 28  TRP A CE3  1 
ATOM   511  C CZ2  . TRP A 1 28  ? 20.117 7.588  15.942 1.000 18.27  ? 28  TRP A CZ2  1 
ATOM   512  C CZ3  . TRP A 1 28  ? 21.701 9.459  15.827 1.000 20.92  ? 28  TRP A CZ3  1 
ATOM   513  C CH2  . TRP A 1 28  ? 20.692 8.645  15.312 1.000 22.34  ? 28  TRP A CH2  1 
ATOM   514  H H    . TRP A 1 28  ? 23.633 5.707  20.190 1.000 10.33  ? 28  TRP A H    1 
ATOM   515  H HA   . TRP A 1 28  ? 24.522 7.847  18.910 1.000 10.27  ? 28  TRP A HA   1 
ATOM   516  H HB2  . TRP A 1 28  ? 22.590 7.773  20.984 1.000 10.91  ? 28  TRP A HB2  1 
ATOM   517  H HB3  . TRP A 1 28  ? 22.858 9.037  20.097 1.000 10.91  ? 28  TRP A HB3  1 
ATOM   518  H HD1  . TRP A 1 28  ? 20.950 6.019  20.018 1.000 12.80  ? 28  TRP A HD1  1 
ATOM   519  H HE1  . TRP A 1 28  ? 19.666 5.763  18.016 1.000 15.11  ? 28  TRP A HE1  1 
ATOM   520  H HE3  . TRP A 1 28  ? 22.843 9.690  17.487 1.000 16.56  ? 28  TRP A HE3  1 
ATOM   521  H HZ2  . TRP A 1 28  ? 19.453 7.072  15.543 1.000 21.92  ? 28  TRP A HZ2  1 
ATOM   522  H HZ3  . TRP A 1 28  ? 22.050 10.165 15.332 1.000 25.10  ? 28  TRP A HZ3  1 
ATOM   523  H HH2  . TRP A 1 28  ? 20.383 8.845  14.458 1.000 26.81  ? 28  TRP A HH2  1 
ATOM   524  N N    . VAL A 1 29  ? 25.397 7.608  21.971 1.000 8.38   ? 29  VAL A N    1 
ATOM   525  C CA   . VAL A 1 29  ? 26.356 8.095  22.944 1.000 8.57   ? 29  VAL A CA   1 
ATOM   526  C C    . VAL A 1 29  ? 27.764 7.870  22.426 1.000 8.50   ? 29  VAL A C    1 
ATOM   527  O O    . VAL A 1 29  ? 28.621 8.736  22.513 1.000 9.60   ? 29  VAL A O    1 
ATOM   528  C CB   . VAL A 1 29  ? 26.111 7.445  24.307 1.000 9.24   ? 29  VAL A CB   1 
ATOM   529  C CG1  . VAL A 1 29  ? 27.155 7.920  25.322 1.000 11.86  ? 29  VAL A CG1  1 
ATOM   530  C CG2  . VAL A 1 29  ? 24.708 7.788  24.828 1.000 11.26  ? 29  VAL A CG2  1 
ATOM   531  H H    . VAL A 1 29  ? 24.905 6.930  22.165 1.000 10.05  ? 29  VAL A H    1 
ATOM   532  H HA   . VAL A 1 29  ? 26.221 9.061  23.042 1.000 10.28  ? 29  VAL A HA   1 
ATOM   533  H HB   . VAL A 1 29  ? 26.184 6.472  24.211 1.000 11.08  ? 29  VAL A HB   1 
ATOM   534  H HG11 . VAL A 1 29  ? 26.989 7.503  26.171 1.000 17.79  ? 29  VAL A HG11 1 
ATOM   535  H HG12 . VAL A 1 29  ? 28.033 7.680  25.015 1.000 17.79  ? 29  VAL A HG12 1 
ATOM   536  H HG13 . VAL A 1 29  ? 27.099 8.873  25.417 1.000 17.79  ? 29  VAL A HG13 1 
ATOM   537  H HG21 . VAL A 1 29  ? 24.574 7.372  25.682 1.000 16.89  ? 29  VAL A HG21 1 
ATOM   538  H HG22 . VAL A 1 29  ? 24.625 8.740  24.919 1.000 16.89  ? 29  VAL A HG22 1 
ATOM   539  H HG23 . VAL A 1 29  ? 24.049 7.467  24.208 1.000 16.89  ? 29  VAL A HG23 1 
ATOM   540  N N    . CYS A 1 30  ? 28.023 6.690  21.867 1.000 8.80   ? 30  CYS A N    1 
ATOM   541  C CA   . CYS A 1 30  ? 29.320 6.381  21.287 1.000 9.27   ? 30  CYS A CA   1 
ATOM   542  C C    . CYS A 1 30  ? 29.682 7.363  20.167 1.000 8.73   ? 30  CYS A C    1 
ATOM   543  O O    . CYS A 1 30  ? 30.804 7.854  20.098 1.000 9.53   ? 30  CYS A O    1 
ATOM   544  C CB   . CYS A 1 30  ? 29.320 4.914  20.809 1.000 9.72   ? 30  CYS A CB   1 
ATOM   545  S SG   . CYS A 1 30  ? 30.919 4.343  20.208 1.000 11.21  ? 30  CYS A SG   1 
ATOM   546  H H    . CYS A 1 30  ? 27.405 6.092  21.848 1.000 10.56  ? 30  CYS A H    1 
ATOM   547  H HA   . CYS A 1 30  ? 29.994 6.468  21.993 1.000 11.13  ? 30  CYS A HA   1 
ATOM   548  H HB2  . CYS A 1 30  ? 29.042 4.346  21.545 1.000 11.66  ? 30  CYS A HB2  1 
ATOM   549  H HB3  . CYS A 1 30  ? 28.667 4.817  20.099 1.000 11.66  ? 30  CYS A HB3  1 
ATOM   550  N N    . ALA A 1 31  ? 28.726 7.638  19.288 1.000 8.55   ? 31  ALA A N    1 
ATOM   551  C CA   . ALA A 1 31  ? 28.971 8.549  18.197 1.000 9.01   ? 31  ALA A CA   1 
ATOM   552  C C    . ALA A 1 31  ? 29.379 9.917  18.750 1.000 8.47   ? 31  ALA A C    1 
ATOM   553  O O    . ALA A 1 31  ? 30.342 10.527 18.252 1.000 9.65   ? 31  ALA A O    1 
ATOM   554  C CB   . ALA A 1 31  ? 27.779 8.673  17.293 1.000 10.39  ? 31  ALA A CB   1 
ATOM   555  H H    . ALA A 1 31  ? 27.953 7.270  19.371 1.000 10.26  ? 31  ALA A H    1 
ATOM   556  H HA   . ALA A 1 31  ? 29.718 8.198  17.670 1.000 10.81  ? 31  ALA A HA   1 
ATOM   557  H HB1  . ALA A 1 31  ? 27.979 9.285  16.582 1.000 15.59  ? 31  ALA A HB1  1 
ATOM   558  H HB2  . ALA A 1 31  ? 27.566 7.812  16.925 1.000 15.59  ? 31  ALA A HB2  1 
ATOM   559  H HB3  . ALA A 1 31  ? 27.029 9.000  17.795 1.000 15.59  ? 31  ALA A HB3  1 
ATOM   560  N N    . ALA A 1 32  ? 28.658 10.429 19.740 1.000 8.22   ? 32  ALA A N    1 
ATOM   561  C CA   . ALA A 1 32  ? 29.005 11.716 20.311 1.000 8.32   ? 32  ALA A CA   1 
ATOM   562  C C    . ALA A 1 32  ? 30.368 11.723 20.964 1.000 8.09   ? 32  ALA A C    1 
ATOM   563  O O    . ALA A 1 32  ? 31.115 12.684 20.869 1.000 9.71   ? 32  ALA A O    1 
ATOM   564  C CB   . ALA A 1 32  ? 27.939 12.138 21.310 1.000 9.93   ? 32  ALA A CB   1 
ATOM   565  H H    . ALA A 1 32  ? 27.982 9.994  20.044 1.000 9.86   ? 32  ALA A H    1 
ATOM   566  H HA   . ALA A 1 32  ? 29.015 12.375 19.585 1.000 9.98   ? 32  ALA A HA   1 
ATOM   567  H HB1  . ALA A 1 32  ? 28.172 12.990 21.686 1.000 14.90  ? 32  ALA A HB1  1 
ATOM   568  H HB2  . ALA A 1 32  ? 27.091 12.205 20.865 1.000 14.90  ? 32  ALA A HB2  1 
ATOM   569  H HB3  . ALA A 1 32  ? 27.881 11.484 22.011 1.000 14.90  ? 32  ALA A HB3  1 
ATOM   570  N N    . LYS A 1 33  ? 30.725 10.628 21.655 1.000 8.33   ? 33  LYS A N    1 
ATOM   571  C CA   . LYS A 1 33  ? 32.035 10.551 22.299 1.000 8.84   ? 33  LYS A CA   1 
ATOM   572  C C    . LYS A 1 33  ? 33.130 10.734 21.276 1.000 8.74   ? 33  LYS A C    1 
ATOM   573  O O    . LYS A 1 33  ? 34.073 11.515 21.503 1.000 10.57  ? 33  LYS A O    1 
ATOM   574  C CB   . LYS A 1 33  ? 32.183 9.171  22.964 1.000 9.89   ? 33  LYS A CB   1 
ATOM   575  C CG   . LYS A 1 33  ? 33.590 8.868  23.477 1.000 12.68  ? 33  LYS A CG   1 
ATOM   576  C CD   . LYS A 1 33  ? 34.045 9.837  24.603 1.000 15.06  ? 33  LYS A CD   1 
ATOM   577  C CE   . LYS A 1 33  ? 35.488 9.427  24.931 1.000 18.98  ? 33  LYS A CE   1 
ATOM   578  N NZ   . LYS A 1 33  ? 36.029 10.333 25.992 1.000 24.87  ? 33  LYS A NZ   1 
ATOM   579  H H    . LYS A 1 33  ? 30.179 9.967  21.718 1.000 9.99   ? 33  LYS A H    1 
ATOM   580  H HA   . LYS A 1 33  ? 32.105 11.251 22.981 1.000 10.60  ? 33  LYS A HA   1 
ATOM   581  H HB2  . LYS A 1 33  ? 31.563 9.117  23.708 1.000 11.86  ? 33  LYS A HB2  1 
ATOM   582  H HB3  . LYS A 1 33  ? 31.933 8.488  22.323 1.000 11.86  ? 33  LYS A HB3  1 
ATOM   583  H HG2  . LYS A 1 33  ? 33.615 7.958  23.815 1.000 15.22  ? 33  LYS A HG2  1 
ATOM   584  H HG3  . LYS A 1 33  ? 34.216 8.926  22.738 1.000 15.22  ? 33  LYS A HG3  1 
ATOM   585  H HD2  . LYS A 1 33  ? 34.011 10.757 24.297 1.000 18.08  ? 33  LYS A HD2  1 
ATOM   586  H HD3  . LYS A 1 33  ? 33.477 9.746  25.383 1.000 18.08  ? 33  LYS A HD3  1 
ATOM   587  H HE2  . LYS A 1 33  ? 35.506 8.508  25.242 1.000 22.77  ? 33  LYS A HE2  1 
ATOM   588  H HE3  . LYS A 1 33  ? 36.037 9.489  24.134 1.000 22.77  ? 33  LYS A HE3  1 
ATOM   589  H HZ1  . LYS A 1 33  ? 36.865 10.098 26.185 1.000 37.30  ? 33  LYS A HZ1  1 
ATOM   590  H HZ2  . LYS A 1 33  ? 36.017 11.173 25.699 1.000 37.30  ? 33  LYS A HZ2  1 
ATOM   591  H HZ3  . LYS A 1 33  ? 35.526 10.267 26.724 1.000 37.30  ? 33  LYS A HZ3  1 
ATOM   592  N N    . PHE A 1 34  ? 33.076 10.022 20.167 1.000 8.87   ? 34  PHE A N    1 
ATOM   593  C CA   . PHE A 1 34  ? 34.172 10.028 19.219 1.000 9.51   ? 34  PHE A CA   1 
ATOM   594  C C    . PHE A 1 34  ? 34.106 11.158 18.212 1.000 10.26  ? 34  PHE A C    1 
ATOM   595  O O    . PHE A 1 34  ? 35.105 11.525 17.646 1.000 14.00  ? 34  PHE A O    1 
ATOM   596  C CB   . PHE A 1 34  ? 34.354 8.638  18.594 1.000 10.77  ? 34  PHE A CB   1 
ATOM   597  C CG   . PHE A 1 34  ? 34.846 7.665  19.626 1.000 11.04  ? 34  PHE A CG   1 
ATOM   598  C CD1  . PHE A 1 34  ? 36.110 7.780  20.176 1.000 12.32  ? 34  PHE A CD1  1 
ATOM   599  C CD2  . PHE A 1 34  ? 34.007 6.654  20.073 1.000 13.05  ? 34  PHE A CD2  1 
ATOM   600  C CE1  . PHE A 1 34  ? 36.545 6.853  21.113 1.000 15.99  ? 34  PHE A CE1  1 
ATOM   601  C CE2  . PHE A 1 34  ? 34.459 5.737  21.012 1.000 16.66  ? 34  PHE A CE2  1 
ATOM   602  C CZ   . PHE A 1 34  ? 35.700 5.854  21.522 1.000 16.71  ? 34  PHE A CZ   1 
ATOM   603  H H    . PHE A 1 34  ? 32.379 9.546  20.004 1.000 10.65  ? 34  PHE A H    1 
ATOM   604  H HA   . PHE A 1 34  ? 34.981 10.190 19.748 1.000 11.42  ? 34  PHE A HA   1 
ATOM   605  H HB2  . PHE A 1 34  ? 33.509 8.330  18.232 1.000 12.92  ? 34  PHE A HB2  1 
ATOM   606  H HB3  . PHE A 1 34  ? 34.993 8.690  17.865 1.000 12.92  ? 34  PHE A HB3  1 
ATOM   607  H HD1  . PHE A 1 34  ? 36.668 8.478  19.919 1.000 14.78  ? 34  PHE A HD1  1 
ATOM   608  H HD2  . PHE A 1 34  ? 33.140 6.590  19.742 1.000 15.66  ? 34  PHE A HD2  1 
ATOM   609  H HE1  . PHE A 1 34  ? 37.405 6.909  21.461 1.000 19.19  ? 34  PHE A HE1  1 
ATOM   610  H HE2  . PHE A 1 34  ? 33.906 5.043  21.289 1.000 19.99  ? 34  PHE A HE2  1 
ATOM   611  H HZ   . PHE A 1 34  ? 35.989 5.247  22.164 1.000 20.05  ? 34  PHE A HZ   1 
ATOM   612  N N    . GLU A 1 35  ? 32.925 11.744 17.993 1.000 8.67   ? 35  GLU A N    1 
ATOM   613  C CA   . GLU A 1 35  ? 32.818 12.916 17.131 1.000 8.68   ? 35  GLU A CA   1 
ATOM   614  C C    . GLU A 1 35  ? 33.333 14.176 17.828 1.000 8.82   ? 35  GLU A C    1 
ATOM   615  O O    . GLU A 1 35  ? 34.046 14.953 17.224 1.000 10.48  ? 35  GLU A O    1 
ATOM   616  C CB   . GLU A 1 35  ? 31.385 13.133 16.663 1.000 8.84   ? 35  GLU A CB   1 
ATOM   617  C CG   . GLU A 1 35  ? 30.907 12.151 15.622 1.000 10.31  ? 35  GLU A CG   1 
ATOM   618  C CD   . GLU A 1 35  ? 31.597 12.231 14.268 1.000 11.13  ? 35  GLU A CD   1 
ATOM   619  O OE1  . GLU A 1 35  ? 32.273 13.306 14.075 1.000 14.13  ? 35  GLU A OE1  1 
ATOM   620  O OE2  . GLU A 1 35  ? 31.451 11.321 13.455 1.000 14.68  ? 35  GLU A OE2  1 
ATOM   621  H H    . GLU A 1 35  ? 32.218 11.426 18.366 1.000 10.40  ? 35  GLU A H    1 
ATOM   622  H HA   . GLU A 1 35  ? 33.374 12.760 16.339 1.000 10.42  ? 35  GLU A HA   1 
ATOM   623  H HB2  . GLU A 1 35  ? 30.797 13.078 17.432 1.000 10.60  ? 35  GLU A HB2  1 
ATOM   624  H HB3  . GLU A 1 35  ? 31.310 14.029 16.300 1.000 10.60  ? 35  GLU A HB3  1 
ATOM   625  H HG2  . GLU A 1 35  ? 31.025 11.254 15.971 1.000 12.37  ? 35  GLU A HG2  1 
ATOM   626  H HG3  . GLU A 1 35  ? 29.956 12.288 15.487 1.000 12.37  ? 35  GLU A HG3  1 
ATOM   627  N N    . SER A 1 36  ? 32.906 14.402 19.079 1.000 9.47   ? 36  SER A N    1 
ATOM   628  C CA   . SER A 1 36  ? 33.097 15.680 19.736 1.000 9.58   ? 36  SER A CA   1 
ATOM   629  C C    . SER A 1 36  ? 33.682 15.577 21.126 1.000 9.37   ? 36  SER A C    1 
ATOM   630  O O    . SER A 1 36  ? 33.883 16.618 21.782 1.000 10.62  ? 36  SER A O    1 
ATOM   631  C CB   . SER A 1 36  ? 31.796 16.446 19.868 1.000 9.53   ? 36  SER A CB   1 
ATOM   632  O OG   . SER A 1 36  ? 30.934 15.772 20.746 1.000 9.11   ? 36  SER A OG   1 
ATOM   633  H H    . SER A 1 36  ? 32.506 13.770 19.505 1.000 11.36  ? 36  SER A H    1 
ATOM   634  H HA   . SER A 1 36  ? 33.709 16.215 19.188 1.000 11.50  ? 36  SER A HA   1 
ATOM   635  H HB2  . SER A 1 36  ? 31.974 17.338 20.205 1.000 11.44  ? 36  SER A HB2  1 
ATOM   636  H HB3  . SER A 1 36  ? 31.376 16.529 18.997 1.000 11.44  ? 36  SER A HB3  1 
ATOM   637  H HG   . SER A 1 36  ? 31.281 15.725 21.487 1.000 13.67  ? 36  SER A HG   1 
ATOM   638  N N    A ASN A 1 37  ? 33.875 14.395 21.683 0.522 9.43   ? 37  ASN A N    1 
ATOM   639  N N    B ASN A 1 37  ? 33.914 14.376 21.624 0.478 10.04  ? 37  ASN A N    1 
ATOM   640  C CA   A ASN A 1 37  ? 34.302 14.287 23.098 0.522 10.87  ? 37  ASN A CA   1 
ATOM   641  C CA   B ASN A 1 37  ? 34.217 14.126 23.041 0.478 10.15  ? 37  ASN A CA   1 
ATOM   642  C C    A ASN A 1 37  ? 33.247 14.856 24.028 0.522 9.50   ? 37  ASN A C    1 
ATOM   643  C C    B ASN A 1 37  ? 33.257 14.891 23.942 0.478 9.54   ? 37  ASN A C    1 
ATOM   644  O O    A ASN A 1 37  ? 33.484 15.278 25.153 0.522 12.11  ? 37  ASN A O    1 
ATOM   645  O O    B ASN A 1 37  ? 33.689 15.481 24.917 0.478 10.76  ? 37  ASN A O    1 
ATOM   646  C CB   A ASN A 1 37  ? 35.711 14.911 23.279 0.522 13.38  ? 37  ASN A CB   1 
ATOM   647  C CB   B ASN A 1 37  ? 35.686 14.462 23.406 0.478 13.97  ? 37  ASN A CB   1 
ATOM   648  C CG   A ASN A 1 37  ? 36.629 13.970 24.013 0.522 16.22  ? 37  ASN A CG   1 
ATOM   649  C CG   B ASN A 1 37  ? 36.063 13.732 24.692 0.478 14.96  ? 37  ASN A CG   1 
ATOM   650  O OD1  A ASN A 1 37  ? 36.273 12.859 24.416 0.522 20.01  ? 37  ASN A OD1  1 
ATOM   651  O OD1  B ASN A 1 37  ? 35.516 12.688 25.063 0.478 17.13  ? 37  ASN A OD1  1 
ATOM   652  N ND2  A ASN A 1 37  ? 37.874 14.404 24.178 0.522 19.39  ? 37  ASN A ND2  1 
ATOM   653  N ND2  B ASN A 1 37  ? 37.028 14.267 25.411 0.478 18.96  ? 37  ASN A ND2  1 
ATOM   654  H H    A ASN A 1 37  ? 33.751 13.681 21.220 0.522 11.32  ? 37  ASN A H    1 
ATOM   655  H H    B ASN A 1 37  ? 33.886 13.703 21.089 0.478 12.05  ? 37  ASN A H    1 
ATOM   656  H HA   A ASN A 1 37  ? 34.382 13.332 23.303 0.522 13.04  ? 37  ASN A HA   1 
ATOM   657  H HA   B ASN A 1 37  ? 34.081 13.170 23.208 0.478 12.18  ? 37  ASN A HA   1 
ATOM   658  H HB2  A ASN A 1 37  ? 36.088 15.116 22.409 0.522 16.05  ? 37  ASN A HB2  1 
ATOM   659  H HB2  B ASN A 1 37  ? 36.275 14.187 22.686 0.478 16.76  ? 37  ASN A HB2  1 
ATOM   660  H HB3  A ASN A 1 37  ? 35.636 15.740 23.776 0.522 16.05  ? 37  ASN A HB3  1 
ATOM   661  H HB3  B ASN A 1 37  ? 35.783 15.419 23.530 0.478 16.76  ? 37  ASN A HB3  1 
ATOM   662  H HD21 A ASN A 1 37  ? 38.454 13.907 24.573 0.522 23.27  ? 37  ASN A HD21 1 
ATOM   663  H HD21 B ASN A 1 37  ? 37.279 13.890 26.142 0.478 22.75  ? 37  ASN A HD21 1 
ATOM   664  H HD22 A ASN A 1 37  ? 38.100 15.181 23.889 0.522 23.27  ? 37  ASN A HD22 1 
ATOM   665  H HD22 B ASN A 1 37  ? 37.406 14.994 25.150 0.478 22.75  ? 37  ASN A HD22 1 
ATOM   666  N N    . PHE A 1 38  ? 31.976 14.799 23.604 1.000 9.08   ? 38  PHE A N    1 
ATOM   667  C CA   . PHE A 1 38  ? 30.857 15.260 24.384 1.000 9.04   ? 38  PHE A CA   1 
ATOM   668  C C    . PHE A 1 38  ? 30.794 16.785 24.535 1.000 8.96   ? 38  PHE A C    1 
ATOM   669  O O    . PHE A 1 38  ? 30.084 17.285 25.397 1.000 10.61  ? 38  PHE A O    1 
ATOM   670  C CB   . PHE A 1 38  ? 30.753 14.595 25.754 1.000 10.68  ? 38  PHE A CB   1 
ATOM   671  C CG   . PHE A 1 38  ? 30.626 13.114 25.790 1.000 9.48   ? 38  PHE A CG   1 
ATOM   672  C CD1  . PHE A 1 38  ? 29.921 12.382 24.849 1.000 10.32  ? 38  PHE A CD1  1 
ATOM   673  C CD2  . PHE A 1 38  ? 31.181 12.392 26.803 1.000 13.76  ? 38  PHE A CD2  1 
ATOM   674  C CE1  . PHE A 1 38  ? 29.757 11.030 24.970 1.000 10.98  ? 38  PHE A CE1  1 
ATOM   675  C CE2  . PHE A 1 38  ? 30.980 11.046 26.918 1.000 15.56  ? 38  PHE A CE2  1 
ATOM   676  C CZ   . PHE A 1 38  ? 30.262 10.343 26.029 1.000 12.50  ? 38  PHE A CZ   1 
ATOM   677  H H    A PHE A 1 38  ? 31.822 14.471 22.824 1.000 10.89  ? 38  PHE A H    1 
ATOM   678  H HA   . PHE A 1 38  ? 30.051 14.999 23.890 1.000 10.85  ? 38  PHE A HA   1 
ATOM   679  H HB2  . PHE A 1 38  ? 31.540 14.840 26.266 1.000 12.81  ? 38  PHE A HB2  1 
ATOM   680  H HB3  . PHE A 1 38  ? 29.985 14.972 26.212 1.000 12.81  ? 38  PHE A HB3  1 
ATOM   681  H HD1  . PHE A 1 38  ? 29.549 12.820 24.118 1.000 12.39  ? 38  PHE A HD1  1 
ATOM   682  H HD2  . PHE A 1 38  ? 31.711 12.826 27.432 1.000 16.51  ? 38  PHE A HD2  1 
ATOM   683  H HE1  . PHE A 1 38  ? 29.289 10.569 24.312 1.000 13.18  ? 38  PHE A HE1  1 
ATOM   684  H HE2  . PHE A 1 38  ? 31.355 10.599 27.642 1.000 18.67  ? 38  PHE A HE2  1 
ATOM   685  H HZ   . PHE A 1 38  ? 30.117 9.430  26.132 1.000 15.00  ? 38  PHE A HZ   1 
ATOM   686  N N    A ASN A 1 39  ? 31.505 17.515 23.692 0.471 10.48  ? 39  ASN A N    1 
ATOM   687  N N    B ASN A 1 39  ? 31.446 17.524 23.664 0.529 9.11   ? 39  ASN A N    1 
ATOM   688  C CA   A ASN A 1 39  ? 31.558 18.981 23.746 0.471 9.85   ? 39  ASN A CA   1 
ATOM   689  C CA   B ASN A 1 39  ? 31.576 18.983 23.770 0.529 9.17   ? 39  ASN A CA   1 
ATOM   690  C C    A ASN A 1 39  ? 30.502 19.558 22.795 0.471 8.66   ? 39  ASN A C    1 
ATOM   691  C C    B ASN A 1 39  ? 30.603 19.684 22.811 0.529 8.41   ? 39  ASN A C    1 
ATOM   692  O O    A ASN A 1 39  ? 30.520 19.325 21.585 0.471 8.98   ? 39  ASN A O    1 
ATOM   693  O O    B ASN A 1 39  ? 30.792 19.617 21.596 0.529 8.17   ? 39  ASN A O    1 
ATOM   694  C CB   A ASN A 1 39  ? 32.953 19.468 23.364 0.471 10.83  ? 39  ASN A CB   1 
ATOM   695  C CB   B ASN A 1 39  ? 33.028 19.312 23.431 0.529 11.36  ? 39  ASN A CB   1 
ATOM   696  C CG   A ASN A 1 39  ? 33.225 20.868 23.875 0.471 11.41  ? 39  ASN A CG   1 
ATOM   697  C CG   B ASN A 1 39  ? 33.235 20.811 23.332 0.529 10.98  ? 39  ASN A CG   1 
ATOM   698  O OD1  A ASN A 1 39  ? 32.328 21.693 24.007 0.471 13.57  ? 39  ASN A OD1  1 
ATOM   699  O OD1  B ASN A 1 39  ? 32.388 21.613 23.693 0.529 11.14  ? 39  ASN A OD1  1 
ATOM   700  N ND2  A ASN A 1 39  ? 34.464 21.200 24.243 0.471 17.08  ? 39  ASN A ND2  1 
ATOM   701  N ND2  B ASN A 1 39  ? 34.383 21.247 22.833 0.529 18.23  ? 39  ASN A ND2  1 
ATOM   702  H H    A ASN A 1 39  ? 31.959 17.112 23.083 0.471 12.58  ? 39  ASN A H    1 
ATOM   703  H H    B ASN A 1 39  ? 31.818 17.131 22.996 0.529 10.94  ? 39  ASN A H    1 
ATOM   704  H HA   A ASN A 1 39  ? 31.358 19.274 24.660 0.471 11.82  ? 39  ASN A HA   1 
ATOM   705  H HA   B ASN A 1 39  ? 31.384 19.262 24.690 0.529 11.01  ? 39  ASN A HA   1 
ATOM   706  H HB2  A ASN A 1 39  ? 33.614 18.860 23.729 0.471 12.99  ? 39  ASN A HB2  1 
ATOM   707  H HB2  B ASN A 1 39  ? 33.610 18.950 24.118 0.529 13.63  ? 39  ASN A HB2  1 
ATOM   708  H HB3  A ASN A 1 39  ? 33.040 19.458 22.398 0.471 12.99  ? 39  ASN A HB3  1 
ATOM   709  H HB3  B ASN A 1 39  ? 33.265 18.897 22.587 0.529 13.63  ? 39  ASN A HB3  1 
ATOM   710  H HD21 A ASN A 1 39  ? 34.621 21.981 24.567 0.471 20.50  ? 39  ASN A HD21 1 
ATOM   711  H HD21 B ASN A 1 39  ? 34.529 22.091 22.763 0.529 21.88  ? 39  ASN A HD21 1 
ATOM   712  H HD22 A ASN A 1 39  ? 35.105 20.633 24.157 0.471 20.50  ? 39  ASN A HD22 1 
ATOM   713  H HD22 B ASN A 1 39  ? 34.982 20.685 22.578 0.529 21.88  ? 39  ASN A HD22 1 
ATOM   714  N N    . THR A 1 40  ? 29.569 20.318 23.358 1.000 8.77   ? 40  THR A N    1 
ATOM   715  C CA   . THR A 1 40  ? 28.553 20.968 22.548 1.000 9.00   ? 40  THR A CA   1 
ATOM   716  C C    . THR A 1 40  ? 29.093 22.075 21.663 1.000 8.68   ? 40  THR A C    1 
ATOM   717  O O    . THR A 1 40  ? 28.399 22.437 20.703 1.000 10.58  ? 40  THR A O    1 
ATOM   718  C CB   . THR A 1 40  ? 27.396 21.502 23.414 1.000 10.72  ? 40  THR A CB   1 
ATOM   719  O OG1  . THR A 1 40  ? 27.902 22.517 24.309 1.000 11.98  ? 40  THR A OG1  1 
ATOM   720  C CG2  . THR A 1 40  ? 26.723 20.411 24.225 1.000 12.65  ? 40  THR A CG2  1 
ATOM   721  H H    A THR A 1 40  ? 29.567 20.427 24.211 1.000 10.52  ? 40  THR A H    1 
ATOM   722  H HA   . THR A 1 40  ? 28.177 20.284 21.955 1.000 10.79  ? 40  THR A HA   1 
ATOM   723  H HB   . THR A 1 40  ? 26.727 21.910 22.825 1.000 12.87  ? 40  THR A HB   1 
ATOM   724  H HG1  . THR A 1 40  ? 28.274 23.104 23.874 1.000 17.97  ? 40  THR A HG1  1 
ATOM   725  H HG21 . THR A 1 40  ? 26.385 19.735 23.633 1.000 18.97  ? 40  THR A HG21 1 
ATOM   726  H HG22 . THR A 1 40  ? 27.361 20.020 24.826 1.000 18.97  ? 40  THR A HG22 1 
ATOM   727  H HG23 . THR A 1 40  ? 25.997 20.788 24.728 1.000 18.97  ? 40  THR A HG23 1 
ATOM   728  N N    A GLN A 1 41  ? 30.260 22.588 21.968 0.621 9.06   ? 41  GLN A N    1 
ATOM   729  N N    B GLN A 1 41  ? 30.216 22.686 21.965 0.379 8.76   ? 41  GLN A N    1 
ATOM   730  C CA   A GLN A 1 41  ? 30.799 23.732 21.243 0.621 9.37   ? 41  GLN A CA   1 
ATOM   731  C CA   B GLN A 1 41  ? 30.855 23.770 21.251 0.379 11.44  ? 41  GLN A CA   1 
ATOM   732  C C    A GLN A 1 41  ? 31.758 23.312 20.150 0.621 9.62   ? 41  GLN A C    1 
ATOM   733  C C    B GLN A 1 41  ? 31.903 23.312 20.256 0.379 9.07   ? 41  GLN A C    1 
ATOM   734  O O    A GLN A 1 41  ? 32.275 24.176 19.437 0.621 10.64  ? 41  GLN A O    1 
ATOM   735  O O    B GLN A 1 41  ? 32.640 24.148 19.726 0.379 10.87  ? 41  GLN A O    1 
ATOM   736  C CB   A GLN A 1 41  ? 31.445 24.710 22.224 0.621 13.77  ? 41  GLN A CB   1 
ATOM   737  C CB   B GLN A 1 41  ? 31.529 24.716 22.263 0.379 13.94  ? 41  GLN A CB   1 
ATOM   738  C CG   A GLN A 1 41  ? 30.336 25.393 23.059 0.621 19.38  ? 41  GLN A CG   1 
ATOM   739  C CG   B GLN A 1 41  ? 30.467 25.490 23.050 0.379 18.33  ? 41  GLN A CG   1 
ATOM   740  C CD   A GLN A 1 41  ? 30.984 26.447 23.930 0.621 20.05  ? 41  GLN A CD   1 
ATOM   741  C CD   B GLN A 1 41  ? 29.820 26.532 22.148 0.379 27.10  ? 41  GLN A CD   1 
ATOM   742  O OE1  A GLN A 1 41  ? 30.672 27.629 23.913 0.621 34.88  ? 41  GLN A OE1  1 
ATOM   743  O OE1  B GLN A 1 41  ? 30.521 27.049 21.271 0.379 28.11  ? 41  GLN A OE1  1 
ATOM   744  N NE2  A GLN A 1 41  ? 31.941 26.052 24.773 0.621 25.24  ? 41  GLN A NE2  1 
ATOM   745  N NE2  B GLN A 1 41  ? 28.543 26.744 22.334 0.379 28.49  ? 41  GLN A NE2  1 
ATOM   746  H H    A GLN A 1 41  ? 30.717 22.243 22.610 0.621 10.87  ? 41  GLN A H    1 
ATOM   747  H H    B GLN A 1 41  ? 30.620 22.408 22.672 0.379 10.52  ? 41  GLN A H    1 
ATOM   748  H HA   A GLN A 1 41  ? 30.047 24.193 20.816 0.621 11.25  ? 41  GLN A HA   1 
ATOM   749  H HA   B GLN A 1 41  ? 30.166 24.272 20.767 0.379 13.73  ? 41  GLN A HA   1 
ATOM   750  H HB2  A GLN A 1 41  ? 32.055 24.235 22.810 0.621 16.53  ? 41  GLN A HB2  1 
ATOM   751  H HB2  B GLN A 1 41  ? 32.077 24.201 22.875 0.379 16.73  ? 41  GLN A HB2  1 
ATOM   752  H HB3  A GLN A 1 41  ? 31.950 25.380 21.737 0.621 16.53  ? 41  GLN A HB3  1 
ATOM   753  H HB3  B GLN A 1 41  ? 32.104 25.340 21.793 0.379 16.73  ? 41  GLN A HB3  1 
ATOM   754  H HG2  A GLN A 1 41  ? 29.681 25.803 22.473 0.621 23.26  ? 41  GLN A HG2  1 
ATOM   755  H HG2  B GLN A 1 41  ? 29.792 24.877 23.379 0.379 21.99  ? 41  GLN A HG2  1 
ATOM   756  H HG3  A GLN A 1 41  ? 29.884 24.737 23.612 0.621 23.26  ? 41  GLN A HG3  1 
ATOM   757  H HG3  B GLN A 1 41  ? 30.878 25.927 23.812 0.379 21.99  ? 41  GLN A HG3  1 
ATOM   758  H HE21 A GLN A 1 41  ? 32.323 26.624 25.289 0.621 30.29  ? 41  GLN A HE21 1 
ATOM   759  H HE21 B GLN A 1 41  ? 28.118 27.287 21.820 0.379 34.19  ? 41  GLN A HE21 1 
ATOM   760  H HE22 A GLN A 1 41  ? 32.175 25.225 24.800 0.621 30.29  ? 41  GLN A HE22 1 
ATOM   761  H HE22 B GLN A 1 41  ? 28.128 26.342 22.971 0.379 34.19  ? 41  GLN A HE22 1 
ATOM   762  N N    . ALA A 1 42  ? 32.029 22.019 19.997 1.000 9.43   ? 42  ALA A N    1 
ATOM   763  C CA   . ALA A 1 42  ? 33.037 21.557 19.061 1.000 9.51   ? 42  ALA A CA   1 
ATOM   764  C C    . ALA A 1 42  ? 32.761 22.038 17.657 1.000 8.65   ? 42  ALA A C    1 
ATOM   765  O O    . ALA A 1 42  ? 31.618 21.964 17.168 1.000 9.75   ? 42  ALA A O    1 
ATOM   766  C CB   . ALA A 1 42  ? 33.082 20.045 19.075 1.000 11.53  ? 42  ALA A CB   1 
ATOM   767  H H    A ALA A 1 42  ? 31.595 21.442 20.464 1.000 11.32  ? 42  ALA A H    1 
ATOM   768  H HA   . ALA A 1 42  ? 33.910 21.900 19.345 1.000 11.41  ? 42  ALA A HA   1 
ATOM   769  H HB1  . ALA A 1 42  ? 33.749 19.739 18.456 1.000 17.29  ? 42  ALA A HB1  1 
ATOM   770  H HB2  . ALA A 1 42  ? 33.301 19.739 19.958 1.000 17.29  ? 42  ALA A HB2  1 
ATOM   771  H HB3  . ALA A 1 42  ? 32.225 19.697 18.819 1.000 17.29  ? 42  ALA A HB3  1 
ATOM   772  N N    A THR A 1 43  ? 33.785 22.526 16.982 0.621 9.40   ? 43  THR A N    1 
ATOM   773  N N    B THR A 1 43  ? 33.805 22.460 16.953 0.379 9.77   ? 43  THR A N    1 
ATOM   774  C CA   A THR A 1 43  ? 33.700 22.819 15.558 0.621 9.66   ? 43  THR A CA   1 
ATOM   775  C CA   B THR A 1 43  ? 33.740 23.044 15.613 0.379 10.43  ? 43  THR A CA   1 
ATOM   776  C C    A THR A 1 43  ? 34.933 22.207 14.914 0.621 10.10  ? 43  THR A C    1 
ATOM   777  C C    B THR A 1 43  ? 34.945 22.609 14.778 0.379 10.93  ? 43  THR A C    1 
ATOM   778  O O    A THR A 1 43  ? 36.008 22.120 15.465 0.621 13.88  ? 43  THR A O    1 
ATOM   779  O O    B THR A 1 43  ? 36.053 23.004 15.190 0.379 15.48  ? 43  THR A O    1 
ATOM   780  C CB   A THR A 1 43  ? 33.664 24.308 15.218 0.621 11.46  ? 43  THR A CB   1 
ATOM   781  C CB   B THR A 1 43  ? 33.629 24.575 15.750 0.379 11.91  ? 43  THR A CB   1 
ATOM   782  O OG1  A THR A 1 43  ? 34.785 24.973 15.817 0.621 15.84  ? 43  THR A OG1  1 
ATOM   783  O OG1  B THR A 1 43  ? 32.488 24.943 16.539 0.379 14.47  ? 43  THR A OG1  1 
ATOM   784  C CG2  A THR A 1 43  ? 32.414 24.961 15.732 0.621 13.65  ? 43  THR A CG2  1 
ATOM   785  C CG2  B THR A 1 43  ? 33.395 25.187 14.390 0.379 17.80  ? 43  THR A CG2  1 
ATOM   786  H H    A THR A 1 43  ? 34.524 22.676 17.396 0.621 11.28  ? 43  THR A H    1 
ATOM   787  H H    B THR A 1 43  ? 34.581 22.385 17.314 0.379 11.73  ? 43  THR A H    1 
ATOM   788  H HA   A THR A 1 43  ? 32.900 22.388 15.190 0.621 11.59  ? 43  THR A HA   1 
ATOM   789  H HA   B THR A 1 43  ? 32.927 22.716 15.175 0.379 12.51  ? 43  THR A HA   1 
ATOM   790  H HB   A THR A 1 43  ? 33.708 24.417 14.245 0.621 13.75  ? 43  THR A HB   1 
ATOM   791  H HB   B THR A 1 43  ? 34.447 24.939 16.148 0.379 14.29  ? 43  THR A HB   1 
ATOM   792  H HG1  A THR A 1 43  ? 35.477 24.717 15.461 0.621 23.76  ? 43  THR A HG1  1 
ATOM   793  H HG1  B THR A 1 43  ? 32.587 24.671 17.306 0.379 17.36  ? 43  THR A HG1  1 
ATOM   794  H HG21 A THR A 1 43  ? 31.647 24.532 15.345 0.621 20.48  ? 43  THR A HG21 1 
ATOM   795  H HG21 B THR A 1 43  ? 34.132 24.974 13.812 0.379 26.70  ? 43  THR A HG21 1 
ATOM   796  H HG22 A THR A 1 43  ? 32.379 24.877 16.688 0.621 20.48  ? 43  THR A HG22 1 
ATOM   797  H HG22 B THR A 1 43  ? 32.583 24.836 14.016 0.379 26.70  ? 43  THR A HG22 1 
ATOM   798  H HG23 A THR A 1 43  ? 32.416 25.890 15.492 0.621 20.48  ? 43  THR A HG23 1 
ATOM   799  H HG23 B THR A 1 43  ? 33.322 26.140 14.476 0.379 26.70  ? 43  THR A HG23 1 
ATOM   800  N N    . ASN A 1 44  ? 34.764 21.866 13.660 1.000 9.88   ? 44  ASN A N    1 
ATOM   801  C CA   . ASN A 1 44  ? 35.885 21.427 12.826 1.000 10.36  ? 44  ASN A CA   1 
ATOM   802  C C    . ASN A 1 44  ? 35.718 22.110 11.474 1.000 8.84   ? 44  ASN A C    1 
ATOM   803  O O    . ASN A 1 44  ? 34.772 21.851 10.747 1.000 10.23  ? 44  ASN A O    1 
ATOM   804  C CB   . ASN A 1 44  ? 35.869 19.906 12.653 1.000 12.80  ? 44  ASN A CB   1 
ATOM   805  C CG   . ASN A 1 44  ? 37.020 19.405 11.797 1.000 16.23  ? 44  ASN A CG   1 
ATOM   806  O OD1  . ASN A 1 44  ? 38.124 19.718 12.039 1.000 28.73  ? 44  ASN A OD1  1 
ATOM   807  N ND2  . ASN A 1 44  ? 36.642 18.871 10.622 1.000 28.16  ? 44  ASN A ND2  1 
ATOM   808  H H    A ASN A 1 44  ? 33.976 21.901 13.318 1.000 11.86  ? 44  ASN A H    1 
ATOM   809  H HA   . ASN A 1 44  ? 36.730 21.705 13.236 1.000 12.43  ? 44  ASN A HA   1 
ATOM   810  H HB2  . ASN A 1 44  ? 35.918 19.487 13.526 1.000 15.36  ? 44  ASN A HB2  1 
ATOM   811  H HB3  . ASN A 1 44  ? 35.031 19.642 12.243 1.000 15.36  ? 44  ASN A HB3  1 
ATOM   812  H HD21 . ASN A 1 44  ? 37.222 18.744 10.000 1.000 33.80  ? 44  ASN A HD21 1 
ATOM   813  H HD22 . ASN A 1 44  ? 35.819 18.658 10.492 1.000 33.80  ? 44  ASN A HD22 1 
ATOM   814  N N    A ARG A 1 45  ? 36.648 22.981 11.146 0.561 10.80  ? 45  ARG A N    1 
ATOM   815  N N    B ARG A 1 45  ? 36.626 22.998 11.146 0.439 9.90   ? 45  ARG A N    1 
ATOM   816  C CA   A ARG A 1 45  ? 36.596 23.783 9.930  0.561 9.71   ? 45  ARG A CA   1 
ATOM   817  C CA   B ARG A 1 45  ? 36.590 23.787 9.908  0.439 11.46  ? 45  ARG A CA   1 
ATOM   818  C C    A ARG A 1 45  ? 37.365 23.087 8.810  0.561 11.19  ? 45  ARG A C    1 
ATOM   819  C C    B ARG A 1 45  ? 37.402 23.027 8.861  0.439 9.59   ? 45  ARG A C    1 
ATOM   820  O O    A ARG A 1 45  ? 38.577 22.993 8.913  0.561 13.29  ? 45  ARG A O    1 
ATOM   821  O O    B ARG A 1 45  ? 38.583 22.763 9.026  0.439 13.09  ? 45  ARG A O    1 
ATOM   822  C CB   A ARG A 1 45  ? 37.162 25.176 10.188 0.561 12.31  ? 45  ARG A CB   1 
ATOM   823  C CB   B ARG A 1 45  ? 37.043 25.204 10.268 0.439 15.58  ? 45  ARG A CB   1 
ATOM   824  C CG   A ARG A 1 45  ? 36.292 25.988 11.119 0.561 16.44  ? 45  ARG A CG   1 
ATOM   825  C CG   B ARG A 1 45  ? 36.301 25.768 11.477 0.439 17.14  ? 45  ARG A CG   1 
ATOM   826  C CD   A ARG A 1 45  ? 36.796 27.380 11.435 0.561 23.06  ? 45  ARG A CD   1 
ATOM   827  C CD   B ARG A 1 45  ? 35.859 27.198 11.362 0.439 28.29  ? 45  ARG A CD   1 
ATOM   828  N NE   A ARG A 1 45  ? 35.966 27.975 12.488 0.561 32.22  ? 45  ARG A NE   1 
ATOM   829  N NE   B ARG A 1 45  ? 35.065 27.731 12.473 0.439 30.10  ? 45  ARG A NE   1 
ATOM   830  C CZ   A ARG A 1 45  ? 36.214 28.000 13.777 0.561 33.15  ? 45  ARG A CZ   1 
ATOM   831  C CZ   B ARG A 1 45  ? 33.837 28.223 12.298 0.439 34.85  ? 45  ARG A CZ   1 
ATOM   832  N NH1  A ARG A 1 45  ? 37.314 27.447 14.300 0.561 42.75  ? 45  ARG A NH1  1 
ATOM   833  N NH1  B ARG A 1 45  ? 33.117 28.674 13.321 0.439 32.45  ? 45  ARG A NH1  1 
ATOM   834  N NH2  A ARG A 1 45  ? 35.314 28.555 14.579 0.561 35.29  ? 45  ARG A NH2  1 
ATOM   835  N NH2  B ARG A 1 45  ? 33.316 28.172 11.070 0.439 32.10  ? 45  ARG A NH2  1 
ATOM   836  H H    A ARG A 1 45  ? 37.319 23.082 11.675 0.561 12.96  ? 45  ARG A H    1 
ATOM   837  H H    B ARG A 1 45  ? 37.281 23.126 11.689 0.439 11.88  ? 45  ARG A H    1 
ATOM   838  H HA   A ARG A 1 45  ? 35.660 23.873 9.656  0.561 11.65  ? 45  ARG A HA   1 
ATOM   839  H HA   B ARG A 1 45  ? 35.661 23.832 9.601  0.439 13.76  ? 45  ARG A HA   1 
ATOM   840  H HB2  A ARG A 1 45  ? 38.048 25.092 10.573 0.561 14.78  ? 45  ARG A HB2  1 
ATOM   841  H HB2  B ARG A 1 45  ? 37.995 25.194 10.456 0.439 18.69  ? 45  ARG A HB2  1 
ATOM   842  H HB3  A ARG A 1 45  ? 37.248 25.645 9.343  0.561 14.78  ? 45  ARG A HB3  1 
ATOM   843  H HB3  B ARG A 1 45  ? 36.897 25.786 9.506  0.439 18.69  ? 45  ARG A HB3  1 
ATOM   844  H HG2  A ARG A 1 45  ? 35.409 26.064 10.724 0.561 19.72  ? 45  ARG A HG2  1 
ATOM   845  H HG2  B ARG A 1 45  ? 35.518 25.218 11.637 0.439 20.56  ? 45  ARG A HG2  1 
ATOM   846  H HG3  A ARG A 1 45  ? 36.197 25.500 11.952 0.561 19.72  ? 45  ARG A HG3  1 
ATOM   847  H HG3  B ARG A 1 45  ? 36.876 25.687 12.253 0.439 20.56  ? 45  ARG A HG3  1 
ATOM   848  H HD2  A ARG A 1 45  ? 37.718 27.336 11.730 0.561 27.67  ? 45  ARG A HD2  1 
ATOM   849  H HD2  B ARG A 1 45  ? 36.650 27.751 11.263 0.439 33.94  ? 45  ARG A HD2  1 
ATOM   850  H HD3  A ARG A 1 45  ? 36.759 27.931 10.637 0.561 27.67  ? 45  ARG A HD3  1 
ATOM   851  H HD3  B ARG A 1 45  ? 35.340 27.289 10.548 0.439 33.94  ? 45  ARG A HD3  1 
ATOM   852  H HE   A ARG A 1 45  ? 35.235 28.349 12.232 0.561 38.66  ? 45  ARG A HE   1 
ATOM   853  H HE   B ARG A 1 45  ? 35.401 27.726 13.264 0.439 36.13  ? 45  ARG A HE   1 
ATOM   854  H HH11 A ARG A 1 45  ? 37.886 27.060 13.788 0.561 51.30  ? 45  ARG A HH11 1 
ATOM   855  H HH11 B ARG A 1 45  ? 33.441 28.652 14.118 0.439 38.94  ? 45  ARG A HH11 1 
ATOM   856  H HH12 A ARG A 1 45  ? 37.449 27.480 15.149 0.561 51.30  ? 45  ARG A HH12 1 
ATOM   857  H HH12 B ARG A 1 45  ? 32.328 28.987 13.187 0.439 38.94  ? 45  ARG A HH12 1 
ATOM   858  H HH21 A ARG A 1 45  ? 34.591 28.886 14.251 0.561 42.34  ? 45  ARG A HH21 1 
ATOM   859  H HH21 B ARG A 1 45  ? 32.508 28.433 10.935 0.439 38.52  ? 45  ARG A HH21 1 
ATOM   860  H HH22 A ARG A 1 45  ? 35.453 28.584 15.428 0.561 42.34  ? 45  ARG A HH22 1 
ATOM   861  H HH22 B ARG A 1 45  ? 33.789 27.879 10.414 0.439 38.52  ? 45  ARG A HH22 1 
ATOM   862  N N    . ASN A 1 46  ? 36.724 22.622 7.802  1.000 10.53  ? 46  ASN A N    1 
ATOM   863  C CA   . ASN A 1 46  ? 37.321 21.808 6.768  1.000 11.26  ? 46  ASN A CA   1 
ATOM   864  C C    . ASN A 1 46  ? 37.878 22.651 5.630  1.000 10.83  ? 46  ASN A C    1 
ATOM   865  O O    . ASN A 1 46  ? 37.471 23.760 5.397  1.000 13.48  ? 46  ASN A O    1 
ATOM   866  C CB   . ASN A 1 46  ? 36.283 20.837 6.202  1.000 11.98  ? 46  ASN A CB   1 
ATOM   867  C CG   . ASN A 1 46  ? 35.749 19.931 7.247  1.000 13.11  ? 46  ASN A CG   1 
ATOM   868  O OD1  . ASN A 1 46  ? 36.539 19.251 7.911  1.000 21.16  ? 46  ASN A OD1  1 
ATOM   869  N ND2  . ASN A 1 46  ? 34.484 19.925 7.489  1.000 14.60  ? 46  ASN A ND2  1 
ATOM   870  H H    A ASN A 1 46  ? 35.886 22.807 7.736  1.000 12.64  ? 46  ASN A H    1 
ATOM   871  H HA   . ASN A 1 46  ? 38.054 21.289 7.162  1.000 13.51  ? 46  ASN A HA   1 
ATOM   872  H HB2  . ASN A 1 46  ? 35.552 21.342 5.813  1.000 14.38  ? 46  ASN A HB2  1 
ATOM   873  H HB3  . ASN A 1 46  ? 36.689 20.309 5.497  1.000 14.38  ? 46  ASN A HB3  1 
ATOM   874  H HD21 . ASN A 1 46  ? 34.170 19.439 8.126  1.000 17.52  ? 46  ASN A HD21 1 
ATOM   875  H HD22 . ASN A 1 46  ? 33.953 20.406 7.013  1.000 17.52  ? 46  ASN A HD22 1 
ATOM   876  N N    A THR A 1 47  ? 38.896 22.095 4.963  0.566 15.83  ? 47  THR A N    1 
ATOM   877  N N    B THR A 1 47  ? 38.731 22.071 4.778  0.434 9.64   ? 47  THR A N    1 
ATOM   878  C CA   A THR A 1 47  ? 39.389 22.834 3.795  0.566 12.77  ? 47  THR A CA   1 
ATOM   879  C CA   B THR A 1 47  ? 39.381 22.765 3.643  0.434 11.26  ? 47  THR A CA   1 
ATOM   880  C C    A THR A 1 47  ? 38.477 22.959 2.593  0.566 13.21  ? 47  THR A C    1 
ATOM   881  C C    B THR A 1 47  ? 38.487 22.822 2.424  0.434 10.45  ? 47  THR A C    1 
ATOM   882  O O    A THR A 1 47  ? 38.894 23.783 1.785  0.566 16.40  ? 47  THR A O    1 
ATOM   883  O O    B THR A 1 47  ? 38.699 23.522 1.459  0.434 13.10  ? 47  THR A O    1 
ATOM   884  C CB   A THR A 1 47  ? 40.693 22.209 3.327  0.566 14.52  ? 47  THR A CB   1 
ATOM   885  C CB   B THR A 1 47  ? 40.728 22.169 3.260  0.434 11.68  ? 47  THR A CB   1 
ATOM   886  O OG1  A THR A 1 47  ? 40.379 20.904 2.847  0.566 14.24  ? 47  THR A OG1  1 
ATOM   887  O OG1  B THR A 1 47  ? 40.625 20.797 2.874  0.434 12.49  ? 47  THR A OG1  1 
ATOM   888  C CG2  A THR A 1 47  ? 41.739 22.145 4.459  0.566 16.36  ? 47  THR A CG2  1 
ATOM   889  C CG2  B THR A 1 47  ? 41.728 22.268 4.442  0.434 16.48  ? 47  THR A CG2  1 
ATOM   890  H H    A THR A 1 47  ? 39.243 21.347 5.206  0.566 18.99  ? 47  THR A H    1 
ATOM   891  H H    B THR A 1 47  ? 38.914 21.240 4.897  0.434 11.57  ? 47  THR A H    1 
ATOM   892  H HA   A THR A 1 47  ? 39.597 23.743 4.096  0.566 15.32  ? 47  THR A HA   1 
ATOM   893  H HA   B THR A 1 47  ? 39.544 23.689 3.925  0.434 13.51  ? 47  THR A HA   1 
ATOM   894  H HB   A THR A 1 47  ? 41.054 22.742 2.589  0.566 17.42  ? 47  THR A HB   1 
ATOM   895  H HB   B THR A 1 47  ? 41.089 22.678 2.504  0.434 14.01  ? 47  THR A HB   1 
ATOM   896  H HG1  A THR A 1 47  ? 39.580 20.757 2.958  0.566 21.36  ? 47  THR A HG1  1 
ATOM   897  H HG1  B THR A 1 47  ? 39.858 20.535 2.997  0.434 14.99  ? 47  THR A HG1  1 
ATOM   898  H HG21 A THR A 1 47  ? 41.933 23.034 4.765  0.566 24.55  ? 47  THR A HG21 1 
ATOM   899  H HG21 B THR A 1 47  ? 41.810 23.185 4.715  0.434 24.72  ? 47  THR A HG21 1 
ATOM   900  H HG22 A THR A 1 47  ? 41.392 21.625 5.187  0.566 24.55  ? 47  THR A HG22 1 
ATOM   901  H HG22 B THR A 1 47  ? 41.407 21.742 5.178  0.434 24.72  ? 47  THR A HG22 1 
ATOM   902  H HG23 A THR A 1 47  ? 42.543 21.738 4.129  0.566 24.55  ? 47  THR A HG23 1 
ATOM   903  H HG23 B THR A 1 47  ? 42.586 21.939 4.164  0.434 24.72  ? 47  THR A HG23 1 
ATOM   904  N N    A ASP A 1 48  ? 37.337 22.316 2.429  0.566 11.94  ? 48  ASP A N    1 
ATOM   905  N N    B ASP A 1 48  ? 37.415 22.034 2.546  0.434 12.95  ? 48  ASP A N    1 
ATOM   906  C CA   A ASP A 1 48  ? 36.412 22.393 1.336  0.566 13.98  ? 48  ASP A CA   1 
ATOM   907  C CA   B ASP A 1 48  ? 36.405 22.100 1.496  0.434 13.98  ? 48  ASP A CA   1 
ATOM   908  C C    A ASP A 1 48  ? 35.366 23.475 1.492  0.566 13.88  ? 48  ASP A C    1 
ATOM   909  C C    B ASP A 1 48  ? 35.457 23.268 1.707  0.434 14.97  ? 48  ASP A C    1 
ATOM   910  O O    A ASP A 1 48  ? 34.408 23.555 0.745  0.566 19.88  ? 48  ASP A O    1 
ATOM   911  O O    B ASP A 1 48  ? 34.541 23.431 0.892  0.434 21.13  ? 48  ASP A O    1 
ATOM   912  C CB   A ASP A 1 48  ? 35.727 21.022 1.152  0.566 16.66  ? 48  ASP A CB   1 
ATOM   913  C CB   B ASP A 1 48  ? 35.701 20.761 1.317  0.434 15.33  ? 48  ASP A CB   1 
ATOM   914  C CG   A ASP A 1 48  ? 34.739 20.664 2.220  0.566 14.78  ? 48  ASP A CG   1 
ATOM   915  C CG   B ASP A 1 48  ? 34.931 20.337 2.546  0.434 14.62  ? 48  ASP A CG   1 
ATOM   916  O OD1  A ASP A 1 48  ? 34.564 21.327 3.235  0.566 17.62  ? 48  ASP A OD1  1 
ATOM   917  O OD1  B ASP A 1 48  ? 34.661 21.222 3.363  0.434 10.07  ? 48  ASP A OD1  1 
ATOM   918  O OD2  A ASP A 1 48  ? 34.021 19.642 2.048  0.566 23.65  ? 48  ASP A OD2  1 
ATOM   919  O OD2  B ASP A 1 48  ? 34.563 19.136 2.672  0.434 24.06  ? 48  ASP A OD2  1 
ATOM   920  H H    A ASP A 1 48  ? 37.120 21.778 3.063  0.566 14.33  ? 48  ASP A H    1 
ATOM   921  H H    B ASP A 1 48  ? 37.324 21.507 3.220  0.434 15.53  ? 48  ASP A H    1 
ATOM   922  H HA   A ASP A 1 48  ? 36.923 22.586 0.522  0.566 16.77  ? 48  ASP A HA   1 
ATOM   923  H HA   B ASP A 1 48  ? 36.884 22.277 0.660  0.434 16.78  ? 48  ASP A HA   1 
ATOM   924  H HB2  A ASP A 1 48  ? 35.271 21.016 0.295  0.566 19.99  ? 48  ASP A HB2  1 
ATOM   925  H HB2  B ASP A 1 48  ? 35.091 20.822 0.566  0.434 18.40  ? 48  ASP A HB2  1 
ATOM   926  H HB3  A ASP A 1 48  ? 36.412 20.336 1.122  0.566 19.99  ? 48  ASP A HB3  1 
ATOM   927  H HB3  B ASP A 1 48  ? 36.362 20.082 1.108  0.434 18.40  ? 48  ASP A HB3  1 
ATOM   928  N N    A GLY A 1 49  ? 35.517 24.279 2.547  0.566 12.38  ? 49  GLY A N    1 
ATOM   929  N N    B GLY A 1 49  ? 35.673 24.031 2.782  0.434 14.91  ? 49  GLY A N    1 
ATOM   930  C CA   A GLY A 1 49  ? 34.609 25.374 2.826  0.566 14.98  ? 49  GLY A CA   1 
ATOM   931  C CA   B GLY A 1 49  ? 34.886 25.243 3.028  0.434 16.42  ? 49  GLY A CA   1 
ATOM   932  C C    A GLY A 1 49  ? 33.484 25.010 3.757  0.566 11.24  ? 49  GLY A C    1 
ATOM   933  C C    B GLY A 1 49  ? 33.712 25.020 3.951  0.434 12.64  ? 49  GLY A C    1 
ATOM   934  O O    A GLY A 1 49  ? 32.704 25.898 4.058  0.566 13.12  ? 49  GLY A O    1 
ATOM   935  O O    B GLY A 1 49  ? 33.075 25.943 4.450  0.434 15.31  ? 49  GLY A O    1 
ATOM   936  H H    A GLY A 1 49  ? 36.177 24.142 3.081  0.566 14.85  ? 49  GLY A H    1 
ATOM   937  H H    B GLY A 1 49  ? 36.287 23.807 3.341  0.434 17.89  ? 49  GLY A H    1 
ATOM   938  H HA2  A GLY A 1 49  ? 35.113 26.106 3.215  0.566 17.98  ? 49  GLY A HA2  1 
ATOM   939  H HA2  B GLY A 1 49  ? 35.464 25.920 3.414  0.434 19.70  ? 49  GLY A HA2  1 
ATOM   940  H HA3  A GLY A 1 49  ? 34.232 25.688 1.989  0.566 17.98  ? 49  GLY A HA3  1 
ATOM   941  H HA3  B GLY A 1 49  ? 34.559 25.583 2.180  0.434 19.70  ? 49  GLY A HA3  1 
ATOM   942  N N    . SER A 1 50  ? 33.382 23.757 4.182  1.000 10.32  ? 50  SER A N    1 
ATOM   943  C CA   . SER A 1 50  ? 32.335 23.358 5.108  1.000 9.47   ? 50  SER A CA   1 
ATOM   944  C C    . SER A 1 50  ? 32.904 23.280 6.529  1.000 8.68   ? 50  SER A C    1 
ATOM   945  O O    . SER A 1 50  ? 34.126 23.239 6.729  1.000 11.01  ? 50  SER A O    1 
ATOM   946  C CB   . SER A 1 50  ? 31.745 22.005 4.743  1.000 10.16  ? 50  SER A CB   1 
ATOM   947  O OG   . SER A 1 50  ? 32.607 20.925 5.036  1.000 10.79  ? 50  SER A OG   1 
ATOM   948  H H    A SER A 1 50  ? 33.946 23.170 3.904  1.000 12.38  ? 50  SER A H    1 
ATOM   949  H HA   . SER A 1 50  ? 31.622 24.030 5.088  1.000 11.36  ? 50  SER A HA   1 
ATOM   950  H HB2  . SER A 1 50  ? 30.913 21.884 5.227  1.000 12.19  ? 50  SER A HB2  1 
ATOM   951  H HB3  . SER A 1 50  ? 31.540 21.996 3.795  1.000 12.19  ? 50  SER A HB3  1 
ATOM   952  H HG   . SER A 1 50  ? 33.300 21.004 4.604  1.000 16.18  ? 50  SER A HG   1 
ATOM   953  N N    . THR A 1 51  ? 32.018 23.223 7.498  1.000 7.97   ? 51  THR A N    1 
ATOM   954  C CA   . THR A 1 51  ? 32.340 23.115 8.889  1.000 7.61   ? 51  THR A CA   1 
ATOM   955  C C    . THR A 1 51  ? 31.413 22.069 9.513  1.000 7.11   ? 51  THR A C    1 
ATOM   956  O O    . THR A 1 51  ? 30.256 21.985 9.162  1.000 8.04   ? 51  THR A O    1 
ATOM   957  C CB   . THR A 1 51  ? 32.190 24.483 9.568  1.000 8.61   ? 51  THR A CB   1 
ATOM   958  O OG1  . THR A 1 51  ? 33.094 25.404 8.968  1.000 10.66  ? 51  THR A OG1  1 
ATOM   959  C CG2  . THR A 1 51  ? 32.480 24.495 11.048 1.000 9.97   ? 51  THR A CG2  1 
ATOM   960  H H    . THR A 1 51  ? 31.186 23.253 7.281  1.000 9.56   ? 51  THR A H    1 
ATOM   961  H HA   . THR A 1 51  ? 33.268 22.814 8.979  1.000 9.13   ? 51  THR A HA   1 
ATOM   962  H HB   . THR A 1 51  ? 31.275 24.804 9.425  1.000 10.33  ? 51  THR A HB   1 
ATOM   963  H HG1  . THR A 1 51  ? 32.947 25.446 8.162  1.000 15.98  ? 51  THR A HG1  1 
ATOM   964  H HG21 . THR A 1 51  ? 31.889 23.884 11.494 1.000 14.95  ? 51  THR A HG21 1 
ATOM   965  H HG22 . THR A 1 51  ? 33.389 24.228 11.198 1.000 14.95  ? 51  THR A HG22 1 
ATOM   966  H HG23 . THR A 1 51  ? 32.345 25.380 11.393 1.000 14.95  ? 51  THR A HG23 1 
ATOM   967  N N    A ASP A 1 52  ? 31.951 21.320 10.468 0.740 7.27   ? 52  ASP A N    1 
ATOM   968  N N    B ASP A 1 52  ? 31.994 21.351 10.470 0.260 8.07   ? 52  ASP A N    1 
ATOM   969  C CA   A ASP A 1 52  ? 31.175 20.350 11.256 0.740 7.78   ? 52  ASP A CA   1 
ATOM   970  C CA   B ASP A 1 52  ? 31.285 20.394 11.306 0.260 6.86   ? 52  ASP A CA   1 
ATOM   971  C C    A ASP A 1 52  ? 30.924 20.986 12.610 0.740 7.16   ? 52  ASP A C    1 
ATOM   972  C C    B ASP A 1 52  ? 30.942 20.998 12.662 0.260 7.23   ? 52  ASP A C    1 
ATOM   973  O O    A ASP A 1 52  ? 31.815 21.502 13.261 0.740 9.33   ? 52  ASP A O    1 
ATOM   974  O O    B ASP A 1 52  ? 31.854 21.490 13.322 0.260 8.43   ? 52  ASP A O    1 
ATOM   975  C CB   A ASP A 1 52  ? 31.954 19.063 11.420 0.740 8.61   ? 52  ASP A CB   1 
ATOM   976  C CB   B ASP A 1 52  ? 32.127 19.149 11.560 0.260 7.74   ? 52  ASP A CB   1 
ATOM   977  C CG   A ASP A 1 52  ? 32.470 18.502 10.106 0.740 10.66  ? 52  ASP A CG   1 
ATOM   978  C CG   B ASP A 1 52  ? 32.434 18.368 10.301 0.260 10.03  ? 52  ASP A CG   1 
ATOM   979  O OD1  A ASP A 1 52  ? 31.656 18.308 9.214  0.740 14.28  ? 52  ASP A OD1  1 
ATOM   980  O OD1  B ASP A 1 52  ? 31.790 18.623 9.279  0.260 15.35  ? 52  ASP A OD1  1 
ATOM   981  O OD2  A ASP A 1 52  ? 33.688 18.210 10.055 0.740 14.68  ? 52  ASP A OD2  1 
ATOM   982  O OD2  B ASP A 1 52  ? 33.337 17.503 10.393 0.260 15.28  ? 52  ASP A OD2  1 
ATOM   983  H H    A ASP A 1 52  ? 32.791 21.405 10.634 0.740 8.72   ? 52  ASP A H    1 
ATOM   984  H H    B ASP A 1 52  ? 32.838 21.458 10.601 0.260 9.68   ? 52  ASP A H    1 
ATOM   985  H HA   A ASP A 1 52  ? 30.321 20.168 10.811 0.740 9.33   ? 52  ASP A HA   1 
ATOM   986  H HA   B ASP A 1 52  ? 30.455 20.131 10.856 0.260 8.23   ? 52  ASP A HA   1 
ATOM   987  H HB2  A ASP A 1 52  ? 32.707 19.224 12.010 0.740 10.34  ? 52  ASP A HB2  1 
ATOM   988  H HB2  B ASP A 1 52  ? 32.961 19.414 11.978 0.260 9.29   ? 52  ASP A HB2  1 
ATOM   989  H HB3  A ASP A 1 52  ? 31.383 18.402 11.842 0.740 10.34  ? 52  ASP A HB3  1 
ATOM   990  H HB3  B ASP A 1 52  ? 31.655 18.572 12.181 0.260 9.29   ? 52  ASP A HB3  1 
ATOM   991  N N    . TYR A 1 53  ? 29.670 20.939 13.054 1.000 7.15   ? 53  TYR A N    1 
ATOM   992  C CA   . TYR A 1 53  ? 29.209 21.679 14.212 1.000 7.20   ? 53  TYR A CA   1 
ATOM   993  C C    . TYR A 1 53  ? 28.615 20.781 15.298 1.000 7.15   ? 53  TYR A C    1 
ATOM   994  O O    . TYR A 1 53  ? 27.712 19.976 15.055 1.000 7.90   ? 53  TYR A O    1 
ATOM   995  C CB   . TYR A 1 53  ? 28.105 22.659 13.795 1.000 8.39   ? 53  TYR A CB   1 
ATOM   996  C CG   . TYR A 1 53  ? 28.566 23.797 12.943 1.000 8.04   ? 53  TYR A CG   1 
ATOM   997  C CD1  . TYR A 1 53  ? 29.006 24.978 13.504 1.000 10.30  ? 53  TYR A CD1  1 
ATOM   998  C CD2  . TYR A 1 53  ? 28.548 23.749 11.566 1.000 7.75   ? 53  TYR A CD2  1 
ATOM   999  C CE1  . TYR A 1 53  ? 29.426 26.053 12.750 1.000 10.16  ? 53  TYR A CE1  1 
ATOM   1000 C CE2  . TYR A 1 53  ? 28.952 24.822 10.801 1.000 8.07   ? 53  TYR A CE2  1 
ATOM   1001 C CZ   . TYR A 1 53  ? 29.395 25.982 11.398 1.000 8.77   ? 53  TYR A CZ   1 
ATOM   1002 O OH   . TYR A 1 53  ? 29.829 27.062 10.661 1.000 10.57  ? 53  TYR A OH   1 
ATOM   1003 H H    A TYR A 1 53  ? 29.105 20.445 12.633 1.000 8.57   ? 53  TYR A H    1 
ATOM   1004 H HA   . TYR A 1 53  ? 29.959 22.184 14.589 1.000 8.64   ? 53  TYR A HA   1 
ATOM   1005 H HB2  . TYR A 1 53  ? 27.423 22.167 13.312 1.000 10.06  ? 53  TYR A HB2  1 
ATOM   1006 H HB3  . TYR A 1 53  ? 27.694 23.019 14.596 1.000 10.06  ? 53  TYR A HB3  1 
ATOM   1007 H HD1  . TYR A 1 53  ? 29.021 25.051 14.431 1.000 12.36  ? 53  TYR A HD1  1 
ATOM   1008 H HD2  . TYR A 1 53  ? 28.257 22.973 11.143 1.000 9.30   ? 53  TYR A HD2  1 
ATOM   1009 H HE1  . TYR A 1 53  ? 29.729 26.826 13.169 1.000 12.19  ? 53  TYR A HE1  1 
ATOM   1010 H HE2  . TYR A 1 53  ? 28.925 24.762 9.873  1.000 9.69   ? 53  TYR A HE2  1 
ATOM   1011 H HH   . TYR A 1 53  ? 29.775 26.887 9.862  1.000 15.86  ? 53  TYR A HH   1 
ATOM   1012 N N    . GLY A 1 54  ? 29.058 21.025 16.525 1.000 7.67   ? 54  GLY A N    1 
ATOM   1013 C CA   . GLY A 1 54  ? 28.400 20.565 17.721 1.000 8.04   ? 54  GLY A CA   1 
ATOM   1014 C C    . GLY A 1 54  ? 28.712 19.157 18.114 1.000 7.44   ? 54  GLY A C    1 
ATOM   1015 O O    . GLY A 1 54  ? 29.641 18.503 17.637 1.000 8.03   ? 54  GLY A O    1 
ATOM   1016 H H    . GLY A 1 54  ? 29.780 21.484 16.611 1.000 9.20   ? 54  GLY A H    1 
ATOM   1017 H HA2  . GLY A 1 54  ? 28.647 21.151 18.453 1.000 9.65   ? 54  GLY A HA2  1 
ATOM   1018 H HA3  . GLY A 1 54  ? 27.441 20.644 17.595 1.000 9.65   ? 54  GLY A HA3  1 
ATOM   1019 N N    . ILE A 1 55  ? 27.904 18.664 19.058 1.000 7.64   ? 55  ILE A N    1 
ATOM   1020 C CA   . ILE A 1 55  ? 28.156 17.402 19.724 1.000 8.16   ? 55  ILE A CA   1 
ATOM   1021 C C    . ILE A 1 55  ? 28.158 16.215 18.785 1.000 7.87   ? 55  ILE A C    1 
ATOM   1022 O O    . ILE A 1 55  ? 28.823 15.225 19.059 1.000 9.46   ? 55  ILE A O    1 
ATOM   1023 C CB   . ILE A 1 55  ? 27.155 17.246 20.883 1.000 10.18  ? 55  ILE A CB   1 
ATOM   1024 C CG1  . ILE A 1 55  ? 27.690 16.238 21.937 1.000 14.08  ? 55  ILE A CG1  1 
ATOM   1025 C CG2  . ILE A 1 55  ? 25.759 17.033 20.426 1.000 13.20  ? 55  ILE A CG2  1 
ATOM   1026 C CD1  . ILE A 1 55  ? 27.080 16.346 23.273 1.000 17.43  ? 55  ILE A CD1  1 
ATOM   1027 H H    . ILE A 1 55  ? 27.206 19.115 19.280 1.000 9.17   ? 55  ILE A H    1 
ATOM   1028 H HA   . ILE A 1 55  ? 29.050 17.458 20.121 1.000 9.80   ? 55  ILE A HA   1 
ATOM   1029 H HB   . ILE A 1 55  ? 27.149 18.115 21.337 1.000 12.22  ? 55  ILE A HB   1 
ATOM   1030 H HG12 . ILE A 1 55  ? 27.544 15.339 21.604 1.000 16.90  ? 55  ILE A HG12 1 
ATOM   1031 H HG13 . ILE A 1 55  ? 28.648 16.365 22.025 1.000 16.90  ? 55  ILE A HG13 1 
ATOM   1032 H HG21 . ILE A 1 55  ? 25.183 16.943 21.188 1.000 19.80  ? 55  ILE A HG21 1 
ATOM   1033 H HG22 . ILE A 1 55  ? 25.477 17.784 19.899 1.000 19.80  ? 55  ILE A HG22 1 
ATOM   1034 H HG23 . ILE A 1 55  ? 25.714 16.235 19.895 1.000 19.80  ? 55  ILE A HG23 1 
ATOM   1035 H HD11 . ILE A 1 55  ? 27.468 15.689 23.856 1.000 26.15  ? 55  ILE A HD11 1 
ATOM   1036 H HD12 . ILE A 1 55  ? 27.240 17.223 23.628 1.000 26.15  ? 55  ILE A HD12 1 
ATOM   1037 H HD13 . ILE A 1 55  ? 26.134 16.195 23.206 1.000 26.15  ? 55  ILE A HD13 1 
ATOM   1038 N N    A LEU A 1 56  ? 27.421 16.318 17.677 0.785 7.64   ? 56  LEU A N    1 
ATOM   1039 N N    B LEU A 1 56  ? 27.455 16.320 17.660 0.215 7.32   ? 56  LEU A N    1 
ATOM   1040 C CA   A LEU A 1 56  ? 27.352 15.269 16.658 0.785 7.90   ? 56  LEU A CA   1 
ATOM   1041 C CA   B LEU A 1 56  ? 27.492 15.210 16.702 0.215 8.24   ? 56  LEU A CA   1 
ATOM   1042 C C    A LEU A 1 56  ? 28.006 15.689 15.335 0.785 8.08   ? 56  LEU A C    1 
ATOM   1043 C C    B LEU A 1 56  ? 28.196 15.597 15.411 0.215 6.88   ? 56  LEU A C    1 
ATOM   1044 O O    A LEU A 1 56  ? 27.875 14.997 14.346 0.785 9.39   ? 56  LEU A O    1 
ATOM   1045 O O    B LEU A 1 56  ? 28.275 14.840 14.454 0.215 8.06   ? 56  LEU A O    1 
ATOM   1046 C CB   A LEU A 1 56  ? 25.921 14.786 16.411 0.785 9.98   ? 56  LEU A CB   1 
ATOM   1047 C CB   B LEU A 1 56  ? 26.059 14.718 16.461 0.215 7.43   ? 56  LEU A CB   1 
ATOM   1048 C CG   A LEU A 1 56  ? 25.364 13.951 17.571 0.785 12.41  ? 56  LEU A CG   1 
ATOM   1049 C CG   B LEU A 1 56  ? 25.626 13.652 17.483 0.215 9.58   ? 56  LEU A CG   1 
ATOM   1050 C CD1  A LEU A 1 56  ? 23.870 13.818 17.341 0.785 17.02  ? 56  LEU A CD1  1 
ATOM   1051 C CD1  B LEU A 1 56  ? 24.144 13.366 17.429 0.215 12.46  ? 56  LEU A CD1  1 
ATOM   1052 C CD2  A LEU A 1 56  ? 26.043 12.619 17.748 0.785 15.92  ? 56  LEU A CD2  1 
ATOM   1053 C CD2  B LEU A 1 56  ? 26.417 12.376 17.243 0.215 10.19  ? 56  LEU A CD2  1 
ATOM   1054 H H    A LEU A 1 56  ? 26.964 17.036 17.556 0.785 9.17   ? 56  LEU A H    1 
ATOM   1055 H H    B LEU A 1 56  ? 26.989 17.024 17.498 0.215 8.78   ? 56  LEU A H    1 
ATOM   1056 H HA   A LEU A 1 56  ? 27.860 14.503 16.999 0.785 9.48   ? 56  LEU A HA   1 
ATOM   1057 H HA   B LEU A 1 56  ? 27.996 14.476 17.111 0.215 9.89   ? 56  LEU A HA   1 
ATOM   1058 H HB2  A LEU A 1 56  ? 25.347 15.555 16.272 0.785 11.98  ? 56  LEU A HB2  1 
ATOM   1059 H HB2  B LEU A 1 56  ? 25.451 15.472 16.512 0.215 8.92   ? 56  LEU A HB2  1 
ATOM   1060 H HB3  A LEU A 1 56  ? 25.903 14.252 15.602 0.785 11.98  ? 56  LEU A HB3  1 
ATOM   1061 H HB3  B LEU A 1 56  ? 25.997 14.346 15.567 0.215 8.92   ? 56  LEU A HB3  1 
ATOM   1062 H HG   A LEU A 1 56  ? 25.494 14.464 18.397 0.785 14.89  ? 56  LEU A HG   1 
ATOM   1063 H HG   B LEU A 1 56  ? 25.842 13.982 18.380 0.215 11.50  ? 56  LEU A HG   1 
ATOM   1064 H HD11 A LEU A 1 56  ? 23.483 14.690 17.234 0.785 25.53  ? 56  LEU A HD11 1 
ATOM   1065 H HD11 B LEU A 1 56  ? 23.656 14.179 17.581 0.215 18.69  ? 56  LEU A HD11 1 
ATOM   1066 H HD12 A LEU A 1 56  ? 23.714 13.300 16.548 0.785 25.53  ? 56  LEU A HD12 1 
ATOM   1067 H HD12 B LEU A 1 56  ? 23.917 13.015 16.565 0.215 18.69  ? 56  LEU A HD12 1 
ATOM   1068 H HD13 A LEU A 1 56  ? 23.468 13.380 18.094 0.785 25.53  ? 56  LEU A HD13 1 
ATOM   1069 H HD13 B LEU A 1 56  ? 23.916 12.725 18.105 0.215 18.69  ? 56  LEU A HD13 1 
ATOM   1070 H HD21 A LEU A 1 56  ? 26.982 12.755 17.891 0.785 23.88  ? 56  LEU A HD21 1 
ATOM   1071 H HD21 B LEU A 1 56  ? 27.356 12.570 17.280 0.215 15.28  ? 56  LEU A HD21 1 
ATOM   1072 H HD22 A LEU A 1 56  ? 25.666 12.166 18.507 0.785 23.88  ? 56  LEU A HD22 1 
ATOM   1073 H HD22 B LEU A 1 56  ? 26.197 11.731 17.919 0.215 15.28  ? 56  LEU A HD22 1 
ATOM   1074 H HD23 A LEU A 1 56  ? 25.912 12.086 16.960 0.785 23.88  ? 56  LEU A HD23 1 
ATOM   1075 H HD23 B LEU A 1 56  ? 26.197 12.021 16.378 0.215 15.28  ? 56  LEU A HD23 1 
ATOM   1076 N N    . GLN A 1 57  ? 28.772 16.796 15.359 1.000 7.34   ? 57  GLN A N    1 
ATOM   1077 C CA   . GLN A 1 57  ? 29.635 17.189 14.242 1.000 7.31   ? 57  GLN A CA   1 
ATOM   1078 C C    . GLN A 1 57  ? 28.875 17.126 12.903 1.000 7.76   ? 57  GLN A C    1 
ATOM   1079 O O    . GLN A 1 57  ? 29.312 16.527 11.940 1.000 10.47  ? 57  GLN A O    1 
ATOM   1080 C CB   . GLN A 1 57  ? 30.927 16.391 14.223 1.000 8.03   ? 57  GLN A CB   1 
ATOM   1081 C CG   . GLN A 1 57  ? 31.852 16.756 15.390 1.000 8.77   ? 57  GLN A CG   1 
ATOM   1082 C CD   . GLN A 1 57  ? 32.470 18.092 15.200 1.000 8.84   ? 57  GLN A CD   1 
ATOM   1083 O OE1  . GLN A 1 57  ? 33.457 18.263 14.479 1.000 11.31  ? 57  GLN A OE1  1 
ATOM   1084 N NE2  . GLN A 1 57  ? 31.870 19.105 15.802 1.000 9.83   ? 57  GLN A NE2  1 
ATOM   1085 H H    A GLN A 1 57  ? 28.755 17.293 16.060 1.000 8.81   ? 57  GLN A H    1 
ATOM   1086 H HA   . GLN A 1 57  ? 29.880 18.126 14.387 1.000 8.77   ? 57  GLN A HA   1 
ATOM   1087 H HB2  . GLN A 1 57  ? 30.718 15.445 14.268 1.000 9.63   ? 57  GLN A HB2  1 
ATOM   1088 H HB3  . GLN A 1 57  ? 31.390 16.554 13.387 1.000 9.63   ? 57  GLN A HB3  1 
ATOM   1089 H HG2  . GLN A 1 57  ? 31.343 16.753 16.216 1.000 10.52  ? 57  GLN A HG2  1 
ATOM   1090 H HG3  . GLN A 1 57  ? 32.551 16.088 15.467 1.000 10.52  ? 57  GLN A HG3  1 
ATOM   1091 H HE21 . GLN A 1 57  ? 32.166 19.905 15.694 1.000 11.79  ? 57  GLN A HE21 1 
ATOM   1092 H HE22 . GLN A 1 57  ? 31.184 18.964 16.300 1.000 11.79  ? 57  GLN A HE22 1 
ATOM   1093 N N    . ILE A 1 58  ? 27.768 17.818 12.876 1.000 7.54   ? 58  ILE A N    1 
ATOM   1094 C CA   . ILE A 1 58  ? 26.891 17.866 11.696 1.000 7.69   ? 58  ILE A CA   1 
ATOM   1095 C C    . ILE A 1 58  ? 27.449 18.888 10.696 1.000 7.41   ? 58  ILE A C    1 
ATOM   1096 O O    . ILE A 1 58  ? 27.797 20.010 11.049 1.000 8.49   ? 58  ILE A O    1 
ATOM   1097 C CB   . ILE A 1 58  ? 25.469 18.166 12.165 1.000 8.42   ? 58  ILE A CB   1 
ATOM   1098 C CG1  . ILE A 1 58  ? 24.918 16.978 12.923 1.000 10.53  ? 58  ILE A CG1  1 
ATOM   1099 C CG2  . ILE A 1 58  ? 24.580 18.566 10.986 1.000 10.01  ? 58  ILE A CG2  1 
ATOM   1100 C CD1  . ILE A 1 58  ? 23.610 17.182 13.646 1.000 13.64  ? 58  ILE A CD1  1 
ATOM   1101 H H    . ILE A 1 58  ? 27.543 18.263 13.576 1.000 9.04   ? 58  ILE A H    1 
ATOM   1102 H HA   . ILE A 1 58  ? 26.896 16.983 11.270 1.000 9.22   ? 58  ILE A HA   1 
ATOM   1103 H HB   . ILE A 1 58  ? 25.510 18.925 12.783 1.000 10.10  ? 58  ILE A HB   1 
ATOM   1104 H HG12 . ILE A 1 58  ? 24.805 16.246 12.297 1.000 12.64  ? 58  ILE A HG12 1 
ATOM   1105 H HG13 . ILE A 1 58  ? 25.582 16.701 13.574 1.000 12.64  ? 58  ILE A HG13 1 
ATOM   1106 H HG21 . ILE A 1 58  ? 24.967 19.321 10.535 1.000 15.01  ? 58  ILE A HG21 1 
ATOM   1107 H HG22 . ILE A 1 58  ? 24.509 17.830 10.374 1.000 15.01  ? 58  ILE A HG22 1 
ATOM   1108 H HG23 . ILE A 1 58  ? 23.707 18.799 11.309 1.000 15.01  ? 58  ILE A HG23 1 
ATOM   1109 H HD11 . ILE A 1 58  ? 23.359 16.368 14.089 1.000 20.47  ? 58  ILE A HD11 1 
ATOM   1110 H HD12 . ILE A 1 58  ? 23.709 17.882 14.295 1.000 20.47  ? 58  ILE A HD12 1 
ATOM   1111 H HD13 . ILE A 1 58  ? 22.930 17.426 13.014 1.000 20.47  ? 58  ILE A HD13 1 
ATOM   1112 N N    . ASN A 1 59  ? 27.539 18.473 9.438  1.000 8.52   ? 59  ASN A N    1 
ATOM   1113 C CA   . ASN A 1 59  ? 28.222 19.252 8.417  1.000 8.30   ? 59  ASN A CA   1 
ATOM   1114 C C    . ASN A 1 59  ? 27.330 20.261 7.715  1.000 7.88   ? 59  ASN A C    1 
ATOM   1115 O O    . ASN A 1 59  ? 26.166 20.024 7.395  1.000 9.99   ? 59  ASN A O    1 
ATOM   1116 C CB   . ASN A 1 59  ? 28.826 18.257 7.406  1.000 9.51   ? 59  ASN A CB   1 
ATOM   1117 C CG   . ASN A 1 59  ? 29.681 18.913 6.362  1.000 9.32   ? 59  ASN A CG   1 
ATOM   1118 O OD1  . ASN A 1 59  ? 29.236 19.213 5.247  1.000 11.13  ? 59  ASN A OD1  1 
ATOM   1119 N ND2  . ASN A 1 59  ? 30.919 19.178 6.697  1.000 11.56  ? 59  ASN A ND2  1 
ATOM   1120 H H    . ASN A 1 59  ? 27.183 17.721 9.220  1.000 10.23  ? 59  ASN A H    1 
ATOM   1121 H HA   . ASN A 1 59  ? 28.958 19.739 8.844  1.000 9.96   ? 59  ASN A HA   1 
ATOM   1122 H HB2  . ASN A 1 59  ? 29.362 17.607 7.887  1.000 11.41  ? 59  ASN A HB2  1 
ATOM   1123 H HB3  . ASN A 1 59  ? 28.106 17.779 6.967  1.000 11.41  ? 59  ASN A HB3  1 
ATOM   1124 H HD21 . ASN A 1 59  ? 31.442 19.569 6.136  1.000 13.87  ? 59  ASN A HD21 1 
ATOM   1125 H HD22 . ASN A 1 59  ? 31.210 18.962 7.477  1.000 13.87  ? 59  ASN A HD22 1 
ATOM   1126 N N    . SER A 1 60  ? 27.924 21.410 7.414  1.000 7.82   ? 60  SER A N    1 
ATOM   1127 C CA   . SER A 1 60  ? 27.253 22.562 6.837  1.000 8.00   ? 60  SER A CA   1 
ATOM   1128 C C    . SER A 1 60  ? 26.993 22.501 5.339  1.000 8.36   ? 60  SER A C    1 
ATOM   1129 O O    . SER A 1 60  ? 26.312 23.394 4.816  1.000 11.03  ? 60  SER A O    1 
ATOM   1130 C CB   . SER A 1 60  ? 28.007 23.818 7.150  1.000 8.48   ? 60  SER A CB   1 
ATOM   1131 O OG   . SER A 1 60  ? 29.275 23.785 6.519  1.000 8.74   ? 60  SER A OG   1 
ATOM   1132 H H    . SER A 1 60  ? 28.766 21.477 7.573  1.000 9.39   ? 60  SER A H    1 
ATOM   1133 H HA   . SER A 1 60  ? 26.380 22.635 7.276  1.000 9.60   ? 60  SER A HA   1 
ATOM   1134 H HB2  . SER A 1 60  ? 27.506 24.587 6.837  1.000 10.17  ? 60  SER A HB2  1 
ATOM   1135 H HB3  . SER A 1 60  ? 28.121 23.901 8.110  1.000 10.17  ? 60  SER A HB3  1 
ATOM   1136 H HG   . SER A 1 60  ? 29.681 24.477 6.686  1.000 13.12  ? 60  SER A HG   1 
ATOM   1137 N N    . ARG A 1 61  ? 27.491 21.519 4.624  1.000 8.29   ? 61  ARG A N    1 
ATOM   1138 C CA   . ARG A 1 61  ? 27.147 21.443 3.202  1.000 8.51   ? 61  ARG A CA   1 
ATOM   1139 C C    . ARG A 1 61  ? 25.723 20.933 3.025  1.000 8.46   ? 61  ARG A C    1 
ATOM   1140 O O    . ARG A 1 61  ? 24.968 21.521 2.268  1.000 14.06  ? 61  ARG A O    1 
ATOM   1141 C CB   . ARG A 1 61  ? 28.139 20.603 2.437  1.000 10.67  ? 61  ARG A CB   1 
ATOM   1142 C CG   . ARG A 1 61  ? 27.914 20.701 0.948  1.000 13.51  ? 61  ARG A CG   1 
ATOM   1143 C CD   . ARG A 1 61  ? 28.852 19.829 0.161  1.000 17.90  ? 61  ARG A CD   1 
ATOM   1144 N NE   . ARG A 1 61  ? 30.223 20.071 0.439  1.000 24.84  ? 61  ARG A NE   1 
ATOM   1145 C CZ   . ARG A 1 61  ? 31.097 20.962 0.023  1.000 30.87  ? 61  ARG A CZ   1 
ATOM   1146 N NH1  . ARG A 1 61  ? 30.870 21.940 -0.852 1.000 54.85  ? 61  ARG A NH1  1 
ATOM   1147 N NH2  . ARG A 1 61  ? 32.299 20.905 0.520  1.000 44.14  ? 61  ARG A NH2  1 
ATOM   1148 H H    . ARG A 1 61  ? 28.008 20.933 4.983  1.000 9.95   ? 61  ARG A H    1 
ATOM   1149 H HA   . ARG A 1 61  ? 27.185 22.352 2.838  1.000 10.21  ? 61  ARG A HA   1 
ATOM   1150 H HB2  . ARG A 1 61  ? 29.039 20.898 2.646  1.000 12.81  ? 61  ARG A HB2  1 
ATOM   1151 H HB3  . ARG A 1 61  ? 28.056 19.677 2.713  1.000 12.81  ? 61  ARG A HB3  1 
ATOM   1152 H HG2  . ARG A 1 61  ? 27.000 20.445 0.748  1.000 16.21  ? 61  ARG A HG2  1 
ATOM   1153 H HG3  . ARG A 1 61  ? 28.031 21.623 0.671  1.000 16.21  ? 61  ARG A HG3  1 
ATOM   1154 H HD2  . ARG A 1 61  ? 28.652 18.900 0.354  1.000 21.48  ? 61  ARG A HD2  1 
ATOM   1155 H HD3  . ARG A 1 61  ? 28.694 19.974 -0.785 1.000 21.48  ? 61  ARG A HD3  1 
ATOM   1156 H HE   . ARG A 1 61  ? 30.555 19.513 1.004  1.000 29.80  ? 61  ARG A HE   1 
ATOM   1157 H HH11 . ARG A 1 61  ? 31.500 22.488 -1.059 1.000 65.82  ? 61  ARG A HH11 1 
ATOM   1158 H HH12 . ARG A 1 61  ? 30.093 22.024 -1.211 1.000 65.82  ? 61  ARG A HH12 1 
ATOM   1159 H HH21 . ARG A 1 61  ? 32.498 20.300 1.099  1.000 52.97  ? 61  ARG A HH21 1 
ATOM   1160 H HH22 . ARG A 1 61  ? 32.895 21.472 0.270  1.000 52.97  ? 61  ARG A HH22 1 
ATOM   1161 N N    . TRP A 1 62  ? 25.329 19.868 3.675  1.000 9.35   ? 62  TRP A N    1 
ATOM   1162 C CA   . TRP A 1 62  ? 23.996 19.327 3.455  1.000 10.04  ? 62  TRP A CA   1 
ATOM   1163 C C    . TRP A 1 62  ? 23.009 19.765 4.538  1.000 7.97   ? 62  TRP A C    1 
ATOM   1164 O O    . TRP A 1 62  ? 21.825 19.854 4.203  1.000 9.68   ? 62  TRP A O    1 
ATOM   1165 C CB   . TRP A 1 62  ? 23.875 17.841 3.289  1.000 13.98  ? 62  TRP A CB   1 
ATOM   1166 C CG   . TRP A 1 62  ? 24.385 17.302 1.990  1.000 13.39  ? 62  TRP A CG   1 
ATOM   1167 C CD1  . TRP A 1 62  ? 25.082 17.918 1.009  1.000 16.08  ? 62  TRP A CD1  1 
ATOM   1168 C CD2  . TRP A 1 62  ? 24.194 15.970 1.526  1.000 15.70  ? 62  TRP A CD2  1 
ATOM   1169 N NE1  . TRP A 1 62  ? 25.364 17.072 -0.006 1.000 19.55  ? 62  TRP A NE1  1 
ATOM   1170 C CE2  . TRP A 1 62  ? 24.815 15.830 0.287  1.000 18.18  ? 62  TRP A CE2  1 
ATOM   1171 C CE3  . TRP A 1 62  ? 23.552 14.812 2.070  1.000 22.93  ? 62  TRP A CE3  1 
ATOM   1172 C CZ2  . TRP A 1 62  ? 24.800 14.631 -0.398 1.000 21.92  ? 62  TRP A CZ2  1 
ATOM   1173 C CZ3  . TRP A 1 62  ? 23.547 13.630 1.386  1.000 26.07  ? 62  TRP A CZ3  1 
ATOM   1174 C CH2  . TRP A 1 62  ? 24.172 13.508 0.125  1.000 28.55  ? 62  TRP A CH2  1 
ATOM   1175 H H    . TRP A 1 62  ? 25.860 19.486 4.234  1.000 11.22  ? 62  TRP A H    1 
ATOM   1176 H HA   . TRP A 1 62  ? 23.676 19.722 2.618  1.000 12.05  ? 62  TRP A HA   1 
ATOM   1177 H HB2  . TRP A 1 62  ? 24.358 17.410 4.012  1.000 16.77  ? 62  TRP A HB2  1 
ATOM   1178 H HB3  . TRP A 1 62  ? 22.940 17.597 3.378  1.000 16.77  ? 62  TRP A HB3  1 
ATOM   1179 H HD1  . TRP A 1 62  ? 25.337 18.812 1.030  1.000 19.30  ? 62  TRP A HD1  1 
ATOM   1180 H HE1  . TRP A 1 62  ? 25.808 17.269 -0.715 1.000 23.46  ? 62  TRP A HE1  1 
ATOM   1181 H HE3  . TRP A 1 62  ? 23.133 14.866 2.898  1.000 27.52  ? 62  TRP A HE3  1 
ATOM   1182 H HZ2  . TRP A 1 62  ? 25.220 14.574 -1.225 1.000 26.30  ? 62  TRP A HZ2  1 
ATOM   1183 H HZ3  . TRP A 1 62  ? 23.124 12.890 1.759  1.000 31.28  ? 62  TRP A HZ3  1 
ATOM   1184 H HH2  . TRP A 1 62  ? 24.162 12.703 -0.341 1.000 34.26  ? 62  TRP A HH2  1 
ATOM   1185 N N    . TRP A 1 63  ? 23.402 19.972 5.794  1.000 7.59   ? 63  TRP A N    1 
ATOM   1186 C CA   . TRP A 1 63  ? 22.428 19.857 6.873  1.000 7.04   ? 63  TRP A CA   1 
ATOM   1187 C C    . TRP A 1 63  ? 22.012 21.156 7.518  1.000 7.23   ? 63  TRP A C    1 
ATOM   1188 O O    . TRP A 1 63  ? 20.858 21.281 7.918  1.000 9.37   ? 63  TRP A O    1 
ATOM   1189 C CB   . TRP A 1 63  ? 22.920 18.849 7.935  1.000 8.64   ? 63  TRP A CB   1 
ATOM   1190 C CG   . TRP A 1 63  ? 23.204 17.532 7.308  1.000 8.98   ? 63  TRP A CG   1 
ATOM   1191 C CD1  . TRP A 1 63  ? 24.420 16.963 7.126  1.000 11.86  ? 63  TRP A CD1  1 
ATOM   1192 C CD2  . TRP A 1 63  ? 22.241 16.625 6.727  1.000 9.14   ? 63  TRP A CD2  1 
ATOM   1193 N NE1  . TRP A 1 63  ? 24.310 15.777 6.494  1.000 13.58  ? 63  TRP A NE1  1 
ATOM   1194 C CE2  . TRP A 1 63  ? 22.979 15.539 6.236  1.000 11.22  ? 63  TRP A CE2  1 
ATOM   1195 C CE3  . TRP A 1 63  ? 20.866 16.628 6.630  1.000 9.81   ? 63  TRP A CE3  1 
ATOM   1196 C CZ2  . TRP A 1 63  ? 22.328 14.481 5.606  1.000 13.03  ? 63  TRP A CZ2  1 
ATOM   1197 C CZ3  . TRP A 1 63  ? 20.249 15.554 5.988  1.000 12.31  ? 63  TRP A CZ3  1 
ATOM   1198 C CH2  . TRP A 1 63  ? 20.979 14.497 5.495  1.000 13.68  ? 63  TRP A CH2  1 
ATOM   1199 H H    . TRP A 1 63  ? 24.220 20.171 5.966  1.000 9.10   ? 63  TRP A H    1 
ATOM   1200 H HA   . TRP A 1 63  ? 21.619 19.471 6.477  1.000 8.45   ? 63  TRP A HA   1 
ATOM   1201 H HB2  . TRP A 1 63  ? 23.724 19.188 8.358  1.000 10.37  ? 63  TRP A HB2  1 
ATOM   1202 H HB3  . TRP A 1 63  ? 22.241 18.742 8.620  1.000 10.37  ? 63  TRP A HB3  1 
ATOM   1203 H HD1  . TRP A 1 63  ? 25.225 17.340 7.401  1.000 14.23  ? 63  TRP A HD1  1 
ATOM   1204 H HE1  . TRP A 1 63  ? 24.962 15.257 6.286  1.000 16.30  ? 63  TRP A HE1  1 
ATOM   1205 H HE3  . TRP A 1 63  ? 20.364 17.326 6.983  1.000 11.77  ? 63  TRP A HE3  1 
ATOM   1206 H HZ2  . TRP A 1 63  ? 22.817 13.768 5.263  1.000 15.64  ? 63  TRP A HZ2  1 
ATOM   1207 H HZ3  . TRP A 1 63  ? 19.324 15.553 5.891  1.000 14.77  ? 63  TRP A HZ3  1 
ATOM   1208 H HH2  . TRP A 1 63  ? 20.542 13.787 5.082  1.000 16.41  ? 63  TRP A HH2  1 
ATOM   1209 N N    . CYS A 1 64  ? 22.888 22.121 7.686  1.000 9.37   ? 64  CYS A N    1 
ATOM   1210 C CA   . CYS A 1 64  ? 22.565 23.380 8.344  1.000 8.80   ? 64  CYS A CA   1 
ATOM   1211 C C    . CYS A 1 64  ? 23.157 24.505 7.543  1.000 8.75   ? 64  CYS A C    1 
ATOM   1212 O O    . CYS A 1 64  ? 24.095 24.290 6.773  1.000 10.43  ? 64  CYS A O    1 
ATOM   1213 C CB   . CYS A 1 64  ? 23.058 23.396 9.786  1.000 8.81   ? 64  CYS A CB   1 
ATOM   1214 S SG   . CYS A 1 64  ? 24.863 23.256 10.005 1.000 9.18   ? 64  CYS A SG   1 
ATOM   1215 H H    . CYS A 1 64  ? 23.689 22.004 7.394  1.000 11.24  ? 64  CYS A H    1 
ATOM   1216 H HA   . CYS A 1 64  ? 21.591 23.484 8.349  1.000 10.56  ? 64  CYS A HA   1 
ATOM   1217 H HB2  . CYS A 1 64  ? 22.763 24.221 10.201 1.000 10.57  ? 64  CYS A HB2  1 
ATOM   1218 H HB3  . CYS A 1 64  ? 22.635 22.664 10.261 1.000 10.57  ? 64  CYS A HB3  1 
ATOM   1219 N N    A ASN A 1 65  ? 22.633 25.710 7.730  0.611 9.39   ? 65  ASN A N    1 
ATOM   1220 N N    B ASN A 1 65  ? 22.639 25.710 7.757  0.389 9.15   ? 65  ASN A N    1 
ATOM   1221 C CA   A ASN A 1 65  ? 23.118 26.880 7.002  0.611 9.78   ? 65  ASN A CA   1 
ATOM   1222 C CA   B ASN A 1 65  ? 23.122 26.879 7.035  0.389 9.93   ? 65  ASN A CA   1 
ATOM   1223 C C    A ASN A 1 65  ? 24.066 27.706 7.858  0.611 8.72   ? 65  ASN A C    1 
ATOM   1224 C C    B ASN A 1 65  ? 24.077 27.702 7.887  0.389 9.07   ? 65  ASN A C    1 
ATOM   1225 O O    A ASN A 1 65  ? 23.648 28.223 8.896  0.611 9.99   ? 65  ASN A O    1 
ATOM   1226 O O    B ASN A 1 65  ? 23.722 28.201 8.958  0.389 10.43  ? 65  ASN A O    1 
ATOM   1227 C CB   A ASN A 1 65  ? 21.908 27.746 6.621  0.611 13.22  ? 65  ASN A CB   1 
ATOM   1228 C CB   B ASN A 1 65  ? 21.905 27.730 6.626  0.389 13.15  ? 65  ASN A CB   1 
ATOM   1229 C CG   A ASN A 1 65  ? 22.305 28.852 5.678  0.611 16.95  ? 65  ASN A CG   1 
ATOM   1230 C CG   B ASN A 1 65  ? 22.379 28.978 5.919  0.389 16.05  ? 65  ASN A CG   1 
ATOM   1231 O OD1  A ASN A 1 65  ? 23.419 28.949 5.157  0.611 17.02  ? 65  ASN A OD1  1 
ATOM   1232 O OD1  B ASN A 1 65  ? 23.099 28.838 4.925  0.389 15.42  ? 65  ASN A OD1  1 
ATOM   1233 N ND2  A ASN A 1 65  ? 21.345 29.716 5.416  0.611 26.94  ? 65  ASN A ND2  1 
ATOM   1234 N ND2  B ASN A 1 65  ? 22.013 30.147 6.395  0.389 20.35  ? 65  ASN A ND2  1 
ATOM   1235 H H    A ASN A 1 65  ? 21.991 25.805 8.294  0.611 11.27  ? 65  ASN A H    1 
ATOM   1236 H H    B ASN A 1 65  ? 22.007 25.801 8.332  0.389 10.98  ? 65  ASN A H    1 
ATOM   1237 H HA   A ASN A 1 65  ? 23.581 26.589 6.189  0.611 11.74  ? 65  ASN A HA   1 
ATOM   1238 H HA   B ASN A 1 65  ? 23.591 26.584 6.226  0.389 11.92  ? 65  ASN A HA   1 
ATOM   1239 H HB2  A ASN A 1 65  ? 21.234 27.190 6.199  0.611 15.86  ? 65  ASN A HB2  1 
ATOM   1240 H HB2  B ASN A 1 65  ? 21.329 27.217 6.038  0.389 15.78  ? 65  ASN A HB2  1 
ATOM   1241 H HB3  A ASN A 1 65  ? 21.522 28.130 7.423  0.611 15.86  ? 65  ASN A HB3  1 
ATOM   1242 H HB3  B ASN A 1 65  ? 21.395 27.972 7.415  0.389 15.78  ? 65  ASN A HB3  1 
ATOM   1243 H HD21 A ASN A 1 65  ? 21.488 30.365 4.871  0.611 32.32  ? 65  ASN A HD21 1 
ATOM   1244 H HD21 B ASN A 1 65  ? 22.276 30.869 6.010  0.389 24.42  ? 65  ASN A HD21 1 
ATOM   1245 H HD22 A ASN A 1 65  ? 20.575 29.630 5.790  0.611 32.32  ? 65  ASN A HD22 1 
ATOM   1246 H HD22 B ASN A 1 65  ? 21.510 30.189 7.092  0.389 24.42  ? 65  ASN A HD22 1 
ATOM   1247 N N    . ASP A 1 66  ? 25.298 27.890 7.390  1.000 9.15   ? 66  ASP A N    1 
ATOM   1248 C CA   . ASP A 1 66  ? 26.232 28.843 8.016  1.000 9.38   ? 66  ASP A CA   1 
ATOM   1249 C C    . ASP A 1 66  ? 26.547 30.014 7.127  1.000 10.18  ? 66  ASP A C    1 
ATOM   1250 O O    . ASP A 1 66  ? 27.335 30.872 7.518  1.000 12.60  ? 66  ASP A O    1 
ATOM   1251 C CB   . ASP A 1 66  ? 27.489 28.174 8.554  1.000 9.50   ? 66  ASP A CB   1 
ATOM   1252 C CG   . ASP A 1 66  ? 28.440 27.632 7.536  1.000 8.67   ? 66  ASP A CG   1 
ATOM   1253 O OD1  . ASP A 1 66  ? 28.238 27.843 6.329  1.000 10.35  ? 66  ASP A OD1  1 
ATOM   1254 O OD2  . ASP A 1 66  ? 29.419 26.992 8.004  1.000 10.37  ? 66  ASP A OD2  1 
ATOM   1255 H H    A ASP A 1 66  ? 25.557 27.441 6.704  1.000 10.98  ? 66  ASP A H    1 
ATOM   1256 H HA   . ASP A 1 66  ? 25.765 29.211 8.795  1.000 11.25  ? 66  ASP A HA   1 
ATOM   1257 H HB2  . ASP A 1 66  ? 27.966 28.818 9.100  1.000 11.40  ? 66  ASP A HB2  1 
ATOM   1258 H HB3  . ASP A 1 66  ? 27.220 27.445 9.135  1.000 11.40  ? 66  ASP A HB3  1 
ATOM   1259 N N    A GLY A 1 67  ? 26.052 30.107 5.900  0.437 12.59  ? 67  GLY A N    1 
ATOM   1260 N N    B GLY A 1 67  ? 25.905 30.076 5.977  0.563 10.92  ? 67  GLY A N    1 
ATOM   1261 C CA   A GLY A 1 67  ? 26.209 31.296 5.039  0.437 14.02  ? 67  GLY A CA   1 
ATOM   1262 C CA   B GLY A 1 67  ? 26.080 31.184 5.036  0.563 15.51  ? 67  GLY A CA   1 
ATOM   1263 C C    A GLY A 1 67  ? 27.572 31.416 4.416  0.437 14.49  ? 67  GLY A C    1 
ATOM   1264 C C    B GLY A 1 67  ? 27.367 31.172 4.252  0.563 16.29  ? 67  GLY A C    1 
ATOM   1265 O O    A GLY A 1 67  ? 27.995 32.371 3.791  0.437 17.32  ? 67  GLY A O    1 
ATOM   1266 O O    B GLY A 1 67  ? 27.376 31.978 3.322  0.563 24.68  ? 67  GLY A O    1 
ATOM   1267 H H    A GLY A 1 67  ? 25.615 29.435 5.588  0.437 15.11  ? 67  GLY A H    1 
ATOM   1268 H H    B GLY A 1 67  ? 25.362 29.441 5.772  0.563 13.10  ? 67  GLY A H    1 
ATOM   1269 H HA2  A GLY A 1 67  ? 25.544 31.260 4.334  0.437 16.82  ? 67  GLY A HA2  1 
ATOM   1270 H HA2  B GLY A 1 67  ? 25.340 31.173 4.409  0.563 18.61  ? 67  GLY A HA2  1 
ATOM   1271 H HA3  A GLY A 1 67  ? 26.035 32.090 5.568  0.437 16.82  ? 67  GLY A HA3  1 
ATOM   1272 H HA3  B GLY A 1 67  ? 26.030 32.017 5.530  0.563 18.61  ? 67  GLY A HA3  1 
ATOM   1273 N N    . ARG A 1 68  ? 28.364 30.371 4.588  1.000 13.32  ? 68  ARG A N    1 
ATOM   1274 C CA   . ARG A 1 68  ? 29.730 30.431 4.077  1.000 16.88  ? 68  ARG A CA   1 
ATOM   1275 C C    . ARG A 1 68  ? 30.087 29.180 3.281  1.000 15.44  ? 68  ARG A C    1 
ATOM   1276 O O    . ARG A 1 68  ? 31.166 29.101 2.724  1.000 22.86  ? 68  ARG A O    1 
ATOM   1277 C CB   . ARG A 1 68  ? 30.747 30.626 5.217  1.000 25.85  ? 68  ARG A CB   1 
ATOM   1278 C CG   . ARG A 1 68  ? 30.515 31.917 5.995  1.000 34.89  ? 68  ARG A CG   1 
ATOM   1279 C CD   . ARG A 1 68  ? 31.576 32.232 7.050  1.000 48.07  ? 68  ARG A CD   1 
ATOM   1280 N NE   . ARG A 1 68  ? 31.889 31.113 7.911  1.000 46.76  ? 68  ARG A NE   1 
ATOM   1281 C CZ   . ARG A 1 68  ? 31.391 30.454 8.921  1.000 45.95  ? 68  ARG A CZ   1 
ATOM   1282 N NH1  . ARG A 1 68  ? 30.997 29.195 8.760  1.000 78.27  ? 68  ARG A NH1  1 
ATOM   1283 N NH2  . ARG A 1 68  ? 31.375 30.988 10.119 1.000 68.03  ? 68  ARG A NH2  1 
ATOM   1284 H H    A ARG A 1 68  ? 28.079 29.668 4.993  1.000 15.99  ? 68  ARG A H    1 
ATOM   1285 H HA   . ARG A 1 68  ? 29.796 31.202 3.476  1.000 20.26  ? 68  ARG A HA   1 
ATOM   1286 H HB2  . ARG A 1 68  ? 30.688 29.874 5.827  1.000 31.02  ? 68  ARG A HB2  1 
ATOM   1287 H HB3  . ARG A 1 68  ? 31.643 30.636 4.845  1.000 31.02  ? 68  ARG A HB3  1 
ATOM   1288 H HG2  . ARG A 1 68  ? 30.478 32.654 5.365  1.000 41.87  ? 68  ARG A HG2  1 
ATOM   1289 H HG3  . ARG A 1 68  ? 29.651 31.863 6.433  1.000 41.87  ? 68  ARG A HG3  1 
ATOM   1290 H HD2  . ARG A 1 68  ? 32.387 32.519 6.602  1.000 57.68  ? 68  ARG A HD2  1 
ATOM   1291 H HD3  . ARG A 1 68  ? 31.264 32.970 7.596  1.000 57.68  ? 68  ARG A HD3  1 
ATOM   1292 H HE   . ARG A 1 68  ? 32.647 30.775 7.686  1.000 56.12  ? 68  ARG A HE   1 
ATOM   1293 H HH11 . ARG A 1 68  ? 31.070 28.816 7.991  1.000 93.92  ? 68  ARG A HH11 1 
ATOM   1294 H HH12 . ARG A 1 68  ? 30.669 28.759 9.425  1.000 93.92  ? 68  ARG A HH12 1 
ATOM   1295 H HH21 . ARG A 1 68  ? 31.693 31.778 10.242 1.000 81.64  ? 68  ARG A HH21 1 
ATOM   1296 H HH22 . ARG A 1 68  ? 31.046 30.549 10.781 1.000 81.64  ? 68  ARG A HH22 1 
ATOM   1297 N N    . THR A 1 69  ? 29.194 28.181 3.193  1.000 11.91  ? 69  THR A N    1 
ATOM   1298 C CA   . THR A 1 69  ? 29.538 26.897 2.623  1.000 10.55  ? 69  THR A CA   1 
ATOM   1299 C C    . THR A 1 69  ? 28.997 26.767 1.218  1.000 11.24  ? 69  THR A C    1 
ATOM   1300 O O    . THR A 1 69  ? 27.807 26.916 0.981  1.000 13.14  ? 69  THR A O    1 
ATOM   1301 C CB   . THR A 1 69  ? 28.952 25.755 3.476  1.000 9.83   ? 69  THR A CB   1 
ATOM   1302 O OG1  . THR A 1 69  ? 29.441 25.892 4.816  1.000 10.31  ? 69  THR A OG1  1 
ATOM   1303 C CG2  . THR A 1 69  ? 29.414 24.422 2.941  1.000 10.90  ? 69  THR A CG2  1 
ATOM   1304 H H    . THR A 1 69  ? 28.395 28.309 3.483  1.000 14.29  ? 69  THR A H    1 
ATOM   1305 H HA   . THR A 1 69  ? 30.514 26.809 2.599  1.000 12.66  ? 69  THR A HA   1 
ATOM   1306 H HB   . THR A 1 69  ? 27.973 25.799 3.469  1.000 11.80  ? 69  THR A HB   1 
ATOM   1307 H HG1  . THR A 1 69  ? 29.203 26.615 5.121  1.000 15.47  ? 69  THR A HG1  1 
ATOM   1308 H HG21 . THR A 1 69  ? 29.096 24.310 2.042  1.000 16.35  ? 69  THR A HG21 1 
ATOM   1309 H HG22 . THR A 1 69  ? 30.374 24.390 2.947  1.000 16.35  ? 69  THR A HG22 1 
ATOM   1310 H HG23 . THR A 1 69  ? 29.067 23.717 3.493  1.000 16.35  ? 69  THR A HG23 1 
ATOM   1311 N N    . PRO A 1 70  ? 29.834 26.459 0.216  1.000 11.84  ? 70  PRO A N    1 
ATOM   1312 C CA   . PRO A 1 70  ? 29.311 26.236 -1.139 1.000 13.03  ? 70  PRO A CA   1 
ATOM   1313 C C    . PRO A 1 70  ? 28.357 25.067 -1.201 1.000 13.51  ? 70  PRO A C    1 
ATOM   1314 O O    . PRO A 1 70  ? 28.563 24.061 -0.525 1.000 16.84  ? 70  PRO A O    1 
ATOM   1315 C CB   . PRO A 1 70  ? 30.564 26.033 -1.995 1.000 16.01  ? 70  PRO A CB   1 
ATOM   1316 C CG   . PRO A 1 70  ? 31.687 26.587 -1.170 1.000 21.91  ? 70  PRO A CG   1 
ATOM   1317 C CD   . PRO A 1 70  ? 31.261 26.354 0.256  1.000 15.70  ? 70  PRO A CD   1 
ATOM   1318 H HA   . PRO A 1 70  ? 28.846 27.045 -1.440 1.000 15.63  ? 70  PRO A HA   1 
ATOM   1319 H HB2  . PRO A 1 70  ? 30.705 25.092 -2.181 1.000 19.22  ? 70  PRO A HB2  1 
ATOM   1320 H HB3  . PRO A 1 70  ? 30.487 26.511 -2.836 1.000 19.22  ? 70  PRO A HB3  1 
ATOM   1321 H HG2  . PRO A 1 70  ? 32.517 26.123 -1.362 1.000 26.29  ? 70  PRO A HG2  1 
ATOM   1322 H HG3  . PRO A 1 70  ? 31.808 27.533 -1.344 1.000 26.29  ? 70  PRO A HG3  1 
ATOM   1323 H HD2  . PRO A 1 70  ? 31.536 25.475 0.560  1.000 18.84  ? 70  PRO A HD2  1 
ATOM   1324 H HD3  . PRO A 1 70  ? 31.641 27.025 0.845  1.000 18.84  ? 70  PRO A HD3  1 
ATOM   1325 N N    . GLY A 1 71  ? 27.338 25.148 -2.059 1.000 15.70  ? 71  GLY A N    1 
ATOM   1326 C CA   . GLY A 1 71  ? 26.486 24.018 -2.278 1.000 19.05  ? 71  GLY A CA   1 
ATOM   1327 C C    . GLY A 1 71  ? 25.498 23.701 -1.181 1.000 13.83  ? 71  GLY A C    1 
ATOM   1328 O O    . GLY A 1 71  ? 25.014 22.584 -1.081 1.000 18.89  ? 71  GLY A O    1 
ATOM   1329 H H    . GLY A 1 71  ? 27.192 25.882 -2.483 1.000 18.84  ? 71  GLY A H    1 
ATOM   1330 H HA2  . GLY A 1 71  ? 25.990 24.167 -3.098 1.000 22.86  ? 71  GLY A HA2  1 
ATOM   1331 H HA3  . GLY A 1 71  ? 27.046 23.238 -2.416 1.000 22.86  ? 71  GLY A HA3  1 
ATOM   1332 N N    . SER A 1 72  ? 25.234 24.646 -0.327 1.000 13.12  ? 72  SER A N    1 
ATOM   1333 C CA   . SER A 1 72  ? 24.401 24.419 0.842  1.000 12.17  ? 72  SER A CA   1 
ATOM   1334 C C    . SER A 1 72  ? 23.001 23.950 0.501  1.000 10.95  ? 72  SER A C    1 
ATOM   1335 O O    . SER A 1 72  ? 22.326 24.582 -0.312 1.000 15.73  ? 72  SER A O    1 
ATOM   1336 C CB   . SER A 1 72  ? 24.356 25.769 1.626  1.000 16.92  ? 72  SER A CB   1 
ATOM   1337 O OG   . SER A 1 72  ? 23.497 25.671 2.723  1.000 27.77  ? 72  SER A OG   1 
ATOM   1338 H H    . SER A 1 72  ? 25.563 25.430 -0.458 1.000 15.75  ? 72  SER A H    1 
ATOM   1339 H HA   . SER A 1 72  ? 24.830 23.743 1.407  1.000 14.60  ? 72  SER A HA   1 
ATOM   1340 H HB2  . SER A 1 72  ? 25.248 25.997 1.932  1.000 20.31  ? 72  SER A HB2  1 
ATOM   1341 H HB3  . SER A 1 72  ? 24.050 26.476 1.037  1.000 20.31  ? 72  SER A HB3  1 
ATOM   1342 H HG   . SER A 1 72  ? 23.804 25.137 3.264  1.000 41.66  ? 72  SER A HG   1 
ATOM   1343 N N    . ARG A 1 73  ? 22.552 22.893 1.157  1.000 9.33   ? 73  ARG A N    1 
ATOM   1344 C CA   . ARG A 1 73  ? 21.205 22.365 1.026  1.000 9.27   ? 73  ARG A CA   1 
ATOM   1345 C C    . ARG A 1 73  ? 20.312 22.689 2.202  1.000 8.64   ? 73  ARG A C    1 
ATOM   1346 O O    . ARG A 1 73  ? 19.089 22.668 2.085  1.000 10.53  ? 73  ARG A O    1 
ATOM   1347 C CB   . ARG A 1 73  ? 21.202 20.848 0.823  1.000 9.83   ? 73  ARG A CB   1 
ATOM   1348 C CG   . ARG A 1 73  ? 22.004 20.404 -0.356 1.000 11.02  ? 73  ARG A CG   1 
ATOM   1349 C CD   . ARG A 1 73  ? 21.882 18.932 -0.664 1.000 13.97  ? 73  ARG A CD   1 
ATOM   1350 N NE   . ARG A 1 73  ? 22.897 18.566 -1.636 1.000 17.63  ? 73  ARG A NE   1 
ATOM   1351 C CZ   . ARG A 1 73  ? 22.880 17.406 -2.255 1.000 21.55  ? 73  ARG A CZ   1 
ATOM   1352 N NH1  . ARG A 1 73  ? 21.900 16.551 -2.099 1.000 32.91  ? 73  ARG A NH1  1 
ATOM   1353 N NH2  . ARG A 1 73  ? 23.831 17.193 -3.135 1.000 28.88  ? 73  ARG A NH2  1 
ATOM   1354 H H    . ARG A 1 73  ? 23.091 22.494 1.695  1.000 11.20  ? 73  ARG A H    1 
ATOM   1355 H HA   . ARG A 1 73  ? 20.804 22.771 0.229  1.000 11.13  ? 73  ARG A HA   1 
ATOM   1356 H HB2  . ARG A 1 73  ? 21.556 20.424 1.620  1.000 11.80  ? 73  ARG A HB2  1 
ATOM   1357 H HB3  . ARG A 1 73  ? 20.287 20.548 0.711  1.000 11.80  ? 73  ARG A HB3  1 
ATOM   1358 H HG2  . ARG A 1 73  ? 21.721 20.910 -1.134 1.000 13.22  ? 73  ARG A HG2  1 
ATOM   1359 H HG3  . ARG A 1 73  ? 22.938 20.612 -0.195 1.000 13.22  ? 73  ARG A HG3  1 
ATOM   1360 H HD2  . ARG A 1 73  ? 22.000 18.414 0.147  1.000 16.76  ? 73  ARG A HD2  1 
ATOM   1361 H HD3  . ARG A 1 73  ? 21.000 18.742 -1.021 1.000 16.76  ? 73  ARG A HD3  1 
ATOM   1362 H HE   . ARG A 1 73  ? 23.527 19.124 -1.811 1.000 21.16  ? 73  ARG A HE   1 
ATOM   1363 H HH11 . ARG A 1 73  ? 21.873 15.837 -2.577 1.000 39.49  ? 73  ARG A HH11 1 
ATOM   1364 H HH12 . ARG A 1 73  ? 21.284 16.704 -1.519 1.000 39.49  ? 73  ARG A HH12 1 
ATOM   1365 H HH21 . ARG A 1 73  ? 23.818 16.483 -3.619 1.000 34.66  ? 73  ARG A HH21 1 
ATOM   1366 H HH22 . ARG A 1 73  ? 24.469 17.763 -3.226 1.000 34.66  ? 73  ARG A HH22 1 
ATOM   1367 N N    . ASN A 1 74  ? 20.893 22.892 3.386  1.000 8.32   ? 74  ASN A N    1 
ATOM   1368 C CA   . ASN A 1 74  ? 20.171 23.176 4.617  1.000 7.89   ? 74  ASN A CA   1 
ATOM   1369 C C    . ASN A 1 74  ? 18.975 22.260 4.830  1.000 7.50   ? 74  ASN A C    1 
ATOM   1370 O O    . ASN A 1 74  ? 17.848 22.703 5.066  1.000 8.61   ? 74  ASN A O    1 
ATOM   1371 C CB   . ASN A 1 74  ? 19.761 24.631 4.711  1.000 9.38   ? 74  ASN A CB   1 
ATOM   1372 C CG   . ASN A 1 74  ? 19.310 25.016 6.097  1.000 9.36   ? 74  ASN A CG   1 
ATOM   1373 O OD1  . ASN A 1 74  ? 19.521 24.279 7.060  1.000 9.84   ? 74  ASN A OD1  1 
ATOM   1374 N ND2  . ASN A 1 74  ? 18.685 26.184 6.186  1.000 12.87  ? 74  ASN A ND2  1 
ATOM   1375 H H    . ASN A 1 74  ? 21.752 22.852 3.424  1.000 9.99   ? 74  ASN A H    1 
ATOM   1376 H HA   . ASN A 1 74  ? 20.793 23.007 5.356  1.000 9.46   ? 74  ASN A HA   1 
ATOM   1377 H HB2  . ASN A 1 74  ? 20.512 25.189 4.455  1.000 11.26  ? 74  ASN A HB2  1 
ATOM   1378 H HB3  . ASN A 1 74  ? 19.040 24.798 4.084  1.000 11.26  ? 74  ASN A HB3  1 
ATOM   1379 H HD21 . ASN A 1 74  ? 18.402 26.463 6.949  1.000 15.44  ? 74  ASN A HD21 1 
ATOM   1380 H HD22 . ASN A 1 74  ? 18.563 26.661 5.481  1.000 15.44  ? 74  ASN A HD22 1 
ATOM   1381 N N    . LEU A 1 75  ? 19.216 20.948 4.834  1.000 7.42   ? 75  LEU A N    1 
ATOM   1382 C CA   . LEU A 1 75  ? 18.115 20.001 4.896  1.000 7.61   ? 75  LEU A CA   1 
ATOM   1383 C C    . LEU A 1 75  ? 17.476 19.914 6.283  1.000 7.54   ? 75  LEU A C    1 
ATOM   1384 O O    . LEU A 1 75  ? 16.324 19.514 6.392  1.000 9.43   ? 75  LEU A O    1 
ATOM   1385 C CB   . LEU A 1 75  ? 18.552 18.619 4.432  1.000 8.27   ? 75  LEU A CB   1 
ATOM   1386 C CG   . LEU A 1 75  ? 19.006 18.571 2.968  1.000 9.07   ? 75  LEU A CG   1 
ATOM   1387 C CD1  . LEU A 1 75  ? 19.470 17.157 2.646  1.000 12.37  ? 75  LEU A CD1  1 
ATOM   1388 C CD2  . LEU A 1 75  ? 17.929 19.032 2.005  1.000 11.29  ? 75  LEU A CD2  1 
ATOM   1389 H H    . LEU A 1 75  ? 20.026 20.661 4.799  1.000 8.90   ? 75  LEU A H    1 
ATOM   1390 H HA   . LEU A 1 75  ? 17.425 20.314 4.275  1.000 9.13   ? 75  LEU A HA   1 
ATOM   1391 H HB2  . LEU A 1 75  ? 19.282 18.317 4.995  1.000 9.92   ? 75  LEU A HB2  1 
ATOM   1392 H HB3  . LEU A 1 75  ? 17.813 18.002 4.550  1.000 9.92   ? 75  LEU A HB3  1 
ATOM   1393 H HG   . LEU A 1 75  ? 19.775 19.171 2.870  1.000 10.89  ? 75  LEU A HG   1 
ATOM   1394 H HD11 . LEU A 1 75  ? 20.150 16.893 3.270  1.000 18.55  ? 75  LEU A HD11 1 
ATOM   1395 H HD12 . LEU A 1 75  ? 18.726 16.554 2.709  1.000 18.55  ? 75  LEU A HD12 1 
ATOM   1396 H HD13 . LEU A 1 75  ? 19.827 17.132 1.755  1.000 18.55  ? 75  LEU A HD13 1 
ATOM   1397 H HD21 . LEU A 1 75  ? 17.658 19.925 2.233  1.000 16.94  ? 75  LEU A HD21 1 
ATOM   1398 H HD22 . LEU A 1 75  ? 18.275 19.021 1.110  1.000 16.94  ? 75  LEU A HD22 1 
ATOM   1399 H HD23 . LEU A 1 75  ? 17.174 18.443 2.064  1.000 16.94  ? 75  LEU A HD23 1 
ATOM   1400 N N    . CYS A 1 76  ? 18.201 20.294 7.349  1.000 7.30   ? 76  CYS A N    1 
ATOM   1401 C CA   . CYS A 1 76  ? 17.595 20.389 8.668  1.000 7.44   ? 76  CYS A CA   1 
ATOM   1402 C C    . CYS A 1 76  ? 16.864 21.693 8.887  1.000 7.76   ? 76  CYS A C    1 
ATOM   1403 O O    . CYS A 1 76  ? 16.200 21.866 9.911  1.000 9.56   ? 76  CYS A O    1 
ATOM   1404 C CB   . CYS A 1 76  ? 18.625 20.177 9.773  1.000 7.81   ? 76  CYS A CB   1 
ATOM   1405 S SG   . CYS A 1 76  ? 19.155 18.444 9.773  1.000 8.51   ? 76  CYS A SG   1 
ATOM   1406 H H    . CYS A 1 76  ? 19.034 20.484 7.250  1.000 8.75   ? 76  CYS A H    1 
ATOM   1407 H HA   . CYS A 1 76  ? 16.936 19.668 8.740  1.000 8.93   ? 76  CYS A HA   1 
ATOM   1408 H HB2  . CYS A 1 76  ? 19.390 20.755 9.625  1.000 9.38   ? 76  CYS A HB2  1 
ATOM   1409 H HB3  . CYS A 1 76  ? 18.236 20.402 10.632 1.000 9.38   ? 76  CYS A HB3  1 
ATOM   1410 N N    . ASN A 1 77  ? 16.996 22.656 7.968  1.000 7.60   ? 77  ASN A N    1 
ATOM   1411 C CA   . ASN A 1 77  ? 16.302 23.936 8.035  1.000 7.87   ? 77  ASN A CA   1 
ATOM   1412 C C    . ASN A 1 77  ? 16.616 24.687 9.310  1.000 8.24   ? 77  ASN A C    1 
ATOM   1413 O O    . ASN A 1 77  ? 15.743 25.196 9.994  1.000 10.34  ? 77  ASN A O    1 
ATOM   1414 C CB   . ASN A 1 77  ? 14.786 23.783 7.851  1.000 9.05   ? 77  ASN A CB   1 
ATOM   1415 C CG   . ASN A 1 77  ? 14.129 25.100 7.523  1.000 10.60  ? 77  ASN A CG   1 
ATOM   1416 O OD1  . ASN A 1 77  ? 14.755 26.021 7.049  1.000 12.73  ? 77  ASN A OD1  1 
ATOM   1417 N ND2  . ASN A 1 77  ? 12.852 25.168 7.825  1.000 16.00  ? 77  ASN A ND2  1 
ATOM   1418 H H    . ASN A 1 77  ? 17.520 22.513 7.301  1.000 9.12   ? 77  ASN A H    1 
ATOM   1419 H HA   . ASN A 1 77  ? 16.630 24.482 7.290  1.000 9.45   ? 77  ASN A HA   1 
ATOM   1420 H HB2  . ASN A 1 77  ? 14.612 23.152 7.136  1.000 10.86  ? 77  ASN A HB2  1 
ATOM   1421 H HB3  . ASN A 1 77  ? 14.399 23.426 8.666  1.000 10.86  ? 77  ASN A HB3  1 
ATOM   1422 H HD21 . ASN A 1 77  ? 12.416 25.897 7.688  1.000 19.20  ? 77  ASN A HD21 1 
ATOM   1423 H HD22 . ASN A 1 77  ? 12.452 24.485 8.161  1.000 19.20  ? 77  ASN A HD22 1 
ATOM   1424 N N    . ILE A 1 78  ? 17.923 24.832 9.599  1.000 8.19   ? 78  ILE A N    1 
ATOM   1425 C CA   . ILE A 1 78  ? 18.358 25.520 10.791 1.000 8.60   ? 78  ILE A CA   1 
ATOM   1426 C C    . ILE A 1 78  ? 19.677 26.227 10.511 1.000 8.45   ? 78  ILE A C    1 
ATOM   1427 O O    . ILE A 1 78  ? 20.506 25.738 9.746  1.000 9.63   ? 78  ILE A O    1 
ATOM   1428 C CB   . ILE A 1 78  ? 18.579 24.590 11.981 1.000 10.42  ? 78  ILE A CB   1 
ATOM   1429 C CG1  . ILE A 1 78  ? 19.485 23.403 11.601 1.000 11.22  ? 78  ILE A CG1  1 
ATOM   1430 C CG2  . ILE A 1 78  ? 17.299 24.170 12.661 1.000 13.97  ? 78  ILE A CG2  1 
ATOM   1431 C CD1  . ILE A 1 78  ? 20.033 22.644 12.766 1.000 17.40  ? 78  ILE A CD1  1 
ATOM   1432 H H    . ILE A 1 78  ? 18.511 24.509 9.061  1.000 9.83   ? 78  ILE A H    1 
ATOM   1433 H HA   . ILE A 1 78  ? 17.685 26.190 11.033 1.000 10.32  ? 78  ILE A HA   1 
ATOM   1434 H HB   . ILE A 1 78  ? 19.079 25.112 12.643 1.000 12.50  ? 78  ILE A HB   1 
ATOM   1435 H HG12 . ILE A 1 78  ? 18.978 22.792 11.044 1.000 13.46  ? 78  ILE A HG12 1 
ATOM   1436 H HG13 . ILE A 1 78  ? 20.227 23.736 11.072 1.000 13.46  ? 78  ILE A HG13 1 
ATOM   1437 H HG21 . ILE A 1 78  ? 17.504 23.589 13.397 1.000 20.96  ? 78  ILE A HG21 1 
ATOM   1438 H HG22 . ILE A 1 78  ? 16.839 24.948 12.985 1.000 20.96  ? 78  ILE A HG22 1 
ATOM   1439 H HG23 . ILE A 1 78  ? 16.740 23.707 12.033 1.000 20.96  ? 78  ILE A HG23 1 
ATOM   1440 H HD11 . ILE A 1 78  ? 20.584 21.924 12.449 1.000 26.10  ? 78  ILE A HD11 1 
ATOM   1441 H HD12 . ILE A 1 78  ? 20.559 23.232 13.313 1.000 26.10  ? 78  ILE A HD12 1 
ATOM   1442 H HD13 . ILE A 1 78  ? 19.309 22.287 13.285 1.000 26.10  ? 78  ILE A HD13 1 
ATOM   1443 N N    . PRO A 1 79  ? 19.927 27.319 11.230 1.000 8.90   ? 79  PRO A N    1 
ATOM   1444 C CA   . PRO A 1 79  ? 21.278 27.877 11.234 1.000 8.96   ? 79  PRO A CA   1 
ATOM   1445 C C    . PRO A 1 79  ? 22.206 26.929 11.961 1.000 8.12   ? 79  PRO A C    1 
ATOM   1446 O O    . PRO A 1 79  ? 21.840 26.328 12.976 1.000 8.84   ? 79  PRO A O    1 
ATOM   1447 C CB   . PRO A 1 79  ? 21.089 29.202 12.012 1.000 11.46  ? 79  PRO A CB   1 
ATOM   1448 C CG   . PRO A 1 79  ? 19.917 29.006 12.887 1.000 13.84  ? 79  PRO A CG   1 
ATOM   1449 C CD   . PRO A 1 79  ? 19.010 28.061 12.101 1.000 10.90  ? 79  PRO A CD   1 
ATOM   1450 H HA   . PRO A 1 79  ? 21.592 28.046 10.321 1.000 10.75  ? 79  PRO A HA   1 
ATOM   1451 H HB2  . PRO A 1 79  ? 21.878 29.400 12.540 1.000 13.75  ? 79  PRO A HB2  1 
ATOM   1452 H HB3  . PRO A 1 79  ? 20.935 29.937 11.397 1.000 13.75  ? 79  PRO A HB3  1 
ATOM   1453 H HG2  . PRO A 1 79  ? 20.180 28.610 13.732 1.000 16.61  ? 79  PRO A HG2  1 
ATOM   1454 H HG3  . PRO A 1 79  ? 19.470 29.849 13.060 1.000 16.61  ? 79  PRO A HG3  1 
ATOM   1455 H HD2  . PRO A 1 79  ? 18.538 27.459 12.697 1.000 13.08  ? 79  PRO A HD2  1 
ATOM   1456 H HD3  . PRO A 1 79  ? 18.362 28.558 11.578 1.000 13.08  ? 79  PRO A HD3  1 
ATOM   1457 N N    . CYS A 1 80  ? 23.439 26.819 11.477 1.000 8.07   ? 80  CYS A N    1 
ATOM   1458 C CA   . CYS A 1 80  ? 24.379 25.927 12.136 1.000 7.94   ? 80  CYS A CA   1 
ATOM   1459 C C    . CYS A 1 80  ? 24.660 26.348 13.576 1.000 7.76   ? 80  CYS A C    1 
ATOM   1460 O O    . CYS A 1 80  ? 24.979 25.493 14.404 1.000 8.95   ? 80  CYS A O    1 
ATOM   1461 C CB   . CYS A 1 80  ? 25.698 25.825 11.376 1.000 8.37   ? 80  CYS A CB   1 
ATOM   1462 S SG   . CYS A 1 80  ? 25.540 25.145 9.692  1.000 8.53   ? 80  CYS A SG   1 
ATOM   1463 H H    . CYS A 1 80  ? 23.678 27.270 10.785 1.000 9.68   ? 80  CYS A H    1 
ATOM   1464 H HA   . CYS A 1 80  ? 23.977 25.034 12.159 1.000 9.53   ? 80  CYS A HA   1 
ATOM   1465 H HB2  . CYS A 1 80  ? 26.093 26.708 11.319 1.000 10.04  ? 80  CYS A HB2  1 
ATOM   1466 H HB3  . CYS A 1 80  ? 26.306 25.263 11.883 1.000 10.04  ? 80  CYS A HB3  1 
ATOM   1467 N N    . SER A 1 81  ? 24.556 27.635 13.889 1.000 8.08   ? 81  SER A N    1 
ATOM   1468 C CA   . SER A 1 81  ? 24.777 28.067 15.243 1.000 8.99   ? 81  SER A CA   1 
ATOM   1469 C C    . SER A 1 81  ? 23.825 27.420 16.241 1.000 8.30   ? 81  SER A C    1 
ATOM   1470 O O    . SER A 1 81  ? 24.166 27.306 17.426 1.000 10.20  ? 81  SER A O    1 
ATOM   1471 C CB   . SER A 1 81  ? 24.679 29.579 15.325 1.000 11.63  ? 81  SER A CB   1 
ATOM   1472 O OG   . SER A 1 81  ? 23.419 30.022 14.977 1.000 14.40  ? 81  SER A OG   1 
ATOM   1473 H H    . SER A 1 81  ? 24.357 28.210 13.282 1.000 9.70   ? 81  SER A H    1 
ATOM   1474 H HA   . SER A 1 81  ? 25.690 27.813 15.493 1.000 10.79  ? 81  SER A HA   1 
ATOM   1475 H HB2  . SER A 1 81  ? 24.882 29.865 16.229 1.000 13.96  ? 81  SER A HB2  1 
ATOM   1476 H HB3  . SER A 1 81  ? 25.335 29.976 14.731 1.000 13.96  ? 81  SER A HB3  1 
ATOM   1477 H HG   . SER A 1 81  ? 22.864 29.694 15.483 1.000 21.60  ? 81  SER A HG   1 
ATOM   1478 N N    . ALA A 1 82  ? 22.652 26.989 15.809 1.000 8.37   ? 82  ALA A N    1 
ATOM   1479 C CA   . ALA A 1 82  ? 21.718 26.303 16.704 1.000 8.93   ? 82  ALA A CA   1 
ATOM   1480 C C    . ALA A 1 82  ? 22.288 24.997 17.195 1.000 8.51   ? 82  ALA A C    1 
ATOM   1481 O O    . ALA A 1 82  ? 21.882 24.483 18.243 1.000 10.96  ? 82  ALA A O    1 
ATOM   1482 C CB   . ALA A 1 82  ? 20.389 26.060 15.999 1.000 10.68  ? 82  ALA A CB   1 
ATOM   1483 H H    . ALA A 1 82  ? 22.434 27.113 14.987 1.000 10.04  ? 82  ALA A H    1 
ATOM   1484 H HA   . ALA A 1 82  ? 21.555 26.879 17.480 1.000 10.72  ? 82  ALA A HA   1 
ATOM   1485 H HB1  . ALA A 1 82  ? 19.787 25.611 16.596 1.000 16.02  ? 82  ALA A HB1  1 
ATOM   1486 H HB2  . ALA A 1 82  ? 20.009 26.901 15.734 1.000 16.02  ? 82  ALA A HB2  1 
ATOM   1487 H HB3  . ALA A 1 82  ? 20.534 25.516 15.221 1.000 16.02  ? 82  ALA A HB3  1 
ATOM   1488 N N    . LEU A 1 83  ? 23.238 24.432 16.461 1.000 8.31   ? 83  LEU A N    1 
ATOM   1489 C CA   . LEU A 1 83  ? 23.880 23.161 16.812 1.000 8.96   ? 83  LEU A CA   1 
ATOM   1490 C C    . LEU A 1 83  ? 24.982 23.329 17.856 1.000 10.04  ? 83  LEU A C    1 
ATOM   1491 O O    . LEU A 1 83  ? 25.567 22.331 18.238 1.000 13.25  ? 83  LEU A O    1 
ATOM   1492 C CB   . LEU A 1 83  ? 24.418 22.508 15.585 1.000 9.71   ? 83  LEU A CB   1 
ATOM   1493 C CG   . LEU A 1 83  ? 23.407 22.169 14.502 1.000 10.68  ? 83  LEU A CG   1 
ATOM   1494 C CD1  . LEU A 1 83  ? 24.120 21.643 13.263 1.000 15.12  ? 83  LEU A CD1  1 
ATOM   1495 C CD2  . LEU A 1 83  ? 22.398 21.181 14.992 1.000 15.96  ? 83  LEU A CD2  1 
ATOM   1496 H H    . LEU A 1 83  ? 23.490 24.832 15.742 1.000 9.97   ? 83  LEU A H    1 
ATOM   1497 H HA   . LEU A 1 83  ? 23.194 22.572 17.191 1.000 10.76  ? 83  LEU A HA   1 
ATOM   1498 H HB2  . LEU A 1 83  ? 25.090 23.092 15.201 1.000 11.65  ? 83  LEU A HB2  1 
ATOM   1499 H HB3  . LEU A 1 83  ? 24.865 21.688 15.850 1.000 11.65  ? 83  LEU A HB3  1 
ATOM   1500 H HG   . LEU A 1 83  ? 22.935 22.992 14.257 1.000 12.82  ? 83  LEU A HG   1 
ATOM   1501 H HD11 . LEU A 1 83  ? 24.762 22.290 12.964 1.000 22.67  ? 83  LEU A HD11 1 
ATOM   1502 H HD12 . LEU A 1 83  ? 24.569 20.821 13.477 1.000 22.67  ? 83  LEU A HD12 1 
ATOM   1503 H HD13 . LEU A 1 83  ? 23.477 21.484 12.567 1.000 22.67  ? 83  LEU A HD13 1 
ATOM   1504 H HD21 . LEU A 1 83  ? 21.773 20.986 14.290 1.000 23.93  ? 83  LEU A HD21 1 
ATOM   1505 H HD22 . LEU A 1 83  ? 22.844 20.373 15.258 1.000 23.93  ? 83  LEU A HD22 1 
ATOM   1506 H HD23 . LEU A 1 83  ? 21.929 21.550 15.745 1.000 23.93  ? 83  LEU A HD23 1 
ATOM   1507 N N    . LEU A 1 84  ? 25.277 24.552 18.265 1.000 9.24   ? 84  LEU A N    1 
ATOM   1508 C CA   . LEU A 1 84  ? 26.310 24.860 19.241 1.000 9.87   ? 84  LEU A CA   1 
ATOM   1509 C C    . LEU A 1 84  ? 25.720 25.264 20.571 1.000 11.38  ? 84  LEU A C    1 
ATOM   1510 O O    . LEU A 1 84  ? 26.446 25.724 21.442 1.000 16.55  ? 84  LEU A O    1 
ATOM   1511 C CB   . LEU A 1 84  ? 27.247 25.953 18.727 1.000 9.79   ? 84  LEU A CB   1 
ATOM   1512 C CG   . LEU A 1 84  ? 28.000 25.594 17.440 1.000 10.26  ? 84  LEU A CG   1 
ATOM   1513 C CD1  . LEU A 1 84  ? 28.821 26.810 16.997 1.000 14.02  ? 84  LEU A CD1  1 
ATOM   1514 C CD2  . LEU A 1 84  ? 28.883 24.407 17.594 1.000 14.41  ? 84  LEU A CD2  1 
ATOM   1515 H H    . LEU A 1 84  ? 24.829 25.207 17.932 1.000 11.09  ? 84  LEU A H    1 
ATOM   1516 H HA   . LEU A 1 84  ? 26.842 24.050 19.382 1.000 11.84  ? 84  LEU A HA   1 
ATOM   1517 H HB2  . LEU A 1 84  ? 26.728 26.757 18.568 1.000 11.75  ? 84  LEU A HB2  1 
ATOM   1518 H HB3  . LEU A 1 84  ? 27.896 26.156 19.419 1.000 11.75  ? 84  LEU A HB3  1 
ATOM   1519 H HG   . LEU A 1 84  ? 27.340 25.398 16.743 1.000 12.31  ? 84  LEU A HG   1 
ATOM   1520 H HD11 . LEU A 1 84  ? 28.241 27.569 16.901 1.000 21.03  ? 84  LEU A HD11 1 
ATOM   1521 H HD12 . LEU A 1 84  ? 29.492 27.000 17.656 1.000 21.03  ? 84  LEU A HD12 1 
ATOM   1522 H HD13 . LEU A 1 84  ? 29.243 26.621 16.155 1.000 21.03  ? 84  LEU A HD13 1 
ATOM   1523 H HD21 . LEU A 1 84  ? 28.360 23.652 17.872 1.000 21.61  ? 84  LEU A HD21 1 
ATOM   1524 H HD22 . LEU A 1 84  ? 29.306 24.212 16.754 1.000 21.61  ? 84  LEU A HD22 1 
ATOM   1525 H HD23 . LEU A 1 84  ? 29.555 24.592 18.254 1.000 21.61  ? 84  LEU A HD23 1 
ATOM   1526 N N    A SER A 1 85  ? 24.580 24.791 20.995 0.436 15.17  ? 85  SER A N    1 
ATOM   1527 N N    B SER A 1 85  ? 24.431 25.133 20.700 0.564 13.02  ? 85  SER A N    1 
ATOM   1528 C CA   A SER A 1 85  ? 23.881 25.028 22.238 0.436 13.85  ? 85  SER A CA   1 
ATOM   1529 C CA   B SER A 1 85  ? 23.783 25.381 21.966 0.564 13.47  ? 85  SER A CA   1 
ATOM   1530 C C    A SER A 1 85  ? 24.241 24.029 23.347 0.436 12.89  ? 85  SER A C    1 
ATOM   1531 C C    B SER A 1 85  ? 24.142 24.346 23.020 0.564 10.91  ? 85  SER A C    1 
ATOM   1532 O O    A SER A 1 85  ? 24.419 22.864 23.068 0.436 12.50  ? 85  SER A O    1 
ATOM   1533 O O    B SER A 1 85  ? 24.633 23.273 22.726 0.564 12.20  ? 85  SER A O    1 
ATOM   1534 C CB   A SER A 1 85  ? 22.361 24.974 22.035 0.436 13.58  ? 85  SER A CB   1 
ATOM   1535 C CB   B SER A 1 85  ? 22.262 25.308 21.709 0.564 14.03  ? 85  SER A CB   1 
ATOM   1536 O OG   A SER A 1 85  ? 21.738 23.962 21.297 0.436 15.07  ? 85  SER A OG   1 
ATOM   1537 O OG   B SER A 1 85  ? 21.758 25.409 23.015 0.564 17.38  ? 85  SER A OG   1 
ATOM   1538 H H    A SER A 1 85  ? 24.183 24.256 20.451 0.436 18.20  ? 85  SER A H    1 
ATOM   1539 H H    B SER A 1 85  ? 23.959 24.895 20.022 0.564 15.62  ? 85  SER A H    1 
ATOM   1540 H HA   A SER A 1 85  ? 24.114 25.927 22.551 0.436 16.61  ? 85  SER A HA   1 
ATOM   1541 H HA   B SER A 1 85  ? 24.021 26.276 22.288 0.564 16.17  ? 85  SER A HA   1 
ATOM   1542 H HB2  A SER A 1 85  ? 21.962 24.961 22.919 0.436 16.29  ? 85  SER A HB2  1 
ATOM   1543 H HB2  B SER A 1 85  ? 21.959 26.044 21.154 0.564 16.83  ? 85  SER A HB2  1 
ATOM   1544 H HB3  A SER A 1 85  ? 22.104 25.815 21.627 0.436 16.29  ? 85  SER A HB3  1 
ATOM   1545 H HB3  B SER A 1 85  ? 22.011 24.468 21.295 0.564 16.83  ? 85  SER A HB3  1 
ATOM   1546 H HG   A SER A 1 85  ? 21.860 23.240 21.666 0.436 22.61  ? 85  SER A HG   1 
ATOM   1547 H HG   B SER A 1 85  ? 21.933 26.150 23.319 0.564 26.07  ? 85  SER A HG   1 
ATOM   1548 N N    A SER A 1 86  ? 24.242 24.526 24.585 0.590 14.05  ? 86  SER A N    1 
ATOM   1549 N N    B SER A 1 86  ? 23.810 24.660 24.290 0.410 10.57  ? 86  SER A N    1 
ATOM   1550 C CA   A SER A 1 86  ? 24.235 23.562 25.680 0.590 15.61  ? 86  SER A CA   1 
ATOM   1551 C CA   B SER A 1 86  ? 24.156 23.727 25.354 0.410 12.52  ? 86  SER A CA   1 
ATOM   1552 C C    A SER A 1 86  ? 23.011 22.644 25.693 0.590 14.41  ? 86  SER A C    1 
ATOM   1553 C C    B SER A 1 86  ? 23.123 22.634 25.591 0.410 11.20  ? 86  SER A C    1 
ATOM   1554 O O    A SER A 1 86  ? 23.063 21.605 26.310 0.590 17.31  ? 86  SER A O    1 
ATOM   1555 O O    B SER A 1 86  ? 23.501 21.552 25.984 0.410 14.66  ? 86  SER A O    1 
ATOM   1556 C CB   A SER A 1 86  ? 24.303 24.264 27.048 0.590 21.66  ? 86  SER A CB   1 
ATOM   1557 C CB   B SER A 1 86  ? 24.354 24.512 26.653 0.410 16.21  ? 86  SER A CB   1 
ATOM   1558 O OG   A SER A 1 86  ? 23.179 25.112 27.185 0.590 30.42  ? 86  SER A OG   1 
ATOM   1559 O OG   B SER A 1 86  ? 25.653 25.061 26.700 0.410 26.23  ? 86  SER A OG   1 
ATOM   1560 H H    A SER A 1 86  ? 24.246 25.374 24.730 0.590 16.86  ? 86  SER A H    1 
ATOM   1561 H H    B SER A 1 86  ? 23.403 25.396 24.467 0.410 12.69  ? 86  SER A H    1 
ATOM   1562 H HA   A SER A 1 86  ? 25.032 22.999 25.590 0.590 18.73  ? 86  SER A HA   1 
ATOM   1563 H HA   B SER A 1 86  ? 25.007 23.299 25.122 0.410 15.02  ? 86  SER A HA   1 
ATOM   1564 H HB2  A SER A 1 86  ? 24.307 23.604 27.759 0.590 25.99  ? 86  SER A HB2  1 
ATOM   1565 H HB2  B SER A 1 86  ? 23.698 25.225 26.706 0.410 19.45  ? 86  SER A HB2  1 
ATOM   1566 H HB3  A SER A 1 86  ? 25.119 24.785 27.112 0.590 25.99  ? 86  SER A HB3  1 
ATOM   1567 H HB3  B SER A 1 86  ? 24.222 23.924 27.413 0.410 19.45  ? 86  SER A HB3  1 
ATOM   1568 H HG   A SER A 1 86  ? 23.171 25.657 26.572 0.590 45.62  ? 86  SER A HG   1 
ATOM   1569 H HG   B SER A 1 86  ? 25.791 25.494 26.018 0.410 39.34  ? 86  SER A HG   1 
ATOM   1570 N N    A ASP A 1 87  ? 21.927 23.016 25.034 0.686 12.39  ? 87  ASP A N    1 
ATOM   1571 N N    B ASP A 1 87  ? 21.852 22.926 25.353 0.314 10.68  ? 87  ASP A N    1 
ATOM   1572 C CA   A ASP A 1 87  ? 20.727 22.196 24.927 0.686 12.74  ? 87  ASP A CA   1 
ATOM   1573 C CA   B ASP A 1 87  ? 20.862 21.876 25.188 0.314 10.95  ? 87  ASP A CA   1 
ATOM   1574 C C    A ASP A 1 87  ? 20.905 21.310 23.671 0.686 12.19  ? 87  ASP A C    1 
ATOM   1575 C C    B ASP A 1 87  ? 20.903 21.318 23.748 0.314 10.63  ? 87  ASP A C    1 
ATOM   1576 O O    A ASP A 1 87  ? 21.234 21.863 22.637 0.686 14.25  ? 87  ASP A O    1 
ATOM   1577 O O    B ASP A 1 87  ? 21.052 22.085 22.808 0.314 14.35  ? 87  ASP A O    1 
ATOM   1578 C CB   A ASP A 1 87  ? 19.490 23.091 24.861 0.686 15.18  ? 87  ASP A CB   1 
ATOM   1579 C CB   B ASP A 1 87  ? 19.443 22.365 25.406 0.314 11.63  ? 87  ASP A CB   1 
ATOM   1580 C CG   A ASP A 1 87  ? 18.255 22.189 24.943 0.686 19.84  ? 87  ASP A CG   1 
ATOM   1581 C CG   B ASP A 1 87  ? 18.990 23.226 24.244 0.314 11.83  ? 87  ASP A CG   1 
ATOM   1582 O OD1  A ASP A 1 87  ? 17.893 21.566 23.991 0.686 28.71  ? 87  ASP A OD1  1 
ATOM   1583 O OD1  B ASP A 1 87  ? 19.504 24.373 24.128 0.314 13.97  ? 87  ASP A OD1  1 
ATOM   1584 O OD2  A ASP A 1 87  ? 17.731 22.080 26.075 0.686 32.82  ? 87  ASP A OD2  1 
ATOM   1585 O OD2  B ASP A 1 87  ? 18.125 22.859 23.438 0.314 16.10  ? 87  ASP A OD2  1 
ATOM   1586 H H    A ASP A 1 87  ? 21.930 23.784 24.647 0.686 14.87  ? 87  ASP A H    1 
ATOM   1587 H H    B ASP A 1 87  ? 21.610 23.749 25.295 0.314 12.82  ? 87  ASP A H    1 
ATOM   1588 H HA   A ASP A 1 87  ? 20.662 21.620 25.717 0.686 15.29  ? 87  ASP A HA   1 
ATOM   1589 H HA   B ASP A 1 87  ? 21.054 21.152 25.819 0.314 13.14  ? 87  ASP A HA   1 
ATOM   1590 H HB2  A ASP A 1 87  ? 19.494 23.721 25.599 0.686 18.21  ? 87  ASP A HB2  1 
ATOM   1591 H HB2  B ASP A 1 87  ? 18.848 21.604 25.497 0.314 13.96  ? 87  ASP A HB2  1 
ATOM   1592 H HB3  A ASP A 1 87  ? 19.484 23.591 24.030 0.686 18.21  ? 87  ASP A HB3  1 
ATOM   1593 H HB3  B ASP A 1 87  ? 19.400 22.880 26.227 0.314 13.96  ? 87  ASP A HB3  1 
ATOM   1594 N N    . ILE A 1 88  ? 20.690 20.031 23.705 1.000 11.07  ? 88  ILE A N    1 
ATOM   1595 C CA   . ILE A 1 88  ? 20.976 19.172 22.549 1.000 10.22  ? 88  ILE A CA   1 
ATOM   1596 C C    . ILE A 1 88  ? 19.818 19.054 21.589 1.000 9.76   ? 88  ILE A C    1 
ATOM   1597 O O    . ILE A 1 88  ? 19.946 18.342 20.591 1.000 10.36  ? 88  ILE A O    1 
ATOM   1598 C CB   . ILE A 1 88  ? 21.459 17.753 22.971 1.000 11.91  ? 88  ILE A CB   1 
ATOM   1599 C CG1  . ILE A 1 88  ? 20.386 16.912 23.628 1.000 13.62  ? 88  ILE A CG1  1 
ATOM   1600 C CG2  . ILE A 1 88  ? 22.743 17.879 23.798 1.000 16.48  ? 88  ILE A CG2  1 
ATOM   1601 C CD1  . ILE A 1 88  ? 20.703 15.440 23.814 1.000 16.89  ? 88  ILE A CD1  1 
ATOM   1602 H H    A ILE A 1 88  ? 20.372 19.677 24.422 1.000 13.28  ? 88  ILE A H    1 
ATOM   1603 H HA   . ILE A 1 88  ? 21.714 19.591 22.058 1.000 12.26  ? 88  ILE A HA   1 
ATOM   1604 H HB   . ILE A 1 88  ? 21.707 17.289 22.145 1.000 14.30  ? 88  ILE A HB   1 
ATOM   1605 H HG12 . ILE A 1 88  ? 20.193 17.293 24.499 1.000 16.34  ? 88  ILE A HG12 1 
ATOM   1606 H HG13 . ILE A 1 88  ? 19.578 16.983 23.096 1.000 16.34  ? 88  ILE A HG13 1 
ATOM   1607 H HG21 . ILE A 1 88  ? 23.377 18.422 23.324 1.000 24.72  ? 88  ILE A HG21 1 
ATOM   1608 H HG22 . ILE A 1 88  ? 22.541 18.286 24.643 1.000 24.72  ? 88  ILE A HG22 1 
ATOM   1609 H HG23 . ILE A 1 88  ? 23.116 17.006 23.944 1.000 24.72  ? 88  ILE A HG23 1 
ATOM   1610 H HD11 . ILE A 1 88  ? 19.959 15.003 24.236 1.000 25.34  ? 88  ILE A HD11 1 
ATOM   1611 H HD12 . ILE A 1 88  ? 20.866 15.037 22.958 1.000 25.34  ? 88  ILE A HD12 1 
ATOM   1612 H HD13 . ILE A 1 88  ? 21.483 15.348 24.365 1.000 25.34  ? 88  ILE A HD13 1 
ATOM   1613 N N    A THR A 1 89  ? 18.693 19.676 21.813 0.678 10.59  ? 89  THR A N    1 
ATOM   1614 N N    B THR A 1 89  ? 18.722 19.772 21.848 0.322 11.85  ? 89  THR A N    1 
ATOM   1615 C CA   A THR A 1 89  ? 17.510 19.370 21.006 0.678 10.72  ? 89  THR A CA   1 
ATOM   1616 C CA   B THR A 1 89  ? 17.461 19.761 21.109 0.322 11.76  ? 89  THR A CA   1 
ATOM   1617 C C    A THR A 1 89  ? 17.724 19.633 19.521 0.678 10.30  ? 89  THR A C    1 
ATOM   1618 C C    B THR A 1 89  ? 17.714 19.705 19.605 0.322 9.93   ? 89  THR A C    1 
ATOM   1619 O O    A THR A 1 89  ? 17.300 18.832 18.676 0.678 10.88  ? 89  THR A O    1 
ATOM   1620 O O    B THR A 1 89  ? 17.337 18.774 18.891 0.322 9.75   ? 89  THR A O    1 
ATOM   1621 C CB   A THR A 1 89  ? 16.337 20.201 21.545 0.678 11.18  ? 89  THR A CB   1 
ATOM   1622 C CB   B THR A 1 89  ? 16.531 20.960 21.411 0.322 14.33  ? 89  THR A CB   1 
ATOM   1623 O OG1  A THR A 1 89  ? 16.113 19.897 22.921 0.678 13.08  ? 89  THR A OG1  1 
ATOM   1624 O OG1  B THR A 1 89  ? 16.135 20.891 22.784 0.322 16.75  ? 89  THR A OG1  1 
ATOM   1625 C CG2  A THR A 1 89  ? 15.046 19.926 20.777 0.678 14.14  ? 89  THR A CG2  1 
ATOM   1626 C CG2  B THR A 1 89  ? 15.258 20.892 20.589 0.322 18.67  ? 89  THR A CG2  1 
ATOM   1627 H H    A THR A 1 89  ? 18.646 20.266 22.437 0.678 12.71  ? 89  THR A H    1 
ATOM   1628 H H    B THR A 1 89  ? 18.763 20.300 22.526 0.322 14.22  ? 89  THR A H    1 
ATOM   1629 H HA   A THR A 1 89  ? 17.295 18.421 21.123 0.678 12.86  ? 89  THR A HA   1 
ATOM   1630 H HA   B THR A 1 89  ? 16.981 18.944 21.358 0.322 14.11  ? 89  THR A HA   1 
ATOM   1631 H HB   A THR A 1 89  ? 16.558 21.152 21.463 0.678 13.42  ? 89  THR A HB   1 
ATOM   1632 H HB   B THR A 1 89  ? 17.000 21.803 21.238 0.322 17.19  ? 89  THR A HB   1 
ATOM   1633 H HG1  A THR A 1 89  ? 16.790 20.062 23.352 0.678 19.63  ? 89  THR A HG1  1 
ATOM   1634 H HG1  B THR A 1 89  ? 16.794 20.978 23.263 0.322 20.11  ? 89  THR A HG1  1 
ATOM   1635 H HG21 A THR A 1 89  ? 15.177 20.125 19.848 0.678 21.21  ? 89  THR A HG21 1 
ATOM   1636 H HG21 B THR A 1 89  ? 15.478 20.935 19.655 0.322 28.00  ? 89  THR A HG21 1 
ATOM   1637 H HG22 A THR A 1 89  ? 14.806 19.001 20.876 0.678 21.21  ? 89  THR A HG22 1 
ATOM   1638 H HG22 B THR A 1 89  ? 14.803 20.067 20.772 0.322 28.00  ? 89  THR A HG22 1 
ATOM   1639 H HG23 A THR A 1 89  ? 14.342 20.478 21.126 0.678 21.21  ? 89  THR A HG23 1 
ATOM   1640 H HG23 B THR A 1 89  ? 14.689 21.630 20.818 0.322 28.00  ? 89  THR A HG23 1 
ATOM   1641 N N    . ALA A 1 90  ? 18.339 20.753 19.111 1.000 10.13  ? 90  ALA A N    1 
ATOM   1642 C CA   . ALA A 1 90  ? 18.501 20.982 17.682 1.000 9.79   ? 90  ALA A CA   1 
ATOM   1643 C C    . ALA A 1 90  ? 19.388 19.925 17.042 1.000 8.55   ? 90  ALA A C    1 
ATOM   1644 O O    . ALA A 1 90  ? 19.148 19.454 15.930 1.000 9.42   ? 90  ALA A O    1 
ATOM   1645 C CB   . ALA A 1 90  ? 19.042 22.366 17.401 1.000 12.49  ? 90  ALA A CB   1 
ATOM   1646 H H    A ALA A 1 90  ? 18.631 21.326 19.682 1.000 12.15  ? 90  ALA A H    1 
ATOM   1647 H HA   . ALA A 1 90  ? 17.615 20.919 17.268 1.000 11.75  ? 90  ALA A HA   1 
ATOM   1648 H HB1  . ALA A 1 90  ? 19.138 22.485 16.453 1.000 18.74  ? 90  ALA A HB1  1 
ATOM   1649 H HB2  . ALA A 1 90  ? 18.434 23.023 17.746 1.000 18.74  ? 90  ALA A HB2  1 
ATOM   1650 H HB3  . ALA A 1 90  ? 19.898 22.467 17.824 1.000 18.74  ? 90  ALA A HB3  1 
ATOM   1651 N N    . SER A 1 91  ? 20.465 19.537 17.734 1.000 8.24   ? 91  SER A N    1 
ATOM   1652 C CA   . SER A 1 91  ? 21.327 18.484 17.237 1.000 8.08   ? 91  SER A CA   1 
ATOM   1653 C C    . SER A 1 91  ? 20.595 17.158 17.109 1.000 8.09   ? 91  SER A C    1 
ATOM   1654 O O    . SER A 1 91  ? 20.778 16.447 16.129 1.000 9.30   ? 91  SER A O    1 
ATOM   1655 C CB   . SER A 1 91  ? 22.562 18.333 18.115 1.000 8.95   ? 91  SER A CB   1 
ATOM   1656 O OG   . SER A 1 91  ? 23.456 19.415 17.937 1.000 10.63  ? 91  SER A OG   1 
ATOM   1657 H H    . SER A 1 91  ? 20.649 19.918 18.482 1.000 9.89   ? 91  SER A H    1 
ATOM   1658 H HA   . SER A 1 91  ? 21.629 18.744 16.342 1.000 9.69   ? 91  SER A HA   1 
ATOM   1659 H HB2  . SER A 1 91  ? 22.291 18.290 19.046 1.000 10.73  ? 91  SER A HB2  1 
ATOM   1660 H HB3  . SER A 1 91  ? 23.013 17.503 17.896 1.000 10.73  ? 91  SER A HB3  1 
ATOM   1661 H HG   . SER A 1 91  ? 23.073 20.118 18.114 1.000 15.95  ? 91  SER A HG   1 
ATOM   1662 N N    . VAL A 1 92  ? 19.781 16.804 18.111 1.000 8.47   ? 92  VAL A N    1 
ATOM   1663 C CA   . VAL A 1 92  ? 19.022 15.581 18.033 1.000 9.20   ? 92  VAL A CA   1 
ATOM   1664 C C    . VAL A 1 92  ? 18.005 15.624 16.914 1.000 8.76   ? 92  VAL A C    1 
ATOM   1665 O O    . VAL A 1 92  ? 17.857 14.649 16.168 1.000 10.11  ? 92  VAL A O    1 
ATOM   1666 C CB   . VAL A 1 92  ? 18.328 15.267 19.387 1.000 12.37  ? 92  VAL A CB   1 
ATOM   1667 C CG1  . VAL A 1 92  ? 17.319 14.113 19.190 1.000 15.49  ? 92  VAL A CG1  1 
ATOM   1668 C CG2  . VAL A 1 92  ? 19.355 14.947 20.418 1.000 16.56  ? 92  VAL A CG2  1 
ATOM   1669 H H    . VAL A 1 92  ? 19.711 17.308 18.804 1.000 10.17  ? 92  VAL A H    1 
ATOM   1670 H HA   . VAL A 1 92  ? 19.648 14.852 17.841 1.000 11.04  ? 92  VAL A HA   1 
ATOM   1671 H HB   . VAL A 1 92  ? 17.836 16.064 19.676 1.000 14.84  ? 92  VAL A HB   1 
ATOM   1672 H HG11 . VAL A 1 92  ? 16.678 14.359 18.520 1.000 23.23  ? 92  VAL A HG11 1 
ATOM   1673 H HG12 . VAL A 1 92  ? 17.788 13.323 18.909 1.000 23.23  ? 92  VAL A HG12 1 
ATOM   1674 H HG13 . VAL A 1 92  ? 16.866 13.939 20.018 1.000 23.23  ? 92  VAL A HG13 1 
ATOM   1675 H HG21 . VAL A 1 92  ? 19.959 15.688 20.509 1.000 24.84  ? 92  VAL A HG21 1 
ATOM   1676 H HG22 . VAL A 1 92  ? 18.923 14.782 21.260 1.000 24.84  ? 92  VAL A HG22 1 
ATOM   1677 H HG23 . VAL A 1 92  ? 19.845 14.166 20.151 1.000 24.84  ? 92  VAL A HG23 1 
ATOM   1678 N N    . ASN A 1 93  ? 17.292 16.736 16.764 1.000 9.20   ? 93  ASN A N    1 
ATOM   1679 C CA   . ASN A 1 93  ? 16.292 16.832 15.694 1.000 10.17  ? 93  ASN A CA   1 
ATOM   1680 C C    . ASN A 1 93  ? 16.951 16.691 14.324 1.000 8.91   ? 93  ASN A C    1 
ATOM   1681 O O    . ASN A 1 93  ? 16.397 16.028 13.430 1.000 10.52  ? 93  ASN A O    1 
ATOM   1682 C CB   . ASN A 1 93  ? 15.520 18.146 15.795 1.000 12.71  ? 93  ASN A CB   1 
ATOM   1683 C CG   . ASN A 1 93  ? 14.563 18.243 16.916 1.000 15.40  ? 93  ASN A CG   1 
ATOM   1684 O OD1  . ASN A 1 93  ? 14.150 17.227 17.479 1.000 22.34  ? 93  ASN A OD1  1 
ATOM   1685 N ND2  . ASN A 1 93  ? 14.141 19.438 17.288 1.000 19.32  ? 93  ASN A ND2  1 
ATOM   1686 H H    . ASN A 1 93  ? 17.418 17.400 17.295 1.000 11.04  ? 93  ASN A H    1 
ATOM   1687 H HA   . ASN A 1 93  ? 15.656 16.095 15.804 1.000 12.21  ? 93  ASN A HA   1 
ATOM   1688 H HB2  . ASN A 1 93  ? 16.160 18.871 15.877 1.000 15.25  ? 93  ASN A HB2  1 
ATOM   1689 H HB3  . ASN A 1 93  ? 15.035 18.280 14.966 1.000 15.25  ? 93  ASN A HB3  1 
ATOM   1690 H HD21 . ASN A 1 93  ? 13.573 19.513 17.929 1.000 23.19  ? 93  ASN A HD21 1 
ATOM   1691 H HD22 . ASN A 1 93  ? 14.435 20.141 16.889 1.000 23.19  ? 93  ASN A HD22 1 
ATOM   1692 N N    . CYS A 1 94  ? 18.094 17.290 14.142 1.000 8.08   ? 94  CYS A N    1 
ATOM   1693 C CA   . CYS A 1 94  ? 18.780 17.184 12.867 1.000 7.94   ? 94  CYS A CA   1 
ATOM   1694 C C    . CYS A 1 94  ? 19.368 15.795 12.669 1.000 7.76   ? 94  CYS A C    1 
ATOM   1695 O O    . CYS A 1 94  ? 19.291 15.255 11.565 1.000 9.02   ? 94  CYS A O    1 
ATOM   1696 C CB   . CYS A 1 94  ? 19.802 18.320 12.739 1.000 8.33   ? 94  CYS A CB   1 
ATOM   1697 S SG   . CYS A 1 94  ? 20.646 18.415 11.150 1.000 8.52   ? 94  CYS A SG   1 
ATOM   1698 H H    . CYS A 1 94  ? 18.444 17.750 14.780 1.000 9.69   ? 94  CYS A H    1 
ATOM   1699 H HA   . CYS A 1 94  ? 18.109 17.317 12.165 1.000 9.53   ? 94  CYS A HA   1 
ATOM   1700 H HB2  . CYS A 1 94  ? 19.346 19.162 12.896 1.000 10.00  ? 94  CYS A HB2  1 
ATOM   1701 H HB3  . CYS A 1 94  ? 20.468 18.215 13.436 1.000 10.00  ? 94  CYS A HB3  1 
ATOM   1702 N N    . ALA A 1 95  ? 19.920 15.167 13.710 1.000 7.71   ? 95  ALA A N    1 
ATOM   1703 C CA   . ALA A 1 95  ? 20.397 13.827 13.600 1.000 8.43   ? 95  ALA A CA   1 
ATOM   1704 C C    . ALA A 1 95  ? 19.277 12.865 13.173 1.000 8.50   ? 95  ALA A C    1 
ATOM   1705 O O    . ALA A 1 95  ? 19.520 11.938 12.391 1.000 10.22  ? 95  ALA A O    1 
ATOM   1706 C CB   . ALA A 1 95  ? 20.994 13.364 14.909 1.000 10.46  ? 95  ALA A CB   1 
ATOM   1707 H H    . ALA A 1 95  ? 19.989 15.578 14.462 1.000 9.25   ? 95  ALA A H    1 
ATOM   1708 H HA   . ALA A 1 95  ? 21.099 13.805 12.916 1.000 10.11  ? 95  ALA A HA   1 
ATOM   1709 H HB1  . ALA A 1 95  ? 21.310 12.462 14.816 1.000 15.68  ? 95  ALA A HB1  1 
ATOM   1710 H HB2  . ALA A 1 95  ? 21.728 13.937 15.146 1.000 15.68  ? 95  ALA A HB2  1 
ATOM   1711 H HB3  . ALA A 1 95  ? 20.325 13.401 15.597 1.000 15.68  ? 95  ALA A HB3  1 
ATOM   1712 N N    . LYS A 1 96  ? 18.074 13.052 13.695 1.000 9.02   ? 96  LYS A N    1 
ATOM   1713 C CA   . LYS A 1 96  ? 16.940 12.211 13.280 1.000 9.72   ? 96  LYS A CA   1 
ATOM   1714 C C    . LYS A 1 96  ? 16.691 12.371 11.793 1.000 10.81  ? 96  LYS A C    1 
ATOM   1715 O O    . LYS A 1 96  ? 16.379 11.408 11.111 1.000 13.93  ? 96  LYS A O    1 
ATOM   1716 C CB   . LYS A 1 96  ? 15.690 12.563 14.086 1.000 11.10  ? 96  LYS A CB   1 
ATOM   1717 C CG   . LYS A 1 96  ? 15.729 12.082 15.524 1.000 11.25  ? 96  LYS A CG   1 
ATOM   1718 C CD   . LYS A 1 96  ? 14.515 12.560 16.297 1.000 14.29  ? 96  LYS A CD   1 
ATOM   1719 C CE   . LYS A 1 96  ? 14.425 12.024 17.668 1.000 16.47  ? 96  LYS A CE   1 
ATOM   1720 N NZ   . LYS A 1 96  ? 13.287 12.612 18.394 1.000 21.03  ? 96  LYS A NZ   1 
ATOM   1721 H H    . LYS A 1 96  ? 17.955 13.670 14.281 1.000 10.83  ? 96  LYS A H    1 
ATOM   1722 H HA   . LYS A 1 96  ? 17.169 11.275 13.457 1.000 11.67  ? 96  LYS A HA   1 
ATOM   1723 H HB2  . LYS A 1 96  ? 15.576 13.526 14.082 1.000 13.32  ? 96  LYS A HB2  1 
ATOM   1724 H HB3  . LYS A 1 96  ? 14.917 12.174 13.648 1.000 13.32  ? 96  LYS A HB3  1 
ATOM   1725 H HG2  . LYS A 1 96  ? 15.758 11.112 15.539 1.000 13.50  ? 96  LYS A HG2  1 
ATOM   1726 H HG3  . LYS A 1 96  ? 16.534 12.412 15.953 1.000 13.50  ? 96  LYS A HG3  1 
ATOM   1727 H HD2  . LYS A 1 96  ? 14.536 13.529 16.342 1.000 17.15  ? 96  LYS A HD2  1 
ATOM   1728 H HD3  . LYS A 1 96  ? 13.715 12.306 15.811 1.000 17.15  ? 96  LYS A HD3  1 
ATOM   1729 H HE2  . LYS A 1 96  ? 14.321 11.061 17.631 1.000 19.77  ? 96  LYS A HE2  1 
ATOM   1730 H HE3  . LYS A 1 96  ? 15.247 12.219 18.145 1.000 19.77  ? 96  LYS A HE3  1 
ATOM   1731 H HZ1  . LYS A 1 96  ? 13.253 12.274 19.216 1.000 31.55  ? 96  LYS A HZ1  1 
ATOM   1732 H HZ2  . LYS A 1 96  ? 13.388 13.495 18.440 1.000 31.55  ? 96  LYS A HZ2  1 
ATOM   1733 H HZ3  . LYS A 1 96  ? 12.531 12.422 17.964 1.000 31.55  ? 96  LYS A HZ3  1 
ATOM   1734 N N    A LYS A 1 97  ? 16.754 13.655 11.353 0.535 9.89   ? 97  LYS A N    1 
ATOM   1735 N N    B LYS A 1 97  ? 16.860 13.519 11.170 0.465 10.84  ? 97  LYS A N    1 
ATOM   1736 C CA   A LYS A 1 97  ? 16.505 14.023 9.943  0.535 9.07   ? 97  LYS A CA   1 
ATOM   1737 C CA   B LYS A 1 97  ? 16.807 13.568 9.707  0.465 12.97  ? 97  LYS A CA   1 
ATOM   1738 C C    A LYS A 1 97  ? 17.553 13.364 9.039  0.535 8.91   ? 97  LYS A C    1 
ATOM   1739 C C    B LYS A 1 97  ? 17.962 12.863 9.026  0.465 12.27  ? 97  LYS A C    1 
ATOM   1740 O O    A LYS A 1 97  ? 17.237 12.885 7.936  0.535 11.15  ? 97  LYS A O    1 
ATOM   1741 O O    B LYS A 1 97  ? 17.749 12.133 8.034  0.465 15.43  ? 97  LYS A O    1 
ATOM   1742 C CB   A LYS A 1 97  ? 16.439 15.521 9.720  0.535 10.22  ? 97  LYS A CB   1 
ATOM   1743 C CB   B LYS A 1 97  ? 16.789 15.053 9.334  0.465 14.81  ? 97  LYS A CB   1 
ATOM   1744 C CG   A LYS A 1 97  ? 16.390 16.025 8.292  0.535 13.89  ? 97  LYS A CG   1 
ATOM   1745 C CG   B LYS A 1 97  ? 16.548 15.394 7.883  0.465 20.73  ? 97  LYS A CG   1 
ATOM   1746 C CD   A LYS A 1 97  ? 15.151 15.692 7.578  0.535 20.51  ? 97  LYS A CD   1 
ATOM   1747 C CD   B LYS A 1 97  ? 15.544 14.580 7.144  0.465 30.37  ? 97  LYS A CD   1 
ATOM   1748 C CE   A LYS A 1 97  ? 14.922 16.431 6.298  0.535 26.71  ? 97  LYS A CE   1 
ATOM   1749 C CE   B LYS A 1 97  ? 14.830 15.344 6.037  0.465 29.46  ? 97  LYS A CE   1 
ATOM   1750 N NZ   A LYS A 1 97  ? 14.181 15.607 5.305  0.535 31.46  ? 97  LYS A NZ   1 
ATOM   1751 N NZ   B LYS A 1 97  ? 15.599 16.564 5.646  0.465 45.97  ? 97  LYS A NZ   1 
ATOM   1752 H H    A LYS A 1 97  ? 16.947 14.276 11.915 0.535 11.87  ? 97  LYS A H    1 
ATOM   1753 H H    B LYS A 1 97  ? 17.002 14.238 11.620 0.465 13.01  ? 97  LYS A H    1 
ATOM   1754 H HA   A LYS A 1 97  ? 15.632 13.653 9.695  0.535 10.89  ? 97  LYS A HA   1 
ATOM   1755 H HA   B LYS A 1 97  ? 15.968 13.158 9.409  0.465 15.57  ? 97  LYS A HA   1 
ATOM   1756 H HB2  A LYS A 1 97  ? 15.653 15.855 10.180 0.535 12.27  ? 97  LYS A HB2  1 
ATOM   1757 H HB2  B LYS A 1 97  ? 16.101 15.487 9.863  0.465 17.77  ? 97  LYS A HB2  1 
ATOM   1758 H HB3  A LYS A 1 97  ? 17.212 15.919 10.150 0.535 12.27  ? 97  LYS A HB3  1 
ATOM   1759 H HB3  B LYS A 1 97  ? 17.640 15.439 9.596  0.465 17.77  ? 97  LYS A HB3  1 
ATOM   1760 H HG2  A LYS A 1 97  ? 16.496 16.989 8.298  0.535 16.67  ? 97  LYS A HG2  1 
ATOM   1761 H HG2  B LYS A 1 97  ? 16.272 16.322 7.836  0.465 24.87  ? 97  LYS A HG2  1 
ATOM   1762 H HG3  A LYS A 1 97  ? 17.141 15.650 7.804  0.535 16.67  ? 97  LYS A HG3  1 
ATOM   1763 H HG3  B LYS A 1 97  ? 17.394 15.321 7.415  0.465 24.87  ? 97  LYS A HG3  1 
ATOM   1764 H HD2  A LYS A 1 97  ? 15.156 14.741 7.385  0.535 24.61  ? 97  LYS A HD2  1 
ATOM   1765 H HD2  B LYS A 1 97  ? 15.990 13.811 6.756  0.465 36.45  ? 97  LYS A HD2  1 
ATOM   1766 H HD3  A LYS A 1 97  ? 14.402 15.865 8.169  0.535 24.61  ? 97  LYS A HD3  1 
ATOM   1767 H HD3  B LYS A 1 97  ? 14.883 14.251 7.774  0.465 36.45  ? 97  LYS A HD3  1 
ATOM   1768 H HE2  A LYS A 1 97  ? 14.418 17.239 6.482  0.535 32.06  ? 97  LYS A HE2  1 
ATOM   1769 H HE2  B LYS A 1 97  ? 14.723 14.768 5.264  0.465 35.35  ? 97  LYS A HE2  1 
ATOM   1770 H HE3  A LYS A 1 97  ? 15.777 16.692 5.922  0.535 32.06  ? 97  LYS A HE3  1 
ATOM   1771 H HE3  B LYS A 1 97  ? 13.946 15.604 6.342  0.465 35.35  ? 97  LYS A HE3  1 
ATOM   1772 H HZ1  A LYS A 1 97  ? 14.063 16.078 4.559  0.535 47.18  ? 97  LYS A HZ1  1 
ATOM   1773 H HZ1  B LYS A 1 97  ? 15.165 16.994 4.999  0.465 68.96  ? 97  LYS A HZ1  1 
ATOM   1774 H HZ2  A LYS A 1 97  ? 14.648 14.872 5.122  0.535 47.18  ? 97  LYS A HZ2  1 
ATOM   1775 H HZ2  B LYS A 1 97  ? 15.686 17.099 6.352  0.465 68.96  ? 97  LYS A HZ2  1 
ATOM   1776 H HZ3  A LYS A 1 97  ? 13.389 15.380 5.641  0.535 47.18  ? 97  LYS A HZ3  1 
ATOM   1777 H HZ3  B LYS A 1 97  ? 16.406 16.325 5.354  0.465 68.96  ? 97  LYS A HZ3  1 
ATOM   1778 N N    A ILE A 1 98  ? 18.794 13.334 9.459  0.535 8.59   ? 98  ILE A N    1 
ATOM   1779 N N    B ILE A 1 98  ? 19.186 13.051 9.500  0.465 10.78  ? 98  ILE A N    1 
ATOM   1780 C CA   A ILE A 1 98  ? 19.835 12.724 8.676  0.535 8.47   ? 98  ILE A CA   1 
ATOM   1781 C CA   B ILE A 1 98  ? 20.363 12.482 8.893  0.465 11.09  ? 98  ILE A CA   1 
ATOM   1782 C C    A ILE A 1 98  ? 19.489 11.273 8.429  0.535 9.27   ? 98  ILE A C    1 
ATOM   1783 C C    B ILE A 1 98  ? 20.246 10.965 8.860  0.465 12.01  ? 98  ILE A C    1 
ATOM   1784 O O    A ILE A 1 98  ? 19.556 10.761 7.297  0.535 11.82  ? 98  ILE A O    1 
ATOM   1785 O O    B ILE A 1 98  ? 20.481 10.372 7.794  0.465 14.35  ? 98  ILE A O    1 
ATOM   1786 C CB   A ILE A 1 98  ? 21.210 12.892 9.384  0.535 8.69   ? 98  ILE A CB   1 
ATOM   1787 C CB   B ILE A 1 98  ? 21.646 12.927 9.621  0.465 10.95  ? 98  ILE A CB   1 
ATOM   1788 C CG1  A ILE A 1 98  ? 21.606 14.368 9.398  0.535 8.93   ? 98  ILE A CG1  1 
ATOM   1789 C CG1  B ILE A 1 98  ? 21.904 14.424 9.399  0.465 12.40  ? 98  ILE A CG1  1 
ATOM   1790 C CG2  A ILE A 1 98  ? 22.234 11.973 8.780  0.535 11.14  ? 98  ILE A CG2  1 
ATOM   1791 C CG2  B ILE A 1 98  ? 22.850 12.123 9.210  0.465 12.98  ? 98  ILE A CG2  1 
ATOM   1792 C CD1  A ILE A 1 98  ? 22.897 14.673 10.085 0.535 11.62  ? 98  ILE A CD1  1 
ATOM   1793 C CD1  B ILE A 1 98  ? 22.786 15.012 10.467 0.465 11.55  ? 98  ILE A CD1  1 
ATOM   1794 H H    A ILE A 1 98  ? 18.990 13.686 10.218 0.535 10.30  ? 98  ILE A H    1 
ATOM   1795 H H    B ILE A 1 98  ? 19.282 13.535 10.204 0.465 12.94  ? 98  ILE A H    1 
ATOM   1796 H HA   A ILE A 1 98  ? 19.877 13.182 7.810  0.535 10.16  ? 98  ILE A HA   1 
ATOM   1797 H HA   B ILE A 1 98  ? 20.413 12.803 7.968  0.465 13.31  ? 98  ILE A HA   1 
ATOM   1798 H HB   A ILE A 1 98  ? 21.089 12.617 10.317 0.535 10.43  ? 98  ILE A HB   1 
ATOM   1799 H HB   B ILE A 1 98  ? 21.508 12.788 10.581 0.465 13.14  ? 98  ILE A HB   1 
ATOM   1800 H HG12 A ILE A 1 98  ? 21.664 14.679 8.481  0.535 10.72  ? 98  ILE A HG12 1 
ATOM   1801 H HG12 B ILE A 1 98  ? 22.324 14.550 8.534  0.465 14.89  ? 98  ILE A HG12 1 
ATOM   1802 H HG13 A ILE A 1 98  ? 20.900 14.872 9.833  0.535 10.72  ? 98  ILE A HG13 1 
ATOM   1803 H HG13 B ILE A 1 98  ? 21.056 14.895 9.390  0.465 14.89  ? 98  ILE A HG13 1 
ATOM   1804 H HG21 A ILE A 1 98  ? 21.910 11.070 8.809  0.535 16.72  ? 98  ILE A HG21 1 
ATOM   1805 H HG21 B ILE A 1 98  ? 22.676 11.190 9.354  0.465 19.47  ? 98  ILE A HG21 1 
ATOM   1806 H HG22 A ILE A 1 98  ? 22.393 12.227 7.868  0.535 16.72  ? 98  ILE A HG22 1 
ATOM   1807 H HG22 B ILE A 1 98  ? 23.034 12.274 8.280  0.465 19.47  ? 98  ILE A HG22 1 
ATOM   1808 H HG23 A ILE A 1 98  ? 23.053 12.036 9.276  0.535 16.72  ? 98  ILE A HG23 1 
ATOM   1809 H HG23 B ILE A 1 98  ? 23.609 12.391 9.733  0.465 19.47  ? 98  ILE A HG23 1 
ATOM   1810 H HD11 A ILE A 1 98  ? 23.065 15.617 10.046 0.535 17.43  ? 98  ILE A HD11 1 
ATOM   1811 H HD11 B ILE A 1 98  ? 22.922 15.946 10.291 0.465 17.32  ? 98  ILE A HD11 1 
ATOM   1812 H HD12 A ILE A 1 98  ? 22.844 14.395 11.002 0.535 17.43  ? 98  ILE A HD12 1 
ATOM   1813 H HD12 B ILE A 1 98  ? 22.366 14.905 11.323 0.465 17.32  ? 98  ILE A HD12 1 
ATOM   1814 H HD13 A ILE A 1 98  ? 23.610 14.202 9.648  0.535 17.43  ? 98  ILE A HD13 1 
ATOM   1815 H HD13 B ILE A 1 98  ? 23.633 14.560 10.467 0.465 17.32  ? 98  ILE A HD13 1 
ATOM   1816 N N    A VAL A 1 99  ? 19.079 10.546 9.483  0.535 9.37   ? 99  VAL A N    1 
ATOM   1817 N N    B VAL A 1 99  ? 19.879 10.320 9.976  0.465 11.93  ? 99  VAL A N    1 
ATOM   1818 C CA   A VAL A 1 99  ? 18.703 9.143  9.296  0.535 11.99  ? 99  VAL A CA   1 
ATOM   1819 C CA   B VAL A 1 99  ? 19.886 8.888  9.946  0.465 15.03  ? 99  VAL A CA   1 
ATOM   1820 C C    A VAL A 1 99  ? 17.443 9.015  8.451  0.535 14.32  ? 99  VAL A C    1 
ATOM   1821 C C    B VAL A 1 99  ? 18.727 8.339  9.088  0.465 17.61  ? 99  VAL A C    1 
ATOM   1822 O O    A VAL A 1 99  ? 17.307 8.184  7.546  0.535 19.35  ? 99  VAL A O    1 
ATOM   1823 O O    B VAL A 1 99  ? 18.889 7.186  8.705  0.465 27.10  ? 99  VAL A O    1 
ATOM   1824 C CB   A VAL A 1 99  ? 18.600 8.536  10.681 0.535 14.23  ? 99  VAL A CB   1 
ATOM   1825 C CB   B VAL A 1 99  ? 19.632 8.117  11.243 0.465 18.86  ? 99  VAL A CB   1 
ATOM   1826 C CG1  A VAL A 1 99  ? 18.153 7.089  10.570 0.535 18.99  ? 99  VAL A CG1  1 
ATOM   1827 C CG1  B VAL A 1 99  ? 20.866 7.765  12.013 0.465 30.67  ? 99  VAL A CG1  1 
ATOM   1828 C CG2  A VAL A 1 99  ? 19.923 8.573  11.452 0.535 13.95  ? 99  VAL A CG2  1 
ATOM   1829 C CG2  B VAL A 1 99  ? 18.630 8.820  12.106 0.465 20.30  ? 99  VAL A CG2  1 
ATOM   1830 H H    A VAL A 1 99  ? 19.039 10.903 10.265 0.535 11.25  ? 99  VAL A H    1 
ATOM   1831 H H    B VAL A 1 99  ? 19.647 10.749 10.684 0.465 14.32  ? 99  VAL A H    1 
ATOM   1832 H HA   A VAL A 1 99  ? 19.433 8.693  8.821  0.535 14.39  ? 99  VAL A HA   1 
ATOM   1833 H HA   B VAL A 1 99  ? 20.735 8.585  9.561  0.465 18.04  ? 99  VAL A HA   1 
ATOM   1834 H HB   A VAL A 1 99  ? 17.927 9.033  11.191 0.535 17.08  ? 99  VAL A HB   1 
ATOM   1835 H HB   B VAL A 1 99  ? 19.220 7.267  10.981 0.465 22.64  ? 99  VAL A HB   1 
ATOM   1836 H HG11 A VAL A 1 99  ? 18.088 6.705  11.447 0.535 28.48  ? 99  VAL A HG11 1 
ATOM   1837 H HG11 B VAL A 1 99  ? 21.487 7.317  11.435 0.465 46.01  ? 99  VAL A HG11 1 
ATOM   1838 H HG12 A VAL A 1 99  ? 17.295 7.052  10.140 0.535 28.48  ? 99  VAL A HG12 1 
ATOM   1839 H HG12 B VAL A 1 99  ? 21.269 8.566  12.356 0.465 46.01  ? 99  VAL A HG12 1 
ATOM   1840 H HG13 A VAL A 1 99  ? 18.792 6.595  10.051 0.535 28.48  ? 99  VAL A HG13 1 
ATOM   1841 H HG13 B VAL A 1 99  ? 20.634 7.186  12.743 0.465 46.01  ? 99  VAL A HG13 1 
ATOM   1842 H HG21 A VAL A 1 99  ? 19.799 8.177  12.318 0.535 20.92  ? 99  VAL A HG21 1 
ATOM   1843 H HG21 B VAL A 1 99  ? 17.851 9.032  11.586 0.465 30.44  ? 99  VAL A HG21 1 
ATOM   1844 H HG22 A VAL A 1 99  ? 20.589 8.080  10.968 0.535 20.92  ? 99  VAL A HG22 1 
ATOM   1845 H HG22 B VAL A 1 99  ? 18.380 8.250  12.837 0.465 30.44  ? 99  VAL A HG22 1 
ATOM   1846 H HG23 A VAL A 1 99  ? 20.208 9.483  11.554 0.535 20.92  ? 99  VAL A HG23 1 
ATOM   1847 H HG23 B VAL A 1 99  ? 19.015 9.630  12.450 0.465 30.44  ? 99  VAL A HG23 1 
ATOM   1848 N N    A SER A 1 100 ? 16.480 9.919  8.627  0.535 12.77  ? 100 SER A N    1 
ATOM   1849 N N    B SER A 1 100 ? 17.646 9.066  8.945  0.465 18.30  ? 100 SER A N    1 
ATOM   1850 C CA   A SER A 1 100 ? 15.226 9.902  7.859  0.535 16.11  ? 100 SER A CA   1 
ATOM   1851 C CA   B SER A 1 100 ? 16.513 8.695  8.104  0.465 20.41  ? 100 SER A CA   1 
ATOM   1852 C C    A SER A 1 100 ? 15.419 10.161 6.373  0.535 15.46  ? 100 SER A C    1 
ATOM   1853 C C    B SER A 1 100 ? 16.663 9.021  6.612  0.465 23.88  ? 100 SER A C    1 
ATOM   1854 O O    A SER A 1 100 ? 14.568 9.773  5.564  0.535 17.66  ? 100 SER A O    1 
ATOM   1855 O O    B SER A 1 100 ? 16.354 8.176  5.756  0.465 30.20  ? 100 SER A O    1 
ATOM   1856 C CB   A SER A 1 100 ? 14.284 10.943 8.476  0.535 19.99  ? 100 SER A CB   1 
ATOM   1857 C CB   B SER A 1 100 ? 15.261 9.389  8.694  0.465 22.32  ? 100 SER A CB   1 
ATOM   1858 O OG   A SER A 1 100 ? 13.971 10.592 9.793  0.535 27.41  ? 100 SER A OG   1 
ATOM   1859 O OG   B SER A 1 100 ? 14.740 8.519  9.680  0.465 33.48  ? 100 SER A OG   1 
ATOM   1860 H H    A SER A 1 100 ? 16.596 10.536 9.214  0.535 15.33  ? 100 SER A H    1 
ATOM   1861 H H    B SER A 1 100 ? 17.601 9.809  9.375  0.465 21.96  ? 100 SER A H    1 
ATOM   1862 H HA   A SER A 1 100 ? 14.815 9.019  7.965  0.535 19.34  ? 100 SER A HA   1 
ATOM   1863 H HA   B SER A 1 100 ? 16.384 7.727  8.186  0.465 24.50  ? 100 SER A HA   1 
ATOM   1864 H HB2  A SER A 1 100 ? 14.709 11.815 8.463  0.535 23.99  ? 100 SER A HB2  1 
ATOM   1865 H HB2  B SER A 1 100 ? 15.501 10.242 9.089  0.465 26.78  ? 100 SER A HB2  1 
ATOM   1866 H HB3  A SER A 1 100 ? 13.470 10.997 7.951  0.535 23.99  ? 100 SER A HB3  1 
ATOM   1867 H HB3  B SER A 1 100 ? 14.602 9.545  7.999  0.465 26.78  ? 100 SER A HB3  1 
ATOM   1868 H HG   A SER A 1 100 ? 13.692 9.821  9.811  0.535 41.11  ? 100 SER A HG   1 
ATOM   1869 H HG   B SER A 1 100 ? 14.215 8.930  10.157 0.465 50.22  ? 100 SER A HG   1 
ATOM   1870 N N    A ASP A 1 101 ? 16.486 10.870 6.011  0.535 13.17  ? 101 ASP A N    1 
ATOM   1871 N N    B ASP A 1 101 ? 17.118 10.205 6.210  0.465 23.94  ? 101 ASP A N    1 
ATOM   1872 C CA   A ASP A 1 101 ? 16.822 11.220 4.638  0.535 14.65  ? 101 ASP A CA   1 
ATOM   1873 C CA   B ASP A 1 101 ? 17.372 10.719 4.865  0.465 27.44  ? 101 ASP A CA   1 
ATOM   1874 C C    A ASP A 1 101 ? 17.698 10.142 3.986  0.535 18.36  ? 101 ASP A C    1 
ATOM   1875 C C    B ASP A 1 101 ? 18.461 9.927  4.161  0.465 31.37  ? 101 ASP A C    1 
ATOM   1876 O O    A ASP A 1 101 ? 18.482 10.496 3.099  0.535 33.63  ? 101 ASP A O    1 
ATOM   1877 O O    B ASP A 1 101 ? 18.678 10.046 2.941  0.465 34.03  ? 101 ASP A O    1 
ATOM   1878 C CB   A ASP A 1 101 ? 17.510 12.581 4.432  0.535 14.96  ? 101 ASP A CB   1 
ATOM   1879 C CB   B ASP A 1 101 ? 17.791 12.209 4.864  0.465 30.55  ? 101 ASP A CB   1 
ATOM   1880 C CG   A ASP A 1 101 ? 16.448 13.647 4.197  0.535 11.31  ? 101 ASP A CG   1 
ATOM   1881 C CG   B ASP A 1 101 ? 16.675 13.172 4.519  0.465 28.85  ? 101 ASP A CG   1 
ATOM   1882 O OD1  A ASP A 1 101 ? 15.285 13.401 3.958  0.535 15.84  ? 101 ASP A OD1  1 
ATOM   1883 O OD1  B ASP A 1 101 ? 15.619 12.673 4.076  0.465 38.14  ? 101 ASP A OD1  1 
ATOM   1884 O OD2  A ASP A 1 101 ? 16.948 14.814 4.130  0.535 11.89  ? 101 ASP A OD2  1 
ATOM   1885 O OD2  B ASP A 1 101 ? 16.857 14.404 4.681  0.465 35.70  ? 101 ASP A OD2  1 
ATOM   1886 H H    A ASP A 1 101 ? 17.015 11.141 6.633  0.535 15.80  ? 101 ASP A H    1 
ATOM   1887 H H    B ASP A 1 101 ? 17.290 10.759 6.845  0.465 28.73  ? 101 ASP A H    1 
ATOM   1888 H HA   A ASP A 1 101 ? 15.981 11.246 4.136  0.535 17.58  ? 101 ASP A HA   1 
ATOM   1889 H HA   B ASP A 1 101 ? 16.546 10.633 4.344  0.465 32.93  ? 101 ASP A HA   1 
ATOM   1890 H HB2  A ASP A 1 101 ? 18.035 12.807 5.216  0.535 17.96  ? 101 ASP A HB2  1 
ATOM   1891 H HB2  B ASP A 1 101 ? 18.135 12.435 5.742  0.465 36.65  ? 101 ASP A HB2  1 
ATOM   1892 H HB3  A ASP A 1 101 ? 18.107 12.537 3.669  0.535 17.96  ? 101 ASP A HB3  1 
ATOM   1893 H HB3  B ASP A 1 101 ? 18.512 12.328 4.227  0.465 36.65  ? 101 ASP A HB3  1 
ATOM   1894 N N    A GLY A 1 102 ? 17.497 8.914  4.439  0.535 18.95  ? 102 GLY A N    1 
ATOM   1895 N N    B GLY A 1 102 ? 19.168 9.038  4.868  0.465 27.75  ? 102 GLY A N    1 
ATOM   1896 C CA   A GLY A 1 102 ? 17.923 7.635  3.942  0.535 23.41  ? 102 GLY A CA   1 
ATOM   1897 C CA   B GLY A 1 102 ? 19.300 7.740  4.221  0.465 29.28  ? 102 GLY A CA   1 
ATOM   1898 C C    A GLY A 1 102 ? 19.385 7.349  4.207  0.535 23.74  ? 102 GLY A C    1 
ATOM   1899 C C    B GLY A 1 102 ? 20.301 6.710  4.620  0.465 29.12  ? 102 GLY A C    1 
ATOM   1900 O O    A GLY A 1 102 ? 20.004 6.641  3.442  0.535 32.62  ? 102 GLY A O    1 
ATOM   1901 O O    B GLY A 1 102 ? 20.043 5.483  4.582  0.465 34.24  ? 102 GLY A O    1 
ATOM   1902 H H    A GLY A 1 102 ? 17.028 8.875  5.159  0.535 22.74  ? 102 GLY A H    1 
ATOM   1903 H H    B GLY A 1 102 ? 19.513 9.217  5.635  0.465 33.30  ? 102 GLY A H    1 
ATOM   1904 H HA2  A GLY A 1 102 ? 17.386 6.942  4.358  0.535 28.09  ? 102 GLY A HA2  1 
ATOM   1905 H HA2  B GLY A 1 102 ? 18.430 7.314  4.284  0.465 35.13  ? 102 GLY A HA2  1 
ATOM   1906 H HA3  A GLY A 1 102 ? 17.763 7.600  2.986  0.535 28.09  ? 102 GLY A HA3  1 
ATOM   1907 H HA3  B GLY A 1 102 ? 19.451 7.918  3.280  0.465 35.13  ? 102 GLY A HA3  1 
ATOM   1908 N N    A ASN A 1 103 ? 19.935 7.862  5.271  0.535 18.07  ? 103 ASN A N    1 
ATOM   1909 N N    B ASN A 1 103 ? 21.525 7.045  4.969  0.465 29.05  ? 103 ASN A N    1 
ATOM   1910 C CA   A ASN A 1 103 ? 21.257 7.532  5.766  0.535 17.30  ? 103 ASN A CA   1 
ATOM   1911 C CA   B ASN A 1 103 ? 22.651 6.156  5.167  0.465 30.71  ? 103 ASN A CA   1 
ATOM   1912 C C    A ASN A 1 103 ? 21.090 6.555  6.929  0.535 18.38  ? 103 ASN A C    1 
ATOM   1913 C C    B ASN A 1 103 ? 22.731 5.490  6.523  0.465 27.43  ? 103 ASN A C    1 
ATOM   1914 O O    A ASN A 1 103 ? 20.140 6.631  7.706  0.535 23.97  ? 103 ASN A O    1 
ATOM   1915 O O    B ASN A 1 103 ? 23.712 4.868  6.913  0.465 23.33  ? 103 ASN A O    1 
ATOM   1916 C CB   A ASN A 1 103 ? 21.995 8.834  6.146  0.535 18.06  ? 103 ASN A CB   1 
ATOM   1917 C CB   B ASN A 1 103 ? 23.887 7.091  5.106  0.465 34.33  ? 103 ASN A CB   1 
ATOM   1918 C CG   A ASN A 1 103 ? 22.025 9.748  4.909  0.535 19.89  ? 103 ASN A CG   1 
ATOM   1919 C CG   B ASN A 1 103 ? 23.380 8.452  5.584  0.465 33.06  ? 103 ASN A CG   1 
ATOM   1920 O OD1  A ASN A 1 103 ? 22.662 9.611  3.865  0.535 28.07  ? 103 ASN A OD1  1 
ATOM   1921 O OD1  B ASN A 1 103 ? 23.504 9.429  4.833  0.465 41.13  ? 103 ASN A OD1  1 
ATOM   1922 N ND2  A ASN A 1 103 ? 21.273 10.825 4.964  0.535 20.74  ? 103 ASN A ND2  1 
ATOM   1923 N ND2  B ASN A 1 103 ? 22.790 8.545  6.791  0.465 37.85  ? 103 ASN A ND2  1 
ATOM   1924 H H    A ASN A 1 103 ? 19.479 8.441  5.714  0.535 21.68  ? 103 ASN A H    1 
ATOM   1925 H H    B ASN A 1 103 ? 21.672 7.883  5.092  0.465 34.86  ? 103 ASN A H    1 
ATOM   1926 H HA   A ASN A 1 103 ? 21.757 7.086  5.051  0.535 20.75  ? 103 ASN A HA   1 
ATOM   1927 H HA   B ASN A 1 103 ? 22.691 5.486  4.453  0.465 36.85  ? 103 ASN A HA   1 
ATOM   1928 H HB2  A ASN A 1 103 ? 21.535 9.276  6.876  0.535 21.68  ? 103 ASN A HB2  1 
ATOM   1929 H HB2  B ASN A 1 103 ? 24.593 6.765  5.686  0.465 41.20  ? 103 ASN A HB2  1 
ATOM   1930 H HB3  A ASN A 1 103 ? 22.900 8.632  6.432  0.535 21.68  ? 103 ASN A HB3  1 
ATOM   1931 H HB3  B ASN A 1 103 ? 24.228 7.150  4.200  0.465 41.20  ? 103 ASN A HB3  1 
ATOM   1932 H HD21 A ASN A 1 103 ? 21.253 11.370 4.300  0.535 24.89  ? 103 ASN A HD21 1 
ATOM   1933 H HD21 B ASN A 1 103 ? 22.485 9.301  7.064  0.465 45.42  ? 103 ASN A HD21 1 
ATOM   1934 H HD22 A ASN A 1 103 ? 20.801 10.984 5.665  0.535 24.89  ? 103 ASN A HD22 1 
ATOM   1935 H HD22 B ASN A 1 103 ? 22.719 7.847  7.289  0.465 45.42  ? 103 ASN A HD22 1 
ATOM   1936 N N    A GLY A 1 104 ? 22.022 5.610  7.048  0.535 20.46  ? 104 GLY A N    1 
ATOM   1937 N N    B GLY A 1 104 ? 21.666 5.699  7.324  0.465 21.49  ? 104 GLY A N    1 
ATOM   1938 C CA   A GLY A 1 104 ? 22.178 5.046  8.396  0.535 15.57  ? 104 GLY A CA   1 
ATOM   1939 C CA   B GLY A 1 104 ? 21.748 5.337  8.725  0.465 18.49  ? 104 GLY A CA   1 
ATOM   1940 C C    A GLY A 1 104 ? 23.121 5.858  9.235  0.535 13.76  ? 104 GLY A C    1 
ATOM   1941 C C    B GLY A 1 104 ? 22.837 6.044  9.493  0.465 15.14  ? 104 GLY A C    1 
ATOM   1942 O O    A GLY A 1 104 ? 23.581 6.967  8.926  0.535 13.78  ? 104 GLY A O    1 
ATOM   1943 O O    B GLY A 1 104 ? 23.052 7.248  9.289  0.465 18.64  ? 104 GLY A O    1 
ATOM   1944 H H    A GLY A 1 104 ? 22.498 5.347  6.382  0.535 24.55  ? 104 GLY A H    1 
ATOM   1945 H H    B GLY A 1 104 ? 20.945 6.044  7.007  0.465 25.79  ? 104 GLY A H    1 
ATOM   1946 H HA2  A GLY A 1 104 ? 21.312 5.012  8.831  0.535 18.69  ? 104 GLY A HA2  1 
ATOM   1947 H HA2  B GLY A 1 104 ? 20.896 5.532  9.145  0.465 22.19  ? 104 GLY A HA2  1 
ATOM   1948 H HA3  A GLY A 1 104 ? 22.513 4.138  8.326  0.535 18.69  ? 104 GLY A HA3  1 
ATOM   1949 H HA3  B GLY A 1 104 ? 21.895 4.380  8.790  0.465 22.19  ? 104 GLY A HA3  1 
ATOM   1950 N N    . MET A 1 105 ? 23.511 5.310  10.387 1.000 13.10  ? 105 MET A N    1 
ATOM   1951 C CA   . MET A 1 105 ? 24.538 5.930  11.215 1.000 11.58  ? 105 MET A CA   1 
ATOM   1952 C C    . MET A 1 105 ? 25.894 5.961  10.580 1.000 12.53  ? 105 MET A C    1 
ATOM   1953 O O    . MET A 1 105 ? 26.812 6.608  11.068 1.000 12.81  ? 105 MET A O    1 
ATOM   1954 C CB   . MET A 1 105 ? 24.609 5.325  12.613 1.000 12.08  ? 105 MET A CB   1 
ATOM   1955 C CG   . MET A 1 105 ? 23.415 5.770  13.464 1.000 12.11  ? 105 MET A CG   1 
ATOM   1956 S SD   . MET A 1 105 ? 23.622 5.451  15.209 1.000 13.73  ? 105 MET A SD   1 
ATOM   1957 C CE   . MET A 1 105 ? 24.706 6.828  15.619 1.000 13.84  ? 105 MET A CE   1 
ATOM   1958 H H    A MET A 1 105 ? 23.149 4.575  10.647 1.000 15.72  ? 105 MET A H    1 
ATOM   1959 H HA   . MET A 1 105 ? 24.268 6.864  11.333 1.000 13.90  ? 105 MET A HA   1 
ATOM   1960 H HB2  . MET A 1 105 ? 24.615 4.358  12.547 1.000 14.50  ? 105 MET A HB2  1 
ATOM   1961 H HB3  . MET A 1 105 ? 25.433 5.602  13.043 1.000 14.50  ? 105 MET A HB3  1 
ATOM   1962 H HG2  . MET A 1 105 ? 23.274 6.721  13.335 1.000 14.53  ? 105 MET A HG2  1 
ATOM   1963 H HG3  . MET A 1 105 ? 22.619 5.309  13.154 1.000 14.53  ? 105 MET A HG3  1 
ATOM   1964 H HE1  . MET A 1 105 ? 24.919 6.799  16.555 1.000 20.76  ? 105 MET A HE1  1 
ATOM   1965 H HE2  . MET A 1 105 ? 25.514 6.763  15.105 1.000 20.76  ? 105 MET A HE2  1 
ATOM   1966 H HE3  . MET A 1 105 ? 24.263 7.655  15.417 1.000 20.76  ? 105 MET A HE3  1 
ATOM   1967 N N    . ASN A 1 106 ? 26.037 5.328  9.425  1.000 16.80  ? 106 ASN A N    1 
ATOM   1968 C CA   . ASN A 1 106 ? 27.229 5.468  8.609  1.000 18.45  ? 106 ASN A CA   1 
ATOM   1969 C C    . ASN A 1 106 ? 27.510 6.895  8.171  1.000 17.07  ? 106 ASN A C    1 
ATOM   1970 O O    . ASN A 1 106 ? 28.663 7.204  7.766  1.000 20.52  ? 106 ASN A O    1 
ATOM   1971 C CB   . ASN A 1 106 ? 27.051 4.600  7.339  1.000 36.98  ? 106 ASN A CB   1 
ATOM   1972 C CG   . ASN A 1 106 ? 27.362 3.160  7.618  1.000 38.66  ? 106 ASN A CG   1 
ATOM   1973 O OD1  . ASN A 1 106 ? 28.305 2.649  8.239  1.000 45.11  ? 106 ASN A OD1  1 
ATOM   1974 N ND2  . ASN A 1 106 ? 26.459 2.315  7.092  1.000 51.92  ? 106 ASN A ND2  1 
ATOM   1975 H H    . ASN A 1 106 ? 25.402 4.817  9.150  1.000 20.16  ? 106 ASN A H    1 
ATOM   1976 H HA   . ASN A 1 106 ? 28.000 5.134  9.114  1.000 22.14  ? 106 ASN A HA   1 
ATOM   1977 H HB2  . ASN A 1 106 ? 26.137 4.676  7.023  1.000 44.37  ? 106 ASN A HB2  1 
ATOM   1978 H HB3  . ASN A 1 106 ? 27.638 4.927  6.640  1.000 44.37  ? 106 ASN A HB3  1 
ATOM   1979 H HD21 . ASN A 1 106 ? 26.553 1.466  7.195  1.000 62.30  ? 106 ASN A HD21 1 
ATOM   1980 H HD22 . ASN A 1 106 ? 25.787 2.623  6.652  1.000 62.30  ? 106 ASN A HD22 1 
ATOM   1981 N N    . ALA A 1 107 ? 26.521 7.781  8.313  1.000 15.97  ? 107 ALA A N    1 
ATOM   1982 C CA   . ALA A 1 107 ? 26.771 9.195  8.077  1.000 16.23  ? 107 ALA A CA   1 
ATOM   1983 C C    . ALA A 1 107 ? 27.795 9.810  8.985  1.000 14.99  ? 107 ALA A C    1 
ATOM   1984 O O    . ALA A 1 107 ? 28.384 10.816 8.664  1.000 20.24  ? 107 ALA A O    1 
ATOM   1985 C CB   . ALA A 1 107 ? 25.459 9.959  8.159  1.000 20.65  ? 107 ALA A CB   1 
ATOM   1986 H H    . ALA A 1 107 ? 25.736 7.516  8.543  1.000 19.17  ? 107 ALA A H    1 
ATOM   1987 H HA   . ALA A 1 107 ? 27.104 9.284  7.160  1.000 19.47  ? 107 ALA A HA   1 
ATOM   1988 H HB1  . ALA A 1 107 ? 25.622 10.893 8.004  1.000 30.98  ? 107 ALA A HB1  1 
ATOM   1989 H HB2  . ALA A 1 107 ? 24.852 9.626  7.494  1.000 30.98  ? 107 ALA A HB2  1 
ATOM   1990 H HB3  . ALA A 1 107 ? 25.074 9.842  9.030  1.000 30.98  ? 107 ALA A HB3  1 
ATOM   1991 N N    . TRP A 1 108 ? 28.023 9.194  10.145 1.000 11.91  ? 108 TRP A N    1 
ATOM   1992 C CA   . TRP A 1 108 ? 29.028 9.647  11.104 1.000 10.92  ? 108 TRP A CA   1 
ATOM   1993 C C    . TRP A 1 108 ? 30.266 8.794  10.976 1.000 11.05  ? 108 TRP A C    1 
ATOM   1994 O O    . TRP A 1 108 ? 30.268 7.610  11.323 1.000 12.17  ? 108 TRP A O    1 
ATOM   1995 C CB   . TRP A 1 108 ? 28.498 9.627  12.536 1.000 10.95  ? 108 TRP A CB   1 
ATOM   1996 C CG   . TRP A 1 108 ? 27.482 10.709 12.776 1.000 10.93  ? 108 TRP A CG   1 
ATOM   1997 C CD1  . TRP A 1 108 ? 27.787 11.987 13.127 1.000 13.11  ? 108 TRP A CD1  1 
ATOM   1998 C CD2  . TRP A 1 108 ? 26.071 10.634 12.660 1.000 9.99   ? 108 TRP A CD2  1 
ATOM   1999 N NE1  . TRP A 1 108 ? 26.647 12.703 13.213 1.000 13.02  ? 108 TRP A NE1  1 
ATOM   2000 C CE2  . TRP A 1 108 ? 25.567 11.931 12.959 1.000 10.72  ? 108 TRP A CE2  1 
ATOM   2001 C CE3  . TRP A 1 108 ? 25.155 9.655  12.332 1.000 12.02  ? 108 TRP A CE3  1 
ATOM   2002 C CZ2  . TRP A 1 108 ? 24.196 12.213 12.938 1.000 11.79  ? 108 TRP A CZ2  1 
ATOM   2003 C CZ3  . TRP A 1 108 ? 23.829 9.940  12.320 1.000 13.64  ? 108 TRP A CZ3  1 
ATOM   2004 C CH2  . TRP A 1 108 ? 23.354 11.177 12.609 1.000 12.85  ? 108 TRP A CH2  1 
ATOM   2005 H H    . TRP A 1 108 ? 27.557 8.498  10.338 1.000 14.29  ? 108 TRP A H    1 
ATOM   2006 H HA   . TRP A 1 108 ? 29.270 10.570 10.880 1.000 13.11  ? 108 TRP A HA   1 
ATOM   2007 H HB2  . TRP A 1 108 ? 28.092 8.764  12.713 1.000 13.14  ? 108 TRP A HB2  1 
ATOM   2008 H HB3  . TRP A 1 108 ? 29.238 9.741  13.152 1.000 13.14  ? 108 TRP A HB3  1 
ATOM   2009 H HD1  . TRP A 1 108 ? 28.644 12.314 13.282 1.000 15.73  ? 108 TRP A HD1  1 
ATOM   2010 H HE1  . TRP A 1 108 ? 26.612 13.540 13.404 1.000 15.63  ? 108 TRP A HE1  1 
ATOM   2011 H HE3  . TRP A 1 108 ? 25.448 8.799  12.118 1.000 14.42  ? 108 TRP A HE3  1 
ATOM   2012 H HZ2  . TRP A 1 108 ? 23.870 13.062 13.137 1.000 14.15  ? 108 TRP A HZ2  1 
ATOM   2013 H HZ3  . TRP A 1 108 ? 23.226 9.265  12.106 1.000 16.37  ? 108 TRP A HZ3  1 
ATOM   2014 H HH2  . TRP A 1 108 ? 22.437 11.328 12.585 1.000 15.42  ? 108 TRP A HH2  1 
ATOM   2015 N N    A VAL A 1 109 ? 31.374 9.375  10.510 0.569 11.84  ? 109 VAL A N    1 
ATOM   2016 N N    B VAL A 1 109 ? 31.333 9.388  10.487 0.431 11.49  ? 109 VAL A N    1 
ATOM   2017 C CA   A VAL A 1 109 ? 32.589 8.576  10.301 0.569 12.78  ? 109 VAL A CA   1 
ATOM   2018 C CA   B VAL A 1 109 ? 32.599 8.689  10.270 0.431 11.71  ? 109 VAL A CA   1 
ATOM   2019 C C    A VAL A 1 109 ? 33.049 7.981  11.599 0.569 10.65  ? 109 VAL A C    1 
ATOM   2020 C C    B VAL A 1 109 ? 33.150 8.098  11.538 0.431 11.62  ? 109 VAL A C    1 
ATOM   2021 O O    A VAL A 1 109 ? 33.474 6.825  11.675 0.569 11.73  ? 109 VAL A O    1 
ATOM   2022 O O    B VAL A 1 109 ? 33.756 7.022  11.538 0.431 11.84  ? 109 VAL A O    1 
ATOM   2023 C CB   A VAL A 1 109 ? 33.693 9.414  9.623  0.569 17.44  ? 109 VAL A CB   1 
ATOM   2024 C CB   B VAL A 1 109 ? 33.586 9.672  9.600  0.431 16.60  ? 109 VAL A CB   1 
ATOM   2025 C CG1  A VAL A 1 109 ? 34.159 10.600 10.459 0.569 21.42  ? 109 VAL A CG1  1 
ATOM   2026 C CG1  B VAL A 1 109 ? 34.960 9.055  9.455  0.431 22.70  ? 109 VAL A CG1  1 
ATOM   2027 C CG2  A VAL A 1 109 ? 34.838 8.472  9.245  0.569 25.76  ? 109 VAL A CG2  1 
ATOM   2028 C CG2  B VAL A 1 109 ? 33.062 10.097 8.226  0.431 21.41  ? 109 VAL A CG2  1 
ATOM   2029 H H    A VAL A 1 109 ? 31.377 10.217 10.332 0.569 14.20  ? 109 VAL A H    1 
ATOM   2030 H H    B VAL A 1 109 ? 31.283 10.223 10.287 0.431 13.79  ? 109 VAL A H    1 
ATOM   2031 H HA   A VAL A 1 109 ? 32.361 7.838  9.698  0.569 15.33  ? 109 VAL A HA   1 
ATOM   2032 H HA   B VAL A 1 109 ? 32.433 7.954  9.643  0.431 14.05  ? 109 VAL A HA   1 
ATOM   2033 H HB   A VAL A 1 109 ? 33.320 9.771  8.790  0.569 20.93  ? 109 VAL A HB   1 
ATOM   2034 H HB   B VAL A 1 109 ? 33.661 10.470 10.164 0.431 19.92  ? 109 VAL A HB   1 
ATOM   2035 H HG11 A VAL A 1 109 ? 33.407 11.158 10.669 0.569 32.12  ? 109 VAL A HG11 1 
ATOM   2036 H HG11 B VAL A 1 109 ? 35.285 8.791  10.319 0.431 34.04  ? 109 VAL A HG11 1 
ATOM   2037 H HG12 A VAL A 1 109 ? 34.558 10.281 11.272 0.569 32.12  ? 109 VAL A HG12 1 
ATOM   2038 H HG12 B VAL A 1 109 ? 34.908 8.286  8.884  0.431 34.04  ? 109 VAL A HG12 1 
ATOM   2039 H HG13 A VAL A 1 109 ? 34.806 11.107 9.963  0.569 32.12  ? 109 VAL A HG13 1 
ATOM   2040 H HG13 B VAL A 1 109 ? 35.561 9.699  9.071  0.431 34.04  ? 109 VAL A HG13 1 
ATOM   2041 H HG21 A VAL A 1 109 ? 34.494 7.744  8.721  0.569 38.64  ? 109 VAL A HG21 1 
ATOM   2042 H HG21 B VAL A 1 109 ? 32.190 10.487 8.323  0.431 32.12  ? 109 VAL A HG21 1 
ATOM   2043 H HG22 A VAL A 1 109 ? 35.493 8.953  8.734  0.569 38.64  ? 109 VAL A HG22 1 
ATOM   2044 H HG22 B VAL A 1 109 ? 33.660 10.741 7.841  0.431 32.12  ? 109 VAL A HG22 1 
ATOM   2045 H HG23 A VAL A 1 109 ? 35.245 8.127  10.043 0.569 38.64  ? 109 VAL A HG23 1 
ATOM   2046 H HG23 B VAL A 1 109 ? 33.007 9.328  7.653  0.431 32.12  ? 109 VAL A HG23 1 
ATOM   2047 N N    . ALA A 1 110 ? 32.936 8.742  12.691 1.000 11.35  ? 110 ALA A N    1 
ATOM   2048 C CA   . ALA A 1 110 ? 33.428 8.211  13.938 1.000 12.46  ? 110 ALA A CA   1 
ATOM   2049 C C    . ALA A 1 110 ? 32.599 7.021  14.392 1.000 11.71  ? 110 ALA A C    1 
ATOM   2050 O O    . ALA A 1 110 ? 33.151 6.130  15.014 1.000 14.09  ? 110 ALA A O    1 
ATOM   2051 C CB   . ALA A 1 110 ? 33.520 9.290  14.975 1.000 16.92  ? 110 ALA A CB   1 
ATOM   2052 H H    A ALA A 1 110 ? 32.580 9.525  12.651 1.000 13.62  ? 110 ALA A H    1 
ATOM   2053 H HA   . ALA A 1 110 ? 34.338 7.886  13.776 1.000 14.95  ? 110 ALA A HA   1 
ATOM   2054 H HB1  . ALA A 1 110 ? 33.849 8.917  15.796 1.000 25.38  ? 110 ALA A HB1  1 
ATOM   2055 H HB2  . ALA A 1 110 ? 34.119 9.975  14.671 1.000 25.38  ? 110 ALA A HB2  1 
ATOM   2056 H HB3  . ALA A 1 110 ? 32.649 9.668  15.121 1.000 25.38  ? 110 ALA A HB3  1 
ATOM   2057 N N    . TRP A 1 111 ? 31.302 7.011  14.094 1.000 11.44  ? 111 TRP A N    1 
ATOM   2058 C CA   . TRP A 1 111 ? 30.504 5.839  14.394 1.000 11.86  ? 111 TRP A CA   1 
ATOM   2059 C C    . TRP A 1 111 ? 30.986 4.618  13.630 1.000 11.58  ? 111 TRP A C    1 
ATOM   2060 O O    . TRP A 1 111 ? 31.175 3.549  14.156 1.000 12.81  ? 111 TRP A O    1 
ATOM   2061 C CB   . TRP A 1 111 ? 28.997 6.086  14.183 1.000 12.17  ? 111 TRP A CB   1 
ATOM   2062 C CG   . TRP A 1 111 ? 28.212 4.874  14.507 1.000 12.13  ? 111 TRP A CG   1 
ATOM   2063 C CD1  . TRP A 1 111 ? 27.720 4.541  15.762 1.000 12.71  ? 111 TRP A CD1  1 
ATOM   2064 C CD2  . TRP A 1 111 ? 27.819 3.808  13.626 1.000 12.78  ? 111 TRP A CD2  1 
ATOM   2065 N NE1  . TRP A 1 111 ? 27.073 3.344  15.663 1.000 13.72  ? 111 TRP A NE1  1 
ATOM   2066 C CE2  . TRP A 1 111 ? 27.103 2.876  14.368 1.000 13.37  ? 111 TRP A CE2  1 
ATOM   2067 C CE3  . TRP A 1 111 ? 27.978 3.593  12.244 1.000 13.85  ? 111 TRP A CE3  1 
ATOM   2068 C CZ2  . TRP A 1 111 ? 26.563 1.711  13.828 1.000 16.10  ? 111 TRP A CZ2  1 
ATOM   2069 C CZ3  . TRP A 1 111 ? 27.450 2.427  11.701 1.000 16.31  ? 111 TRP A CZ3  1 
ATOM   2070 C CH2  . TRP A 1 111 ? 26.756 1.529  12.477 1.000 17.97  ? 111 TRP A CH2  1 
ATOM   2071 H H    . TRP A 1 111 ? 30.939 7.698  13.725 1.000 13.72  ? 111 TRP A H    1 
ATOM   2072 H HA   . TRP A 1 111 ? 30.630 5.645  15.346 1.000 14.23  ? 111 TRP A HA   1 
ATOM   2073 H HB2  . TRP A 1 111 ? 28.708 6.819  14.749 1.000 14.60  ? 111 TRP A HB2  1 
ATOM   2074 H HB3  . TRP A 1 111 ? 28.837 6.338  13.261 1.000 14.60  ? 111 TRP A HB3  1 
ATOM   2075 H HD1  . TRP A 1 111 ? 27.815 5.047  16.536 1.000 15.25  ? 111 TRP A HD1  1 
ATOM   2076 H HE1  . TRP A 1 111 ? 26.698 2.937  16.320 1.000 16.46  ? 111 TRP A HE1  1 
ATOM   2077 H HE3  . TRP A 1 111 ? 28.423 4.212  11.711 1.000 16.62  ? 111 TRP A HE3  1 
ATOM   2078 H HZ2  . TRP A 1 111 ? 26.101 1.094  14.348 1.000 19.32  ? 111 TRP A HZ2  1 
ATOM   2079 H HZ3  . TRP A 1 111 ? 27.568 2.252  10.795 1.000 19.57  ? 111 TRP A HZ3  1 
ATOM   2080 H HH2  . TRP A 1 111 ? 26.404 0.768  12.074 1.000 21.57  ? 111 TRP A HH2  1 
ATOM   2081 N N    . ARG A 1 112 ? 31.160 4.801  12.312 1.000 12.17  ? 112 ARG A N    1 
ATOM   2082 C CA   . ARG A 1 112 ? 31.570 3.703  11.470 1.000 13.62  ? 112 ARG A CA   1 
ATOM   2083 C C    . ARG A 1 112 ? 32.927 3.149  11.857 1.000 14.74  ? 112 ARG A C    1 
ATOM   2084 O O    . ARG A 1 112 ? 33.167 1.947  11.749 1.000 20.18  ? 112 ARG A O    1 
ATOM   2085 C CB   . ARG A 1 112 ? 31.625 4.207  10.039 1.000 19.19  ? 112 ARG A CB   1 
ATOM   2086 C CG   . ARG A 1 112 ? 31.853 3.136  9.032  1.000 29.09  ? 112 ARG A CG   1 
ATOM   2087 C CD   . ARG A 1 112 ? 32.324 3.774  7.750  1.000 40.60  ? 112 ARG A CD   1 
ATOM   2088 N NE   . ARG A 1 112 ? 31.650 5.019  7.433  1.000 41.02  ? 112 ARG A NE   1 
ATOM   2089 C CZ   . ARG A 1 112 ? 32.080 5.937  6.584  1.000 58.17  ? 112 ARG A CZ   1 
ATOM   2090 N NH1  . ARG A 1 112 ? 31.402 7.080  6.614  1.000 47.39  ? 112 ARG A NH1  1 
ATOM   2091 N NH2  . ARG A 1 112 ? 33.110 5.697  5.772  1.000 76.95  ? 112 ARG A NH2  1 
ATOM   2092 H H    . ARG A 1 112 ? 31.027 5.578  11.967 1.000 14.60  ? 112 ARG A H    1 
ATOM   2093 H HA   . ARG A 1 112 ? 30.903 2.988  11.532 1.000 16.34  ? 112 ARG A HA   1 
ATOM   2094 H HB2  . ARG A 1 112 ? 30.790 4.656  9.833  1.000 23.03  ? 112 ARG A HB2  1 
ATOM   2095 H HB3  . ARG A 1 112 ? 32.337 4.862  9.965  1.000 23.03  ? 112 ARG A HB3  1 
ATOM   2096 H HG2  . ARG A 1 112 ? 32.522 2.513  9.358  1.000 34.90  ? 112 ARG A HG2  1 
ATOM   2097 H HG3  . ARG A 1 112 ? 31.030 2.647  8.876  1.000 34.90  ? 112 ARG A HG3  1 
ATOM   2098 H HD2  . ARG A 1 112 ? 33.277 3.943  7.817  1.000 48.72  ? 112 ARG A HD2  1 
ATOM   2099 H HD3  . ARG A 1 112 ? 32.186 3.149  7.021  1.000 48.72  ? 112 ARG A HD3  1 
ATOM   2100 H HE   . ARG A 1 112 ? 30.905 5.174  7.833  1.000 49.23  ? 112 ARG A HE   1 
ATOM   2101 H HH11 . ARG A 1 112 ? 30.743 7.174  7.158  1.000 56.87  ? 112 ARG A HH11 1 
ATOM   2102 H HH12 . ARG A 1 112 ? 31.624 7.725  6.090  1.000 56.87  ? 112 ARG A HH12 1 
ATOM   2103 H HH21 . ARG A 1 112 ? 33.507 4.935  5.795  1.000 92.34  ? 112 ARG A HH21 1 
ATOM   2104 H HH22 . ARG A 1 112 ? 33.377 6.305  5.225  1.000 92.34  ? 112 ARG A HH22 1 
ATOM   2105 N N    A ASN A 1 113 ? 33.858 3.981  12.271 0.485 14.01  ? 113 ASN A N    1 
ATOM   2106 N N    B ASN A 1 113 ? 33.812 4.010  12.311 0.515 12.88  ? 113 ASN A N    1 
ATOM   2107 C CA   A ASN A 1 113 ? 35.209 3.468  12.552 0.485 16.01  ? 113 ASN A CA   1 
ATOM   2108 C CA   B ASN A 1 113 ? 35.196 3.651  12.579 0.515 13.98  ? 113 ASN A CA   1 
ATOM   2109 C C    A ASN A 1 113 ? 35.430 3.157  14.026 0.485 15.30  ? 113 ASN A C    1 
ATOM   2110 C C    B ASN A 1 113 ? 35.367 3.153  14.007 0.515 12.93  ? 113 ASN A C    1 
ATOM   2111 O O    A ASN A 1 113 ? 36.371 2.458  14.438 0.485 18.85  ? 113 ASN A O    1 
ATOM   2112 O O    B ASN A 1 113 ? 36.233 2.313  14.217 0.515 15.90  ? 113 ASN A O    1 
ATOM   2113 C CB   A ASN A 1 113 ? 36.222 4.485  12.072 0.485 17.22  ? 113 ASN A CB   1 
ATOM   2114 C CB   B ASN A 1 113 ? 36.090 4.834  12.254 0.515 16.29  ? 113 ASN A CB   1 
ATOM   2115 C CG   A ASN A 1 113 ? 36.231 4.811  10.610 0.485 20.87  ? 113 ASN A CG   1 
ATOM   2116 C CG   B ASN A 1 113 ? 36.435 4.715  10.771 0.515 19.54  ? 113 ASN A CG   1 
ATOM   2117 O OD1  A ASN A 1 113 ? 35.660 4.157  9.740  0.485 23.53  ? 113 ASN A OD1  1 
ATOM   2118 O OD1  B ASN A 1 113 ? 37.233 3.851  10.449 0.515 31.64  ? 113 ASN A OD1  1 
ATOM   2119 N ND2  A ASN A 1 113 ? 36.909 5.912  10.303 0.485 22.53  ? 113 ASN A ND2  1 
ATOM   2120 N ND2  B ASN A 1 113 ? 35.760 5.537  10.006 0.515 27.45  ? 113 ASN A ND2  1 
ATOM   2121 H H    A ASN A 1 113 ? 33.679 4.815  12.377 0.485 16.81  ? 113 ASN A H    1 
ATOM   2122 H H    B ASN A 1 113 ? 33.562 4.820  12.456 0.515 15.46  ? 113 ASN A H    1 
ATOM   2123 H HA   A ASN A 1 113 ? 35.337 2.642  12.041 0.485 19.21  ? 113 ASN A HA   1 
ATOM   2124 H HA   B ASN A 1 113 ? 35.437 2.918  11.975 0.515 16.78  ? 113 ASN A HA   1 
ATOM   2125 H HB2  A ASN A 1 113 ? 36.073 5.309  12.561 0.485 20.66  ? 113 ASN A HB2  1 
ATOM   2126 H HB2  B ASN A 1 113 ? 35.627 5.668  12.428 0.515 19.55  ? 113 ASN A HB2  1 
ATOM   2127 H HB3  A ASN A 1 113 ? 37.105 4.164  12.312 0.485 20.66  ? 113 ASN A HB3  1 
ATOM   2128 H HB3  B ASN A 1 113 ? 36.896 4.808  12.793 0.515 19.55  ? 113 ASN A HB3  1 
ATOM   2129 H HD21 A ASN A 1 113 ? 36.954 6.176  9.486  0.485 27.04  ? 113 ASN A HD21 1 
ATOM   2130 H HD21 B ASN A 1 113 ? 35.856 5.506  9.151  0.515 32.93  ? 113 ASN A HD21 1 
ATOM   2131 H HD22 A ASN A 1 113 ? 37.304 6.360  10.922 0.485 27.04  ? 113 ASN A HD22 1 
ATOM   2132 H HD22 B ASN A 1 113 ? 35.222 6.109  10.357 0.515 32.93  ? 113 ASN A HD22 1 
ATOM   2133 N N    . ARG A 1 114 ? 34.622 3.678  14.961 1.000 14.55  ? 114 ARG A N    1 
ATOM   2134 C CA   . ARG A 1 114 ? 34.946 3.499  16.350 1.000 15.37  ? 114 ARG A CA   1 
ATOM   2135 C C    . ARG A 1 114 ? 33.828 2.917  17.196 1.000 14.80  ? 114 ARG A C    1 
ATOM   2136 O O    . ARG A 1 114 ? 34.025 2.543  18.348 1.000 20.49  ? 114 ARG A O    1 
ATOM   2137 C CB   . ARG A 1 114 ? 35.404 4.776  17.008 1.000 16.26  ? 114 ARG A CB   1 
ATOM   2138 C CG   . ARG A 1 114 ? 36.483 5.437  16.118 1.000 18.26  ? 114 ARG A CG   1 
ATOM   2139 C CD   . ARG A 1 114 ? 37.401 6.333  16.806 1.000 19.03  ? 114 ARG A CD   1 
ATOM   2140 N NE   . ARG A 1 114 ? 38.204 5.653  17.837 1.000 17.67  ? 114 ARG A NE   1 
ATOM   2141 C CZ   . ARG A 1 114 ? 39.063 6.319  18.582 1.000 16.94  ? 114 ARG A CZ   1 
ATOM   2142 N NH1  . ARG A 1 114 ? 39.826 5.673  19.394 1.000 22.26  ? 114 ARG A NH1  1 
ATOM   2143 N NH2  . ARG A 1 114 ? 39.088 7.651  18.475 1.000 20.17  ? 114 ARG A NH2  1 
ATOM   2144 H H    A ARG A 1 114 ? 33.917 4.115  14.732 1.000 17.45  ? 114 ARG A H    1 
ATOM   2145 H HA   . ARG A 1 114 ? 35.696 2.869  16.391 1.000 18.44  ? 114 ARG A HA   1 
ATOM   2146 H HB2  . ARG A 1 114 ? 34.652 5.378  17.120 1.000 19.51  ? 114 ARG A HB2  1 
ATOM   2147 H HB3  . ARG A 1 114 ? 35.772 4.582  17.885 1.000 19.51  ? 114 ARG A HB3  1 
ATOM   2148 H HG2  . ARG A 1 114 ? 37.001 4.736  15.692 1.000 21.91  ? 114 ARG A HG2  1 
ATOM   2149 H HG3  . ARG A 1 114 ? 36.037 5.936  15.416 1.000 21.91  ? 114 ARG A HG3  1 
ATOM   2150 H HD2  . ARG A 1 114 ? 37.998 6.734  16.154 1.000 22.84  ? 114 ARG A HD2  1 
ATOM   2151 H HD3  . ARG A 1 114 ? 36.893 7.047  17.221 1.000 22.84  ? 114 ARG A HD3  1 
ATOM   2152 H HE   . ARG A 1 114 ? 38.111 4.806  17.955 1.000 21.20  ? 114 ARG A HE   1 
ATOM   2153 H HH11 . ARG A 1 114 ? 39.771 4.817  19.445 1.000 26.72  ? 114 ARG A HH11 1 
ATOM   2154 H HH12 . ARG A 1 114 ? 40.390 6.098  19.884 1.000 26.72  ? 114 ARG A HH12 1 
ATOM   2155 H HH21 . ARG A 1 114 ? 39.629 8.112  18.960 1.000 24.21  ? 114 ARG A HH21 1 
ATOM   2156 H HH22 . ARG A 1 114 ? 38.563 8.048  17.921 1.000 24.21  ? 114 ARG A HH22 1 
ATOM   2157 N N    . CYS A 1 115 ? 32.619 2.814  16.647 1.000 12.79  ? 115 CYS A N    1 
ATOM   2158 C CA   . CYS A 1 115 ? 31.486 2.257  17.352 1.000 12.66  ? 115 CYS A CA   1 
ATOM   2159 C C    . CYS A 1 115 ? 30.926 1.014  16.718 1.000 12.79  ? 115 CYS A C    1 
ATOM   2160 O O    . CYS A 1 115 ? 30.599 0.071  17.403 1.000 14.76  ? 115 CYS A O    1 
ATOM   2161 C CB   . CYS A 1 115 ? 30.350 3.297  17.431 1.000 11.58  ? 115 CYS A CB   1 
ATOM   2162 S SG   . CYS A 1 115 ? 30.882 4.840  18.239 1.000 11.90  ? 115 CYS A SG   1 
ATOM   2163 H H    . CYS A 1 115 ? 32.508 3.089  15.839 1.000 15.35  ? 115 CYS A H    1 
ATOM   2164 H HA   . CYS A 1 115 ? 31.768 2.038  18.265 1.000 15.19  ? 115 CYS A HA   1 
ATOM   2165 H HB2  . CYS A 1 115 ? 30.040 3.498  16.534 1.000 13.89  ? 115 CYS A HB2  1 
ATOM   2166 H HB3  . CYS A 1 115 ? 29.606 2.919  17.926 1.000 13.89  ? 115 CYS A HB3  1 
ATOM   2167 N N    . LYS A 1 116 ? 30.793 0.982  15.393 1.000 14.10  ? 116 LYS A N    1 
ATOM   2168 C CA   . LYS A 1 116 ? 30.303 -0.161 14.655 1.000 15.06  ? 116 LYS A CA   1 
ATOM   2169 C C    . LYS A 1 116 ? 31.106 -1.409 15.016 1.000 17.45  ? 116 LYS A C    1 
ATOM   2170 O O    . LYS A 1 116 ? 32.364 -1.393 14.986 1.000 22.00  ? 116 LYS A O    1 
ATOM   2171 C CB   . LYS A 1 116 ? 30.416 0.144  13.130 1.000 15.72  ? 116 LYS A CB   1 
ATOM   2172 C CG   . LYS A 1 116 ? 29.907 -0.904 12.211 1.000 18.33  ? 116 LYS A CG   1 
ATOM   2173 C CD   . LYS A 1 116 ? 30.219 -0.489 10.775 1.000 18.56  ? 116 LYS A CD   1 
ATOM   2174 C CE   . LYS A 1 116 ? 29.765 -1.558 9.825  1.000 19.81  ? 116 LYS A CE   1 
ATOM   2175 N NZ   . LYS A 1 116 ? 30.235 -1.173 8.499  1.000 20.18  ? 116 LYS A NZ   1 
ATOM   2176 H H    . LYS A 1 116 ? 31.013 1.685  14.949 1.000 16.92  ? 116 LYS A H    1 
ATOM   2177 H HA   . LYS A 1 116 ? 29.362 -0.309 14.883 1.000 18.07  ? 116 LYS A HA   1 
ATOM   2178 H HB2  . LYS A 1 116 ? 29.934 0.966  12.949 1.000 18.86  ? 116 LYS A HB2  1 
ATOM   2179 H HB3  . LYS A 1 116 ? 31.350 0.304  12.921 1.000 18.86  ? 116 LYS A HB3  1 
ATOM   2180 H HG2  . LYS A 1 116 ? 30.332 -1.753 12.410 1.000 21.99  ? 116 LYS A HG2  1 
ATOM   2181 H HG3  . LYS A 1 116 ? 28.950 -1.008 12.325 1.000 21.99  ? 116 LYS A HG3  1 
ATOM   2182 H HD2  . LYS A 1 116 ? 29.767 0.344  10.570 1.000 22.27  ? 116 LYS A HD2  1 
ATOM   2183 H HD3  . LYS A 1 116 ? 31.174 -0.348 10.675 1.000 22.27  ? 116 LYS A HD3  1 
ATOM   2184 H HE2  . LYS A 1 116 ? 30.139 -2.416 10.079 1.000 23.77  ? 116 LYS A HE2  1 
ATOM   2185 H HE3  . LYS A 1 116 ? 28.798 -1.628 9.833  1.000 23.77  ? 116 LYS A HE3  1 
ATOM   2186 H HZ1  . LYS A 1 116 ? 29.983 -1.787 7.905  1.000 30.26  ? 116 LYS A HZ1  1 
ATOM   2187 H HZ2  . LYS A 1 116 ? 29.885 -0.385 8.278  1.000 30.26  ? 116 LYS A HZ2  1 
ATOM   2188 H HZ3  . LYS A 1 116 ? 31.123 -1.113 8.505  1.000 30.26  ? 116 LYS A HZ3  1 
ATOM   2189 N N    A GLY A 1 117 ? 30.309 -2.440 15.359 0.717 20.43  ? 117 GLY A N    1 
ATOM   2190 N N    B GLY A 1 117 ? 30.628 -2.587 15.389 0.283 21.26  ? 117 GLY A N    1 
ATOM   2191 C CA   A GLY A 1 117 ? 30.763 -3.778 15.697 0.717 23.69  ? 117 GLY A CA   1 
ATOM   2192 C CA   B GLY A 1 117 ? 31.693 -3.580 15.690 0.283 16.82  ? 117 GLY A CA   1 
ATOM   2193 C C    A GLY A 1 117 ? 31.297 -3.904 17.127 0.717 21.71  ? 117 GLY A C    1 
ATOM   2194 C C    B GLY A 1 117 ? 32.048 -3.647 17.153 0.283 15.78  ? 117 GLY A C    1 
ATOM   2195 O O    A GLY A 1 117 ? 31.613 -5.063 17.423 0.717 26.38  ? 117 GLY A O    1 
ATOM   2196 O O    B GLY A 1 117 ? 32.885 -4.384 17.700 0.283 16.19  ? 117 GLY A O    1 
ATOM   2197 H H    A GLY A 1 117 ? 29.462 -2.293 15.380 0.717 24.52  ? 117 GLY A H    1 
ATOM   2198 H H    B GLY A 1 117 ? 29.788 -2.760 15.450 0.283 25.51  ? 117 GLY A H    1 
ATOM   2199 H HA2  A GLY A 1 117 ? 30.024 -4.397 15.583 0.717 28.43  ? 117 GLY A HA2  1 
ATOM   2200 H HA2  B GLY A 1 117 ? 31.397 -4.456 15.398 0.283 20.19  ? 117 GLY A HA2  1 
ATOM   2201 H HA3  A GLY A 1 117 ? 31.462 -4.037 15.077 0.717 28.43  ? 117 GLY A HA3  1 
ATOM   2202 H HA3  B GLY A 1 117 ? 32.488 -3.352 15.183 0.283 20.19  ? 117 GLY A HA3  1 
ATOM   2203 N N    . THR A 1 118 ? 31.345 -2.813 17.923 1.000 20.20  ? 118 THR A N    1 
ATOM   2204 C CA   . THR A 1 118 ? 31.824 -2.767 19.311 1.000 20.22  ? 118 THR A CA   1 
ATOM   2205 C C    . THR A 1 118 ? 30.658 -2.995 20.276 1.000 20.45  ? 118 THR A C    1 
ATOM   2206 O O    . THR A 1 118 ? 29.489 -2.959 19.897 1.000 21.06  ? 118 THR A O    1 
ATOM   2207 C CB   . THR A 1 118 ? 32.579 -1.483 19.731 1.000 21.52  ? 118 THR A CB   1 
ATOM   2208 O OG1  . THR A 1 118 ? 31.613 -0.490 19.855 1.000 18.79  ? 118 THR A OG1  1 
ATOM   2209 C CG2  . THR A 1 118 ? 33.712 -1.095 18.765 1.000 25.07  ? 118 THR A CG2  1 
ATOM   2210 H H    A THR A 1 118 ? 31.068 -2.073 17.584 1.000 24.24  ? 118 THR A H    1 
ATOM   2211 H HA   . THR A 1 118 ? 32.445 -3.517 19.427 1.000 24.26  ? 118 THR A HA   1 
ATOM   2212 H HB   . THR A 1 118 ? 32.973 -1.637 20.616 1.000 25.82  ? 118 THR A HB   1 
ATOM   2213 H HG1  . THR A 1 118 ? 31.968 0.208  20.096 1.000 28.18  ? 118 THR A HG1  1 
ATOM   2214 H HG21 . THR A 1 118 ? 34.350 -1.810 18.715 1.000 37.60  ? 118 THR A HG21 1 
ATOM   2215 H HG22 . THR A 1 118 ? 33.346 -0.931 17.892 1.000 37.60  ? 118 THR A HG22 1 
ATOM   2216 H HG23 . THR A 1 118 ? 34.146 -0.300 19.083 1.000 37.60  ? 118 THR A HG23 1 
ATOM   2217 N N    . ASP A 1 119 ? 30.959 -3.185 21.546 1.000 20.95  ? 119 ASP A N    1 
ATOM   2218 C CA   . ASP A 1 119 ? 29.910 -3.340 22.547 1.000 24.25  ? 119 ASP A CA   1 
ATOM   2219 C C    . ASP A 1 119 ? 29.393 -1.986 22.944 1.000 20.51  ? 119 ASP A C    1 
ATOM   2220 O O    . ASP A 1 119 ? 29.839 -1.438 23.911 1.000 23.71  ? 119 ASP A O    1 
ATOM   2221 C CB   . ASP A 1 119 ? 30.418 -4.178 23.741 1.000 32.32  ? 119 ASP A CB   1 
ATOM   2222 C CG   . ASP A 1 119 ? 29.489 -4.147 24.932 1.000 41.79  ? 119 ASP A CG   1 
ATOM   2223 O OD1  . ASP A 1 119 ? 28.289 -3.818 24.726 1.000 48.31  ? 119 ASP A OD1  1 
ATOM   2224 O OD2  . ASP A 1 119 ? 29.999 -4.465 26.054 1.000 57.96  ? 119 ASP A OD2  1 
ATOM   2225 H H    . ASP A 1 119 ? 31.784 -3.217 21.787 1.000 25.14  ? 119 ASP A H    1 
ATOM   2226 H HA   . ASP A 1 119 ? 29.171 -3.831 22.131 1.000 29.10  ? 119 ASP A HA   1 
ATOM   2227 H HB2  . ASP A 1 119 ? 30.531 -5.098 23.455 1.000 38.78  ? 119 ASP A HB2  1 
ATOM   2228 H HB3  . ASP A 1 119 ? 31.288 -3.845 24.012 1.000 38.78  ? 119 ASP A HB3  1 
ATOM   2229 N N    . VAL A 1 120 ? 28.420 -1.420 22.189 1.000 18.64  ? 120 VAL A N    1 
ATOM   2230 C CA   . VAL A 1 120 ? 28.042 -0.049 22.450 1.000 16.76  ? 120 VAL A CA   1 
ATOM   2231 C C    . VAL A 1 120 ? 27.224 0.112  23.693 1.000 17.99  ? 120 VAL A C    1 
ATOM   2232 O O    . VAL A 1 120 ? 27.063 1.187  24.189 1.000 19.20  ? 120 VAL A O    1 
ATOM   2233 C CB   . VAL A 1 120 ? 27.274 0.563  21.246 1.000 16.88  ? 120 VAL A CB   1 
ATOM   2234 C CG1  . VAL A 1 120 ? 28.226 0.747  20.051 1.000 19.43  ? 120 VAL A CG1  1 
ATOM   2235 C CG2  . VAL A 1 120 ? 26.039 -0.246 20.953 1.000 19.01  ? 120 VAL A CG2  1 
ATOM   2236 H H    . VAL A 1 120 ? 28.033 -1.869 21.566 1.000 22.37  ? 120 VAL A H    1 
ATOM   2237 H HA   . VAL A 1 120 ? 28.866 0.468  22.569 1.000 20.11  ? 120 VAL A HA   1 
ATOM   2238 H HB   . VAL A 1 120 ? 26.976 1.456  21.518 1.000 20.26  ? 120 VAL A HB   1 
ATOM   2239 H HG11 . VAL A 1 120 ? 28.983 1.271  20.323 1.000 29.15  ? 120 VAL A HG11 1 
ATOM   2240 H HG12 . VAL A 1 120 ? 28.525 -0.112 19.745 1.000 29.15  ? 120 VAL A HG12 1 
ATOM   2241 H HG13 . VAL A 1 120 ? 27.764 1.197  19.340 1.000 29.15  ? 120 VAL A HG13 1 
ATOM   2242 H HG21 . VAL A 1 120 ? 25.503 -0.312 21.747 1.000 28.51  ? 120 VAL A HG21 1 
ATOM   2243 H HG22 . VAL A 1 120 ? 25.532 0.183  20.260 1.000 28.51  ? 120 VAL A HG22 1 
ATOM   2244 H HG23 . VAL A 1 120 ? 26.293 -1.126 20.665 1.000 28.51  ? 120 VAL A HG23 1 
ATOM   2245 N N    . GLN A 1 121 ? 26.727 -1.004 24.245 1.000 19.25  ? 121 GLN A N    1 
ATOM   2246 C CA   . GLN A 1 121 ? 25.983 -0.955 25.473 1.000 20.09  ? 121 GLN A CA   1 
ATOM   2247 C C    . GLN A 1 121 ? 26.883 -0.511 26.610 1.000 18.58  ? 121 GLN A C    1 
ATOM   2248 O O    . GLN A 1 121 ? 26.412 0.054  27.632 1.000 18.84  ? 121 GLN A O    1 
ATOM   2249 C CB   . GLN A 1 121 ? 25.352 -2.318 25.847 1.000 24.62  ? 121 GLN A CB   1 
ATOM   2250 C CG   . GLN A 1 121 ? 24.281 -2.832 24.911 1.000 41.97  ? 121 GLN A CG   1 
ATOM   2251 C CD   . GLN A 1 121 ? 22.990 -3.355 25.509 1.000 56.87  ? 121 GLN A CD   1 
ATOM   2252 O OE1  . GLN A 1 121 ? 22.416 -4.361 25.030 1.000 75.70  ? 121 GLN A OE1  1 
ATOM   2253 N NE2  . GLN A 1 121 ? 22.485 -2.713 26.575 1.000 77.55  ? 121 GLN A NE2  1 
ATOM   2254 H H    . GLN A 1 121 ? 26.857 -1.761 23.858 1.000 23.10  ? 121 GLN A H    1 
ATOM   2255 H HA   . GLN A 1 121 ? 25.263 -0.297 25.373 1.000 24.11  ? 121 GLN A HA   1 
ATOM   2256 H HB2  . GLN A 1 121 ? 26.060 -2.980 25.892 1.000 29.54  ? 121 GLN A HB2  1 
ATOM   2257 H HB3  . GLN A 1 121 ? 24.969 -2.243 26.735 1.000 29.54  ? 121 GLN A HB3  1 
ATOM   2258 H HG2  . GLN A 1 121 ? 24.054 -2.113 24.300 1.000 50.36  ? 121 GLN A HG2  1 
ATOM   2259 H HG3  . GLN A 1 121 ? 24.670 -3.545 24.381 1.000 50.36  ? 121 GLN A HG3  1 
ATOM   2260 H HE21 . GLN A 1 121 ? 21.757 -2.991 26.940 1.000 93.06  ? 121 GLN A HE21 1 
ATOM   2261 H HE22 . GLN A 1 121 ? 22.889 -2.023 26.893 1.000 93.06  ? 121 GLN A HE22 1 
ATOM   2262 N N    . ALA A 1 122 ? 28.183 -0.709 26.473 1.000 18.99  ? 122 ALA A N    1 
ATOM   2263 C CA   . ALA A 1 122 ? 29.114 -0.196 27.466 1.000 20.47  ? 122 ALA A CA   1 
ATOM   2264 C C    . ALA A 1 122 ? 28.908 1.284  27.711 1.000 17.89  ? 122 ALA A C    1 
ATOM   2265 O O    . ALA A 1 122 ? 29.139 1.773  28.832 1.000 23.05  ? 122 ALA A O    1 
ATOM   2266 C CB   . ALA A 1 122 ? 30.569 -0.458 27.081 1.000 23.59  ? 122 ALA A CB   1 
ATOM   2267 H H    . ALA A 1 122 ? 28.480 -1.144 25.793 1.000 22.79  ? 122 ALA A H    1 
ATOM   2268 H HA   . ALA A 1 122 ? 28.940 -0.664 28.309 1.000 24.56  ? 122 ALA A HA   1 
ATOM   2269 H HB1  . ALA A 1 122 ? 31.148 -0.104 27.760 1.000 35.39  ? 122 ALA A HB1  1 
ATOM   2270 H HB2  . ALA A 1 122 ? 30.712 -1.403 26.998 1.000 35.39  ? 122 ALA A HB2  1 
ATOM   2271 H HB3  . ALA A 1 122 ? 30.760 -0.030 26.243 1.000 35.39  ? 122 ALA A HB3  1 
ATOM   2272 N N    A TRP A 1 123 ? 28.453 2.028  26.701 0.520 16.55  ? 123 TRP A N    1 
ATOM   2273 N N    B TRP A 1 123 ? 28.449 2.034  26.703 0.480 16.82  ? 123 TRP A N    1 
ATOM   2274 C CA   A TRP A 1 123 ? 28.427 3.480  26.866 0.520 16.42  ? 123 TRP A CA   1 
ATOM   2275 C CA   B TRP A 1 123 ? 28.384 3.489  26.805 0.480 16.79  ? 123 TRP A CA   1 
ATOM   2276 C C    A TRP A 1 123 ? 27.256 3.917  27.736 0.520 16.54  ? 123 TRP A C    1 
ATOM   2277 C C    B TRP A 1 123 ? 27.250 3.931  27.721 0.480 16.00  ? 123 TRP A C    1 
ATOM   2278 O O    A TRP A 1 123 ? 27.289 5.046  28.182 0.520 17.60  ? 123 TRP A O    1 
ATOM   2279 O O    B TRP A 1 123 ? 27.288 5.043  28.220 0.480 23.69  ? 123 TRP A O    1 
ATOM   2280 C CB   A TRP A 1 123 ? 28.370 4.188  25.502 0.520 16.59  ? 123 TRP A CB   1 
ATOM   2281 C CB   B TRP A 1 123 ? 28.213 4.165  25.425 0.480 16.39  ? 123 TRP A CB   1 
ATOM   2282 C CG   A TRP A 1 123 ? 29.751 4.068  24.931 0.520 17.72  ? 123 TRP A CG   1 
ATOM   2283 C CG   B TRP A 1 123 ? 29.490 3.924  24.665 0.480 16.37  ? 123 TRP A CG   1 
ATOM   2284 C CD1  A TRP A 1 123 ? 30.214 3.205  23.978 0.520 18.75  ? 123 TRP A CD1  1 
ATOM   2285 C CD1  B TRP A 1 123 ? 29.743 3.001  23.693 0.480 17.78  ? 123 TRP A CD1  1 
ATOM   2286 C CD2  A TRP A 1 123 ? 30.854 4.859  25.360 0.520 19.15  ? 123 TRP A CD2  1 
ATOM   2287 C CD2  B TRP A 1 123 ? 30.704 4.632  24.895 0.480 15.88  ? 123 TRP A CD2  1 
ATOM   2288 N NE1  A TRP A 1 123 ? 31.540 3.423  23.769 0.520 18.31  ? 123 TRP A NE1  1 
ATOM   2289 N NE1  B TRP A 1 123 ? 31.044 3.110  23.288 0.480 18.25  ? 123 TRP A NE1  1 
ATOM   2290 C CE2  A TRP A 1 123 ? 31.959 4.432  24.602 0.520 18.65  ? 123 TRP A CE2  1 
ATOM   2291 C CE2  B TRP A 1 123 ? 31.661 4.094  24.003 0.480 17.53  ? 123 TRP A CE2  1 
ATOM   2292 C CE3  A TRP A 1 123 ? 30.982 5.896  26.296 0.520 20.03  ? 123 TRP A CE3  1 
ATOM   2293 C CE3  B TRP A 1 123 ? 31.051 5.674  25.765 0.480 19.24  ? 123 TRP A CE3  1 
ATOM   2294 C CZ2  A TRP A 1 123 ? 33.218 5.006  24.758 0.520 19.54  ? 123 TRP A CZ2  1 
ATOM   2295 C CZ2  B TRP A 1 123 ? 32.970 4.593  23.979 0.480 21.42  ? 123 TRP A CZ2  1 
ATOM   2296 C CZ3  A TRP A 1 123 ? 32.235 6.447  26.442 0.520 20.49  ? 123 TRP A CZ3  1 
ATOM   2297 C CZ3  B TRP A 1 123 ? 32.341 6.146  25.733 0.480 21.05  ? 123 TRP A CZ3  1 
ATOM   2298 C CH2  A TRP A 1 123 ? 33.312 6.001  25.682 0.520 20.78  ? 123 TRP A CH2  1 
ATOM   2299 C CH2  B TRP A 1 123 ? 33.266 5.598  24.844 0.480 22.16  ? 123 TRP A CH2  1 
ATOM   2300 H H    A TRP A 1 123 ? 28.181 1.662  25.971 0.520 19.86  ? 123 TRP A H    1 
ATOM   2301 H H    B TRP A 1 123 ? 28.185 1.651  25.979 0.480 20.18  ? 123 TRP A H    1 
ATOM   2302 H HA   A TRP A 1 123 ? 29.256 3.749  27.314 0.520 19.70  ? 123 TRP A HA   1 
ATOM   2303 H HA   B TRP A 1 123 ? 29.227 3.803  27.193 0.480 20.15  ? 123 TRP A HA   1 
ATOM   2304 H HB2  A TRP A 1 123 ? 27.721 3.760  24.921 0.520 19.90  ? 123 TRP A HB2  1 
ATOM   2305 H HB2  B TRP A 1 123 ? 27.459 3.780  24.951 0.480 19.66  ? 123 TRP A HB2  1 
ATOM   2306 H HB3  A TRP A 1 123 ? 28.125 5.120  25.611 0.520 19.90  ? 123 TRP A HB3  1 
ATOM   2307 H HB3  B TRP A 1 123 ? 28.057 5.117  25.531 0.480 19.66  ? 123 TRP A HB3  1 
ATOM   2308 H HD1  A TRP A 1 123 ? 29.701 2.566  23.540 0.520 22.50  ? 123 TRP A HD1  1 
ATOM   2309 H HD1  B TRP A 1 123 ? 29.126 2.392  23.357 0.480 21.34  ? 123 TRP A HD1  1 
ATOM   2310 H HE1  A TRP A 1 123 ? 32.035 2.999  23.208 0.520 21.97  ? 123 TRP A HE1  1 
ATOM   2311 H HE1  B TRP A 1 123 ? 31.416 2.632  22.678 0.480 21.90  ? 123 TRP A HE1  1 
ATOM   2312 H HE3  A TRP A 1 123 ? 30.256 6.196  26.794 0.520 24.04  ? 123 TRP A HE3  1 
ATOM   2313 H HE3  B TRP A 1 123 ? 30.425 6.036  26.350 0.480 23.09  ? 123 TRP A HE3  1 
ATOM   2314 H HZ2  A TRP A 1 123 ? 33.952 4.727  24.260 0.520 23.45  ? 123 TRP A HZ2  1 
ATOM   2315 H HZ2  B TRP A 1 123 ? 33.609 4.251  23.397 0.480 25.70  ? 123 TRP A HZ2  1 
ATOM   2316 H HZ3  A TRP A 1 123 ? 32.364 7.130  27.060 0.520 24.58  ? 123 TRP A HZ3  1 
ATOM   2317 H HZ3  B TRP A 1 123 ? 32.599 6.832  26.305 0.480 25.26  ? 123 TRP A HZ3  1 
ATOM   2318 H HH2  A TRP A 1 123 ? 34.141 6.403  25.813 0.520 24.94  ? 123 TRP A HH2  1 
ATOM   2319 H HH2  B TRP A 1 123 ? 34.131 5.939  24.842 0.480 26.59  ? 123 TRP A HH2  1 
ATOM   2320 N N    . ILE A 1 124 ? 26.284 3.047  27.987 1.000 15.32  ? 124 ILE A N    1 
ATOM   2321 C CA   . ILE A 1 124 ? 25.188 3.408  28.881 1.000 15.48  ? 124 ILE A CA   1 
ATOM   2322 C C    . ILE A 1 124 ? 25.208 2.555  30.158 1.000 16.78  ? 124 ILE A C    1 
ATOM   2323 O O    . ILE A 1 124 ? 24.380 2.759  31.028 1.000 17.64  ? 124 ILE A O    1 
ATOM   2324 C CB   . ILE A 1 124 ? 23.805 3.367  28.216 1.000 17.61  ? 124 ILE A CB   1 
ATOM   2325 C CG1  . ILE A 1 124 ? 23.403 1.959  27.805 1.000 19.86  ? 124 ILE A CG1  1 
ATOM   2326 C CG2  . ILE A 1 124 ? 23.798 4.340  27.051 1.000 20.51  ? 124 ILE A CG2  1 
ATOM   2327 C CD1  . ILE A 1 124 ? 21.949 1.904  27.371 1.000 35.06  ? 124 ILE A CD1  1 
ATOM   2328 H H    A ILE A 1 124 ? 26.301 2.269  27.622 1.000 18.38  ? 124 ILE A H    1 
ATOM   2329 H HA   . ILE A 1 124 ? 25.342 4.335  29.158 1.000 18.58  ? 124 ILE A HA   1 
ATOM   2330 H HB   . ILE A 1 124 ? 23.149 3.684  28.872 1.000 21.14  ? 124 ILE A HB   1 
ATOM   2331 H HG12 . ILE A 1 124 ? 23.968 1.664  27.075 1.000 23.83  ? 124 ILE A HG12 1 
ATOM   2332 H HG13 . ILE A 1 124 ? 23.538 1.355  28.552 1.000 23.83  ? 124 ILE A HG13 1 
ATOM   2333 H HG21 . ILE A 1 124 ? 24.057 5.211  27.360 1.000 30.77  ? 124 ILE A HG21 1 
ATOM   2334 H HG22 . ILE A 1 124 ? 24.416 4.041  26.381 1.000 30.77  ? 124 ILE A HG22 1 
ATOM   2335 H HG23 . ILE A 1 124 ? 22.915 4.383  26.675 1.000 30.77  ? 124 ILE A HG23 1 
ATOM   2336 H HD11 . ILE A 1 124 ? 21.724 1.006  27.118 1.000 52.59  ? 124 ILE A HD11 1 
ATOM   2337 H HD12 . ILE A 1 124 ? 21.387 2.182  28.098 1.000 52.59  ? 124 ILE A HD12 1 
ATOM   2338 H HD13 . ILE A 1 124 ? 21.816 2.490  26.622 1.000 52.59  ? 124 ILE A HD13 1 
ATOM   2339 N N    . ARG A 1 125 ? 26.087 1.614  30.264 1.000 18.32  ? 125 ARG A N    1 
ATOM   2340 C CA   . ARG A 1 125 ? 26.184 0.700  31.404 1.000 19.09  ? 125 ARG A CA   1 
ATOM   2341 C C    . ARG A 1 125 ? 26.436 1.509  32.672 1.000 20.91  ? 125 ARG A C    1 
ATOM   2342 O O    . ARG A 1 125 ? 27.292 2.375  32.732 1.000 25.38  ? 125 ARG A O    1 
ATOM   2343 C CB   . ARG A 1 125 ? 27.254 -0.339 31.164 1.000 23.30  ? 125 ARG A CB   1 
ATOM   2344 C CG   . ARG A 1 125 ? 27.170 -1.458 32.197 1.000 29.22  ? 125 ARG A CG   1 
ATOM   2345 C CD   . ARG A 1 125 ? 28.278 -2.466 31.932 1.000 40.67  ? 125 ARG A CD   1 
ATOM   2346 N NE   . ARG A 1 125 ? 28.109 -3.018 30.618 1.000 39.62  ? 125 ARG A NE   1 
ATOM   2347 C CZ   . ARG A 1 125 ? 29.027 -3.265 29.713 1.000 44.50  ? 125 ARG A CZ   1 
ATOM   2348 N NH1  . ARG A 1 125 ? 30.323 -3.090 29.942 1.000 53.54  ? 125 ARG A NH1  1 
ATOM   2349 N NH2  . ARG A 1 125 ? 28.564 -3.716 28.550 1.000 44.26  ? 125 ARG A NH2  1 
ATOM   2350 H H    . ARG A 1 125 ? 26.652 1.518  29.623 1.000 21.98  ? 125 ARG A H    1 
ATOM   2351 H HA   . ARG A 1 125 ? 25.325 0.239  31.501 1.000 22.91  ? 125 ARG A HA   1 
ATOM   2352 H HB2  . ARG A 1 125 ? 27.149 -0.711 30.275 1.000 27.95  ? 125 ARG A HB2  1 
ATOM   2353 H HB3  . ARG A 1 125 ? 28.128 0.080  31.213 1.000 27.95  ? 125 ARG A HB3  1 
ATOM   2354 H HG2  . ARG A 1 125 ? 27.266 -1.090 33.090 1.000 35.06  ? 125 ARG A HG2  1 
ATOM   2355 H HG3  . ARG A 1 125 ? 26.306 -1.895 32.139 1.000 35.06  ? 125 ARG A HG3  1 
ATOM   2356 H HD2  . ARG A 1 125 ? 29.142 -2.030 31.998 1.000 48.80  ? 125 ARG A HD2  1 
ATOM   2357 H HD3  . ARG A 1 125 ? 28.243 -3.174 32.594 1.000 48.80  ? 125 ARG A HD3  1 
ATOM   2358 H HE   . ARG A 1 125 ? 27.302 -3.212 30.395 1.000 47.55  ? 125 ARG A HE   1 
ATOM   2359 H HH11 . ARG A 1 125 ? 30.589 -2.805 30.708 1.000 64.25  ? 125 ARG A HH11 1 
ATOM   2360 H HH12 . ARG A 1 125 ? 30.896 -3.263 29.324 1.000 64.25  ? 125 ARG A HH12 1 
ATOM   2361 H HH21 . ARG A 1 125 ? 27.718 -3.826 28.437 1.000 53.11  ? 125 ARG A HH21 1 
ATOM   2362 H HH22 . ARG A 1 125 ? 29.110 -3.899 27.911 1.000 53.11  ? 125 ARG A HH22 1 
ATOM   2363 N N    . GLY A 1 126 ? 25.683 1.190  33.721 1.000 24.00  ? 126 GLY A N    1 
ATOM   2364 C CA   . GLY A 1 126 ? 25.835 1.813  34.992 1.000 25.81  ? 126 GLY A CA   1 
ATOM   2365 C C    . GLY A 1 126 ? 25.020 3.110  35.115 1.000 26.04  ? 126 GLY A C    1 
ATOM   2366 O O    . GLY A 1 126 ? 24.900 3.677  36.173 1.000 38.19  ? 126 GLY A O    1 
ATOM   2367 H H    . GLY A 1 126 ? 25.080 0.584  33.628 1.000 28.80  ? 126 GLY A H    1 
ATOM   2368 H HA2  . GLY A 1 126 ? 25.552 1.195  35.684 1.000 30.98  ? 126 GLY A HA2  1 
ATOM   2369 H HA3  . GLY A 1 126 ? 26.773 2.013  35.137 1.000 30.98  ? 126 GLY A HA3  1 
ATOM   2370 N N    . CYS A 1 127 ? 24.411 3.644  34.058 1.000 21.84  ? 127 CYS A N    1 
ATOM   2371 C CA   . CYS A 1 127 ? 23.728 4.914  34.110 1.000 20.80  ? 127 CYS A CA   1 
ATOM   2372 C C    . CYS A 1 127 ? 22.293 4.813  34.563 1.000 27.35  ? 127 CYS A C    1 
ATOM   2373 O O    . CYS A 1 127 ? 21.632 3.811  34.298 1.000 32.34  ? 127 CYS A O    1 
ATOM   2374 C CB   . CYS A 1 127 ? 23.675 5.557  32.721 1.000 18.47  ? 127 CYS A CB   1 
ATOM   2375 S SG   . CYS A 1 127 ? 25.336 5.839  32.003 1.000 16.94  ? 127 CYS A SG   1 
ATOM   2376 H H    . CYS A 1 127 ? 24.425 3.214  33.314 1.000 26.21  ? 127 CYS A H    1 
ATOM   2377 H HA   . CYS A 1 127 ? 24.212 5.510  34.718 1.000 24.96  ? 127 CYS A HA   1 
ATOM   2378 H HB2  . CYS A 1 127 ? 23.167 4.985  32.127 1.000 22.16  ? 127 CYS A HB2  1 
ATOM   2379 H HB3  . CYS A 1 127 ? 23.210 6.406  32.784 1.000 22.16  ? 127 CYS A HB3  1 
ATOM   2380 N N    . ARG A 1 128 ? 21.722 5.823  35.191 1.000 29.75  ? 128 ARG A N    1 
ATOM   2381 C CA   . ARG A 1 128 ? 20.315 5.863  35.593 1.000 33.33  ? 128 ARG A CA   1 
ATOM   2382 C C    . ARG A 1 128 ? 19.474 6.340  34.436 1.000 37.09  ? 128 ARG A C    1 
ATOM   2383 O O    . ARG A 1 128 ? 19.628 7.431  33.896 1.000 39.18  ? 128 ARG A O    1 
ATOM   2384 C CB   . ARG A 1 128 ? 20.180 6.790  36.802 1.000 42.71  ? 128 ARG A CB   1 
ATOM   2385 C CG   . ARG A 1 128 ? 20.624 6.245  38.163 1.000 57.56  ? 128 ARG A CG   1 
ATOM   2386 C CD   . ARG A 1 128 ? 21.558 7.176  38.940 1.000 67.10  ? 128 ARG A CD   1 
ATOM   2387 N NE   . ARG A 1 128 ? 21.624 6.971  40.383 1.000 55.58  ? 128 ARG A NE   1 
ATOM   2388 C CZ   . ARG A 1 128 ? 21.380 7.860  41.330 1.000 56.12  ? 128 ARG A CZ   1 
ATOM   2389 N NH1  . ARG A 1 128 ? 20.677 8.982  41.115 1.000 65.09  ? 128 ARG A NH1  1 
ATOM   2390 N NH2  . ARG A 1 128 ? 21.805 7.670  42.589 1.000 60.71  ? 128 ARG A NH2  1 
ATOM   2391 H H    . ARG A 1 128 ? 22.210 6.506  35.378 1.000 35.70  ? 128 ARG A H    1 
ATOM   2392 H HA   . ARG A 1 128 ? 20.028 4.961  35.847 1.000 39.99  ? 128 ARG A HA   1 
ATOM   2393 H HB2  . ARG A 1 128 ? 20.692 7.594  36.621 1.000 51.25  ? 128 ARG A HB2  1 
ATOM   2394 H HB3  . ARG A 1 128 ? 19.249 7.053  36.875 1.000 51.25  ? 128 ARG A HB3  1 
ATOM   2395 H HG2  . ARG A 1 128 ? 19.836 6.074  38.702 1.000 69.07  ? 128 ARG A HG2  1 
ATOM   2396 H HG3  . ARG A 1 128 ? 21.075 5.397  38.026 1.000 69.07  ? 128 ARG A HG3  1 
ATOM   2397 H HD2  . ARG A 1 128 ? 22.453 7.078  38.578 1.000 80.51  ? 128 ARG A HD2  1 
ATOM   2398 H HD3  . ARG A 1 128 ? 21.278 8.090  38.776 1.000 80.51  ? 128 ARG A HD3  1 
ATOM   2399 H HE   . ARG A 1 128 ? 21.847 6.184  40.646 1.000 66.70  ? 128 ARG A HE   1 
ATOM   2400 H HH11 . ARG A 1 128 ? 20.362 9.148  40.332 1.000 78.10  ? 128 ARG A HH11 1 
ATOM   2401 H HH12 . ARG A 1 128 ? 20.540 9.534  41.759 1.000 78.10  ? 128 ARG A HH12 1 
ATOM   2402 H HH21 . ARG A 1 128 ? 22.245 6.960  42.792 1.000 72.85  ? 128 ARG A HH21 1 
ATOM   2403 H HH22 . ARG A 1 128 ? 21.637 8.259  43.193 1.000 72.85  ? 128 ARG A HH22 1 
ATOM   2404 N N    . LEU A 1 129 ? 18.496 5.613  33.887 1.000 39.98  ? 129 LEU A N    1 
ATOM   2405 C CA   . LEU A 1 129 ? 18.017 6.252  32.653 1.000 41.55  ? 129 LEU A CA   1 
ATOM   2406 C C    . LEU A 1 129 ? 16.575 6.685  32.623 1.000 58.94  ? 129 LEU A C    1 
ATOM   2407 O O    . LEU A 1 129 ? 16.270 7.552  31.760 1.000 74.96  ? 129 LEU A O    1 
ATOM   2408 C CB   . LEU A 1 129 ? 18.348 5.281  31.494 1.000 33.87  ? 129 LEU A CB   1 
ATOM   2409 C CG   . LEU A 1 129 ? 19.768 5.398  30.994 1.000 27.65  ? 129 LEU A CG   1 
ATOM   2410 C CD1  . LEU A 1 129 ? 19.976 4.395  29.852 1.000 58.39  ? 129 LEU A CD1  1 
ATOM   2411 C CD2  . LEU A 1 129 ? 20.215 6.761  30.501 1.000 38.84  ? 129 LEU A CD2  1 
ATOM   2412 O OXT  . LEU A 1 129 ? 15.816 6.164  33.454 1.000 56.44  ? 129 LEU A OXT  1 
ATOM   2413 H H    . LEU A 1 129 ? 18.189 4.878  34.210 1.000 47.98  ? 129 LEU A H    1 
ATOM   2414 H HA   . LEU A 1 129 ? 18.561 7.056  32.517 1.000 49.86  ? 129 LEU A HA   1 
ATOM   2415 H HB2  . LEU A 1 129 ? 18.195 4.372  31.794 1.000 40.64  ? 129 LEU A HB2  1 
ATOM   2416 H HB3  . LEU A 1 129 ? 17.741 5.455  30.758 1.000 40.64  ? 129 LEU A HB3  1 
ATOM   2417 H HG   . LEU A 1 129 ? 20.363 5.139  31.728 1.000 33.19  ? 129 LEU A HG   1 
ATOM   2418 H HD11 . LEU A 1 129 ? 20.877 4.462  29.527 1.000 87.59  ? 129 LEU A HD11 1 
ATOM   2419 H HD12 . LEU A 1 129 ? 19.818 3.505  30.175 1.000 87.59  ? 129 LEU A HD12 1 
ATOM   2420 H HD13 . LEU A 1 129 ? 19.364 4.590  29.139 1.000 87.59  ? 129 LEU A HD13 1 
ATOM   2421 H HD21 . LEU A 1 129 ? 21.128 6.713  30.211 1.000 58.26  ? 129 LEU A HD21 1 
ATOM   2422 H HD22 . LEU A 1 129 ? 19.660 7.034  29.767 1.000 58.26  ? 129 LEU A HD22 1 
ATOM   2423 H HD23 . LEU A 1 129 ? 20.139 7.400  31.214 1.000 58.26  ? 129 LEU A HD23 1 
HETATM 2424 N N    . NO3 B 2 .   ? 25.870 29.980 11.534 1.000 15.87  ? 201 NO3 A N    1 
HETATM 2425 O O1   . NO3 B 2 .   ? 26.155 31.008 10.875 1.000 23.64  ? 201 NO3 A O1   1 
HETATM 2426 O O2   . NO3 B 2 .   ? 26.773 29.104 11.784 1.000 22.43  ? 201 NO3 A O2   1 
HETATM 2427 O O3   . NO3 B 2 .   ? 24.760 29.767 11.869 1.000 20.13  ? 201 NO3 A O3   1 
HETATM 2428 N N    . NO3 C 2 .   ? 22.847 13.279 -3.443 0.680 24.00  ? 202 NO3 A N    1 
HETATM 2429 O O1   . NO3 C 2 .   ? 21.987 13.295 -2.555 0.680 31.52  ? 202 NO3 A O1   1 
HETATM 2430 O O2   . NO3 C 2 .   ? 23.215 12.178 -3.903 0.680 39.04  ? 202 NO3 A O2   1 
HETATM 2431 O O3   . NO3 C 2 .   ? 23.373 14.260 -3.921 0.680 24.93  ? 202 NO3 A O3   1 
HETATM 2432 N N    . NO3 D 2 .   ? 18.754 18.688 26.554 0.736 33.17  ? 203 NO3 A N    1 
HETATM 2433 O O1   . NO3 D 2 .   ? 19.946 19.029 26.611 0.736 29.26  ? 203 NO3 A O1   1 
HETATM 2434 O O2   . NO3 D 2 .   ? 17.994 19.121 25.657 0.736 40.04  ? 203 NO3 A O2   1 
HETATM 2435 O O3   . NO3 D 2 .   ? 18.329 17.905 27.403 0.736 38.75  ? 203 NO3 A O3   1 
HETATM 2436 N N    . NO3 E 2 .   ? 37.436 8.123  13.435 0.647 35.17  ? 204 NO3 A N    1 
HETATM 2437 O O1   . NO3 E 2 .   ? 37.168 8.860  12.493 0.647 43.15  ? 204 NO3 A O1   1 
HETATM 2438 O O2   . NO3 E 2 .   ? 38.236 7.174  13.298 0.647 35.62  ? 204 NO3 A O2   1 
HETATM 2439 O O3   . NO3 E 2 .   ? 36.898 8.357  14.527 0.647 42.85  ? 204 NO3 A O3   1 
HETATM 2440 N N    . NO3 F 2 .   ? 33.569 -0.737 8.213  0.730 17.56  ? 205 NO3 A N    1 
HETATM 2441 O O1   . NO3 F 2 .   ? 34.756 -0.604 7.932  0.730 31.15  ? 205 NO3 A O1   1 
HETATM 2442 O O2   . NO3 F 2 .   ? 33.132 -1.777 8.513  0.730 17.20  ? 205 NO3 A O2   1 
HETATM 2443 O O3   . NO3 F 2 .   ? 32.813 0.253  8.190  0.730 30.62  ? 205 NO3 A O3   1 
HETATM 2444 N N    . NO3 G 2 .   ? 11.010 12.641 28.844 1.000 59.94  ? 206 NO3 A N    1 
HETATM 2445 O O1   . NO3 G 2 .   ? 10.710 12.749 27.649 1.000 43.99  ? 206 NO3 A O1   1 
HETATM 2446 O O2   . NO3 G 2 .   ? 11.523 11.552 29.244 1.000 63.01  ? 206 NO3 A O2   1 
HETATM 2447 O O3   . NO3 G 2 .   ? 10.865 13.530 29.742 1.000 47.81  ? 206 NO3 A O3   1 
HETATM 2448 N N    . NO3 H 2 .   ? 22.377 0.156  24.286 0.589 23.69  ? 207 NO3 A N    1 
HETATM 2449 O O1   . NO3 H 2 .   ? 21.940 -0.820 24.926 0.589 27.18  ? 207 NO3 A O1   1 
HETATM 2450 O O2   . NO3 H 2 .   ? 23.373 0.351  23.639 0.589 27.03  ? 207 NO3 A O2   1 
HETATM 2451 O O3   . NO3 H 2 .   ? 21.655 1.143  24.284 0.589 21.67  ? 207 NO3 A O3   1 
HETATM 2452 N N    . NO3 I 2 .   ? 36.508 30.825 9.437  0.417 22.29  ? 208 NO3 A N    1 
HETATM 2453 O O1   . NO3 I 2 .   ? 37.388 30.065 9.004  0.417 30.38  ? 208 NO3 A O1   1 
HETATM 2454 O O2   . NO3 I 2 .   ? 35.562 30.333 10.047 0.417 22.73  ? 208 NO3 A O2   1 
HETATM 2455 O O3   . NO3 I 2 .   ? 36.487 32.051 9.296  0.417 25.73  ? 208 NO3 A O3   1 
HETATM 2456 N N    . NO3 J 2 .   ? 26.899 15.623 8.846  0.645 16.35  ? 209 NO3 A N    1 
HETATM 2457 O O1   . NO3 J 2 .   ? 26.399 14.702 8.175  0.645 59.84  ? 209 NO3 A O1   1 
HETATM 2458 O O2   . NO3 J 2 .   ? 28.050 15.722 9.006  0.645 27.11  ? 209 NO3 A O2   1 
HETATM 2459 O O3   . NO3 J 2 .   ? 26.085 16.445 9.313  0.645 57.03  ? 209 NO3 A O3   1 
HETATM 2460 C C    . ACT K 3 .   ? 38.669 18.808 4.555  0.379 25.01  ? 210 ACT A C    1 
HETATM 2461 O O    . ACT K 3 .   ? 37.929 19.154 3.564  0.379 22.65  ? 210 ACT A O    1 
HETATM 2462 O OXT  . ACT K 3 .   ? 39.283 19.353 5.538  0.379 16.87  ? 210 ACT A OXT  1 
HETATM 2463 C CH3  . ACT K 3 .   ? 38.795 17.251 4.583  0.379 31.32  ? 210 ACT A CH3  1 
HETATM 2464 H H1   . ACT K 3 .   ? 38.324 16.878 3.834  0.379 46.97  ? 210 ACT A H1   1 
HETATM 2465 H H2   . ACT K 3 .   ? 39.721 17.003 4.534  0.379 46.97  ? 210 ACT A H2   1 
HETATM 2466 H H3   . ACT K 3 .   ? 38.416 16.914 5.399  0.379 46.97  ? 210 ACT A H3   1 
HETATM 2467 O O    . HOH L 4 .   ? 12.539 8.185  10.252 0.804 34.13  ? 301 HOH A O    1 
HETATM 2468 O O    . HOH L 4 .   ? 26.630 13.088 9.835  0.638 29.67  ? 302 HOH A O    1 
HETATM 2469 O O    . HOH L 4 .   ? 37.716 24.703 15.664 0.729 57.74  ? 303 HOH A O    1 
HETATM 2470 O O    . HOH L 4 .   ? 18.449 4.807  8.220  0.964 51.38  ? 304 HOH A O    1 
HETATM 2471 O O    . HOH L 4 .   ? 32.090 26.861 19.374 1.000 33.20  ? 305 HOH A O    1 
HETATM 2472 O O    . HOH L 4 .   ? 29.023 31.717 9.805  0.771 30.62  ? 306 HOH A O    1 
HETATM 2473 O O    . HOH L 4 .   ? 30.410 29.534 11.888 0.978 25.54  ? 307 HOH A O    1 
HETATM 2474 O O    . HOH L 4 .   ? 17.610 -0.642 19.788 1.000 29.38  ? 308 HOH A O    1 
HETATM 2475 O O    . HOH L 4 .   ? 31.945 23.435 25.831 1.000 19.37  ? 309 HOH A O    1 
HETATM 2476 O O    . HOH L 4 .   ? 38.890 18.288 8.277  0.564 45.79  ? 310 HOH A O    1 
HETATM 2477 O O    . HOH L 4 .   ? 37.436 9.596  16.724 1.000 29.92  ? 311 HOH A O    1 
HETATM 2478 O O    . HOH L 4 .   ? 33.622 13.850 11.945 0.620 23.18  ? 312 HOH A O    1 
HETATM 2479 O O    . HOH L 4 .   ? 26.220 20.750 20.176 1.000 13.04  ? 313 HOH A O    1 
HETATM 2480 O O    . HOH L 4 .   ? 35.956 1.910  19.947 0.679 44.13  ? 314 HOH A O    1 
HETATM 2481 O O    . HOH L 4 .   ? 34.572 16.366 8.410  1.000 87.23  ? 315 HOH A O    1 
HETATM 2482 O O    . HOH L 4 .   ? 34.474 16.584 12.554 1.000 20.28  ? 316 HOH A O    1 
HETATM 2483 O O    . HOH L 4 .   ? 22.252 20.885 28.693 1.000 31.99  ? 317 HOH A O    1 
HETATM 2484 O O    . HOH L 4 .   ? 28.422 25.804 27.438 1.000 47.15  ? 318 HOH A O    1 
HETATM 2485 O O    . HOH L 4 .   ? 24.755 22.068 32.724 1.000 44.45  ? 319 HOH A O    1 
HETATM 2486 O O    . HOH L 4 .   ? 27.581 11.956 6.395  0.502 38.99  ? 320 HOH A O    1 
HETATM 2487 O O    . HOH L 4 .   ? 41.816 18.896 4.329  1.000 17.04  ? 321 HOH A O    1 
HETATM 2488 O O    . HOH L 4 .   ? 18.847 22.976 20.865 1.000 26.63  ? 322 HOH A O    1 
HETATM 2489 O O    . HOH L 4 .   ? 21.200 26.981 2.277  1.000 45.52  ? 323 HOH A O    1 
HETATM 2490 O O    . HOH L 4 .   ? 32.309 1.038  21.946 1.000 32.00  ? 324 HOH A O    1 
HETATM 2491 O O    . HOH L 4 .   ? 27.230 25.148 24.052 1.000 19.16  ? 325 HOH A O    1 
HETATM 2492 O O    . HOH L 4 .   ? 25.315 20.119 -2.118 1.000 24.74  ? 326 HOH A O    1 
HETATM 2493 O O    . HOH L 4 .   ? 30.563 15.235 9.938  0.777 46.70  ? 327 HOH A O    1 
HETATM 2494 O O    . HOH L 4 .   ? 23.896 20.636 21.639 1.000 18.58  ? 328 HOH A O    1 
HETATM 2495 O O    . HOH L 4 .   ? 33.918 28.496 4.096  1.000 73.88  ? 329 HOH A O    1 
HETATM 2496 O O    . HOH L 4 .   ? 11.773 2.874  17.083 0.563 26.79  ? 330 HOH A O    1 
HETATM 2497 O O    . HOH L 4 .   ? 38.185 10.970 23.954 1.000 44.08  ? 331 HOH A O    1 
HETATM 2498 O O    . HOH L 4 .   ? 28.406 18.762 32.203 1.000 15.05  ? 332 HOH A O    1 
HETATM 2499 O O    . HOH L 4 .   ? 31.867 26.635 6.797  1.000 12.14  ? 333 HOH A O    1 
HETATM 2500 O O    . HOH L 4 .   ? 19.135 0.943  25.352 0.576 32.30  ? 334 HOH A O    1 
HETATM 2501 O O    . HOH L 4 .   ? 23.523 23.352 4.250  1.000 15.11  ? 335 HOH A O    1 
HETATM 2502 O O    . HOH L 4 .   ? 23.671 -0.697 33.566 0.643 37.58  ? 336 HOH A O    1 
HETATM 2503 O O    . HOH L 4 .   ? 35.473 17.552 25.346 0.271 18.77  ? 337 HOH A O    1 
HETATM 2504 O O    . HOH L 4 .   ? 27.035 17.749 4.426  0.690 14.30  ? 338 HOH A O    1 
HETATM 2505 O O    . HOH L 4 .   ? 17.146 -0.101 22.330 0.551 22.77  ? 339 HOH A O    1 
HETATM 2506 O O    . HOH L 4 .   ? 25.959 28.021 -0.782 0.753 34.91  ? 340 HOH A O    1 
HETATM 2507 O O    . HOH L 4 .   ? 13.711 15.733 12.762 0.620 26.35  ? 341 HOH A O    1 
HETATM 2508 O O    . HOH L 4 .   ? 20.885 -0.977 17.513 1.000 17.95  ? 342 HOH A O    1 
HETATM 2509 O O    . HOH L 4 .   ? 35.754 14.394 15.088 0.688 48.17  ? 343 HOH A O    1 
HETATM 2510 O O    . HOH L 4 .   ? 12.969 7.588  6.258  0.370 24.45  ? 344 HOH A O    1 
HETATM 2511 O O    . HOH L 4 .   ? 38.086 28.759 16.662 0.774 50.05  ? 345 HOH A O    1 
HETATM 2512 O O    . HOH L 4 .   ? 19.584 25.261 19.671 1.000 18.96  ? 346 HOH A O    1 
HETATM 2513 O O    . HOH L 4 .   ? 20.780 14.799 31.427 1.000 22.28  ? 347 HOH A O    1 
HETATM 2514 O O    . HOH L 4 .   ? 38.747 2.420  12.906 1.000 24.73  ? 348 HOH A O    1 
HETATM 2515 O O    . HOH L 4 .   ? 23.315 27.399 24.801 0.512 45.93  ? 349 HOH A O    1 
HETATM 2516 O O    . HOH L 4 .   ? 35.841 18.643 21.499 0.673 28.94  ? 350 HOH A O    1 
HETATM 2517 O O    . HOH L 4 .   ? 15.756 16.887 28.004 1.000 62.91  ? 351 HOH A O    1 
HETATM 2518 O O    . HOH L 4 .   ? 21.904 9.141  33.607 0.839 37.06  ? 352 HOH A O    1 
HETATM 2519 O O    . HOH L 4 .   ? 38.583 10.457 18.511 1.000 60.76  ? 353 HOH A O    1 
HETATM 2520 O O    . HOH L 4 .   ? 26.247 28.241 2.969  1.000 18.92  ? 354 HOH A O    1 
HETATM 2521 O O    . HOH L 4 .   ? 14.595 7.217  23.788 1.000 18.80  ? 355 HOH A O    1 
HETATM 2522 O O    . HOH L 4 .   ? 20.450 18.708 29.407 1.000 48.77  ? 356 HOH A O    1 
HETATM 2523 O O    . HOH L 4 .   ? 24.157 17.575 32.299 1.000 18.35  ? 357 HOH A O    1 
HETATM 2524 O O    . HOH L 4 .   ? 17.232 20.847 14.296 1.000 20.73  ? 358 HOH A O    1 
HETATM 2525 O O    . HOH L 4 .   ? 15.915 20.011 12.097 1.000 23.15  ? 359 HOH A O    1 
HETATM 2526 O O    . HOH L 4 .   ? 25.763 18.433 16.516 1.000 9.78   ? 360 HOH A O    1 
HETATM 2527 O O    . HOH L 4 .   ? 14.596 26.191 4.166  0.669 51.04  ? 361 HOH A O    1 
HETATM 2528 O O    . HOH L 4 .   ? 31.159 12.223 9.935  1.000 42.87  ? 362 HOH A O    1 
HETATM 2529 O O    . HOH L 4 .   ? 13.727 20.110 7.525  1.000 35.26  ? 363 HOH A O    1 
HETATM 2530 O O    . HOH L 4 .   ? 36.969 11.462 21.496 0.459 23.18  ? 364 HOH A O    1 
HETATM 2531 O O    . HOH L 4 .   ? 22.075 21.358 19.590 1.000 16.73  ? 365 HOH A O    1 
HETATM 2532 O O    . HOH L 4 .   ? 12.455 5.207  22.661 1.000 52.45  ? 366 HOH A O    1 
HETATM 2533 O O    . HOH L 4 .   ? 23.011 31.039 9.250  0.637 25.89  ? 367 HOH A O    1 
HETATM 2534 O O    . HOH L 4 .   ? 25.812 26.264 5.029  1.000 12.89  ? 368 HOH A O    1 
HETATM 2535 O O    . HOH L 4 .   ? 38.871 23.450 12.977 1.000 30.10  ? 369 HOH A O    1 
HETATM 2536 O O    . HOH L 4 .   ? 21.670 29.956 17.326 0.603 21.71  ? 370 HOH A O    1 
HETATM 2537 O O    . HOH L 4 .   ? 35.765 25.757 6.713  1.000 21.90  ? 371 HOH A O    1 
HETATM 2538 O O    . HOH L 4 .   ? 27.779 -2.925 17.497 1.000 44.52  ? 372 HOH A O    1 
HETATM 2539 O O    . HOH L 4 .   ? 30.751 21.778 30.934 1.000 19.03  ? 373 HOH A O    1 
HETATM 2540 O O    . HOH L 4 .   ? 23.571 7.947  36.109 0.872 31.02  ? 374 HOH A O    1 
HETATM 2541 O O    . HOH L 4 .   ? 26.695 16.518 31.799 1.000 13.10  ? 375 HOH A O    1 
HETATM 2542 O O    . HOH L 4 .   ? 31.288 10.987 32.147 1.000 33.44  ? 376 HOH A O    1 
HETATM 2543 O O    . HOH L 4 .   ? 31.161 18.797 3.016  1.000 26.68  ? 377 HOH A O    1 
HETATM 2544 O O    . HOH L 4 .   ? 34.999 0.251  16.010 0.571 20.91  ? 378 HOH A O    1 
HETATM 2545 O O    . HOH L 4 .   ? 38.696 27.813 7.499  0.937 44.99  ? 379 HOH A O    1 
HETATM 2546 O O    . HOH L 4 .   ? 36.332 22.683 18.578 0.746 30.98  ? 380 HOH A O    1 
HETATM 2547 O O    . HOH L 4 .   ? 11.979 19.642 19.461 0.710 56.90  ? 381 HOH A O    1 
HETATM 2548 O O    . HOH L 4 .   ? 38.823 9.042  25.917 1.000 38.79  ? 382 HOH A O    1 
HETATM 2549 O O    . HOH L 4 .   ? 32.795 -0.603 24.203 0.432 35.95  ? 383 HOH A O    1 
HETATM 2550 O O    . HOH L 4 .   ? 18.953 27.749 3.538  1.000 48.15  ? 384 HOH A O    1 
HETATM 2551 O O    . HOH L 4 .   ? 35.805 27.833 17.574 1.000 50.43  ? 385 HOH A O    1 
HETATM 2552 O O    . HOH L 4 .   ? 11.809 15.218 16.845 1.000 60.12  ? 386 HOH A O    1 
HETATM 2553 O O    . HOH L 4 .   ? 22.250 28.181 19.787 0.306 18.95  ? 387 HOH A O    1 
HETATM 2554 O O    . HOH L 4 .   ? 15.365 22.031 15.946 1.000 26.61  ? 388 HOH A O    1 
HETATM 2555 O O    . HOH L 4 .   ? 33.473 23.316 -2.344 1.000 72.06  ? 389 HOH A O    1 
HETATM 2556 O O    . HOH L 4 .   ? 34.109 -3.414 22.269 0.426 17.17  ? 390 HOH A O    1 
HETATM 2557 O O    . HOH L 4 .   ? 38.064 16.471 8.642  0.521 47.82  ? 391 HOH A O    1 
HETATM 2558 O O    . HOH L 4 .   ? 39.969 21.109 14.341 1.000 47.18  ? 392 HOH A O    1 
HETATM 2559 O O    . HOH L 4 .   ? 17.536 13.597 1.155  1.000 17.23  ? 393 HOH A O    1 
HETATM 2560 O O    . HOH L 4 .   ? 12.995 21.149 10.356 1.000 35.19  ? 394 HOH A O    1 
HETATM 2561 O O    . HOH L 4 .   ? 27.655 16.221 2.277  1.000 46.44  ? 395 HOH A O    1 
HETATM 2562 O O    . HOH L 4 .   ? 38.600 15.476 28.106 1.000 60.20  ? 396 HOH A O    1 
HETATM 2563 O O    . HOH L 4 .   ? 39.481 4.338  14.610 1.000 33.21  ? 397 HOH A O    1 
HETATM 2564 O O    . HOH L 4 .   ? 21.020 11.224 -0.020 0.385 34.90  ? 398 HOH A O    1 
HETATM 2565 O O    . HOH L 4 .   ? 19.656 13.461 33.795 0.785 92.12  ? 399 HOH A O    1 
HETATM 2566 O O    . HOH L 4 .   ? 37.240 15.619 11.602 0.568 48.31  ? 400 HOH A O    1 
HETATM 2567 O O    . HOH L 4 .   ? 28.411 21.952 32.860 1.000 60.55  ? 401 HOH A O    1 
HETATM 2568 O O    . HOH L 4 .   ? 12.440 5.041  5.163  1.000 122.88 ? 402 HOH A O    1 
HETATM 2569 O O    . HOH L 4 .   ? 38.253 20.720 -1.121 1.000 29.94  ? 403 HOH A O    1 
HETATM 2570 O O    . HOH L 4 .   ? 38.382 3.297  6.759  0.934 49.88  ? 404 HOH A O    1 
HETATM 2571 O O    . HOH L 4 .   ? 40.782 24.922 11.627 1.000 29.82  ? 405 HOH A O    1 
HETATM 2572 O O    . HOH L 4 .   ? 33.931 23.233 30.194 0.520 27.70  ? 406 HOH A O    1 
HETATM 2573 O O    . HOH L 4 .   ? 43.819 24.438 3.014  0.483 23.30  ? 407 HOH A O    1 
HETATM 2574 O O    . HOH L 4 .   ? 38.054 3.019  4.472  0.673 43.82  ? 408 HOH A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A LYS A 1   ? 0.1718 0.1656 0.1139 0.0079  -0.0096 0.0192  1   LYS A N   
2    N N   B LYS A 1   ? 0.2523 0.1233 0.1304 -0.0042 -0.0010 0.0070  1   LYS A N   
3    C CA  A LYS A 1   ? 0.1825 0.1464 0.1202 -0.0104 -0.0047 0.0143  1   LYS A CA  
4    C CA  B LYS A 1   ? 0.2238 0.1383 0.0967 0.0016  -0.0046 -0.0086 1   LYS A CA  
5    C C   A LYS A 1   ? 0.1817 0.1574 0.0828 -0.0012 -0.0023 0.0162  1   LYS A C   
6    C C   B LYS A 1   ? 0.1708 0.1265 0.0952 -0.0129 -0.0087 0.0029  1   LYS A C   
7    O O   A LYS A 1   ? 0.2031 0.1695 0.0765 -0.0218 -0.0078 0.0223  1   LYS A O   
8    O O   B LYS A 1   ? 0.2921 0.1532 0.0943 0.0606  -0.0293 -0.0048 1   LYS A O   
9    C CB  A LYS A 1   ? 0.1793 0.1419 0.0952 -0.0159 -0.0139 -0.0307 1   LYS A CB  
10   C CB  B LYS A 1   ? 0.2243 0.1779 0.1298 0.0347  0.0224  0.0018  1   LYS A CB  
11   C CG  A LYS A 1   ? 0.1766 0.1304 0.1149 -0.0338 -0.0144 -0.0376 1   LYS A CG  
12   C CG  B LYS A 1   ? 0.1811 0.1572 0.1077 -0.0099 -0.0250 -0.0199 1   LYS A CG  
13   C CD  A LYS A 1   ? 0.1785 0.1284 0.1175 -0.0012 -0.0151 -0.0057 1   LYS A CD  
14   C CD  B LYS A 1   ? 0.2010 0.2074 0.1746 -0.0106 0.0136  -0.0052 1   LYS A CD  
15   C CE  A LYS A 1   ? 0.1754 0.1442 0.1239 -0.0121 -0.0230 0.0083  1   LYS A CE  
16   C CE  B LYS A 1   ? 0.2000 0.1898 0.2064 -0.0227 0.0096  -0.0021 1   LYS A CE  
17   N NZ  A LYS A 1   ? 0.1676 0.1711 0.1252 -0.0092 -0.0237 0.0084  1   LYS A NZ  
18   N NZ  B LYS A 1   ? 0.2347 0.2090 0.2124 -0.0029 0.0501  0.0079  1   LYS A NZ  
49   N N   . VAL A 2   ? 0.1743 0.1374 0.0913 -0.0163 -0.0215 0.0029  2   VAL A N   
50   C CA  . VAL A 2   ? 0.1466 0.1347 0.0882 -0.0188 -0.0185 0.0014  2   VAL A CA  
51   C C   . VAL A 2   ? 0.1342 0.1354 0.0791 -0.0147 -0.0275 0.0038  2   VAL A C   
52   O O   . VAL A 2   ? 0.1595 0.1811 0.0744 -0.0414 -0.0232 -0.0021 2   VAL A O   
53   C CB  . VAL A 2   ? 0.1438 0.1793 0.1090 -0.0329 -0.0208 0.0226  2   VAL A CB  
54   C CG1 . VAL A 2   ? 0.1500 0.1977 0.1405 0.0002  -0.0090 0.0252  2   VAL A CG1 
55   C CG2 . VAL A 2   ? 0.1668 0.2215 0.2066 -0.0655 -0.0423 0.0775  2   VAL A CG2 
65   N N   . PHE A 3   ? 0.1350 0.1365 0.0753 -0.0191 -0.0223 0.0011  3   PHE A N   
66   C CA  . PHE A 3   ? 0.1236 0.1340 0.0779 -0.0157 -0.0205 -0.0085 3   PHE A CA  
67   C C   . PHE A 3   ? 0.1159 0.1375 0.0715 -0.0225 -0.0167 -0.0021 3   PHE A C   
68   O O   . PHE A 3   ? 0.1371 0.1714 0.0951 0.0005  0.0005  0.0162  3   PHE A O   
69   C CB  . PHE A 3   ? 0.1255 0.1506 0.0998 -0.0215 -0.0324 -0.0053 3   PHE A CB  
70   C CG  . PHE A 3   ? 0.1190 0.1496 0.0732 -0.0240 -0.0180 0.0002  3   PHE A CG  
71   C CD1 . PHE A 3   ? 0.1252 0.1900 0.1024 -0.0193 -0.0193 0.0335  3   PHE A CD1 
72   C CD2 . PHE A 3   ? 0.1405 0.1714 0.0858 -0.0294 -0.0059 0.0086  3   PHE A CD2 
73   C CE1 . PHE A 3   ? 0.1575 0.2044 0.1324 0.0048  -0.0382 0.0311  3   PHE A CE1 
74   C CE2 . PHE A 3   ? 0.1338 0.2140 0.1118 -0.0137 -0.0013 -0.0208 3   PHE A CE2 
75   C CZ  . PHE A 3   ? 0.1382 0.2172 0.1374 0.0151  -0.0325 -0.0089 3   PHE A CZ  
85   N N   . GLY A 4   ? 0.1341 0.1484 0.0759 -0.0273 -0.0137 0.0013  4   GLY A N   
86   C CA  . GLY A 4   ? 0.1288 0.1633 0.0855 -0.0235 -0.0242 0.0160  4   GLY A CA  
87   C C   . GLY A 4   ? 0.1128 0.1410 0.0822 -0.0055 -0.0210 0.0143  4   GLY A C   
88   O O   . GLY A 4   ? 0.1143 0.1382 0.1098 0.0021  -0.0299 -0.0014 4   GLY A O   
92   N N   A ARG A 5   ? 0.1349 0.1457 0.1128 0.0031  -0.0488 0.0176  5   ARG A N   
93   N N   B ARG A 5   ? 0.1256 0.1396 0.1175 0.0033  -0.0101 0.0300  5   ARG A N   
94   C CA  A ARG A 5   ? 0.1354 0.1241 0.1045 -0.0001 -0.0257 0.0270  5   ARG A CA  
95   C CA  B ARG A 5   ? 0.1300 0.1386 0.1324 0.0154  0.0014  0.0065  5   ARG A CA  
96   C C   A ARG A 5   ? 0.1346 0.1164 0.0949 0.0120  -0.0253 0.0201  5   ARG A C   
97   C C   B ARG A 5   ? 0.1208 0.1220 0.0951 0.0222  -0.0182 0.0069  5   ARG A C   
98   O O   A ARG A 5   ? 0.1245 0.1081 0.0914 0.0176  -0.0146 0.0003  5   ARG A O   
99   O O   B ARG A 5   ? 0.1402 0.1654 0.1156 0.0252  -0.0383 0.0087  5   ARG A O   
100  C CB  A ARG A 5   ? 0.1236 0.1419 0.1390 0.0031  -0.0445 0.0124  5   ARG A CB  
101  C CB  B ARG A 5   ? 0.0963 0.1664 0.1371 0.0242  -0.0385 -0.0111 5   ARG A CB  
102  C CG  A ARG A 5   ? 0.1511 0.1447 0.1442 0.0158  -0.0413 -0.0115 5   ARG A CG  
103  C CG  B ARG A 5   ? 0.1829 0.1259 0.1708 0.0215  -0.0405 -0.0059 5   ARG A CG  
104  C CD  A ARG A 5   ? 0.1764 0.1602 0.2465 0.0329  -0.0627 -0.0028 5   ARG A CD  
105  C CD  B ARG A 5   ? 0.2116 0.1203 0.2336 0.0311  -0.0506 -0.0188 5   ARG A CD  
106  N NE  A ARG A 5   ? 0.2473 0.1735 0.2534 0.0233  -0.1137 0.0163  5   ARG A NE  
107  N NE  B ARG A 5   ? 0.2192 0.1736 0.2547 0.0583  -0.0936 -0.0073 5   ARG A NE  
108  C CZ  A ARG A 5   ? 0.2703 0.1685 0.2172 0.0370  -0.0850 0.0024  5   ARG A CZ  
109  C CZ  B ARG A 5   ? 0.3194 0.1399 0.1965 0.0648  -0.0434 -0.0130 5   ARG A CZ  
110  N NH1 A ARG A 5   ? 0.2740 0.1775 0.2386 0.0065  -0.0785 0.0243  5   ARG A NH1 
111  N NH1 B ARG A 5   ? 0.4270 0.2020 0.2414 -0.0975 -0.0821 0.0717  5   ARG A NH1 
112  N NH2 A ARG A 5   ? 0.3824 0.2394 0.2120 0.0469  -0.0740 -0.0079 5   ARG A NH2 
113  N NH2 B ARG A 5   ? 0.3868 0.2529 0.2086 0.1329  -0.0308 0.0242  5   ARG A NH2 
140  N N   . CYS A 6   ? 0.1441 0.1291 0.0937 -0.0062 -0.0250 0.0100  6   CYS A N   
141  C CA  . CYS A 6   ? 0.1553 0.1178 0.0941 -0.0151 -0.0246 0.0188  6   CYS A CA  
142  C C   . CYS A 6   ? 0.1341 0.1304 0.0731 -0.0250 -0.0131 0.0027  6   CYS A C   
143  O O   . CYS A 6   ? 0.1358 0.1457 0.1165 -0.0221 -0.0158 0.0107  6   CYS A O   
144  C CB  . CYS A 6   ? 0.1938 0.1571 0.0893 -0.0203 -0.0201 0.0155  6   CYS A CB  
145  S SG  . CYS A 6   ? 0.2580 0.1734 0.1486 0.0146  -0.0346 0.0609  6   CYS A SG  
150  N N   . GLU A 7   ? 0.1297 0.1245 0.0799 -0.0094 -0.0167 0.0057  7   GLU A N   
151  C CA  . GLU A 7   ? 0.1236 0.1318 0.0818 -0.0083 0.0001  -0.0055 7   GLU A CA  
152  C C   . GLU A 7   ? 0.1113 0.1147 0.0828 -0.0045 -0.0049 -0.0068 7   GLU A C   
153  O O   . GLU A 7   ? 0.1155 0.1552 0.0913 0.0068  -0.0030 -0.0146 7   GLU A O   
154  C CB  . GLU A 7   ? 0.1491 0.1299 0.0923 -0.0117 -0.0190 -0.0124 7   GLU A CB  
155  C CG  . GLU A 7   ? 0.1673 0.1827 0.1034 -0.0070 -0.0287 -0.0244 7   GLU A CG  
156  C CD  . GLU A 7   ? 0.1492 0.1687 0.0879 -0.0212 -0.0172 -0.0087 7   GLU A CD  
157  O OE1 . GLU A 7   ? 0.1524 0.1971 0.0979 -0.0154 -0.0116 -0.0196 7   GLU A OE1 
158  O OE2 . GLU A 7   ? 0.2119 0.2307 0.0962 0.0033  -0.0186 -0.0154 7   GLU A OE2 
165  N N   . LEU A 8   ? 0.1072 0.1268 0.0742 -0.0009 -0.0100 -0.0001 8   LEU A N   
166  C CA  . LEU A 8   ? 0.1001 0.1175 0.0733 0.0016  -0.0167 -0.0001 8   LEU A CA  
167  C C   . LEU A 8   ? 0.0901 0.1313 0.0745 -0.0050 -0.0057 -0.0016 8   LEU A C   
168  O O   . LEU A 8   ? 0.0980 0.1377 0.0885 -0.0094 -0.0128 0.0050  8   LEU A O   
169  C CB  . LEU A 8   ? 0.1045 0.1294 0.0850 -0.0118 -0.0067 -0.0020 8   LEU A CB  
170  C CG  . LEU A 8   ? 0.1175 0.1470 0.0830 -0.0156 -0.0029 0.0035  8   LEU A CG  
171  C CD1 . LEU A 8   ? 0.1633 0.1735 0.0889 0.0095  -0.0097 0.0169  8   LEU A CD1 
172  C CD2 . LEU A 8   ? 0.1462 0.2516 0.1012 0.0324  0.0120  -0.0007 8   LEU A CD2 
184  N N   . ALA A 9   ? 0.1067 0.1228 0.0894 -0.0108 -0.0149 -0.0023 9   ALA A N   
185  C CA  . ALA A 9   ? 0.1145 0.1305 0.0927 -0.0098 -0.0031 -0.0109 9   ALA A CA  
186  C C   . ALA A 9   ? 0.1125 0.1210 0.0995 -0.0138 -0.0104 -0.0050 9   ALA A C   
187  O O   . ALA A 9   ? 0.1144 0.1398 0.1119 -0.0177 -0.0126 -0.0156 9   ALA A O   
188  C CB  . ALA A 9   ? 0.1413 0.1240 0.1260 -0.0072 -0.0170 -0.0076 9   ALA A CB  
194  N N   . ALA A 10  ? 0.1178 0.1465 0.0870 -0.0053 -0.0030 -0.0008 10  ALA A N   
195  C CA  . ALA A 10  ? 0.1191 0.1524 0.0969 -0.0207 0.0071  0.0045  10  ALA A CA  
196  C C   . ALA A 10  ? 0.1006 0.1501 0.0967 -0.0076 0.0103  -0.0153 10  ALA A C   
197  O O   . ALA A 10  ? 0.1113 0.1823 0.1242 -0.0165 0.0000  -0.0086 10  ALA A O   
198  C CB  . ALA A 10  ? 0.1467 0.2039 0.0979 0.0110  0.0126  -0.0020 10  ALA A CB  
204  N N   . ALA A 11  ? 0.1076 0.1357 0.0950 -0.0005 0.0026  -0.0129 11  ALA A N   
205  C CA  . ALA A 11  ? 0.1149 0.1419 0.0998 0.0089  0.0040  -0.0187 11  ALA A CA  
206  C C   . ALA A 11  ? 0.1001 0.1297 0.1057 0.0037  -0.0089 -0.0098 11  ALA A C   
207  O O   . ALA A 11  ? 0.1141 0.1568 0.1222 0.0184  -0.0164 -0.0150 11  ALA A O   
208  C CB  . ALA A 11  ? 0.1786 0.1264 0.1182 -0.0160 -0.0116 -0.0186 11  ALA A CB  
214  N N   . MET A 12  ? 0.0917 0.1301 0.0905 -0.0044 -0.0079 -0.0121 12  MET A N   
215  C CA  . MET A 12  ? 0.0958 0.1343 0.0951 -0.0031 -0.0123 -0.0088 12  MET A CA  
216  C C   . MET A 12  ? 0.1005 0.1463 0.1008 -0.0057 -0.0121 -0.0181 12  MET A C   
217  O O   . MET A 12  ? 0.1117 0.1887 0.1179 -0.0171 -0.0236 -0.0113 12  MET A O   
218  C CB  . MET A 12  ? 0.1018 0.1319 0.0872 -0.0043 -0.0091 -0.0142 12  MET A CB  
219  C CG  . MET A 12  ? 0.1094 0.1297 0.0886 -0.0033 -0.0009 -0.0075 12  MET A CG  
220  S SD  . MET A 12  ? 0.1186 0.1552 0.1235 0.0046  0.0067  -0.0194 12  MET A SD  
221  C CE  . MET A 12  ? 0.1539 0.2141 0.1924 -0.0374 0.0578  -0.0074 12  MET A CE  
231  N N   . LYS A 13  ? 0.1069 0.1399 0.1140 -0.0191 -0.0029 -0.0119 13  LYS A N   
232  C CA  . LYS A 13  ? 0.1073 0.1614 0.1380 -0.0229 0.0010  -0.0142 13  LYS A CA  
233  C C   . LYS A 13  ? 0.1082 0.1657 0.1240 -0.0196 0.0021  -0.0074 13  LYS A C   
234  O O   . LYS A 13  ? 0.1103 0.1870 0.1588 -0.0304 -0.0024 -0.0249 13  LYS A O   
235  C CB  . LYS A 13  ? 0.1495 0.1733 0.1790 -0.0275 -0.0047 0.0277  13  LYS A CB  
236  C CG  . LYS A 13  ? 0.1972 0.2320 0.2704 -0.0680 0.0205  0.0485  13  LYS A CG  
237  C CD  . LYS A 13  ? 0.3434 0.2901 0.4546 -0.1303 -0.0498 0.1926  13  LYS A CD  
238  C CE  . LYS A 13  ? 0.4357 0.4339 0.5926 -0.0812 0.1088  0.2822  13  LYS A CE  
239  N NZ  . LYS A 13  ? 0.6102 0.5277 0.9305 0.0245  0.3672  0.2679  13  LYS A NZ  
253  N N   . ARG A 14  ? 0.0979 0.1666 0.1244 -0.0066 -0.0050 -0.0189 14  ARG A N   
254  C CA  . ARG A 14  ? 0.1065 0.1957 0.1306 -0.0010 0.0151  -0.0201 14  ARG A CA  
255  C C   . ARG A 14  ? 0.1057 0.1899 0.1412 0.0131  0.0045  -0.0093 14  ARG A C   
256  O O   . ARG A 14  ? 0.1081 0.3138 0.1719 0.0387  0.0050  0.0075  14  ARG A O   
257  C CB  . ARG A 14  ? 0.1476 0.2042 0.1509 0.0195  0.0129  -0.0432 14  ARG A CB  
258  C CG  . ARG A 14  ? 0.1775 0.3117 0.1443 0.0067  0.0119  -0.0362 14  ARG A CG  
259  C CD  . ARG A 14  ? 0.2144 0.3891 0.1768 0.0492  -0.0007 -0.1091 14  ARG A CD  
260  N NE  . ARG A 14  ? 0.2249 0.4411 0.2887 0.0189  -0.0028 -0.2322 14  ARG A NE  
261  C CZ  . ARG A 14  ? 0.2463 0.4996 0.3449 0.0452  -0.0457 -0.3045 14  ARG A CZ  
262  N NH1 . ARG A 14  ? 0.3358 0.7563 0.3326 0.1021  -0.0709 -0.1846 14  ARG A NH1 
263  N NH2 . ARG A 14  ? 0.2158 0.5703 0.5233 0.0183  0.0013  -0.3859 14  ARG A NH2 
277  N N   A HIS A 15  ? 0.0990 0.1414 0.1266 0.0278  -0.0066 -0.0083 15  HIS A N   
278  N N   B HIS A 15  ? 0.1170 0.1979 0.1293 0.0036  0.0128  -0.0075 15  HIS A N   
279  C CA  A HIS A 15  ? 0.1543 0.1837 0.1333 0.0203  -0.0233 0.0042  15  HIS A CA  
280  C CA  B HIS A 15  ? 0.1332 0.1807 0.1427 0.0244  0.0036  0.0010  15  HIS A CA  
281  C C   A HIS A 15  ? 0.1406 0.2143 0.1457 0.0332  -0.0469 -0.0137 15  HIS A C   
282  C C   B HIS A 15  ? 0.1490 0.2148 0.1392 0.0344  -0.0194 -0.0092 15  HIS A C   
283  O O   A HIS A 15  ? 0.2423 0.2759 0.1574 0.0148  -0.0881 -0.0067 15  HIS A O   
284  O O   B HIS A 15  ? 0.2476 0.2882 0.1348 0.0398  -0.0286 -0.0118 15  HIS A O   
285  C CB  A HIS A 15  ? 0.1713 0.2169 0.1297 0.0056  -0.0236 0.0271  15  HIS A CB  
286  C CB  B HIS A 15  ? 0.1662 0.2216 0.1634 0.0053  0.0187  0.0341  15  HIS A CB  
287  C CG  A HIS A 15  ? 0.1889 0.1879 0.2167 0.0025  -0.0262 0.0411  15  HIS A CG  
288  C CG  B HIS A 15  ? 0.1759 0.1987 0.1976 -0.0176 -0.0065 0.0582  15  HIS A CG  
289  N ND1 A HIS A 15  ? 0.2121 0.2179 0.2572 0.0269  -0.0451 0.0234  15  HIS A ND1 
290  N ND1 B HIS A 15  ? 0.2698 0.2201 0.2024 0.0217  0.0229  0.0655  15  HIS A ND1 
291  C CD2 A HIS A 15  ? 0.2080 0.1543 0.2707 0.0064  -0.0452 0.0308  15  HIS A CD2 
292  C CD2 B HIS A 15  ? 0.1782 0.2018 0.2361 -0.0008 -0.0474 0.0293  15  HIS A CD2 
293  C CE1 A HIS A 15  ? 0.2303 0.2121 0.2984 0.0402  -0.0716 0.0161  15  HIS A CE1 
294  C CE1 B HIS A 15  ? 0.2745 0.1974 0.2740 0.0154  0.0047  0.0491  15  HIS A CE1 
295  N NE2 A HIS A 15  ? 0.2487 0.1484 0.2762 0.0393  -0.0890 0.0607  15  HIS A NE2 
296  N NE2 B HIS A 15  ? 0.2863 0.2111 0.2777 -0.0061 -0.0396 0.0176  15  HIS A NE2 
313  N N   . GLY A 16  ? 0.1451 0.2013 0.1499 0.0207  -0.0249 -0.0347 16  GLY A N   
314  C CA  . GLY A 16  ? 0.1231 0.2368 0.1798 0.0159  -0.0194 -0.0522 16  GLY A CA  
315  C C   . GLY A 16  ? 0.1241 0.1869 0.1609 0.0041  -0.0297 -0.0422 16  GLY A C   
316  O O   . GLY A 16  ? 0.1391 0.2801 0.1934 -0.0052 -0.0458 -0.0914 16  GLY A O   
320  N N   . LEU A 17  ? 0.1188 0.1672 0.1349 -0.0041 -0.0225 -0.0331 17  LEU A N   
321  C CA  . LEU A 17  ? 0.1167 0.1562 0.1192 -0.0125 -0.0198 -0.0199 17  LEU A CA  
322  C C   . LEU A 17  ? 0.1230 0.1501 0.1275 -0.0251 0.0001  -0.0284 17  LEU A C   
323  O O   . LEU A 17  ? 0.1585 0.1615 0.1371 -0.0304 0.0237  -0.0339 17  LEU A O   
324  C CB  . LEU A 17  ? 0.1181 0.1550 0.1265 -0.0208 -0.0157 -0.0061 17  LEU A CB  
325  C CG  . LEU A 17  ? 0.1560 0.1487 0.1453 -0.0063 -0.0302 -0.0091 17  LEU A CG  
326  C CD1 . LEU A 17  ? 0.1708 0.1780 0.1745 -0.0398 -0.0244 0.0176  17  LEU A CD1 
327  C CD2 . LEU A 17  ? 0.2004 0.2082 0.1504 -0.0169 -0.0465 0.0288  17  LEU A CD2 
339  N N   . ASP A 18  ? 0.1321 0.1621 0.1140 -0.0174 -0.0041 -0.0230 18  ASP A N   
340  C CA  . ASP A 18  ? 0.1322 0.1482 0.1135 -0.0162 -0.0108 -0.0205 18  ASP A CA  
341  C C   . ASP A 18  ? 0.1161 0.1553 0.1183 -0.0191 -0.0053 -0.0089 18  ASP A C   
342  O O   . ASP A 18  ? 0.1156 0.1949 0.1854 -0.0102 0.0001  -0.0439 18  ASP A O   
343  C CB  . ASP A 18  ? 0.1672 0.2072 0.1243 -0.0364 -0.0096 -0.0028 18  ASP A CB  
344  C CG  . ASP A 18  ? 0.1704 0.2322 0.1481 -0.0144 0.0067  0.0425  18  ASP A CG  
345  O OD1 . ASP A 18  ? 0.1605 0.2089 0.1646 -0.0357 -0.0031 0.0210  18  ASP A OD1 
346  O OD2 . ASP A 18  ? 0.3444 0.2862 0.3136 0.0243  0.1646  0.1041  18  ASP A OD2 
351  N N   . ASN A 19  ? 0.1124 0.1298 0.1114 -0.0180 -0.0181 0.0028  19  ASN A N   
352  C CA  . ASN A 19  ? 0.1324 0.1288 0.1118 -0.0249 -0.0143 0.0045  19  ASN A CA  
353  C C   . ASN A 19  ? 0.1259 0.1294 0.1288 -0.0245 -0.0277 0.0060  19  ASN A C   
354  O O   . ASN A 19  ? 0.1727 0.1450 0.1543 -0.0542 -0.0578 0.0187  19  ASN A O   
355  C CB  . ASN A 19  ? 0.1490 0.1384 0.1188 -0.0351 -0.0143 0.0036  19  ASN A CB  
356  C CG  . ASN A 19  ? 0.1605 0.1361 0.1221 -0.0214 0.0006  -0.0102 19  ASN A CG  
357  O OD1 . ASN A 19  ? 0.2076 0.1731 0.1738 -0.0123 0.0294  -0.0404 19  ASN A OD1 
358  N ND2 . ASN A 19  ? 0.1896 0.1723 0.1666 -0.0609 -0.0006 -0.0299 19  ASN A ND2 
365  N N   . TYR A 20  ? 0.1278 0.1263 0.1097 -0.0281 -0.0207 0.0058  20  TYR A N   
366  C CA  . TYR A 20  ? 0.1203 0.1293 0.1139 -0.0202 -0.0161 0.0034  20  TYR A CA  
367  C C   . TYR A 20  ? 0.1170 0.1154 0.1172 -0.0206 -0.0180 0.0056  20  TYR A C   
368  O O   . TYR A 20  ? 0.1196 0.1333 0.1304 -0.0193 -0.0139 -0.0026 20  TYR A O   
369  C CB  . TYR A 20  ? 0.1459 0.1185 0.1240 -0.0163 -0.0151 -0.0018 20  TYR A CB  
370  C CG  . TYR A 20  ? 0.1224 0.1195 0.1295 -0.0280 -0.0134 0.0050  20  TYR A CG  
371  C CD1 . TYR A 20  ? 0.1362 0.1775 0.2302 -0.0046 0.0071  0.0646  20  TYR A CD1 
372  C CD2 . TYR A 20  ? 0.1775 0.1268 0.1418 -0.0149 0.0115  0.0183  20  TYR A CD2 
373  C CE1 . TYR A 20  ? 0.1520 0.1876 0.2924 -0.0297 -0.0691 0.0862  20  TYR A CE1 
374  C CE2 . TYR A 20  ? 0.2617 0.1438 0.1310 -0.0348 -0.0065 0.0167  20  TYR A CE2 
375  C CZ  . TYR A 20  ? 0.2522 0.1354 0.1948 -0.0569 -0.0878 0.0425  20  TYR A CZ  
376  O OH  . TYR A 20  ? 0.4014 0.1916 0.2701 -0.0896 -0.1906 0.0903  20  TYR A OH  
386  N N   . ARG A 21  ? 0.1299 0.1328 0.1192 -0.0033 -0.0284 -0.0079 21  ARG A N   
387  C CA  . ARG A 21  ? 0.1643 0.1279 0.1200 -0.0056 -0.0361 -0.0084 21  ARG A CA  
388  C C   . ARG A 21  ? 0.1514 0.1330 0.1141 -0.0145 -0.0279 -0.0130 21  ARG A C   
389  O O   . ARG A 21  ? 0.1859 0.1382 0.1406 0.0028  -0.0058 -0.0078 21  ARG A O   
390  C CB  . ARG A 21  ? 0.2417 0.1481 0.1135 0.0011  -0.0296 0.0045  21  ARG A CB  
391  C CG  . ARG A 21  ? 0.2914 0.1586 0.1453 0.0185  -0.0470 0.0158  21  ARG A CG  
392  C CD  . ARG A 21  ? 0.3008 0.2584 0.2588 -0.0356 -0.1172 0.0981  21  ARG A CD  
393  N NE  . ARG A 21  ? 0.7298 0.2111 0.2654 -0.0971 -0.1882 0.0324  21  ARG A NE  
394  C CZ  . ARG A 21  ? 0.9621 0.1953 0.2127 0.0087  -0.1666 -0.0005 21  ARG A CZ  
395  N NH1 . ARG A 21  ? 0.9094 0.1759 0.2316 -0.0566 -0.1202 0.0008  21  ARG A NH1 
396  N NH2 . ARG A 21  ? 1.2753 0.2118 0.2618 -0.0278 -0.1489 -0.0927 21  ARG A NH2 
410  N N   . GLY A 22  ? 0.1305 0.1196 0.1376 -0.0239 -0.0320 0.0072  22  GLY A N   
411  C CA  . GLY A 22  ? 0.1392 0.1126 0.1559 -0.0325 -0.0375 0.0035  22  GLY A CA  
412  C C   . GLY A 22  ? 0.1329 0.1165 0.1415 -0.0289 -0.0299 0.0165  22  GLY A C   
413  O O   . GLY A 22  ? 0.1667 0.1119 0.2598 -0.0207 -0.0676 0.0192  22  GLY A O   
417  N N   . TYR A 23  ? 0.1172 0.1119 0.1262 -0.0231 -0.0245 0.0062  23  TYR A N   
418  C CA  . TYR A 23  ? 0.1047 0.1349 0.1223 -0.0244 -0.0154 0.0011  23  TYR A CA  
419  C C   . TYR A 23  ? 0.1055 0.1277 0.1129 -0.0162 -0.0129 0.0011  23  TYR A C   
420  O O   . TYR A 23  ? 0.1202 0.1340 0.1279 -0.0082 -0.0097 0.0036  23  TYR A O   
421  C CB  . TYR A 23  ? 0.1316 0.1308 0.1239 -0.0363 -0.0098 0.0002  23  TYR A CB  
422  C CG  . TYR A 23  ? 0.1441 0.1230 0.1326 -0.0437 -0.0005 -0.0111 23  TYR A CG  
423  C CD1 . TYR A 23  ? 0.1689 0.1303 0.1474 -0.0309 0.0183  0.0002  23  TYR A CD1 
424  C CD2 . TYR A 23  ? 0.1440 0.1800 0.1333 -0.0489 -0.0042 0.0019  23  TYR A CD2 
425  C CE1 . TYR A 23  ? 0.2036 0.1392 0.1628 -0.0152 0.0291  -0.0089 23  TYR A CE1 
426  C CE2 . TYR A 23  ? 0.1790 0.2115 0.1340 -0.0360 -0.0110 -0.0091 23  TYR A CE2 
427  C CZ  . TYR A 23  ? 0.2034 0.1590 0.1378 -0.0504 0.0162  -0.0193 23  TYR A CZ  
428  O OH  . TYR A 23  ? 0.2856 0.2380 0.1485 -0.0300 0.0424  -0.0346 23  TYR A OH  
438  N N   A SER A 24  ? 0.1274 0.1343 0.1194 -0.0058 -0.0086 0.0061  24  SER A N   
439  N N   B SER A 24  ? 0.1309 0.1370 0.1198 0.0023  -0.0159 -0.0008 24  SER A N   
440  C CA  A SER A 24  ? 0.1051 0.1526 0.1160 -0.0299 -0.0096 0.0138  24  SER A CA  
441  C CA  B SER A 24  ? 0.1279 0.1407 0.1123 -0.0114 -0.0092 0.0157  24  SER A CA  
442  C C   A SER A 24  ? 0.0878 0.1481 0.1155 -0.0253 -0.0011 0.0119  24  SER A C   
443  C C   B SER A 24  ? 0.1194 0.1359 0.1009 -0.0033 -0.0192 0.0212  24  SER A C   
444  O O   A SER A 24  ? 0.0749 0.1108 0.1478 0.0060  -0.0004 0.0615  24  SER A O   
445  O O   B SER A 24  ? 0.1129 0.1521 0.1020 -0.0069 -0.0176 0.0244  24  SER A O   
446  C CB  A SER A 24  ? 0.2455 0.1476 0.1093 0.0144  0.0432  0.0253  24  SER A CB  
447  C CB  B SER A 24  ? 0.1627 0.1464 0.1501 0.0005  -0.0324 0.0203  24  SER A CB  
448  O OG  A SER A 24  ? 0.2928 0.1473 0.3050 0.0164  -0.0165 -0.0060 24  SER A OG  
449  O OG  B SER A 24  ? 0.1691 0.2308 0.1685 0.0480  -0.0264 0.0196  24  SER A OG  
460  N N   . LEU A 25  ? 0.1181 0.1398 0.1133 -0.0152 -0.0017 0.0174  25  LEU A N   
461  C CA  . LEU A 25  ? 0.1289 0.1259 0.1065 -0.0167 -0.0012 0.0208  25  LEU A CA  
462  C C   . LEU A 25  ? 0.1280 0.1085 0.1016 -0.0155 -0.0023 0.0135  25  LEU A C   
463  O O   . LEU A 25  ? 0.1380 0.1064 0.1329 -0.0137 0.0185  0.0105  25  LEU A O   
464  C CB  . LEU A 25  ? 0.1247 0.1351 0.1169 -0.0082 0.0078  0.0144  25  LEU A CB  
465  C CG  . LEU A 25  ? 0.1535 0.1408 0.1318 -0.0189 0.0017  -0.0033 25  LEU A CG  
466  C CD1 . LEU A 25  ? 0.3030 0.1386 0.1565 0.0185  0.0146  0.0039  25  LEU A CD1 
467  C CD2 . LEU A 25  ? 0.1902 0.1924 0.1251 0.0040  0.0032  -0.0049 25  LEU A CD2 
479  N N   . GLY A 26  ? 0.1353 0.1106 0.1036 -0.0153 -0.0055 0.0261  26  GLY A N   
480  C CA  . GLY A 26  ? 0.1283 0.1277 0.1097 -0.0141 -0.0240 0.0241  26  GLY A CA  
481  C C   . GLY A 26  ? 0.1167 0.1025 0.1114 -0.0046 -0.0189 0.0163  26  GLY A C   
482  O O   . GLY A 26  ? 0.1152 0.1337 0.1139 -0.0136 -0.0227 0.0181  26  GLY A O   
486  N N   . ASN A 27  ? 0.1143 0.1121 0.1049 -0.0132 -0.0092 0.0077  27  ASN A N   
487  C CA  . ASN A 27  ? 0.1072 0.1092 0.1016 -0.0086 -0.0067 0.0017  27  ASN A CA  
488  C C   . ASN A 27  ? 0.1029 0.1102 0.0922 0.0028  -0.0166 0.0082  27  ASN A C   
489  O O   . ASN A 27  ? 0.1075 0.1118 0.1099 -0.0084 -0.0024 0.0021  27  ASN A O   
490  C CB  . ASN A 27  ? 0.1206 0.1247 0.1007 -0.0150 -0.0120 0.0002  27  ASN A CB  
491  C CG  . ASN A 27  ? 0.1505 0.1253 0.1171 -0.0291 -0.0043 -0.0041 27  ASN A CG  
492  O OD1 . ASN A 27  ? 0.1892 0.1126 0.1563 -0.0028 0.0239  -0.0007 27  ASN A OD1 
493  N ND2 . ASN A 27  ? 0.1936 0.1556 0.1860 -0.0715 0.0081  -0.0063 27  ASN A ND2 
500  N N   . TRP A 28  ? 0.1031 0.1057 0.0988 0.0008  -0.0050 0.0130  28  TRP A N   
501  C CA  . TRP A 28  ? 0.1083 0.1054 0.0923 0.0026  -0.0134 0.0081  28  TRP A CA  
502  C C   . TRP A 28  ? 0.1009 0.1077 0.0909 0.0071  -0.0074 0.0101  28  TRP A C   
503  O O   . TRP A 28  ? 0.1198 0.1119 0.1010 -0.0088 -0.0179 0.0200  28  TRP A O   
504  C CB  . TRP A 28  ? 0.1064 0.1132 0.1053 0.0103  -0.0149 0.0061  28  TRP A CB  
505  C CG  . TRP A 28  ? 0.1059 0.1040 0.1030 0.0033  -0.0142 0.0084  28  TRP A CG  
506  C CD1 . TRP A 28  ? 0.1215 0.1281 0.1314 -0.0114 -0.0070 0.0107  28  TRP A CD1 
507  C CD2 . TRP A 28  ? 0.1298 0.1174 0.1097 0.0170  -0.0175 0.0150  28  TRP A CD2 
508  N NE1 . TRP A 28  ? 0.1242 0.1658 0.1598 -0.0189 -0.0232 -0.0311 28  TRP A NE1 
509  C CE2 . TRP A 28  ? 0.1272 0.1781 0.1251 0.0286  -0.0406 -0.0173 28  TRP A CE2 
510  C CE3 . TRP A 28  ? 0.2389 0.1285 0.1259 0.0142  0.0047  0.0303  28  TRP A CE3 
511  C CZ2 . TRP A 28  ? 0.2454 0.2766 0.1308 0.0660  -0.0760 -0.0410 28  TRP A CZ2 
512  C CZ3 . TRP A 28  ? 0.3952 0.2071 0.1452 0.0609  -0.0217 0.0622  28  TRP A CZ3 
513  C CH2 . TRP A 28  ? 0.3290 0.3283 0.1410 0.0951  -0.0637 0.0383  28  TRP A CH2 
524  N N   . VAL A 29  ? 0.1076 0.1080 0.0838 -0.0080 -0.0109 0.0098  29  VAL A N   
525  C CA  . VAL A 29  ? 0.1037 0.1098 0.0926 -0.0067 -0.0149 0.0170  29  VAL A CA  
526  C C   . VAL A 29  ? 0.1099 0.1051 0.0886 -0.0044 -0.0156 0.0161  29  VAL A C   
527  O O   . VAL A 29  ? 0.1180 0.1175 0.1078 -0.0147 -0.0094 0.0060  29  VAL A O   
528  C CB  . VAL A 29  ? 0.1210 0.1207 0.0884 -0.0043 -0.0091 0.0156  29  VAL A CB  
529  C CG1 . VAL A 29  ? 0.1559 0.1743 0.0935 -0.0262 -0.0296 0.0239  29  VAL A CG1 
530  C CG2 . VAL A 29  ? 0.1299 0.1666 0.1058 -0.0194 0.0061  0.0108  29  VAL A CG2 
540  N N   . CYS A 30  ? 0.1062 0.1030 0.1052 -0.0072 -0.0096 0.0052  30  CYS A N   
541  C CA  . CYS A 30  ? 0.1071 0.1163 0.1079 -0.0024 -0.0096 0.0098  30  CYS A CA  
542  C C   . CYS A 30  ? 0.1020 0.0979 0.1120 0.0022  -0.0043 0.0018  30  CYS A C   
543  O O   . CYS A 30  ? 0.1015 0.1135 0.1257 -0.0007 -0.0055 0.0127  30  CYS A O   
544  C CB  . CYS A 30  ? 0.1220 0.1100 0.1152 0.0074  -0.0103 0.0160  30  CYS A CB  
545  S SG  . CYS A 30  ? 0.1305 0.1252 0.1448 0.0215  -0.0076 0.0094  30  CYS A SG  
550  N N   . ALA A 31  ? 0.1026 0.1043 0.0986 -0.0032 -0.0070 0.0050  31  ALA A N   
551  C CA  . ALA A 31  ? 0.1100 0.1104 0.1015 -0.0047 -0.0005 0.0080  31  ALA A CA  
552  C C   . ALA A 31  ? 0.1039 0.1094 0.0895 -0.0052 -0.0101 0.0133  31  ALA A C   
553  O O   . ALA A 31  ? 0.1135 0.1246 0.1065 -0.0117 0.0022  0.0072  31  ALA A O   
554  C CB  . ALA A 31  ? 0.1344 0.1314 0.1055 -0.0106 -0.0234 0.0042  31  ALA A CB  
560  N N   . ALA A 32  ? 0.0890 0.1090 0.0955 -0.0023 -0.0089 0.0130  32  ALA A N   
561  C CA  . ALA A 32  ? 0.0956 0.0992 0.1023 0.0034  -0.0089 0.0144  32  ALA A CA  
562  C C   . ALA A 32  ? 0.0966 0.0950 0.0973 0.0011  -0.0021 0.0081  32  ALA A C   
563  O O   . ALA A 32  ? 0.0982 0.1046 0.1441 -0.0037 -0.0123 0.0125  32  ALA A O   
564  C CB  . ALA A 32  ? 0.0997 0.1236 0.1316 0.0121  -0.0033 -0.0025 32  ALA A CB  
570  N N   . LYS A 33  ? 0.0881 0.1065 0.1031 -0.0023 -0.0111 0.0144  33  LYS A N   
571  C CA  . LYS A 33  ? 0.0942 0.1211 0.1004 0.0084  -0.0138 0.0049  33  LYS A CA  
572  C C   . LYS A 33  ? 0.0870 0.1125 0.1129 0.0116  -0.0164 0.0122  33  LYS A C   
573  O O   . LYS A 33  ? 0.0970 0.1324 0.1483 0.0008  -0.0113 -0.0014 33  LYS A O   
574  C CB  . LYS A 33  ? 0.1117 0.1319 0.1096 0.0157  -0.0183 0.0227  33  LYS A CB  
575  C CG  . LYS A 33  ? 0.1335 0.1607 0.1590 0.0135  -0.0355 0.0354  33  LYS A CG  
576  C CD  . LYS A 33  ? 0.1427 0.2368 0.1587 0.0143  -0.0545 0.0174  33  LYS A CD  
577  C CE  . LYS A 33  ? 0.1738 0.2541 0.2503 0.0361  -0.1076 0.0125  33  LYS A CE  
578  N NZ  . LYS A 33  ? 0.2694 0.2793 0.3399 0.0120  -0.2010 -0.0087 33  LYS A NZ  
592  N N   . PHE A 34  ? 0.1016 0.1111 0.1043 0.0167  -0.0056 0.0120  34  PHE A N   
593  C CA  . PHE A 34  ? 0.0928 0.1262 0.1210 0.0264  -0.0027 0.0154  34  PHE A CA  
594  C C   . PHE A 34  ? 0.1010 0.1384 0.1274 0.0315  0.0187  0.0264  34  PHE A C   
595  O O   . PHE A 34  ? 0.1046 0.1866 0.2091 0.0389  0.0371  0.0743  34  PHE A O   
596  C CB  . PHE A 34  ? 0.1283 0.1376 0.1190 0.0483  0.0075  0.0102  34  PHE A CB  
597  C CG  . PHE A 34  ? 0.1299 0.1238 0.1407 0.0485  0.0032  0.0100  34  PHE A CG  
598  C CD1 . PHE A 34  ? 0.1210 0.1631 0.1562 0.0408  0.0033  0.0221  34  PHE A CD1 
599  C CD2 . PHE A 34  ? 0.1391 0.1346 0.1927 0.0244  -0.0173 0.0361  34  PHE A CD2 
600  C CE1 . PHE A 34  ? 0.1449 0.1976 0.2290 0.0514  -0.0269 0.0574  34  PHE A CE1 
601  C CE2 . PHE A 34  ? 0.1830 0.1842 0.2280 0.0193  -0.0262 0.0751  34  PHE A CE2 
602  C CZ  . PHE A 34  ? 0.1906 0.1809 0.2256 0.0414  -0.0391 0.0724  34  PHE A CZ  
612  N N   . GLU A 35  ? 0.0952 0.1131 0.1014 0.0189  0.0034  0.0145  35  GLU A N   
613  C CA  . GLU A 35  ? 0.1008 0.1134 0.0961 0.0105  0.0041  0.0142  35  GLU A CA  
614  C C   . GLU A 35  ? 0.0921 0.1238 0.0992 0.0087  -0.0030 0.0202  35  GLU A C   
615  O O   . GLU A 35  ? 0.1206 0.1385 0.1155 -0.0187 0.0117  0.0247  35  GLU A O   
616  C CB  . GLU A 35  ? 0.1010 0.1150 0.0997 0.0154  -0.0019 0.0165  35  GLU A CB  
617  C CG  . GLU A 35  ? 0.1323 0.1312 0.1049 -0.0011 -0.0155 0.0123  35  GLU A CG  
618  C CD  . GLU A 35  ? 0.1477 0.1469 0.1032 0.0192  -0.0134 -0.0003 35  GLU A CD  
619  O OE1 . GLU A 35  ? 0.2177 0.1615 0.1256 -0.0036 0.0325  0.0050  35  GLU A OE1 
620  O OE2 . GLU A 35  ? 0.2183 0.1779 0.1281 0.0097  -0.0097 -0.0159 35  GLU A OE2 
627  N N   . SER A 36  ? 0.1218 0.1165 0.1000 -0.0096 0.0104  0.0084  36  SER A N   
628  C CA  . SER A 36  ? 0.1101 0.1192 0.1131 -0.0200 0.0001  0.0112  36  SER A CA  
629  C C   . SER A 36  ? 0.0934 0.1205 0.1208 -0.0015 -0.0063 -0.0003 36  SER A C   
630  O O   . SER A 36  ? 0.1125 0.1263 0.1407 -0.0111 -0.0238 -0.0034 36  SER A O   
631  C CB  . SER A 36  ? 0.1272 0.1083 0.1049 -0.0027 -0.0245 0.0158  36  SER A CB  
632  O OG  . SER A 36  ? 0.1071 0.1197 0.0989 0.0140  -0.0139 0.0095  36  SER A OG  
638  N N   A ASN A 37  ? 0.0803 0.1287 0.1281 0.0194  -0.0042 0.0019  37  ASN A N   
639  N N   B ASN A 37  ? 0.1172 0.1237 0.1180 0.0091  -0.0288 -0.0120 37  ASN A N   
640  C CA  A ASN A 37  ? 0.1209 0.1264 0.1410 0.0243  -0.0334 0.0043  37  ASN A CA  
641  C CA  B ASN A 37  ? 0.1083 0.1274 0.1269 0.0107  -0.0388 -0.0062 37  ASN A CA  
642  C C   A ASN A 37  ? 0.1242 0.1090 0.1063 0.0167  -0.0413 0.0158  37  ASN A C   
643  C C   B ASN A 37  ? 0.1219 0.1124 0.1065 0.0132  -0.0373 0.0063  37  ASN A C   
644  O O   A ASN A 37  ? 0.1440 0.1788 0.1100 0.0199  -0.0507 0.0043  37  ASN A O   
645  O O   B ASN A 37  ? 0.1409 0.1388 0.1049 -0.0173 -0.0279 0.0040  37  ASN A O   
646  C CB  A ASN A 37  ? 0.1086 0.1673 0.2021 0.0301  -0.0473 -0.0275 37  ASN A CB  
647  C CB  B ASN A 37  ? 0.1015 0.1857 0.2119 0.0339  -0.0699 -0.0132 37  ASN A CB  
648  C CG  A ASN A 37  ? 0.1282 0.2107 0.2409 0.0292  -0.0545 0.0105  37  ASN A CG  
649  C CG  B ASN A 37  ? 0.1448 0.1878 0.2021 0.0390  -0.0850 -0.0279 37  ASN A CG  
650  O OD1 A ASN A 37  ? 0.1619 0.2459 0.3071 0.0194  -0.0780 0.0715  37  ASN A OD1 
651  O OD1 B ASN A 37  ? 0.1849 0.1923 0.2347 0.0312  -0.1159 0.0057  37  ASN A OD1 
652  N ND2 A ASN A 37  ? 0.1278 0.2692 0.2958 0.0234  -0.0807 0.0343  37  ASN A ND2 
653  N ND2 B ASN A 37  ? 0.1623 0.3012 0.2140 -0.0174 -0.0929 -0.0106 37  ASN A ND2 
666  N N   . PHE A 38  ? 0.1177 0.1231 0.0836 0.0130  -0.0225 0.0116  38  PHE A N   
667  C CA  . PHE A 38  ? 0.1229 0.1151 0.0850 0.0081  -0.0168 0.0125  38  PHE A CA  
668  C C   . PHE A 38  ? 0.1214 0.1229 0.0760 0.0086  -0.0156 0.0094  38  PHE A C   
669  O O   . PHE A 38  ? 0.1612 0.1270 0.0907 0.0005  0.0070  0.0014  38  PHE A O   
670  C CB  . PHE A 38  ? 0.1668 0.1300 0.0847 -0.0002 -0.0102 0.0150  38  PHE A CB  
671  C CG  . PHE A 38  ? 0.1307 0.1272 0.0809 0.0018  -0.0015 0.0219  38  PHE A CG  
672  C CD1 . PHE A 38  ? 0.1200 0.1401 0.1089 -0.0029 -0.0163 0.0213  38  PHE A CD1 
673  C CD2 . PHE A 38  ? 0.1951 0.1489 0.1477 -0.0132 -0.0710 0.0394  38  PHE A CD2 
674  C CE1 . PHE A 38  ? 0.1349 0.1420 0.1155 -0.0178 -0.0116 0.0023  38  PHE A CE1 
675  C CE2 . PHE A 38  ? 0.2385 0.1502 0.1672 -0.0122 -0.0773 0.0528  38  PHE A CE2 
676  C CZ  . PHE A 38  ? 0.1691 0.1364 0.1411 -0.0071 -0.0074 0.0280  38  PHE A CZ  
686  N N   A ASN A 39  ? 0.1386 0.1183 0.1177 0.0298  0.0160  0.0289  39  ASN A N   
687  N N   B ASN A 39  ? 0.1289 0.1149 0.0819 0.0177  -0.0101 0.0178  39  ASN A N   
688  C CA  A ASN A 39  ? 0.1244 0.1202 0.1074 0.0168  -0.0098 0.0144  39  ASN A CA  
689  C CA  B ASN A 39  ? 0.1240 0.1180 0.0857 0.0137  -0.0103 0.0127  39  ASN A CA  
690  C C   A ASN A 39  ? 0.1156 0.0957 0.0981 0.0023  -0.0118 -0.0038 39  ASN A C   
691  C C   B ASN A 39  ? 0.1131 0.1136 0.0739 0.0016  0.0066  0.0216  39  ASN A C   
692  O O   A ASN A 39  ? 0.1162 0.1078 0.0970 0.0004  -0.0050 -0.0001 39  ASN A O   
693  O O   B ASN A 39  ? 0.1162 0.1035 0.0724 -0.0118 0.0015  0.0164  39  ASN A O   
694  C CB  A ASN A 39  ? 0.1204 0.1510 0.1155 0.0113  -0.0208 0.0240  39  ASN A CB  
695  C CB  B ASN A 39  ? 0.1261 0.1389 0.1409 0.0075  -0.0090 0.0323  39  ASN A CB  
696  C CG  A ASN A 39  ? 0.1375 0.1698 0.1004 -0.0174 -0.0142 0.0111  39  ASN A CG  
697  C CG  B ASN A 39  ? 0.1323 0.1452 0.1149 -0.0174 -0.0354 0.0066  39  ASN A CG  
698  O OD1 A ASN A 39  ? 0.1623 0.1602 0.1624 -0.0066 -0.0200 -0.0145 39  ASN A OD1 
699  O OD1 B ASN A 39  ? 0.1550 0.1285 0.1146 -0.0086 -0.0469 0.0049  39  ASN A OD1 
700  N ND2 A ASN A 39  ? 0.1425 0.2152 0.2527 -0.0452 -0.0331 0.0202  39  ASN A ND2 
701  N ND2 B ASN A 39  ? 0.1414 0.1854 0.3246 -0.0257 0.0044  0.0581  39  ASN A ND2 
714  N N   . THR A 40  ? 0.1181 0.1139 0.0813 0.0118  -0.0028 0.0148  40  THR A N   
715  C CA  . THR A 40  ? 0.1126 0.1129 0.0960 0.0073  -0.0044 0.0187  40  THR A CA  
716  C C   . THR A 40  ? 0.1182 0.1096 0.0823 0.0107  -0.0040 0.0119  40  THR A C   
717  O O   . THR A 40  ? 0.1409 0.1315 0.1056 0.0055  -0.0266 0.0288  40  THR A O   
718  C CB  . THR A 40  ? 0.1321 0.1359 0.1152 0.0171  0.0085  0.0160  40  THR A CB  
719  O OG1 . THR A 40  ? 0.1782 0.1406 0.1093 0.0202  0.0151  0.0013  40  THR A OG1 
720  C CG2 . THR A 40  ? 0.1438 0.1624 0.1458 -0.0024 0.0298  0.0175  40  THR A CG2 
728  N N   A GLN A 41  ? 0.1244 0.1041 0.0951 0.0035  -0.0137 0.0181  41  GLN A N   
729  N N   B GLN A 41  ? 0.1383 0.1088 0.0660 -0.0084 -0.0037 -0.0017 41  GLN A N   
730  C CA  A GLN A 41  ? 0.1412 0.1010 0.0929 -0.0077 -0.0132 0.0078  41  GLN A CA  
731  C CA  B GLN A 41  ? 0.1874 0.1109 0.1105 -0.0278 0.0317  -0.0064 41  GLN A CA  
732  C C   A GLN A 41  ? 0.1481 0.1067 0.0888 -0.0191 -0.0097 0.0060  41  GLN A C   
733  C C   B GLN A 41  ? 0.1379 0.1108 0.0754 -0.0269 -0.0080 0.0036  41  GLN A C   
734  O O   A GLN A 41  ? 0.1581 0.1195 0.1027 -0.0359 -0.0103 0.0061  41  GLN A O   
735  O O   B GLN A 41  ? 0.1449 0.1308 0.1127 -0.0372 0.0065  0.0059  41  GLN A O   
736  C CB  A GLN A 41  ? 0.2139 0.1496 0.1287 -0.0529 0.0002  -0.0311 41  GLN A CB  
737  C CB  B GLN A 41  ? 0.2441 0.1287 0.1254 -0.0604 0.0397  -0.0238 41  GLN A CB  
738  C CG  A GLN A 41  ? 0.3239 0.2085 0.1603 -0.0057 0.0314  -0.0598 41  GLN A CG  
739  C CG  B GLN A 41  ? 0.3560 0.0992 0.1997 -0.0457 0.1000  -0.0347 41  GLN A CG  
740  C CD  A GLN A 41  ? 0.4260 0.1344 0.1561 -0.0353 0.0542  -0.0272 41  GLN A CD  
741  C CD  B GLN A 41  ? 0.5021 0.1754 0.2907 0.0916  0.1598  0.0267  41  GLN A CD  
742  O OE1 A GLN A 41  ? 0.7193 0.1471 0.3799 0.0200  0.0064  -0.0321 41  GLN A OE1 
743  O OE1 B GLN A 41  ? 0.4372 0.3573 0.2099 0.0347  0.0482  0.0789  41  GLN A OE1 
744  N NE2 A GLN A 41  ? 0.5124 0.1910 0.1984 -0.1181 -0.0516 -0.0219 41  GLN A NE2 
745  N NE2 B GLN A 41  ? 0.4786 0.2519 0.2875 0.0742  0.1154  0.0713  41  GLN A NE2 
762  N N   . ALA A 42  ? 0.1326 0.1150 0.0895 -0.0165 0.0006  -0.0011 42  ALA A N   
763  C CA  . ALA A 42  ? 0.1163 0.1297 0.0938 -0.0129 -0.0064 0.0020  42  ALA A CA  
764  C C   . ALA A 42  ? 0.1032 0.1156 0.0904 -0.0123 0.0010  0.0010  42  ALA A C   
765  O O   . ALA A 42  ? 0.1016 0.1398 0.1068 -0.0214 -0.0082 0.0068  42  ALA A O   
766  C CB  . ALA A 42  ? 0.1639 0.1331 0.1149 0.0236  0.0173  0.0185  42  ALA A CB  
772  N N   A THR A 43  ? 0.0939 0.1504 0.0916 -0.0178 -0.0077 0.0036  43  THR A N   
773  N N   B THR A 43  ? 0.0995 0.1590 0.0908 -0.0278 -0.0077 0.0015  43  THR A N   
774  C CA  A THR A 43  ? 0.1071 0.1405 0.0975 -0.0151 -0.0042 0.0160  43  THR A CA  
775  C CA  B THR A 43  ? 0.1061 0.1687 0.0978 -0.0415 -0.0039 0.0109  43  THR A CA  
776  C C   A THR A 43  ? 0.0886 0.1786 0.0938 -0.0121 -0.0022 0.0324  43  THR A C   
777  C C   B THR A 43  ? 0.0959 0.1999 0.0946 -0.0306 -0.0086 0.0219  43  THR A C   
778  O O   A THR A 43  ? 0.1018 0.2958 0.0985 -0.0034 -0.0161 0.0050  43  THR A O   
779  O O   B THR A 43  ? 0.1040 0.3122 0.1370 -0.0641 -0.0113 0.0099  43  THR A O   
780  C CB  A THR A 43  ? 0.1458 0.1463 0.1173 -0.0217 0.0107  0.0075  43  THR A CB  
781  C CB  B THR A 43  ? 0.1355 0.1663 0.1237 -0.0434 -0.0220 0.0142  43  THR A CB  
782  O OG1 A THR A 43  ? 0.1959 0.1638 0.2063 -0.0805 -0.0029 0.0114  43  THR A OG1 
783  O OG1 B THR A 43  ? 0.1879 0.1586 0.1704 0.0055  0.0168  0.0529  43  THR A OG1 
784  C CG2 A THR A 43  ? 0.1973 0.1460 0.1445 0.0163  0.0317  0.0229  43  THR A CG2 
785  C CG2 B THR A 43  ? 0.3121 0.1936 0.1303 0.0175  0.0021  0.0290  43  THR A CG2 
800  N N   . ASN A 44  ? 0.0838 0.1699 0.0994 -0.0063 -0.0008 0.0196  44  ASN A N   
801  C CA  . ASN A 44  ? 0.0843 0.1754 0.1105 0.0005  0.0042  0.0292  44  ASN A CA  
802  C C   . ASN A 44  ? 0.0735 0.1409 0.1014 -0.0011 0.0044  0.0149  44  ASN A C   
803  O O   . ASN A 44  ? 0.0847 0.1614 0.1196 -0.0167 -0.0090 0.0286  44  ASN A O   
804  C CB  . ASN A 44  ? 0.1373 0.1635 0.1566 0.0237  0.0157  0.0464  44  ASN A CB  
805  C CG  . ASN A 44  ? 0.1574 0.1951 0.2272 0.0416  0.0235  0.0124  44  ASN A CG  
806  O OD1 . ASN A 44  ? 0.1304 0.3717 0.5247 0.0225  0.0673  -0.1013 44  ASN A OD1 
807  N ND2 . ASN A 44  ? 0.3486 0.4789 0.1789 0.1409  0.0118  -0.0402 44  ASN A ND2 
814  N N   A ARG A 45  ? 0.0881 0.1760 0.1219 -0.0255 -0.0051 0.0278  45  ARG A N   
815  N N   B ARG A 45  ? 0.1033 0.1597 0.0908 -0.0291 -0.0045 0.0059  45  ARG A N   
816  C CA  A ARG A 45  ? 0.0945 0.1384 0.1140 -0.0228 0.0116  0.0101  45  ARG A CA  
817  C CA  B ARG A 45  ? 0.1521 0.1514 0.1061 -0.0184 0.0174  0.0178  45  ARG A CA  
818  C C   A ARG A 45  ? 0.0795 0.1823 0.1380 -0.0238 0.0185  -0.0075 45  ARG A C   
819  C C   B ARG A 45  ? 0.1164 0.1284 0.0977 -0.0038 0.0020  0.0466  45  ARG A C   
820  O O   A ARG A 45  ? 0.0771 0.2027 0.1951 -0.0165 0.0135  -0.0008 45  ARG A O   
821  O O   B ARG A 45  ? 0.1291 0.2128 0.1257 0.0230  -0.0230 0.0251  45  ARG A O   
822  C CB  A ARG A 45  ? 0.1338 0.1641 0.1421 -0.0595 -0.0094 0.0060  45  ARG A CB  
823  C CB  B ARG A 45  ? 0.2661 0.1637 0.1269 -0.0523 0.0158  0.0086  45  ARG A CB  
824  C CG  A ARG A 45  ? 0.3074 0.1383 0.1417 -0.0765 0.0435  -0.0172 45  ARG A CG  
825  C CG  B ARG A 45  ? 0.3371 0.1321 0.1431 -0.0730 0.0474  0.0066  45  ARG A CG  
826  C CD  A ARG A 45  ? 0.3794 0.1893 0.2552 -0.1442 0.0564  -0.0662 45  ARG A CD  
827  C CD  B ARG A 45  ? 0.5692 0.1853 0.2562 0.0448  0.1475  0.0424  45  ARG A CD  
828  N NE  A ARG A 45  ? 0.6697 0.1480 0.3336 -0.1663 0.2068  -0.0884 45  ARG A NE  
829  N NE  B ARG A 45  ? 0.5384 0.1841 0.3533 0.0135  0.2335  0.0589  45  ARG A NE  
830  C CZ  A ARG A 45  ? 0.7250 0.1315 0.3281 -0.0989 0.2064  -0.0754 45  ARG A CZ  
831  C CZ  B ARG A 45  ? 0.6061 0.0992 0.5398 0.0783  0.2139  0.0719  45  ARG A CZ  
832  N NH1 A ARG A 45  ? 0.8620 0.2665 0.3991 0.0373  0.1509  -0.0745 45  ARG A NH1 
833  N NH1 B ARG A 45  ? 0.4776 0.1209 0.5609 0.0173  0.1420  -0.0403 45  ARG A NH1 
834  N NH2 A ARG A 45  ? 0.6843 0.2166 0.3599 -0.1611 0.2170  -0.1379 45  ARG A NH2 
835  N NH2 B ARG A 45  ? 0.4631 0.1643 0.5196 0.1309  0.2605  0.1228  45  ARG A NH2 
862  N N   . ASN A 46  ? 0.0934 0.1743 0.1086 0.0111  0.0127  0.0022  46  ASN A N   
863  C CA  . ASN A 46  ? 0.1131 0.1694 0.1198 0.0146  0.0255  0.0103  46  ASN A CA  
864  C C   . ASN A 46  ? 0.1105 0.1603 0.1161 0.0098  0.0267  0.0087  46  ASN A C   
865  O O   . ASN A 46  ? 0.1618 0.1667 0.1531 0.0213  0.0610  0.0195  46  ASN A O   
866  C CB  . ASN A 46  ? 0.1402 0.1609 0.1270 -0.0064 0.0265  -0.0009 46  ASN A CB  
867  C CG  . ASN A 46  ? 0.1475 0.1581 0.1628 0.0030  0.0169  0.0270  46  ASN A CG  
868  O OD1 . ASN A 46  ? 0.1931 0.2853 0.2778 0.0331  0.0135  0.1396  46  ASN A OD1 
869  N ND2 . ASN A 46  ? 0.1626 0.1888 0.1702 0.0094  0.0535  0.0334  46  ASN A ND2 
876  N N   A THR A 47  ? 0.1742 0.1972 0.1942 0.0471  0.0998  0.0527  47  THR A N   
877  N N   B THR A 47  ? 0.0983 0.1580 0.0882 -0.0014 -0.0020 -0.0041 47  THR A N   
878  C CA  A THR A 47  ? 0.1028 0.1916 0.1617 -0.0306 0.0447  0.0093  47  THR A CA  
879  C CA  B THR A 47  ? 0.1290 0.1723 0.1009 0.0117  0.0226  0.0039  47  THR A CA  
880  C C   A THR A 47  ? 0.1204 0.1879 0.1637 0.0035  0.0340  -0.0082 47  THR A C   
881  C C   B THR A 47  ? 0.1101 0.1645 0.0987 0.0116  0.0290  0.0115  47  THR A C   
882  O O   A THR A 47  ? 0.1471 0.2359 0.2030 -0.0385 0.0091  0.0411  47  THR A O   
883  O O   B THR A 47  ? 0.1261 0.2220 0.1201 -0.0232 0.0105  0.0451  47  THR A O   
884  C CB  A THR A 47  ? 0.1366 0.2472 0.1349 0.0269  0.0437  0.0432  47  THR A CB  
885  C CB  B THR A 47  ? 0.0844 0.1818 0.1510 -0.0283 0.0025  -0.0357 47  THR A CB  
886  O OG1 A THR A 47  ? 0.0998 0.2463 0.1628 0.0571  0.0172  0.0326  47  THR A OG1 
887  O OG1 B THR A 47  ? 0.1293 0.1896 0.1275 -0.0094 0.0116  -0.0538 47  THR A OG1 
888  C CG2 A THR A 47  ? 0.1167 0.2866 0.1814 0.0030  0.0276  0.0394  47  THR A CG2 
889  C CG2 B THR A 47  ? 0.1421 0.2322 0.2147 -0.0224 -0.0592 -0.0568 47  THR A CG2 
904  N N   A ASP A 48  ? 0.0953 0.2050 0.1264 0.0124  0.0328  0.0354  48  ASP A N   
905  N N   B ASP A 48  ? 0.1529 0.1812 0.1284 -0.0362 0.0374  -0.0210 48  ASP A N   
906  C CA  A ASP A 48  ? 0.1368 0.2245 0.1381 0.0106  0.0073  0.0164  48  ASP A CA  
907  C CA  B ASP A 48  ? 0.1350 0.2652 0.0993 -0.0417 0.0546  -0.0290 48  ASP A CA  
908  C C   A ASP A 48  ? 0.1063 0.2643 0.1252 0.0200  0.0071  0.0343  48  ASP A C   
909  C C   B ASP A 48  ? 0.1691 0.2580 0.1080 -0.0130 0.0662  0.0346  48  ASP A C   
910  O O   A ASP A 48  ? 0.1460 0.3978 0.1665 0.0465  -0.0397 0.0339  48  ASP A O   
911  O O   B ASP A 48  ? 0.2236 0.4074 0.1242 0.0436  0.0315  0.0178  48  ASP A O   
912  C CB  A ASP A 48  ? 0.1847 0.2567 0.1540 -0.0322 0.0243  -0.0046 48  ASP A CB  
913  C CB  B ASP A 48  ? 0.1555 0.2805 0.1119 -0.0556 0.0593  -0.0656 48  ASP A CB  
914  C CG  A ASP A 48  ? 0.1523 0.2472 0.1286 -0.0413 -0.0124 -0.0045 48  ASP A CG  
915  C CG  B ASP A 48  ? 0.1829 0.2213 0.1180 -0.0634 0.0605  -0.0651 48  ASP A CG  
916  O OD1 A ASP A 48  ? 0.2557 0.2074 0.1664 -0.0475 0.0588  -0.0060 48  ASP A OD1 
917  O OD1 B ASP A 48  ? 0.0916 0.1773 0.0908 0.0279  0.0289  -0.0051 48  ASP A OD1 
918  O OD2 A ASP A 48  ? 0.2933 0.3809 0.1707 -0.1790 0.0237  -0.0674 48  ASP A OD2 
919  O OD2 B ASP A 48  ? 0.4065 0.2202 0.2329 -0.0849 0.1704  -0.0817 48  ASP A OD2 
928  N N   A GLY A 49  ? 0.1130 0.1799 0.1493 0.0013  0.0284  0.0444  49  GLY A N   
929  N N   B GLY A 49  ? 0.1772 0.2242 0.1312 -0.0091 0.0766  0.0187  49  GLY A N   
930  C CA  A GLY A 49  ? 0.1381 0.1784 0.2188 0.0178  0.0661  0.0736  49  GLY A CA  
931  C CA  B GLY A 49  ? 0.2052 0.1992 0.1822 -0.0050 0.0868  0.0579  49  GLY A CA  
932  C C   A GLY A 49  ? 0.0968 0.1647 0.1401 0.0029  0.0134  0.0486  49  GLY A C   
933  C C   B GLY A 49  ? 0.1601 0.1571 0.1346 -0.0041 0.0487  0.0297  49  GLY A C   
934  O O   A GLY A 49  ? 0.1214 0.1619 0.1854 0.0146  0.0480  0.0687  49  GLY A O   
935  O O   B GLY A 49  ? 0.1847 0.1564 0.2060 0.0102  0.0537  0.0180  49  GLY A O   
942  N N   . SER A 50  ? 0.1142 0.1540 0.1005 0.0049  0.0266  0.0273  50  SER A N   
943  C CA  . SER A 50  ? 0.1013 0.1443 0.0927 0.0075  0.0120  0.0290  50  SER A CA  
944  C C   . SER A 50  ? 0.0865 0.1308 0.0927 0.0035  0.0125  0.0166  50  SER A C   
945  O O   . SER A 50  ? 0.0829 0.1961 0.1143 0.0061  0.0112  0.0111  50  SER A O   
946  C CB  . SER A 50  ? 0.1026 0.1579 0.1025 0.0003  0.0094  0.0005  50  SER A CB  
947  O OG  . SER A 50  ? 0.1189 0.1473 0.1192 0.0029  0.0229  0.0050  50  SER A OG  
953  N N   . THR A 51  ? 0.0799 0.1166 0.0882 -0.0024 0.0036  0.0226  51  THR A N   
954  C CA  . THR A 51  ? 0.0749 0.1091 0.0879 0.0017  0.0040  0.0155  51  THR A CA  
955  C C   . THR A 51  ? 0.0732 0.1018 0.0791 0.0021  0.0006  0.0086  51  THR A C   
956  O O   . THR A 51  ? 0.0788 0.1192 0.0891 -0.0111 -0.0113 0.0205  51  THR A O   
957  C CB  . THR A 51  ? 0.0901 0.1086 0.1089 -0.0019 -0.0004 0.0087  51  THR A CB  
958  O OG1 . THR A 51  ? 0.1145 0.1181 0.1482 -0.0247 -0.0002 0.0140  51  THR A OG1 
959  C CG2 . THR A 51  ? 0.1125 0.1285 0.1153 0.0026  -0.0097 -0.0118 51  THR A CG2 
967  N N   A ASP A 52  ? 0.0720 0.1130 0.0747 -0.0101 -0.0062 0.0135  52  ASP A N   
968  N N   B ASP A 52  ? 0.0650 0.1248 0.0986 0.0088  0.0091  0.0328  52  ASP A N   
969  C CA  A ASP A 52  ? 0.0845 0.1084 0.0850 -0.0075 0.0037  0.0186  52  ASP A CA  
970  C CA  B ASP A 52  ? 0.0527 0.1097 0.0827 -0.0094 -0.0104 0.0130  52  ASP A CA  
971  C C   A ASP A 52  ? 0.0719 0.1039 0.0800 -0.0070 -0.0084 0.0220  52  ASP A C   
972  C C   B ASP A 52  ? 0.0744 0.1011 0.0829 -0.0089 -0.0062 0.0142  52  ASP A C   
973  O O   A ASP A 52  ? 0.0806 0.1643 0.0886 -0.0158 -0.0035 -0.0053 52  ASP A O   
974  O O   B ASP A 52  ? 0.0819 0.1415 0.0779 -0.0228 -0.0028 0.0068  52  ASP A O   
975  C CB  A ASP A 52  ? 0.1008 0.1101 0.0969 0.0026  -0.0070 0.0152  52  ASP A CB  
976  C CB  B ASP A 52  ? 0.0814 0.1097 0.0856 0.0004  -0.0013 0.0182  52  ASP A CB  
977  C CG  A ASP A 52  ? 0.1463 0.1291 0.1056 0.0165  0.0100  0.0144  52  ASP A CG  
978  C CG  B ASP A 52  ? 0.1462 0.1131 0.0992 0.0117  0.0115  0.0134  52  ASP A CG  
979  O OD1 A ASP A 52  ? 0.2276 0.1650 0.1177 0.0481  -0.0285 -0.0235 52  ASP A OD1 
980  O OD1 B ASP A 52  ? 0.2776 0.1573 0.1136 0.0411  -0.0514 -0.0342 52  ASP A OD1 
981  O OD2 A ASP A 52  ? 0.1513 0.1858 0.1875 0.0252  0.0522  -0.0250 52  ASP A OD2 
982  O OD2 B ASP A 52  ? 0.2269 0.1378 0.1813 0.0707  0.0184  -0.0074 52  ASP A OD2 
991  N N   . TYR A 53  ? 0.0784 0.0986 0.0783 -0.0063 -0.0031 0.0092  53  TYR A N   
992  C CA  . TYR A 53  ? 0.0818 0.0928 0.0826 -0.0018 -0.0050 0.0112  53  TYR A CA  
993  C C   . TYR A 53  ? 0.0768 0.0959 0.0827 0.0030  0.0027  0.0116  53  TYR A C   
994  O O   . TYR A 53  ? 0.0952 0.1072 0.0798 -0.0124 -0.0005 0.0085  53  TYR A O   
995  C CB  . TYR A 53  ? 0.0970 0.1079 0.0948 0.0138  0.0024  0.0220  53  TYR A CB  
996  C CG  . TYR A 53  ? 0.0953 0.1011 0.0911 0.0141  0.0042  0.0157  53  TYR A CG  
997  C CD1 . TYR A 53  ? 0.1773 0.1049 0.0860 0.0101  -0.0081 0.0126  53  TYR A CD1 
998  C CD2 . TYR A 53  ? 0.0803 0.1030 0.0936 0.0059  -0.0013 0.0086  53  TYR A CD2 
999  C CE1 . TYR A 53  ? 0.1606 0.0981 0.1044 0.0046  -0.0120 0.0081  53  TYR A CE1 
1000 C CE2 . TYR A 53  ? 0.0792 0.1207 0.0886 0.0021  -0.0044 0.0139  53  TYR A CE2 
1001 C CZ  . TYR A 53  ? 0.1130 0.1000 0.1001 0.0077  -0.0045 0.0255  53  TYR A CZ  
1002 O OH  . TYR A 53  ? 0.1551 0.1141 0.1085 -0.0106 -0.0109 0.0261  53  TYR A OH  
1012 N N   . GLY A 54  ? 0.0891 0.1018 0.0830 -0.0086 -0.0069 0.0128  54  GLY A N   
1013 C CA  . GLY A 54  ? 0.1116 0.0991 0.0766 0.0061  -0.0021 0.0086  54  GLY A CA  
1014 C C   . GLY A 54  ? 0.0951 0.1050 0.0658 0.0013  -0.0110 0.0053  54  GLY A C   
1015 O O   . GLY A 54  ? 0.0957 0.1091 0.0822 0.0021  -0.0049 0.0075  54  GLY A O   
1019 N N   . ILE A 55  ? 0.0958 0.1064 0.0707 0.0071  -0.0056 0.0128  55  ILE A N   
1020 C CA  . ILE A 55  ? 0.1085 0.1105 0.0728 0.0104  -0.0130 0.0169  55  ILE A CA  
1021 C C   . ILE A 55  ? 0.1004 0.1015 0.0792 -0.0053 -0.0137 0.0218  55  ILE A C   
1022 O O   . ILE A 55  ? 0.1319 0.1054 0.1008 0.0178  -0.0298 0.0157  55  ILE A O   
1023 C CB  . ILE A 55  ? 0.1399 0.1327 0.0912 -0.0009 0.0127  0.0257  55  ILE A CB  
1024 C CG1 . ILE A 55  ? 0.2242 0.1559 0.1230 0.0072  0.0260  0.0496  55  ILE A CG1 
1025 C CG2 . ILE A 55  ? 0.1373 0.2022 0.1320 -0.0148 0.0393  0.0132  55  ILE A CG2 
1026 C CD1 . ILE A 55  ? 0.2672 0.2449 0.1110 0.0391  0.0032  0.0643  55  ILE A CD1 
1038 N N   A LEU A 56  ? 0.0923 0.0975 0.0832 0.0005  -0.0165 0.0175  56  LEU A N   
1039 N N   B LEU A 56  ? 0.0860 0.1076 0.0679 -0.0045 -0.0018 0.0247  56  LEU A N   
1040 C CA  A LEU A 56  ? 0.1038 0.0931 0.0856 -0.0070 -0.0224 0.0171  56  LEU A CA  
1041 C CA  B LEU A 56  ? 0.1046 0.1150 0.0749 -0.0088 -0.0038 0.0164  56  LEU A CA  
1042 C C   A LEU A 56  ? 0.1036 0.0935 0.0917 -0.0040 -0.0161 0.0128  56  LEU A C   
1043 C C   B LEU A 56  ? 0.0869 0.0903 0.0688 0.0049  -0.0162 0.0149  56  LEU A C   
1044 O O   A LEU A 56  ? 0.1356 0.1050 0.0950 -0.0153 -0.0062 0.0006  56  LEU A O   
1045 O O   B LEU A 56  ? 0.0860 0.1088 0.0931 -0.0039 0.0150  -0.0080 56  LEU A O   
1046 C CB  A LEU A 56  ? 0.1134 0.1352 0.1082 -0.0271 -0.0156 0.0107  56  LEU A CB  
1047 C CB  B LEU A 56  ? 0.1098 0.0952 0.0605 -0.0100 -0.0223 0.0519  56  LEU A CB  
1048 C CG  A LEU A 56  ? 0.1247 0.1978 0.1209 -0.0482 -0.0117 0.0328  56  LEU A CG  
1049 C CG  B LEU A 56  ? 0.1454 0.0855 0.1115 -0.0066 0.0012  0.0645  56  LEU A CG  
1050 C CD1 A LEU A 56  ? 0.1227 0.2335 0.2519 -0.0638 -0.0057 0.0355  56  LEU A CD1 
1051 C CD1 B LEU A 56  ? 0.1526 0.1585 0.1341 -0.0364 0.0143  0.0791  56  LEU A CD1 
1052 C CD2 A LEU A 56  ? 0.1747 0.2109 0.1832 -0.0337 -0.0170 0.0829  56  LEU A CD2 
1053 C CD2 B LEU A 56  ? 0.1766 0.0669 0.1204 -0.0283 0.0060  0.0315  56  LEU A CD2 
1076 N N   . GLN A 57  ? 0.0924 0.0918 0.0780 0.0006  -0.0095 0.0101  57  GLN A N   
1077 C CA  . GLN A 57  ? 0.0927 0.0942 0.0744 0.0035  -0.0094 0.0132  57  GLN A CA  
1078 C C   . GLN A 57  ? 0.0960 0.1015 0.0798 0.0005  -0.0054 0.0085  57  GLN A C   
1079 O O   . GLN A 57  ? 0.1257 0.1645 0.0838 0.0264  -0.0056 -0.0085 57  GLN A O   
1080 C CB  . GLN A 57  ? 0.0940 0.0987 0.0941 0.0087  -0.0055 0.0174  57  GLN A CB  
1081 C CG  . GLN A 57  ? 0.1004 0.1101 0.1029 0.0153  -0.0161 0.0252  57  GLN A CG  
1082 C CD  . GLN A 57  ? 0.0918 0.1262 0.0977 0.0019  -0.0103 0.0184  57  GLN A CD  
1083 O OE1 . GLN A 57  ? 0.1040 0.1593 0.1411 -0.0041 0.0159  0.0234  57  GLN A OE1 
1084 N NE2 . GLN A 57  ? 0.1111 0.1172 0.1229 -0.0160 0.0038  -0.0003 57  GLN A NE2 
1093 N N   . ILE A 58  ? 0.0894 0.1054 0.0745 0.0038  -0.0127 0.0090  58  ILE A N   
1094 C CA  . ILE A 58  ? 0.0918 0.1100 0.0729 -0.0118 -0.0145 0.0136  58  ILE A CA  
1095 C C   . ILE A 58  ? 0.0815 0.1072 0.0761 -0.0143 -0.0148 0.0110  58  ILE A C   
1096 O O   . ILE A 58  ? 0.1022 0.1159 0.0852 -0.0188 -0.0105 0.0109  58  ILE A O   
1097 C CB  . ILE A 58  ? 0.0840 0.1337 0.0830 -0.0065 -0.0110 0.0200  58  ILE A CB  
1098 C CG1 . ILE A 58  ? 0.1060 0.1720 0.0983 -0.0224 -0.0088 0.0438  58  ILE A CG1 
1099 C CG2 . ILE A 58  ? 0.0933 0.1595 0.1048 -0.0131 -0.0258 0.0297  58  ILE A CG2 
1100 C CD1 . ILE A 58  ? 0.1117 0.2311 0.1448 -0.0327 0.0031  0.0522  58  ILE A CD1 
1112 N N   . ASN A 59  ? 0.1048 0.1235 0.0762 -0.0237 -0.0135 0.0136  59  ASN A N   
1113 C CA  . ASN A 59  ? 0.0979 0.1199 0.0787 -0.0209 -0.0073 0.0115  59  ASN A CA  
1114 C C   . ASN A 59  ? 0.0871 0.1247 0.0697 -0.0181 -0.0011 0.0104  59  ASN A C   
1115 O O   . ASN A 59  ? 0.0968 0.1467 0.1136 -0.0294 -0.0223 0.0229  59  ASN A O   
1116 C CB  . ASN A 59  ? 0.1173 0.1226 0.1000 -0.0088 0.0037  0.0070  59  ASN A CB  
1117 C CG  . ASN A 59  ? 0.1210 0.1226 0.0895 0.0024  0.0108  0.0022  59  ASN A CG  
1118 O OD1 . ASN A 59  ? 0.1356 0.1650 0.0970 0.0135  0.0031  0.0143  59  ASN A OD1 
1119 N ND2 . ASN A 59  ? 0.1157 0.1793 0.1180 -0.0078 0.0047  0.0317  59  ASN A ND2 
1126 N N   . SER A 60  ? 0.0774 0.1214 0.0808 -0.0104 -0.0028 0.0139  60  SER A N   
1127 C CA  . SER A 60  ? 0.0787 0.1258 0.0813 0.0049  0.0018  0.0086  60  SER A CA  
1128 C C   . SER A 60  ? 0.0792 0.1416 0.0777 0.0135  -0.0045 0.0071  60  SER A C   
1129 O O   . SER A 60  ? 0.1258 0.1697 0.0988 0.0421  -0.0202 0.0076  60  SER A O   
1130 C CB  . SER A 60  ? 0.0919 0.1172 0.0938 0.0071  -0.0055 0.0080  60  SER A CB  
1131 O OG  . SER A 60  ? 0.0881 0.1098 0.1146 0.0029  -0.0036 0.0310  60  SER A OG  
1137 N N   . ARG A 61  ? 0.0960 0.1262 0.0742 0.0030  -0.0013 0.0117  61  ARG A N   
1138 C CA  . ARG A 61  ? 0.1039 0.1281 0.0721 0.0033  -0.0062 0.0113  61  ARG A CA  
1139 C C   . ARG A 61  ? 0.1027 0.1248 0.0750 0.0016  -0.0035 0.0102  61  ARG A C   
1140 O O   . ARG A 61  ? 0.1400 0.2010 0.1613 -0.0421 -0.0617 0.0891  61  ARG A O   
1141 C CB  . ARG A 61  ? 0.1096 0.1831 0.0886 0.0098  0.0134  0.0004  61  ARG A CB  
1142 C CG  . ARG A 61  ? 0.1670 0.2263 0.0893 -0.0020 0.0135  -0.0114 61  ARG A CG  
1143 C CD  . ARG A 61  ? 0.2249 0.3007 0.1141 -0.0009 0.0414  -0.0570 61  ARG A CD  
1144 N NE  . ARG A 61  ? 0.2028 0.4258 0.2588 -0.0041 0.0894  -0.1059 61  ARG A NE  
1145 C CZ  . ARG A 61  ? 0.1926 0.3944 0.5159 0.0179  0.1510  -0.0942 61  ARG A CZ  
1146 N NH1 . ARG A 61  ? 0.5639 0.5666 0.8294 0.1803  0.4447  0.1903  61  ARG A NH1 
1147 N NH2 . ARG A 61  ? 0.2187 0.6814 0.6773 -0.0438 0.0598  -0.4158 61  ARG A NH2 
1161 N N   . TRP A 62  ? 0.1016 0.1290 0.1034 0.0149  0.0103  0.0256  62  TRP A N   
1162 C CA  . TRP A 62  ? 0.1194 0.1225 0.1170 -0.0069 0.0301  -0.0062 62  TRP A CA  
1163 C C   . TRP A 62  ? 0.0944 0.1067 0.0838 -0.0013 -0.0014 -0.0016 62  TRP A C   
1164 O O   . TRP A 62  ? 0.0994 0.1681 0.0785 -0.0033 -0.0099 -0.0100 62  TRP A O   
1165 C CB  . TRP A 62  ? 0.1797 0.1353 0.1845 -0.0181 0.0735  -0.0349 62  TRP A CB  
1166 C CG  . TRP A 62  ? 0.1549 0.1872 0.1365 0.0062  -0.0039 -0.0320 62  TRP A CG  
1167 C CD1 . TRP A 62  ? 0.1759 0.2512 0.1476 -0.0209 0.0329  -0.0539 62  TRP A CD1 
1168 C CD2 . TRP A 62  ? 0.1939 0.2022 0.1648 0.0125  -0.0177 -0.0564 62  TRP A CD2 
1169 N NE1 . TRP A 62  ? 0.2158 0.3133 0.1694 -0.0234 0.0314  -0.0882 62  TRP A NE1 
1170 C CE2 . TRP A 62  ? 0.2056 0.2615 0.1825 0.0301  -0.0054 -0.0815 62  TRP A CE2 
1171 C CE3 . TRP A 62  ? 0.3429 0.2176 0.2589 -0.0699 0.0271  -0.0847 62  TRP A CE3 
1172 C CZ2 . TRP A 62  ? 0.2988 0.2802 0.2043 0.0598  -0.0391 -0.1010 62  TRP A CZ2 
1173 C CZ3 . TRP A 62  ? 0.4614 0.1983 0.2718 -0.0098 -0.0149 -0.0720 62  TRP A CZ3 
1174 C CH2 . TRP A 62  ? 0.4327 0.2554 0.3320 0.0248  0.0276  -0.1299 62  TRP A CH2 
1185 N N   . TRP A 63  ? 0.0830 0.0998 0.0883 -0.0016 -0.0071 0.0001  63  TRP A N   
1186 C CA  . TRP A 63  ? 0.0801 0.0947 0.0770 -0.0039 -0.0127 0.0049  63  TRP A CA  
1187 C C   . TRP A 63  ? 0.0851 0.1030 0.0702 -0.0054 -0.0120 0.0039  63  TRP A C   
1188 O O   . TRP A 63  ? 0.0878 0.1089 0.1381 -0.0041 0.0032  -0.0145 63  TRP A O   
1189 C CB  . TRP A 63  ? 0.1094 0.1086 0.0906 -0.0041 -0.0256 0.0133  63  TRP A CB  
1190 C CG  . TRP A 63  ? 0.1196 0.0986 0.1026 0.0026  -0.0118 0.0176  63  TRP A CG  
1191 C CD1 . TRP A 63  ? 0.1215 0.1163 0.1858 0.0128  -0.0039 0.0117  63  TRP A CD1 
1192 C CD2 . TRP A 63  ? 0.1337 0.0959 0.0968 -0.0031 -0.0063 0.0117  63  TRP A CD2 
1193 N NE1 . TRP A 63  ? 0.1609 0.1124 0.2121 0.0225  0.0257  0.0073  63  TRP A NE1 
1194 C CE2 . TRP A 63  ? 0.1802 0.0982 0.1224 0.0040  0.0099  0.0155  63  TRP A CE2 
1195 C CE3 . TRP A 63  ? 0.1366 0.1153 0.0985 -0.0185 -0.0182 0.0164  63  TRP A CE3 
1196 C CZ2 . TRP A 63  ? 0.2345 0.1066 0.1246 -0.0094 0.0231  0.0023  63  TRP A CZ2 
1197 C CZ3 . TRP A 63  ? 0.1815 0.1378 0.1205 -0.0358 -0.0312 0.0088  63  TRP A CZ3 
1198 C CH2 . TRP A 63  ? 0.2390 0.1159 0.1337 -0.0433 -0.0169 -0.0030 63  TRP A CH2 
1209 N N   . CYS A 64  ? 0.0853 0.1226 0.1267 -0.0113 0.0092  -0.0354 64  CYS A N   
1210 C CA  . CYS A 64  ? 0.0883 0.1100 0.1161 -0.0122 0.0024  -0.0249 64  CYS A CA  
1211 C C   . CYS A 64  ? 0.0956 0.1210 0.0961 -0.0100 0.0035  -0.0233 64  CYS A C   
1212 O O   . CYS A 64  ? 0.1180 0.1373 0.1174 -0.0059 0.0197  -0.0191 64  CYS A O   
1213 C CB  . CYS A 64  ? 0.1019 0.1045 0.1084 -0.0104 0.0048  -0.0171 64  CYS A CB  
1214 S SG  . CYS A 64  ? 0.1057 0.1045 0.1177 0.0070  -0.0008 -0.0146 64  CYS A SG  
1219 N N   A ASN A 65  ? 0.0915 0.1213 0.1228 -0.0054 0.0053  -0.0079 65  ASN A N   
1220 N N   B ASN A 65  ? 0.0985 0.1195 0.1089 -0.0037 -0.0014 -0.0105 65  ASN A N   
1221 C CA  A ASN A 65  ? 0.1081 0.1330 0.1083 -0.0076 -0.0121 0.0076  65  ASN A CA  
1222 C CA  B ASN A 65  ? 0.1009 0.1320 0.1220 -0.0017 -0.0080 0.0088  65  ASN A CA  
1223 C C   A ASN A 65  ? 0.1040 0.1051 0.1023 0.0059  -0.0037 0.0082  65  ASN A C   
1224 C C   B ASN A 65  ? 0.1042 0.1023 0.1176 0.0080  0.0012  0.0049  65  ASN A C   
1225 O O   A ASN A 65  ? 0.1135 0.1286 0.1147 0.0043  0.0004  -0.0035 65  ASN A O   
1226 O O   B ASN A 65  ? 0.1305 0.1099 0.1325 0.0034  0.0155  -0.0052 65  ASN A O   
1227 C CB  A ASN A 65  ? 0.1328 0.1538 0.1856 0.0013  -0.0486 0.0128  65  ASN A CB  
1228 C CB  B ASN A 65  ? 0.1146 0.1821 0.1733 0.0089  -0.0200 0.0501  65  ASN A CB  
1229 C CG  A ASN A 65  ? 0.1713 0.1972 0.2373 -0.0012 -0.0706 0.0720  65  ASN A CG  
1230 C CG  B ASN A 65  ? 0.2009 0.1784 0.1940 0.0230  0.0033  0.0658  65  ASN A CG  
1231 O OD1 A ASN A 65  ? 0.1731 0.2136 0.2216 -0.0305 -0.0806 0.0863  65  ASN A OD1 
1232 O OD1 B ASN A 65  ? 0.1435 0.2315 0.1761 -0.0132 -0.0233 0.0637  65  ASN A OD1 
1233 N ND2 A ASN A 65  ? 0.2886 0.3139 0.3599 0.1211  -0.0086 0.1482  65  ASN A ND2 
1234 N ND2 B ASN A 65  ? 0.3189 0.1811 0.2272 0.0498  -0.0217 0.0520  65  ASN A ND2 
1247 N N   . ASP A 66  ? 0.1047 0.1123 0.1099 0.0001  -0.0035 -0.0055 66  ASP A N   
1248 C CA  . ASP A 66  ? 0.1064 0.1132 0.1155 -0.0007 -0.0101 -0.0073 66  ASP A CA  
1249 C C   . ASP A 66  ? 0.1334 0.0994 0.1311 0.0038  -0.0163 -0.0028 66  ASP A C   
1250 O O   . ASP A 66  ? 0.1749 0.1210 0.1544 -0.0295 -0.0243 0.0056  66  ASP A O   
1251 C CB  . ASP A 66  ? 0.1070 0.1311 0.1012 -0.0051 -0.0067 0.0115  66  ASP A CB  
1252 C CG  . ASP A 66  ? 0.1166 0.0925 0.1008 -0.0040 0.0017  0.0224  66  ASP A CG  
1253 O OD1 . ASP A 66  ? 0.1320 0.1354 0.1024 0.0104  -0.0013 0.0293  66  ASP A OD1 
1254 O OD2 . ASP A 66  ? 0.1276 0.1315 0.1112 0.0198  0.0070  0.0326  66  ASP A OD2 
1259 N N   A GLY A 67  ? 0.1892 0.1163 0.1443 -0.0168 -0.0365 0.0164  67  GLY A N   
1260 N N   B GLY A 67  ? 0.1551 0.0881 0.1470 0.0242  -0.0317 0.0045  67  GLY A N   
1261 C CA  A GLY A 67  ? 0.2153 0.1247 0.1609 -0.0084 -0.0313 0.0338  67  GLY A CA  
1262 C CA  B GLY A 67  ? 0.2547 0.1190 0.1803 0.0502  -0.0225 0.0458  67  GLY A CA  
1263 C C   A GLY A 67  ? 0.2313 0.1054 0.1811 -0.0355 -0.0230 0.0233  67  GLY A C   
1264 C C   B GLY A 67  ? 0.3104 0.1010 0.1709 0.0288  0.0177  0.0541  67  GLY A C   
1265 O O   A GLY A 67  ? 0.1931 0.1250 0.3008 -0.0450 -0.0523 0.0843  67  GLY A O   
1266 O O   B GLY A 67  ? 0.4467 0.1870 0.2482 0.0295  0.0321  0.1443  67  GLY A O   
1273 N N   . ARG A 68  ? 0.2234 0.1152 0.1374 -0.0223 0.0085  0.0275  68  ARG A N   
1274 C CA  . ARG A 68  ? 0.2525 0.1458 0.2050 -0.0569 0.0671  -0.0005 68  ARG A CA  
1275 C C   . ARG A 68  ? 0.2435 0.1449 0.1634 -0.0567 0.0690  0.0164  68  ARG A C   
1276 O O   . ARG A 68  ? 0.3073 0.1816 0.3279 -0.0775 0.1767  -0.0205 68  ARG A O   
1277 C CB  . ARG A 68  ? 0.2263 0.3550 0.3424 -0.1317 0.0380  -0.1449 68  ARG A CB  
1278 C CG  . ARG A 68  ? 0.4101 0.3937 0.4428 -0.2410 0.1295  -0.2283 68  ARG A CG  
1279 C CD  . ARG A 68  ? 0.5618 0.5066 0.6491 -0.2011 -0.0374 -0.3407 68  ARG A CD  
1280 N NE  . ARG A 68  ? 0.4538 0.5715 0.6456 -0.2036 -0.0896 -0.3185 68  ARG A NE  
1281 C CZ  . ARG A 68  ? 0.3081 0.6321 0.7019 -0.1697 -0.1053 -0.2501 68  ARG A CZ  
1282 N NH1 . ARG A 68  ? 0.9960 0.6375 1.1633 -0.3012 0.2422  -0.2790 68  ARG A NH1 
1283 N NH2 . ARG A 68  ? 0.7783 0.9622 0.6904 -0.1495 0.0512  -0.2976 68  ARG A NH2 
1297 N N   . THR A 69  ? 0.1779 0.1151 0.1326 -0.0039 0.0030  0.0292  69  THR A N   
1298 C CA  . THR A 69  ? 0.1372 0.1202 0.1196 0.0031  0.0109  0.0400  69  THR A CA  
1299 C C   . THR A 69  ? 0.1504 0.1389 0.1124 0.0130  0.0170  0.0342  69  THR A C   
1300 O O   . THR A 69  ? 0.1516 0.2037 0.1143 0.0327  0.0123  0.0424  69  THR A O   
1301 C CB  . THR A 69  ? 0.1287 0.1180 0.1046 0.0003  -0.0009 0.0295  69  THR A CB  
1302 O OG1 . THR A 69  ? 0.1443 0.1196 0.1045 0.0067  -0.0036 0.0265  69  THR A OG1 
1303 C CG2 . THR A 69  ? 0.1594 0.1200 0.1100 -0.0035 0.0042  0.0232  69  THR A CG2 
1311 N N   . PRO A 70  ? 0.1595 0.1414 0.1222 0.0054  0.0316  0.0306  70  PRO A N   
1312 C CA  . PRO A 70  ? 0.1791 0.1694 0.1170 -0.0124 0.0374  0.0341  70  PRO A CA  
1313 C C   . PRO A 70  ? 0.1974 0.1641 0.1211 -0.0169 0.0416  0.0091  70  PRO A C   
1314 O O   . PRO A 70  ? 0.2703 0.1579 0.1736 -0.0321 0.0056  0.0219  70  PRO A O   
1315 C CB  . PRO A 70  ? 0.2045 0.2226 0.1451 -0.0095 0.0587  0.0153  70  PRO A CB  
1316 C CG  . PRO A 70  ? 0.1970 0.3986 0.1873 -0.0559 0.0728  -0.0263 70  PRO A CG  
1317 C CD  . PRO A 70  ? 0.1568 0.2346 0.1696 -0.0096 0.0363  0.0215  70  PRO A CD  
1325 N N   . GLY A 71  ? 0.2142 0.2218 0.1250 -0.0408 0.0288  0.0218  71  GLY A N   
1326 C CA  . GLY A 71  ? 0.2594 0.2937 0.1275 -0.0937 0.0334  -0.0248 71  GLY A CA  
1327 C C   . GLY A 71  ? 0.1836 0.1822 0.1284 -0.0352 0.0050  0.0176  71  GLY A C   
1328 O O   . GLY A 71  ? 0.2659 0.2039 0.2053 -0.0649 0.0518  -0.0284 71  GLY A O   
1332 N N   . SER A 72  ? 0.1797 0.1602 0.1291 -0.0363 0.0113  0.0308  72  SER A N   
1333 C CA  . SER A 72  ? 0.1495 0.1604 0.1248 -0.0306 -0.0024 0.0332  72  SER A CA  
1334 C C   . SER A 72  ? 0.1455 0.1398 0.1059 -0.0154 -0.0139 0.0232  72  SER A C   
1335 O O   . SER A 72  ? 0.1935 0.1815 0.1871 -0.0230 -0.0520 0.0775  72  SER A O   
1336 C CB  . SER A 72  ? 0.2075 0.2470 0.1503 -0.0864 0.0194  -0.0436 72  SER A CB  
1337 O OG  . SER A 72  ? 0.3824 0.3436 0.2665 -0.0943 0.1603  -0.0749 72  SER A OG  
1343 N N   . ARG A 73  ? 0.1172 0.1408 0.0755 -0.0063 -0.0033 0.0145  73  ARG A N   
1344 C CA  . ARG A 73  ? 0.1174 0.1409 0.0731 0.0020  -0.0087 0.0119  73  ARG A CA  
1345 C C   . ARG A 73  ? 0.1104 0.1268 0.0716 -0.0035 -0.0106 0.0068  73  ARG A C   
1346 O O   . ARG A 73  ? 0.1080 0.1874 0.0809 -0.0028 -0.0126 -0.0047 73  ARG A O   
1347 C CB  . ARG A 73  ? 0.1251 0.1488 0.0774 -0.0056 -0.0070 0.0010  73  ARG A CB  
1348 C CG  . ARG A 73  ? 0.1516 0.1567 0.0854 0.0259  -0.0102 0.0008  73  ARG A CG  
1349 C CD  . ARG A 73  ? 0.1604 0.1704 0.1682 0.0086  -0.0304 -0.0344 73  ARG A CD  
1350 N NE  . ARG A 73  ? 0.2678 0.2202 0.1420 0.0711  -0.0114 -0.0505 73  ARG A NE  
1351 C CZ  . ARG A 73  ? 0.1843 0.2888 0.2971 0.0765  -0.0553 -0.1439 73  ARG A CZ  
1352 N NH1 . ARG A 73  ? 0.1679 0.3635 0.6446 0.0281  -0.0374 -0.2984 73  ARG A NH1 
1353 N NH2 . ARG A 73  ? 0.3587 0.3761 0.2973 0.1215  0.0272  -0.1611 73  ARG A NH2 
1367 N N   . ASN A 74  ? 0.1004 0.1247 0.0722 -0.0101 -0.0066 0.0041  74  ASN A N   
1368 C CA  . ASN A 74  ? 0.1017 0.1057 0.0744 -0.0077 -0.0092 0.0063  74  ASN A CA  
1369 C C   . ASN A 74  ? 0.0924 0.1111 0.0647 -0.0037 -0.0046 0.0018  74  ASN A C   
1370 O O   . ASN A 74  ? 0.0965 0.1129 0.0982 0.0041  -0.0077 -0.0003 74  ASN A O   
1371 C CB  . ASN A 74  ? 0.1224 0.1106 0.1023 -0.0080 0.0015  0.0064  74  ASN A CB  
1372 C CG  . ASN A 74  ? 0.1059 0.1144 0.1142 -0.0107 0.0014  -0.0078 74  ASN A CG  
1373 O OD1 . ASN A 74  ? 0.1098 0.1485 0.0933 0.0034  -0.0009 -0.0148 74  ASN A OD1 
1374 N ND2 . ASN A 74  ? 0.1636 0.1257 0.1706 0.0144  0.0350  -0.0013 74  ASN A ND2 
1381 N N   . LEU A 75  ? 0.0846 0.1111 0.0693 -0.0010 -0.0080 0.0014  75  LEU A N   
1382 C CA  . LEU A 75  ? 0.0901 0.1134 0.0684 -0.0077 -0.0181 0.0011  75  LEU A CA  
1383 C C   . LEU A 75  ? 0.0878 0.1104 0.0712 -0.0050 -0.0069 -0.0051 75  LEU A C   
1384 O O   . LEU A 75  ? 0.0938 0.1550 0.0883 -0.0288 -0.0089 -0.0092 75  LEU A O   
1385 C CB  . LEU A 75  ? 0.1096 0.1096 0.0762 -0.0043 -0.0092 0.0004  75  LEU A CB  
1386 C CG  . LEU A 75  ? 0.1250 0.1252 0.0740 -0.0097 -0.0078 -0.0121 75  LEU A CG  
1387 C CD1 . LEU A 75  ? 0.1781 0.1518 0.1120 0.0276  -0.0007 -0.0278 75  LEU A CD1 
1388 C CD2 . LEU A 75  ? 0.1584 0.1591 0.0861 -0.0053 -0.0219 -0.0065 75  LEU A CD2 
1400 N N   . CYS A 76  ? 0.0847 0.1094 0.0666 -0.0063 -0.0073 -0.0016 76  CYS A N   
1401 C CA  . CYS A 76  ? 0.0878 0.1053 0.0728 -0.0121 -0.0051 0.0038  76  CYS A CA  
1402 C C   . CYS A 76  ? 0.0834 0.1178 0.0761 -0.0009 -0.0065 0.0036  76  CYS A C   
1403 O O   . CYS A 76  ? 0.1176 0.1347 0.0895 0.0130  0.0120  0.0040  76  CYS A O   
1404 C CB  . CYS A 76  ? 0.1059 0.1014 0.0719 0.0035  -0.0069 0.0010  76  CYS A CB  
1405 S SG  . CYS A 76  ? 0.1288 0.0983 0.0770 0.0006  -0.0146 0.0006  76  CYS A SG  
1410 N N   . ASN A 77  ? 0.0802 0.1108 0.0806 0.0003  -0.0001 0.0017  77  ASN A N   
1411 C CA  . ASN A 77  ? 0.0782 0.1123 0.0908 -0.0037 -0.0075 0.0069  77  ASN A CA  
1412 C C   . ASN A 77  ? 0.0769 0.1192 0.0982 0.0044  -0.0022 -0.0031 77  ASN A C   
1413 O O   . ASN A 77  ? 0.0829 0.1556 0.1309 0.0047  0.0048  -0.0294 77  ASN A O   
1414 C CB  . ASN A 77  ? 0.0829 0.1314 0.1090 -0.0045 -0.0099 0.0026  77  ASN A CB  
1415 C CG  . ASN A 77  ? 0.0799 0.1524 0.1462 0.0027  -0.0124 0.0189  77  ASN A CG  
1416 O OD1 . ASN A 77  ? 0.1121 0.1576 0.1852 0.0105  0.0030  0.0507  77  ASN A OD1 
1417 N ND2 . ASN A 77  ? 0.0775 0.1975 0.2966 0.0151  0.0009  0.0616  77  ASN A ND2 
1424 N N   . ILE A 78  ? 0.0769 0.1154 0.1003 0.0056  -0.0065 -0.0188 78  ILE A N   
1425 C CA  . ILE A 78  ? 0.0801 0.1211 0.1062 0.0031  -0.0055 -0.0204 78  ILE A CA  
1426 C C   . ILE A 78  ? 0.0869 0.1098 0.1051 0.0064  -0.0126 -0.0227 78  ILE A C   
1427 O O   . ILE A 78  ? 0.0902 0.1339 0.1200 -0.0130 0.0094  -0.0394 78  ILE A O   
1428 C CB  . ILE A 78  ? 0.1286 0.1399 0.1036 0.0008  -0.0034 -0.0081 78  ILE A CB  
1429 C CG1 . ILE A 78  ? 0.1408 0.1274 0.1327 0.0007  -0.0155 -0.0029 78  ILE A CG1 
1430 C CG2 . ILE A 78  ? 0.1585 0.1958 0.1450 -0.0108 0.0227  0.0028  78  ILE A CG2 
1431 C CD1 . ILE A 78  ? 0.2271 0.1862 0.2086 0.0260  -0.0865 0.0164  78  ILE A CD1 
1443 N N   . PRO A 79  ? 0.0812 0.1101 0.1267 0.0138  -0.0127 -0.0270 79  PRO A N   
1444 C CA  . PRO A 79  ? 0.0926 0.0939 0.1337 0.0057  -0.0196 -0.0122 79  PRO A CA  
1445 C C   . PRO A 79  ? 0.0826 0.0994 0.1082 -0.0010 -0.0111 -0.0139 79  PRO A C   
1446 O O   . PRO A 79  ? 0.0927 0.1104 0.1129 -0.0017 -0.0025 -0.0045 79  PRO A O   
1447 C CB  . PRO A 79  ? 0.1263 0.1002 0.1831 0.0088  -0.0356 -0.0336 79  PRO A CB  
1448 C CG  . PRO A 79  ? 0.1428 0.1250 0.2267 0.0134  0.0000  -0.0673 79  PRO A CG  
1449 C CD  . PRO A 79  ? 0.1154 0.1188 0.1554 0.0232  -0.0028 -0.0355 79  PRO A CD  
1457 N N   . CYS A 80  ? 0.0895 0.1045 0.0942 0.0040  -0.0054 -0.0038 80  CYS A N   
1458 C CA  . CYS A 80  ? 0.0890 0.0883 0.1065 0.0063  -0.0060 -0.0075 80  CYS A CA  
1459 C C   . CYS A 80  ? 0.0856 0.0852 0.1066 0.0029  -0.0020 0.0021  80  CYS A C   
1460 O O   . CYS A 80  ? 0.1048 0.1053 0.1097 0.0125  -0.0036 0.0100  80  CYS A O   
1461 C CB  . CYS A 80  ? 0.0947 0.1045 0.0998 0.0058  -0.0036 -0.0057 80  CYS A CB  
1462 S SG  . CYS A 80  ? 0.0911 0.1145 0.0994 -0.0003 0.0001  -0.0048 80  CYS A SG  
1467 N N   . SER A 81  ? 0.0963 0.0921 0.1005 -0.0096 -0.0124 0.0002  81  SER A N   
1468 C CA  . SER A 81  ? 0.1222 0.0938 0.1054 -0.0133 -0.0168 -0.0022 81  SER A CA  
1469 C C   . SER A 81  ? 0.1226 0.0745 0.0996 -0.0038 -0.0151 -0.0062 81  SER A C   
1470 O O   . SER A 81  ? 0.1572 0.1070 0.1001 -0.0130 -0.0210 -0.0073 81  SER A O   
1471 C CB  . SER A 81  ? 0.1855 0.0961 0.1340 -0.0363 -0.0170 -0.0098 81  SER A CB  
1472 O OG  . SER A 81  ? 0.2075 0.0986 0.2084 0.0177  -0.0013 0.0045  81  SER A OG  
1478 N N   . ALA A 82  ? 0.1106 0.0885 0.1000 0.0011  -0.0069 -0.0036 82  ALA A N   
1479 C CA  . ALA A 82  ? 0.1105 0.1034 0.1053 0.0048  0.0042  -0.0085 82  ALA A CA  
1480 C C   . ALA A 82  ? 0.1048 0.0985 0.1005 -0.0086 -0.0002 -0.0002 82  ALA A C   
1481 O O   . ALA A 82  ? 0.1334 0.1389 0.1194 0.0126  0.0179  0.0233  82  ALA A O   
1482 C CB  . ALA A 82  ? 0.1032 0.1365 0.1419 0.0037  -0.0003 0.0151  82  ALA A CB  
1488 N N   . LEU A 83  ? 0.1004 0.0904 0.1061 0.0016  -0.0063 0.0080  83  LEU A N   
1489 C CA  . LEU A 83  ? 0.1094 0.0876 0.1232 -0.0015 -0.0081 0.0134  83  LEU A CA  
1490 C C   . LEU A 83  ? 0.1275 0.0947 0.1364 -0.0011 -0.0202 0.0161  83  LEU A C   
1491 O O   . LEU A 83  ? 0.1963 0.1069 0.1703 0.0201  -0.0579 0.0241  83  LEU A O   
1492 C CB  . LEU A 83  ? 0.1215 0.0905 0.1348 0.0090  -0.0034 0.0042  83  LEU A CB  
1493 C CG  . LEU A 83  ? 0.1514 0.0974 0.1330 -0.0075 -0.0087 0.0038  83  LEU A CG  
1494 C CD1 . LEU A 83  ? 0.2263 0.1615 0.1523 0.0246  -0.0055 -0.0383 83  LEU A CD1 
1495 C CD2 . LEU A 83  ? 0.1999 0.1867 0.1835 -0.0752 -0.0420 0.0322  83  LEU A CD2 
1507 N N   . LEU A 84  ? 0.1127 0.1031 0.1146 0.0048  -0.0181 0.0121  84  LEU A N   
1508 C CA  . LEU A 84  ? 0.1284 0.1173 0.1070 -0.0045 -0.0123 0.0077  84  LEU A CA  
1509 C C   . LEU A 84  ? 0.1537 0.1362 0.1167 -0.0063 -0.0031 0.0037  84  LEU A C   
1510 O O   . LEU A 84  ? 0.2202 0.2278 0.1432 -0.0266 -0.0112 -0.0374 84  LEU A O   
1511 C CB  . LEU A 84  ? 0.1248 0.1101 0.1149 -0.0044 -0.0149 0.0028  84  LEU A CB  
1512 C CG  . LEU A 84  ? 0.1300 0.1163 0.1203 -0.0055 -0.0089 0.0204  84  LEU A CG  
1513 C CD1 . LEU A 84  ? 0.1910 0.1432 0.1666 -0.0373 0.0271  0.0100  84  LEU A CD1 
1514 C CD2 . LEU A 84  ? 0.2034 0.1662 0.1452 0.0600  0.0357  0.0404  84  LEU A CD2 
1526 N N   A SER A 85  ? 0.2186 0.1556 0.1679 -0.0494 0.0714  -0.0363 85  SER A N   
1527 N N   B SER A 85  ? 0.1560 0.1694 0.1397 0.0154  0.0193  0.0027  85  SER A N   
1528 C CA  A SER A 85  ? 0.2040 0.1352 0.1555 0.0032  0.0498  -0.0135 85  SER A CA  
1529 C CA  B SER A 85  ? 0.1834 0.1568 0.1412 0.0475  0.0256  0.0125  85  SER A CA  
1530 C C   A SER A 85  ? 0.1483 0.1545 0.1577 0.0141  0.0338  -0.0182 85  SER A C   
1531 C C   B SER A 85  ? 0.1218 0.1347 0.1333 0.0079  0.0001  -0.0079 85  SER A C   
1532 O O   A SER A 85  ? 0.1545 0.1479 0.1444 0.0032  0.0354  -0.0029 85  SER A O   
1533 O O   B SER A 85  ? 0.1646 0.1226 0.1486 0.0091  0.0224  0.0066  85  SER A O   
1534 C CB  A SER A 85  ? 0.2027 0.1155 0.1670 0.0169  0.0420  0.0513  85  SER A CB  
1535 C CB  B SER A 85  ? 0.1797 0.1659 0.1556 0.0713  0.0273  0.0575  85  SER A CB  
1536 O OG  A SER A 85  ? 0.1856 0.1779 0.1750 0.0128  0.0165  0.0355  85  SER A OG  
1537 O OG  B SER A 85  ? 0.1779 0.2701 0.1731 0.0683  0.0365  0.0108  85  SER A OG  
1548 N N   A SER A 86  ? 0.1370 0.1928 0.1724 0.0186  -0.0440 -0.0415 86  SER A N   
1549 N N   B SER A 86  ? 0.1026 0.1511 0.1242 0.0052  -0.0267 -0.0132 86  SER A N   
1550 C CA  A SER A 86  ? 0.1713 0.2424 0.1439 0.0227  -0.0478 -0.0365 86  SER A CA  
1551 C CA  B SER A 86  ? 0.1436 0.1710 0.1328 0.0003  -0.0468 -0.0025 86  SER A CA  
1552 C C   A SER A 86  ? 0.1591 0.2255 0.1303 0.0411  -0.0112 -0.0120 86  SER A C   
1553 C C   B SER A 86  ? 0.1490 0.1585 0.0928 0.0113  -0.0153 -0.0167 86  SER A C   
1554 O O   A SER A 86  ? 0.2059 0.2337 0.1790 0.0584  -0.0128 0.0134  86  SER A O   
1555 O O   B SER A 86  ? 0.1688 0.1745 0.1806 0.0326  0.0310  0.0288  86  SER A O   
1556 C CB  A SER A 86  ? 0.3360 0.2679 0.1701 0.0171  -0.0452 -0.0695 86  SER A CB  
1557 C CB  B SER A 86  ? 0.2244 0.2210 0.1337 -0.0523 -0.0648 -0.0085 86  SER A CB  
1558 O OG  A SER A 86  ? 0.4328 0.4024 0.2517 0.1268  -0.1056 -0.1931 86  SER A OG  
1559 O OG  B SER A 86  ? 0.2814 0.4280 0.2278 -0.1609 -0.0417 -0.0882 86  SER A OG  
1570 N N   A ASP A 87  ? 0.1607 0.1631 0.1190 0.0122  -0.0179 -0.0346 87  ASP A N   
1571 N N   B ASP A 87  ? 0.1416 0.1415 0.0986 0.0077  0.0122  -0.0174 87  ASP A N   
1572 C CA  A ASP A 87  ? 0.1527 0.1726 0.1300 0.0143  0.0083  -0.0452 87  ASP A CA  
1573 C CA  B ASP A 87  ? 0.1407 0.1394 0.1111 0.0148  -0.0149 -0.0206 87  ASP A CA  
1574 C C   A ASP A 87  ? 0.1444 0.1695 0.1217 -0.0234 0.0266  -0.0382 87  ASP A C   
1575 C C   B ASP A 87  ? 0.1218 0.1571 0.1008 0.0026  -0.0013 -0.0128 87  ASP A C   
1576 O O   A ASP A 87  ? 0.2129 0.1490 0.1473 -0.0265 0.0715  -0.0461 87  ASP A O   
1577 O O   B ASP A 87  ? 0.1958 0.1897 0.1272 -0.0019 0.0165  0.0141  87  ASP A O   
1578 C CB  A ASP A 87  ? 0.1570 0.2134 0.1719 0.0342  -0.0030 -0.0452 87  ASP A CB  
1579 C CB  B ASP A 87  ? 0.1391 0.1669 0.1096 0.0141  -0.0001 -0.0199 87  ASP A CB  
1580 C CG  A ASP A 87  ? 0.1616 0.2593 0.2880 0.0150  0.0550  -0.1088 87  ASP A CG  
1581 C CG  B ASP A 87  ? 0.1647 0.1474 0.1108 0.0499  -0.0047 -0.0355 87  ASP A CG  
1582 O OD1 A ASP A 87  ? 0.2146 0.4384 0.3728 -0.0989 0.1101  -0.2195 87  ASP A OD1 
1583 O OD1 B ASP A 87  ? 0.1974 0.1528 0.1490 0.0353  -0.0240 -0.0143 87  ASP A OD1 
1584 O OD2 A ASP A 87  ? 0.3376 0.4951 0.3401 -0.1163 0.1502  -0.1016 87  ASP A OD2 
1585 O OD2 B ASP A 87  ? 0.2292 0.2044 0.1418 -0.0139 -0.0477 0.0004  87  ASP A OD2 
1594 N N   . ILE A 88  ? 0.1533 0.1572 0.0849 0.0027  -0.0009 -0.0182 88  ILE A N   
1595 C CA  . ILE A 88  ? 0.1232 0.1572 0.0847 0.0012  0.0000  -0.0182 88  ILE A CA  
1596 C C   . ILE A 88  ? 0.1222 0.1431 0.0835 -0.0020 0.0039  -0.0046 88  ILE A C   
1597 O O   . ILE A 88  ? 0.1432 0.1418 0.0852 0.0095  -0.0063 -0.0110 88  ILE A O   
1598 C CB  . ILE A 88  ? 0.1526 0.1652 0.1079 0.0262  -0.0200 -0.0159 88  ILE A CB  
1599 C CG1 . ILE A 88  ? 0.2001 0.1757 0.1107 0.0233  -0.0060 0.0177  88  ILE A CG1 
1600 C CG2 . ILE A 88  ? 0.1950 0.2216 0.1722 0.0359  -0.0722 -0.0309 88  ILE A CG2 
1601 C CD1 . ILE A 88  ? 0.2465 0.1811 0.1760 0.0265  -0.0278 0.0255  88  ILE A CD1 
1613 N N   A THR A 89  ? 0.1330 0.1504 0.0950 0.0124  0.0069  -0.0108 89  THR A N   
1614 N N   B THR A 89  ? 0.1168 0.2218 0.0849 0.0099  -0.0022 -0.0460 89  THR A N   
1615 C CA  A THR A 89  ? 0.1211 0.1502 0.1117 0.0115  0.0051  -0.0144 89  THR A CA  
1616 C CA  B THR A 89  ? 0.1044 0.2112 0.1045 -0.0110 -0.0010 -0.0310 89  THR A CA  
1617 C C   A THR A 89  ? 0.1120 0.1449 0.1111 0.0194  0.0036  -0.0168 89  THR A C   
1618 C C   B THR A 89  ? 0.0837 0.1684 0.1028 0.0005  -0.0157 -0.0168 89  THR A C   
1619 O O   A THR A 89  ? 0.1117 0.1667 0.1103 -0.0065 0.0065  -0.0096 89  THR A O   
1620 O O   B THR A 89  ? 0.1095 0.1523 0.0865 0.0041  -0.0284 0.0026  89  THR A O   
1621 C CB  A THR A 89  ? 0.1353 0.1400 0.1243 0.0059  0.0287  -0.0150 89  THR A CB  
1622 C CB  B THR A 89  ? 0.1060 0.2601 0.1458 0.0104  -0.0057 -0.0702 89  THR A CB  
1623 O OG1 A THR A 89  ? 0.1570 0.1784 0.1320 0.0105  0.0385  0.0020  89  THR A OG1 
1624 O OG1 B THR A 89  ? 0.1377 0.3033 0.1576 0.0535  0.0165  -0.0460 89  THR A OG1 
1625 C CG2 A THR A 89  ? 0.1268 0.2093 0.1691 0.0305  0.0128  -0.0076 89  THR A CG2 
1626 C CG2 B THR A 89  ? 0.1176 0.3620 0.1875 0.0532  -0.0233 -0.0927 89  THR A CG2 
1641 N N   . ALA A 90  ? 0.1152 0.1411 0.1055 0.0205  -0.0084 -0.0145 90  ALA A N   
1642 C CA  . ALA A 90  ? 0.1177 0.1187 0.1135 0.0155  -0.0246 -0.0093 90  ALA A CA  
1643 C C   . ALA A 90  ? 0.1098 0.1073 0.0885 0.0045  -0.0121 0.0063  90  ALA A C   
1644 O O   . ALA A 90  ? 0.1265 0.1221 0.0880 0.0109  -0.0206 -0.0001 90  ALA A O   
1645 C CB  . ALA A 90  ? 0.1743 0.1152 0.1569 0.0117  -0.0061 -0.0016 90  ALA A CB  
1651 N N   . SER A 91  ? 0.1004 0.1155 0.0785 0.0070  -0.0114 -0.0056 91  SER A N   
1652 C CA  . SER A 91  ? 0.0958 0.1085 0.0843 0.0010  -0.0018 -0.0015 91  SER A CA  
1653 C C   . SER A 91  ? 0.0914 0.1145 0.0834 0.0055  -0.0077 0.0004  91  SER A C   
1654 O O   . SER A 91  ? 0.1167 0.1214 0.0941 -0.0001 -0.0008 -0.0191 91  SER A O   
1655 C CB  . SER A 91  ? 0.0991 0.1259 0.0946 -0.0016 -0.0087 0.0012  91  SER A CB  
1656 O OG  . SER A 91  ? 0.0994 0.1461 0.1345 -0.0152 -0.0069 0.0063  91  SER A OG  
1662 N N   . VAL A 92  ? 0.1099 0.1104 0.0825 -0.0008 -0.0025 -0.0001 92  VAL A N   
1663 C CA  . VAL A 92  ? 0.1364 0.1089 0.0835 -0.0030 -0.0035 0.0019  92  VAL A CA  
1664 C C   . VAL A 92  ? 0.1061 0.1174 0.0895 -0.0176 0.0039  0.0012  92  VAL A C   
1665 O O   . VAL A 92  ? 0.1329 0.1235 0.1049 -0.0217 -0.0040 -0.0058 92  VAL A O   
1666 C CB  . VAL A 92  ? 0.2155 0.1342 0.0921 -0.0477 0.0026  0.0175  92  VAL A CB  
1667 C CG1 . VAL A 92  ? 0.2383 0.1721 0.1431 -0.0742 0.0204  0.0245  92  VAL A CG1 
1668 C CG2 . VAL A 92  ? 0.3139 0.1687 0.1090 -0.0447 -0.0463 0.0329  92  VAL A CG2 
1678 N N   . ASN A 93  ? 0.1037 0.1305 0.0946 -0.0099 0.0020  -0.0012 93  ASN A N   
1679 C CA  . ASN A 93  ? 0.0977 0.1587 0.1071 -0.0140 -0.0009 0.0029  93  ASN A CA  
1680 C C   . ASN A 93  ? 0.0997 0.1222 0.0964 -0.0080 -0.0131 0.0004  93  ASN A C   
1681 O O   . ASN A 93  ? 0.1084 0.1574 0.1103 -0.0189 -0.0163 -0.0063 93  ASN A O   
1682 C CB  . ASN A 93  ? 0.1107 0.2069 0.1365 0.0303  -0.0089 -0.0180 93  ASN A CB  
1683 C CG  . ASN A 93  ? 0.1074 0.2620 0.1808 0.0084  0.0139  -0.0350 93  ASN A CG  
1684 O OD1 . ASN A 93  ? 0.1918 0.3279 0.2787 -0.0250 0.0768  0.0224  93  ASN A OD1 
1685 N ND2 . ASN A 93  ? 0.1723 0.3180 0.2002 0.0908  0.0133  -0.0498 93  ASN A ND2 
1692 N N   . CYS A 94  ? 0.0991 0.1065 0.0830 -0.0065 -0.0059 0.0002  94  CYS A N   
1693 C CA  . CYS A 94  ? 0.1076 0.0982 0.0780 -0.0033 -0.0123 0.0051  94  CYS A CA  
1694 C C   . CYS A 94  ? 0.0987 0.1026 0.0760 -0.0049 -0.0112 0.0046  94  CYS A C   
1695 O O   . CYS A 94  ? 0.1442 0.1022 0.0761 -0.0013 -0.0178 -0.0011 94  CYS A O   
1696 C CB  . CYS A 94  ? 0.1115 0.1022 0.0840 -0.0057 -0.0144 0.0058  94  CYS A CB  
1697 S SG  . CYS A 94  ? 0.1019 0.1125 0.0899 0.0073  -0.0047 0.0116  94  CYS A SG  
1702 N N   . ALA A 95  ? 0.0989 0.0952 0.0813 -0.0016 -0.0121 0.0002  95  ALA A N   
1703 C CA  . ALA A 95  ? 0.1045 0.1048 0.0918 0.0060  -0.0070 -0.0017 95  ALA A CA  
1704 C C   . ALA A 95  ? 0.1238 0.0955 0.0842 -0.0049 -0.0097 0.0035  95  ALA A C   
1705 O O   . ALA A 95  ? 0.1499 0.1051 0.1100 -0.0103 0.0087  -0.0097 95  ALA A O   
1706 C CB  . ALA A 95  ? 0.1307 0.1219 0.1210 0.0253  -0.0356 0.0027  95  ALA A CB  
1712 N N   . LYS A 96  ? 0.1231 0.1084 0.0910 -0.0186 -0.0018 0.0015  96  LYS A N   
1713 C CA  . LYS A 96  ? 0.1328 0.1090 0.1056 -0.0284 -0.0060 0.0059  96  LYS A CA  
1714 C C   . LYS A 96  ? 0.1258 0.1492 0.1114 -0.0470 -0.0170 -0.0015 96  LYS A C   
1715 O O   . LYS A 96  ? 0.2064 0.1669 0.1243 -0.0752 -0.0122 -0.0207 96  LYS A O   
1716 C CB  . LYS A 96  ? 0.1263 0.1516 0.1187 -0.0315 -0.0006 0.0140  96  LYS A CB  
1717 C CG  . LYS A 96  ? 0.1287 0.1460 0.1272 -0.0314 0.0057  0.0171  96  LYS A CG  
1718 C CD  . LYS A 96  ? 0.1473 0.2141 0.1492 -0.0333 0.0284  0.0053  96  LYS A CD  
1719 C CE  . LYS A 96  ? 0.1908 0.2439 0.1539 -0.0322 0.0273  0.0112  96  LYS A CE  
1720 N NZ  . LYS A 96  ? 0.2161 0.3710 0.1644 0.0070  0.0557  0.0422  96  LYS A NZ  
1734 N N   A LYS A 97  ? 0.1260 0.1393 0.0881 -0.0139 -0.0031 -0.0059 97  LYS A N   
1735 N N   B LYS A 97  ? 0.1208 0.1669 0.0996 -0.0573 -0.0333 0.0099  97  LYS A N   
1736 C CA  A LYS A 97  ? 0.0957 0.1403 0.0883 -0.0249 -0.0180 -0.0186 97  LYS A CA  
1737 C CA  B LYS A 97  ? 0.1584 0.2049 0.1001 -0.0249 -0.0358 0.0076  97  LYS A CA  
1738 C C   A LYS A 97  ? 0.1237 0.1083 0.0864 -0.0197 -0.0129 -0.0228 97  LYS A C   
1739 C C   B LYS A 97  ? 0.1737 0.1653 0.0996 -0.0311 -0.0240 0.0134  97  LYS A C   
1740 O O   A LYS A 97  ? 0.1659 0.1400 0.0926 -0.0150 -0.0320 -0.0321 97  LYS A O   
1741 O O   B LYS A 97  ? 0.2070 0.2047 0.1396 -0.0222 -0.0509 -0.0260 97  LYS A O   
1742 C CB  A LYS A 97  ? 0.1330 0.1386 0.0937 0.0070  -0.0132 -0.0093 97  LYS A CB  
1743 C CB  B LYS A 97  ? 0.1825 0.2157 0.1310 0.0235  -0.0107 0.0439  97  LYS A CB  
1744 C CG  A LYS A 97  ? 0.2435 0.1465 0.1063 -0.0318 -0.0372 -0.0025 97  LYS A CG  
1745 C CG  B LYS A 97  ? 0.3470 0.2600 0.1337 0.0465  -0.0324 0.0336  97  LYS A CG  
1746 C CD  A LYS A 97  ? 0.3325 0.2192 0.1812 -0.0352 -0.1464 0.0233  97  LYS A CD  
1747 C CD  B LYS A 97  ? 0.4376 0.4335 0.2142 0.0298  -0.1318 -0.0212 97  LYS A CD  
1748 C CE  A LYS A 97  ? 0.5099 0.2525 0.1921 -0.0572 -0.1807 0.0357  97  LYS A CE  
1749 C CE  B LYS A 97  ? 0.4489 0.3425 0.2612 -0.0810 -0.1447 0.0449  97  LYS A CE  
1750 N NZ  A LYS A 97  ? 0.5255 0.3530 0.2455 -0.1864 -0.2586 0.1157  97  LYS A NZ  
1751 N NZ  B LYS A 97  ? 0.6867 0.4116 0.5444 -0.1351 0.1065  0.0800  97  LYS A NZ  
1778 N N   A ILE A 98  ? 0.1220 0.1036 0.0813 -0.0160 -0.0059 -0.0156 98  ILE A N   
1779 N N   B ILE A 98  ? 0.1690 0.1288 0.0875 -0.0281 -0.0135 0.0081  98  ILE A N   
1780 C CA  A ILE A 98  ? 0.1244 0.0965 0.0816 -0.0159 0.0052  0.0010  98  ILE A CA  
1781 C CA  B ILE A 98  ? 0.1772 0.1388 0.0802 -0.0178 -0.0146 0.0180  98  ILE A CA  
1782 C C   A ILE A 98  ? 0.1506 0.1048 0.0758 -0.0141 0.0056  -0.0092 98  ILE A C   
1783 C C   B ILE A 98  ? 0.1900 0.1424 0.0966 -0.0187 -0.0269 -0.0048 98  ILE A C   
1784 O O   A ILE A 98  ? 0.2200 0.1227 0.0796 -0.0069 0.0069  -0.0153 98  ILE A O   
1785 O O   B ILE A 98  ? 0.2259 0.1714 0.1156 -0.0249 -0.0158 -0.0286 98  ILE A O   
1786 C CB  A ILE A 98  ? 0.1250 0.0936 0.0920 -0.0134 0.0007  0.0204  98  ILE A CB  
1787 C CB  B ILE A 98  ? 0.1659 0.1366 0.0888 -0.0179 -0.0011 -0.0027 98  ILE A CB  
1788 C CG1 A ILE A 98  ? 0.1065 0.1054 0.1072 -0.0277 -0.0010 0.0334  98  ILE A CG1 
1789 C CG1 B ILE A 98  ? 0.1721 0.1385 0.1327 -0.0212 0.0262  -0.0104 98  ILE A CG1 
1790 C CG2 A ILE A 98  ? 0.1366 0.1369 0.1247 0.0078  0.0036  0.0025  98  ILE A CG2 
1791 C CG2 B ILE A 98  ? 0.1797 0.1564 0.1277 0.0032  -0.0035 -0.0082 98  ILE A CG2 
1792 C CD1 A ILE A 98  ? 0.1405 0.1416 0.1332 -0.0235 -0.0303 -0.0086 98  ILE A CD1 
1793 C CD1 B ILE A 98  ? 0.1557 0.1263 0.1306 -0.0197 0.0338  -0.0113 98  ILE A CD1 
1816 N N   A VAL A 99  ? 0.1526 0.0999 0.0824 -0.0239 0.0063  -0.0080 99  VAL A N   
1817 N N   B VAL A 99  ? 0.1927 0.1204 0.1132 -0.0225 -0.0216 -0.0004 99  VAL A N   
1818 C CA  A VAL A 99  ? 0.2021 0.0959 0.1305 -0.0250 0.0394  -0.0150 99  VAL A CA  
1819 C CA  B VAL A 99  ? 0.2228 0.1216 0.1926 -0.0498 0.0099  -0.0086 99  VAL A CA  
1820 C C   A VAL A 99  ? 0.2308 0.1050 0.1757 -0.0630 0.0036  -0.0397 99  VAL A C   
1821 C C   B VAL A 99  ? 0.2480 0.1696 0.2117 -0.0673 0.0195  -0.0676 99  VAL A C   
1822 O O   A VAL A 99  ? 0.3225 0.1253 0.2437 -0.0407 -0.0225 -0.0848 99  VAL A O   
1823 O O   B VAL A 99  ? 0.3368 0.1823 0.4494 -0.0751 -0.0059 -0.1394 99  VAL A O   
1824 C CB  A VAL A 99  ? 0.2499 0.1085 0.1502 -0.0320 0.0445  0.0122  99  VAL A CB  
1825 C CB  B VAL A 99  ? 0.3063 0.1354 0.2323 0.0181  0.0247  0.0484  99  VAL A CB  
1826 C CG1 A VAL A 99  ? 0.3039 0.1246 0.2501 -0.0723 0.0571  0.0276  99  VAL A CG1 
1827 C CG1 B VAL A 99  ? 0.3001 0.5914 0.2047 0.1555  0.0889  0.1166  99  VAL A CG1 
1828 C CG2 A VAL A 99  ? 0.2718 0.0777 0.1489 -0.0026 0.0261  0.0181  99  VAL A CG2 
1829 C CG2 B VAL A 99  ? 0.2143 0.3519 0.1591 0.0183  -0.0279 0.0036  99  VAL A CG2 
1848 N N   A SER A 100 ? 0.2100 0.1284 0.1180 -0.0578 -0.0032 -0.0197 100 SER A N   
1849 N N   B SER A 100 ? 0.2405 0.2090 0.2045 -0.0678 -0.0274 -0.0743 100 SER A N   
1850 C CA  A SER A 100 ? 0.2269 0.1891 0.1598 -0.0753 -0.0294 -0.0063 100 SER A CA  
1851 C CA  B SER A 100 ? 0.2862 0.2230 0.2203 -0.1035 -0.0420 -0.0762 100 SER A CA  
1852 C C   A SER A 100 ? 0.2602 0.1450 0.1471 -0.0608 -0.0446 -0.0271 100 SER A C   
1853 C C   B SER A 100 ? 0.3587 0.2875 0.2071 -0.0194 -0.0594 -0.0712 100 SER A C   
1854 O O   A SER A 100 ? 0.2658 0.1847 0.1806 -0.0675 -0.0721 -0.0081 100 SER A O   
1855 O O   B SER A 100 ? 0.4079 0.4362 0.2351 -0.1664 -0.0487 -0.1106 100 SER A O   
1856 C CB  A SER A 100 ? 0.1711 0.3284 0.2149 -0.0603 -0.0213 -0.0816 100 SER A CB  
1857 C CB  B SER A 100 ? 0.2058 0.3091 0.2826 -0.1520 -0.0319 -0.0853 100 SER A CB  
1858 O OG  A SER A 100 ? 0.3534 0.3667 0.2592 -0.0892 0.0682  -0.0671 100 SER A OG  
1859 O OG  B SER A 100 ? 0.4043 0.4753 0.3168 0.0786  0.0708  0.0849  100 SER A OG  
1870 N N   A ASP A 101 ? 0.2010 0.1447 0.1248 -0.0099 -0.0480 0.0018  101 ASP A N   
1871 N N   B ASP A 101 ? 0.4031 0.2957 0.1567 -0.0059 -0.0376 -0.0582 101 ASP A N   
1872 C CA  A ASP A 101 ? 0.2316 0.1775 0.1143 0.0033  -0.0735 0.0211  101 ASP A CA  
1873 C CA  B ASP A 101 ? 0.4780 0.3304 0.1720 0.1018  -0.0080 -0.0313 101 ASP A CA  
1874 C C   A ASP A 101 ? 0.3240 0.2247 0.1074 0.0405  -0.0378 0.0064  101 ASP A C   
1875 C C   B ASP A 101 ? 0.5089 0.4121 0.2000 0.1398  0.0199  -0.0267 101 ASP A C   
1876 O O   A ASP A 101 ? 0.6544 0.3220 0.2253 0.1109  0.1833  0.0624  101 ASP A O   
1877 O O   B ASP A 101 ? 0.4711 0.6037 0.1410 0.1880  -0.0872 -0.1199 101 ASP A O   
1878 C CB  A ASP A 101 ? 0.2352 0.1905 0.1090 0.0071  -0.0354 0.0351  101 ASP A CB  
1879 C CB  B ASP A 101 ? 0.4861 0.3398 0.2656 0.0875  0.0337  0.0361  101 ASP A CB  
1880 C CG  A ASP A 101 ? 0.1803 0.1577 0.0661 -0.0331 -0.0200 0.0206  101 ASP A CG  
1881 C CG  B ASP A 101 ? 0.4721 0.3014 0.2574 0.0585  -0.0448 -0.0387 101 ASP A CG  
1882 O OD1 A ASP A 101 ? 0.1916 0.1791 0.1954 -0.0579 -0.0450 0.0285  101 ASP A OD1 
1883 O OD1 B ASP A 101 ? 0.5397 0.4902 0.3328 0.0661  -0.1209 -0.1956 101 ASP A OD1 
1884 O OD2 A ASP A 101 ? 0.1583 0.1627 0.1038 -0.0367 -0.0393 0.0299  101 ASP A OD2 
1885 O OD2 B ASP A 101 ? 0.5820 0.2880 0.4057 0.0504  0.0252  -0.0232 101 ASP A OD2 
1894 N N   A GLY A 102 ? 0.3142 0.1924 0.1706 0.0139  -0.0284 -0.0402 102 GLY A N   
1895 N N   B GLY A 102 ? 0.4158 0.3810 0.1947 0.0890  -0.0267 -0.0680 102 GLY A N   
1896 C CA  A GLY A 102 ? 0.3126 0.2435 0.2803 0.0618  -0.1029 -0.1080 102 GLY A CA  
1897 C CA  B GLY A 102 ? 0.3962 0.3637 0.2862 0.0503  0.0028  -0.0841 102 GLY A CA  
1898 C C   A GLY A 102 ? 0.3035 0.3173 0.2273 0.0572  -0.0762 -0.1440 102 GLY A C   
1899 C C   B GLY A 102 ? 0.4074 0.3467 0.2864 0.0474  0.0208  -0.0644 102 GLY A C   
1900 O O   A GLY A 102 ? 0.3691 0.5390 0.2576 0.1536  -0.0971 -0.2301 102 GLY A O   
1901 O O   B GLY A 102 ? 0.4754 0.3588 0.3893 -0.0134 0.1064  0.0747  102 GLY A O   
1908 N N   A ASN A 103 ? 0.2758 0.2259 0.1439 0.0205  -0.0418 -0.0465 103 ASN A N   
1909 N N   B ASN A 103 ? 0.4481 0.4000 0.1898 0.0526  -0.0442 -0.0400 103 ASN A N   
1910 C CA  A ASN A 103 ? 0.2561 0.2252 0.1367 0.0114  -0.0143 -0.0245 103 ASN A CA  
1911 C CA  B ASN A 103 ? 0.4083 0.4676 0.2215 0.0637  0.0491  0.0279  103 ASN A CA  
1912 C C   A ASN A 103 ? 0.2525 0.2191 0.1851 0.0398  0.0062  0.0056  103 ASN A C   
1913 C C   B ASN A 103 ? 0.3873 0.4149 0.1779 0.1040  0.0392  -0.0306 103 ASN A C   
1914 O O   A ASN A 103 ? 0.3482 0.2424 0.2660 0.0849  0.0972  0.0628  103 ASN A O   
1915 O O   B ASN A 103 ? 0.3481 0.2927 0.1928 0.0535  0.0350  -0.0740 103 ASN A O   
1916 C CB  A ASN A 103 ? 0.2221 0.2104 0.2130 0.0258  -0.0070 -0.0259 103 ASN A CB  
1917 C CB  B ASN A 103 ? 0.4358 0.4881 0.3028 0.0353  0.0738  0.0008  103 ASN A CB  
1918 C CG  A ASN A 103 ? 0.3307 0.2127 0.1675 0.0025  0.0439  -0.0590 103 ASN A CG  
1919 C CG  B ASN A 103 ? 0.4277 0.4759 0.2776 0.0311  0.1233  0.0299  103 ASN A CG  
1920 O OD1 A ASN A 103 ? 0.3464 0.4387 0.2178 0.0449  0.0914  -0.0460 103 ASN A OD1 
1921 O OD1 B ASN A 103 ? 0.7658 0.4947 0.2093 0.0688  0.1548  0.0168  103 ASN A OD1 
1922 N ND2 A ASN A 103 ? 0.3966 0.1985 0.1459 0.0200  0.0334  -0.0178 103 ASN A ND2 
1923 N ND2 B ASN A 103 ? 0.5766 0.5650 0.2108 0.2310  0.0838  0.1211  103 ASN A ND2 
1936 N N   A GLY A 104 ? 0.2497 0.3266 0.1548 0.0823  -0.0661 -0.0138 104 GLY A N   
1937 N N   B GLY A 104 ? 0.2486 0.3670 0.1522 -0.0117 -0.0432 -0.0736 104 GLY A N   
1938 C CA  A GLY A 104 ? 0.1943 0.2130 0.1492 -0.0009 -0.0377 -0.0294 104 GLY A CA  
1939 C CA  B GLY A 104 ? 0.1840 0.3269 0.1497 -0.0070 -0.0327 -0.0827 104 GLY A CA  
1940 C C   A GLY A 104 ? 0.1784 0.1914 0.1219 -0.0146 -0.0104 -0.0080 104 GLY A C   
1941 C C   B GLY A 104 ? 0.1979 0.2068 0.1363 -0.0232 -0.0334 -0.0069 104 GLY A C   
1942 O O   A GLY A 104 ? 0.1789 0.1918 0.1217 -0.0060 -0.0105 0.0026  104 GLY A O   
1943 O O   B GLY A 104 ? 0.3298 0.2010 0.1354 -0.0050 -0.0152 0.0016  104 GLY A O   
1950 N N   . MET A 105 ? 0.1683 0.1710 0.1288 -0.0377 -0.0152 -0.0089 105 MET A N   
1951 C CA  . MET A 105 ? 0.1378 0.1422 0.1338 -0.0277 -0.0017 -0.0139 105 MET A CA  
1952 C C   . MET A 105 ? 0.1514 0.1523 0.1439 -0.0144 0.0080  -0.0278 105 MET A C   
1953 O O   . MET A 105 ? 0.1458 0.1601 0.1519 -0.0163 0.0015  -0.0010 105 MET A O   
1954 C CB  . MET A 105 ? 0.1393 0.1597 0.1327 -0.0193 -0.0154 -0.0082 105 MET A CB  
1955 C CG  . MET A 105 ? 0.1209 0.1760 0.1358 -0.0226 -0.0118 -0.0044 105 MET A CG  
1956 S SD  . MET A 105 ? 0.1788 0.1751 0.1366 -0.0200 -0.0169 0.0126  105 MET A SD  
1957 C CE  . MET A 105 ? 0.1843 0.1769 0.1333 0.0015  -0.0311 -0.0174 105 MET A CE  
1967 N N   . ASN A 106 ? 0.2006 0.2279 0.1719 -0.0279 0.0276  -0.0721 106 ASN A N   
1968 C CA  . ASN A 106 ? 0.2203 0.2716 0.1674 -0.0066 0.0376  -0.0542 106 ASN A CA  
1969 C C   . ASN A 106 ? 0.1960 0.2833 0.1309 -0.0075 0.0282  -0.0418 106 ASN A C   
1970 O O   . ASN A 106 ? 0.2099 0.3382 0.1853 -0.0041 0.0605  -0.0309 106 ASN A O   
1971 C CB  . ASN A 106 ? 0.5813 0.4203 0.3197 -0.1003 0.2140  -0.2447 106 ASN A CB  
1972 C CG  . ASN A 106 ? 0.5897 0.4302 0.3617 -0.0819 0.0334  -0.2647 106 ASN A CG  
1973 O OD1 . ASN A 106 ? 0.5187 0.5833 0.5101 -0.2185 0.0086  -0.0456 106 ASN A OD1 
1974 N ND2 . ASN A 106 ? 0.6744 0.4336 0.7472 -0.1072 -0.1880 -0.1839 106 ASN A ND2 
1981 N N   . ALA A 107 ? 0.1687 0.2677 0.1343 -0.0199 0.0039  0.0164  107 ALA A N   
1982 C CA  . ALA A 107 ? 0.1731 0.2817 0.1250 -0.0243 -0.0116 0.0421  107 ALA A CA  
1983 C C   . ALA A 107 ? 0.1702 0.2198 0.1458 -0.0023 -0.0190 0.0568  107 ALA A C   
1984 O O   . ALA A 107 ? 0.2553 0.2613 0.2068 -0.0699 -0.0482 0.0962  107 ALA A O   
1985 C CB  . ALA A 107 ? 0.1813 0.2788 0.2780 -0.0123 -0.0698 0.0920  107 ALA A CB  
1991 N N   . TRP A 108 ? 0.1293 0.1694 0.1269 0.0007  -0.0057 0.0255  108 TRP A N   
1992 C CA  . TRP A 108 ? 0.1265 0.1283 0.1354 0.0048  -0.0026 0.0114  108 TRP A CA  
1993 C C   . TRP A 108 ? 0.1249 0.1359 0.1340 0.0036  -0.0105 0.0073  108 TRP A C   
1994 O O   . TRP A 108 ? 0.1222 0.1394 0.1732 0.0035  -0.0116 0.0279  108 TRP A O   
1995 C CB  . TRP A 108 ? 0.1266 0.1317 0.1330 0.0076  -0.0134 0.0066  108 TRP A CB  
1996 C CG  . TRP A 108 ? 0.1440 0.1276 0.1188 0.0102  -0.0225 -0.0057 108 TRP A CG  
1997 C CD1 . TRP A 108 ? 0.1522 0.1487 0.1674 -0.0025 -0.0229 -0.0282 108 TRP A CD1 
1998 C CD2 . TRP A 108 ? 0.1273 0.1155 0.1140 0.0076  0.0030  0.0038  108 TRP A CD2 
1999 N NE1 . TRP A 108 ? 0.1631 0.1310 0.1713 0.0033  -0.0066 -0.0375 108 TRP A NE1 
2000 C CE2 . TRP A 108 ? 0.1516 0.1168 0.1148 0.0043  0.0003  -0.0085 108 TRP A CE2 
2001 C CE3 . TRP A 108 ? 0.1512 0.1043 0.1739 0.0032  0.0044  -0.0066 108 TRP A CE3 
2002 C CZ2 . TRP A 108 ? 0.1549 0.1259 0.1406 0.0245  0.0186  0.0064  108 TRP A CZ2 
2003 C CZ3 . TRP A 108 ? 0.1335 0.1375 0.2164 -0.0090 0.0187  -0.0119 108 TRP A CZ3 
2004 C CH2 . TRP A 108 ? 0.1381 0.1509 0.1700 0.0156  0.0166  0.0122  108 TRP A CH2 
2015 N N   A VAL A 109 ? 0.1476 0.1481 0.1272 0.0295  0.0261  0.0391  109 VAL A N   
2016 N N   B VAL A 109 ? 0.1258 0.1236 0.1611 -0.0149 -0.0052 -0.0230 109 VAL A N   
2017 C CA  A VAL A 109 ? 0.1486 0.1731 0.1348 0.0281  0.0265  0.0127  109 VAL A CA  
2018 C CA  B VAL A 109 ? 0.1485 0.1375 0.1323 -0.0025 0.0282  -0.0029 109 VAL A CA  
2019 C C   A VAL A 109 ? 0.0922 0.1367 0.1517 0.0085  -0.0013 -0.0042 109 VAL A C   
2020 C C   B VAL A 109 ? 0.1256 0.1430 0.1464 0.0005  0.0270  0.0050  109 VAL A C   
2021 O O   A VAL A 109 ? 0.1178 0.1379 0.1633 0.0146  0.0210  0.0029  109 VAL A O   
2022 O O   B VAL A 109 ? 0.1156 0.1487 0.1587 0.0011  0.0443  0.0118  109 VAL A O   
2023 C CB  A VAL A 109 ? 0.1609 0.2396 0.2226 0.0328  0.0608  0.0618  109 VAL A CB  
2024 C CB  B VAL A 109 ? 0.1881 0.2098 0.1954 0.0061  0.0799  0.0498  109 VAL A CB  
2025 C CG1 A VAL A 109 ? 0.2042 0.2241 0.3369 -0.0294 0.0659  0.0550  109 VAL A CG1 
2026 C CG1 B VAL A 109 ? 0.1981 0.2663 0.3467 0.0246  0.1323  0.0939  109 VAL A CG1 
2027 C CG2 A VAL A 109 ? 0.2229 0.3066 0.3909 0.0611  0.1608  0.0491  109 VAL A CG2 
2028 C CG2 B VAL A 109 ? 0.2284 0.3505 0.1862 -0.0423 0.0838  0.0871  109 VAL A CG2 
2047 N N   . ALA A 110 ? 0.1222 0.1390 0.1442 0.0107  -0.0088 0.0005  110 ALA A N   
2048 C CA  . ALA A 110 ? 0.1319 0.1573 0.1559 0.0182  -0.0230 -0.0037 110 ALA A CA  
2049 C C   . ALA A 110 ? 0.1387 0.1506 0.1289 0.0331  -0.0103 0.0093  110 ALA A C   
2050 O O   . ALA A 110 ? 0.1650 0.1513 0.1874 0.0369  -0.0427 0.0113  110 ALA A O   
2051 C CB  . ALA A 110 ? 0.2604 0.1748 0.1694 0.0203  -0.0564 -0.0180 110 ALA A CB  
2057 N N   . TRP A 111 ? 0.1317 0.1309 0.1461 0.0307  0.0080  0.0175  111 TRP A N   
2058 C CA  . TRP A 111 ? 0.1332 0.1374 0.1530 0.0300  0.0156  0.0277  111 TRP A CA  
2059 C C   . TRP A 111 ? 0.1097 0.1374 0.1666 0.0297  0.0086  0.0286  111 TRP A C   
2060 O O   . TRP A 111 ? 0.1372 0.1350 0.1856 0.0324  0.0055  0.0270  111 TRP A O   
2061 C CB  . TRP A 111 ? 0.1275 0.1416 0.1656 0.0367  0.0267  0.0219  111 TRP A CB  
2062 C CG  . TRP A 111 ? 0.1285 0.1498 0.1550 0.0301  0.0293  0.0391  111 TRP A CG  
2063 C CD1 . TRP A 111 ? 0.1421 0.1577 0.1544 0.0394  0.0325  0.0327  111 TRP A CD1 
2064 C CD2 . TRP A 111 ? 0.1309 0.1576 0.1680 0.0313  0.0213  0.0224  111 TRP A CD2 
2065 N NE1 . TRP A 111 ? 0.1471 0.1622 0.1808 0.0207  0.0253  0.0479  111 TRP A NE1 
2066 C CE2 . TRP A 111 ? 0.1364 0.1577 0.1835 0.0200  0.0054  0.0398  111 TRP A CE2 
2067 C CE3 . TRP A 111 ? 0.1530 0.1711 0.1707 0.0238  0.0140  0.0183  111 TRP A CE3 
2068 C CZ2 . TRP A 111 ? 0.1752 0.1637 0.2365 0.0116  0.0261  0.0116  111 TRP A CZ2 
2069 C CZ3 . TRP A 111 ? 0.1782 0.1933 0.2113 0.0018  0.0111  -0.0073 111 TRP A CZ3 
2070 C CH2 . TRP A 111 ? 0.2102 0.1813 0.2507 -0.0123 0.0453  -0.0247 111 TRP A CH2 
2081 N N   . ARG A 112 ? 0.1345 0.1384 0.1619 0.0262  0.0084  0.0138  112 ARG A N   
2082 C CA  . ARG A 112 ? 0.1367 0.1594 0.1905 0.0094  0.0065  -0.0109 112 ARG A CA  
2083 C C   . ARG A 112 ? 0.1394 0.1447 0.2428 0.0078  -0.0053 -0.0240 112 ARG A C   
2084 O O   . ARG A 112 ? 0.1681 0.1458 0.4071 0.0231  -0.0304 -0.0444 112 ARG A O   
2085 C CB  . ARG A 112 ? 0.2615 0.2453 0.1789 0.0527  0.0055  -0.0169 112 ARG A CB  
2086 C CG  . ARG A 112 ? 0.4029 0.4058 0.2306 0.1485  -0.0198 -0.1071 112 ARG A CG  
2087 C CD  . ARG A 112 ? 0.7572 0.4696 0.2239 0.1355  0.0628  -0.1136 112 ARG A CD  
2088 N NE  . ARG A 112 ? 0.7108 0.5038 0.2512 0.0862  -0.0697 -0.0423 112 ARG A NE  
2089 C CZ  . ARG A 112 ? 1.0231 0.6206 0.4351 0.2177  0.2005  0.0798  112 ARG A CZ  
2090 N NH1 . ARG A 112 ? 0.7092 0.5169 0.4673 0.0386  0.0708  0.0512  112 ARG A NH1 
2091 N NH2 . ARG A 112 ? 1.1968 0.8695 0.6835 0.4055  0.4077  0.2572  112 ARG A NH2 
2105 N N   A ASN A 113 ? 0.1531 0.1670 0.1807 0.0091  -0.0091 -0.0441 113 ASN A N   
2106 N N   B ASN A 113 ? 0.1095 0.1279 0.2230 0.0408  0.0048  -0.0238 113 ASN A N   
2107 C CA  A ASN A 113 ? 0.1467 0.1833 0.2420 -0.0022 -0.0181 -0.0613 113 ASN A CA  
2108 C CA  B ASN A 113 ? 0.0997 0.1469 0.2529 0.0405  0.0278  -0.0123 113 ASN A CA  
2109 C C   A ASN A 113 ? 0.1275 0.1635 0.2557 0.0390  -0.0200 -0.0274 113 ASN A C   
2110 C C   B ASN A 113 ? 0.1176 0.0955 0.2488 0.0079  -0.0350 -0.0400 113 ASN A C   
2111 O O   A ASN A 113 ? 0.1513 0.1790 0.3432 0.0681  0.0090  0.0184  113 ASN A O   
2112 O O   B ASN A 113 ? 0.1677 0.1238 0.2767 0.0488  -0.0591 -0.0724 113 ASN A O   
2113 C CB  A ASN A 113 ? 0.1423 0.1792 0.2938 0.0293  -0.0086 -0.0019 113 ASN A CB  
2114 C CB  B ASN A 113 ? 0.1259 0.1790 0.2772 0.0050  0.0229  -0.0142 113 ASN A CB  
2115 C CG  A ASN A 113 ? 0.1632 0.2954 0.2873 0.0429  0.0069  0.0090  113 ASN A CG  
2116 C CG  B ASN A 113 ? 0.1663 0.2516 0.2804 -0.0149 0.0544  -0.0096 113 ASN A CG  
2117 O OD1 A ASN A 113 ? 0.3051 0.2469 0.2888 0.0259  -0.0290 0.0299  113 ASN A OD1 
2118 O OD1 B ASN A 113 ? 0.3840 0.3848 0.3617 0.1240  0.1526  -0.0097 113 ASN A OD1 
2119 N ND2 A ASN A 113 ? 0.1821 0.3759 0.2471 -0.0204 -0.0264 0.0308  113 ASN A ND2 
2120 N ND2 B ASN A 113 ? 0.2207 0.4450 0.3150 0.0281  0.0657  0.0961  113 ASN A ND2 
2133 N N   . ARG A 114 ? 0.1152 0.1739 0.2307 0.0349  -0.0136 0.0051  114 ARG A N   
2134 C CA  . ARG A 114 ? 0.1299 0.1821 0.2372 0.0386  -0.0309 0.0129  114 ARG A CA  
2135 C C   . ARG A 114 ? 0.1571 0.1597 0.2120 0.0371  -0.0406 0.0241  114 ARG A C   
2136 O O   . ARG A 114 ? 0.2175 0.2789 0.2357 0.0025  -0.0669 0.0713  114 ARG A O   
2137 C CB  . ARG A 114 ? 0.1296 0.2122 0.2393 0.0070  -0.0605 0.0217  114 ARG A CB  
2138 C CG  . ARG A 114 ? 0.1295 0.2611 0.2618 -0.0194 -0.0626 0.0211  114 ARG A CG  
2139 C CD  . ARG A 114 ? 0.1575 0.3088 0.2139 -0.0475 -0.0415 -0.0011 114 ARG A CD  
2140 N NE  . ARG A 114 ? 0.1170 0.3019 0.2124 -0.0030 -0.0377 -0.0631 114 ARG A NE  
2141 C CZ  . ARG A 114 ? 0.0966 0.3169 0.1917 0.0144  -0.0145 -0.0810 114 ARG A CZ  
2142 N NH1 . ARG A 114 ? 0.1557 0.4363 0.2036 0.0532  -0.0516 -0.0732 114 ARG A NH1 
2143 N NH2 . ARG A 114 ? 0.1409 0.3213 0.2587 -0.0351 0.0225  -0.0911 114 ARG A NH2 
2157 N N   . CYS A 115 ? 0.1352 0.1460 0.1758 0.0442  -0.0046 0.0115  115 CYS A N   
2158 C CA  . CYS A 115 ? 0.1693 0.1274 0.1555 0.0346  -0.0044 0.0138  115 CYS A CA  
2159 C C   . CYS A 115 ? 0.1777 0.1197 0.1594 0.0383  0.0092  0.0101  115 CYS A C   
2160 O O   . CYS A 115 ? 0.2181 0.1276 0.1816 0.0294  0.0337  0.0080  115 CYS A O   
2161 C CB  . CYS A 115 ? 0.1463 0.1243 0.1430 0.0272  0.0109  0.0038  115 CYS A CB  
2162 S SG  . CYS A 115 ? 0.1610 0.1199 0.1443 0.0123  0.0144  0.0074  115 CYS A SG  
2167 N N   . LYS A 116 ? 0.2056 0.1327 0.1655 0.0288  -0.0059 0.0068  116 LYS A N   
2168 C CA  . LYS A 116 ? 0.2416 0.1250 0.1715 0.0394  0.0266  -0.0122 116 LYS A CA  
2169 C C   . LYS A 116 ? 0.3076 0.1538 0.1621 0.0746  0.0691  0.0042  116 LYS A C   
2170 O O   . LYS A 116 ? 0.3097 0.2417 0.2348 0.1373  0.0893  0.0629  116 LYS A O   
2171 C CB  . LYS A 116 ? 0.2434 0.1467 0.1715 0.0346  0.0175  -0.0021 116 LYS A CB  
2172 C CG  . LYS A 116 ? 0.3092 0.1566 0.1890 0.0570  0.0030  -0.0224 116 LYS A CG  
2173 C CD  . LYS A 116 ? 0.2729 0.2084 0.1819 0.0615  -0.0356 0.0012  116 LYS A CD  
2174 C CE  . LYS A 116 ? 0.3313 0.1749 0.2016 0.0386  0.0169  -0.0104 116 LYS A CE  
2175 N NZ  . LYS A 116 ? 0.2790 0.2360 0.2059 0.0307  0.0255  -0.0268 116 LYS A NZ  
2189 N N   A GLY A 117 ? 0.4156 0.1184 0.1960 0.0571  0.0850  0.0075  117 GLY A N   
2190 N N   B GLY A 117 ? 0.3747 0.1529 0.2320 0.1045  0.0961  0.0384  117 GLY A N   
2191 C CA  A GLY A 117 ? 0.4785 0.1613 0.2068 0.1207  0.1508  0.0360  117 GLY A CA  
2192 C CA  B GLY A 117 ? 0.2268 0.1212 0.2531 0.0278  0.1148  0.0127  117 GLY A CA  
2193 C C   A GLY A 117 ? 0.3823 0.1735 0.2199 0.1380  0.1589  0.0532  117 GLY A C   
2194 C C   B GLY A 117 ? 0.1758 0.1287 0.2594 0.0454  0.1327  0.0552  117 GLY A C   
2195 O O   A GLY A 117 ? 0.4887 0.1888 0.2652 0.1800  0.1097  0.0364  117 GLY A O   
2196 O O   B GLY A 117 ? 0.1808 0.0900 0.3079 0.0260  0.0701  0.0056  117 GLY A O   
2203 N N   . THR A 118 ? 0.3058 0.1892 0.2270 0.1277  0.1016  0.0413  118 THR A N   
2204 C CA  . THR A 118 ? 0.2624 0.2217 0.2385 0.1257  0.0818  0.0678  118 THR A CA  
2205 C C   . THR A 118 ? 0.2568 0.2419 0.2321 0.1248  0.0630  0.1150  118 THR A C   
2206 O O   . THR A 118 ? 0.2536 0.2645 0.2344 0.0989  0.0562  0.0486  118 THR A O   
2207 C CB  . THR A 118 ? 0.2473 0.2491 0.2726 0.1082  0.0409  0.0802  118 THR A CB  
2208 O OG1 . THR A 118 ? 0.2283 0.2331 0.2100 0.0898  0.0193  0.0384  118 THR A OG1 
2209 C CG2 . THR A 118 ? 0.2033 0.3396 0.3529 0.0861  0.0650  0.0406  118 THR A CG2 
2217 N N   . ASP A 119 ? 0.3043 0.2242 0.2202 0.1107  0.0491  0.0713  119 ASP A N   
2218 C CA  . ASP A 119 ? 0.3614 0.2635 0.2416 0.1499  0.0891  0.1246  119 ASP A CA  
2219 C C   . ASP A 119 ? 0.2598 0.2700 0.2032 0.1122  0.0322  0.0670  119 ASP A C   
2220 O O   . ASP A 119 ? 0.2862 0.3528 0.2083 0.1099  -0.0129 0.0780  119 ASP A O   
2221 C CB  . ASP A 119 ? 0.5220 0.3852 0.2476 0.2473  0.0845  0.1515  119 ASP A CB  
2222 C CG  . ASP A 119 ? 0.7792 0.3864 0.3276 0.2804  0.2364  0.2316  119 ASP A CG  
2223 O OD1 . ASP A 119 ? 0.7035 0.5126 0.5102 0.2444  0.3600  0.2665  119 ASP A OD1 
2224 O OD2 . ASP A 119 ? 1.2071 0.5768 0.2871 0.4920  0.2317  0.2313  119 ASP A OD2 
2229 N N   . VAL A 120 ? 0.2676 0.2117 0.1868 0.0774  0.0073  0.0371  120 VAL A N   
2230 C CA  . VAL A 120 ? 0.2186 0.1988 0.1816 0.0569  -0.0154 0.0361  120 VAL A CA  
2231 C C   . VAL A 120 ? 0.2657 0.2067 0.1706 0.0935  -0.0211 0.0335  120 VAL A C   
2232 O O   . VAL A 120 ? 0.2920 0.2140 0.1801 0.0968  -0.0317 0.0184  120 VAL A O   
2233 C CB  . VAL A 120 ? 0.2193 0.2052 0.1788 0.0454  -0.0206 0.0360  120 VAL A CB  
2234 C CG1 . VAL A 120 ? 0.2728 0.2222 0.1995 0.0326  0.0083  0.0609  120 VAL A CG1 
2235 C CG2 . VAL A 120 ? 0.2351 0.2431 0.2010 0.0245  -0.0330 0.0364  120 VAL A CG2 
2245 N N   . GLN A 121 ? 0.2863 0.2241 0.1774 0.0616  0.0076  0.0214  121 GLN A N   
2246 C CA  . GLN A 121 ? 0.2907 0.2400 0.1872 0.0900  0.0225  0.0151  121 GLN A CA  
2247 C C   . GLN A 121 ? 0.3105 0.1785 0.1748 0.0760  0.0198  0.0487  121 GLN A C   
2248 O O   . GLN A 121 ? 0.2955 0.1893 0.1886 0.0185  0.0201  0.0185  121 GLN A O   
2249 C CB  . GLN A 121 ? 0.3569 0.2894 0.2334 -0.0040 0.0828  -0.0294 121 GLN A CB  
2250 C CG  . GLN A 121 ? 0.3708 0.5182 0.6106 -0.0331 -0.0631 -0.1250 121 GLN A CG  
2251 C CD  . GLN A 121 ? 0.4563 0.6756 0.9002 -0.1709 0.0833  -0.3174 121 GLN A CD  
2252 O OE1 . GLN A 121 ? 0.4754 0.8368 1.3927 -0.2470 -0.0580 -0.4367 121 GLN A OE1 
2253 N NE2 . GLN A 121 ? 0.9872 0.6628 1.1209 -0.0837 0.4946  -0.2419 121 GLN A NE2 
2262 N N   . ALA A 122 ? 0.3110 0.1938 0.1738 0.0917  0.0013  0.0517  122 ALA A N   
2263 C CA  . ALA A 122 ? 0.3298 0.2239 0.1777 0.0921  -0.0186 0.0664  122 ALA A CA  
2264 C C   . ALA A 122 ? 0.2563 0.2151 0.1679 0.0668  -0.0315 0.0617  122 ALA A C   
2265 O O   . ALA A 122 ? 0.3971 0.2612 0.1654 0.0835  -0.0605 0.0578  122 ALA A O   
2266 C CB  . ALA A 122 ? 0.3263 0.2899 0.2268 0.1261  -0.0332 0.0247  122 ALA A CB  
2272 N N   A TRP A 123 ? 0.2431 0.1956 0.1527 0.0513  -0.0154 0.0535  123 TRP A N   
2273 N N   B TRP A 123 ? 0.2419 0.2026 0.1564 0.0510  -0.0186 0.0582  123 TRP A N   
2274 C CA  A TRP A 123 ? 0.2352 0.1920 0.1593 0.0429  -0.0252 0.0540  123 TRP A CA  
2275 C CA  B TRP A 123 ? 0.2531 0.1978 0.1491 0.0354  -0.0133 0.0671  123 TRP A CA  
2276 C C   A TRP A 123 ? 0.2574 0.1794 0.1543 0.0222  -0.0169 0.0231  123 TRP A C   
2277 C C   B TRP A 123 ? 0.2589 0.1687 0.1441 0.0409  -0.0181 0.0701  123 TRP A C   
2278 O O   A TRP A 123 ? 0.2472 0.1827 0.1989 0.0388  -0.0598 0.0084  123 TRP A O   
2279 O O   B TRP A 123 ? 0.4387 0.1696 0.2381 -0.0226 0.1202  0.0447  123 TRP A O   
2280 C CB  A TRP A 123 ? 0.2530 0.1823 0.1574 0.0336  -0.0230 0.0492  123 TRP A CB  
2281 C CB  B TRP A 123 ? 0.2187 0.2140 0.1529 0.0289  -0.0189 0.0725  123 TRP A CB  
2282 C CG  A TRP A 123 ? 0.2525 0.2018 0.1789 0.0311  -0.0144 0.0574  123 TRP A CG  
2283 C CG  B TRP A 123 ? 0.2086 0.2300 0.1464 0.0564  -0.0282 0.0913  123 TRP A CG  
2284 C CD1 A TRP A 123 ? 0.2464 0.2584 0.1653 0.0357  -0.0227 0.0403  123 TRP A CD1 
2285 C CD1 B TRP A 123 ? 0.2199 0.2746 0.1409 0.0477  -0.0311 0.0721  123 TRP A CD1 
2286 C CD2 A TRP A 123 ? 0.2546 0.2754 0.1543 0.0177  -0.0226 0.0399  123 TRP A CD2 
2287 C CD2 B TRP A 123 ? 0.2161 0.2264 0.1248 0.0441  -0.0184 0.1040  123 TRP A CD2 
2288 N NE1 A TRP A 123 ? 0.2443 0.2376 0.1723 0.0427  -0.0229 0.0560  123 TRP A NE1 
2289 N NE1 B TRP A 123 ? 0.2275 0.2868 0.1378 0.0507  -0.0135 0.0719  123 TRP A NE1 
2290 C CE2 A TRP A 123 ? 0.2560 0.2568 0.1537 0.0179  -0.0168 0.0624  123 TRP A CE2 
2291 C CE2 B TRP A 123 ? 0.2234 0.2443 0.1588 0.0428  -0.0025 0.0941  123 TRP A CE2 
2292 C CE3 A TRP A 123 ? 0.3033 0.2668 0.1457 -0.0280 0.0129  0.0486  123 TRP A CE3 
2293 C CE3 B TRP A 123 ? 0.2885 0.2651 0.1341 -0.0142 0.0144  0.0839  123 TRP A CE3 
2294 C CZ2 A TRP A 123 ? 0.2603 0.2470 0.1910 0.0044  -0.0059 0.0785  123 TRP A CZ2 
2295 C CZ2 B TRP A 123 ? 0.2508 0.3115 0.2030 -0.0026 0.0414  0.0458  123 TRP A CZ2 
2296 C CZ3 A TRP A 123 ? 0.3072 0.2504 0.1744 -0.0248 -0.0051 0.0632  123 TRP A CZ3 
2297 C CZ3 B TRP A 123 ? 0.3031 0.2679 0.1813 -0.0318 0.0225  0.0552  123 TRP A CZ3 
2298 C CH2 A TRP A 123 ? 0.2778 0.2716 0.1932 -0.0162 -0.0180 0.0692  123 TRP A CH2 
2299 C CH2 B TRP A 123 ? 0.2906 0.2836 0.2175 -0.0284 0.0395  0.0607  123 TRP A CH2 
2320 N N   . ILE A 124 ? 0.2538 0.1691 0.1244 0.0401  -0.0118 0.0341  124 ILE A N   
2321 C CA  . ILE A 124 ? 0.2707 0.1653 0.1173 0.0324  -0.0077 0.0296  124 ILE A CA  
2322 C C   . ILE A 124 ? 0.3117 0.1649 0.1229 0.0153  -0.0202 0.0392  124 ILE A C   
2323 O O   . ILE A 124 ? 0.3276 0.1737 0.1291 -0.0023 -0.0024 0.0384  124 ILE A O   
2324 C CB  . ILE A 124 ? 0.2675 0.2272 0.1347 0.0447  -0.0198 0.0217  124 ILE A CB  
2325 C CG1 . ILE A 124 ? 0.2594 0.2495 0.2008 0.0108  -0.0053 0.0025  124 ILE A CG1 
2326 C CG2 . ILE A 124 ? 0.2998 0.2648 0.1684 0.1064  0.0010  0.0641  124 ILE A CG2 
2327 C CD1 . ILE A 124 ? 0.3205 0.5179 0.4143 0.0312  -0.1214 -0.2215 124 ILE A CD1 
2339 N N   . ARG A 125 ? 0.3609 0.1669 0.1268 0.0384  -0.0151 0.0481  125 ARG A N   
2340 C CA  . ARG A 125 ? 0.4060 0.1460 0.1302 -0.0006 -0.0522 0.0425  125 ARG A CA  
2341 C C   . ARG A 125 ? 0.4668 0.1400 0.1404 0.0058  -0.0751 0.0473  125 ARG A C   
2342 O O   . ARG A 125 ? 0.5176 0.1755 0.2138 -0.0330 -0.1208 0.0286  125 ARG A O   
2343 C CB  . ARG A 125 ? 0.4821 0.1650 0.1853 0.0552  -0.0613 0.0476  125 ARG A CB  
2344 C CG  . ARG A 125 ? 0.6393 0.1989 0.2059 0.0753  -0.0675 0.0718  125 ARG A CG  
2345 C CD  . ARG A 125 ? 0.8720 0.2632 0.3180 0.2385  -0.0378 0.1147  125 ARG A CD  
2346 N NE  . ARG A 125 ? 0.9073 0.2104 0.2982 0.1649  0.0989  0.1210  125 ARG A NE  
2347 C CZ  . ARG A 125 ? 0.9498 0.2065 0.4339 0.0692  0.2245  0.1428  125 ARG A CZ  
2348 N NH1 . ARG A 125 ? 0.9484 0.3638 0.6010 0.0586  0.2177  0.0956  125 ARG A NH1 
2349 N NH2 . ARG A 125 ? 0.8908 0.3500 0.3406 0.2920  0.2390  0.1566  125 ARG A NH2 
2363 N N   . GLY A 126 ? 0.5761 0.1456 0.1360 0.0185  -0.0401 0.0332  126 GLY A N   
2364 C CA  . GLY A 126 ? 0.6129 0.1666 0.1429 -0.0150 -0.0553 0.0276  126 GLY A CA  
2365 C C   . GLY A 126 ? 0.6463 0.1553 0.1288 -0.0185 -0.0288 0.0133  126 GLY A C   
2366 O O   . GLY A 126 ? 0.9785 0.2373 0.1489 0.0557  -0.0203 -0.0190 126 GLY A O   
2370 N N   . CYS A 127 ? 0.4880 0.1491 0.1433 -0.0451 0.0175  0.0399  127 CYS A N   
2371 C CA  . CYS A 127 ? 0.4253 0.1632 0.1547 -0.0535 0.0403  0.0177  127 CYS A CA  
2372 C C   . CYS A 127 ? 0.4867 0.2300 0.2608 -0.0740 0.1409  0.0412  127 CYS A C   
2373 O O   . CYS A 127 ? 0.4905 0.2760 0.3890 -0.1180 0.1300  0.0585  127 CYS A O   
2374 C CB  . CYS A 127 ? 0.3106 0.1693 0.1800 -0.0416 0.0188  0.0499  127 CYS A CB  
2375 S SG  . CYS A 127 ? 0.2998 0.1357 0.1700 0.0005  0.0222  0.0334  127 CYS A SG  
2380 N N   . ARG A 128 ? 0.5157 0.2913 0.2561 0.0193  0.1288  0.0595  128 ARG A N   
2381 C CA  . ARG A 128 ? 0.5075 0.4070 0.2763 -0.0082 0.1226  0.0090  128 ARG A CA  
2382 C C   . ARG A 128 ? 0.4793 0.5186 0.3273 -0.0882 0.0778  0.0501  128 ARG A C   
2383 O O   . ARG A 128 ? 0.4282 0.5560 0.4157 -0.0623 0.0129  0.1210  128 ARG A O   
2384 C CB  . ARG A 128 ? 0.5848 0.6318 0.3095 -0.0162 0.1729  -0.0937 128 ARG A CB  
2385 C CG  . ARG A 128 ? 0.8155 0.9098 0.3314 0.0106  0.0043  -0.1332 128 ARG A CG  
2386 C CD  . ARG A 128 ? 0.7948 1.0832 0.5195 -0.0054 -0.0302 -0.2488 128 ARG A CD  
2387 N NE  . ARG A 128 ? 0.5123 0.9701 0.5038 -0.1729 0.0371  -0.2792 128 ARG A NE  
2388 C CZ  . ARG A 128 ? 0.5234 0.9250 0.5569 -0.1609 0.1264  -0.2541 128 ARG A CZ  
2389 N NH1 . ARG A 128 ? 0.5841 0.8799 0.8617 -0.1520 0.2831  -0.1174 128 ARG A NH1 
2390 N NH2 . ARG A 128 ? 0.4486 1.1507 0.5701 -0.1558 0.0384  -0.4155 128 ARG A NH2 
2404 N N   . LEU A 129 ? 0.4953 0.6033 0.3300 -0.1208 0.1200  -0.0257 129 LEU A N   
2405 C CA  . LEU A 129 ? 0.4509 0.6717 0.3620 -0.0386 0.0701  -0.0511 129 LEU A CA  
2406 C C   . LEU A 129 ? 0.5151 0.9567 0.6342 0.1080  0.0887  -0.0556 129 LEU A C   
2407 O O   . LEU A 129 ? 0.5912 1.3045 0.7829 0.2877  0.0886  0.1335  129 LEU A O   
2408 C CB  . LEU A 129 ? 0.4047 0.4659 0.3397 -0.1172 -0.0136 -0.0042 129 LEU A CB  
2409 C CG  . LEU A 129 ? 0.3908 0.3349 0.2625 0.0388  -0.0230 0.0844  129 LEU A CG  
2410 C CD1 . LEU A 129 ? 1.3126 0.4705 0.3034 0.3388  0.2138  0.0862  129 LEU A CD1 
2411 C CD2 . LEU A 129 ? 0.5844 0.4752 0.3284 -0.0193 0.1108  0.2176  129 LEU A CD2 
2412 O OXT . LEU A 129 ? 0.3328 0.9591 0.7249 -0.0904 -0.0276 -0.1118 129 LEU A OXT 
2424 N N   . NO3 B .   ? 0.2686 0.1664 0.1322 -0.0574 0.0140  -0.0090 201 NO3 A N   
2425 O O1  . NO3 B .   ? 0.3629 0.2019 0.2800 -0.0964 0.0278  0.0509  201 NO3 A O1  
2426 O O2  . NO3 B .   ? 0.3236 0.1748 0.3031 0.0098  0.0826  -0.0259 201 NO3 A O2  
2427 O O3  . NO3 B .   ? 0.2403 0.2206 0.2584 -0.0640 -0.0282 0.0905  201 NO3 A O3  
2428 N N   . NO3 C .   ? 0.3956 0.2292 0.2328 0.0772  -0.1613 -0.0351 202 NO3 A N   
2429 O O1  . NO3 C .   ? 0.3367 0.5014 0.2881 -0.0104 -0.1584 -0.0422 202 NO3 A O1  
2430 O O2  . NO3 C .   ? 0.7970 0.2278 0.3703 0.0874  -0.1281 -0.0871 202 NO3 A O2  
2431 O O3  . NO3 C .   ? 0.3582 0.2375 0.2950 0.0282  -0.1512 -0.0798 202 NO3 A O3  
2432 N N   . NO3 D .   ? 0.5822 0.3061 0.2970 0.0454  -0.0105 0.0185  203 NO3 A N   
2433 O O1  . NO3 D .   ? 0.5441 0.3378 0.1637 0.0933  0.0683  -0.0397 203 NO3 A O1  
2434 O O2  . NO3 D .   ? 0.7306 0.2949 0.4053 -0.0812 -0.1807 0.0548  203 NO3 A O2  
2435 O O3  . NO3 D .   ? 0.5189 0.3867 0.4789 0.1251  0.0434  0.1631  203 NO3 A O3  
2436 N N   . NO3 E .   ? 0.2438 0.3826 0.6304 -0.1346 -0.1167 0.1990  204 NO3 A N   
2437 O O1  . NO3 E .   ? 0.2958 0.5110 0.7351 -0.0627 -0.0492 0.3178  204 NO3 A O1  
2438 O O2  . NO3 E .   ? 0.3949 0.2814 0.5964 -0.1354 -0.1859 0.1090  204 NO3 A O2  
2439 O O3  . NO3 E .   ? 0.2643 0.5708 0.6960 -0.1060 -0.0318 0.2116  204 NO3 A O3  
2440 N N   . NO3 F .   ? 0.2346 0.1636 0.2294 0.0369  0.0601  -0.0464 205 NO3 A N   
2441 O O1  . NO3 F .   ? 0.2800 0.3115 0.5216 0.0162  0.1744  0.0105  205 NO3 A O1  
2442 O O2  . NO3 F .   ? 0.2326 0.1727 0.2095 0.0268  0.0041  -0.0196 205 NO3 A O2  
2443 O O3  . NO3 F .   ? 0.3810 0.2095 0.5038 0.1189  0.1348  0.0341  205 NO3 A O3  
2444 N N   . NO3 G .   ? 0.8312 0.9892 0.3212 0.3659  -0.0943 -0.0194 206 NO3 A N   
2445 O O1  . NO3 G .   ? 0.2537 0.9890 0.3291 0.0449  -0.0373 0.0844  206 NO3 A O1  
2446 O O2  . NO3 G .   ? 0.7018 1.1368 0.4128 0.4249  0.1174  0.1834  206 NO3 A O2  
2447 O O3  . NO3 G .   ? 0.2614 0.9941 0.4530 -0.1106 0.1672  -0.1176 206 NO3 A O3  
2448 N N   . NO3 H .   ? 0.3610 0.2223 0.2634 -0.1019 -0.0966 0.0736  207 NO3 A N   
2449 O O1  . NO3 H .   ? 0.4872 0.1631 0.3208 -0.0413 0.0599  0.0440  207 NO3 A O1  
2450 O O2  . NO3 H .   ? 0.4653 0.1666 0.3338 -0.0979 0.0069  0.0498  207 NO3 A O2  
2451 O O3  . NO3 H .   ? 0.3768 0.1917 0.2058 -0.1164 -0.0944 0.0789  207 NO3 A O3  
2452 N N   . NO3 I .   ? 0.3130 0.2628 0.2208 -0.0228 -0.0052 -0.0876 208 NO3 A N   
2453 O O1  . NO3 I .   ? 0.3908 0.2752 0.4194 -0.0403 0.1660  -0.0891 208 NO3 A O1  
2454 O O2  . NO3 I .   ? 0.3865 0.2241 0.2016 0.0971  0.0818  -0.0016 208 NO3 A O2  
2455 O O3  . NO3 I .   ? 0.3030 0.2670 0.3494 -0.0307 0.0189  -0.0628 208 NO3 A O3  
2456 N N   . NO3 J .   ? 0.3158 0.0831 0.1853 -0.0009 -0.0311 0.0164  209 NO3 A N   
2457 O O1  . NO3 J .   ? 0.8626 0.5602 0.7156 -0.3241 -0.0961 -0.3021 209 NO3 A O1  
2458 O O2  . NO3 J .   ? 0.3194 0.3781 0.2710 0.0081  -0.0032 0.0190  209 NO3 A O2  
2459 O O3  . NO3 J .   ? 0.5440 0.5857 0.9080 0.2702  0.1438  -0.1717 209 NO3 A O3  
2460 C C   . ACT K .   ? 0.3199 0.2404 0.3334 0.1296  -0.0373 -0.0186 210 ACT A C   
2461 O O   . ACT K .   ? 0.2689 0.2380 0.3025 0.0802  -0.0039 0.0020  210 ACT A O   
2462 O OXT . ACT K .   ? 0.1711 0.1923 0.2396 0.0555  0.0696  0.0538  210 ACT A OXT 
2463 C CH3 . ACT K .   ? 0.4601 0.2327 0.4262 0.1276  -0.1272 -0.0335 210 ACT A CH3 
2467 O O   . HOH L .   ? 0.7450 0.2196 0.2548 0.0173  -0.0061 -0.0116 301 HOH A O   
2468 O O   . HOH L .   ? 0.4573 0.2927 0.3101 0.1383  0.1452  0.1282  302 HOH A O   
2469 O O   . HOH L .   ? 0.3352 0.5867 1.1414 -0.2535 0.0389  -0.3576 303 HOH A O   
2470 O O   . HOH L .   ? 0.3567 0.6198 0.8594 0.0251  -0.0541 -0.2739 304 HOH A O   
2471 O O   . HOH L .   ? 0.7725 0.1856 0.2283 -0.0868 -0.1075 0.0235  305 HOH A O   
2472 O O   . HOH L .   ? 0.5210 0.3623 0.2110 0.1606  0.0221  -0.0340 306 HOH A O   
2473 O O   . HOH L .   ? 0.4173 0.1879 0.3073 -0.0452 0.0421  -0.0529 307 HOH A O   
2474 O O   . HOH L .   ? 0.3877 0.3619 0.3002 -0.1800 -0.1330 0.0233  308 HOH A O   
2475 O O   . HOH L .   ? 0.2550 0.2409 0.1964 -0.0328 -0.0161 -0.0250 309 HOH A O   
2476 O O   . HOH L .   ? 0.3138 0.6375 0.6847 0.2419  0.0522  0.3089  310 HOH A O   
2477 O O   . HOH L .   ? 0.2993 0.3661 0.4036 -0.0799 0.0293  0.0773  311 HOH A O   
2478 O O   . HOH L .   ? 0.3717 0.2742 0.1822 -0.0013 0.1139  0.0076  312 HOH A O   
2479 O O   . HOH L .   ? 0.1717 0.1745 0.1196 0.0518  0.0136  0.0259  313 HOH A O   
2480 O O   . HOH L .   ? 0.5955 0.5680 0.4134 0.2049  -0.2805 0.0472  314 HOH A O   
2481 O O   . HOH L .   ? 1.6299 0.3522 1.1350 0.0059  0.9407  -0.2553 315 HOH A O   
2482 O O   . HOH L .   ? 0.2172 0.2332 0.2741 0.0127  0.0596  -0.0002 316 HOH A O   
2483 O O   . HOH L .   ? 0.3069 0.4078 0.4283 0.0844  0.0736  0.1042  317 HOH A O   
2484 O O   . HOH L .   ? 0.6072 0.2343 0.8433 0.1102  0.0679  -0.1848 318 HOH A O   
2485 O O   . HOH L .   ? 0.6978 0.5566 0.3338 -0.0130 0.0972  -0.1378 319 HOH A O   
2486 O O   . HOH L .   ? 0.4809 0.3876 0.5246 0.1604  -0.2091 -0.1572 320 HOH A O   
2487 O O   . HOH L .   ? 0.1579 0.2841 0.1667 0.0181  -0.0488 -0.0568 321 HOH A O   
2488 O O   . HOH L .   ? 0.5376 0.2315 0.1825 -0.0280 -0.0683 -0.0374 322 HOH A O   
2489 O O   . HOH L .   ? 0.5794 0.5010 0.5461 0.1343  0.2455  0.1794  323 HOH A O   
2490 O O   . HOH L .   ? 0.3718 0.3751 0.3964 0.1640  -0.1071 -0.0166 324 HOH A O   
2491 O O   . HOH L .   ? 0.2494 0.1678 0.2676 -0.0132 -0.0667 0.0190  325 HOH A O   
2492 O O   . HOH L .   ? 0.2470 0.2727 0.3644 0.0243  0.0901  -0.0551 326 HOH A O   
2493 O O   . HOH L .   ? 0.5158 0.4792 0.6738 0.0137  0.2375  -0.3550 327 HOH A O   
2494 O O   . HOH L .   ? 0.1619 0.2965 0.2056 -0.0246 0.0222  -0.0603 328 HOH A O   
2495 O O   . HOH L .   ? 0.3373 0.3024 2.0000 -0.0755 0.3223  0.0403  329 HOH A O   
2496 O O   . HOH L .   ? 0.1986 0.1766 0.5821 0.0318  -0.1275 -0.0558 330 HOH A O   
2497 O O   . HOH L .   ? 0.2569 0.4913 0.8269 -0.0859 0.0360  -0.2494 331 HOH A O   
2498 O O   . HOH L .   ? 0.1768 0.2313 0.1295 0.0032  -0.0363 -0.0123 332 HOH A O   
2499 O O   . HOH L .   ? 0.1375 0.1403 0.1559 0.0067  0.0036  0.0280  333 HOH A O   
2500 O O   . HOH L .   ? 0.3026 0.3126 0.5391 -0.0153 -0.1593 0.1280  334 HOH A O   
2501 O O   . HOH L .   ? 0.1105 0.3052 0.1241 -0.0031 -0.0127 -0.0165 335 HOH A O   
2502 O O   . HOH L .   ? 0.4663 0.3137 0.5630 -0.0348 -0.1753 0.1673  336 HOH A O   
2503 O O   . HOH L .   ? 0.1781 0.2056 0.2869 -0.0691 0.0496  -0.1265 337 HOH A O   
2504 O O   . HOH L .   ? 0.1480 0.1876 0.1754 0.0020  -0.0376 0.0312  338 HOH A O   
2505 O O   . HOH L .   ? 0.3181 0.2259 0.2696 -0.1127 -0.0721 0.0495  339 HOH A O   
2506 O O   . HOH L .   ? 0.5459 0.3688 0.3329 0.1962  -0.0666 0.0497  340 HOH A O   
2507 O O   . HOH L .   ? 0.1422 0.3011 0.4983 -0.0143 -0.1013 0.0638  341 HOH A O   
2508 O O   . HOH L .   ? 0.2440 0.1847 0.2128 0.0384  -0.0513 -0.0111 342 HOH A O   
2509 O O   . HOH L .   ? 0.3657 1.0082 0.3474 -0.0718 0.2351  -0.0468 343 HOH A O   
2510 O O   . HOH L .   ? 0.3410 0.4007 0.1318 -0.2039 -0.0173 -0.0107 344 HOH A O   
2511 O O   . HOH L .   ? 1.2960 0.2309 0.2616 0.3410  0.0201  -0.0105 345 HOH A O   
2512 O O   . HOH L .   ? 0.2180 0.2545 0.2049 0.0683  0.0120  0.0039  346 HOH A O   
2513 O O   . HOH L .   ? 0.2489 0.3423 0.2048 0.0535  0.0346  -0.0787 347 HOH A O   
2514 O O   . HOH L .   ? 0.2428 0.2115 0.4294 0.0341  0.0143  -0.0029 348 HOH A O   
2515 O O   . HOH L .   ? 1.0763 0.1839 0.3811 0.0966  0.3237  -0.0688 349 HOH A O   
2516 O O   . HOH L .   ? 0.1847 0.2647 0.5847 -0.0812 0.0459  0.0028  350 HOH A O   
2517 O O   . HOH L .   ? 1.3065 0.5757 0.3656 -0.2480 0.1354  -0.0624 351 HOH A O   
2518 O O   . HOH L .   ? 0.2626 0.7672 0.2943 0.0872  0.0633  0.2727  352 HOH A O   
2519 O O   . HOH L .   ? 0.3770 0.5402 1.2538 -0.0604 0.1623  0.3518  353 HOH A O   
2520 O O   . HOH L .   ? 0.2262 0.2312 0.2187 -0.0352 -0.0087 -0.0108 354 HOH A O   
2521 O O   . HOH L .   ? 0.1869 0.2505 0.2345 -0.0429 0.0534  -0.0681 355 HOH A O   
2522 O O   . HOH L .   ? 0.3720 0.9128 0.4579 0.0731  0.1048  -0.0878 356 HOH A O   
2523 O O   . HOH L .   ? 0.2836 0.2172 0.1547 0.0320  0.0647  0.0050  357 HOH A O   
2524 O O   . HOH L .   ? 0.2441 0.2180 0.2785 0.0402  -0.0512 0.0591  358 HOH A O   
2525 O O   . HOH L .   ? 0.2602 0.3873 0.1797 -0.0264 0.0199  0.0861  359 HOH A O   
2526 O O   . HOH L .   ? 0.1006 0.1284 0.1206 -0.0034 -0.0116 0.0349  360 HOH A O   
2527 O O   . HOH L .   ? 1.1969 0.3650 0.2620 0.0919  0.2982  0.0932  361 HOH A O   
2528 O O   . HOH L .   ? 0.4150 0.1789 0.9380 -0.0049 0.2142  0.1200  362 HOH A O   
2529 O O   . HOH L .   ? 0.2495 0.4142 0.5961 -0.0965 0.1910  -0.2113 363 HOH A O   
2530 O O   . HOH L .   ? 0.0962 0.3959 0.3364 -0.0206 0.0004  -0.1534 364 HOH A O   
2531 O O   . HOH L .   ? 0.2287 0.2131 0.1561 -0.0388 -0.0089 -0.0272 365 HOH A O   
2532 O O   . HOH L .   ? 0.3234 0.6000 0.9509 0.1573  0.1486  0.2086  366 HOH A O   
2533 O O   . HOH L .   ? 0.4122 0.2040 0.3090 0.0640  -0.0452 -0.0099 367 HOH A O   
2534 O O   . HOH L .   ? 0.1616 0.1587 0.1401 -0.0061 0.0203  -0.0094 368 HOH A O   
2535 O O   . HOH L .   ? 0.2167 0.5860 0.2728 -0.1310 -0.0786 0.0900  369 HOH A O   
2536 O O   . HOH L .   ? 0.2600 0.2017 0.3141 0.0811  0.0784  0.0399  370 HOH A O   
2537 O O   . HOH L .   ? 0.2195 0.2415 0.3216 0.0046  -0.0028 -0.0109 371 HOH A O   
2538 O O   . HOH L .   ? 0.4811 0.4701 0.6396 0.2015  -0.1431 -0.1810 372 HOH A O   
2539 O O   . HOH L .   ? 0.2821 0.2416 0.1563 0.0291  -0.0837 -0.0529 373 HOH A O   
2540 O O   . HOH L .   ? 0.4753 0.3737 0.2594 -0.1198 0.0522  -0.0334 374 HOH A O   
2541 O O   . HOH L .   ? 0.1726 0.1705 0.1248 -0.0175 -0.0102 -0.0079 375 HOH A O   
2542 O O   . HOH L .   ? 0.2624 0.3066 0.6259 0.0310  -0.2071 -0.0219 376 HOH A O   
2543 O O   . HOH L .   ? 0.3601 0.3359 0.2575 0.1404  0.0717  0.0234  377 HOH A O   
2544 O O   . HOH L .   ? 0.3304 0.1874 0.2293 -0.0614 0.0657  -0.0532 378 HOH A O   
2545 O O   . HOH L .   ? 0.4292 0.4356 0.7428 0.2328  0.0479  0.1950  379 HOH A O   
2546 O O   . HOH L .   ? 0.1665 0.7234 0.2170 -0.1145 -0.0520 0.0194  380 HOH A O   
2547 O O   . HOH L .   ? 0.1945 1.5081 0.3305 0.0602  0.0495  -0.2495 381 HOH A O   
2548 O O   . HOH L .   ? 0.1536 0.3916 0.8407 -0.0207 -0.0602 0.1899  382 HOH A O   
2549 O O   . HOH L .   ? 0.5170 0.4234 0.3443 0.2028  0.2192  0.1415  383 HOH A O   
2550 O O   . HOH L .   ? 0.9591 0.2877 0.4737 -0.0073 -0.1599 0.1878  384 HOH A O   
2551 O O   . HOH L .   ? 0.5783 0.2232 1.0005 -0.0695 0.2735  -0.0337 385 HOH A O   
2552 O O   . HOH L .   ? 0.6416 0.9600 0.5466 0.2081  -0.0426 -0.4277 386 HOH A O   
2553 O O   . HOH L .   ? 0.2475 0.2652 0.1644 -0.0541 0.0450  -0.0419 387 HOH A O   
2554 O O   . HOH L .   ? 0.2491 0.2823 0.4195 0.0689  -0.0451 -0.0579 388 HOH A O   
2555 O O   . HOH L .   ? 1.4011 0.3924 0.7815 0.3784  0.6550  0.1247  389 HOH A O   
2556 O O   . HOH L .   ? 0.2082 0.2009 0.2044 0.0606  -0.0067 0.0151  390 HOH A O   
2557 O O   . HOH L .   ? 0.5380 0.6155 0.5554 0.0794  -0.1210 0.0889  391 HOH A O   
2558 O O   . HOH L .   ? 0.4278 0.7315 0.5267 0.0595  -0.1496 0.1805  392 HOH A O   
2559 O O   . HOH L .   ? 0.2328 0.2477 0.1351 -0.0259 -0.0535 0.0027  393 HOH A O   
2560 O O   . HOH L .   ? 0.2696 0.5650 0.4228 0.1042  -0.0117 0.2168  394 HOH A O   
2561 O O   . HOH L .   ? 0.6920 0.5186 0.4488 0.1510  0.0275  -0.1930 395 HOH A O   
2562 O O   . HOH L .   ? 0.3075 1.0801 0.7637 0.1172  0.0682  0.2809  396 HOH A O   
2563 O O   . HOH L .   ? 0.1410 0.6785 0.3673 0.0088  -0.0180 -0.2153 397 HOH A O   
2564 O O   . HOH L .   ? 0.3773 0.4088 0.4610 -0.0212 -0.2312 -0.1084 398 HOH A O   
2565 O O   . HOH L .   ? 2.6187 0.4118 0.2613 0.2912  0.0826  -0.1803 399 HOH A O   
2566 O O   . HOH L .   ? 0.2017 0.4382 1.0864 0.0382  0.0237  0.1653  400 HOH A O   
2567 O O   . HOH L .   ? 1.3131 0.4740 0.3764 0.4947  0.0977  0.0248  401 HOH A O   
2568 O O   . HOH L .   ? 1.4263 0.9665 1.9979 0.7881  1.3594  0.9483  402 HOH A O   
2569 O O   . HOH L .   ? 0.3407 0.4322 0.2969 -0.0028 0.1626  -0.0694 403 HOH A O   
2570 O O   . HOH L .   ? 0.5332 0.4004 0.8486 -0.1214 0.1105  0.1205  404 HOH A O   
2571 O O   . HOH L .   ? 0.2394 0.5079 0.3184 -0.0655 0.1074  0.0224  405 HOH A O   
2572 O O   . HOH L .   ? 0.4566 0.2593 0.2739 -0.1235 -0.0902 0.1542  406 HOH A O   
2573 O O   . HOH L .   ? 0.1551 0.2611 0.4162 0.0540  -0.0512 0.1378  407 HOH A O   
2574 O O   . HOH L .   ? 0.4678 0.4068 0.6914 -0.0031 -0.0206 0.1868  408 HOH A O   
# 
