data_9FCA
# 
_entry.id   9FCA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9FCA         pdb_00009fca 10.2210/pdb9fca/pdb 
WWPDB D_1292137236 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FCA 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-15 
_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              alke.meents@desy.de 
_pdbx_contact_author.name_first         Alke 
_pdbx_contact_author.name_last          Meents 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6078-4095 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Reinke, P.Y.A.'       1  0000-0002-7354-0839 
'Guenther, S.'         2  ?                   
'Falke, S.'            3  ?                   
'Galchenkova, M.'      4  ?                   
'Rahmani Mashhour, A.' 5  ?                   
'Creon, A.'            6  ?                   
'Lieske, J.'           7  ?                   
'Ewert, W.'            8  ?                   
'Rorigues, A.C.'       9  ?                   
'Thekku Veedu, S.'     10 ?                   
'Fischer, P.'          11 ?                   
'Meents, A.'           12 0000-0001-6078-4095 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Exploring the conformational space of proteins by systematic variation of the relative humidity' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Reinke, P.Y.A.' 1 0000-0002-7354-0839 
primary 'Meents, A.'     2 0000-0001-6078-4095 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Lysozyme C'   14331.160 1   3.2.1.17 ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL 62.068    6   ?        ? ? ? 
3 non-polymer syn 'CHLORIDE ION' 35.453    4   ?        ? ? ? 
4 non-polymer syn 'SODIUM ION'   22.990    2   ?        ? ? ? 
5 water       nat water          18.015    104 ?        ? ? ? 
# 
_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 1,2-ETHANEDIOL EDO 
3 'CHLORIDE ION' CL  
4 'SODIUM ION'   NA  
5 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_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   129 
_entity_src_gen.gene_src_common_name               chicken 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 LYZ 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Gallus gallus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9031 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Gallus gallus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9031 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'  ?                 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE       ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                 'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'    ?                 'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 EDO 1   201 206 EDO EDO A . 
C 2 EDO 1   202 207 EDO EDO A . 
D 2 EDO 1   203 208 EDO EDO A . 
E 2 EDO 1   204 209 EDO EDO A . 
F 2 EDO 1   205 215 EDO EDO A . 
G 2 EDO 1   206 216 EDO EDO A . 
H 3 CL  1   207 2   CL  CL  A . 
I 3 CL  1   208 3   CL  CL  A . 
J 3 CL  1   209 4   CL  CL  A . 
K 3 CL  1   210 5   CL  CL  A . 
L 4 NA  1   211 1   NA  NA  A . 
M 4 NA  1   212 2   NA  NA  A . 
N 5 HOH 1   301 35  HOH HOH A . 
N 5 HOH 2   302 81  HOH HOH A . 
N 5 HOH 3   303 100 HOH HOH A . 
N 5 HOH 4   304 5   HOH HOH A . 
N 5 HOH 5   305 109 HOH HOH A . 
N 5 HOH 6   306 97  HOH HOH A . 
N 5 HOH 7   307 27  HOH HOH A . 
N 5 HOH 8   308 130 HOH HOH A . 
N 5 HOH 9   309 106 HOH HOH A . 
N 5 HOH 10  310 25  HOH HOH A . 
N 5 HOH 11  311 1   HOH HOH A . 
N 5 HOH 12  312 3   HOH HOH A . 
N 5 HOH 13  313 4   HOH HOH A . 
N 5 HOH 14  314 57  HOH HOH A . 
N 5 HOH 15  315 43  HOH HOH A . 
N 5 HOH 16  316 41  HOH HOH A . 
N 5 HOH 17  317 11  HOH HOH A . 
N 5 HOH 18  318 2   HOH HOH A . 
N 5 HOH 19  319 6   HOH HOH A . 
N 5 HOH 20  320 47  HOH HOH A . 
N 5 HOH 21  321 105 HOH HOH A . 
N 5 HOH 22  322 7   HOH HOH A . 
N 5 HOH 23  323 127 HOH HOH A . 
N 5 HOH 24  324 15  HOH HOH A . 
N 5 HOH 25  325 138 HOH HOH A . 
N 5 HOH 26  326 28  HOH HOH A . 
N 5 HOH 27  327 16  HOH HOH A . 
N 5 HOH 28  328 33  HOH HOH A . 
N 5 HOH 29  329 14  HOH HOH A . 
N 5 HOH 30  330 30  HOH HOH A . 
N 5 HOH 31  331 115 HOH HOH A . 
N 5 HOH 32  332 9   HOH HOH A . 
N 5 HOH 33  333 134 HOH HOH A . 
N 5 HOH 34  334 117 HOH HOH A . 
N 5 HOH 35  335 122 HOH HOH A . 
N 5 HOH 36  336 124 HOH HOH A . 
N 5 HOH 37  337 46  HOH HOH A . 
N 5 HOH 38  338 94  HOH HOH A . 
N 5 HOH 39  339 12  HOH HOH A . 
N 5 HOH 40  340 50  HOH HOH A . 
N 5 HOH 41  341 128 HOH HOH A . 
N 5 HOH 42  342 34  HOH HOH A . 
N 5 HOH 43  343 45  HOH HOH A . 
N 5 HOH 44  344 49  HOH HOH A . 
N 5 HOH 45  345 17  HOH HOH A . 
N 5 HOH 46  346 131 HOH HOH A . 
N 5 HOH 47  347 67  HOH HOH A . 
N 5 HOH 48  348 10  HOH HOH A . 
N 5 HOH 49  349 108 HOH HOH A . 
N 5 HOH 50  350 129 HOH HOH A . 
N 5 HOH 51  351 36  HOH HOH A . 
N 5 HOH 52  352 61  HOH HOH A . 
N 5 HOH 53  353 8   HOH HOH A . 
N 5 HOH 54  354 111 HOH HOH A . 
N 5 HOH 55  355 39  HOH HOH A . 
N 5 HOH 56  356 24  HOH HOH A . 
N 5 HOH 57  357 20  HOH HOH A . 
N 5 HOH 58  358 13  HOH HOH A . 
N 5 HOH 59  359 89  HOH HOH A . 
N 5 HOH 60  360 22  HOH HOH A . 
N 5 HOH 61  361 55  HOH HOH A . 
N 5 HOH 62  362 23  HOH HOH A . 
N 5 HOH 63  363 66  HOH HOH A . 
N 5 HOH 64  364 29  HOH HOH A . 
N 5 HOH 65  365 62  HOH HOH A . 
N 5 HOH 66  366 86  HOH HOH A . 
N 5 HOH 67  367 18  HOH HOH A . 
N 5 HOH 68  368 44  HOH HOH A . 
N 5 HOH 69  369 118 HOH HOH A . 
N 5 HOH 70  370 77  HOH HOH A . 
N 5 HOH 71  371 75  HOH HOH A . 
N 5 HOH 72  372 112 HOH HOH A . 
N 5 HOH 73  373 133 HOH HOH A . 
N 5 HOH 74  374 79  HOH HOH A . 
N 5 HOH 75  375 143 HOH HOH A . 
N 5 HOH 76  376 71  HOH HOH A . 
N 5 HOH 77  377 37  HOH HOH A . 
N 5 HOH 78  378 53  HOH HOH A . 
N 5 HOH 79  379 59  HOH HOH A . 
N 5 HOH 80  380 99  HOH HOH A . 
N 5 HOH 81  381 56  HOH HOH A . 
N 5 HOH 82  382 52  HOH HOH A . 
N 5 HOH 83  383 126 HOH HOH A . 
N 5 HOH 84  384 60  HOH HOH A . 
N 5 HOH 85  385 139 HOH HOH A . 
N 5 HOH 86  386 132 HOH HOH A . 
N 5 HOH 87  387 78  HOH HOH A . 
N 5 HOH 88  388 58  HOH HOH A . 
N 5 HOH 89  389 74  HOH HOH A . 
N 5 HOH 90  390 87  HOH HOH A . 
N 5 HOH 91  391 107 HOH HOH A . 
N 5 HOH 92  392 93  HOH HOH A . 
N 5 HOH 93  393 135 HOH HOH A . 
N 5 HOH 94  394 116 HOH HOH A . 
N 5 HOH 95  395 96  HOH HOH A . 
N 5 HOH 96  396 63  HOH HOH A . 
N 5 HOH 97  397 26  HOH HOH A . 
N 5 HOH 98  398 125 HOH HOH A . 
N 5 HOH 99  399 137 HOH HOH A . 
N 5 HOH 100 400 91  HOH HOH A . 
N 5 HOH 101 401 101 HOH HOH A . 
N 5 HOH 102 402 110 HOH HOH A . 
N 5 HOH 103 403 72  HOH HOH A . 
N 5 HOH 104 404 73  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FCA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     79.051 
_cell.length_a_esd                 ? 
_cell.length_b                     79.051 
_cell.length_b_esd                 ? 
_cell.length_c                     37.343 
_cell.length_c_esd                 ? 
_cell.volume                       233358.670 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9FCA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            'P 4nw 2abw' 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FCA 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.04 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.57 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              3.5 
_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    '1M NaCl, 35% (v/v) ethylene glycol, 20% (w/v) PEG4000, 50 mM sodium acetate pH 3.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     298 
_diffrn.ambient_temp_details             'Humidity chamber controlled' 
_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 EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-12 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.7749 
_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                        'PETRA III, DESY BEAMLINE P09 HiPhaX' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.7749 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P09 HiPhaX' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          17.95 
_reflns.entry_id                                       9FCA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.4 
_reflns.d_resolution_low                               39.53 
_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                                     23886 
_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                           99.97 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.20 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.4 
_reflns_shell.d_res_low                                     1.45 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.16 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2335 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.885 
_reflns_shell.pdbx_CC_star                                  0.969 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.18 
_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                                 9FCA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.40 
_refine.ls_d_res_low                             39.53 
_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                     23886 
_refine.ls_number_reflns_R_free                  1976 
_refine.ls_number_reflns_R_work                  21910 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 8.27 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1563 
_refine.ls_R_factor_R_free                       0.1769 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1545 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 17.2013 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1332 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        39.53 
_refine_hist.number_atoms_solvent             104 
_refine_hist.number_atoms_total               1135 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1001 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0093  ? 1268 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0852  ? 1720 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0835  ? 168  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0103  ? 237  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.9309 ? 479  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.40 1.43  . . 135 1547 99.82  . . . . 0.2389 . . . . . . . . . . . 0.2280 
'X-RAY DIFFRACTION' 1.44 1.47  . . 136 1527 100.00 . . . . 0.2129 . . . . . . . . . . . 0.2372 
'X-RAY DIFFRACTION' 1.47 1.52  . . 143 1518 100.00 . . . . 0.1859 . . . . . . . . . . . 0.2360 
'X-RAY DIFFRACTION' 1.52 1.57  . . 132 1548 100.00 . . . . 0.1783 . . . . . . . . . . . 0.2155 
'X-RAY DIFFRACTION' 1.57 1.62  . . 146 1552 100.00 . . . . 0.1671 . . . . . . . . . . . 0.2031 
'X-RAY DIFFRACTION' 1.62 1.69  . . 133 1542 100.00 . . . . 0.1704 . . . . . . . . . . . 0.1672 
'X-RAY DIFFRACTION' 1.69 1.76  . . 145 1533 100.00 . . . . 0.1787 . . . . . . . . . . . 0.2231 
'X-RAY DIFFRACTION' 1.76 1.86  . . 135 1555 100.00 . . . . 0.1592 . . . . . . . . . . . 0.2132 
'X-RAY DIFFRACTION' 1.86 1.97  . . 143 1557 100.00 . . . . 0.1440 . . . . . . . . . . . 0.1874 
'X-RAY DIFFRACTION' 1.97 2.13  . . 142 1563 100.00 . . . . 0.1349 . . . . . . . . . . . 0.1416 
'X-RAY DIFFRACTION' 2.13 2.34  . . 144 1571 100.00 . . . . 0.1301 . . . . . . . . . . . 0.1473 
'X-RAY DIFFRACTION' 2.34 2.68  . . 141 1584 100.00 . . . . 0.1316 . . . . . . . . . . . 0.1551 
'X-RAY DIFFRACTION' 2.68 3.37  . . 146 1607 99.94  . . . . 0.1399 . . . . . . . . . . . 0.1452 
'X-RAY DIFFRACTION' 3.37 39.53 . . 155 1706 99.89  . . . . 0.1677 . . . . . . . . . . . 0.1926 
# 
_struct.entry_id                     9FCA 
_struct.title                        'HEN EGG-WHITE Lysozyme incubated at 40% relative humidity' 
_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        9FCA 
_struct_keywords.text            'Hydrolase, relative humidity' 
_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 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 5 ? 
# 
_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              9FCA 
_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)' 1780 ? 
1 MORE         -42  ? 
1 'SSA (A^2)'  6710 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   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  ? SER A 100 ? ILE A 88  SER A 100 1 ? 13 
HELX_P HELX_P6 AA6 ASN A 103 ? ALA A 107 ? ASN A 103 ALA A 107 5 ? 5  
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 ? ARG A 125 ? ASP A 119 ARG A 125 5 ? 7  
# 
_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 ? ? ? ? ? ? ? 2.007 ? ? 
disulf2 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 115 SG ? ? A CYS 30  A CYS 115 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 80  SG ? ? A CYS 64  A CYS 80  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf4 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 94  SG ? ? A CYS 76  A CYS 94  1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc1 metalc ? ? A SER 24 OG ? ? ? 1_555 M NA  .   NA ? ? A SER 24  A NA  212 1_555 ? ? ? ? ? ? ? 2.899 ? ? 
metalc2 metalc ? ? A SER 60 O  A ? ? 1_555 L NA  .   NA ? ? A SER 60  A NA  211 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc3 metalc ? ? A SER 60 O  B ? ? 1_555 L NA  .   NA ? ? A SER 60  A NA  211 1_555 ? ? ? ? ? ? ? 2.568 ? ? 
metalc4 metalc ? ? A CYS 64 O  ? ? ? 1_555 L NA  .   NA ? ? A CYS 64  A NA  211 1_555 ? ? ? ? ? ? ? 2.441 ? ? 
metalc5 metalc ? ? A SER 72 OG ? ? ? 1_555 L NA  .   NA ? ? A SER 72  A NA  211 1_555 ? ? ? ? ? ? ? 2.512 ? ? 
metalc6 metalc ? ? A ARG 73 O  ? ? ? 1_555 L NA  .   NA ? ? A ARG 73  A NA  211 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc7 metalc ? ? L NA  .  NA ? ? ? 1_555 N HOH .   O  ? ? A NA  211 A HOH 353 1_555 ? ? ? ? ? ? ? 2.598 ? ? 
metalc8 metalc ? ? L NA  .  NA ? ? ? 1_555 N HOH .   O  ? ? A NA  211 A HOH 356 1_555 ? ? ? ? ? ? ? 2.516 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O  A A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  B A SER 60 ? A SER 60  ? 1_555 11.1  ? 
2  O  A A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? A CYS 64 ? A CYS 64  ? 1_555 85.7  ? 
3  O  B A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? A CYS 64 ? A CYS 64  ? 1_555 94.9  ? 
4  O  A A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 OG ? A SER 72 ? A SER 72  ? 1_555 93.8  ? 
5  O  B A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 OG ? A SER 72 ? A SER 72  ? 1_555 83.3  ? 
6  O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 OG ? A SER 72 ? A SER 72  ? 1_555 165.5 ? 
7  O  A A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? A ARG 73 ? A ARG 73  ? 1_555 93.6  ? 
8  O  B A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? A ARG 73 ? A ARG 73  ? 1_555 99.3  ? 
9  O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? A ARG 73 ? A ARG 73  ? 1_555 93.5  ? 
10 OG ? A SER 72 ? A SER 72  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? A ARG 73 ? A ARG 73  ? 1_555 101.0 ? 
11 O  A A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 353 ? 1_555 103.1 ? 
12 O  B A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 353 ? 1_555 97.2  ? 
13 O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 353 ? 1_555 87.7  ? 
14 OG ? A SER 72 ? A SER 72  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 353 ? 1_555 78.3  ? 
15 O  ? A ARG 73 ? A ARG 73  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 353 ? 1_555 163.4 ? 
16 O  A A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 356 ? 1_555 177.3 ? 
17 O  B A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 356 ? 1_555 166.8 ? 
18 O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 356 ? 1_555 94.8  ? 
19 OG ? A SER 72 ? A SER 72  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 356 ? 1_555 85.1  ? 
20 O  ? A ARG 73 ? A ARG 73  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 356 ? 1_555 89.1  ? 
21 O  ? N HOH .  ? A HOH 353 ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 356 ? 1_555 74.3  ? 
# 
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                   9FCA 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TRP A 62 ? B -133.86 -30.57 
2 1 ARG A 68 ? ? -143.30 25.63  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     384 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   N 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+3/4  
3 y+1/2,-x+1/2,z+1/4  
4 x+1/2,-y+1/2,-z+1/4 
5 -x+1/2,y+1/2,-z+3/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
NA  NA   NA N N 261 
PHE N    N  N N 262 
PHE CA   C  N S 263 
PHE C    C  N N 264 
PHE O    O  N N 265 
PHE CB   C  N N 266 
PHE CG   C  Y N 267 
PHE CD1  C  Y N 268 
PHE CD2  C  Y N 269 
PHE CE1  C  Y N 270 
PHE CE2  C  Y N 271 
PHE CZ   C  Y N 272 
PHE OXT  O  N N 273 
PHE H    H  N N 274 
PHE H2   H  N N 275 
PHE HA   H  N N 276 
PHE HB2  H  N N 277 
PHE HB3  H  N N 278 
PHE HD1  H  N N 279 
PHE HD2  H  N N 280 
PHE HE1  H  N N 281 
PHE HE2  H  N N 282 
PHE HZ   H  N N 283 
PHE HXT  H  N N 284 
PRO N    N  N N 285 
PRO CA   C  N S 286 
PRO C    C  N N 287 
PRO O    O  N N 288 
PRO CB   C  N N 289 
PRO CG   C  N N 290 
PRO CD   C  N N 291 
PRO OXT  O  N N 292 
PRO H    H  N N 293 
PRO HA   H  N N 294 
PRO HB2  H  N N 295 
PRO HB3  H  N N 296 
PRO HG2  H  N N 297 
PRO HG3  H  N N 298 
PRO HD2  H  N N 299 
PRO HD3  H  N N 300 
PRO HXT  H  N N 301 
SER N    N  N N 302 
SER CA   C  N S 303 
SER C    C  N N 304 
SER O    O  N N 305 
SER CB   C  N N 306 
SER OG   O  N N 307 
SER OXT  O  N N 308 
SER H    H  N N 309 
SER H2   H  N N 310 
SER HA   H  N N 311 
SER HB2  H  N N 312 
SER HB3  H  N N 313 
SER HG   H  N N 314 
SER HXT  H  N N 315 
THR N    N  N N 316 
THR CA   C  N S 317 
THR C    C  N N 318 
THR O    O  N N 319 
THR CB   C  N R 320 
THR OG1  O  N N 321 
THR CG2  C  N N 322 
THR OXT  O  N N 323 
THR H    H  N N 324 
THR H2   H  N N 325 
THR HA   H  N N 326 
THR HB   H  N N 327 
THR HG1  H  N N 328 
THR HG21 H  N N 329 
THR HG22 H  N N 330 
THR HG23 H  N N 331 
THR HXT  H  N N 332 
TRP N    N  N N 333 
TRP CA   C  N S 334 
TRP C    C  N N 335 
TRP O    O  N N 336 
TRP CB   C  N N 337 
TRP CG   C  Y N 338 
TRP CD1  C  Y N 339 
TRP CD2  C  Y N 340 
TRP NE1  N  Y N 341 
TRP CE2  C  Y N 342 
TRP CE3  C  Y N 343 
TRP CZ2  C  Y N 344 
TRP CZ3  C  Y N 345 
TRP CH2  C  Y N 346 
TRP OXT  O  N N 347 
TRP H    H  N N 348 
TRP H2   H  N N 349 
TRP HA   H  N N 350 
TRP HB2  H  N N 351 
TRP HB3  H  N N 352 
TRP HD1  H  N N 353 
TRP HE1  H  N N 354 
TRP HE3  H  N N 355 
TRP HZ2  H  N N 356 
TRP HZ3  H  N N 357 
TRP HH2  H  N N 358 
TRP HXT  H  N N 359 
TYR N    N  N N 360 
TYR CA   C  N S 361 
TYR C    C  N N 362 
TYR O    O  N N 363 
TYR CB   C  N N 364 
TYR CG   C  Y N 365 
TYR CD1  C  Y N 366 
TYR CD2  C  Y N 367 
TYR CE1  C  Y N 368 
TYR CE2  C  Y N 369 
TYR CZ   C  Y N 370 
TYR OH   O  N N 371 
TYR OXT  O  N N 372 
TYR H    H  N N 373 
TYR H2   H  N N 374 
TYR HA   H  N N 375 
TYR HB2  H  N N 376 
TYR HB3  H  N N 377 
TYR HD1  H  N N 378 
TYR HD2  H  N N 379 
TYR HE1  H  N N 380 
TYR HE2  H  N N 381 
TYR HH   H  N N 382 
TYR HXT  H  N N 383 
VAL N    N  N N 384 
VAL CA   C  N S 385 
VAL C    C  N N 386 
VAL O    O  N N 387 
VAL CB   C  N N 388 
VAL CG1  C  N N 389 
VAL CG2  C  N N 390 
VAL OXT  O  N N 391 
VAL H    H  N N 392 
VAL H2   H  N N 393 
VAL HA   H  N N 394 
VAL HB   H  N N 395 
VAL HG11 H  N N 396 
VAL HG12 H  N N 397 
VAL HG13 H  N N 398 
VAL HG21 H  N N 399 
VAL HG22 H  N N 400 
VAL HG23 H  N N 401 
VAL HXT  H  N N 402 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Helmholtz Association' Germany FISCOV 1 
'Helmholtz Association' Germany FRAGX  2 
'Helmholtz Association' Germany HIR3X  3 
# 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'intern model of RT lysozyme' 
# 
_space_group.name_H-M_alt     'P 43 21 2' 
_space_group.name_Hall        'P 4nw 2abw' 
_space_group.IT_number        96 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FCA 
_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]   0.012650 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012650 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.026779 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A LYS A 1 1   ? -2.74400  -9.76000  -8.58100  0.560 18.22000  ? 1   LYS A N    1 
ATOM   2    N  N    B LYS A 1 1   ? -2.66200  -9.70900  -8.59400  0.440 18.14000  ? 1   LYS A N    1 
ATOM   3    C  CA   A LYS A 1 1   ? -1.79800  -10.13100 -9.66000  0.560 18.33000  ? 1   LYS A CA   1 
ATOM   4    C  CA   B LYS A 1 1   ? -1.75300  -10.10400 -9.70100  0.440 18.34000  ? 1   LYS A CA   1 
ATOM   5    C  C    A LYS A 1 1   ? -1.90900  -11.62300 -9.91800  0.560 15.88000  ? 1   LYS A C    1 
ATOM   6    C  C    B LYS A 1 1   ? -1.85000  -11.60400 -9.92000  0.440 15.84000  ? 1   LYS A C    1 
ATOM   7    O  O    A LYS A 1 1   ? -2.02600  -12.40200 -8.98000  0.560 17.37000  ? 1   LYS A O    1 
ATOM   8    O  O    B LYS A 1 1   ? -1.89200  -12.35800 -8.95200  0.440 17.50000  ? 1   LYS A O    1 
ATOM   9    C  CB   A LYS A 1 1   ? -0.37700  -9.78800  -9.22500  0.560 20.33000  ? 1   LYS A CB   1 
ATOM   10   C  CB   B LYS A 1 1   ? -0.31800  -9.72300  -9.33600  0.440 21.09000  ? 1   LYS A CB   1 
ATOM   11   C  CG   A LYS A 1 1   ? 0.68700   -10.25000 -10.20500 0.560 23.72000  ? 1   LYS A CG   1 
ATOM   12   C  CG   B LYS A 1 1   ? 0.74900   -10.29000 -10.26900 0.440 23.61000  ? 1   LYS A CG   1 
ATOM   13   C  CD   A LYS A 1 1   ? 2.04900   -9.80800  -9.74500  0.560 28.85000  ? 1   LYS A CD   1 
ATOM   14   C  CD   B LYS A 1 1   ? 2.10000   -9.67200  -9.94200  0.440 29.76000  ? 1   LYS A CD   1 
ATOM   15   C  CE   A LYS A 1 1   ? 3.12700   -10.47000 -10.57800 0.560 30.90000  ? 1   LYS A CE   1 
ATOM   16   C  CE   B LYS A 1 1   ? 3.24600   -10.35200 -10.68000 0.440 30.85000  ? 1   LYS A CE   1 
ATOM   17   N  NZ   A LYS A 1 1   ? 4.30300   -9.59000  -10.74100 0.560 31.58000  ? 1   LYS A NZ   1 
ATOM   18   N  NZ   B LYS A 1 1   ? 3.17400   -10.19000 -12.15400 0.440 24.90000  ? 1   LYS A NZ   1 
ATOM   19   H  H1   A LYS A 1 1   ? -3.52000  -10.17600 -8.70900  0.560 21.85000  ? 1   LYS A H1   1 
ATOM   20   H  H1   B LYS A 1 1   ? -2.98900  -10.43900 -8.20300  0.440 21.76000  ? 1   LYS A H1   1 
ATOM   21   H  H2   A LYS A 1 1   ? -2.40500  -10.00000 -7.79400  0.560 21.85000  ? 1   LYS A H2   1 
ATOM   22   H  H2   B LYS A 1 1   ? -2.21000  -9.22900  -7.99500  0.440 21.76000  ? 1   LYS A H2   1 
ATOM   23   H  H3   A LYS A 1 1   ? -2.87400  -8.87900  -8.59100  0.560 21.85000  ? 1   LYS A H3   1 
ATOM   24   H  H3   B LYS A 1 1   ? -3.33200  -9.22100  -8.91900  0.440 21.76000  ? 1   LYS A H3   1 
ATOM   25   H  HA   A LYS A 1 1   ? -1.99500  -9.64800  -10.47800 0.560 21.98000  ? 1   LYS A HA   1 
ATOM   26   H  HA   B LYS A 1 1   ? -1.99200  -9.64900  -10.52400 0.440 22.00000  ? 1   LYS A HA   1 
ATOM   27   H  HB2  A LYS A 1 1   ? -0.30100  -8.82500  -9.13600  0.560 24.39000  ? 1   LYS A HB2  1 
ATOM   28   H  HB2  B LYS A 1 1   ? -0.24100  -8.75600  -9.35700  0.440 25.29000  ? 1   LYS A HB2  1 
ATOM   29   H  HB3  A LYS A 1 1   ? -0.19900  -10.21400 -8.37100  0.560 24.39000  ? 1   LYS A HB3  1 
ATOM   30   H  HB3  B LYS A 1 1   ? -0.13000  -10.05100 -8.44300  0.440 25.29000  ? 1   LYS A HB3  1 
ATOM   31   H  HG2  A LYS A 1 1   ? 0.67900   -11.21800 -10.26300 0.560 28.46000  ? 1   LYS A HG2  1 
ATOM   32   H  HG2  B LYS A 1 1   ? 0.81000   -11.25100 -10.15200 0.440 28.31000  ? 1   LYS A HG2  1 
ATOM   33   H  HG3  A LYS A 1 1   ? 0.51500   -9.86400  -11.07800 0.560 28.46000  ? 1   LYS A HG3  1 
ATOM   34   H  HG3  B LYS A 1 1   ? 0.52500   -10.08100 -11.18900 0.440 28.31000  ? 1   LYS A HG3  1 
ATOM   35   H  HD2  A LYS A 1 1   ? 2.13000   -8.84600  -9.84200  0.560 34.61000  ? 1   LYS A HD2  1 
ATOM   36   H  HD2  B LYS A 1 1   ? 2.09100   -8.73600  -10.19700 0.440 35.70000  ? 1   LYS A HD2  1 
ATOM   37   H  HD3  A LYS A 1 1   ? 2.17700   -10.05900 -8.81700  0.560 34.61000  ? 1   LYS A HD3  1 
ATOM   38   H  HD3  B LYS A 1 1   ? 2.26400   -9.75400  -8.99000  0.440 35.70000  ? 1   LYS A HD3  1 
ATOM   39   H  HE2  A LYS A 1 1   ? 3.41500   -11.28600 -10.13900 0.560 37.06000  ? 1   LYS A HE2  1 
ATOM   40   H  HE2  B LYS A 1 1   ? 4.08500   -9.96800  -10.38000 0.440 37.00000  ? 1   LYS A HE2  1 
ATOM   41   H  HE3  A LYS A 1 1   ? 2.77300   -10.67300 -11.45800 0.560 37.06000  ? 1   LYS A HE3  1 
ATOM   42   H  HE3  B LYS A 1 1   ? 3.22700   -11.30200 -10.48400 0.440 37.00000  ? 1   LYS A HE3  1 
ATOM   43   H  HZ1  A LYS A 1 1   ? 5.00400   -10.06600 -11.01400 0.560 37.88000  ? 1   LYS A HZ1  1 
ATOM   44   H  HZ1  B LYS A 1 1   ? 3.09400   -9.32800  -12.36200 0.440 29.87000  ? 1   LYS A HZ1  1 
ATOM   45   H  HZ2  A LYS A 1 1   ? 4.13000   -8.95900  -11.34400 0.560 37.88000  ? 1   LYS A HZ2  1 
ATOM   46   H  HZ2  B LYS A 1 1   ? 3.91300   -10.51100 -12.53200 0.440 29.87000  ? 1   LYS A HZ2  1 
ATOM   47   H  HZ3  A LYS A 1 1   ? 4.50200   -9.20100  -9.96600  0.560 37.88000  ? 1   LYS A HZ3  1 
ATOM   48   H  HZ3  B LYS A 1 1   ? 2.47100   -10.63100 -12.47400 0.440 29.87000  ? 1   LYS A HZ3  1 
ATOM   49   N  N    . VAL A 1 2   ? -1.90200  -12.03200 -11.18100 1.000 17.25000  ? 2   VAL A N    1 
ATOM   50   C  CA   . VAL A 1 2   ? -1.83300  -13.43900 -11.55000 1.000 16.14000  ? 2   VAL A CA   1 
ATOM   51   C  C    . VAL A 1 2   ? -0.42000  -13.68000 -12.04300 1.000 21.40000  ? 2   VAL A C    1 
ATOM   52   O  O    . VAL A 1 2   ? 0.00800   -13.06300 -13.02200 1.000 20.30000  ? 2   VAL A O    1 
ATOM   53   C  CB   . VAL A 1 2   ? -2.88300  -13.79600 -12.60800 1.000 22.18000  ? 2   VAL A CB   1 
ATOM   54   C  CG1  . VAL A 1 2   ? -2.75100  -15.23300 -13.06200 1.000 24.55000  ? 2   VAL A CG1  1 
ATOM   55   C  CG2  . VAL A 1 2   ? -4.27600  -13.55000 -12.05400 1.000 20.37000  ? 2   VAL A CG2  1 
ATOM   56   H  H    . VAL A 1 2   ? -1.93800  -11.50300 -11.85800 1.000 20.69000  ? 2   VAL A H    1 
ATOM   57   H  HA   . VAL A 1 2   ? -1.99800  -14.00700 -10.78100 1.000 19.35000  ? 2   VAL A HA   1 
ATOM   58   H  HB   . VAL A 1 2   ? -2.74000  -13.23100 -13.38300 1.000 26.60000  ? 2   VAL A HB   1 
ATOM   59   H  HG11 . VAL A 1 2   ? -3.52200  -15.46600 -13.60200 1.000 29.44000  ? 2   VAL A HG11 1 
ATOM   60   H  HG12 . VAL A 1 2   ? -1.93900  -15.32600 -13.58500 1.000 29.44000  ? 2   VAL A HG12 1 
ATOM   61   H  HG13 . VAL A 1 2   ? -2.70800  -15.80800 -12.28100 1.000 29.44000  ? 2   VAL A HG13 1 
ATOM   62   H  HG21 . VAL A 1 2   ? -4.93000  -13.78300 -12.73100 1.000 24.43000  ? 2   VAL A HG21 1 
ATOM   63   H  HG22 . VAL A 1 2   ? -4.40400  -14.10100 -11.26600 1.000 24.43000  ? 2   VAL A HG22 1 
ATOM   64   H  HG23 . VAL A 1 2   ? -4.36100  -12.61300 -11.82000 1.000 24.43000  ? 2   VAL A HG23 1 
ATOM   65   N  N    . PHE A 1 3   ? 0.31800   -14.53000 -11.34100 1.000 17.48000  ? 3   PHE A N    1 
ATOM   66   C  CA   . PHE A 1 3   ? 1.69700   -14.80900 -11.68000 1.000 17.94000  ? 3   PHE A CA   1 
ATOM   67   C  C    . PHE A 1 3   ? 1.76200   -15.85900 -12.76900 1.000 18.92000  ? 3   PHE A C    1 
ATOM   68   O  O    . PHE A 1 3   ? 0.92800   -16.76400 -12.86900 1.000 18.41000  ? 3   PHE A O    1 
ATOM   69   C  CB   . PHE A 1 3   ? 2.42400   -15.38200 -10.46500 1.000 18.93000  ? 3   PHE A CB   1 
ATOM   70   C  CG   . PHE A 1 3   ? 2.93200   -14.35900 -9.51200  1.000 16.41000  ? 3   PHE A CG   1 
ATOM   71   C  CD1  . PHE A 1 3   ? 2.10100   -13.76900 -8.56200  1.000 22.28000  ? 3   PHE A CD1  1 
ATOM   72   C  CD2  . PHE A 1 3   ? 4.27000   -13.99600 -9.53200  1.000 19.25000  ? 3   PHE A CD2  1 
ATOM   73   C  CE1  . PHE A 1 3   ? 2.59000   -12.84500 -7.67100  1.000 19.77000  ? 3   PHE A CE1  1 
ATOM   74   C  CE2  . PHE A 1 3   ? 4.76800   -13.07800 -8.64400  1.000 19.75000  ? 3   PHE A CE2  1 
ATOM   75   C  CZ   . PHE A 1 3   ? 3.92600   -12.49100 -7.71100  1.000 22.86000  ? 3   PHE A CZ   1 
ATOM   76   H  H    . PHE A 1 3   ? 0.03500   -14.96400 -10.65500 1.000 20.97000  ? 3   PHE A H    1 
ATOM   77   H  HA   . PHE A 1 3   ? 2.12600   -13.99000 -11.97400 1.000 21.51000  ? 3   PHE A HA   1 
ATOM   78   H  HB2  . PHE A 1 3   ? 1.81100   -15.95500 -9.98000  1.000 22.70000  ? 3   PHE A HB2  1 
ATOM   79   H  HB3  . PHE A 1 3   ? 3.18500   -15.89700 -10.77500 1.000 22.70000  ? 3   PHE A HB3  1 
ATOM   80   H  HD1  . PHE A 1 3   ? 1.20200   -14.00300 -8.53200  1.000 26.73000  ? 3   PHE A HD1  1 
ATOM   81   H  HD2  . PHE A 1 3   ? 4.83900   -14.38100 -10.15900 1.000 23.08000  ? 3   PHE A HD2  1 
ATOM   82   H  HE1  . PHE A 1 3   ? 2.02400   -12.46000 -7.04200  1.000 23.71000  ? 3   PHE A HE1  1 
ATOM   83   H  HE2  . PHE A 1 3   ? 5.66900   -12.85000 -8.66700  1.000 23.69000  ? 3   PHE A HE2  1 
ATOM   84   H  HZ   . PHE A 1 3   ? 4.25900   -11.86000 -7.11400  1.000 27.42000  ? 3   PHE A HZ   1 
ATOM   85   N  N    . GLY A 1 4   ? 2.81500   -15.75800 -13.57600 1.000 20.84000  ? 4   GLY A N    1 
ATOM   86   C  CA   . GLY A 1 4   ? 3.24000   -16.90700 -14.35200 1.000 21.61000  ? 4   GLY A CA   1 
ATOM   87   C  C    . GLY A 1 4   ? 3.92400   -17.94100 -13.47700 1.000 15.92000  ? 4   GLY A C    1 
ATOM   88   O  O    . GLY A 1 4   ? 4.44800   -17.63600 -12.41300 1.000 18.18000  ? 4   GLY A O    1 
ATOM   89   H  H    . GLY A 1 4   ? 3.28800   -15.04800 -13.68800 1.000 25.00000  ? 4   GLY A H    1 
ATOM   90   H  HA2  . GLY A 1 4   ? 2.46800   -17.31800 -14.77300 1.000 25.92000  ? 4   GLY A HA2  1 
ATOM   91   H  HA3  . GLY A 1 4   ? 3.86100   -16.62300 -15.04100 1.000 25.92000  ? 4   GLY A HA3  1 
ATOM   92   N  N    . ARG A 1 5   ? 3.93300   -19.18800 -13.96200 1.000 21.22000  ? 5   ARG A N    1 
ATOM   93   C  CA   . ARG A 1 5   ? 4.51400   -20.29600 -13.21100 1.000 18.33000  ? 5   ARG A CA   1 
ATOM   94   C  C    . ARG A 1 5   ? 5.97900   -20.02400 -12.86600 1.000 19.81000  ? 5   ARG A C    1 
ATOM   95   O  O    . ARG A 1 5   ? 6.39700   -20.11000 -11.69800 1.000 18.09000  ? 5   ARG A O    1 
ATOM   96   C  CB   . ARG A 1 5   ? 4.36500   -21.57200 -14.05000 1.000 24.80000  ? 5   ARG A CB   1 
ATOM   97   C  CG   . ARG A 1 5   ? 5.04700   -22.79000 -13.47700 1.000 22.76000  ? 5   ARG A CG   1 
ATOM   98   C  CD   . ARG A 1 5   ? 4.81800   -24.04700 -14.35200 1.000 24.39000  ? 5   ARG A CD   1 
ATOM   99   N  NE   . ARG A 1 5   ? 5.45200   -23.97500 -15.66900 1.000 28.80000  ? 5   ARG A NE   1 
ATOM   100  C  CZ   . ARG A 1 5   ? 6.66700   -24.42800 -15.96000 1.000 26.45000  ? 5   ARG A CZ   1 
ATOM   101  N  NH1  . ARG A 1 5   ? 7.43100   -24.99900 -15.05000 1.000 24.52000  ? 5   ARG A NH1  1 
ATOM   102  N  NH2  . ARG A 1 5   ? 7.12000   -24.32400 -17.20500 1.000 30.86000  ? 5   ARG A NH2  1 
ATOM   103  H  H    . ARG A 1 5   ? 3.60700   -19.41600 -14.72400 1.000 25.45000  ? 5   ARG A H    1 
ATOM   104  H  HA   . ARG A 1 5   ? 4.04500   -20.41400 -12.37000 1.000 21.98000  ? 5   ARG A HA   1 
ATOM   105  H  HB2  . ARG A 1 5   ? 3.42100   -21.77800 -14.13100 1.000 29.74000  ? 5   ARG A HB2  1 
ATOM   106  H  HB3  . ARG A 1 5   ? 4.74600   -21.40900 -14.92700 1.000 29.74000  ? 5   ARG A HB3  1 
ATOM   107  H  HG2  . ARG A 1 5   ? 6.00200   -22.62600 -13.42600 1.000 27.29000  ? 5   ARG A HG2  1 
ATOM   108  H  HG3  . ARG A 1 5   ? 4.69300   -22.96800 -12.59200 1.000 27.29000  ? 5   ARG A HG3  1 
ATOM   109  H  HD2  . ARG A 1 5   ? 5.18300   -24.81800 -13.89100 1.000 29.26000  ? 5   ARG A HD2  1 
ATOM   110  H  HD3  . ARG A 1 5   ? 3.86500   -24.16200 -14.48900 1.000 29.26000  ? 5   ARG A HD3  1 
ATOM   111  H  HE   . ARG A 1 5   ? 5.00200   -23.61200 -16.30600 1.000 34.55000  ? 5   ARG A HE   1 
ATOM   112  H  HH11 . ARG A 1 5   ? 7.14700   -25.08600 -14.24300 1.000 29.41000  ? 5   ARG A HH11 1 
ATOM   113  H  HH12 . ARG A 1 5   ? 8.21400   -25.28300 -15.26300 1.000 29.41000  ? 5   ARG A HH12 1 
ATOM   114  H  HH21 . ARG A 1 5   ? 6.62700   -23.96600 -17.81200 1.000 37.02000  ? 5   ARG A HH21 1 
ATOM   115  H  HH22 . ARG A 1 5   ? 7.90500   -24.61300 -17.40300 1.000 37.02000  ? 5   ARG A HH22 1 
ATOM   116  N  N    . CYS A 1 6   ? 6.79700   -19.70600 -13.88000 1.000 19.80000  ? 6   CYS A N    1 
ATOM   117  C  CA   . CYS A 1 6   ? 8.20700   -19.50500 -13.58500 1.000 21.61000  ? 6   CYS A CA   1 
ATOM   118  C  C    . CYS A 1 6   ? 8.45300   -18.18400 -12.87400 1.000 17.26000  ? 6   CYS A C    1 
ATOM   119  O  O    . CYS A 1 6   ? 9.41500   -18.07600 -12.12200 1.000 20.72000  ? 6   CYS A O    1 
ATOM   120  C  CB   . CYS A 1 6   ? 9.05800   -19.58000 -14.86900 1.000 20.46000  ? 6   CYS A CB   1 
ATOM   121  S  SG   . CYS A 1 6   ? 9.07600   -21.23900 -15.58400 1.000 21.64000  ? 6   CYS A SG   1 
ATOM   122  H  H    . CYS A 1 6   ? 6.56600   -19.60700 -14.70200 1.000 23.74000  ? 6   CYS A H    1 
ATOM   123  H  HA   . CYS A 1 6   ? 8.49300   -20.22500 -13.00100 1.000 25.92000  ? 6   CYS A HA   1 
ATOM   124  H  HB2  . CYS A 1 6   ? 8.69100   -18.97100 -15.52900 1.000 24.54000  ? 6   CYS A HB2  1 
ATOM   125  H  HB3  . CYS A 1 6   ? 9.97200   -19.33100 -14.65900 1.000 24.54000  ? 6   CYS A HB3  1 
ATOM   126  N  N    . GLU A 1 7   ? 7.62000   -17.15600 -13.12200 1.000 17.59000  ? 7   GLU A N    1 
ATOM   127  C  CA   . GLU A 1 7   ? 7.75000   -15.89100 -12.40600 1.000 18.91000  ? 7   GLU A CA   1 
ATOM   128  C  C    . GLU A 1 7   ? 7.52500   -16.08900 -10.91400 1.000 15.93000  ? 7   GLU A C    1 
ATOM   129  O  O    . GLU A 1 7   ? 8.25600   -15.55100 -10.07900 1.000 17.63000  ? 7   GLU A O    1 
ATOM   130  C  CB   . GLU A 1 7   ? 6.69400   -14.93000 -12.95100 1.000 21.67000  ? 7   GLU A CB   1 
ATOM   131  C  CG   . GLU A 1 7   ? 6.72700   -13.53400 -12.35500 1.000 21.39000  ? 7   GLU A CG   1 
ATOM   132  C  CD   . GLU A 1 7   ? 5.49600   -12.69500 -12.72000 1.000 23.32000  ? 7   GLU A CD   1 
ATOM   133  O  OE1  . GLU A 1 7   ? 4.47400   -13.23400 -13.22800 1.000 22.75000  ? 7   GLU A OE1  1 
ATOM   134  O  OE2  . GLU A 1 7   ? 5.58700   -11.47200 -12.48900 1.000 26.36000  ? 7   GLU A OE2  1 
ATOM   135  H  H    . GLU A 1 7   ? 6.97900   -17.17200 -13.69600 1.000 21.10000  ? 7   GLU A H    1 
ATOM   136  H  HA   . GLU A 1 7   ? 8.63800   -15.52400 -12.53900 1.000 22.68000  ? 7   GLU A HA   1 
ATOM   137  H  HB2  . GLU A 1 7   ? 6.82600   -14.84000 -13.90800 1.000 25.99000  ? 7   GLU A HB2  1 
ATOM   138  H  HB3  . GLU A 1 7   ? 5.81700   -15.30300 -12.77000 1.000 25.99000  ? 7   GLU A HB3  1 
ATOM   139  H  HG2  . GLU A 1 7   ? 6.76300   -13.60500 -11.38800 1.000 25.65000  ? 7   GLU A HG2  1 
ATOM   140  H  HG3  . GLU A 1 7   ? 7.51200   -13.06900 -12.68400 1.000 25.65000  ? 7   GLU A HG3  1 
ATOM   141  N  N    . LEU A 1 8   ? 6.52200   -16.90300 -10.56400 1.000 17.38000  ? 8   LEU A N    1 
ATOM   142  C  CA   . LEU A 1 8   ? 6.27600   -17.18000 -9.15800  1.000 16.53000  ? 8   LEU A CA   1 
ATOM   143  C  C    . LEU A 1 8   ? 7.40300   -17.99800 -8.56100  1.000 16.24000  ? 8   LEU A C    1 
ATOM   144  O  O    . LEU A 1 8   ? 7.83500   -17.73800 -7.43200  1.000 16.12000  ? 8   LEU A O    1 
ATOM   145  C  CB   . LEU A 1 8   ? 4.95400   -17.92200 -9.01400  1.000 16.67000  ? 8   LEU A CB   1 
ATOM   146  C  CG   . LEU A 1 8   ? 4.58300   -18.23800 -7.57100  1.000 18.75000  ? 8   LEU A CG   1 
ATOM   147  C  CD1  . LEU A 1 8   ? 4.38800   -16.97000 -6.75100  1.000 21.07000  ? 8   LEU A CD1  1 
ATOM   148  C  CD2  . LEU A 1 8   ? 3.36200   -19.13300 -7.49000  1.000 21.26000  ? 8   LEU A CD2  1 
ATOM   149  H  H    . LEU A 1 8   ? 5.98600   -17.29300 -11.11100 1.000 20.85000  ? 8   LEU A H    1 
ATOM   150  H  HA   . LEU A 1 8   ? 6.21800   -16.34300 -8.67100  1.000 19.83000  ? 8   LEU A HA   1 
ATOM   151  H  HB2  . LEU A 1 8   ? 4.24700   -17.37400 -9.38800  1.000 19.99000  ? 8   LEU A HB2  1 
ATOM   152  H  HB3  . LEU A 1 8   ? 5.01400   -18.76100 -9.49600  1.000 19.99000  ? 8   LEU A HB3  1 
ATOM   153  H  HG   . LEU A 1 8   ? 5.32400   -18.72600 -7.17900  1.000 22.49000  ? 8   LEU A HG   1 
ATOM   154  H  HD11 . LEU A 1 8   ? 4.11600   -17.21400 -5.85200  1.000 25.27000  ? 8   LEU A HD11 1 
ATOM   155  H  HD12 . LEU A 1 8   ? 5.22500   -16.48000 -6.72200  1.000 25.27000  ? 8   LEU A HD12 1 
ATOM   156  H  HD13 . LEU A 1 8   ? 3.70100   -16.42600 -7.16800  1.000 25.27000  ? 8   LEU A HD13 1 
ATOM   157  H  HD21 . LEU A 1 8   ? 3.11000   -19.23700 -6.55900  1.000 25.50000  ? 8   LEU A HD21 1 
ATOM   158  H  HD22 . LEU A 1 8   ? 2.63700   -18.72200 -7.98500  1.000 25.50000  ? 8   LEU A HD22 1 
ATOM   159  H  HD23 . LEU A 1 8   ? 3.57800   -19.99700 -7.87300  1.000 25.50000  ? 8   LEU A HD23 1 
ATOM   160  N  N    . ALA A 1 9   ? 7.87600   -19.00600 -9.28800  1.000 17.03000  ? 9   ALA A N    1 
ATOM   161  C  CA   . ALA A 1 9   ? 8.98300   -19.78800 -8.75600  1.000 16.19000  ? 9   ALA A CA   1 
ATOM   162  C  C    . ALA A 1 9   ? 10.17800  -18.89400 -8.45000  1.000 16.97000  ? 9   ALA A C    1 
ATOM   163  O  O    . ALA A 1 9   ? 10.84400  -19.06900 -7.42700  1.000 17.03000  ? 9   ALA A O    1 
ATOM   164  C  CB   . ALA A 1 9   ? 9.35500   -20.88600 -9.75600  1.000 18.74000  ? 9   ALA A CB   1 
ATOM   165  H  H    . ALA A 1 9   ? 7.58500   -19.24700 -10.06100 1.000 20.42000  ? 9   ALA A H    1 
ATOM   166  H  HA   . ALA A 1 9   ? 8.71500   -20.21500 -7.92800  1.000 19.42000  ? 9   ALA A HA   1 
ATOM   167  H  HB1  . ALA A 1 9   ? 10.08900  -21.40600 -9.39400  1.000 22.47000  ? 9   ALA A HB1  1 
ATOM   168  H  HB2  . ALA A 1 9   ? 8.58400   -21.45600 -9.89900  1.000 22.47000  ? 9   ALA A HB2  1 
ATOM   169  H  HB3  . ALA A 1 9   ? 9.62100   -20.47400 -10.59200 1.000 22.47000  ? 9   ALA A HB3  1 
ATOM   170  N  N    . ALA A 1 10  ? 10.49400  -17.95000 -9.34500  1.000 17.20000  ? 10  ALA A N    1 
ATOM   171  C  CA   . ALA A 1 10  ? 11.63000  -17.07000 -9.09500  1.000 17.81000  ? 10  ALA A CA   1 
ATOM   172  C  C    . ALA A 1 10  ? 11.39200  -16.18500 -7.88700  1.000 16.73000  ? 10  ALA A C    1 
ATOM   173  O  O    . ALA A 1 10  ? 12.30300  -15.95600 -7.08100  1.000 19.00000  ? 10  ALA A O    1 
ATOM   174  C  CB   . ALA A 1 10  ? 11.91800  -16.20600 -10.32200 1.000 22.26000  ? 10  ALA A CB   1 
ATOM   175  H  H    . ALA A 1 10  ? 10.07600  -17.80600 -10.08300 1.000 20.63000  ? 10  ALA A H    1 
ATOM   176  H  HA   . ALA A 1 10  ? 12.40800  -17.62300 -8.92300  1.000 21.36000  ? 10  ALA A HA   1 
ATOM   177  H  HB1  . ALA A 1 10  ? 12.57500  -15.53200 -10.08700 1.000 26.70000  ? 10  ALA A HB1  1 
ATOM   178  H  HB2  . ALA A 1 10  ? 12.26300  -16.77100 -11.03200 1.000 26.70000  ? 10  ALA A HB2  1 
ATOM   179  H  HB3  . ALA A 1 10  ? 11.09500  -15.78000 -10.60900 1.000 26.70000  ? 10  ALA A HB3  1 
ATOM   180  N  N    . ALA A 1 11  ? 10.17800  -15.66400 -7.74500  1.000 16.64000  ? 11  ALA A N    1 
ATOM   181  C  CA   . ALA A 1 11  ? 9.90500   -14.82800 -6.59000  1.000 18.29000  ? 11  ALA A CA   1 
ATOM   182  C  C    . ALA A 1 11  ? 10.00800  -15.62400 -5.29900  1.000 17.95000  ? 11  ALA A C    1 
ATOM   183  O  O    . ALA A 1 11  ? 10.52800  -15.12600 -4.29800  1.000 19.58000  ? 11  ALA A O    1 
ATOM   184  C  CB   . ALA A 1 11  ? 8.53000   -14.18100 -6.70500  1.000 21.39000  ? 11  ALA A CB   1 
ATOM   185  H  H    . ALA A 1 11  ? 9.51800   -15.77600 -8.28500  1.000 19.95000  ? 11  ALA A H    1 
ATOM   186  H  HA   . ALA A 1 11  ? 10.56500  -14.11700 -6.56500  1.000 21.94000  ? 11  ALA A HA   1 
ATOM   187  H  HB1  . ALA A 1 11  ? 8.36900   -13.63900 -5.91700  1.000 25.65000  ? 11  ALA A HB1  1 
ATOM   188  H  HB2  . ALA A 1 11  ? 8.50900   -13.62400 -7.49900  1.000 25.65000  ? 11  ALA A HB2  1 
ATOM   189  H  HB3  . ALA A 1 11  ? 7.85800   -14.87700 -6.77200  1.000 25.65000  ? 11  ALA A HB3  1 
ATOM   190  N  N    . MET A 1 12  ? 9.51100   -16.86600 -5.29400  1.000 17.23000  ? 12  MET A N    1 
ATOM   191  C  CA   . MET A 1 12  ? 9.59800   -17.69600 -4.08500  1.000 16.41000  ? 12  MET A CA   1 
ATOM   192  C  C    . MET A 1 12  ? 11.03900  -18.05000 -3.75500  1.000 18.15000  ? 12  MET A C    1 
ATOM   193  O  O    . MET A 1 12  ? 11.41200  -18.08900 -2.57200  1.000 19.40000  ? 12  MET A O    1 
ATOM   194  C  CB   . MET A 1 12  ? 8.80400   -18.94900 -4.33900  1.000 16.60000  ? 12  MET A CB   1 
ATOM   195  C  CG   . MET A 1 12  ? 7.33300   -18.67500 -4.46800  1.000 18.21000  ? 12  MET A CG   1 
ATOM   196  S  SD   . MET A 1 12  ? 6.36100   -20.19200 -4.50000  1.000 18.64000  ? 12  MET A SD   1 
ATOM   197  C  CE   . MET A 1 12  ? 4.77400   -19.74700 -3.79100  1.000 21.83000  ? 12  MET A CE   1 
ATOM   198  H  H    . MET A 1 12  ? 9.12600   -17.24500 -5.96200  1.000 20.67000  ? 12  MET A H    1 
ATOM   199  H  HA   . MET A 1 12  ? 9.22700   -17.21600 -3.32800  1.000 19.68000  ? 12  MET A HA   1 
ATOM   200  H  HB2  . MET A 1 12  ? 9.10900   -19.35600 -5.16500  1.000 19.91000  ? 12  MET A HB2  1 
ATOM   201  H  HB3  . MET A 1 12  ? 8.93400   -19.56200 -3.59900  1.000 19.91000  ? 12  MET A HB3  1 
ATOM   202  H  HG2  . MET A 1 12  ? 7.04000   -18.14400 -3.71100  1.000 21.84000  ? 12  MET A HG2  1 
ATOM   203  H  HG3  . MET A 1 12  ? 7.16900   -18.19300 -5.29400  1.000 21.84000  ? 12  MET A HG3  1 
ATOM   204  H  HE1  . MET A 1 12  ? 4.20600   -20.53300 -3.76900  1.000 26.19000  ? 12  MET A HE1  1 
ATOM   205  H  HE2  . MET A 1 12  ? 4.91300   -19.41500 -2.89000  1.000 26.19000  ? 12  MET A HE2  1 
ATOM   206  H  HE3  . MET A 1 12  ? 4.36500   -19.05900 -4.33800  1.000 26.19000  ? 12  MET A HE3  1 
ATOM   207  N  N    A LYS A 1 13  ? 11.86700  -18.30900 -4.77000  0.560 17.50000  ? 13  LYS A N    1 
ATOM   208  N  N    B LYS A 1 13  ? 11.85100  -18.29400 -4.79700  0.440 17.43000  ? 13  LYS A N    1 
ATOM   209  C  CA   A LYS A 1 13  ? 13.28200  -18.56100 -4.49700  0.560 20.81000  ? 13  LYS A CA   1 
ATOM   210  C  CA   B LYS A 1 13  ? 13.27400  -18.58700 -4.62100  0.440 20.82000  ? 13  LYS A CA   1 
ATOM   211  C  C    A LYS A 1 13  ? 13.96800  -17.31900 -3.92300  0.560 20.50000  ? 13  LYS A C    1 
ATOM   212  C  C    B LYS A 1 13  ? 14.01500  -17.41000 -3.99000  0.440 20.30000  ? 13  LYS A C    1 
ATOM   213  O  O    A LYS A 1 13  ? 14.71600  -17.40400 -2.94000  0.560 20.22000  ? 13  LYS A O    1 
ATOM   214  O  O    B LYS A 1 13  ? 14.81700  -17.59500 -3.07100  0.440 21.96000  ? 13  LYS A O    1 
ATOM   215  C  CB   A LYS A 1 13  ? 13.96400  -19.01500 -5.78200  0.560 19.36000  ? 13  LYS A CB   1 
ATOM   216  C  CB   B LYS A 1 13  ? 13.88900  -18.94700 -5.97800  0.440 18.81000  ? 13  LYS A CB   1 
ATOM   217  C  CG   A LYS A 1 13  ? 15.40200  -19.44100 -5.55800  0.560 21.24000  ? 13  LYS A CG   1 
ATOM   218  C  CG   B LYS A 1 13  ? 15.40600  -19.19800 -5.93800  0.440 27.72000  ? 13  LYS A CG   1 
ATOM   219  C  CD   A LYS A 1 13  ? 15.96200  -20.19500 -6.74100  0.560 22.01000  ? 13  LYS A CD   1 
ATOM   220  C  CD   B LYS A 1 13  ? 15.76400  -20.63500 -6.27500  0.440 32.32000  ? 13  LYS A CD   1 
ATOM   221  C  CE   A LYS A 1 13  ? 17.38100  -20.69100 -6.41800  0.560 33.19000  ? 13  LYS A CE   1 
ATOM   222  C  CE   B LYS A 1 13  ? 17.27500  -20.88200 -6.16100  0.440 32.13000  ? 13  LYS A CE   1 
ATOM   223  N  NZ   A LYS A 1 13  ? 17.44700  -21.58000 -5.21400  0.560 35.87000  ? 13  LYS A NZ   1 
ATOM   224  N  NZ   B LYS A 1 13  ? 18.02200  -20.60400 -7.42800  0.440 34.60000  ? 13  LYS A NZ   1 
ATOM   225  H  H    A LYS A 1 13  ? 11.64200  -18.34400 -5.59900  0.560 20.99000  ? 13  LYS A H    1 
ATOM   226  H  H    B LYS A 1 13  ? 11.59700  -18.29600 -5.61900  0.440 20.90000  ? 13  LYS A H    1 
ATOM   227  H  HA   A LYS A 1 13  ? 13.36400  -19.26800 -3.83900  0.560 24.96000  ? 13  LYS A HA   1 
ATOM   228  H  HA   B LYS A 1 13  ? 13.36800  -19.34500 -4.02500  0.440 24.97000  ? 13  LYS A HA   1 
ATOM   229  H  HB2  A LYS A 1 13  ? 13.47900  -19.77100 -6.14700  0.560 23.22000  ? 13  LYS A HB2  1 
ATOM   230  H  HB2  B LYS A 1 13  ? 13.46600  -19.75700 -6.30500  0.440 22.56000  ? 13  LYS A HB2  1 
ATOM   231  H  HB3  A LYS A 1 13  ? 13.96300  -18.28100 -6.41700  0.560 23.22000  ? 13  LYS A HB3  1 
ATOM   232  H  HB3  B LYS A 1 13  ? 13.72800  -18.21600 -6.59500  0.440 22.56000  ? 13  LYS A HB3  1 
ATOM   233  H  HG2  A LYS A 1 13  ? 15.94900  -18.65300 -5.41400  0.560 25.48000  ? 13  LYS A HG2  1 
ATOM   234  H  HG2  B LYS A 1 13  ? 15.84100  -18.61900 -6.58300  0.440 33.25000  ? 13  LYS A HG2  1 
ATOM   235  H  HG3  A LYS A 1 13  ? 15.44500  -20.02100 -4.78200  0.560 25.48000  ? 13  LYS A HG3  1 
ATOM   236  H  HG3  B LYS A 1 13  ? 15.73600  -19.00700 -5.04600  0.440 33.25000  ? 13  LYS A HG3  1 
ATOM   237  H  HD2  A LYS A 1 13  ? 15.40100  -20.96100 -6.93800  0.560 26.40000  ? 13  LYS A HD2  1 
ATOM   238  H  HD2  B LYS A 1 13  ? 15.31100  -21.23200 -5.66000  0.440 38.78000  ? 13  LYS A HD2  1 
ATOM   239  H  HD3  A LYS A 1 13  ? 16.00600  -19.60800 -7.51300  0.560 26.40000  ? 13  LYS A HD3  1 
ATOM   240  H  HD3  B LYS A 1 13  ? 15.49200  -20.82800 -7.18600  0.440 38.78000  ? 13  LYS A HD3  1 
ATOM   241  H  HE2  A LYS A 1 13  ? 17.71600  -21.19500 -7.17600  0.560 39.82000  ? 13  LYS A HE2  1 
ATOM   242  H  HE2  B LYS A 1 13  ? 17.63600  -20.30400 -5.47100  0.440 38.55000  ? 13  LYS A HE2  1 
ATOM   243  H  HE3  A LYS A 1 13  ? 17.95000  -19.92400 -6.25000  0.560 39.82000  ? 13  LYS A HE3  1 
ATOM   244  H  HE3  B LYS A 1 13  ? 17.42400  -21.81100 -5.92700  0.440 38.55000  ? 13  LYS A HE3  1 
ATOM   245  H  HZ1  A LYS A 1 13  ? 18.27700  -21.88300 -5.10500  0.560 43.03000  ? 13  LYS A HZ1  1 
ATOM   246  H  HZ1  B LYS A 1 13  ? 18.88600  -20.78600 -7.31800  0.440 41.51000  ? 13  LYS A HZ1  1 
ATOM   247  H  HZ2  A LYS A 1 13  ? 17.20700  -21.12700 -4.48700  0.560 43.03000  ? 13  LYS A HZ2  1 
ATOM   248  H  HZ2  B LYS A 1 13  ? 17.70200  -21.11000 -8.08700  0.440 41.51000  ? 13  LYS A HZ2  1 
ATOM   249  H  HZ3  A LYS A 1 13  ? 16.89900  -22.27300 -5.31700  0.560 43.03000  ? 13  LYS A HZ3  1 
ATOM   250  H  HZ3  B LYS A 1 13  ? 17.93300  -19.74800 -7.65200  0.440 41.51000  ? 13  LYS A HZ3  1 
ATOM   251  N  N    A ARG A 1 14  ? 13.70700  -16.14800 -4.50500  0.560 18.42000  ? 14  ARG A N    1 
ATOM   252  N  N    B ARG A 1 14  ? 13.77800  -16.18500 -4.47700  0.440 18.47000  ? 14  ARG A N    1 
ATOM   253  C  CA   A ARG A 1 14  ? 14.32600  -14.92300 -4.00400  0.560 20.76000  ? 14  ARG A CA   1 
ATOM   254  C  CA   B ARG A 1 14  ? 14.47400  -15.04400 -3.88500  0.440 19.21000  ? 14  ARG A CA   1 
ATOM   255  C  C    A ARG A 1 14  ? 13.99900  -14.68400 -2.53200  0.560 21.31000  ? 14  ARG A C    1 
ATOM   256  C  C    B ARG A 1 14  ? 14.08100  -14.84200 -2.42900  0.440 23.33000  ? 14  ARG A C    1 
ATOM   257  O  O    A ARG A 1 14  ? 14.80600  -14.10200 -1.79800  0.560 25.37000  ? 14  ARG A O    1 
ATOM   258  O  O    B ARG A 1 14  ? 14.91600  -14.44200 -1.60800  0.440 21.44000  ? 14  ARG A O    1 
ATOM   259  C  CB   A ARG A 1 14  ? 13.85500  -13.75200 -4.87200  0.560 24.37000  ? 14  ARG A CB   1 
ATOM   260  C  CB   B ARG A 1 14  ? 14.21000  -13.75200 -4.66200  0.440 27.01000  ? 14  ARG A CB   1 
ATOM   261  C  CG   A ARG A 1 14  ? 14.04400  -12.37000 -4.27700  0.560 32.35000  ? 14  ARG A CG   1 
ATOM   262  C  CG   B ARG A 1 14  ? 14.93900  -12.53900 -4.04700  0.440 31.87000  ? 14  ARG A CG   1 
ATOM   263  C  CD   A ARG A 1 14  ? 13.79800  -11.30500 -5.33900  0.560 27.86000  ? 14  ARG A CD   1 
ATOM   264  C  CD   B ARG A 1 14  ? 14.77200  -11.25900 -4.85900  0.440 31.13000  ? 14  ARG A CD   1 
ATOM   265  N  NE   A ARG A 1 14  ? 12.42400  -11.32500 -5.82200  0.560 38.66000  ? 14  ARG A NE   1 
ATOM   266  N  NE   B ARG A 1 14  ? 13.70800  -10.40800 -4.33600  0.440 33.04000  ? 14  ARG A NE   1 
ATOM   267  C  CZ   A ARG A 1 14  ? 11.41800  -10.67600 -5.25300  0.560 35.32000  ? 14  ARG A CZ   1 
ATOM   268  C  CZ   B ARG A 1 14  ? 13.83200  -9.58800  -3.30100  0.440 25.54000  ? 14  ARG A CZ   1 
ATOM   269  N  NH1  A ARG A 1 14  ? 11.61200  -9.85800  -4.22900  0.560 37.64000  ? 14  ARG A NH1  1 
ATOM   270  N  NH1  B ARG A 1 14  ? 14.98000  -9.45600  -2.65200  0.440 37.77000  ? 14  ARG A NH1  1 
ATOM   271  N  NH2  A ARG A 1 14  ? 10.18600  -10.86500 -5.71100  0.560 28.61000  ? 14  ARG A NH2  1 
ATOM   272  N  NH2  B ARG A 1 14  ? 12.77400  -8.89200  -2.89700  0.440 33.35000  ? 14  ARG A NH2  1 
ATOM   273  H  H    A ARG A 1 14  ? 13.18500  -16.03700 -5.18000  0.560 22.09000  ? 14  ARG A H    1 
ATOM   274  H  H    B ARG A 1 14  ? 13.24100  -15.99800 -5.12200  0.440 22.15000  ? 14  ARG A H    1 
ATOM   275  H  HA   A ARG A 1 14  ? 15.29200  -14.98800 -4.06900  0.560 24.90000  ? 14  ARG A HA   1 
ATOM   276  H  HA   B ARG A 1 14  ? 15.42500  -15.22800 -3.93900  0.440 23.03000  ? 14  ARG A HA   1 
ATOM   277  H  HB2  A ARG A 1 14  ? 14.34800  -13.77600 -5.70700  0.560 29.23000  ? 14  ARG A HB2  1 
ATOM   278  H  HB2  B ARG A 1 14  ? 14.52200  -13.86100 -5.57400  0.440 32.40000  ? 14  ARG A HB2  1 
ATOM   279  H  HB3  A ARG A 1 14  ? 12.90700  -13.86400 -5.04400  0.560 29.23000  ? 14  ARG A HB3  1 
ATOM   280  H  HB3  B ARG A 1 14  ? 13.25800  -13.56700 -4.65700  0.440 32.40000  ? 14  ARG A HB3  1 
ATOM   281  H  HG2  A ARG A 1 14  ? 13.41300  -12.23800 -3.55200  0.560 38.81000  ? 14  ARG A HG2  1 
ATOM   282  H  HG2  B ARG A 1 14  ? 14.58400  -12.37600 -3.15900  0.440 38.23000  ? 14  ARG A HG2  1 
ATOM   283  H  HG3  A ARG A 1 14  ? 14.95200  -12.27700 -3.94800  0.560 38.81000  ? 14  ARG A HG3  1 
ATOM   284  H  HG3  B ARG A 1 14  ? 15.88800  -12.73600 -3.99400  0.440 38.23000  ? 14  ARG A HG3  1 
ATOM   285  H  HD2  A ARG A 1 14  ? 13.97300  -10.43000 -4.96000  0.560 33.41000  ? 14  ARG A HD2  1 
ATOM   286  H  HD2  B ARG A 1 14  ? 15.60100  -10.75500 -4.83400  0.440 37.35000  ? 14  ARG A HD2  1 
ATOM   287  H  HD3  A ARG A 1 14  ? 14.38600  -11.46500 -6.09300  0.560 33.41000  ? 14  ARG A HD3  1 
ATOM   288  H  HD3  B ARG A 1 14  ? 14.55200  -11.49000 -5.77500  0.440 37.35000  ? 14  ARG A HD3  1 
ATOM   289  H  HE   A ARG A 1 14  ? 12.25300  -11.79100 -6.52500  0.560 46.38000  ? 14  ARG A HE   1 
ATOM   290  H  HE   B ARG A 1 14  ? 12.94400  -10.44000 -4.72900  0.440 39.63000  ? 14  ARG A HE   1 
ATOM   291  H  HH11 A ARG A 1 14  ? 12.40500  -9.73800  -3.91900  0.560 45.16000  ? 14  ARG A HH11 1 
ATOM   292  H  HH11 B ARG A 1 14  ? 15.66800  -9.90800  -2.90000  0.440 45.32000  ? 14  ARG A HH11 1 
ATOM   293  H  HH12 A ARG A 1 14  ? 10.94500  -9.44600  -3.87500  0.560 45.16000  ? 14  ARG A HH12 1 
ATOM   294  H  HH12 B ARG A 1 14  ? 15.03600  -8.91900  -1.98300  0.440 45.32000  ? 14  ARG A HH12 1 
ATOM   295  H  HH21 A ARG A 1 14  ? 10.05000  -11.40300 -6.36900  0.560 34.32000  ? 14  ARG A HH21 1 
ATOM   296  H  HH21 B ARG A 1 14  ? 12.02200  -8.97600  -3.30500  0.440 40.01000  ? 14  ARG A HH21 1 
ATOM   297  H  HH22 A ARG A 1 14  ? 9.52500   -10.45000 -5.35100  0.560 34.32000  ? 14  ARG A HH22 1 
ATOM   298  H  HH22 B ARG A 1 14  ? 12.84200  -8.35800  -2.22600  0.440 40.01000  ? 14  ARG A HH22 1 
ATOM   299  N  N    . HIS A 1 15  ? 12.82800  -15.13700 -2.07500  1.000 21.34000  ? 15  HIS A N    1 
ATOM   300  C  CA   . HIS A 1 15  ? 12.38700  -14.98400 -0.70100  1.000 20.53000  ? 15  HIS A CA   1 
ATOM   301  C  C    . HIS A 1 15  ? 12.73400  -16.17500 0.18400   1.000 22.63000  ? 15  HIS A C    1 
ATOM   302  O  O    . HIS A 1 15  ? 12.23200  -16.24100 1.31300   1.000 27.14000  ? 15  HIS A O    1 
ATOM   303  C  CB   . HIS A 1 15  ? 10.87500  -14.75600 -0.64600  1.000 22.01000  ? 15  HIS A CB   1 
ATOM   304  C  CG   . HIS A 1 15  ? 10.44700  -13.40600 -1.10900  1.000 22.19000  ? 15  HIS A CG   1 
ATOM   305  N  ND1  . HIS A 1 15  ? 10.49200  -12.30200 -0.28800  1.000 34.84000  ? 15  HIS A ND1  1 
ATOM   306  C  CD2  . HIS A 1 15  ? 9.95500   -12.97700 -2.29300  1.000 22.25000  ? 15  HIS A CD2  1 
ATOM   307  C  CE1  . HIS A 1 15  ? 10.04700  -11.24900 -0.94800  1.000 30.96000  ? 15  HIS A CE1  1 
ATOM   308  N  NE2  . HIS A 1 15  ? 9.70800   -11.63200 -2.16400  1.000 28.19000  ? 15  HIS A NE2  1 
ATOM   309  H  H    . HIS A 1 15  ? 12.25600  -15.55100 -2.56500  1.000 25.59000  ? 15  HIS A H    1 
ATOM   310  H  HA   . HIS A 1 15  ? 12.83100  -14.20000 -0.34100  1.000 24.62000  ? 15  HIS A HA   1 
ATOM   311  H  HB2  . HIS A 1 15  ? 10.44100  -15.41300 -1.21200  1.000 26.40000  ? 15  HIS A HB2  1 
ATOM   312  H  HB3  . HIS A 1 15  ? 10.57800  -14.86000 0.27200   1.000 26.40000  ? 15  HIS A HB3  1 
ATOM   313  H  HD1  . HIS A 1 15  ? 10.76700  -12.29800 0.52700   1.000 41.80000  ? 15  HIS A HD1  1 
ATOM   314  H  HD2  . HIS A 1 15  ? 9.81200   -13.49500 -3.05100  1.000 26.68000  ? 15  HIS A HD2  1 
ATOM   315  H  HE1  . HIS A 1 15  ? 9.98300   -10.38400 -0.61200  1.000 37.13000  ? 15  HIS A HE1  1 
ATOM   316  N  N    . GLY A 1 16  ? 13.52400  -17.12100 -0.30600  1.000 19.47000  ? 16  GLY A N    1 
ATOM   317  C  CA   . GLY A 1 16  ? 14.07700  -18.15300 0.54200   1.000 20.60000  ? 16  GLY A CA   1 
ATOM   318  C  C    . GLY A 1 16  ? 13.21100  -19.37900 0.76600   1.000 21.57000  ? 16  GLY A C    1 
ATOM   319  O  O    . GLY A 1 16  ? 13.44700  -20.10200 1.74600   1.000 23.38000  ? 16  GLY A O    1 
ATOM   320  H  H    . GLY A 1 16  ? 13.75400  -17.18300 -1.13200  1.000 23.35000  ? 16  GLY A H    1 
ATOM   321  H  HA2  . GLY A 1 16  ? 14.91100  -18.45500 0.15000   1.000 24.71000  ? 16  GLY A HA2  1 
ATOM   322  H  HA3  . GLY A 1 16  ? 14.26000  -17.76600 1.41300   1.000 24.71000  ? 16  GLY A HA3  1 
ATOM   323  N  N    . LEU A 1 17  ? 12.23200  -19.65000 -0.08800  1.000 20.38000  ? 17  LEU A N    1 
ATOM   324  C  CA   . LEU A 1 17  ? 11.40300  -20.84400 0.06300   1.000 20.78000  ? 17  LEU A CA   1 
ATOM   325  C  C    . LEU A 1 17  ? 11.97600  -22.13200 -0.51500  1.000 20.84000  ? 17  LEU A C    1 
ATOM   326  O  O    . LEU A 1 17  ? 11.56600  -23.20200 -0.11800  1.000 20.29000  ? 17  LEU A O    1 
ATOM   327  C  CB   . LEU A 1 17  ? 9.99900   -20.61900 -0.53400  1.000 21.83000  ? 17  LEU A CB   1 
ATOM   328  C  CG   . LEU A 1 17  ? 9.01200   -19.84800 0.32400   1.000 23.78000  ? 17  LEU A CG   1 
ATOM   329  C  CD1  . LEU A 1 17  ? 7.67200   -19.83700 -0.38200  1.000 20.82000  ? 17  LEU A CD1  1 
ATOM   330  C  CD2  . LEU A 1 17  ? 8.86200   -20.47400 1.69500   1.000 20.99000  ? 17  LEU A CD2  1 
ATOM   331  H  H    . LEU A 1 17  ? 12.01900  -19.16600 -0.76900  1.000 24.44000  ? 17  LEU A H    1 
ATOM   332  H  HA   . LEU A 1 17  ? 11.28300  -21.00800 1.01900   1.000 24.93000  ? 17  LEU A HA   1 
ATOM   333  H  HB2  . LEU A 1 17  ? 10.09600  -20.13500 -1.36900  1.000 26.18000  ? 17  LEU A HB2  1 
ATOM   334  H  HB3  . LEU A 1 17  ? 9.60200   -21.48700 -0.70700  1.000 26.18000  ? 17  LEU A HB3  1 
ATOM   335  H  HG   . LEU A 1 17  ? 9.31700   -18.93400 0.43000   1.000 28.52000  ? 17  LEU A HG   1 
ATOM   336  H  HD11 . LEU A 1 17  ? 7.13900   -19.12300 -0.02300  1.000 24.97000  ? 17  LEU A HD11 1 
ATOM   337  H  HD12 . LEU A 1 17  ? 7.82000   -19.70400 -1.32200  1.000 24.97000  ? 17  LEU A HD12 1 
ATOM   338  H  HD13 . LEU A 1 17  ? 7.24300   -20.68400 -0.23100  1.000 24.97000  ? 17  LEU A HD13 1 
ATOM   339  H  HD21 . LEU A 1 17  ? 7.97700   -20.29300 2.02000   1.000 25.17000  ? 17  LEU A HD21 1 
ATOM   340  H  HD22 . LEU A 1 17  ? 8.99600   -21.42300 1.61400   1.000 25.17000  ? 17  LEU A HD22 1 
ATOM   341  H  HD23 . LEU A 1 17  ? 9.51800   -20.09700 2.28700   1.000 25.17000  ? 17  LEU A HD23 1 
ATOM   342  N  N    A ASP A 1 18  ? 12.94000  -22.03400 -1.41500  0.490 20.22000  ? 18  ASP A N    1 
ATOM   343  N  N    B ASP A 1 18  ? 12.98100  -22.00800 -1.40900  0.510 20.34000  ? 18  ASP A N    1 
ATOM   344  C  CA   A ASP A 1 18  ? 13.51400  -23.22500 -1.99900  0.490 20.83000  ? 18  ASP A CA   1 
ATOM   345  C  CA   B ASP A 1 18  ? 13.52900  -23.17600 -2.08400  0.510 20.84000  ? 18  ASP A CA   1 
ATOM   346  C  C    A ASP A 1 18  ? 14.21500  -24.05700 -0.93600  0.490 25.23000  ? 18  ASP A C    1 
ATOM   347  C  C    B ASP A 1 18  ? 14.29500  -24.03500 -1.08400  0.510 23.21000  ? 18  ASP A C    1 
ATOM   348  O  O    A ASP A 1 18  ? 15.20500  -23.62000 -0.37500  0.490 22.48000  ? 18  ASP A O    1 
ATOM   349  O  O    B ASP A 1 18  ? 15.42800  -23.72500 -0.70600  0.510 22.08000  ? 18  ASP A O    1 
ATOM   350  C  CB   A ASP A 1 18  ? 14.48600  -22.89100 -3.11700  0.490 21.71000  ? 18  ASP A CB   1 
ATOM   351  C  CB   B ASP A 1 18  ? 14.42200  -22.75300 -3.24400  0.510 24.00000  ? 18  ASP A CB   1 
ATOM   352  C  CG   A ASP A 1 18  ? 14.87000  -24.11700 -3.94400  0.490 20.58000  ? 18  ASP A CG   1 
ATOM   353  C  CG   B ASP A 1 18  ? 15.48400  -21.74600 -2.83900  0.510 31.41000  ? 18  ASP A CG   1 
ATOM   354  O  OD1  A ASP A 1 18  ? 14.31300  -25.22000 -3.73200  0.490 18.92000  ? 18  ASP A OD1  1 
ATOM   355  O  OD1  B ASP A 1 18  ? 15.15000  -20.73500 -2.17800  0.510 23.69000  ? 18  ASP A OD1  1 
ATOM   356  O  OD2  A ASP A 1 18  ? 15.74400  -23.97700 -4.81900  0.490 29.01000  ? 18  ASP A OD2  1 
ATOM   357  O  OD2  B ASP A 1 18  ? 16.65300  -21.96700 -3.21300  0.510 32.96000  ? 18  ASP A OD2  1 
ATOM   358  H  H    A ASP A 1 18  ? 13.10600  -21.31600 -1.86000  0.490 24.25000  ? 18  ASP A H    1 
ATOM   359  H  H    B ASP A 1 18  ? 13.34500  -21.26600 -1.64400  0.510 24.40000  ? 18  ASP A H    1 
ATOM   360  H  HA   A ASP A 1 18  ? 12.78900  -23.76300 -2.38100  0.490 24.98000  ? 18  ASP A HA   1 
ATOM   361  H  HA   B ASP A 1 18  ? 12.79700  -23.70600 -2.43700  0.510 24.99000  ? 18  ASP A HA   1 
ATOM   362  H  HB2  A ASP A 1 18  ? 14.07200  -22.24500 -3.71100  0.490 26.04000  ? 18  ASP A HB2  1 
ATOM   363  H  HB2  B ASP A 1 18  ? 14.87200  -23.53600 -3.59800  0.510 28.78000  ? 18  ASP A HB2  1 
ATOM   364  H  HB3  A ASP A 1 18  ? 15.29500  -22.51900 -2.73600  0.490 26.04000  ? 18  ASP A HB3  1 
ATOM   365  H  HB3  B ASP A 1 18  ? 13.87200  -22.34700 -3.93300  0.510 28.78000  ? 18  ASP A HB3  1 
ATOM   366  N  N    A ASN A 1 19  ? 13.69100  -25.24100 -0.66400  0.510 18.84000  ? 19  ASN A N    1 
ATOM   367  N  N    B ASN A 1 19  ? 13.67400  -25.13900 -0.67200  0.490 19.01000  ? 19  ASN A N    1 
ATOM   368  C  CA   A ASN A 1 19  ? 14.23700  -26.13700 0.36800   0.510 17.90000  ? 19  ASN A CA   1 
ATOM   369  C  CA   B ASN A 1 19  ? 14.19200  -26.09900 0.30100   0.490 17.85000  ? 19  ASN A CA   1 
ATOM   370  C  C    A ASN A 1 19  ? 14.10700  -25.62200 1.79700   0.510 18.55000  ? 19  ASN A C    1 
ATOM   371  C  C    B ASN A 1 19  ? 14.03200  -25.66700 1.75400   0.490 18.61000  ? 19  ASN A C    1 
ATOM   372  O  O    A ASN A 1 19  ? 14.69900  -26.17600 2.70700   0.510 21.90000  ? 19  ASN A O    1 
ATOM   373  O  O    B ASN A 1 19  ? 14.63100  -26.26400 2.66500   0.490 17.95000  ? 19  ASN A O    1 
ATOM   374  C  CB   A ASN A 1 19  ? 15.67300  -26.55100 0.02100   0.510 23.26000  ? 19  ASN A CB   1 
ATOM   375  C  CB   B ASN A 1 19  ? 15.62000  -26.57400 0.02300   0.490 23.18000  ? 19  ASN A CB   1 
ATOM   376  C  CG   A ASN A 1 19  ? 15.69500  -27.67400 -0.97200  0.510 23.16000  ? 19  ASN A CG   1 
ATOM   377  C  CG   B ASN A 1 19  ? 15.77300  -28.05500 0.28100   0.490 25.26000  ? 19  ASN A CG   1 
ATOM   378  O  OD1  A ASN A 1 19  ? 15.13600  -28.72900 -0.71600  0.510 28.07000  ? 19  ASN A OD1  1 
ATOM   379  O  OD1  B ASN A 1 19  ? 14.79500  -28.80900 0.21300   0.490 24.38000  ? 19  ASN A OD1  1 
ATOM   380  N  ND2  A ASN A 1 19  ? 16.28700  -27.43900 -2.12900  0.510 36.55000  ? 19  ASN A ND2  1 
ATOM   381  N  ND2  B ASN A 1 19  ? 16.98800  -28.48500 0.58800   0.490 34.34000  ? 19  ASN A ND2  1 
ATOM   382  H  H    A ASN A 1 19  ? 13.00100  -25.56100 -1.06700  0.510 22.60000  ? 19  ASN A H    1 
ATOM   383  H  H    B ASN A 1 19  ? 12.89700  -25.36700 -0.96200  0.490 22.80000  ? 19  ASN A H    1 
ATOM   384  H  HA   A ASN A 1 19  ? 13.70300  -26.95900 0.34400   0.510 21.47000  ? 19  ASN A HA   1 
ATOM   385  H  HA   B ASN A 1 19  ? 13.63800  -26.88800 0.19700   0.490 21.40000  ? 19  ASN A HA   1 
ATOM   386  H  HB2  A ASN A 1 19  ? 16.15600  -25.80900 -0.36600  0.510 27.90000  ? 19  ASN A HB2  1 
ATOM   387  H  HB2  B ASN A 1 19  ? 15.84000  -26.40200 -0.90600  0.490 27.81000  ? 19  ASN A HB2  1 
ATOM   388  H  HB3  A ASN A 1 19  ? 16.12200  -26.85800 0.82100   0.510 27.90000  ? 19  ASN A HB3  1 
ATOM   389  H  HB3  B ASN A 1 19  ? 16.23500  -26.09900 0.60400   0.490 27.81000  ? 19  ASN A HB3  1 
ATOM   390  H  HD21 A ASN A 1 19  ? 16.55800  -28.18700 -2.70100  0.510 43.85000  ? 19  ASN A HD21 1 
ATOM   391  H  HD21 B ASN A 1 19  ? 17.12200  -29.32000 0.74300   0.490 41.20000  ? 19  ASN A HD21 1 
ATOM   392  H  HD22 A ASN A 1 19  ? 16.44500  -26.51500 -2.41700  0.510 43.85000  ? 19  ASN A HD22 1 
ATOM   393  H  HD22 B ASN A 1 19  ? 17.64200  -27.92800 0.63300   0.490 41.20000  ? 19  ASN A HD22 1 
ATOM   394  N  N    . TYR A 1 20  ? 13.16500  -24.73000 2.01900   1.000 18.52000  ? 20  TYR A N    1 
ATOM   395  C  CA   . TYR A 1 20  ? 12.88400  -24.28600 3.36200   1.000 16.36000  ? 20  TYR A CA   1 
ATOM   396  C  C    . TYR A 1 20  ? 12.27200  -25.45400 4.11600   1.000 21.84000  ? 20  TYR A C    1 
ATOM   397  O  O    . TYR A 1 20  ? 11.22700  -25.94400 3.72800   1.000 19.77000  ? 20  TYR A O    1 
ATOM   398  C  CB   . TYR A 1 20  ? 11.94900  -23.07100 3.34400   1.000 17.52000  ? 20  TYR A CB   1 
ATOM   399  C  CG   . TYR A 1 20  ? 11.79500  -22.41300 4.68000   1.000 17.19000  ? 20  TYR A CG   1 
ATOM   400  C  CD1  . TYR A 1 20  ? 12.69500  -21.45900 5.10300   1.000 23.37000  ? 20  TYR A CD1  1 
ATOM   401  C  CD2  . TYR A 1 20  ? 10.75500  -22.75500 5.52500   1.000 19.56000  ? 20  TYR A CD2  1 
ATOM   402  C  CE1  . TYR A 1 20  ? 12.56400  -20.85800 6.33000   1.000 25.77000  ? 20  TYR A CE1  1 
ATOM   403  C  CE2  . TYR A 1 20  ? 10.61700  -22.15900 6.75500   1.000 20.88000  ? 20  TYR A CE2  1 
ATOM   404  C  CZ   . TYR A 1 20  ? 11.53000  -21.21500 7.14700   1.000 24.46000  ? 20  TYR A CZ   1 
ATOM   405  O  OH   . TYR A 1 20  ? 11.39900  -20.62100 8.36500   1.000 30.20000  ? 20  TYR A OH   1 
ATOM   406  H  H    . TYR A 1 20  ? 12.59400  -24.46600 1.43300   1.000 22.21000  ? 20  TYR A H    1 
ATOM   407  H  HA   . TYR A 1 20  ? 13.71600  -24.02800 3.80800   1.000 19.62000  ? 20  TYR A HA   1 
ATOM   408  H  HB2  . TYR A 1 20  ? 12.30700  -22.41400 2.72600   1.000 21.01000  ? 20  TYR A HB2  1 
ATOM   409  H  HB3  . TYR A 1 20  ? 11.07100  -23.35500 3.04600   1.000 21.01000  ? 20  TYR A HB3  1 
ATOM   410  H  HD1  . TYR A 1 20  ? 13.39900  -21.22000 4.54500   1.000 28.04000  ? 20  TYR A HD1  1 
ATOM   411  H  HD2  . TYR A 1 20  ? 10.14300  -23.40200 5.25700   1.000 23.46000  ? 20  TYR A HD2  1 
ATOM   412  H  HE1  . TYR A 1 20  ? 13.17500  -20.21400 6.60400   1.000 30.91000  ? 20  TYR A HE1  1 
ATOM   413  H  HE2  . TYR A 1 20  ? 9.91400   -22.39900 7.31600   1.000 25.05000  ? 20  TYR A HE2  1 
ATOM   414  H  HH   . TYR A 1 20  ? 10.61000  -20.63100 8.59000   1.000 36.23000  ? 20  TYR A HH   1 
ATOM   415  N  N    A ARG A 1 21  ? 12.85600  -25.77000 5.26000   0.520 19.41000  ? 21  ARG A N    1 
ATOM   416  N  N    B ARG A 1 21  ? 12.75800  -25.82200 5.15100   0.480 19.46000  ? 21  ARG A N    1 
ATOM   417  C  CA   A ARG A 1 21  ? 12.43800  -26.93300 6.01700   0.520 21.08000  ? 21  ARG A CA   1 
ATOM   418  C  CA   B ARG A 1 21  ? 12.41500  -26.94600 5.98400   0.480 21.11000  ? 21  ARG A CA   1 
ATOM   419  C  C    A ARG A 1 21  ? 12.41800  -28.16500 5.13300   0.520 19.30000  ? 21  ARG A C    1 
ATOM   420  C  C    B ARG A 1 21  ? 12.42100  -28.20300 5.14800   0.480 19.29000  ? 21  ARG A C    1 
ATOM   421  O  O    A ARG A 1 21  ? 11.62400  -29.05900 5.38800   0.520 20.67000  ? 21  ARG A O    1 
ATOM   422  O  O    B ARG A 1 21  ? 11.61800  -29.11700 5.37900   0.480 20.79000  ? 21  ARG A O    1 
ATOM   423  C  CB   A ARG A 1 21  ? 11.06200  -26.72300 6.65700   0.520 19.19000  ? 21  ARG A CB   1 
ATOM   424  C  CB   B ARG A 1 21  ? 11.08700  -26.73900 6.71800   0.480 19.11000  ? 21  ARG A CB   1 
ATOM   425  C  CG   A ARG A 1 21  ? 10.98600  -25.54900 7.60300   0.520 32.42000  ? 21  ARG A CG   1 
ATOM   426  C  CG   B ARG A 1 21  ? 11.05600  -25.50000 7.60100   0.480 32.55000  ? 21  ARG A CG   1 
ATOM   427  C  CD   A ARG A 1 21  ? 11.10400  -26.05600 9.01800   0.520 37.93000  ? 21  ARG A CD   1 
ATOM   428  C  CD   B ARG A 1 21  ? 11.57900  -25.80100 8.99300   0.480 39.57000  ? 21  ARG A CD   1 
ATOM   429  N  NE   A ARG A 1 21  ? 11.19300  -24.97400 9.98500   0.520 49.92000  ? 21  ARG A NE   1 
ATOM   430  N  NE   B ARG A 1 21  ? 11.78600  -24.58800 9.77900   0.480 33.35000  ? 21  ARG A NE   1 
ATOM   431  C  CZ   A ARG A 1 21  ? 11.41100  -25.15300 11.28300  0.520 39.74000  ? 21  ARG A CZ   1 
ATOM   432  C  CZ   B ARG A 1 21  ? 12.96700  -24.02500 10.01000  0.480 36.93000  ? 21  ARG A CZ   1 
ATOM   433  N  NH1  A ARG A 1 21  ? 11.56300  -26.37000 11.78800  0.520 60.84000  ? 21  ARG A NH1  1 
ATOM   434  N  NH1  B ARG A 1 21  ? 14.08600  -24.53200 9.51900   0.480 49.78000  ? 21  ARG A NH1  1 
ATOM   435  N  NH2  A ARG A 1 21  ? 11.47700  -24.10400 12.08500  0.520 46.09000  ? 21  ARG A NH2  1 
ATOM   436  N  NH2  B ARG A 1 21  ? 13.02500  -22.92800 10.76000  0.480 41.84000  ? 21  ARG A NH2  1 
ATOM   437  H  H    A ARG A 1 21  ? 13.29400  -25.20100 5.73300   0.520 23.28000  ? 21  ARG A H    1 
ATOM   438  H  H    B ARG A 1 21  ? 13.40200  -25.35900 5.48400   0.480 23.34000  ? 21  ARG A H    1 
ATOM   439  H  HA   A ARG A 1 21  ? 13.07900  -27.09100 6.73900   0.520 25.28000  ? 21  ARG A HA   1 
ATOM   440  H  HA   B ARG A 1 21  ? 13.08000  -27.04200 6.68300   0.480 25.32000  ? 21  ARG A HA   1 
ATOM   441  H  HB2  A ARG A 1 21  ? 10.39900  -26.59200 5.96300   0.520 23.01000  ? 21  ARG A HB2  1 
ATOM   442  H  HB2  B ARG A 1 21  ? 10.37900  -26.65200 6.06000   0.480 22.92000  ? 21  ARG A HB2  1 
ATOM   443  H  HB3  A ARG A 1 21  ? 10.83800  -27.51000 7.17600   0.520 23.01000  ? 21  ARG A HB3  1 
ATOM   444  H  HB3  B ARG A 1 21  ? 10.92200  -27.51000 7.28300   0.480 22.92000  ? 21  ARG A HB3  1 
ATOM   445  H  HG2  A ARG A 1 21  ? 11.71800  -24.93800 7.42900   0.520 38.89000  ? 21  ARG A HG2  1 
ATOM   446  H  HG2  B ARG A 1 21  ? 11.61300  -24.81000 7.20800   0.480 39.05000  ? 21  ARG A HG2  1 
ATOM   447  H  HG3  A ARG A 1 21  ? 10.13300  -25.09700 7.50500   0.520 38.89000  ? 21  ARG A HG3  1 
ATOM   448  H  HG3  B ARG A 1 21  ? 10.14200  -25.18400 7.67900   0.480 39.05000  ? 21  ARG A HG3  1 
ATOM   449  H  HD2  A ARG A 1 21  ? 10.32000  -26.58500 9.23100   0.520 45.50000  ? 21  ARG A HD2  1 
ATOM   450  H  HD2  B ARG A 1 21  ? 10.93700  -26.35800 9.46100   0.480 47.47000  ? 21  ARG A HD2  1 
ATOM   451  H  HD3  A ARG A 1 21  ? 11.90400  -26.59800 9.08900   0.520 45.50000  ? 21  ARG A HD3  1 
ATOM   452  H  HD3  B ARG A 1 21  ? 12.42900  -26.26300 8.92000   0.480 47.47000  ? 21  ARG A HD3  1 
ATOM   453  H  HE   A ARG A 1 21  ? 10.78700  -24.13200 9.72400   0.520 59.89000  ? 21  ARG A HE   1 
ATOM   454  H  HE   B ARG A 1 21  ? 11.09200  -24.21000 10.11700  0.480 40.01000  ? 21  ARG A HE   1 
ATOM   455  H  HH11 A ARG A 1 21  ? 11.52400  -27.06500 11.28500  0.520 73.00000  ? 21  ARG A HH11 1 
ATOM   456  H  HH11 B ARG A 1 21  ? 14.06200  -25.24300 9.03700   0.480 59.72000  ? 21  ARG A HH11 1 
ATOM   457  H  HH12 A ARG A 1 21  ? 11.70200  -26.46500 12.63000  0.520 73.00000  ? 21  ARG A HH12 1 
ATOM   458  H  HH12 B ARG A 1 21  ? 14.83900  -24.14900 9.68300   0.480 59.72000  ? 21  ARG A HH12 1 
ATOM   459  H  HH21 A ARG A 1 21  ? 11.37600  -23.31400 11.76300  0.520 55.29000  ? 21  ARG A HH21 1 
ATOM   460  H  HH21 B ARG A 1 21  ? 12.30400  -22.59300 11.08800  0.480 50.19000  ? 21  ARG A HH21 1 
ATOM   461  H  HH22 A ARG A 1 21  ? 11.61500  -24.21400 12.92500  0.520 55.29000  ? 21  ARG A HH22 1 
ATOM   462  H  HH22 B ARG A 1 21  ? 13.78300  -22.55400 10.91700  0.480 50.19000  ? 21  ARG A HH22 1 
ATOM   463  N  N    . GLY A 1 22  ? 13.41600  -28.32200 4.25700   1.000 19.89000  ? 22  GLY A N    1 
ATOM   464  C  CA   . GLY A 1 22  ? 13.28200  -29.48100 3.40500   1.000 19.58000  ? 22  GLY A CA   1 
ATOM   465  C  C    . GLY A 1 22  ? 12.33800  -29.52200 2.20700   1.000 17.87000  ? 22  GLY A C    1 
ATOM   466  O  O    . GLY A 1 22  ? 12.36500  -30.52000 1.47300   1.000 17.95000  ? 22  GLY A O    1 
ATOM   467  H  H    . GLY A 1 22  ? 14.14200  -28.10700 4.42500   1.000 23.85000  ? 22  GLY A H    1 
ATOM   468  H  HA2  . GLY A 1 22  ? 14.16400  -29.66900 3.04800   1.000 23.48000  ? 22  GLY A HA2  1 
ATOM   469  H  HA3  . GLY A 1 22  ? 13.00900  -30.21700 3.97600   1.000 23.48000  ? 22  GLY A HA3  1 
ATOM   470  N  N    . TYR A 1 23  ? 11.52600  -28.50600 1.95300   1.000 15.44000  ? 23  TYR A N    1 
ATOM   471  C  CA   . TYR A 1 23  ? 10.52800  -28.55300 0.88100   1.000 13.73000  ? 23  TYR A CA   1 
ATOM   472  C  C    . TYR A 1 23  ? 11.08900  -27.83900 -0.34500  1.000 14.22000  ? 23  TYR A C    1 
ATOM   473  O  O    . TYR A 1 23  ? 11.15800  -26.60300 -0.37700  1.000 15.89000  ? 23  TYR A O    1 
ATOM   474  C  CB   . TYR A 1 23  ? 9.21000   -27.92200 1.34800   1.000 14.39000  ? 23  TYR A CB   1 
ATOM   475  C  CG   . TYR A 1 23  ? 8.52400   -28.76900 2.39200   1.000 13.47000  ? 23  TYR A CG   1 
ATOM   476  C  CD1  . TYR A 1 23  ? 7.68400   -29.80800 2.02700   1.000 14.10000  ? 23  TYR A CD1  1 
ATOM   477  C  CD2  . TYR A 1 23  ? 8.73400   -28.56000 3.74300   1.000 13.51000  ? 23  TYR A CD2  1 
ATOM   478  C  CE1  . TYR A 1 23  ? 7.07600   -30.59500 2.97600   1.000 13.35000  ? 23  TYR A CE1  1 
ATOM   479  C  CE2  . TYR A 1 23  ? 8.14600   -29.35700 4.69400   1.000 13.32000  ? 23  TYR A CE2  1 
ATOM   480  C  CZ   . TYR A 1 23  ? 7.29400   -30.37700 4.29400   1.000 12.73000  ? 23  TYR A CZ   1 
ATOM   481  O  OH   . TYR A 1 23  ? 6.64100   -31.18200 5.21000   1.000 15.45000  ? 23  TYR A OH   1 
ATOM   482  H  H    . TYR A 1 23  ? 11.53000  -27.76600 2.39100   1.000 18.52000  ? 23  TYR A H    1 
ATOM   483  H  HA   . TYR A 1 23  ? 10.35700  -29.47600 0.63600   1.000 16.46000  ? 23  TYR A HA   1 
ATOM   484  H  HB2  . TYR A 1 23  ? 9.39200   -27.05100 1.73400   1.000 17.25000  ? 23  TYR A HB2  1 
ATOM   485  H  HB3  . TYR A 1 23  ? 8.61300   -27.83100 0.58900   1.000 17.25000  ? 23  TYR A HB3  1 
ATOM   486  H  HD1  . TYR A 1 23  ? 7.52800   -29.97600 1.12500   1.000 16.91000  ? 23  TYR A HD1  1 
ATOM   487  H  HD2  . TYR A 1 23  ? 9.28700   -27.86300 4.01300   1.000 16.21000  ? 23  TYR A HD2  1 
ATOM   488  H  HE1  . TYR A 1 23  ? 6.51100   -31.28300 2.71100   1.000 16.01000  ? 23  TYR A HE1  1 
ATOM   489  H  HE2  . TYR A 1 23  ? 8.31700   -29.21500 5.59800   1.000 15.97000  ? 23  TYR A HE2  1 
ATOM   490  H  HH   . TYR A 1 23  ? 6.92600   -31.02400 5.98400   1.000 18.53000  ? 23  TYR A HH   1 
ATOM   491  N  N    . SER A 1 24  ? 11.43000  -28.61800 -1.36400  1.000 14.42000  ? 24  SER A N    1 
ATOM   492  C  CA   . SER A 1 24  ? 11.97800  -28.05700 -2.58700  1.000 15.41000  ? 24  SER A CA   1 
ATOM   493  C  C    . SER A 1 24  ? 10.94900  -27.13800 -3.23800  1.000 15.16000  ? 24  SER A C    1 
ATOM   494  O  O    . SER A 1 24  ? 9.73600   -27.24900 -3.01500  1.000 15.55000  ? 24  SER A O    1 
ATOM   495  C  CB   . SER A 1 24  ? 12.38600  -29.15400 -3.56400  1.000 17.40000  ? 24  SER A CB   1 
ATOM   496  O  OG   . SER A 1 24  ? 11.27200  -29.85100 -4.05300  1.000 20.96000  ? 24  SER A OG   1 
ATOM   497  H  H    . SER A 1 24  ? 11.35300  -29.47400 -1.37200  1.000 17.29000  ? 24  SER A H    1 
ATOM   498  H  HA   . SER A 1 24  ? 12.77500  -27.54500 -2.37800  1.000 18.47000  ? 24  SER A HA   1 
ATOM   499  H  HB2  . SER A 1 24  ? 12.85400  -28.74900 -4.31100  1.000 20.87000  ? 24  SER A HB2  1 
ATOM   500  H  HB3  . SER A 1 24  ? 12.96900  -29.77900 -3.10600  1.000 20.87000  ? 24  SER A HB3  1 
ATOM   501  H  HG   . SER A 1 24  ? 10.90700  -30.28200 -3.43100  1.000 25.14000  ? 24  SER A HG   1 
ATOM   502  N  N    . LEU A 1 25  ? 11.45100  -26.21100 -4.06100  1.000 13.96000  ? 25  LEU A N    1 
ATOM   503  C  CA   . LEU A 1 25  ? 10.62900  -25.17100 -4.65400  1.000 14.27000  ? 25  LEU A CA   1 
ATOM   504  C  C    . LEU A 1 25  ? 9.37600   -25.69400 -5.34300  1.000 14.02000  ? 25  LEU A C    1 
ATOM   505  O  O    . LEU A 1 25  ? 8.32500   -25.04900 -5.26300  1.000 13.85000  ? 25  LEU A O    1 
ATOM   506  C  CB   . LEU A 1 25  ? 11.49800  -24.38200 -5.63500  1.000 15.44000  ? 25  LEU A CB   1 
ATOM   507  C  CG   . LEU A 1 25  ? 10.94800  -23.06500 -6.14400  1.000 17.84000  ? 25  LEU A CG   1 
ATOM   508  C  CD1  . LEU A 1 25  ? 10.63200  -22.11000 -5.00000  1.000 21.79000  ? 25  LEU A CD1  1 
ATOM   509  C  CD2  . LEU A 1 25  ? 11.97400  -22.43900 -7.11600  1.000 18.51000  ? 25  LEU A CD2  1 
ATOM   510  H  H    . LEU A 1 25  ? 12.27800  -26.16800 -4.29200  1.000 16.75000  ? 25  LEU A H    1 
ATOM   511  H  HA   . LEU A 1 25  ? 10.31000  -24.59000 -3.94700  1.000 17.11000  ? 25  LEU A HA   1 
ATOM   512  H  HB2  . LEU A 1 25  ? 12.33900  -24.18400 -5.19500  1.000 18.52000  ? 25  LEU A HB2  1 
ATOM   513  H  HB3  . LEU A 1 25  ? 11.65300  -24.94100 -6.41200  1.000 18.52000  ? 25  LEU A HB3  1 
ATOM   514  H  HG   . LEU A 1 25  ? 10.11300  -23.22000 -6.61200  1.000 21.40000  ? 25  LEU A HG   1 
ATOM   515  H  HD11 . LEU A 1 25  ? 10.38600  -21.24700 -5.36800  1.000 26.14000  ? 25  LEU A HD11 1 
ATOM   516  H  HD12 . LEU A 1 25  ? 9.89600   -22.47100 -4.48200  1.000 26.14000  ? 25  LEU A HD12 1 
ATOM   517  H  HD13 . LEU A 1 25  ? 11.41800  -22.01800 -4.43900  1.000 26.14000  ? 25  LEU A HD13 1 
ATOM   518  H  HD21 . LEU A 1 25  ? 11.62100  -21.60000 -7.45200  1.000 22.20000  ? 25  LEU A HD21 1 
ATOM   519  H  HD22 . LEU A 1 25  ? 12.80500  -22.28100 -6.64100  1.000 22.20000  ? 25  LEU A HD22 1 
ATOM   520  H  HD23 . LEU A 1 25  ? 12.12600  -23.05200 -7.85300  1.000 22.20000  ? 25  LEU A HD23 1 
ATOM   521  N  N    . GLY A 1 26  ? 9.43900   -26.82100 -6.04700  1.000 14.27000  ? 26  GLY A N    1 
ATOM   522  C  CA   . GLY A 1 26  ? 8.26300   -27.31300 -6.76300  1.000 14.27000  ? 26  GLY A CA   1 
ATOM   523  C  C    . GLY A 1 26  ? 7.07200   -27.58200 -5.86300  1.000 13.45000  ? 26  GLY A C    1 
ATOM   524  O  O    . GLY A 1 26  ? 5.92300   -27.47300 -6.29600  1.000 13.01000  ? 26  GLY A O    1 
ATOM   525  H  H    . GLY A 1 26  ? 10.14000  -27.31300 -6.12700  1.000 17.11000  ? 26  GLY A H    1 
ATOM   526  H  HA2  . GLY A 1 26  ? 7.99700   -26.65600 -7.42400  1.000 17.11000  ? 26  GLY A HA2  1 
ATOM   527  H  HA3  . GLY A 1 26  ? 8.49100   -28.14100 -7.21400  1.000 17.11000  ? 26  GLY A HA3  1 
ATOM   528  N  N    . ASN A 1 27  ? 7.32300   -27.93100 -4.60600  1.000 12.69000  ? 27  ASN A N    1 
ATOM   529  C  CA   . ASN A 1 27  ? 6.23300   -28.12300 -3.65300  1.000 12.55000  ? 27  ASN A CA   1 
ATOM   530  C  C    . ASN A 1 27  ? 5.42700   -26.84800 -3.48100  1.000 11.55000  ? 27  ASN A C    1 
ATOM   531  O  O    . ASN A 1 27  ? 4.20000   -26.89200 -3.38100  1.000 13.57000  ? 27  ASN A O    1 
ATOM   532  C  CB   . ASN A 1 27  ? 6.77600   -28.52000 -2.28800  1.000 12.79000  ? 27  ASN A CB   1 
ATOM   533  C  CG   . ASN A 1 27  ? 7.23700   -29.94000 -2.24500  1.000 15.00000  ? 27  ASN A CG   1 
ATOM   534  O  OD1  . ASN A 1 27  ? 6.45200   -30.86700 -2.23200  1.000 14.95000  ? 27  ASN A OD1  1 
ATOM   535  N  ND2  . ASN A 1 27  ? 8.54800   -30.11800 -2.23100  1.000 15.02000  ? 27  ASN A ND2  1 
ATOM   536  H  H    . ASN A 1 27  ? 8.10800   -28.06300 -4.28100  1.000 15.22000  ? 27  ASN A H    1 
ATOM   537  H  HA   . ASN A 1 27  ? 5.66800   -28.83400 -3.99400  1.000 15.04000  ? 27  ASN A HA   1 
ATOM   538  H  HB2  . ASN A 1 27  ? 7.53100   -27.95200 -2.06900  1.000 15.34000  ? 27  ASN A HB2  1 
ATOM   539  H  HB3  . ASN A 1 27  ? 6.07600   -28.41200 -1.62500  1.000 15.34000  ? 27  ASN A HB3  1 
ATOM   540  H  HD21 . ASN A 1 27  ? 8.87400   -30.91300 -2.20600  1.000 18.01000  ? 27  ASN A HD21 1 
ATOM   541  H  HD22 . ASN A 1 27  ? 9.07400   -29.43800 -2.24500  1.000 18.01000  ? 27  ASN A HD22 1 
ATOM   542  N  N    . TRP A 1 28  ? 6.10700   -25.71200 -3.36900  1.000 12.67000  ? 28  TRP A N    1 
ATOM   543  C  CA   . TRP A 1 28  ? 5.45200   -24.43300 -3.12100  1.000 13.35000  ? 28  TRP A CA   1 
ATOM   544  C  C    . TRP A 1 28  ? 4.70700   -23.94200 -4.34600  1.000 13.70000  ? 28  TRP A C    1 
ATOM   545  O  O    . TRP A 1 28  ? 3.61800   -23.37700 -4.22900  1.000 13.94000  ? 28  TRP A O    1 
ATOM   546  C  CB   . TRP A 1 28  ? 6.50600   -23.39900 -2.69200  1.000 14.58000  ? 28  TRP A CB   1 
ATOM   547  C  CG   . TRP A 1 28  ? 7.21900   -23.77100 -1.40500  1.000 13.50000  ? 28  TRP A CG   1 
ATOM   548  C  CD1  . TRP A 1 28  ? 8.43400   -24.35600 -1.27000  1.000 14.19000  ? 28  TRP A CD1  1 
ATOM   549  C  CD2  . TRP A 1 28  ? 6.69300   -23.64200 -0.08400  1.000 13.21000  ? 28  TRP A CD2  1 
ATOM   550  N  NE1  . TRP A 1 28  ? 8.71400   -24.57200 0.05600   1.000 15.62000  ? 28  TRP A NE1  1 
ATOM   551  C  CE2  . TRP A 1 28  ? 7.65400   -24.13600 0.80800   1.000 14.97000  ? 28  TRP A CE2  1 
ATOM   552  C  CE3  . TRP A 1 28  ? 5.48700   -23.14000 0.42900   1.000 15.81000  ? 28  TRP A CE3  1 
ATOM   553  C  CZ2  . TRP A 1 28  ? 7.44500   -24.14100 2.20000   1.000 18.92000  ? 28  TRP A CZ2  1 
ATOM   554  C  CZ3  . TRP A 1 28  ? 5.29400   -23.14700 1.79000   1.000 18.98000  ? 28  TRP A CZ3  1 
ATOM   555  C  CH2  . TRP A 1 28  ? 6.26100   -23.63700 2.65800   1.000 19.22000  ? 28  TRP A CH2  1 
ATOM   556  H  H    . TRP A 1 28  ? 6.96300   -25.65200 -3.43300  1.000 15.19000  ? 28  TRP A H    1 
ATOM   557  H  HA   . TRP A 1 28  ? 4.80700   -24.54200 -2.40500  1.000 16.01000  ? 28  TRP A HA   1 
ATOM   558  H  HB2  . TRP A 1 28  ? 7.17300   -23.32200 -3.39200  1.000 17.49000  ? 28  TRP A HB2  1 
ATOM   559  H  HB3  . TRP A 1 28  ? 6.06900   -22.54400 -2.55500  1.000 17.49000  ? 28  TRP A HB3  1 
ATOM   560  H  HD1  . TRP A 1 28  ? 8.99800   -24.57900 -1.97500  1.000 17.02000  ? 28  TRP A HD1  1 
ATOM   561  H  HE1  . TRP A 1 28  ? 9.43500   -24.92400 0.36400   1.000 18.73000  ? 28  TRP A HE1  1 
ATOM   562  H  HE3  . TRP A 1 28  ? 4.83100   -22.81000 -0.14100  1.000 18.96000  ? 28  TRP A HE3  1 
ATOM   563  H  HZ2  . TRP A 1 28  ? 8.08700   -24.47500 2.78400   1.000 22.69000  ? 28  TRP A HZ2  1 
ATOM   564  H  HZ3  . TRP A 1 28  ? 4.49800   -22.81500 2.13800   1.000 22.76000  ? 28  TRP A HZ3  1 
ATOM   565  H  HH2  . TRP A 1 28  ? 6.09900   -23.62300 3.57300   1.000 23.05000  ? 28  TRP A HH2  1 
ATOM   566  N  N    . VAL A 1 29  ? 5.25400   -24.17500 -5.52900  1.000 12.70000  ? 29  VAL A N    1 
ATOM   567  C  CA   . VAL A 1 29  ? 4.58600   -23.80400 -6.76400  1.000 12.80000  ? 29  VAL A CA   1 
ATOM   568  C  C    . VAL A 1 29  ? 3.35300   -24.66000 -6.96800  1.000 14.57000  ? 29  VAL A C    1 
ATOM   569  O  O    . VAL A 1 29  ? 2.28000   -24.15300 -7.33900  1.000 13.69000  ? 29  VAL A O    1 
ATOM   570  C  CB   . VAL A 1 29  ? 5.56700   -23.88300 -7.95300  1.000 14.35000  ? 29  VAL A CB   1 
ATOM   571  C  CG1  . VAL A 1 29  ? 4.84000   -23.55800 -9.25800  1.000 16.04000  ? 29  VAL A CG1  1 
ATOM   572  C  CG2  . VAL A 1 29  ? 6.72400   -22.93500 -7.74200  1.000 16.53000  ? 29  VAL A CG2  1 
ATOM   573  H  H    . VAL A 1 29  ? 6.01900   -24.55000 -5.64500  1.000 15.23000  ? 29  VAL A H    1 
ATOM   574  H  HA   . VAL A 1 29  ? 4.29300   -22.88200 -6.69800  1.000 15.35000  ? 29  VAL A HA   1 
ATOM   575  H  HB   . VAL A 1 29  ? 5.92000   -24.78400 -8.01600  1.000 17.21000  ? 29  VAL A HB   1 
ATOM   576  H  HG11 . VAL A 1 29  ? 5.48300   -23.54900 -9.98400  1.000 19.23000  ? 29  VAL A HG11 1 
ATOM   577  H  HG12 . VAL A 1 29  ? 4.16700   -24.23700 -9.42200  1.000 19.23000  ? 29  VAL A HG12 1 
ATOM   578  H  HG13 . VAL A 1 29  ? 4.41900   -22.68800 -9.17700  1.000 19.23000  ? 29  VAL A HG13 1 
ATOM   579  H  HG21 . VAL A 1 29  ? 7.33400   -23.00900 -8.49200  1.000 19.83000  ? 29  VAL A HG21 1 
ATOM   580  H  HG22 . VAL A 1 29  ? 6.38200   -22.02900 -7.68200  1.000 19.83000  ? 29  VAL A HG22 1 
ATOM   581  H  HG23 . VAL A 1 29  ? 7.18000   -23.17100 -6.91900  1.000 19.83000  ? 29  VAL A HG23 1 
ATOM   582  N  N    . CYS A 1 30  ? 3.46300   -25.97000 -6.72400  1.000 13.25000  ? 30  CYS A N    1 
ATOM   583  C  CA   . CYS A 1 30  ? 2.32000   -26.85500 -6.84300  1.000 12.93000  ? 30  CYS A CA   1 
ATOM   584  C  C    . CYS A 1 30  ? 1.23100   -26.44400 -5.86700  1.000 13.38000  ? 30  CYS A C    1 
ATOM   585  O  O    . CYS A 1 30  ? 0.04900   -26.40100 -6.22900  1.000 12.65000  ? 30  CYS A O    1 
ATOM   586  C  CB   . CYS A 1 30  ? 2.81500   -28.28200 -6.57300  1.000 12.12000  ? 30  CYS A CB   1 
ATOM   587  S  SG   . CYS A 1 30  ? 1.55800   -29.58300 -6.73300  1.000 14.36000  ? 30  CYS A SG   1 
ATOM   588  H  H    . CYS A 1 30  ? 4.19000   -26.36400 -6.48800  1.000 15.89000  ? 30  CYS A H    1 
ATOM   589  H  HA   . CYS A 1 30  ? 1.93300   -26.82200 -7.73200  1.000 15.50000  ? 30  CYS A HA   1 
ATOM   590  H  HB2  . CYS A 1 30  ? 3.52400   -28.48500 -7.20400  1.000 14.54000  ? 30  CYS A HB2  1 
ATOM   591  H  HB3  . CYS A 1 30  ? 3.15800   -28.32000 -5.66600  1.000 14.54000  ? 30  CYS A HB3  1 
ATOM   592  N  N    . ALA A 1 31  ? 1.60200   -26.15500 -4.62900  1.000 12.95000  ? 31  ALA A N    1 
ATOM   593  C  CA   . ALA A 1 31  ? 0.59300   -25.72600 -3.66900  1.000 12.22000  ? 31  ALA A CA   1 
ATOM   594  C  C    . ALA A 1 31  ? -0.09000  -24.45400 -4.13800  1.000 11.98000  ? 31  ALA A C    1 
ATOM   595  O  O    . ALA A 1 31  ? -1.32700  -24.35300 -4.09200  1.000 14.14000  ? 31  ALA A O    1 
ATOM   596  C  CB   . ALA A 1 31  ? 1.21900   -25.51400 -2.30700  1.000 15.30000  ? 31  ALA A CB   1 
ATOM   597  H  H    . ALA A 1 31  ? 2.40600   -26.19700 -4.32700  1.000 15.53000  ? 31  ALA A H    1 
ATOM   598  H  HA   . ALA A 1 31  ? -0.07400  -26.42500 -3.58700  1.000 14.65000  ? 31  ALA A HA   1 
ATOM   599  H  HB1  . ALA A 1 31  ? 0.51800   -25.32100 -1.66400  1.000 18.34000  ? 31  ALA A HB1  1 
ATOM   600  H  HB2  . ALA A 1 31  ? 1.69300   -26.32000 -2.04800  1.000 18.34000  ? 31  ALA A HB2  1 
ATOM   601  H  HB3  . ALA A 1 31  ? 1.83700   -24.76800 -2.35500  1.000 18.34000  ? 31  ALA A HB3  1 
ATOM   602  N  N    . ALA A 1 32  ? 0.66700   -23.47300 -4.58800  1.000 12.25000  ? 32  ALA A N    1 
ATOM   603  C  CA   . ALA A 1 32  ? 0.04400   -22.22500 -5.03400  1.000 12.81000  ? 32  ALA A CA   1 
ATOM   604  C  C    . ALA A 1 32  ? -0.88800  -22.45800 -6.21700  1.000 13.77000  ? 32  ALA A C    1 
ATOM   605  O  O    . ALA A 1 32  ? -1.93100  -21.78800 -6.34000  1.000 13.76000  ? 32  ALA A O    1 
ATOM   606  C  CB   . ALA A 1 32  ? 1.11700   -21.19600 -5.35900  1.000 14.33000  ? 32  ALA A CB   1 
ATOM   607  H  H    . ALA A 1 32  ? 1.52500   -23.49500 -4.64700  1.000 14.69000  ? 32  ALA A H    1 
ATOM   608  H  HA   . ALA A 1 32  ? -0.49600  -21.86500 -4.31300  1.000 15.36000  ? 32  ALA A HA   1 
ATOM   609  H  HB1  . ALA A 1 32  ? 0.69000   -20.38200 -5.66900  1.000 17.18000  ? 32  ALA A HB1  1 
ATOM   610  H  HB2  . ALA A 1 32  ? 1.63200   -21.01400 -4.55700  1.000 17.18000  ? 32  ALA A HB2  1 
ATOM   611  H  HB3  . ALA A 1 32  ? 1.69600   -21.55100 -6.05100  1.000 17.18000  ? 32  ALA A HB3  1 
ATOM   612  N  N    . LYS A 1 33  ? -0.52700  -23.36500 -7.13000  1.000 12.19000  ? 33  LYS A N    1 
ATOM   613  C  CA   . LYS A 1 33  ? -1.37700  -23.60500 -8.28300  1.000 11.87000  ? 33  LYS A CA   1 
ATOM   614  C  C    . LYS A 1 33  ? -2.75700  -24.07400 -7.84500  1.000 12.58000  ? 33  LYS A C    1 
ATOM   615  O  O    . LYS A 1 33  ? -3.78500  -23.56400 -8.31700  1.000 14.68000  ? 33  LYS A O    1 
ATOM   616  C  CB   . LYS A 1 33  ? -0.74900  -24.65400 -9.20700  1.000 15.63000  ? 33  LYS A CB   1 
ATOM   617  C  CG   . LYS A 1 33  ? -1.61700  -25.04900 -10.39500 1.000 18.11000  ? 33  LYS A CG   1 
ATOM   618  C  CD   . LYS A 1 33  ? -1.71800  -23.96200 -11.41800 1.000 22.54000  ? 33  LYS A CD   1 
ATOM   619  C  CE   . LYS A 1 33  ? -2.57000  -24.41200 -12.59700 1.000 36.65000  ? 33  LYS A CE   1 
ATOM   620  N  NZ   . LYS A 1 33  ? -2.75100  -23.32300 -13.57900 1.000 37.74000  ? 33  LYS A NZ   1 
ATOM   621  H  H    . LYS A 1 33  ? 0.18800   -23.84000 -7.10000  1.000 14.61000  ? 33  LYS A H    1 
ATOM   622  H  HA   . LYS A 1 33  ? -1.46200  -22.77400 -8.77700  1.000 14.23000  ? 33  LYS A HA   1 
ATOM   623  H  HB2  . LYS A 1 33  ? 0.08300   -24.29900 -9.55700  1.000 18.74000  ? 33  LYS A HB2  1 
ATOM   624  H  HB3  . LYS A 1 33  ? -0.57700  -25.45700 -8.69000  1.000 18.74000  ? 33  LYS A HB3  1 
ATOM   625  H  HG2  . LYS A 1 33  ? -1.23300  -25.83000 -10.82200 1.000 21.72000  ? 33  LYS A HG2  1 
ATOM   626  H  HG3  . LYS A 1 33  ? -2.51300  -25.24900 -10.08000 1.000 21.72000  ? 33  LYS A HG3  1 
ATOM   627  H  HD2  . LYS A 1 33  ? -2.13000  -23.17900 -11.02100 1.000 27.03000  ? 33  LYS A HD2  1 
ATOM   628  H  HD3  . LYS A 1 33  ? -0.83200  -23.74100 -11.74400 1.000 27.03000  ? 33  LYS A HD3  1 
ATOM   629  H  HE2  . LYS A 1 33  ? -2.13400  -25.15500 -13.04300 1.000 43.96000  ? 33  LYS A HE2  1 
ATOM   630  H  HE3  . LYS A 1 33  ? -3.44400  -24.68300 -12.27700 1.000 43.96000  ? 33  LYS A HE3  1 
ATOM   631  H  HZ1  . LYS A 1 33  ? -3.31700  -22.71600 -13.25800 1.000 45.27000  ? 33  LYS A HZ1  1 
ATOM   632  H  HZ2  . LYS A 1 33  ? -1.97000  -22.93100 -13.74700 1.000 45.27000  ? 33  LYS A HZ2  1 
ATOM   633  H  HZ3  . LYS A 1 33  ? -3.07900  -23.65100 -14.33900 1.000 45.27000  ? 33  LYS A HZ3  1 
ATOM   634  N  N    . PHE A 1 34  ? -2.81100  -25.05400 -6.96000  1.000 12.48000  ? 34  PHE A N    1 
ATOM   635  C  CA   . PHE A 1 34  ? -4.09100  -25.63100 -6.57900  1.000 13.90000  ? 34  PHE A CA   1 
ATOM   636  C  C    . PHE A 1 34  ? -4.81900  -24.81700 -5.51800  1.000 15.17000  ? 34  PHE A C    1 
ATOM   637  O  O    . PHE A 1 34  ? -6.05000  -24.89300 -5.45200  1.000 18.00000  ? 34  PHE A O    1 
ATOM   638  C  CB   . PHE A 1 34  ? -3.89100  -27.07900 -6.21800  1.000 15.97000  ? 34  PHE A CB   1 
ATOM   639  C  CG   . PHE A 1 34  ? -3.42300  -27.90500 -7.38200  1.000 14.66000  ? 34  PHE A CG   1 
ATOM   640  C  CD1  . PHE A 1 34  ? -4.17100  -27.96000 -8.54200  1.000 16.18000  ? 34  PHE A CD1  1 
ATOM   641  C  CD2  . PHE A 1 34  ? -2.21600  -28.56600 -7.33800  1.000 17.63000  ? 34  PHE A CD2  1 
ATOM   642  C  CE1  . PHE A 1 34  ? -3.73000  -28.68900 -9.63400  1.000 18.51000  ? 34  PHE A CE1  1 
ATOM   643  C  CE2  . PHE A 1 34  ? -1.79400  -29.31500 -8.42300  1.000 25.12000  ? 34  PHE A CE2  1 
ATOM   644  C  CZ   . PHE A 1 34  ? -2.55300  -29.36300 -9.56000  1.000 18.37000  ? 34  PHE A CZ   1 
ATOM   645  H  H    . PHE A 1 34  ? -2.12800  -25.40200 -6.56800  1.000 14.97000  ? 34  PHE A H    1 
ATOM   646  H  HA   . PHE A 1 34  ? -4.70600  -25.63500 -7.33000  1.000 16.67000  ? 34  PHE A HA   1 
ATOM   647  H  HB2  . PHE A 1 34  ? -3.22300  -27.14200 -5.51700  1.000 19.15000  ? 34  PHE A HB2  1 
ATOM   648  H  HB3  . PHE A 1 34  ? -4.73300  -27.44700 -5.90700  1.000 19.15000  ? 34  PHE A HB3  1 
ATOM   649  H  HD1  . PHE A 1 34  ? -4.97900  -27.50300 -8.59100  1.000 19.41000  ? 34  PHE A HD1  1 
ATOM   650  H  HD2  . PHE A 1 34  ? -1.68300  -28.50800 -6.57800  1.000 21.15000  ? 34  PHE A HD2  1 
ATOM   651  H  HE1  . PHE A 1 34  ? -4.23700  -28.71700 -10.41300 1.000 22.20000  ? 34  PHE A HE1  1 
ATOM   652  H  HE2  . PHE A 1 34  ? -0.99300  -29.78700 -8.37800  1.000 30.13000  ? 34  PHE A HE2  1 
ATOM   653  H  HZ   . PHE A 1 34  ? -2.26100  -29.86200 -10.28900 1.000 22.03000  ? 34  PHE A HZ   1 
ATOM   654  N  N    . GLU A 1 35  ? -4.11800  -24.00600 -4.73800  1.000 12.49000  ? 35  GLU A N    1 
ATOM   655  C  CA   . GLU A 1 35  ? -4.77900  -23.13800 -3.76100  1.000 13.17000  ? 35  GLU A CA   1 
ATOM   656  C  C    . GLU A 1 35  ? -5.40300  -21.90600 -4.42300  1.000 14.39000  ? 35  GLU A C    1 
ATOM   657  O  O    . GLU A 1 35  ? -6.50800  -21.50700 -4.05600  1.000 15.31000  ? 35  GLU A O    1 
ATOM   658  C  CB   . GLU A 1 35  ? -3.77500  -22.69900 -2.70600  1.000 13.81000  ? 35  GLU A CB   1 
ATOM   659  C  CG   . GLU A 1 35  ? -3.30600  -23.79800 -1.78000  1.000 13.84000  ? 35  GLU A CG   1 
ATOM   660  C  CD   . GLU A 1 35  ? -4.34800  -24.28000 -0.80700  1.000 16.58000  ? 35  GLU A CD   1 
ATOM   661  O  OE1  . GLU A 1 35  ? -5.50700  -23.80100 -0.84400  1.000 17.21000  ? 35  GLU A OE1  1 
ATOM   662  O  OE2  . GLU A 1 35  ? -3.98800  -25.19300 -0.02900  1.000 18.52000  ? 35  GLU A OE2  1 
ATOM   663  H  H    . GLU A 1 35  ? -3.26100  -23.93600 -4.75000  1.000 14.97000  ? 35  GLU A H    1 
ATOM   664  H  HA   . GLU A 1 35  ? -5.48800  -23.64100 -3.33100  1.000 15.79000  ? 35  GLU A HA   1 
ATOM   665  H  HB2  . GLU A 1 35  ? -2.99300  -22.34300 -3.15500  1.000 16.56000  ? 35  GLU A HB2  1 
ATOM   666  H  HB3  . GLU A 1 35  ? -4.18500  -22.01200 -2.15800  1.000 16.56000  ? 35  GLU A HB3  1 
ATOM   667  H  HG2  . GLU A 1 35  ? -3.03200  -24.55800 -2.31600  1.000 16.60000  ? 35  GLU A HG2  1 
ATOM   668  H  HG3  . GLU A 1 35  ? -2.55400  -23.46700 -1.26400  1.000 16.60000  ? 35  GLU A HG3  1 
ATOM   669  N  N    . SER A 1 36  ? -4.71300  -21.27400 -5.37200  1.000 13.46000  ? 36  SER A N    1 
ATOM   670  C  CA   . SER A 1 36  ? -5.12100  -19.95800 -5.87100  1.000 13.47000  ? 36  SER A CA   1 
ATOM   671  C  C    . SER A 1 36  ? -5.02000  -19.79400 -7.37300  1.000 15.27000  ? 36  SER A C    1 
ATOM   672  O  O    . SER A 1 36  ? -5.35700  -18.70700 -7.87600  1.000 15.08000  ? 36  SER A O    1 
ATOM   673  C  CB   . SER A 1 36  ? -4.25100  -18.89000 -5.23600  1.000 13.41000  ? 36  SER A CB   1 
ATOM   674  O  OG   . SER A 1 36  ? -2.91600  -18.98000 -5.70200  1.000 14.61000  ? 36  SER A OG   1 
ATOM   675  H  H    . SER A 1 36  ? -4.00300  -21.58600 -5.74500  1.000 16.13000  ? 36  SER A H    1 
ATOM   676  H  HA   . SER A 1 36  ? -6.04900  -19.82200 -5.62300  1.000 16.15000  ? 36  SER A HA   1 
ATOM   677  H  HB2  . SER A 1 36  ? -4.60700  -18.01700 -5.46500  1.000 16.08000  ? 36  SER A HB2  1 
ATOM   678  H  HB3  . SER A 1 36  ? -4.25800  -19.01000 -4.27400  1.000 16.08000  ? 36  SER A HB3  1 
ATOM   679  H  HG   . SER A 1 36  ? -2.56500  -19.69400 -5.43300  1.000 17.52000  ? 36  SER A HG   1 
ATOM   680  N  N    . ASN A 1 37  ? -4.54100  -20.79600 -8.10800  1.000 13.94000  ? 37  ASN A N    1 
ATOM   681  C  CA   . ASN A 1 37  ? -4.24800  -20.64000 -9.53600  1.000 16.40000  ? 37  ASN A CA   1 
ATOM   682  C  C    . ASN A 1 37  ? -3.32300  -19.46500 -9.76100  1.000 15.71000  ? 37  ASN A C    1 
ATOM   683  O  O    . ASN A 1 37  ? -3.38900  -18.76800 -10.77800 1.000 16.64000  ? 37  ASN A O    1 
ATOM   684  C  CB   . ASN A 1 37  ? -5.50100  -20.51100 -10.40600 1.000 18.19000  ? 37  ASN A CB   1 
ATOM   685  C  CG   . ASN A 1 37  ? -5.28800  -21.02700 -11.79800 1.000 28.45000  ? 37  ASN A CG   1 
ATOM   686  O  OD1  . ASN A 1 37  ? -4.33000  -21.73600 -12.07500 1.000 26.55000  ? 37  ASN A OD1  1 
ATOM   687  N  ND2  . ASN A 1 37  ? -6.16500  -20.62300 -12.70500 1.000 32.62000  ? 37  ASN A ND2  1 
ATOM   688  H  H    . ASN A 1 37  ? -4.37500  -21.58200 -7.80200  1.000 16.72000  ? 37  ASN A H    1 
ATOM   689  H  HA   . ASN A 1 37  ? -3.80500  -21.45200 -9.82700  1.000 19.67000  ? 37  ASN A HA   1 
ATOM   690  H  HB2  . ASN A 1 37  ? -6.22000  -21.02100 -10.00300 1.000 21.82000  ? 37  ASN A HB2  1 
ATOM   691  H  HB3  . ASN A 1 37  ? -5.75000  -19.57600 -10.46700 1.000 21.82000  ? 37  ASN A HB3  1 
ATOM   692  H  HD21 . ASN A 1 37  ? -6.80700  -20.09700 -12.47900 1.000 39.14000  ? 37  ASN A HD21 1 
ATOM   693  H  HD22 . ASN A 1 37  ? -6.09300  -20.88700 -13.52100 1.000 39.14000  ? 37  ASN A HD22 1 
ATOM   694  N  N    . PHE A 1 38  ? -2.42600  -19.22700 -8.81800  1.000 13.93000  ? 38  PHE A N    1 
ATOM   695  C  CA   . PHE A 1 38  ? -1.38900  -18.21800 -8.91900  1.000 14.02000  ? 38  PHE A CA   1 
ATOM   696  C  C    . PHE A 1 38  ? -1.94800  -16.79100 -8.85600  1.000 12.61000  ? 38  PHE A C    1 
ATOM   697  O  O    . PHE A 1 38  ? -1.25700  -15.83000 -9.21400  1.000 14.90000  ? 38  PHE A O    1 
ATOM   698  C  CB   . PHE A 1 38  ? -0.51400  -18.34500 -10.18700 1.000 16.22000  ? 38  PHE A CB   1 
ATOM   699  C  CG   . PHE A 1 38  ? 0.19800   -19.67500 -10.37900 1.000 15.60000  ? 38  PHE A CG   1 
ATOM   700  C  CD1  . PHE A 1 38  ? 0.65900   -20.44400 -9.34200  1.000 16.96000  ? 38  PHE A CD1  1 
ATOM   701  C  CD2  . PHE A 1 38  ? 0.45900   -20.08700 -11.67400 1.000 19.29000  ? 38  PHE A CD2  1 
ATOM   702  C  CE1  . PHE A 1 38  ? 1.36600   -21.64400 -9.60400  1.000 16.62000  ? 38  PHE A CE1  1 
ATOM   703  C  CE2  . PHE A 1 38  ? 1.12900   -21.27500 -11.93300 1.000 19.33000  ? 38  PHE A CE2  1 
ATOM   704  C  CZ   . PHE A 1 38  ? 1.57900   -22.05000 -10.88500 1.000 14.95000  ? 38  PHE A CZ   1 
ATOM   705  H  H    . PHE A 1 38  ? -2.39800  -19.65900 -8.07500  1.000 16.71000  ? 38  PHE A H    1 
ATOM   706  H  HA   . PHE A 1 38  ? -0.80900  -18.36600 -8.15600  1.000 16.81000  ? 38  PHE A HA   1 
ATOM   707  H  HB2  . PHE A 1 38  ? -1.08200  -18.21100 -10.96200 1.000 19.45000  ? 38  PHE A HB2  1 
ATOM   708  H  HB3  . PHE A 1 38  ? 0.16900   -17.65800 -10.15400 1.000 19.45000  ? 38  PHE A HB3  1 
ATOM   709  H  HD1  . PHE A 1 38  ? 0.50800   -20.17700 -8.46400  1.000 20.34000  ? 38  PHE A HD1  1 
ATOM   710  H  HD2  . PHE A 1 38  ? 0.17900   -19.55800 -12.38500 1.000 23.13000  ? 38  PHE A HD2  1 
ATOM   711  H  HE1  . PHE A 1 38  ? 1.68600   -22.15700 -8.89700  1.000 19.94000  ? 38  PHE A HE1  1 
ATOM   712  H  HE2  . PHE A 1 38  ? 1.27500   -21.54600 -12.81100 1.000 23.18000  ? 38  PHE A HE2  1 
ATOM   713  H  HZ   . PHE A 1 38  ? 2.02600   -22.84800 -11.05300 1.000 17.93000  ? 38  PHE A HZ   1 
ATOM   714  N  N    . ASN A 1 39  ? -3.12600  -16.62500 -8.29200  1.000 13.99000  ? 39  ASN A N    1 
ATOM   715  C  CA   . ASN A 1 39  ? -3.78100  -15.31700 -8.17100  1.000 14.44000  ? 39  ASN A CA   1 
ATOM   716  C  C    . ASN A 1 39  ? -3.65100  -14.78400 -6.74900  1.000 12.34000  ? 39  ASN A C    1 
ATOM   717  O  O    . ASN A 1 39  ? -4.19400  -15.37700 -5.80100  1.000 13.90000  ? 39  ASN A O    1 
ATOM   718  C  CB   . ASN A 1 39  ? -5.24700  -15.48300 -8.53800  1.000 14.73000  ? 39  ASN A CB   1 
ATOM   719  C  CG   . ASN A 1 39  ? -6.01600  -14.18400 -8.54400  1.000 13.90000  ? 39  ASN A CG   1 
ATOM   720  O  OD1  . ASN A 1 39  ? -5.47900  -13.12200 -8.33200  1.000 14.74000  ? 39  ASN A OD1  1 
ATOM   721  N  ND2  . ASN A 1 39  ? -7.30500  -14.30500 -8.72100  1.000 20.80000  ? 39  ASN A ND2  1 
ATOM   722  H  H    . ASN A 1 39  ? -3.58900  -17.26900 -7.95800  1.000 16.77000  ? 39  ASN A H    1 
ATOM   723  H  HA   . ASN A 1 39  ? -3.34900  -14.67400 -8.75400  1.000 17.32000  ? 39  ASN A HA   1 
ATOM   724  H  HB2  . ASN A 1 39  ? -5.30700  -15.86700 -9.42700  1.000 17.66000  ? 39  ASN A HB2  1 
ATOM   725  H  HB3  . ASN A 1 39  ? -5.66700  -16.07300 -7.89200  1.000 17.66000  ? 39  ASN A HB3  1 
ATOM   726  H  HD21 . ASN A 1 39  ? -7.80500  -13.60500 -8.73600  1.000 24.94000  ? 39  ASN A HD21 1 
ATOM   727  H  HD22 . ASN A 1 39  ? -7.65400  -15.08500 -8.82400  1.000 24.94000  ? 39  ASN A HD22 1 
ATOM   728  N  N    . THR A 1 40  ? -2.97600  -13.64200 -6.57600  1.000 13.57000  ? 40  THR A N    1 
ATOM   729  C  CA   . THR A 1 40  ? -2.81000  -13.08400 -5.23900  1.000 13.40000  ? 40  THR A CA   1 
ATOM   730  C  C    . THR A 1 40  ? -4.12300  -12.61500 -4.62100  1.000 13.75000  ? 40  THR A C    1 
ATOM   731  O  O    . THR A 1 40  ? -4.19500  -12.49300 -3.39700  1.000 14.66000  ? 40  THR A O    1 
ATOM   732  C  CB   . THR A 1 40  ? -1.83100  -11.93200 -5.18000  1.000 15.28000  ? 40  THR A CB   1 
ATOM   733  O  OG1  . THR A 1 40  ? -2.36400  -10.82000 -5.90300  1.000 16.69000  ? 40  THR A OG1  1 
ATOM   734  C  CG2  . THR A 1 40  ? -0.47100  -12.29000 -5.74500  1.000 16.05000  ? 40  THR A CG2  1 
ATOM   735  H  H    . THR A 1 40  ? -2.61300  -13.18300 -7.20600  1.000 16.27000  ? 40  THR A H    1 
ATOM   736  H  HA   . THR A 1 40  ? -2.43300  -13.80500 -4.71100  1.000 16.07000  ? 40  THR A HA   1 
ATOM   737  H  HB   . THR A 1 40  ? -1.69600  -11.69800 -4.24800  1.000 18.33000  ? 40  THR A HB   1 
ATOM   738  H  HG1  . THR A 1 40  ? -2.11100  -10.10000 -5.55200  1.000 20.02000  ? 40  THR A HG1  1 
ATOM   739  H  HG21 . THR A 1 40  ? 0.15300   -11.56300 -5.59300  1.000 19.24000  ? 40  THR A HG21 1 
ATOM   740  H  HG22 . THR A 1 40  ? -0.13300  -13.09100 -5.31500  1.000 19.24000  ? 40  THR A HG22 1 
ATOM   741  H  HG23 . THR A 1 40  ? -0.54100  -12.45100 -6.69900  1.000 19.24000  ? 40  THR A HG23 1 
ATOM   742  N  N    A GLN A 1 41  ? -5.14500  -12.37500 -5.42500  0.510 13.18000  ? 41  GLN A N    1 
ATOM   743  N  N    B GLN A 1 41  ? -5.15400  -12.36900 -5.42400  0.490 13.27000  ? 41  GLN A N    1 
ATOM   744  C  CA   A GLN A 1 41  ? -6.40400  -11.84400 -4.90400  0.510 12.85000  ? 41  GLN A CA   1 
ATOM   745  C  CA   B GLN A 1 41  ? -6.43500  -11.85500 -4.92300  0.490 12.79000  ? 41  GLN A CA   1 
ATOM   746  C  C    A GLN A 1 41  ? -7.37100  -12.91500 -4.41500  0.510 14.07000  ? 41  GLN A C    1 
ATOM   747  C  C    B GLN A 1 41  ? -7.46300  -12.94600 -4.63100  0.490 13.64000  ? 41  GLN A C    1 
ATOM   748  O  O    A GLN A 1 41  ? -8.40200  -12.56500 -3.82100  0.510 14.14000  ? 41  GLN A O    1 
ATOM   749  O  O    B GLN A 1 41  ? -8.65600  -12.65700 -4.44900  0.490 14.01000  ? 41  GLN A O    1 
ATOM   750  C  CB   A GLN A 1 41  ? -7.10300  -10.96700 -5.95500  0.510 13.76000  ? 41  GLN A CB   1 
ATOM   751  C  CB   B GLN A 1 41  ? -7.02800  -10.83700 -5.90600  0.490 12.95000  ? 41  GLN A CB   1 
ATOM   752  C  CG   A GLN A 1 41  ? -6.33500  -9.71500  -6.30700  0.510 15.90000  ? 41  GLN A CG   1 
ATOM   753  C  CG   B GLN A 1 41  ? -6.16600  -9.61600  -6.14400  0.490 13.87000  ? 41  GLN A CG   1 
ATOM   754  C  CD   A GLN A 1 41  ? -7.18800  -8.69200  -7.00400  0.510 16.00000  ? 41  GLN A CD   1 
ATOM   755  C  CD   B GLN A 1 41  ? -6.92400  -8.52700  -6.85600  0.490 15.94000  ? 41  GLN A CD   1 
ATOM   756  O  OE1  A GLN A 1 41  ? -8.19200  -8.22700  -6.45400  0.510 13.22000  ? 41  GLN A OE1  1 
ATOM   757  O  OE1  B GLN A 1 41  ? -7.52200  -7.67700  -6.20800  0.490 16.72000  ? 41  GLN A OE1  1 
ATOM   758  N  NE2  A GLN A 1 41  ? -6.78900  -8.31400  -8.21500  0.510 16.09000  ? 41  GLN A NE2  1 
ATOM   759  N  NE2  B GLN A 1 41  ? -6.94400  -8.56800  -8.19600  0.490 15.38000  ? 41  GLN A NE2  1 
ATOM   760  H  H    A GLN A 1 41  ? -5.14000  -12.51000 -6.27500  0.510 15.80000  ? 41  GLN A H    1 
ATOM   761  H  H    B GLN A 1 41  ? -5.14000  -12.49300 -6.27500  0.490 15.91000  ? 41  GLN A H    1 
ATOM   762  H  HA   A GLN A 1 41  ? -6.19100  -11.28000 -4.14400  0.510 15.41000  ? 41  GLN A HA   1 
ATOM   763  H  HA   B GLN A 1 41  ? -6.25600  -11.39500 -4.08700  0.490 15.34000  ? 41  GLN A HA   1 
ATOM   764  H  HB2  A GLN A 1 41  ? -7.21600  -11.48400 -6.76800  0.510 16.50000  ? 41  GLN A HB2  1 
ATOM   765  H  HB2  B GLN A 1 41  ? -7.15900  -11.27500 -6.76100  0.490 15.52000  ? 41  GLN A HB2  1 
ATOM   766  H  HB3  A GLN A 1 41  ? -7.96800  -10.69600 -5.61100  0.510 16.50000  ? 41  GLN A HB3  1 
ATOM   767  H  HB3  B GLN A 1 41  ? -7.87900  -10.53100 -5.55600  0.490 15.52000  ? 41  GLN A HB3  1 
ATOM   768  H  HG2  A GLN A 1 41  ? -5.99000  -9.31600  -5.49300  0.510 19.07000  ? 41  GLN A HG2  1 
ATOM   769  H  HG2  B GLN A 1 41  ? -5.86200  -9.26700  -5.29100  0.490 16.63000  ? 41  GLN A HG2  1 
ATOM   770  H  HG3  A GLN A 1 41  ? -5.60200  -9.94900  -6.89800  0.510 19.07000  ? 41  GLN A HG3  1 
ATOM   771  H  HG3  B GLN A 1 41  ? -5.40400  -9.86400  -6.69100  0.490 16.63000  ? 41  GLN A HG3  1 
ATOM   772  H  HE21 A GLN A 1 41  ? -7.24400  -7.73100  -8.65500  0.510 19.29000  ? 41  GLN A HE21 1 
ATOM   773  H  HE21 B GLN A 1 41  ? -7.36700  -7.96400  -8.63800  0.490 18.44000  ? 41  GLN A HE21 1 
ATOM   774  H  HE22 A GLN A 1 41  ? -6.07800  -8.65300  -8.55900  0.510 19.29000  ? 41  GLN A HE22 1 
ATOM   775  H  HE22 B GLN A 1 41  ? -6.53500  -9.19900  -8.61300  0.490 18.44000  ? 41  GLN A HE22 1 
ATOM   776  N  N    . ALA A 1 42  ? -7.05200  -14.19900 -4.60100  1.000 12.52000  ? 42  ALA A N    1 
ATOM   777  C  CA   . ALA A 1 42  ? -7.96300  -15.27800 -4.26700  1.000 12.73000  ? 42  ALA A CA   1 
ATOM   778  C  C    . ALA A 1 42  ? -8.39400  -15.25800 -2.80200  1.000 12.98000  ? 42  ALA A C    1 
ATOM   779  O  O    . ALA A 1 42  ? -7.59100  -15.09100 -1.90000  1.000 13.66000  ? 42  ALA A O    1 
ATOM   780  C  CB   . ALA A 1 42  ? -7.27000  -16.60600 -4.56300  1.000 15.67000  ? 42  ALA A CB   1 
ATOM   781  H  H    . ALA A 1 42  ? -6.30100  -14.46700 -4.92400  1.000 15.02000  ? 42  ALA A H    1 
ATOM   782  H  HA   . ALA A 1 42  ? -8.76900  -15.18000 -4.79800  1.000 15.26000  ? 42  ALA A HA   1 
ATOM   783  H  HB1  . ALA A 1 42  ? -7.90600  -17.32800 -4.44300  1.000 18.79000  ? 42  ALA A HB1  1 
ATOM   784  H  HB2  . ALA A 1 42  ? -6.94700  -16.59700 -5.47800  1.000 18.79000  ? 42  ALA A HB2  1 
ATOM   785  H  HB3  . ALA A 1 42  ? -6.52500  -16.71600 -3.95100  1.000 18.79000  ? 42  ALA A HB3  1 
ATOM   786  N  N    . THR A 1 43  ? -9.69500  -15.44700 -2.58600  1.000 14.04000  ? 43  THR A N    1 
ATOM   787  C  CA   . THR A 1 43  ? -10.29300 -15.57400 -1.26000  1.000 14.73000  ? 43  THR A CA   1 
ATOM   788  C  C    . THR A 1 43  ? -11.30300 -16.70000 -1.32500  1.000 15.85000  ? 43  THR A C    1 
ATOM   789  O  O    . THR A 1 43  ? -11.96000 -16.89000 -2.34800  1.000 18.46000  ? 43  THR A O    1 
ATOM   790  C  CB   . THR A 1 43  ? -10.98900 -14.31300 -0.77600  1.000 16.33000  ? 43  THR A CB   1 
ATOM   791  O  OG1  . THR A 1 43  ? -12.06400 -13.99000 -1.66800  1.000 18.28000  ? 43  THR A OG1  1 
ATOM   792  C  CG2  . THR A 1 43  ? -10.04900 -13.15700 -0.69700  1.000 18.42000  ? 43  THR A CG2  1 
ATOM   793  H  H    . THR A 1 43  ? -10.27500 -15.50700 -3.21800  1.000 16.84000  ? 43  THR A H    1 
ATOM   794  H  HA   . THR A 1 43  ? -9.59500  -15.76900 -0.61600  1.000 17.66000  ? 43  THR A HA   1 
ATOM   795  H  HB   . THR A 1 43  ? -11.33300 -14.46900 0.11700   1.000 19.59000  ? 43  THR A HB   1 
ATOM   796  H  HG1  . THR A 1 43  ? -12.07900 -13.16200 -1.81200  1.000 21.93000  ? 43  THR A HG1  1 
ATOM   797  H  HG21 . THR A 1 43  ? -10.51600 -12.37200 -0.37100  1.000 22.09000  ? 43  THR A HG21 1 
ATOM   798  H  HG22 . THR A 1 43  ? -9.32000  -13.36400 -0.09100  1.000 22.09000  ? 43  THR A HG22 1 
ATOM   799  H  HG23 . THR A 1 43  ? -9.68500  -12.96600 -1.57500  1.000 22.09000  ? 43  THR A HG23 1 
ATOM   800  N  N    A ASN A 1 44  ? -11.45400 -17.43400 -0.22000  0.560 13.98000  ? 44  ASN A N    1 
ATOM   801  N  N    B ASN A 1 44  ? -11.41300 -17.46900 -0.24500  0.440 14.03000  ? 44  ASN A N    1 
ATOM   802  C  CA   A ASN A 1 44  ? -12.39600 -18.54400 -0.16500  0.560 13.64000  ? 44  ASN A CA   1 
ATOM   803  C  CA   B ASN A 1 44  ? -12.43000 -18.50200 -0.13400  0.440 13.56000  ? 44  ASN A CA   1 
ATOM   804  C  C    A ASN A 1 44  ? -12.83800 -18.78000 1.26600   0.560 14.67000  ? 44  ASN A C    1 
ATOM   805  C  C    B ASN A 1 44  ? -12.89300 -18.57000 1.31000   0.440 13.83000  ? 44  ASN A C    1 
ATOM   806  O  O    A ASN A 1 44  ? -12.00100 -18.84900 2.16400   0.560 13.71000  ? 44  ASN A O    1 
ATOM   807  O  O    B ASN A 1 44  ? -12.14900 -18.22900 2.22500   0.440 14.33000  ? 44  ASN A O    1 
ATOM   808  C  CB   A ASN A 1 44  ? -11.75400 -19.81200 -0.73100  0.560 15.52000  ? 44  ASN A CB   1 
ATOM   809  C  CB   B ASN A 1 44  ? -11.90400 -19.86900 -0.58900  0.440 15.15000  ? 44  ASN A CB   1 
ATOM   810  C  CG   A ASN A 1 44  ? -11.65300 -19.77200 -2.23200  0.560 16.41000  ? 44  ASN A CG   1 
ATOM   811  C  CG   B ASN A 1 44  ? -12.96500 -20.69500 -1.28800  0.440 32.63000  ? 44  ASN A CG   1 
ATOM   812  O  OD1  A ASN A 1 44  ? -12.67200 -19.78400 -2.93000  0.560 17.16000  ? 44  ASN A OD1  1 
ATOM   813  O  OD1  B ASN A 1 44  ? -13.69500 -21.45200 -0.65600  0.440 33.80000  ? 44  ASN A OD1  1 
ATOM   814  N  ND2  A ASN A 1 44  ? -10.43600 -19.65000 -2.74200  0.560 15.96000  ? 44  ASN A ND2  1 
ATOM   815  N  ND2  B ASN A 1 44  ? -13.05900 -20.54200 -2.60300  0.440 28.58000  ? 44  ASN A ND2  1 
ATOM   816  H  H    A ASN A 1 44  ? -11.01900 -17.30500 0.51100   0.560 16.76000  ? 44  ASN A H    1 
ATOM   817  H  H    B ASN A 1 44  ? -10.90300 -17.40800 0.44400   0.440 16.82000  ? 44  ASN A H    1 
ATOM   818  H  HA   A ASN A 1 44  ? -13.18600 -18.32000 -0.68200  0.560 16.36000  ? 44  ASN A HA   1 
ATOM   819  H  HA   B ASN A 1 44  ? -13.19200 -18.28100 -0.69200  0.440 16.26000  ? 44  ASN A HA   1 
ATOM   820  H  HB2  A ASN A 1 44  ? -10.85900 -19.90500 -0.36900  0.560 18.61000  ? 44  ASN A HB2  1 
ATOM   821  H  HB2  B ASN A 1 44  ? -11.16900 -19.73600 -1.20900  0.440 18.17000  ? 44  ASN A HB2  1 
ATOM   822  H  HB3  A ASN A 1 44  ? -12.29300 -20.58000 -0.48400  0.560 18.61000  ? 44  ASN A HB3  1 
ATOM   823  H  HB3  B ASN A 1 44  ? -11.59800 -20.36500 0.18600   0.440 18.17000  ? 44  ASN A HB3  1 
ATOM   824  H  HD21 A ASN A 1 44  ? -9.75400  -19.59900 -2.21900  0.560 19.14000  ? 44  ASN A HD21 1 
ATOM   825  H  HD21 B ASN A 1 44  ? -12.53400 -19.99600 -3.01100  0.440 34.28000  ? 44  ASN A HD21 1 
ATOM   826  H  HD22 A ASN A 1 44  ? -10.32700 -19.62300 -3.59400  0.560 19.14000  ? 44  ASN A HD22 1 
ATOM   827  H  HD22 B ASN A 1 44  ? -13.64600 -20.98800 -3.04700  0.440 34.28000  ? 44  ASN A HD22 1 
ATOM   828  N  N    A ARG A 1 45  ? -14.14400 -18.93900 1.45500   0.560 17.85000  ? 45  ARG A N    1 
ATOM   829  N  N    B ARG A 1 45  ? -14.13600 -18.99700 1.50000   0.440 17.96000  ? 45  ARG A N    1 
ATOM   830  C  CA   A ARG A 1 45  ? -14.70800 -19.15400 2.77800   0.560 19.16000  ? 45  ARG A CA   1 
ATOM   831  C  CA   B ARG A 1 45  ? -14.73400 -19.10700 2.82400   0.440 18.92000  ? 45  ARG A CA   1 
ATOM   832  C  C    A ARG A 1 45  ? -14.60700 -20.62100 3.17300   0.560 19.73000  ? 45  ARG A C    1 
ATOM   833  C  C    B ARG A 1 45  ? -14.78700 -20.57200 3.22800   0.440 19.94000  ? 45  ARG A C    1 
ATOM   834  O  O    A ARG A 1 45  ? -14.75000 -21.52500 2.34400   0.560 23.12000  ? 45  ARG A O    1 
ATOM   835  O  O    B ARG A 1 45  ? -15.27000 -21.41300 2.46300   0.440 19.11000  ? 45  ARG A O    1 
ATOM   836  C  CB   A ARG A 1 45  ? -16.17800 -18.73700 2.77700   0.560 20.87000  ? 45  ARG A CB   1 
ATOM   837  C  CB   B ARG A 1 45  ? -16.15400 -18.54500 2.82400   0.440 20.53000  ? 45  ARG A CB   1 
ATOM   838  C  CG   A ARG A 1 45  ? -16.81000 -18.79100 4.14700   0.560 27.54000  ? 45  ARG A CG   1 
ATOM   839  C  CG   B ARG A 1 45  ? -16.77200 -18.49300 4.21300   0.440 24.26000  ? 45  ARG A CG   1 
ATOM   840  C  CD   A ARG A 1 45  ? -16.33500 -17.63500 4.98000   0.560 27.97000  ? 45  ARG A CD   1 
ATOM   841  C  CD   B ARG A 1 45  ? -16.31200 -17.28600 4.98100   0.440 30.64000  ? 45  ARG A CD   1 
ATOM   842  N  NE   A ARG A 1 45  ? -16.70000 -16.36700 4.36700   0.560 35.35000  ? 45  ARG A NE   1 
ATOM   843  N  NE   B ARG A 1 45  ? -16.58500 -16.07400 4.22900   0.440 36.78000  ? 45  ARG A NE   1 
ATOM   844  C  CZ   A ARG A 1 45  ? -17.58800 -15.50800 4.85400   0.560 43.16000  ? 45  ARG A CZ   1 
ATOM   845  C  CZ   B ARG A 1 45  ? -17.80400 -15.62700 3.96400   0.440 33.00000  ? 45  ARG A CZ   1 
ATOM   846  N  NH1  A ARG A 1 45  ? -18.11800 -15.66200 6.05800   0.560 38.12000  ? 45  ARG A NH1  1 
ATOM   847  N  NH1  B ARG A 1 45  ? -18.88000 -16.20900 4.47000   0.440 32.16000  ? 45  ARG A NH1  1 
ATOM   848  N  NH2  A ARG A 1 45  ? -17.94300 -14.46000 4.11900   0.560 36.29000  ? 45  ARG A NH2  1 
ATOM   849  N  NH2  B ARG A 1 45  ? -17.94700 -14.57500 3.16900   0.440 30.80000  ? 45  ARG A NH2  1 
ATOM   850  H  H    A ARG A 1 45  ? -14.73000 -18.92500 0.82600   0.560 21.41000  ? 45  ARG A H    1 
ATOM   851  H  H    B ARG A 1 45  ? -14.66400 -19.23400 0.86400   0.440 21.54000  ? 45  ARG A H    1 
ATOM   852  H  HA   A ARG A 1 45  ? -14.22100 -18.62600 3.43000   0.560 22.98000  ? 45  ARG A HA   1 
ATOM   853  H  HA   B ARG A 1 45  ? -14.19400 -18.61300 3.46100   0.440 22.69000  ? 45  ARG A HA   1 
ATOM   854  H  HB2  A ARG A 1 45  ? -16.24600 -17.82600 2.45200   0.560 25.04000  ? 45  ARG A HB2  1 
ATOM   855  H  HB2  B ARG A 1 45  ? -16.13500 -17.64100 2.47100   0.440 24.62000  ? 45  ARG A HB2  1 
ATOM   856  H  HB3  A ARG A 1 45  ? -16.67300 -19.33500 2.19600   0.560 25.04000  ? 45  ARG A HB3  1 
ATOM   857  H  HB3  B ARG A 1 45  ? -16.71500 -19.10700 2.26700   0.440 24.62000  ? 45  ARG A HB3  1 
ATOM   858  H  HG2  A ARG A 1 45  ? -17.77500 -18.73900 4.06400   0.560 33.03000  ? 45  ARG A HG2  1 
ATOM   859  H  HG2  B ARG A 1 45  ? -17.73800 -18.45200 4.13300   0.440 29.10000  ? 45  ARG A HG2  1 
ATOM   860  H  HG3  A ARG A 1 45  ? -16.55900 -19.61700 4.59000   0.560 33.03000  ? 45  ARG A HG3  1 
ATOM   861  H  HG3  B ARG A 1 45  ? -16.51400 -19.28600 4.70900   0.440 29.10000  ? 45  ARG A HG3  1 
ATOM   862  H  HD2  A ARG A 1 45  ? -16.74400 -17.68000 5.85900   0.560 33.55000  ? 45  ARG A HD2  1 
ATOM   863  H  HD2  B ARG A 1 45  ? -16.78300 -17.23900 5.82700   0.440 36.76000  ? 45  ARG A HD2  1 
ATOM   864  H  HD3  A ARG A 1 45  ? -15.36900 -17.67000 5.06100   0.560 33.55000  ? 45  ARG A HD3  1 
ATOM   865  H  HD3  B ARG A 1 45  ? -15.35600 -17.34500 5.13700   0.440 36.76000  ? 45  ARG A HD3  1 
ATOM   866  H  HE   A ARG A 1 45  ? -16.31100 -16.15700 3.62900   0.560 42.40000  ? 45  ARG A HE   1 
ATOM   867  H  HE   B ARG A 1 45  ? -15.91600 -15.62000 3.93700   0.440 44.12000  ? 45  ARG A HE   1 
ATOM   868  H  HH11 A ARG A 1 45  ? -17.89000 -16.33200 6.54600   0.560 45.74000  ? 45  ARG A HH11 1 
ATOM   869  H  HH11 B ARG A 1 45  ? -18.79600 -16.89500 4.98300   0.440 38.58000  ? 45  ARG A HH11 1 
ATOM   870  H  HH12 A ARG A 1 45  ? -18.69100 -15.09200 6.35100   0.560 45.74000  ? 45  ARG A HH12 1 
ATOM   871  H  HH12 B ARG A 1 45  ? -19.66200 -15.90300 4.28500   0.440 38.58000  ? 45  ARG A HH12 1 
ATOM   872  H  HH21 A ARG A 1 45  ? -17.59900 -14.34600 3.33900   0.560 43.54000  ? 45  ARG A HH21 1 
ATOM   873  H  HH21 B ARG A 1 45  ? -17.25400 -14.19300 2.83300   0.440 36.94000  ? 45  ARG A HH21 1 
ATOM   874  H  HH22 A ARG A 1 45  ? -18.51600 -13.89600 4.42300   0.560 43.54000  ? 45  ARG A HH22 1 
ATOM   875  H  HH22 B ARG A 1 45  ? -18.73300 -14.27500 2.99000   0.440 36.94000  ? 45  ARG A HH22 1 
ATOM   876  N  N    . ASN A 1 46  ? -14.35500 -20.85500 4.45300   1.000 17.02000  ? 46  ASN A N    1 
ATOM   877  C  CA   . ASN A 1 46  ? -14.35700 -22.20100 5.02400   1.000 19.80000  ? 46  ASN A CA   1 
ATOM   878  C  C    . ASN A 1 46  ? -15.67300 -22.44100 5.76800   1.000 18.60000  ? 46  ASN A C    1 
ATOM   879  O  O    . ASN A 1 46  ? -16.37400 -21.51100 6.14800   1.000 21.27000  ? 46  ASN A O    1 
ATOM   880  C  CB   . ASN A 1 46  ? -13.21400 -22.36400 6.03700   1.000 21.66000  ? 46  ASN A CB   1 
ATOM   881  C  CG   . ASN A 1 46  ? -11.84100 -22.05700 5.44400   1.000 20.99000  ? 46  ASN A CG   1 
ATOM   882  O  OD1  . ASN A 1 46  ? -11.02400 -21.32700 6.04500   1.000 21.85000  ? 46  ASN A OD1  1 
ATOM   883  N  ND2  . ASN A 1 46  ? -11.57600 -22.61000 4.28600   1.000 21.74000  ? 46  ASN A ND2  1 
ATOM   884  H  H    . ASN A 1 46  ? -14.17700 -20.23800 5.02600   1.000 20.42000  ? 46  ASN A H    1 
ATOM   885  H  HA   . ASN A 1 46  ? -14.24700 -22.84700 4.30900   1.000 23.75000  ? 46  ASN A HA   1 
ATOM   886  H  HB2  . ASN A 1 46  ? -13.36200 -21.75800 6.77900   1.000 25.98000  ? 46  ASN A HB2  1 
ATOM   887  H  HB3  . ASN A 1 46  ? -13.20400 -23.28100 6.35500   1.000 25.98000  ? 46  ASN A HB3  1 
ATOM   888  H  HD21 . ASN A 1 46  ? -10.81700 -22.47000 3.90600   1.000 26.08000  ? 46  ASN A HD21 1 
ATOM   889  H  HD22 . ASN A 1 46  ? -12.16200 -23.11200 3.90600   1.000 26.08000  ? 46  ASN A HD22 1 
ATOM   890  N  N    . THR A 1 47  ? -15.95600 -23.71600 6.04800   1.000 24.14000  ? 47  THR A N    1 
ATOM   891  C  CA   . THR A 1 47  ? -17.25000 -24.04800 6.63800   1.000 26.59000  ? 47  THR A CA   1 
ATOM   892  C  C    . THR A 1 47  ? -17.41400 -23.45700 8.03600   1.000 25.18000  ? 47  THR A C    1 
ATOM   893  O  O    . THR A 1 47  ? -18.54300 -23.14300 8.44700   1.000 31.09000  ? 47  THR A O    1 
ATOM   894  C  CB   . THR A 1 47  ? -17.46200 -25.56800 6.65400   1.000 29.95000  ? 47  THR A CB   1 
ATOM   895  O  OG1  . THR A 1 47  ? -16.43900 -26.20300 7.42100   1.000 34.02000  ? 47  THR A OG1  1 
ATOM   896  C  CG2  . THR A 1 47  ? -17.40100 -26.13300 5.25000   1.000 29.97000  ? 47  THR A CG2  1 
ATOM   897  H  H    . THR A 1 47  ? -15.43300 -24.38400 5.91100   1.000 28.96000  ? 47  THR A H    1 
ATOM   898  H  HA   . THR A 1 47  ? -17.94600 -23.66500 6.08100   1.000 31.89000  ? 47  THR A HA   1 
ATOM   899  H  HB   . THR A 1 47  ? -18.33300 -25.75000 7.04100   1.000 35.93000  ? 47  THR A HB   1 
ATOM   900  H  HG1  . THR A 1 47  ? -16.27200 -26.96300 7.10400   1.000 40.82000  ? 47  THR A HG1  1 
ATOM   901  H  HG21 . THR A 1 47  ? -17.51400 -27.09600 5.27500   1.000 35.95000  ? 47  THR A HG21 1 
ATOM   902  H  HG22 . THR A 1 47  ? -18.10700 -25.74800 4.70700   1.000 35.95000  ? 47  THR A HG22 1 
ATOM   903  H  HG23 . THR A 1 47  ? -16.54400 -25.92600 4.84600   1.000 35.95000  ? 47  THR A HG23 1 
ATOM   904  N  N    A ASP A 1 48  ? -16.31100 -23.30100 8.77300   0.710 22.00000  ? 48  ASP A N    1 
ATOM   905  N  N    B ASP A 1 48  ? -16.32400 -23.28700 8.77500   0.290 22.20000  ? 48  ASP A N    1 
ATOM   906  C  CA   A ASP A 1 48  ? -16.35400 -22.76400 10.13300  0.710 23.27000  ? 48  ASP A CA   1 
ATOM   907  C  CA   B ASP A 1 48  ? -16.41200 -22.76100 10.13300  0.290 23.50000  ? 48  ASP A CA   1 
ATOM   908  C  C    A ASP A 1 48  ? -16.50700 -21.24400 10.19600  0.710 22.06000  ? 48  ASP A C    1 
ATOM   909  C  C    B ASP A 1 48  ? -16.53600 -21.24100 10.19300  0.290 22.25000  ? 48  ASP A C    1 
ATOM   910  O  O    A ASP A 1 48  ? -16.55600 -20.68300 11.29700  0.710 27.93000  ? 48  ASP A O    1 
ATOM   911  O  O    B ASP A 1 48  ? -16.58600 -20.68600 11.29600  0.290 27.87000  ? 48  ASP A O    1 
ATOM   912  C  CB   A ASP A 1 48  ? -15.13200 -23.24900 10.92900  0.710 22.41000  ? 48  ASP A CB   1 
ATOM   913  C  CB   B ASP A 1 48  ? -15.19300 -23.20700 10.93300  0.290 22.59000  ? 48  ASP A CB   1 
ATOM   914  C  CG   A ASP A 1 48  ? -13.83000 -22.59100 10.49600  0.710 23.99000  ? 48  ASP A CG   1 
ATOM   915  C  CG   B ASP A 1 48  ? -13.90600 -22.74300 10.31100  0.290 24.54000  ? 48  ASP A CG   1 
ATOM   916  O  OD1  A ASP A 1 48  ? -13.83700 -21.84000 9.50100   0.710 22.41000  ? 48  ASP A OD1  1 
ATOM   917  O  OD1  B ASP A 1 48  ? -13.50000 -23.34700 9.29900   0.290 20.06000  ? 48  ASP A OD1  1 
ATOM   918  O  OD2  A ASP A 1 48  ? -12.79200 -22.85000 11.15000  0.710 27.38000  ? 48  ASP A OD2  1 
ATOM   919  O  OD2  B ASP A 1 48  ? -13.32500 -21.76200 10.81700  0.290 22.79000  ? 48  ASP A OD2  1 
ATOM   920  H  H    A ASP A 1 48  ? -15.51900 -23.50000 8.50400   0.710 26.39000  ? 48  ASP A H    1 
ATOM   921  H  H    B ASP A 1 48  ? -15.52400 -23.46900 8.51500   0.290 26.63000  ? 48  ASP A H    1 
ATOM   922  H  HA   A ASP A 1 48  ? -17.13600 -23.12100 10.58200  0.710 27.91000  ? 48  ASP A HA   1 
ATOM   923  H  HA   B ASP A 1 48  ? -17.20600 -23.12800 10.55200  0.290 28.19000  ? 48  ASP A HA   1 
ATOM   924  H  HB2  A ASP A 1 48  ? -15.26900 -23.04800 11.86800  0.710 26.88000  ? 48  ASP A HB2  1 
ATOM   925  H  HB2  B ASP A 1 48  ? -15.24600 -22.83700 11.82800  0.290 27.10000  ? 48  ASP A HB2  1 
ATOM   926  H  HB3  A ASP A 1 48  ? -15.03700 -24.20600 10.80600  0.710 26.88000  ? 48  ASP A HB3  1 
ATOM   927  H  HB3  B ASP A 1 48  ? -15.17600 -24.17600 10.97500  0.290 27.10000  ? 48  ASP A HB3  1 
ATOM   928  N  N    . GLY A 1 49  ? -16.58300 -20.54900 9.05200   1.000 24.39000  ? 49  GLY A N    1 
ATOM   929  C  CA   . GLY A 1 49  ? -16.70200 -19.10500 9.03400   1.000 24.04000  ? 49  GLY A CA   1 
ATOM   930  C  C    . GLY A 1 49  ? -15.39700 -18.35200 8.82900   1.000 20.43000  ? 49  GLY A C    1 
ATOM   931  O  O    . GLY A 1 49  ? -15.41900 -17.14000 8.58500   1.000 24.14000  ? 49  GLY A O    1 
ATOM   932  H  H    . GLY A 1 49  ? -16.56700 -20.90300 8.26900   1.000 29.25000  ? 49  GLY A H    1 
ATOM   933  H  HA2  . GLY A 1 49  ? -17.30400 -18.85300 8.31600   1.000 28.83000  ? 49  GLY A HA2  1 
ATOM   934  H  HA3  . GLY A 1 49  ? -17.08000 -18.81500 9.87900   1.000 28.83000  ? 49  GLY A HA3  1 
ATOM   935  N  N    . SER A 1 50  ? -14.27600 -19.04000 8.89700   1.000 17.83000  ? 50  SER A N    1 
ATOM   936  C  CA   . SER A 1 50  ? -13.01700 -18.38600 8.58500   1.000 18.68000  ? 50  SER A CA   1 
ATOM   937  C  C    . SER A 1 50  ? -12.85500 -18.28000 7.06100   1.000 15.09000  ? 50  SER A C    1 
ATOM   938  O  O    . SER A 1 50  ? -13.59700 -18.88200 6.28300   1.000 17.75000  ? 50  SER A O    1 
ATOM   939  C  CB   . SER A 1 50  ? -11.87300 -19.16400 9.21900   1.000 15.24000  ? 50  SER A CB   1 
ATOM   940  O  OG   . SER A 1 50  ? -11.77900 -20.44600 8.64700   1.000 16.90000  ? 50  SER A OG   1 
ATOM   941  H  H    . SER A 1 50  ? -14.21500 -19.87000 9.11700   1.000 21.39000  ? 50  SER A H    1 
ATOM   942  H  HA   . SER A 1 50  ? -12.99600 -17.48500 8.94400   1.000 22.40000  ? 50  SER A HA   1 
ATOM   943  H  HB2  . SER A 1 50  ? -11.04100 -18.68700 9.06800   1.000 18.28000  ? 50  SER A HB2  1 
ATOM   944  H  HB3  . SER A 1 50  ? -12.03700 -19.25200 10.17100  1.000 18.28000  ? 50  SER A HB3  1 
ATOM   945  H  HG   . SER A 1 50  ? -12.54400 -20.78600 8.57900   1.000 20.26000  ? 50  SER A HG   1 
ATOM   946  N  N    . THR A 1 51  ? -11.85800 -17.50000 6.65800   1.000 14.47000  ? 51  THR A N    1 
ATOM   947  C  CA   . THR A 1 51  ? -11.59700 -17.21300 5.25500   1.000 11.90000  ? 51  THR A CA   1 
ATOM   948  C  C    . THR A 1 51  ? -10.11600 -17.45500 4.96600   1.000 12.81000  ? 51  THR A C    1 
ATOM   949  O  O    . THR A 1 51  ? -9.24500  -17.22200 5.80800   1.000 13.32000  ? 51  THR A O    1 
ATOM   950  C  CB   . THR A 1 51  ? -12.01400 -15.78300 4.93600   1.000 12.94000  ? 51  THR A CB   1 
ATOM   951  O  OG1  . THR A 1 51  ? -13.40600 -15.61200 5.23600   1.000 15.56000  ? 51  THR A OG1  1 
ATOM   952  C  CG2  . THR A 1 51  ? -11.81300 -15.46500 3.45300   1.000 17.18000  ? 51  THR A CG2  1 
ATOM   953  H  H    . THR A 1 51  ? -11.30600 -17.11600 7.19300   1.000 17.35000  ? 51  THR A H    1 
ATOM   954  H  HA   . THR A 1 51  ? -12.09300 -17.80400 4.66700   1.000 14.27000  ? 51  THR A HA   1 
ATOM   955  H  HB   . THR A 1 51  ? -11.47000 -15.17700 5.46500   1.000 15.52000  ? 51  THR A HB   1 
ATOM   956  H  HG1  . THR A 1 51  ? -13.49500 -15.21400 5.97000   1.000 18.66000  ? 51  THR A HG1  1 
ATOM   957  H  HG21 . THR A 1 51  ? -12.01600 -14.53200 3.28300   1.000 20.60000  ? 51  THR A HG21 1 
ATOM   958  H  HG22 . THR A 1 51  ? -10.89400 -15.63900 3.19800   1.000 20.60000  ? 51  THR A HG22 1 
ATOM   959  H  HG23 . THR A 1 51  ? -12.39900 -16.01900 2.91300   1.000 20.60000  ? 51  THR A HG23 1 
ATOM   960  N  N    A ASP A 1 52  ? -9.83300  -17.89900 3.74100   0.630 12.23000  ? 52  ASP A N    1 
ATOM   961  N  N    B ASP A 1 52  ? -9.84700  -17.93200 3.74400   0.370 12.49000  ? 52  ASP A N    1 
ATOM   962  C  CA   A ASP A 1 52  ? -8.47700  -18.13700 3.25500   0.630 12.60000  ? 52  ASP A CA   1 
ATOM   963  C  CA   B ASP A 1 52  ? -8.50300  -18.16000 3.21700   0.370 12.57000  ? 52  ASP A CA   1 
ATOM   964  C  C    A ASP A 1 52  ? -8.10700  -17.06100 2.24100   0.630 11.05000  ? 52  ASP A C    1 
ATOM   965  C  C    B ASP A 1 52  ? -8.13300  -17.02100 2.27000   0.370 11.10000  ? 52  ASP A C    1 
ATOM   966  O  O    A ASP A 1 52  ? -8.90400  -16.72900 1.35900   0.630 13.39000  ? 52  ASP A O    1 
ATOM   967  O  O    B ASP A 1 52  ? -8.96200  -16.58300 1.46700   0.370 14.26000  ? 52  ASP A O    1 
ATOM   968  C  CB   A ASP A 1 52  ? -8.36500  -19.51700 2.60900   0.630 12.83000  ? 52  ASP A CB   1 
ATOM   969  C  CB   B ASP A 1 52  ? -8.46200  -19.47600 2.43400   0.370 13.32000  ? 52  ASP A CB   1 
ATOM   970  C  CG   A ASP A 1 52  ? -9.05900  -20.59900 3.40600   0.630 14.45000  ? 52  ASP A CG   1 
ATOM   971  C  CG   B ASP A 1 52  ? -8.40100  -20.71000 3.33200   0.370 14.60000  ? 52  ASP A CG   1 
ATOM   972  O  OD1  A ASP A 1 52  ? -8.73300  -20.75800 4.59500   0.630 14.95000  ? 52  ASP A OD1  1 
ATOM   973  O  OD1  B ASP A 1 52  ? -8.17200  -20.56800 4.55000   0.370 14.98000  ? 52  ASP A OD1  1 
ATOM   974  O  OD2  A ASP A 1 52  ? -9.92300  -21.27100 2.83300   0.630 18.54000  ? 52  ASP A OD2  1 
ATOM   975  O  OD2  B ASP A 1 52  ? -8.57300  -21.83600 2.80900   0.370 17.87000  ? 52  ASP A OD2  1 
ATOM   976  H  H    A ASP A 1 52  ? -10.43400 -18.07500 3.15200   0.630 14.66000  ? 52  ASP A H    1 
ATOM   977  H  H    B ASP A 1 52  ? -10.45900 -18.13900 3.17700   0.370 14.97000  ? 52  ASP A H    1 
ATOM   978  H  HA   A ASP A 1 52  ? -7.85100  -18.09600 3.99400   0.630 15.10000  ? 52  ASP A HA   1 
ATOM   979  H  HA   B ASP A 1 52  ? -7.86300  -18.19600 3.94500   0.370 15.07000  ? 52  ASP A HA   1 
ATOM   980  H  HB2  A ASP A 1 52  ? -8.77100  -19.48700 1.72800   0.630 15.38000  ? 52  ASP A HB2  1 
ATOM   981  H  HB2  B ASP A 1 52  ? -9.26100  -19.54300 1.88900   0.370 15.98000  ? 52  ASP A HB2  1 
ATOM   982  H  HB3  A ASP A 1 52  ? -7.42800  -19.75500 2.53400   0.630 15.38000  ? 52  ASP A HB3  1 
ATOM   983  H  HB3  B ASP A 1 52  ? -7.67400  -19.48100 1.86800   0.370 15.98000  ? 52  ASP A HB3  1 
ATOM   984  N  N    . TYR A 1 53  ? -6.88400  -16.55500 2.34500   1.000 12.21000  ? 53  TYR A N    1 
ATOM   985  C  CA   . TYR A 1 53  ? -6.46100  -15.38400 1.59600   1.000 11.78000  ? 53  TYR A CA   1 
ATOM   986  C  C    . TYR A 1 53  ? -5.14900  -15.56400 0.83400   1.000 12.24000  ? 53  TYR A C    1 
ATOM   987  O  O    . TYR A 1 53  ? -4.15600  -16.03400 1.38800   1.000 13.30000  ? 53  TYR A O    1 
ATOM   988  C  CB   . TYR A 1 53  ? -6.25500  -14.21600 2.56300   1.000 14.11000  ? 53  TYR A CB   1 
ATOM   989  C  CG   . TYR A 1 53  ? -7.48000  -13.75600 3.31400   1.000 13.14000  ? 53  TYR A CG   1 
ATOM   990  C  CD1  . TYR A 1 53  ? -7.88400  -14.35600 4.51300   1.000 12.77000  ? 53  TYR A CD1  1 
ATOM   991  C  CD2  . TYR A 1 53  ? -8.24700  -12.73700 2.80000   1.000 13.36000  ? 53  TYR A CD2  1 
ATOM   992  C  CE1  . TYR A 1 53  ? -9.02000  -13.91400 5.16900   1.000 12.73000  ? 53  TYR A CE1  1 
ATOM   993  C  CE2  . TYR A 1 53  ? -9.35400  -12.28200 3.46100   1.000 14.66000  ? 53  TYR A CE2  1 
ATOM   994  C  CZ   . TYR A 1 53  ? -9.74700  -12.88400 4.62000   1.000 14.12000  ? 53  TYR A CZ   1 
ATOM   995  O  OH   . TYR A 1 53  ? -10.87300 -12.42700 5.28600   1.000 15.34000  ? 53  TYR A OH   1 
ATOM   996  H  H    . TYR A 1 53  ? -6.26900  -16.87800 2.85200   1.000 14.64000  ? 53  TYR A H    1 
ATOM   997  H  HA   . TYR A 1 53  ? -7.14800  -15.22400 0.93000   1.000 14.12000  ? 53  TYR A HA   1 
ATOM   998  H  HB2  . TYR A 1 53  ? -5.59700  -14.48200 3.22400   1.000 16.92000  ? 53  TYR A HB2  1 
ATOM   999  H  HB3  . TYR A 1 53  ? -5.92800  -13.45600 2.05600   1.000 16.92000  ? 53  TYR A HB3  1 
ATOM   1000 H  HD1  . TYR A 1 53  ? -7.38700  -15.05500 4.87000   1.000 15.31000  ? 53  TYR A HD1  1 
ATOM   1001 H  HD2  . TYR A 1 53  ? -8.00900  -12.35100 1.98800   1.000 16.02000  ? 53  TYR A HD2  1 
ATOM   1002 H  HE1  . TYR A 1 53  ? -9.28600  -14.30800 5.96800   1.000 15.27000  ? 53  TYR A HE1  1 
ATOM   1003 H  HE2  . TYR A 1 53  ? -9.83800  -11.56500 3.12200   1.000 17.58000  ? 53  TYR A HE2  1 
ATOM   1004 H  HH   . TYR A 1 53  ? -11.54000 -12.89300 5.07500   1.000 18.40000  ? 53  TYR A HH   1 
ATOM   1005 N  N    . GLY A 1 54  ? -5.15400  -15.15700 -0.41700  1.000 12.71000  ? 54  GLY A N    1 
ATOM   1006 C  CA   . GLY A 1 54  ? -3.94500  -14.94600 -1.16500  1.000 12.32000  ? 54  GLY A CA   1 
ATOM   1007 C  C    . GLY A 1 54  ? -3.44700  -16.19900 -1.85600  1.000 13.96000  ? 54  GLY A C    1 
ATOM   1008 O  O    . GLY A 1 54  ? -4.09400  -17.23000 -1.95900  1.000 13.88000  ? 54  GLY A O    1 
ATOM   1009 H  H    . GLY A 1 54  ? -5.86800  -14.99200 -0.86700  1.000 15.24000  ? 54  GLY A H    1 
ATOM   1010 H  HA2  . GLY A 1 54  ? -4.10300  -14.26900 -1.84100  1.000 14.77000  ? 54  GLY A HA2  1 
ATOM   1011 H  HA3  . GLY A 1 54  ? -3.24900  -14.63500 -0.56400  1.000 14.77000  ? 54  GLY A HA3  1 
ATOM   1012 N  N    . ILE A 1 55  ? -2.22100  -16.06000 -2.36700  1.000 14.07000  ? 55  ILE A N    1 
ATOM   1013 C  CA   . ILE A 1 55  ? -1.63700  -17.05700 -3.25200  1.000 13.72000  ? 55  ILE A CA   1 
ATOM   1014 C  C    . ILE A 1 55  ? -1.46800  -18.41300 -2.57100  1.000 14.21000  ? 55  ILE A C    1 
ATOM   1015 O  O    . ILE A 1 55  ? -1.53800  -19.45600 -3.23800  1.000 15.64000  ? 55  ILE A O    1 
ATOM   1016 C  CB   . ILE A 1 55  ? -0.31400  -16.49400 -3.80000  1.000 21.34000  ? 55  ILE A CB   1 
ATOM   1017 C  CG1  . ILE A 1 55  ? 0.12000   -17.25100 -5.05000  1.000 28.94000  ? 55  ILE A CG1  1 
ATOM   1018 C  CG2  . ILE A 1 55  ? 0.75700   -16.49000 -2.72200  1.000 18.92000  ? 55  ILE A CG2  1 
ATOM   1019 C  CD1  . ILE A 1 55  ? 0.66700   -16.37600 -6.12100  1.000 27.57000  ? 55  ILE A CD1  1 
ATOM   1020 H  H    . ILE A 1 55  ? -1.70500  -15.38900 -2.21400  1.000 16.87000  ? 55  ILE A H    1 
ATOM   1021 H  HA   . ILE A 1 55  ? -2.24200  -17.22400 -3.99100  1.000 16.45000  ? 55  ILE A HA   1 
ATOM   1022 H  HB   . ILE A 1 55  ? -0.45700  -15.57200 -4.06400  1.000 25.60000  ? 55  ILE A HB   1 
ATOM   1023 H  HG12 . ILE A 1 55  ? 0.81000   -17.88700 -4.80600  1.000 34.72000  ? 55  ILE A HG12 1 
ATOM   1024 H  HG13 . ILE A 1 55  ? -0.64900  -17.71900 -5.41400  1.000 34.72000  ? 55  ILE A HG13 1 
ATOM   1025 H  HG21 . ILE A 1 55  ? 1.54500   -16.03700 -3.06200  1.000 22.69000  ? 55  ILE A HG21 1 
ATOM   1026 H  HG22 . ILE A 1 55  ? 0.41800   -16.02400 -1.94200  1.000 22.69000  ? 55  ILE A HG22 1 
ATOM   1027 H  HG23 . ILE A 1 55  ? 0.97600   -17.40600 -2.49100  1.000 22.69000  ? 55  ILE A HG23 1 
ATOM   1028 H  HD11 . ILE A 1 55  ? 0.98300   -16.93100 -6.85100  1.000 33.07000  ? 55  ILE A HD11 1 
ATOM   1029 H  HD12 . ILE A 1 55  ? -0.03500  -15.78500 -6.43500  1.000 33.07000  ? 55  ILE A HD12 1 
ATOM   1030 H  HD13 . ILE A 1 55  ? 1.40100   -15.85600 -5.75900  1.000 33.07000  ? 55  ILE A HD13 1 
ATOM   1031 N  N    . LEU A 1 56  ? -1.29000  -18.44900 -1.24400  1.000 13.89000  ? 56  LEU A N    1 
ATOM   1032 C  CA   . LEU A 1 56  ? -1.20000  -19.70400 -0.50100  1.000 14.00000  ? 56  LEU A CA   1 
ATOM   1033 C  C    . LEU A 1 56  ? -2.38900  -19.92500 0.43000   1.000 17.29000  ? 56  LEU A C    1 
ATOM   1034 O  O    . LEU A 1 56  ? -2.36700  -20.82100 1.27000   1.000 15.20000  ? 56  LEU A O    1 
ATOM   1035 C  CB   . LEU A 1 56  ? 0.11900   -19.78400 0.27600   1.000 15.67000  ? 56  LEU A CB   1 
ATOM   1036 C  CG   . LEU A 1 56  ? 1.34200   -20.01600 -0.62100  1.000 15.52000  ? 56  LEU A CG   1 
ATOM   1037 C  CD1  . LEU A 1 56  ? 2.65000   -19.74000 0.16100   1.000 20.25000  ? 56  LEU A CD1  1 
ATOM   1038 C  CD2  . LEU A 1 56  ? 1.34300   -21.44500 -1.15500  1.000 21.48000  ? 56  LEU A CD2  1 
ATOM   1039 H  H    . LEU A 1 56  ? -1.21800  -17.74800 -0.75100  1.000 16.66000  ? 56  LEU A H    1 
ATOM   1040 H  HA   . LEU A 1 56  ? -1.19700  -20.43300 -1.14100  1.000 16.79000  ? 56  LEU A HA   1 
ATOM   1041 H  HB2  . LEU A 1 56  ? 0.25200   -18.95000 0.75200   1.000 18.80000  ? 56  LEU A HB2  1 
ATOM   1042 H  HB3  . LEU A 1 56  ? 0.06700   -20.52100 0.90500   1.000 18.80000  ? 56  LEU A HB3  1 
ATOM   1043 H  HG   . LEU A 1 56  ? 1.30100   -19.40500 -1.37300  1.000 18.62000  ? 56  LEU A HG   1 
ATOM   1044 H  HD11 . LEU A 1 56  ? 3.40700   -19.89000 -0.42600  1.000 24.29000  ? 56  LEU A HD11 1 
ATOM   1045 H  HD12 . LEU A 1 56  ? 2.64600   -18.82000 0.46800   1.000 24.29000  ? 56  LEU A HD12 1 
ATOM   1046 H  HD13 . LEU A 1 56  ? 2.69600   -20.34200 0.92100   1.000 24.29000  ? 56  LEU A HD13 1 
ATOM   1047 H  HD21 . LEU A 1 56  ? 2.12700   -21.57300 -1.71200  1.000 25.77000  ? 56  LEU A HD21 1 
ATOM   1048 H  HD22 . LEU A 1 56  ? 1.36500   -22.06200 -0.40700  1.000 25.77000  ? 56  LEU A HD22 1 
ATOM   1049 H  HD23 . LEU A 1 56  ? 0.53900   -21.58800 -1.67800  1.000 25.77000  ? 56  LEU A HD23 1 
ATOM   1050 N  N    . GLN A 1 57  ? -3.46700  -19.16800 0.25600   1.000 12.70000  ? 57  GLN A N    1 
ATOM   1051 C  CA   . GLN A 1 57  ? -4.72500  -19.42100 0.93800   1.000 13.15000  ? 57  GLN A CA   1 
ATOM   1052 C  C    . GLN A 1 57  ? -4.53700  -19.59500 2.45500   1.000 14.00000  ? 57  GLN A C    1 
ATOM   1053 O  O    . GLN A 1 57  ? -5.01700  -20.55000 3.05100   1.000 14.97000  ? 57  GLN A O    1 
ATOM   1054 C  CB   . GLN A 1 57  ? -5.45300  -20.59800 0.29500   1.000 13.28000  ? 57  GLN A CB   1 
ATOM   1055 C  CG   . GLN A 1 57  ? -5.98600  -20.28000 -1.08700  1.000 13.03000  ? 57  GLN A CG   1 
ATOM   1056 C  CD   . GLN A 1 57  ? -7.16000  -19.31800 -1.03200  1.000 14.93000  ? 57  GLN A CD   1 
ATOM   1057 O  OE1  . GLN A 1 57  ? -8.29000  -19.73100 -0.78300  1.000 15.65000  ? 57  GLN A OE1  1 
ATOM   1058 N  NE2  . GLN A 1 57  ? -6.87900  -18.03100 -1.23800  1.000 15.37000  ? 57  GLN A NE2  1 
ATOM   1059 H  H    . GLN A 1 57  ? -3.49200  -18.48500 -0.26600  1.000 15.22000  ? 57  GLN A H    1 
ATOM   1060 H  HA   . GLN A 1 57  ? -5.28700  -18.63700 0.83800   1.000 15.77000  ? 57  GLN A HA   1 
ATOM   1061 H  HB2  . GLN A 1 57  ? -4.83700  -21.34300 0.21400   1.000 15.92000  ? 57  GLN A HB2  1 
ATOM   1062 H  HB3  . GLN A 1 57  ? -6.20400  -20.84800 0.85500   1.000 15.92000  ? 57  GLN A HB3  1 
ATOM   1063 H  HG2  . GLN A 1 57  ? -5.28200  -19.87000 -1.61400  1.000 15.63000  ? 57  GLN A HG2  1 
ATOM   1064 H  HG3  . GLN A 1 57  ? -6.28400  -21.09900 -1.51100  1.000 15.63000  ? 57  GLN A HG3  1 
ATOM   1065 H  HE21 . GLN A 1 57  ? -6.06900  -17.78700 -1.39100  1.000 18.43000  ? 57  GLN A HE21 1 
ATOM   1066 H  HE22 . GLN A 1 57  ? -7.50800  -17.44600 -1.21800  1.000 18.43000  ? 57  GLN A HE22 1 
ATOM   1067 N  N    . ILE A 1 58  ? -3.94100  -18.59600 3.05900   1.000 12.13000  ? 58  ILE A N    1 
ATOM   1068 C  CA   . ILE A 1 58  ? -3.66700  -18.58900 4.49500   1.000 13.43000  ? 58  ILE A CA   1 
ATOM   1069 C  C    . ILE A 1 58  ? -4.93700  -18.21500 5.24200   1.000 13.25000  ? 58  ILE A C    1 
ATOM   1070 O  O    . ILE A 1 58  ? -5.63600  -17.25700 4.86800   1.000 13.30000  ? 58  ILE A O    1 
ATOM   1071 C  CB   . ILE A 1 58  ? -2.48800  -17.66100 4.77300   1.000 15.59000  ? 58  ILE A CB   1 
ATOM   1072 C  CG1  . ILE A 1 58  ? -1.21100  -18.30200 4.17800   1.000 17.12000  ? 58  ILE A CG1  1 
ATOM   1073 C  CG2  . ILE A 1 58  ? -2.37000  -17.37700 6.27800   1.000 16.60000  ? 58  ILE A CG2  1 
ATOM   1074 C  CD1  . ILE A 1 58  ? -0.00800  -17.38200 4.14900   1.000 21.18000  ? 58  ILE A CD1  1 
ATOM   1075 H  H    . ILE A 1 58  ? -3.67400  -17.88400 2.65800   1.000 14.54000  ? 58  ILE A H    1 
ATOM   1076 H  HA   . ILE A 1 58  ? -3.42300  -19.47300 4.81200   1.000 16.10000  ? 58  ILE A HA   1 
ATOM   1077 H  HB   . ILE A 1 58  ? -2.62400  -16.80100 4.34600   1.000 18.69000  ? 58  ILE A HB   1 
ATOM   1078 H  HG12 . ILE A 1 58  ? -0.97600  -19.07700 4.71200   1.000 20.54000  ? 58  ILE A HG12 1 
ATOM   1079 H  HG13 . ILE A 1 58  ? -1.39700  -18.57200 3.26500   1.000 20.54000  ? 58  ILE A HG13 1 
ATOM   1080 H  HG21 . ILE A 1 58  ? -1.53100  -16.92000 6.44900   1.000 19.90000  ? 58  ILE A HG21 1 
ATOM   1081 H  HG22 . ILE A 1 58  ? -3.11300  -16.81700 6.55300   1.000 19.90000  ? 58  ILE A HG22 1 
ATOM   1082 H  HG23 . ILE A 1 58  ? -2.39300  -18.21800 6.76100   1.000 19.90000  ? 58  ILE A HG23 1 
ATOM   1083 H  HD11 . ILE A 1 58  ? 0.61900   -17.70400 3.48300   1.000 25.40000  ? 58  ILE A HD11 1 
ATOM   1084 H  HD12 . ILE A 1 58  ? -0.30100  -16.48600 3.92100   1.000 25.40000  ? 58  ILE A HD12 1 
ATOM   1085 H  HD13 . ILE A 1 58  ? 0.41000   -17.38100 5.02400   1.000 25.40000  ? 58  ILE A HD13 1 
ATOM   1086 N  N    A ASN A 1 59  ? -5.27700  -18.96700 6.27600   0.470 13.20000  ? 59  ASN A N    1 
ATOM   1087 N  N    B ASN A 1 59  ? -5.18000  -18.91300 6.35500   0.300 13.14000  ? 59  ASN A N    1 
ATOM   1088 N  N    C ASN A 1 59  ? -5.28700  -19.03900 6.23000   0.230 13.32000  ? 59  ASN A N    1 
ATOM   1089 C  CA   A ASN A 1 59  ? -6.59200  -18.81300 6.89400   0.470 14.80000  ? 59  ASN A CA   1 
ATOM   1090 C  CA   B ASN A 1 59  ? -6.47300  -18.95500 7.04200   0.300 14.01000  ? 59  ASN A CA   1 
ATOM   1091 C  CA   C ASN A 1 59  ? -6.60200  -19.03800 6.87500   0.230 13.58000  ? 59  ASN A CA   1 
ATOM   1092 C  C    A ASN A 1 59  ? -6.57200  -17.88100 8.10900   0.470 13.80000  ? 59  ASN A C    1 
ATOM   1093 C  C    B ASN A 1 59  ? -6.59700  -17.85800 8.09800   0.300 13.82000  ? 59  ASN A C    1 
ATOM   1094 C  C    C ASN A 1 59  ? -6.64100  -18.08100 8.06300   0.230 13.69000  ? 59  ASN A C    1 
ATOM   1095 O  O    A ASN A 1 59  ? -5.58400  -17.78100 8.84500   0.470 15.35000  ? 59  ASN A O    1 
ATOM   1096 O  O    B ASN A 1 59  ? -5.62400  -17.50500 8.77800   0.300 13.18000  ? 59  ASN A O    1 
ATOM   1097 O  O    C ASN A 1 59  ? -5.93900  -18.27700 9.05700   0.230 12.05000  ? 59  ASN A O    1 
ATOM   1098 C  CB   A ASN A 1 59  ? -7.18200  -20.16800 7.26500   0.470 15.62000  ? 59  ASN A CB   1 
ATOM   1099 C  CB   B ASN A 1 59  ? -6.62200  -20.32300 7.72000   0.300 14.64000  ? 59  ASN A CB   1 
ATOM   1100 C  CB   C ASN A 1 59  ? -6.94500  -20.45700 7.34300   0.230 16.47000  ? 59  ASN A CB   1 
ATOM   1101 C  CG   A ASN A 1 59  ? -6.52500  -20.76100 8.47700   0.470 14.26000  ? 59  ASN A CG   1 
ATOM   1102 C  CG   B ASN A 1 59  ? -8.06900  -20.69200 8.02500   0.300 16.68000  ? 59  ASN A CG   1 
ATOM   1103 C  CG   C ASN A 1 59  ? -8.15800  -20.50000 8.24600   0.230 16.69000  ? 59  ASN A CG   1 
ATOM   1104 O  OD1  A ASN A 1 59  ? -6.68700  -20.26700 9.58400   0.470 15.55000  ? 59  ASN A OD1  1 
ATOM   1105 O  OD1  B ASN A 1 59  ? -8.92100  -19.82800 8.23600   0.300 20.83000  ? 59  ASN A OD1  1 
ATOM   1106 O  OD1  C ASN A 1 59  ? -8.03900  -20.40000 9.46700   0.230 18.60000  ? 59  ASN A OD1  1 
ATOM   1107 N  ND2  A ASN A 1 59  ? -5.77800  -21.83700 8.28000   0.470 17.10000  ? 59  ASN A ND2  1 
ATOM   1108 N  ND2  B ASN A 1 59  ? -8.34300  -21.99500 8.07000   0.300 18.44000  ? 59  ASN A ND2  1 
ATOM   1109 N  ND2  C ASN A 1 59  ? -9.32800  -20.68700 7.65400   0.230 23.49000  ? 59  ASN A ND2  1 
ATOM   1110 H  H    A ASN A 1 59  ? -4.77500  -19.56600 6.63400   0.470 15.83000  ? 59  ASN A H    1 
ATOM   1111 H  H    B ASN A 1 59  ? -4.58400  -19.39200 6.74900   0.300 15.75000  ? 59  ASN A H    1 
ATOM   1112 H  H    C ASN A 1 59  ? -4.76000  -19.63400 6.55900   0.230 15.97000  ? 59  ASN A H    1 
ATOM   1113 H  HA   A ASN A 1 59  ? -7.17800  -18.39100 6.24600   0.470 17.75000  ? 59  ASN A HA   1 
ATOM   1114 H  HA   B ASN A 1 59  ? -7.18300  -18.81100 6.39700   0.300 16.80000  ? 59  ASN A HA   1 
ATOM   1115 H  HA   C ASN A 1 59  ? -7.27000  -18.74300 6.23700   0.230 16.29000  ? 59  ASN A HA   1 
ATOM   1116 H  HB2  A ASN A 1 59  ? -8.12700  -20.06200 7.45500   0.470 18.73000  ? 59  ASN A HB2  1 
ATOM   1117 H  HB2  B ASN A 1 59  ? -6.25900  -21.00500 7.13300   0.300 17.55000  ? 59  ASN A HB2  1 
ATOM   1118 H  HB2  C ASN A 1 59  ? -7.13000  -21.00900 6.56700   0.230 19.75000  ? 59  ASN A HB2  1 
ATOM   1119 H  HB3  A ASN A 1 59  ? -7.05900  -20.78200 6.52400   0.470 18.73000  ? 59  ASN A HB3  1 
ATOM   1120 H  HB3  B ASN A 1 59  ? -6.13400  -20.31300 8.55800   0.300 17.55000  ? 59  ASN A HB3  1 
ATOM   1121 H  HB3  C ASN A 1 59  ? -6.19200  -20.81800 7.83500   0.230 19.75000  ? 59  ASN A HB3  1 
ATOM   1122 H  HD21 A ASN A 1 59  ? -5.38200  -22.21300 8.94400   0.470 20.51000  ? 59  ASN A HD21 1 
ATOM   1123 H  HD21 B ASN A 1 59  ? -9.14400  -22.26100 8.23800   0.300 22.12000  ? 59  ASN A HD21 1 
ATOM   1124 H  HD21 C ASN A 1 59  ? -9.36800  -20.77600 6.79900   0.230 28.18000  ? 59  ASN A HD21 1 
ATOM   1125 H  HD22 A ASN A 1 59  ? -5.69000  -22.16100 7.48800   0.470 20.51000  ? 59  ASN A HD22 1 
ATOM   1126 H  HD22 B ASN A 1 59  ? -7.72000  -22.57100 7.93000   0.300 22.12000  ? 59  ASN A HD22 1 
ATOM   1127 H  HD22 C ASN A 1 59  ? -10.04800 -20.71900 8.12400   0.230 28.18000  ? 59  ASN A HD22 1 
ATOM   1128 N  N    A SER A 1 60  ? -7.69400  -17.19400 8.31000   0.530 12.63000  ? 60  SER A N    1 
ATOM   1129 N  N    B SER A 1 60  ? -7.81300  -17.32300 8.23800   0.470 13.59000  ? 60  SER A N    1 
ATOM   1130 C  CA   A SER A 1 60  ? -7.81500  -16.20300 9.37100   0.530 12.55000  ? 60  SER A CA   1 
ATOM   1131 C  CA   B SER A 1 60  ? -8.12400  -16.41100 9.33000   0.470 12.63000  ? 60  SER A CA   1 
ATOM   1132 C  C    A SER A 1 60  ? -8.12200  -16.80700 10.73500  0.530 14.96000  ? 60  SER A C    1 
ATOM   1133 C  C    B SER A 1 60  ? -8.47700  -17.13000 10.62300  0.470 13.41000  ? 60  SER A C    1 
ATOM   1134 O  O    A SER A 1 60  ? -8.09200  -16.07000 11.72200  0.530 13.46000  ? 60  SER A O    1 
ATOM   1135 O  O    B SER A 1 60  ? -8.61200  -16.46900 11.65000  0.470 14.55000  ? 60  SER A O    1 
ATOM   1136 C  CB   A SER A 1 60  ? -8.91400  -15.20200 9.00600   0.530 13.40000  ? 60  SER A CB   1 
ATOM   1137 C  CB   B SER A 1 60  ? -9.30000  -15.50400 8.94600   0.470 13.79000  ? 60  SER A CB   1 
ATOM   1138 O  OG   A SER A 1 60  ? -10.14600 -15.86900 8.79800   0.530 14.44000  ? 60  SER A OG   1 
ATOM   1139 O  OG   B SER A 1 60  ? -10.50900 -16.24500 8.80700   0.470 12.96000  ? 60  SER A OG   1 
ATOM   1140 H  H    A SER A 1 60  ? -8.40700  -17.28500 7.83900   0.470 15.14000  ? 60  SER A H    1 
ATOM   1141 H  H    B SER A 1 60  ? -8.47400  -17.47500 7.70900   0.300 16.30000  ? 60  SER A H    1 
ATOM   1142 H  HA   A SER A 1 60  ? -6.97200  -15.72900 9.44800   0.530 15.04000  ? 60  SER A HA   1 
ATOM   1143 H  HA   B SER A 1 60  ? -7.34300  -15.85700 9.48700   0.470 15.14000  ? 60  SER A HA   1 
ATOM   1144 H  HB2  A SER A 1 60  ? -9.01600  -14.56600 9.73100   0.530 16.06000  ? 60  SER A HB2  1 
ATOM   1145 H  HB2  B SER A 1 60  ? -9.42000  -14.83700 9.64000   0.470 16.53000  ? 60  SER A HB2  1 
ATOM   1146 H  HB3  A SER A 1 60  ? -8.66200  -14.73900 8.19200   0.530 16.06000  ? 60  SER A HB3  1 
ATOM   1147 H  HB3  B SER A 1 60  ? -9.09900  -15.07200 8.10100   0.470 16.53000  ? 60  SER A HB3  1 
ATOM   1148 H  HG   A SER A 1 60  ? -10.11100 -16.64400 9.11900   0.530 17.32000  ? 60  SER A HG   1 
ATOM   1149 H  HG   B SER A 1 60  ? -10.72300 -16.58600 9.54500   0.470 15.54000  ? 60  SER A HG   1 
ATOM   1150 N  N    A ARG A 1 61  ? -8.39800  -18.11300 10.81500  0.520 12.36000  ? 61  ARG A N    1 
ATOM   1151 N  N    B ARG A 1 61  ? -8.66900  -18.44900 10.59300  0.480 15.45000  ? 61  ARG A N    1 
ATOM   1152 C  CA   A ARG A 1 61  ? -8.66500  -18.74300 12.10700  0.520 15.91000  ? 61  ARG A CA   1 
ATOM   1153 C  CA   B ARG A 1 61  ? -8.92000  -19.17000 11.83800  0.480 14.93000  ? 61  ARG A CA   1 
ATOM   1154 C  C    A ARG A 1 61  ? -7.41900  -18.70600 12.96800  0.520 17.35000  ? 61  ARG A C    1 
ATOM   1155 C  C    B ARG A 1 61  ? -7.71200  -19.09300 12.76400  0.480 15.11000  ? 61  ARG A C    1 
ATOM   1156 O  O    A ARG A 1 61  ? -7.48200  -18.44100 14.17900  0.520 15.84000  ? 61  ARG A O    1 
ATOM   1157 O  O    B ARG A 1 61  ? -7.88900  -19.08700 13.99000  0.480 16.02000  ? 61  ARG A O    1 
ATOM   1158 C  CB   A ARG A 1 61  ? -9.11000  -20.18900 11.86800  0.520 19.53000  ? 61  ARG A CB   1 
ATOM   1159 C  CB   B ARG A 1 61  ? -9.30600  -20.61900 11.53100  0.480 19.47000  ? 61  ARG A CB   1 
ATOM   1160 C  CG   A ARG A 1 61  ? -9.25100  -21.07300 13.11800  0.520 23.33000  ? 61  ARG A CG   1 
ATOM   1161 C  CG   B ARG A 1 61  ? -9.50000  -21.54000 12.75300  0.480 21.12000  ? 61  ARG A CG   1 
ATOM   1162 C  CD   A ARG A 1 61  ? -10.40900 -20.65100 13.99900  0.520 26.19000  ? 61  ARG A CD   1 
ATOM   1163 C  CD   B ARG A 1 61  ? -10.59500 -21.06400 13.68600  0.480 19.12000  ? 61  ARG A CD   1 
ATOM   1164 N  NE   A ARG A 1 61  ? -11.69100 -20.68800 13.30500  0.520 29.79000  ? 61  ARG A NE   1 
ATOM   1165 N  NE   B ARG A 1 61  ? -11.87500 -20.84900 13.02400  0.480 29.97000  ? 61  ARG A NE   1 
ATOM   1166 C  CZ   A ARG A 1 61  ? -12.74200 -19.95600 13.65100  0.520 39.78000  ? 61  ARG A CZ   1 
ATOM   1167 C  CZ   B ARG A 1 61  ? -12.88000 -20.17100 13.56200  0.480 40.81000  ? 61  ARG A CZ   1 
ATOM   1168 N  NH1  A ARG A 1 61  ? -12.70700 -19.15600 14.70200  0.520 31.91000  ? 61  ARG A NH1  1 
ATOM   1169 N  NH1  B ARG A 1 61  ? -12.78700 -19.64400 14.77300  0.480 35.26000  ? 61  ARG A NH1  1 
ATOM   1170 N  NH2  A ARG A 1 61  ? -13.85300 -20.02700 12.92400  0.520 33.38000  ? 61  ARG A NH2  1 
ATOM   1171 N  NH2  B ARG A 1 61  ? -14.00200 -20.00900 12.86600  0.480 33.09000  ? 61  ARG A NH2  1 
ATOM   1172 H  H    A ARG A 1 61  ? -8.43500  -18.64900 10.14400  0.530 14.82000  ? 61  ARG A H    1 
ATOM   1173 H  H    B ARG A 1 61  ? -8.66000  -18.93700 9.88500   0.470 18.53000  ? 61  ARG A H    1 
ATOM   1174 H  HA   A ARG A 1 61  ? -9.37600  -18.27400 12.57100  0.520 19.07000  ? 61  ARG A HA   1 
ATOM   1175 H  HA   B ARG A 1 61  ? -9.67000  -18.76900 12.30600  0.480 17.91000  ? 61  ARG A HA   1 
ATOM   1176 H  HB2  A ARG A 1 61  ? -9.97700  -20.17100 11.43300  0.520 23.42000  ? 61  ARG A HB2  1 
ATOM   1177 H  HB2  B ARG A 1 61  ? -10.14400 -20.61200 11.04100  0.480 23.35000  ? 61  ARG A HB2  1 
ATOM   1178 H  HB3  A ARG A 1 61  ? -8.45700  -20.61400 11.29000  0.520 23.42000  ? 61  ARG A HB3  1 
ATOM   1179 H  HB3  B ARG A 1 61  ? -8.60700  -21.01000 10.98500  0.480 23.35000  ? 61  ARG A HB3  1 
ATOM   1180 H  HG2  A ARG A 1 61  ? -9.40200  -21.99000 12.84200  0.520 27.99000  ? 61  ARG A HG2  1 
ATOM   1181 H  HG2  B ARG A 1 61  ? -9.73600  -22.42800 12.44400  0.480 25.33000  ? 61  ARG A HG2  1 
ATOM   1182 H  HG3  A ARG A 1 61  ? -8.43700  -21.01300 13.64200  0.520 27.99000  ? 61  ARG A HG3  1 
ATOM   1183 H  HG3  B ARG A 1 61  ? -8.67200  -21.57300 13.25700  0.480 25.33000  ? 61  ARG A HG3  1 
ATOM   1184 H  HD2  A ARG A 1 61  ? -10.46300 -21.25100 14.75900  0.520 31.42000  ? 61  ARG A HD2  1 
ATOM   1185 H  HD2  B ARG A 1 61  ? -10.72800 -21.73100 14.37800  0.480 22.94000  ? 61  ARG A HD2  1 
ATOM   1186 H  HD3  A ARG A 1 61  ? -10.26000 -19.74200 14.30300  0.520 31.42000  ? 61  ARG A HD3  1 
ATOM   1187 H  HD3  B ARG A 1 61  ? -10.32200 -20.22300 14.08500  0.480 22.94000  ? 61  ARG A HD3  1 
ATOM   1188 H  HE   A ARG A 1 61  ? -11.77000 -21.21600 12.63000  0.520 35.74000  ? 61  ARG A HE   1 
ATOM   1189 H  HE   B ARG A 1 61  ? -11.98500 -21.18000 12.23800  0.480 35.95000  ? 61  ARG A HE   1 
ATOM   1190 H  HH11 A ARG A 1 61  ? -11.99200 -19.10100 15.17700  0.520 38.28000  ? 61  ARG A HH11 1 
ATOM   1191 H  HH11 B ARG A 1 61  ? -13.45100 -19.20800 15.10400  0.480 42.29000  ? 61  ARG A HH11 1 
ATOM   1192 H  HH12 A ARG A 1 61  ? -13.39900 -18.69000 14.91000  0.520 38.28000  ? 61  ARG A HH12 1 
ATOM   1193 H  HH12 B ARG A 1 61  ? -12.06400 -19.73700 15.22800  0.480 42.29000  ? 61  ARG A HH12 1 
ATOM   1194 H  HH21 A ARG A 1 61  ? -13.88600 -20.54400 12.23800  0.520 40.04000  ? 61  ARG A HH21 1 
ATOM   1195 H  HH21 B ARG A 1 61  ? -14.07000 -20.34200 12.07600  0.480 39.70000  ? 61  ARG A HH21 1 
ATOM   1196 H  HH22 A ARG A 1 61  ? -14.54000 -19.55700 13.14100  0.520 40.04000  ? 61  ARG A HH22 1 
ATOM   1197 H  HH22 B ARG A 1 61  ? -14.66000 -19.57200 13.20500  0.480 39.70000  ? 61  ARG A HH22 1 
ATOM   1198 N  N    A TRP A 1 62  ? -6.27200  -18.95500 12.35900  0.570 17.27000  ? 62  TRP A N    1 
ATOM   1199 N  N    B TRP A 1 62  ? -6.49400  -18.96100 12.20400  0.430 16.75000  ? 62  TRP A N    1 
ATOM   1200 C  CA   A TRP A 1 62  ? -5.02700  -18.97300 13.09400  0.570 16.94000  ? 62  TRP A CA   1 
ATOM   1201 C  CA   B TRP A 1 62  ? -5.26400  -18.99900 12.99400  0.430 15.22000  ? 62  TRP A CA   1 
ATOM   1202 C  C    A TRP A 1 62  ? -4.08700  -17.85400 12.72800  0.570 19.83000  ? 62  TRP A C    1 
ATOM   1203 C  C    B TRP A 1 62  ? -4.20400  -17.91900 12.71700  0.430 18.49000  ? 62  TRP A C    1 
ATOM   1204 O  O    A TRP A 1 62  ? -3.31600  -17.41100 13.57600  0.570 19.66000  ? 62  TRP A O    1 
ATOM   1205 O  O    B TRP A 1 62  ? -3.47100  -17.55700 13.63700  0.430 19.44000  ? 62  TRP A O    1 
ATOM   1206 C  CB   A TRP A 1 62  ? -4.29000  -20.30300 12.86600  0.570 18.79000  ? 62  TRP A CB   1 
ATOM   1207 C  CB   B TRP A 1 62  ? -4.59000  -20.38200 12.85900  0.430 19.99000  ? 62  TRP A CB   1 
ATOM   1208 C  CG   A TRP A 1 62  ? -5.05500  -21.46900 13.37500  0.570 20.68000  ? 62  TRP A CG   1 
ATOM   1209 C  CG   B TRP A 1 62  ? -5.40300  -21.53100 13.41200  0.430 22.51000  ? 62  TRP A CG   1 
ATOM   1210 C  CD1  A TRP A 1 62  ? -5.79800  -22.34200 12.64700  0.570 26.01000  ? 62  TRP A CD1  1 
ATOM   1211 C  CD1  B TRP A 1 62  ? -6.10000  -22.45900 12.69800  0.430 28.62000  ? 62  TRP A CD1  1 
ATOM   1212 C  CD2  A TRP A 1 62  ? -5.19100  -21.86500 14.74200  0.570 28.17000  ? 62  TRP A CD2  1 
ATOM   1213 C  CD2  B TRP A 1 62  ? -5.60800  -21.85300 14.79500  0.430 23.92000  ? 62  TRP A CD2  1 
ATOM   1214 N  NE1  A TRP A 1 62  ? -6.38200  -23.27300 13.47500  0.570 34.47000  ? 62  TRP A NE1  1 
ATOM   1215 N  NE1  B TRP A 1 62  ? -6.72500  -23.34000 13.55000  0.430 30.44000  ? 62  TRP A NE1  1 
ATOM   1216 C  CE2  A TRP A 1 62  ? -6.02400  -22.99800 14.76700  0.570 27.93000  ? 62  TRP A CE2  1 
ATOM   1217 C  CE2  B TRP A 1 62  ? -6.43600  -22.98900 14.84200  0.430 28.00000  ? 62  TRP A CE2  1 
ATOM   1218 C  CE3  A TRP A 1 62  ? -4.68000  -21.37200 15.94400  0.570 29.11000  ? 62  TRP A CE3  1 
ATOM   1219 C  CE3  B TRP A 1 62  ? -5.17000  -21.28600 15.99500  0.430 30.40000  ? 62  TRP A CE3  1 
ATOM   1220 C  CZ2  A TRP A 1 62  ? -6.35200  -23.65500 15.95100  0.570 41.39000  ? 62  TRP A CZ2  1 
ATOM   1221 C  CZ2  B TRP A 1 62  ? -6.83400  -23.57300 16.04500  0.430 40.92000  ? 62  TRP A CZ2  1 
ATOM   1222 C  CZ3  A TRP A 1 62  ? -5.00900  -22.02200 17.11900  0.570 42.03000  ? 62  TRP A CZ3  1 
ATOM   1223 C  CZ3  B TRP A 1 62  ? -5.56500  -21.86600 17.18700  0.430 37.95000  ? 62  TRP A CZ3  1 
ATOM   1224 C  CH2  A TRP A 1 62  ? -5.83800  -23.14900 17.11400  0.570 44.28000  ? 62  TRP A CH2  1 
ATOM   1225 C  CH2  B TRP A 1 62  ? -6.38800  -22.99600 17.20300  0.430 43.31000  ? 62  TRP A CH2  1 
ATOM   1226 H  H    A TRP A 1 62  ? -6.19200  -19.11700 11.51800  0.520 20.71000  ? 62  TRP A H    1 
ATOM   1227 H  H    B TRP A 1 62  ? -6.36000  -18.84700 11.36200  0.480 20.08000  ? 62  TRP A H    1 
ATOM   1228 H  HA   A TRP A 1 62  ? -5.23500  -18.89700 14.03900  0.570 20.32000  ? 62  TRP A HA   1 
ATOM   1229 H  HA   B TRP A 1 62  ? -5.56700  -18.81700 13.89800  0.430 18.26000  ? 62  TRP A HA   1 
ATOM   1230 H  HB2  A TRP A 1 62  ? -4.14700  -20.42800 11.91500  0.570 22.53000  ? 62  TRP A HB2  1 
ATOM   1231 H  HB2  B TRP A 1 62  ? -4.43500  -20.55900 11.91800  0.430 23.98000  ? 62  TRP A HB2  1 
ATOM   1232 H  HB3  A TRP A 1 62  ? -3.43700  -20.27700 13.32900  0.570 22.53000  ? 62  TRP A HB3  1 
ATOM   1233 H  HB3  B TRP A 1 62  ? -3.74700  -20.36300 13.33700  0.430 23.98000  ? 62  TRP A HB3  1 
ATOM   1234 H  HD1  A TRP A 1 62  ? -5.89800  -22.31400 11.72300  0.570 31.20000  ? 62  TRP A HD1  1 
ATOM   1235 H  HD1  B TRP A 1 62  ? -6.14600  -22.49200 11.77000  0.430 34.34000  ? 62  TRP A HD1  1 
ATOM   1236 H  HE1  A TRP A 1 62  ? -6.88800  -23.92100 13.22200  0.570 41.36000  ? 62  TRP A HE1  1 
ATOM   1237 H  HE1  B TRP A 1 62  ? -7.21700  -24.00400 13.31000  0.430 36.51000  ? 62  TRP A HE1  1 
ATOM   1238 H  HE3  A TRP A 1 62  ? -4.12900  -20.62300 15.95500  0.570 34.92000  ? 62  TRP A HE3  1 
ATOM   1239 H  HE3  B TRP A 1 62  ? -4.62400  -20.53300 15.99200  0.430 36.47000  ? 62  TRP A HE3  1 
ATOM   1240 H  HZ2  A TRP A 1 62  ? -6.89900  -24.40700 15.95100  0.570 49.65000  ? 62  TRP A HZ2  1 
ATOM   1241 H  HZ2  B TRP A 1 62  ? -7.38000  -24.32500 16.05900  0.430 49.09000  ? 62  TRP A HZ2  1 
ATOM   1242 H  HZ3  A TRP A 1 62  ? -4.67500  -21.70400 17.92600  0.570 50.43000  ? 62  TRP A HZ3  1 
ATOM   1243 H  HZ3  B TRP A 1 62  ? -5.27800  -21.49900 17.99200  0.430 45.53000  ? 62  TRP A HZ3  1 
ATOM   1244 H  HH2  A TRP A 1 62  ? -6.04500  -23.56400 17.92000  0.570 53.13000  ? 62  TRP A HH2  1 
ATOM   1245 H  HH2  B TRP A 1 62  ? -6.63800  -23.36400 18.02000  0.430 51.96000  ? 62  TRP A HH2  1 
ATOM   1246 N  N    . TRP A 1 63  ? -4.07900  -17.39600 11.47800  1.000 14.65000  ? 63  TRP A N    1 
ATOM   1247 C  CA   . TRP A 1 63  ? -2.85700  -16.75300 11.01300  1.000 14.97000  ? 63  TRP A CA   1 
ATOM   1248 C  C    . TRP A 1 63  ? -2.92900  -15.27300 10.73400  1.000 15.06000  ? 63  TRP A C    1 
ATOM   1249 O  O    . TRP A 1 63  ? -1.89700  -14.61300 10.70400  1.000 17.73000  ? 63  TRP A O    1 
ATOM   1250 C  CB   . TRP A 1 63  ? -2.33400  -17.46600 9.74300   1.000 15.75000  ? 63  TRP A CB   1 
ATOM   1251 C  CG   . TRP A 1 63  ? -2.16400  -18.94400 9.98400   1.000 16.46000  ? 63  TRP A CG   1 
ATOM   1252 C  CD1  . TRP A 1 63  ? -2.95000  -19.93700 9.54400   1.000 17.57000  ? 63  TRP A CD1  1 
ATOM   1253 C  CD2  . TRP A 1 63  ? -1.16000  -19.56500 10.81800  1.000 16.46000  ? 63  TRP A CD2  1 
ATOM   1254 N  NE1  . TRP A 1 63  ? -2.49200  -21.15100 10.00900  1.000 18.98000  ? 63  TRP A NE1  1 
ATOM   1255 C  CE2  . TRP A 1 63  ? -1.40800  -20.93800 10.80700  1.000 17.07000  ? 63  TRP A CE2  1 
ATOM   1256 C  CE3  . TRP A 1 63  ? -0.07500  -19.07800 11.53600  1.000 17.53000  ? 63  TRP A CE3  1 
ATOM   1257 C  CZ2  . TRP A 1 63  ? -0.58500  -21.85400 11.49100  1.000 18.50000  ? 63  TRP A CZ2  1 
ATOM   1258 C  CZ3  . TRP A 1 63  ? 0.73400   -19.98300 12.21900  1.000 20.23000  ? 63  TRP A CZ3  1 
ATOM   1259 C  CH2  . TRP A 1 63  ? 0.46200   -21.35100 12.18500  1.000 21.30000  ? 63  TRP A CH2  1 
ATOM   1260 H  H    . TRP A 1 63  ? -4.72800  -17.44300 10.91600  1.000 17.56000  ? 63  TRP A H    1 
ATOM   1261 H  HA   . TRP A 1 63  ? -2.20700  -16.84900 11.72700  1.000 17.95000  ? 63  TRP A HA   1 
ATOM   1262 H  HB2  . TRP A 1 63  ? -2.96900  -17.34400 9.02000   1.000 18.89000  ? 63  TRP A HB2  1 
ATOM   1263 H  HB3  . TRP A 1 63  ? -1.47300  -17.09400 9.49500   1.000 18.89000  ? 63  TRP A HB3  1 
ATOM   1264 H  HD1  . TRP A 1 63  ? -3.69800  -19.82300 9.00400   1.000 21.07000  ? 63  TRP A HD1  1 
ATOM   1265 H  HE1  . TRP A 1 63  ? -2.83400  -21.91900 9.82600   1.000 22.76000  ? 63  TRP A HE1  1 
ATOM   1266 H  HE3  . TRP A 1 63  ? 0.10800   -18.16700 11.56000  1.000 21.02000  ? 63  TRP A HE3  1 
ATOM   1267 H  HZ2  . TRP A 1 63  ? -0.75500  -22.76800 11.46700  1.000 22.19000  ? 63  TRP A HZ2  1 
ATOM   1268 H  HZ3  . TRP A 1 63  ? 1.46500   -19.67200 12.70400  1.000 24.26000  ? 63  TRP A HZ3  1 
ATOM   1269 H  HH2  . TRP A 1 63  ? 1.01500   -21.93400 12.65300  1.000 25.55000  ? 63  TRP A HH2  1 
ATOM   1270 N  N    . CYS A 1 64  ? -4.11700  -14.73400 10.49600  1.000 14.67000  ? 64  CYS A N    1 
ATOM   1271 C  CA   . CYS A 1 64  ? -4.24100  -13.31700 10.17500  1.000 16.92000  ? 64  CYS A CA   1 
ATOM   1272 C  C    . CYS A 1 64  ? -5.54500  -12.78800 10.74100  1.000 13.79000  ? 64  CYS A C    1 
ATOM   1273 O  O    . CYS A 1 64  ? -6.43900  -13.54200 11.08000  1.000 15.90000  ? 64  CYS A O    1 
ATOM   1274 C  CB   . CYS A 1 64  ? -4.13500  -13.05100 8.66000   1.000 14.44000  ? 64  CYS A CB   1 
ATOM   1275 S  SG   . CYS A 1 64  ? -5.39700  -13.82400 7.64200   1.000 14.94000  ? 64  CYS A SG   1 
ATOM   1276 H  H    . CYS A 1 64  ? -4.86200  -15.16300 10.51400  1.000 17.59000  ? 64  CYS A H    1 
ATOM   1277 H  HA   . CYS A 1 64  ? -3.51900  -12.83200 10.60200  1.000 20.29000  ? 64  CYS A HA   1 
ATOM   1278 H  HB2  . CYS A 1 64  ? -4.19400  -12.09400 8.51400   1.000 17.32000  ? 64  CYS A HB2  1 
ATOM   1279 H  HB3  . CYS A 1 64  ? -3.27600  -13.38000 8.35300   1.000 17.32000  ? 64  CYS A HB3  1 
ATOM   1280 N  N    . ASN A 1 65  ? -5.64500  -11.45900 10.82200  1.000 15.78000  ? 65  ASN A N    1 
ATOM   1281 C  CA   . ASN A 1 65  ? -6.85900  -10.83100 11.33900  1.000 16.13000  ? 65  ASN A CA   1 
ATOM   1282 C  C    . ASN A 1 65  ? -7.67700  -10.22800 10.19900  1.000 13.27000  ? 65  ASN A C    1 
ATOM   1283 O  O    . ASN A 1 65  ? -7.17900  -9.37300  9.47000   1.000 14.90000  ? 65  ASN A O    1 
ATOM   1284 C  CB   . ASN A 1 65  ? -6.49500  -9.71200  12.31500  1.000 18.72000  ? 65  ASN A CB   1 
ATOM   1285 C  CG   . ASN A 1 65  ? -7.71500  -9.01700  12.84500  1.000 22.67000  ? 65  ASN A CG   1 
ATOM   1286 O  OD1  . ASN A 1 65  ? -8.66500  -9.66800  13.25500  1.000 26.50000  ? 65  ASN A OD1  1 
ATOM   1287 N  ND2  . ASN A 1 65  ? -7.72700  -7.69100  12.75900  1.000 36.72000  ? 65  ASN A ND2  1 
ATOM   1288 H  H    . ASN A 1 65  ? -5.02900  -10.90800 10.58600  1.000 18.93000  ? 65  ASN A H    1 
ATOM   1289 H  HA   . ASN A 1 65  ? -7.39100  -11.51300 11.77800  1.000 19.34000  ? 65  ASN A HA   1 
ATOM   1290 H  HB2  . ASN A 1 65  ? -6.00800  -10.08800 13.06500  1.000 22.45000  ? 65  ASN A HB2  1 
ATOM   1291 H  HB3  . ASN A 1 65  ? -5.94500  -9.05600  11.85800  1.000 22.45000  ? 65  ASN A HB3  1 
ATOM   1292 H  HD21 . ASN A 1 65  ? -7.05700  -7.27700  12.41300  1.000 44.05000  ? 65  ASN A HD21 1 
ATOM   1293 H  HD22 . ASN A 1 65  ? -8.40400  -7.24700  13.04900  1.000 44.05000  ? 65  ASN A HD22 1 
ATOM   1294 N  N    . ASP A 1 66  ? -8.92500  -10.65600 10.08500  1.000 16.11000  ? 66  ASP A N    1 
ATOM   1295 C  CA   . ASP A 1 66  ? -9.84100  -10.05800 9.12900   1.000 14.92000  ? 66  ASP A CA   1 
ATOM   1296 C  C    . ASP A 1 66  ? -11.02300 -9.36100  9.78900   1.000 17.62000  ? 66  ASP A C    1 
ATOM   1297 O  O    . ASP A 1 66  ? -11.90900 -8.86200  9.07200   1.000 18.95000  ? 66  ASP A O    1 
ATOM   1298 C  CB   . ASP A 1 66  ? -10.30000 -11.05000 8.05600   1.000 14.64000  ? 66  ASP A CB   1 
ATOM   1299 C  CG   . ASP A 1 66  ? -11.11800 -12.18900 8.57300   1.000 14.92000  ? 66  ASP A CG   1 
ATOM   1300 O  OD1  . ASP A 1 66  ? -11.51000 -12.22700 9.75500   1.000 16.12000  ? 66  ASP A OD1  1 
ATOM   1301 O  OD2  . ASP A 1 66  ? -11.42700 -13.09600 7.76700   1.000 14.75000  ? 66  ASP A OD2  1 
ATOM   1302 H  H    . ASP A 1 66  ? -9.26500  -11.29300 10.55300  1.000 19.32000  ? 66  ASP A H    1 
ATOM   1303 H  HA   . ASP A 1 66  ? -9.34600  -9.37700  8.64700   1.000 17.89000  ? 66  ASP A HA   1 
ATOM   1304 H  HB2  . ASP A 1 66  ? -10.84000 -10.57400 7.40600   1.000 17.55000  ? 66  ASP A HB2  1 
ATOM   1305 H  HB3  . ASP A 1 66  ? -9.51600  -11.42500 7.62600   1.000 17.55000  ? 66  ASP A HB3  1 
ATOM   1306 N  N    . GLY A 1 67  ? -11.03400 -9.27700  11.11000  1.000 17.62000  ? 67  GLY A N    1 
ATOM   1307 C  CA   . GLY A 1 67  ? -12.09900 -8.58200  11.83400  1.000 19.07000  ? 67  GLY A CA   1 
ATOM   1308 C  C    . GLY A 1 67  ? -13.42300 -9.30000  11.88900  1.000 21.08000  ? 67  GLY A C    1 
ATOM   1309 O  O    . GLY A 1 67  ? -14.38600 -8.74500  12.44600  1.000 24.21000  ? 67  GLY A O    1 
ATOM   1310 H  H    . GLY A 1 67  ? -10.43200 -9.61600  11.62100  1.000 21.13000  ? 67  GLY A H    1 
ATOM   1311 H  HA2  . GLY A 1 67  ? -11.80600 -8.43700  12.74700  1.000 22.87000  ? 67  GLY A HA2  1 
ATOM   1312 H  HA3  . GLY A 1 67  ? -12.24900 -7.72300  11.40900  1.000 22.87000  ? 67  GLY A HA3  1 
ATOM   1313 N  N    . ARG A 1 68  ? -13.54100 -10.51400 11.34500  1.000 18.21000  ? 68  ARG A N    1 
ATOM   1314 C  CA   . ARG A 1 68  ? -14.83000 -11.17700 11.25200  1.000 18.39000  ? 68  ARG A CA   1 
ATOM   1315 C  C    . ARG A 1 68  ? -14.73900 -12.68300 11.47400  1.000 20.03000  ? 68  ARG A C    1 
ATOM   1316 O  O    . ARG A 1 68  ? -15.58100 -13.44000 10.98400  1.000 27.37000  ? 68  ARG A O    1 
ATOM   1317 C  CB   . ARG A 1 68  ? -15.48300 -10.83700 9.92200   1.000 20.13000  ? 68  ARG A CB   1 
ATOM   1318 C  CG   . ARG A 1 68  ? -14.74900 -11.42400 8.71000   1.000 20.79000  ? 68  ARG A CG   1 
ATOM   1319 C  CD   . ARG A 1 68  ? -15.72600 -11.60400 7.59000   1.000 24.89000  ? 68  ARG A CD   1 
ATOM   1320 N  NE   . ARG A 1 68  ? -15.34400 -12.62600 6.63700   1.000 24.52000  ? 68  ARG A NE   1 
ATOM   1321 C  CZ   . ARG A 1 68  ? -15.69400 -12.60000 5.35700   1.000 34.61000  ? 68  ARG A CZ   1 
ATOM   1322 N  NH1  . ARG A 1 68  ? -16.52300 -11.68300 4.89400   1.000 27.18000  ? 68  ARG A NH1  1 
ATOM   1323 N  NH2  . ARG A 1 68  ? -15.25900 -13.55600 4.53600   1.000 26.20000  ? 68  ARG A NH2  1 
ATOM   1324 H  H    . ARG A 1 68  ? -12.88600 -10.97000 11.02400  1.000 21.84000  ? 68  ARG A H    1 
ATOM   1325 H  HA   . ARG A 1 68  ? -15.40600 -10.85700 11.96400  1.000 22.06000  ? 68  ARG A HA   1 
ATOM   1326 H  HB2  . ARG A 1 68  ? -16.38800 -11.18600 9.92000   1.000 24.14000  ? 68  ARG A HB2  1 
ATOM   1327 H  HB3  . ARG A 1 68  ? -15.50000 -9.87200  9.82000   1.000 24.14000  ? 68  ARG A HB3  1 
ATOM   1328 H  HG2  . ARG A 1 68  ? -14.04800 -10.81900 8.42200   1.000 24.94000  ? 68  ARG A HG2  1 
ATOM   1329 H  HG3  . ARG A 1 68  ? -14.37000 -12.28700 8.93900   1.000 24.94000  ? 68  ARG A HG3  1 
ATOM   1330 H  HD2  . ARG A 1 68  ? -16.58600 -11.85500 7.96300   1.000 29.86000  ? 68  ARG A HD2  1 
ATOM   1331 H  HD3  . ARG A 1 68  ? -15.80600 -10.76600 7.10800   1.000 29.86000  ? 68  ARG A HD3  1 
ATOM   1332 H  HE   . ARG A 1 68  ? -14.86500 -13.28400 6.91500   1.000 29.41000  ? 68  ARG A HE   1 
ATOM   1333 H  HH11 . ARG A 1 68  ? -16.84600 -11.08800 5.42500   1.000 32.60000  ? 68  ARG A HH11 1 
ATOM   1334 H  HH12 . ARG A 1 68  ? -16.73900 -11.68000 4.06200   1.000 32.60000  ? 68  ARG A HH12 1 
ATOM   1335 H  HH21 . ARG A 1 68  ? -14.75500 -14.18500 4.83700   1.000 31.43000  ? 68  ARG A HH21 1 
ATOM   1336 H  HH22 . ARG A 1 68  ? -15.48200 -13.54400 3.70600   1.000 31.43000  ? 68  ARG A HH22 1 
ATOM   1337 N  N    . THR A 1 69  ? -13.73200 -13.14600 12.19800  1.000 18.00000  ? 69  THR A N    1 
ATOM   1338 C  CA   . THR A 1 69  ? -13.59400 -14.57000 12.48600  1.000 18.68000  ? 69  THR A CA   1 
ATOM   1339 C  C    . THR A 1 69  ? -13.57700 -14.75100 13.99900  1.000 17.90000  ? 69  THR A C    1 
ATOM   1340 O  O    . THR A 1 69  ? -12.50300 -14.78500 14.61600  1.000 22.57000  ? 69  THR A O    1 
ATOM   1341 C  CB   . THR A 1 69  ? -12.33500 -15.15200 11.84800  1.000 20.78000  ? 69  THR A CB   1 
ATOM   1342 O  OG1  . THR A 1 69  ? -12.28400 -14.79400 10.45400  1.000 18.83000  ? 69  THR A OG1  1 
ATOM   1343 C  CG2  . THR A 1 69  ? -12.36500 -16.64000 11.96500  1.000 18.42000  ? 69  THR A CG2  1 
ATOM   1344 H  H    . THR A 1 69  ? -13.11200 -12.65500 12.53600  1.000 21.58000  ? 69  THR A H    1 
ATOM   1345 H  HA   . THR A 1 69  ? -14.36000 -15.04300 12.12400  1.000 22.40000  ? 69  THR A HA   1 
ATOM   1346 H  HB   . THR A 1 69  ? -11.54600 -14.80700 12.29400  1.000 24.92000  ? 69  THR A HB   1 
ATOM   1347 H  HG1  . THR A 1 69  ? -12.86500 -15.22300 10.02500  1.000 22.58000  ? 69  THR A HG1  1 
ATOM   1348 H  HG21 . THR A 1 69  ? -11.51000 -17.01100 11.69600  1.000 22.09000  ? 69  THR A HG21 1 
ATOM   1349 H  HG22 . THR A 1 69  ? -12.54400 -16.89600 12.88300  1.000 22.09000  ? 69  THR A HG22 1 
ATOM   1350 H  HG23 . THR A 1 69  ? -13.06000 -17.00400 11.39500  1.000 22.09000  ? 69  THR A HG23 1 
ATOM   1351 N  N    . PRO A 1 70  ? -14.74300 -14.90100 14.62700  1.000 19.06000  ? 70  PRO A N    1 
ATOM   1352 C  CA   . PRO A 1 70  ? -14.78800 -14.89500 16.09200  1.000 22.05000  ? 70  PRO A CA   1 
ATOM   1353 C  C    . PRO A 1 70  ? -14.02000 -16.05700 16.68200  1.000 23.02000  ? 70  PRO A C    1 
ATOM   1354 O  O    . PRO A 1 70  ? -14.09500 -17.19000 16.20200  1.000 30.36000  ? 70  PRO A O    1 
ATOM   1355 C  CB   . PRO A 1 70  ? -16.28500 -15.01500 16.39600  1.000 24.87000  ? 70  PRO A CB   1 
ATOM   1356 C  CG   . PRO A 1 70  ? -16.95700 -14.44700 15.21900  1.000 30.89000  ? 70  PRO A CG   1 
ATOM   1357 C  CD   . PRO A 1 70  ? -16.09100 -14.87900 14.04900  1.000 26.16000  ? 70  PRO A CD   1 
ATOM   1358 H  HA   . PRO A 1 70  ? -14.43700 -14.06000 16.43800  1.000 26.44000  ? 70  PRO A HA   1 
ATOM   1359 H  HB2  . PRO A 1 70  ? -16.52400 -15.94800 16.51500  1.000 29.83000  ? 70  PRO A HB2  1 
ATOM   1360 H  HB3  . PRO A 1 70  ? -16.50200 -14.51200 17.19600  1.000 29.83000  ? 70  PRO A HB3  1 
ATOM   1361 H  HG2  . PRO A 1 70  ? -17.85500 -14.80600 15.14200  1.000 37.06000  ? 70  PRO A HG2  1 
ATOM   1362 H  HG3  . PRO A 1 70  ? -16.99200 -13.48000 15.29000  1.000 37.06000  ? 70  PRO A HG3  1 
ATOM   1363 H  HD2  . PRO A 1 70  ? -16.34700 -15.76100 13.73500  1.000 31.38000  ? 70  PRO A HD2  1 
ATOM   1364 H  HD3  . PRO A 1 70  ? -16.14600 -14.24000 13.32200  1.000 31.38000  ? 70  PRO A HD3  1 
ATOM   1365 N  N    . GLY A 1 71  ? -13.27600 -15.75600 17.73800  1.000 24.09000  ? 71  GLY A N    1 
ATOM   1366 C  CA   . GLY A 1 71  ? -12.54600 -16.77500 18.45600  1.000 31.50000  ? 71  GLY A CA   1 
ATOM   1367 C  C    . GLY A 1 71  ? -11.30500 -17.24700 17.74600  1.000 39.70000  ? 71  GLY A C    1 
ATOM   1368 O  O    . GLY A 1 71  ? -10.79900 -18.32800 18.05500  1.000 46.71000  ? 71  GLY A O    1 
ATOM   1369 H  H    . GLY A 1 71  ? -13.18100 -14.96300 18.05700  1.000 28.89000  ? 71  GLY A H    1 
ATOM   1370 H  HA2  . GLY A 1 71  ? -12.28200 -16.42400 19.32000  1.000 37.79000  ? 71  GLY A HA2  1 
ATOM   1371 H  HA3  . GLY A 1 71  ? -13.12500 -17.54200 18.59000  1.000 37.79000  ? 71  GLY A HA3  1 
ATOM   1372 N  N    . SER A 1 72  ? -10.80100 -16.46700 16.80100  1.000 26.33000  ? 72  SER A N    1 
ATOM   1373 C  CA   . SER A 1 72  ? -9.62200  -16.82600 16.03300  1.000 20.70000  ? 72  SER A CA   1 
ATOM   1374 C  C    . SER A 1 72  ? -8.36600  -16.20400 16.63400  1.000 24.60000  ? 72  SER A C    1 
ATOM   1375 O  O    . SER A 1 72  ? -8.40600  -15.42400 17.59200  1.000 25.80000  ? 72  SER A O    1 
ATOM   1376 C  CB   . SER A 1 72  ? -9.80100  -16.36500 14.57700  1.000 21.27000  ? 72  SER A CB   1 
ATOM   1377 O  OG   . SER A 1 72  ? -9.68600  -14.97200 14.47900  1.000 22.21000  ? 72  SER A OG   1 
ATOM   1378 H  H    . SER A 1 72  ? -11.13300 -15.70500 16.58200  1.000 31.59000  ? 72  SER A H    1 
ATOM   1379 H  HA   . SER A 1 72  ? -9.50700  -17.78900 16.05100  1.000 24.83000  ? 72  SER A HA   1 
ATOM   1380 H  HB2  . SER A 1 72  ? -9.11700  -16.77800 14.02800  1.000 25.51000  ? 72  SER A HB2  1 
ATOM   1381 H  HB3  . SER A 1 72  ? -10.68100 -16.63100 14.26800  1.000 25.51000  ? 72  SER A HB3  1 
ATOM   1382 H  HG   . SER A 1 72  ? -10.10900 -14.69500 13.80800  1.000 26.65000  ? 72  SER A HG   1 
ATOM   1383 N  N    . ARG A 1 73  ? -7.22500  -16.59300 16.06800  1.000 21.48000  ? 73  ARG A N    1 
ATOM   1384 C  CA   . ARG A 1 73  ? -5.93100  -16.02800 16.38200  1.000 20.42000  ? 73  ARG A CA   1 
ATOM   1385 C  C    . ARG A 1 73  ? -5.37000  -15.29400 15.16700  1.000 23.22000  ? 73  ARG A C    1 
ATOM   1386 O  O    . ARG A 1 73  ? -5.93600  -15.33100 14.07300  1.000 21.72000  ? 73  ARG A O    1 
ATOM   1387 C  CB   . ARG A 1 73  ? -4.95300  -17.11600 16.84900  1.000 23.63000  ? 73  ARG A CB   1 
ATOM   1388 C  CG   . ARG A 1 73  ? -5.47800  -18.01400 17.98000  1.000 27.52000  ? 73  ARG A CG   1 
ATOM   1389 C  CD   . ARG A 1 73  ? -5.66600  -17.24600 19.28700  1.000 41.08000  ? 73  ARG A CD   1 
ATOM   1390 N  NE   . ARG A 1 73  ? -4.42100  -16.64100 19.74700  1.000 52.40000  ? 73  ARG A NE   1 
ATOM   1391 C  CZ   . ARG A 1 73  ? -3.57000  -17.20400 20.59800  1.000 60.53000  ? 73  ARG A CZ   1 
ATOM   1392 N  NH1  . ARG A 1 73  ? -3.82100  -18.37400 21.16300  1.000 40.73000  ? 73  ARG A NH1  1 
ATOM   1393 N  NH2  . ARG A 1 73  ? -2.43600  -16.57800 20.88900  1.000 38.96000  ? 73  ARG A NH2  1 
ATOM   1394 H  H    . ARG A 1 73  ? -7.18200  -17.21200 15.47200  1.000 25.76000  ? 73  ARG A H    1 
ATOM   1395 H  HA   . ARG A 1 73  ? -6.03200  -15.38900 17.10400  1.000 24.49000  ? 73  ARG A HA   1 
ATOM   1396 H  HB2  . ARG A 1 73  ? -4.74600  -17.68900 16.09500  1.000 28.35000  ? 73  ARG A HB2  1 
ATOM   1397 H  HB3  . ARG A 1 73  ? -4.14500  -16.68600 17.17000  1.000 28.35000  ? 73  ARG A HB3  1 
ATOM   1398 H  HG2  . ARG A 1 73  ? -6.33700  -18.38300 17.72100  1.000 33.01000  ? 73  ARG A HG2  1 
ATOM   1399 H  HG3  . ARG A 1 73  ? -4.84300  -18.73000 18.14000  1.000 33.01000  ? 73  ARG A HG3  1 
ATOM   1400 H  HD2  . ARG A 1 73  ? -6.31500  -16.53800 19.15100  1.000 49.28000  ? 73  ARG A HD2  1 
ATOM   1401 H  HD3  . ARG A 1 73  ? -5.97900  -17.85500 19.97400  1.000 49.28000  ? 73  ARG A HD3  1 
ATOM   1402 H  HE   . ARG A 1 73  ? -4.22200  -15.86100 19.44500  1.000 62.87000  ? 73  ARG A HE   1 
ATOM   1403 H  HH11 . ARG A 1 73  ? -4.55200  -18.79000 20.98300  1.000 48.86000  ? 73  ARG A HH11 1 
ATOM   1404 H  HH12 . ARG A 1 73  ? -3.25400  -18.71700 21.71100  1.000 48.86000  ? 73  ARG A HH12 1 
ATOM   1405 H  HH21 . ARG A 1 73  ? -2.26000  -15.81700 20.52900  1.000 46.74000  ? 73  ARG A HH21 1 
ATOM   1406 H  HH22 . ARG A 1 73  ? -1.87800  -16.93300 21.43900  1.000 46.74000  ? 73  ARG A HH22 1 
ATOM   1407 N  N    . ASN A 1 74  ? -4.25800  -14.61100 15.38100  1.000 21.30000  ? 74  ASN A N    1 
ATOM   1408 C  CA   . ASN A 1 74  ? -3.55000  -13.80800 14.38300  1.000 17.93000  ? 74  ASN A CA   1 
ATOM   1409 C  C    . ASN A 1 74  ? -2.04400  -14.05000 14.57100  1.000 20.56000  ? 74  ASN A C    1 
ATOM   1410 O  O    . ASN A 1 74  ? -1.26400  -13.16600 14.87700  1.000 21.83000  ? 74  ASN A O    1 
ATOM   1411 C  CB   . ASN A 1 74  ? -3.91900  -12.32700 14.50900  1.000 18.96000  ? 74  ASN A CB   1 
ATOM   1412 C  CG   . ASN A 1 74  ? -3.19200  -11.43800 13.52800  1.000 21.39000  ? 74  ASN A CG   1 
ATOM   1413 O  OD1  . ASN A 1 74  ? -2.58300  -11.89100 12.56900  1.000 20.82000  ? 74  ASN A OD1  1 
ATOM   1414 N  ND2  . ASN A 1 74  ? -3.26700  -10.13500 13.75800  1.000 25.98000  ? 74  ASN A ND2  1 
ATOM   1415 H  H    . ASN A 1 74  ? -3.86400  -14.59300 16.14500  1.000 25.54000  ? 74  ASN A H    1 
ATOM   1416 H  HA   . ASN A 1 74  ? -3.79200  -14.10000 13.49000  1.000 21.51000  ? 74  ASN A HA   1 
ATOM   1417 H  HB2  . ASN A 1 74  ? -4.87100  -12.22700 14.35000  1.000 22.74000  ? 74  ASN A HB2  1 
ATOM   1418 H  HB3  . ASN A 1 74  ? -3.69800  -12.02400 15.40300  1.000 22.74000  ? 74  ASN A HB3  1 
ATOM   1419 H  HD21 . ASN A 1 74  ? -2.87100  -9.58300  13.23100  1.000 31.16000  ? 74  ASN A HD21 1 
ATOM   1420 H  HD22 . ASN A 1 74  ? -3.71100  -9.84200  14.43300  1.000 31.16000  ? 74  ASN A HD22 1 
ATOM   1421 N  N    . LEU A 1 75  ? -1.61500  -15.28900 14.31300  1.000 19.69000  ? 75  LEU A N    1 
ATOM   1422 C  CA   . LEU A 1 75  ? -0.26000  -15.67900 14.69900  1.000 21.75000  ? 75  LEU A CA   1 
ATOM   1423 C  C    . LEU A 1 75  ? 0.80700   -15.08100 13.78300  1.000 23.62000  ? 75  LEU A C    1 
ATOM   1424 O  O    . LEU A 1 75  ? 1.97700   -15.01100 14.17500  1.000 25.33000  ? 75  LEU A O    1 
ATOM   1425 C  CB   . LEU A 1 75  ? -0.19200  -17.20000 14.74400  1.000 21.69000  ? 75  LEU A CB   1 
ATOM   1426 C  CG   . LEU A 1 75  ? -0.93700  -17.84100 15.90300  1.000 27.69000  ? 75  LEU A CG   1 
ATOM   1427 C  CD1  . LEU A 1 75  ? -0.80600  -19.36300 15.88800  1.000 31.09000  ? 75  LEU A CD1  1 
ATOM   1428 C  CD2  . LEU A 1 75  ? -0.46600  -17.28800 17.26300  1.000 35.24000  ? 75  LEU A CD2  1 
ATOM   1429 H  H    . LEU A 1 75  ? -2.07700  -15.90300 13.92700  1.000 23.61000  ? 75  LEU A H    1 
ATOM   1430 H  HA   . LEU A 1 75  ? -0.05200  -15.34900 15.58700  1.000 26.09000  ? 75  LEU A HA   1 
ATOM   1431 H  HB2  . LEU A 1 75  ? -0.57500  -17.54800 13.92300  1.000 26.02000  ? 75  LEU A HB2  1 
ATOM   1432 H  HB3  . LEU A 1 75  ? 0.73800   -17.46400 14.81300  1.000 26.02000  ? 75  LEU A HB3  1 
ATOM   1433 H  HG   . LEU A 1 75  ? -1.87500  -17.61600 15.79600  1.000 33.22000  ? 75  LEU A HG   1 
ATOM   1434 H  HD11 . LEU A 1 75  ? -1.28600  -19.72800 16.64700  1.000 37.29000  ? 75  LEU A HD11 1 
ATOM   1435 H  HD12 . LEU A 1 75  ? -1.18400  -19.70400 15.06200  1.000 37.29000  ? 75  LEU A HD12 1 
ATOM   1436 H  HD13 . LEU A 1 75  ? 0.13300   -19.59900 15.94500  1.000 37.29000  ? 75  LEU A HD13 1 
ATOM   1437 H  HD21 . LEU A 1 75  ? -0.89300  -17.79300 17.97400  1.000 42.27000  ? 75  LEU A HD21 1 
ATOM   1438 H  HD22 . LEU A 1 75  ? 0.49700   -17.38000 17.32500  1.000 42.27000  ? 75  LEU A HD22 1 
ATOM   1439 H  HD23 . LEU A 1 75  ? -0.71400  -16.35300 17.32700  1.000 42.27000  ? 75  LEU A HD23 1 
ATOM   1440 N  N    . CYS A 1 76  ? 0.46000   -14.65200 12.56700  1.000 17.93000  ? 76  CYS A N    1 
ATOM   1441 C  CA   . CYS A 1 76  ? 1.40300   -13.94300 11.72400  1.000 17.96000  ? 76  CYS A CA   1 
ATOM   1442 C  C    . CYS A 1 76  ? 1.38300   -12.43800 11.94800  1.000 19.32000  ? 76  CYS A C    1 
ATOM   1443 O  O    . CYS A 1 76  ? 2.16800   -11.71700 11.33000  1.000 21.38000  ? 76  CYS A O    1 
ATOM   1444 C  CB   . CYS A 1 76  ? 1.16900   -14.26000 10.23600  1.000 18.37000  ? 76  CYS A CB   1 
ATOM   1445 S  SG   . CYS A 1 76  ? 1.68400   -15.95200 9.84700   1.000 18.30000  ? 76  CYS A SG   1 
ATOM   1446 H  H    . CYS A 1 76  ? -0.31700  -14.76300 12.21500  1.000 21.50000  ? 76  CYS A H    1 
ATOM   1447 H  HA   . CYS A 1 76  ? 2.29400   -14.26200 11.93900  1.000 21.54000  ? 76  CYS A HA   1 
ATOM   1448 H  HB2  . CYS A 1 76  ? 0.22400   -14.17100 10.03200  1.000 22.03000  ? 76  CYS A HB2  1 
ATOM   1449 H  HB3  . CYS A 1 76  ? 1.68500   -13.64700 9.69000   1.000 22.03000  ? 76  CYS A HB3  1 
ATOM   1450 N  N    A ASN A 1 77  ? 0.48200   -11.96600 12.81000  0.550 20.46000  ? 77  ASN A N    1 
ATOM   1451 N  N    B ASN A 1 77  ? 0.51200   -11.94500 12.82500  0.450 20.64000  ? 77  ASN A N    1 
ATOM   1452 C  CA   A ASN A 1 77  ? 0.41000   -10.56100 13.22000  0.550 20.82000  ? 77  ASN A CA   1 
ATOM   1453 C  CA   B ASN A 1 77  ? 0.47700   -10.52700 13.19700  0.450 20.85000  ? 77  ASN A CA   1 
ATOM   1454 C  C    A ASN A 1 77  ? 0.27400   -9.63300  12.01500  0.550 22.10000  ? 77  ASN A C    1 
ATOM   1455 C  C    B ASN A 1 77  ? 0.29900   -9.62800  11.97700  0.450 22.16000  ? 77  ASN A C    1 
ATOM   1456 O  O    A ASN A 1 77  ? 1.03000   -8.67900  11.83500  0.550 23.63000  ? 77  ASN A O    1 
ATOM   1457 O  O    B ASN A 1 77  ? 1.06300   -8.68800  11.74500  0.450 23.54000  ? 77  ASN A O    1 
ATOM   1458 C  CB   A ASN A 1 77  ? 1.58800   -10.17800 14.12100  0.550 27.53000  ? 77  ASN A CB   1 
ATOM   1459 C  CB   B ASN A 1 77  ? 1.71500   -10.11600 14.00000  0.450 26.47000  ? 77  ASN A CB   1 
ATOM   1460 C  CG   A ASN A 1 77  ? 1.63000   -11.00800 15.39300  0.550 29.21000  ? 77  ASN A CG   1 
ATOM   1461 C  CG   B ASN A 1 77  ? 1.54300   -8.76800  14.67200  0.450 33.00000  ? 77  ASN A CG   1 
ATOM   1462 O  OD1  A ASN A 1 77  ? 2.52300   -11.83700 15.58200  0.550 37.35000  ? 77  ASN A OD1  1 
ATOM   1463 O  OD1  B ASN A 1 77  ? 0.47000   -8.44900  15.18200  0.450 31.72000  ? 77  ASN A OD1  1 
ATOM   1464 N  ND2  A ASN A 1 77  ? 0.65200   -10.79900 16.26900  0.550 39.49000  ? 77  ASN A ND2  1 
ATOM   1465 N  ND2  B ASN A 1 77  ? 2.60500   -7.96800  14.67500  0.450 35.33000  ? 77  ASN A ND2  1 
ATOM   1466 H  H    A ASN A 1 77  ? -0.11800  -12.45500 13.18400  0.550 24.53000  ? 77  ASN A H    1 
ATOM   1467 H  H    B ASN A 1 77  ? -0.08200  -12.41900 13.22800  0.450 24.76000  ? 77  ASN A H    1 
ATOM   1468 H  HA   A ASN A 1 77  ? -0.39500  -10.44000 13.74700  0.550 24.97000  ? 77  ASN A HA   1 
ATOM   1469 H  HA   B ASN A 1 77  ? -0.29800  -10.39900 13.76600  0.450 25.01000  ? 77  ASN A HA   1 
ATOM   1470 H  HB2  A ASN A 1 77  ? 2.41700   -10.32200 13.63900  0.550 33.02000  ? 77  ASN A HB2  1 
ATOM   1471 H  HB2  B ASN A 1 77  ? 1.88000   -10.77800 14.69000  0.450 31.75000  ? 77  ASN A HB2  1 
ATOM   1472 H  HB3  A ASN A 1 77  ? 1.50700   -9.24500  14.37100  0.550 33.02000  ? 77  ASN A HB3  1 
ATOM   1473 H  HB3  B ASN A 1 77  ? 2.47700   -10.06100 13.40300  0.450 31.75000  ? 77  ASN A HB3  1 
ATOM   1474 H  HD21 A ASN A 1 77  ? 0.04000   -10.21900 16.10000  0.550 47.37000  ? 77  ASN A HD21 1 
ATOM   1475 H  HD21 B ASN A 1 77  ? 3.33800   -8.22500  14.30800  0.450 42.38000  ? 77  ASN A HD21 1 
ATOM   1476 H  HD22 A ASN A 1 77  ? 0.63200   -11.24400 17.00500  0.550 47.37000  ? 77  ASN A HD22 1 
ATOM   1477 H  HD22 B ASN A 1 77  ? 2.55800   -7.19200  15.04400  0.450 42.38000  ? 77  ASN A HD22 1 
ATOM   1478 N  N    . ILE A 1 78  ? -0.73200  -9.91500  11.18900  1.000 19.71000  ? 78  ILE A N    1 
ATOM   1479 C  CA   . ILE A 1 78  ? -0.94900  -9.16200  9.96200   1.000 21.54000  ? 78  ILE A CA   1 
ATOM   1480 C  C    . ILE A 1 78  ? -2.43500  -9.09700  9.64100   1.000 16.07000  ? 78  ILE A C    1 
ATOM   1481 O  O    . ILE A 1 78  ? -3.19300  -10.01400 9.98500   1.000 17.74000  ? 78  ILE A O    1 
ATOM   1482 C  CB   . ILE A 1 78  ? -0.23300  -9.78500  8.75300   1.000 22.08000  ? 78  ILE A CB   1 
ATOM   1483 C  CG1  . ILE A 1 78  ? -0.52200  -11.27900 8.67200   1.000 22.94000  ? 78  ILE A CG1  1 
ATOM   1484 C  CG2  . ILE A 1 78  ? 1.26200   -9.48300  8.78200   1.000 38.84000  ? 78  ILE A CG2  1 
ATOM   1485 C  CD1  . ILE A 1 78  ? -0.35200  -11.82900 7.27400   1.000 31.26000  ? 78  ILE A CD1  1 
ATOM   1486 H  H    . ILE A 1 78  ? -1.30500  -10.54200 11.32000  1.000 23.64000  ? 78  ILE A H    1 
ATOM   1487 H  HA   . ILE A 1 78  ? -0.60400  -8.27100  10.12900  1.000 25.84000  ? 78  ILE A HA   1 
ATOM   1488 H  HB   . ILE A 1 78  ? -0.58400  -9.37900  7.94500   1.000 26.48000  ? 78  ILE A HB   1 
ATOM   1489 H  HG12 . ILE A 1 78  ? 0.09000   -11.75100 9.25800   1.000 27.52000  ? 78  ILE A HG12 1 
ATOM   1490 H  HG13 . ILE A 1 78  ? -1.43700  -11.43900 8.95000   1.000 27.52000  ? 78  ILE A HG13 1 
ATOM   1491 H  HG21 . ILE A 1 78  ? 1.68100   -9.88800  8.00700   1.000 46.59000  ? 78  ILE A HG21 1 
ATOM   1492 H  HG22 . ILE A 1 78  ? 1.39000   -8.52100  8.76300   1.000 46.59000  ? 78  ILE A HG22 1 
ATOM   1493 H  HG23 . ILE A 1 78  ? 1.64300   -9.85100  9.59400   1.000 46.59000  ? 78  ILE A HG23 1 
ATOM   1494 H  HD11 . ILE A 1 78  ? -0.54600  -12.77900 7.28300   1.000 37.50000  ? 78  ILE A HD11 1 
ATOM   1495 H  HD12 . ILE A 1 78  ? -0.96500  -11.37100 6.67800   1.000 37.50000  ? 78  ILE A HD12 1 
ATOM   1496 H  HD13 . ILE A 1 78  ? 0.56200   -11.68100 6.98600   1.000 37.50000  ? 78  ILE A HD13 1 
ATOM   1497 N  N    . PRO A 1 79  ? -2.88500  -8.01800  9.01900   1.000 18.57000  ? 79  PRO A N    1 
ATOM   1498 C  CA   . PRO A 1 79  ? -4.23400  -8.02600  8.45100   1.000 16.29000  ? 79  PRO A CA   1 
ATOM   1499 C  C    . PRO A 1 79  ? -4.28300  -8.98400  7.27400   1.000 16.52000  ? 79  PRO A C    1 
ATOM   1500 O  O    . PRO A 1 79  ? -3.36300  -9.04700  6.45800   1.000 16.39000  ? 79  PRO A O    1 
ATOM   1501 C  CB   . PRO A 1 79  ? -4.45400  -6.57100  8.02200   1.000 18.37000  ? 79  PRO A CB   1 
ATOM   1502 C  CG   . PRO A 1 79  ? -3.10900  -5.97900  7.87200   1.000 26.50000  ? 79  PRO A CG   1 
ATOM   1503 C  CD   . PRO A 1 79  ? -2.17900  -6.74700  8.78800   1.000 20.45000  ? 79  PRO A CD   1 
ATOM   1504 H  HA   . PRO A 1 79  ? -4.90800  -8.25900  9.10800   1.000 19.54000  ? 79  PRO A HA   1 
ATOM   1505 H  HB2  . PRO A 1 79  ? -4.93500  -6.54900  7.18000   1.000 22.04000  ? 79  PRO A HB2  1 
ATOM   1506 H  HB3  . PRO A 1 79  ? -4.96000  -6.10300  8.70500   1.000 22.04000  ? 79  PRO A HB3  1 
ATOM   1507 H  HG2  . PRO A 1 79  ? -2.82200  -6.06400  6.95000   1.000 31.79000  ? 79  PRO A HG2  1 
ATOM   1508 H  HG3  . PRO A 1 79  ? -3.13900  -5.04400  8.12600   1.000 31.79000  ? 79  PRO A HG3  1 
ATOM   1509 H  HD2  . PRO A 1 79  ? -1.32400  -6.90200  8.35700   1.000 24.53000  ? 79  PRO A HD2  1 
ATOM   1510 H  HD3  . PRO A 1 79  ? -2.04900  -6.27000  9.62300   1.000 24.53000  ? 79  PRO A HD3  1 
ATOM   1511 N  N    . CYS A 1 80  ? -5.37400  -9.73100  7.18500   1.000 14.34000  ? 80  CYS A N    1 
ATOM   1512 C  CA   . CYS A 1 80  ? -5.50100  -10.69300 6.09300   1.000 13.14000  ? 80  CYS A CA   1 
ATOM   1513 C  C    . CYS A 1 80  ? -5.38900  -10.03600 4.72400   1.000 16.02000  ? 80  CYS A C    1 
ATOM   1514 O  O    . CYS A 1 80  ? -4.86600  -10.64700 3.78300   1.000 15.64000  ? 80  CYS A O    1 
ATOM   1515 C  CB   . CYS A 1 80  ? -6.79100  -11.48700 6.21400   1.000 14.85000  ? 80  CYS A CB   1 
ATOM   1516 S  SG   . CYS A 1 80  ? -6.93700  -12.49000 7.73200   1.000 14.71000  ? 80  CYS A SG   1 
ATOM   1517 H  H    . CYS A 1 80  ? -6.04000  -9.70500  7.72800   1.000 17.20000  ? 80  CYS A H    1 
ATOM   1518 H  HA   . CYS A 1 80  ? -4.76800  -11.32400 6.16800   1.000 15.75000  ? 80  CYS A HA   1 
ATOM   1519 H  HB2  . CYS A 1 80  ? -7.53600  -10.86600 6.20300   1.000 17.81000  ? 80  CYS A HB2  1 
ATOM   1520 H  HB3  . CYS A 1 80  ? -6.85200  -12.09200 5.45900   1.000 17.81000  ? 80  CYS A HB3  1 
ATOM   1521 N  N    . SER A 1 81  ? -5.87300  -8.80000  4.57700   1.000 17.38000  ? 81  SER A N    1 
ATOM   1522 C  CA   . SER A 1 81  ? -5.81100  -8.12600  3.28500   1.000 16.43000  ? 81  SER A CA   1 
ATOM   1523 C  C    . SER A 1 81  ? -4.39800  -7.92100  2.77900   1.000 18.12000  ? 81  SER A C    1 
ATOM   1524 O  O    . SER A 1 81  ? -4.20300  -7.83200  1.55800   1.000 20.23000  ? 81  SER A O    1 
ATOM   1525 C  CB   . SER A 1 81  ? -6.57400  -6.80400  3.36400   1.000 24.80000  ? 81  SER A CB   1 
ATOM   1526 O  OG   . SER A 1 81  ? -5.99100  -5.95600  4.33300   1.000 26.16000  ? 81  SER A OG   1 
ATOM   1527 H  H    . SER A 1 81  ? -6.23800  -8.33700  5.20300   1.000 20.84000  ? 81  SER A H    1 
ATOM   1528 H  HA   . SER A 1 81  ? -6.24900  -8.68300  2.62200   1.000 19.70000  ? 81  SER A HA   1 
ATOM   1529 H  HB2  . SER A 1 81  ? -6.54200  -6.36700  2.49900   1.000 29.74000  ? 81  SER A HB2  1 
ATOM   1530 H  HB3  . SER A 1 81  ? -7.49500  -6.98300  3.61200   1.000 29.74000  ? 81  SER A HB3  1 
ATOM   1531 H  HG   . SER A 1 81  ? -6.24000  -6.18500  5.10200   1.000 31.38000  ? 81  SER A HG   1 
ATOM   1532 N  N    . ALA A 1 82  ? -3.40400  -7.89700  3.66200   1.000 17.86000  ? 82  ALA A N    1 
ATOM   1533 C  CA   . ALA A 1 82  ? -2.02100  -7.79900  3.21200   1.000 21.81000  ? 82  ALA A CA   1 
ATOM   1534 C  C    . ALA A 1 82  ? -1.61000  -9.00700  2.38900   1.000 24.09000  ? 82  ALA A C    1 
ATOM   1535 O  O    . ALA A 1 82  ? -0.64400  -8.94100  1.60700   1.000 24.33000  ? 82  ALA A O    1 
ATOM   1536 C  CB   . ALA A 1 82  ? -1.06500  -7.72600  4.41000   1.000 24.86000  ? 82  ALA A CB   1 
ATOM   1537 H  H    . ALA A 1 82  ? -3.50200  -7.93500  4.51600   1.000 21.42000  ? 82  ALA A H    1 
ATOM   1538 H  HA   . ALA A 1 82  ? -1.94100  -6.98900  2.68400   1.000 26.15000  ? 82  ALA A HA   1 
ATOM   1539 H  HB1  . ALA A 1 82  ? -0.15700  -7.61900  4.08400   1.000 29.81000  ? 82  ALA A HB1  1 
ATOM   1540 H  HB2  . ALA A 1 82  ? -1.30900  -6.96700  4.96300   1.000 29.81000  ? 82  ALA A HB2  1 
ATOM   1541 H  HB3  . ALA A 1 82  ? -1.13800  -8.54600  4.92300   1.000 29.81000  ? 82  ALA A HB3  1 
ATOM   1542 N  N    . LEU A 1 83  ? -2.29000  -10.11300 2.56900   1.000 17.93000  ? 83  LEU A N    1 
ATOM   1543 C  CA   . LEU A 1 83  ? -1.96800  -11.32900 1.83800   1.000 16.95000  ? 83  LEU A CA   1 
ATOM   1544 C  C    . LEU A 1 83  ? -2.47100  -11.30300 0.41300   1.000 20.66000  ? 83  LEU A C    1 
ATOM   1545 O  O    . LEU A 1 83  ? -2.23700  -12.27700 -0.31200  1.000 22.59000  ? 83  LEU A O    1 
ATOM   1546 C  CB   . LEU A 1 83  ? -2.54200  -12.54400 2.54700   1.000 18.37000  ? 83  LEU A CB   1 
ATOM   1547 C  CG   . LEU A 1 83  ? -2.04700  -12.78300 3.96700   1.000 18.98000  ? 83  LEU A CG   1 
ATOM   1548 C  CD1  . LEU A 1 83  ? -2.88400  -13.78600 4.71600   1.000 22.09000  ? 83  LEU A CD1  1 
ATOM   1549 C  CD2  . LEU A 1 83  ? -0.56600  -13.25300 3.91000   1.000 25.47000  ? 83  LEU A CD2  1 
ATOM   1550 H  H    . LEU A 1 83  ? -2.95000  -10.19400 3.11400   1.000 21.51000  ? 83  LEU A H    1 
ATOM   1551 H  HA   . LEU A 1 83  ? -1.00300  -11.42300 1.82000   1.000 20.33000  ? 83  LEU A HA   1 
ATOM   1552 H  HB2  . LEU A 1 83  ? -3.50600  -12.44000 2.59200   1.000 22.03000  ? 83  LEU A HB2  1 
ATOM   1553 H  HB3  . LEU A 1 83  ? -2.31700  -13.33100 2.02700   1.000 22.03000  ? 83  LEU A HB3  1 
ATOM   1554 H  HG   . LEU A 1 83  ? -2.11600  -11.95200 4.46200   1.000 22.76000  ? 83  LEU A HG   1 
ATOM   1555 H  HD11 . LEU A 1 83  ? -2.48600  -13.94100 5.58700   1.000 26.49000  ? 83  LEU A HD11 1 
ATOM   1556 H  HD12 . LEU A 1 83  ? -3.78100  -13.43300 4.82100   1.000 26.49000  ? 83  LEU A HD12 1 
ATOM   1557 H  HD13 . LEU A 1 83  ? -2.91100  -14.61400 4.21200   1.000 26.49000  ? 83  LEU A HD13 1 
ATOM   1558 H  HD21 . LEU A 1 83  ? -0.31800  -13.62200 4.77200   1.000 30.55000  ? 83  LEU A HD21 1 
ATOM   1559 H  HD22 . LEU A 1 83  ? -0.47600  -13.93100 3.22200   1.000 30.55000  ? 83  LEU A HD22 1 
ATOM   1560 H  HD23 . LEU A 1 83  ? -0.00100  -12.49300 3.70000   1.000 30.55000  ? 83  LEU A HD23 1 
ATOM   1561 N  N    . LEU A 1 84  ? -3.20300  -10.26300 0.01700   1.000 17.16000  ? 84  LEU A N    1 
ATOM   1562 C  CA   . LEU A 1 84  ? -3.73100  -10.15400 -1.33000  1.000 20.08000  ? 84  LEU A CA   1 
ATOM   1563 C  C    . LEU A 1 84  ? -2.88100  -9.28000  -2.23400  1.000 21.19000  ? 84  LEU A C    1 
ATOM   1564 O  O    . LEU A 1 84  ? -3.22200  -9.12900  -3.41700  1.000 23.45000  ? 84  LEU A O    1 
ATOM   1565 C  CB   . LEU A 1 84  ? -5.18000  -9.62900  -1.29000  1.000 18.30000  ? 84  LEU A CB   1 
ATOM   1566 C  CG   . LEU A 1 84  ? -6.09800  -10.41800 -0.34800  1.000 17.97000  ? 84  LEU A CG   1 
ATOM   1567 C  CD1  . LEU A 1 84  ? -7.47700  -9.79600  -0.33000  1.000 28.47000  ? 84  LEU A CD1  1 
ATOM   1568 C  CD2  . LEU A 1 84  ? -6.20200  -11.86000 -0.77400  1.000 18.31000  ? 84  LEU A CD2  1 
ATOM   1569 H  H    . LEU A 1 84  ? -3.40700  -9.59900  0.52300   1.000 20.58000  ? 84  LEU A H    1 
ATOM   1570 H  HA   . LEU A 1 84  ? -3.75200  -11.03900 -1.72500  1.000 24.08000  ? 84  LEU A HA   1 
ATOM   1571 H  HB2  . LEU A 1 84  ? -5.16900  -8.70600  -0.99000  1.000 21.95000  ? 84  LEU A HB2  1 
ATOM   1572 H  HB3  . LEU A 1 84  ? -5.55500  -9.68200  -2.18300  1.000 21.95000  ? 84  LEU A HB3  1 
ATOM   1573 H  HG   . LEU A 1 84  ? -5.72100  -10.39200 0.54500   1.000 21.55000  ? 84  LEU A HG   1 
ATOM   1574 H  HD11 . LEU A 1 84  ? -8.05000  -10.31600 0.25500   1.000 34.15000  ? 84  LEU A HD11 1 
ATOM   1575 H  HD12 . LEU A 1 84  ? -7.40800  -8.88600  -0.00300  1.000 34.15000  ? 84  LEU A HD12 1 
ATOM   1576 H  HD13 . LEU A 1 84  ? -7.83500  -9.79700  -1.23100  1.000 34.15000  ? 84  LEU A HD13 1 
ATOM   1577 H  HD21 . LEU A 1 84  ? -6.75300  -12.33900 -0.13500  1.000 21.96000  ? 84  LEU A HD21 1 
ATOM   1578 H  HD22 . LEU A 1 84  ? -6.60700  -11.90100 -1.65500  1.000 21.96000  ? 84  LEU A HD22 1 
ATOM   1579 H  HD23 . LEU A 1 84  ? -5.31300  -12.24700 -0.80000  1.000 21.96000  ? 84  LEU A HD23 1 
ATOM   1580 N  N    A SER A 1 85  ? -1.78700  -8.73100  -1.71500  0.600 22.31000  ? 85  SER A N    1 
ATOM   1581 N  N    B SER A 1 85  ? -1.81600  -8.67300  -1.71500  0.400 22.24000  ? 85  SER A N    1 
ATOM   1582 C  CA   A SER A 1 85  ? -0.94300  -7.79600  -2.44100  0.600 24.04000  ? 85  SER A CA   1 
ATOM   1583 C  CA   B SER A 1 85  ? -1.03300  -7.74400  -2.51400  0.400 24.12000  ? 85  SER A CA   1 
ATOM   1584 C  C    A SER A 1 85  ? -0.19200  -8.48000  -3.58800  0.600 23.97000  ? 85  SER A C    1 
ATOM   1585 C  C    B SER A 1 85  ? -0.27300  -8.46700  -3.62600  0.400 24.06000  ? 85  SER A C    1 
ATOM   1586 O  O    A SER A 1 85  ? 0.04400   -9.69000  -3.58500  0.600 24.10000  ? 85  SER A O    1 
ATOM   1587 O  O    B SER A 1 85  ? -0.12600  -9.68900  -3.63600  0.400 24.14000  ? 85  SER A O    1 
ATOM   1588 C  CB   A SER A 1 85  ? 0.05800   -7.19100  -1.45700  0.600 26.79000  ? 85  SER A CB   1 
ATOM   1589 C  CB   B SER A 1 85  ? -0.03500  -6.98700  -1.63800  0.400 29.65000  ? 85  SER A CB   1 
ATOM   1590 O  OG   A SER A 1 85  ? 1.11800   -6.54500  -2.11400  0.600 22.58000  ? 85  SER A OG   1 
ATOM   1591 O  OG   B SER A 1 85  ? 0.82000   -7.87700  -0.95000  0.400 32.56000  ? 85  SER A OG   1 
ATOM   1592 H  H    A SER A 1 85  ? -1.50400  -8.89000  -0.91900  0.600 26.76000  ? 85  SER A H    1 
ATOM   1593 H  H    B SER A 1 85  ? -1.53200  -8.78300  -0.91100  0.400 26.68000  ? 85  SER A H    1 
ATOM   1594 H  HA   A SER A 1 85  ? -1.48800  -7.09700  -2.83800  0.600 28.83000  ? 85  SER A HA   1 
ATOM   1595 H  HA   B SER A 1 85  ? -1.63900  -7.10700  -2.92300  0.400 28.94000  ? 85  SER A HA   1 
ATOM   1596 H  HB2  A SER A 1 85  ? -0.40300  -6.54400  -0.90100  0.600 32.13000  ? 85  SER A HB2  1 
ATOM   1597 H  HB2  B SER A 1 85  ? 0.50200   -6.40900  -2.20200  0.400 35.57000  ? 85  SER A HB2  1 
ATOM   1598 H  HB3  A SER A 1 85  ? 0.42100   -7.90200  -0.90600  0.600 32.13000  ? 85  SER A HB3  1 
ATOM   1599 H  HB3  B SER A 1 85  ? -0.52400  -6.45700  -0.99000  0.400 35.57000  ? 85  SER A HB3  1 
ATOM   1600 H  HG   A SER A 1 85  ? 1.71300   -6.33300  -1.56000  0.600 27.09000  ? 85  SER A HG   1 
ATOM   1601 H  HG   B SER A 1 85  ? 1.20100   -8.39000  -1.49500  0.400 39.06000  ? 85  SER A HG   1 
ATOM   1602 N  N    . SER A 1 86  ? 0.20300   -7.67600  -4.58500  1.000 21.24000  ? 86  SER A N    1 
ATOM   1603 C  CA   . SER A 1 86  ? 1.03700   -8.20800  -5.66100  1.000 24.11000  ? 86  SER A CA   1 
ATOM   1604 C  C    . SER A 1 86  ? 2.43000   -8.56300  -5.16400  1.000 23.32000  ? 86  SER A C    1 
ATOM   1605 O  O    . SER A 1 86  ? 3.11100   -9.38100  -5.79300  1.000 28.14000  ? 86  SER A O    1 
ATOM   1606 C  CB   . SER A 1 86  ? 1.16500   -7.17900  -6.78500  1.000 30.75000  ? 86  SER A CB   1 
ATOM   1607 O  OG   . SER A 1 86  ? 1.40600   -5.89500  -6.25000  1.000 41.98000  ? 86  SER A OG   1 
ATOM   1608 H  H    . SER A 1 86  ? 0.00500   -6.84200  -4.65400  1.000 25.47000  ? 86  SER A H    1 
ATOM   1609 H  HA   . SER A 1 86  ? 0.61300   -9.00300  -6.01900  1.000 28.92000  ? 86  SER A HA   1 
ATOM   1610 H  HB2  . SER A 1 86  ? 1.90500   -7.42700  -7.36100  1.000 36.88000  ? 86  SER A HB2  1 
ATOM   1611 H  HB3  . SER A 1 86  ? 0.34000   -7.16100  -7.29500  1.000 36.88000  ? 86  SER A HB3  1 
ATOM   1612 H  HG   . SER A 1 86  ? 1.46800   -5.33200  -6.87000  1.000 50.36000  ? 86  SER A HG   1 
ATOM   1613 N  N    . ASP A 1 87  ? 2.84300   -7.99300  -4.03900  1.000 21.33000  ? 87  ASP A N    1 
ATOM   1614 C  CA   . ASP A 1 87  ? 4.09300   -8.31600  -3.36400  1.000 21.89000  ? 87  ASP A CA   1 
ATOM   1615 C  C    . ASP A 1 87  ? 3.81600   -9.47400  -2.41900  1.000 22.83000  ? 87  ASP A C    1 
ATOM   1616 O  O    . ASP A 1 87  ? 3.04100   -9.32100  -1.46900  1.000 22.12000  ? 87  ASP A O    1 
ATOM   1617 C  CB   . ASP A 1 87  ? 4.52800   -7.08400  -2.57100  1.000 27.81000  ? 87  ASP A CB   1 
ATOM   1618 C  CG   . ASP A 1 87  ? 5.79200   -7.30300  -1.75300  1.000 35.54000  ? 87  ASP A CG   1 
ATOM   1619 O  OD1  . ASP A 1 87  ? 6.30300   -8.43100  -1.69900  1.000 28.41000  ? 87  ASP A OD1  1 
ATOM   1620 O  OD2  . ASP A 1 87  ? 6.28600   -6.31600  -1.16700  1.000 47.05000  ? 87  ASP A OD2  1 
ATOM   1621 H  H    . ASP A 1 87  ? 2.39400   -7.38600  -3.62700  1.000 25.59000  ? 87  ASP A H    1 
ATOM   1622 H  HA   . ASP A 1 87  ? 4.79100   -8.57200  -3.98600  1.000 26.26000  ? 87  ASP A HA   1 
ATOM   1623 H  HB2  . ASP A 1 87  ? 4.69800   -6.35700  -3.19000  1.000 33.36000  ? 87  ASP A HB2  1 
ATOM   1624 H  HB3  . ASP A 1 87  ? 3.81700   -6.83900  -1.95800  1.000 33.36000  ? 87  ASP A HB3  1 
ATOM   1625 N  N    . ILE A 1 88  ? 4.43900   -10.62400 -2.68000  1.000 19.13000  ? 88  ILE A N    1 
ATOM   1626 C  CA   . ILE A 1 88  ? 4.13600   -11.83500 -1.91400  1.000 17.19000  ? 88  ILE A CA   1 
ATOM   1627 C  C    . ILE A 1 88  ? 4.92500   -11.95600 -0.62200  1.000 17.97000  ? 88  ILE A C    1 
ATOM   1628 O  O    . ILE A 1 88  ? 4.87500   -12.99800 0.03600   1.000 17.01000  ? 88  ILE A O    1 
ATOM   1629 C  CB   . ILE A 1 88  ? 4.30200   -13.11100 -2.75800  1.000 19.65000  ? 88  ILE A CB   1 
ATOM   1630 C  CG1  . ILE A 1 88  ? 5.78200   -13.31800 -3.14600  1.000 23.20000  ? 88  ILE A CG1  1 
ATOM   1631 C  CG2  . ILE A 1 88  ? 3.40200   -13.05800 -3.99100  1.000 25.81000  ? 88  ILE A CG2  1 
ATOM   1632 C  CD1  . ILE A 1 88  ? 6.06100   -14.70700 -3.69900  1.000 28.74000  ? 88  ILE A CD1  1 
ATOM   1633 H  H    . ILE A 1 88  ? 5.03500   -10.72800 -3.29100  1.000 22.95000  ? 88  ILE A H    1 
ATOM   1634 H  HA   . ILE A 1 88  ? 3.20900   -11.73400 -1.64900  1.000 20.62000  ? 88  ILE A HA   1 
ATOM   1635 H  HB   . ILE A 1 88  ? 4.02900   -13.87200 -2.22300  1.000 23.57000  ? 88  ILE A HB   1 
ATOM   1636 H  HG12 . ILE A 1 88  ? 6.02200   -12.67000 -3.82800  1.000 27.83000  ? 88  ILE A HG12 1 
ATOM   1637 H  HG13 . ILE A 1 88  ? 6.33400   -13.19100 -2.35900  1.000 27.83000  ? 88  ILE A HG13 1 
ATOM   1638 H  HG21 . ILE A 1 88  ? 3.31500   -13.95200 -4.35800  1.000 30.96000  ? 88  ILE A HG21 1 
ATOM   1639 H  HG22 . ILE A 1 88  ? 2.53000   -12.72100 -3.73100  1.000 30.96000  ? 88  ILE A HG22 1 
ATOM   1640 H  HG23 . ILE A 1 88  ? 3.80200   -12.46800 -4.64900  1.000 30.96000  ? 88  ILE A HG23 1 
ATOM   1641 H  HD11 . ILE A 1 88  ? 6.98800   -14.75400 -3.98200  1.000 34.48000  ? 88  ILE A HD11 1 
ATOM   1642 H  HD12 . ILE A 1 88  ? 5.89400   -15.36300 -3.00400  1.000 34.48000  ? 88  ILE A HD12 1 
ATOM   1643 H  HD13 . ILE A 1 88  ? 5.47500   -14.87000 -4.45500  1.000 34.48000  ? 88  ILE A HD13 1 
ATOM   1644 N  N    . THR A 1 89  ? 5.63900   -10.90900 -0.21600  1.000 20.63000  ? 89  THR A N    1 
ATOM   1645 C  CA   . THR A 1 89  ? 6.48700   -11.00600 0.96700   1.000 17.64000  ? 89  THR A CA   1 
ATOM   1646 C  C    . THR A 1 89  ? 5.71200   -11.48100 2.20500   1.000 17.08000  ? 89  THR A C    1 
ATOM   1647 O  O    . THR A 1 89  ? 6.16600   -12.37100 2.93800   1.000 18.79000  ? 89  THR A O    1 
ATOM   1648 C  CB   . THR A 1 89  ? 7.17000   -9.66200  1.22000   1.000 23.57000  ? 89  THR A CB   1 
ATOM   1649 O  OG1  . THR A 1 89  ? 7.97800   -9.35000  0.09300   1.000 25.85000  ? 89  THR A OG1  1 
ATOM   1650 C  CG2  . THR A 1 89  ? 8.05800   -9.72700  2.44100   1.000 27.34000  ? 89  THR A CG2  1 
ATOM   1651 H  H    . THR A 1 89  ? 5.65000   -10.14100 -0.60200  1.000 24.75000  ? 89  THR A H    1 
ATOM   1652 H  HA   . THR A 1 89  ? 7.17400   -11.67000 0.79800   1.000 21.16000  ? 89  THR A HA   1 
ATOM   1653 H  HB   . THR A 1 89  ? 6.49800   -8.97700  1.36700   1.000 28.27000  ? 89  THR A HB   1 
ATOM   1654 H  HG1  . THR A 1 89  ? 8.79000   -9.36800  0.30800   1.000 31.01000  ? 89  THR A HG1  1 
ATOM   1655 H  HG21 . THR A 1 89  ? 8.67100   -8.97500  2.44600   1.000 32.79000  ? 89  THR A HG21 1 
ATOM   1656 H  HG22 . THR A 1 89  ? 7.51800   -9.69700  3.24700   1.000 32.79000  ? 89  THR A HG22 1 
ATOM   1657 H  HG23 . THR A 1 89  ? 8.57100   -10.55000 2.43500   1.000 32.79000  ? 89  THR A HG23 1 
ATOM   1658 N  N    . ALA A 1 90  ? 4.56900   -10.86900 2.49900   1.000 17.19000  ? 90  ALA A N    1 
ATOM   1659 C  CA   . ALA A 1 90  ? 3.85200   -11.24700 3.71000   1.000 19.49000  ? 90  ALA A CA   1 
ATOM   1660 C  C    . ALA A 1 90  ? 3.36500   -12.68600 3.63000   1.000 16.99000  ? 90  ALA A C    1 
ATOM   1661 O  O    . ALA A 1 90  ? 3.38000   -13.41700 4.63700   1.000 18.17000  ? 90  ALA A O    1 
ATOM   1662 C  CB   . ALA A 1 90  ? 2.69100   -10.28100 3.98000   1.000 21.03000  ? 90  ALA A CB   1 
ATOM   1663 H  H    . ALA A 1 90  ? 4.19800   -10.25200 2.02900   1.000 20.62000  ? 90  ALA A H    1 
ATOM   1664 H  HA   . ALA A 1 90  ? 4.45700   -11.17900 4.46500   1.000 23.37000  ? 90  ALA A HA   1 
ATOM   1665 H  HB1  . ALA A 1 90  ? 2.27900   -10.51100 4.82700   1.000 25.23000  ? 90  ALA A HB1  1 
ATOM   1666 H  HB2  . ALA A 1 90  ? 3.03600   -9.37500  4.01600   1.000 25.23000  ? 90  ALA A HB2  1 
ATOM   1667 H  HB3  . ALA A 1 90  ? 2.04100   -10.35900 3.26400   1.000 25.23000  ? 90  ALA A HB3  1 
ATOM   1668 N  N    . SER A 1 91  ? 2.91600   -13.11300 2.44900   1.000 15.95000  ? 91  SER A N    1 
ATOM   1669 C  CA   . SER A 1 91  ? 2.45500   -14.49300 2.31700   1.000 15.86000  ? 91  SER A CA   1 
ATOM   1670 C  C    . SER A 1 91  ? 3.60500   -15.46000 2.54500   1.000 15.18000  ? 91  SER A C    1 
ATOM   1671 O  O    . SER A 1 91  ? 3.42900   -16.47800 3.21700   1.000 16.75000  ? 91  SER A O    1 
ATOM   1672 C  CB   . SER A 1 91  ? 1.86100   -14.72900 0.94100   1.000 17.45000  ? 91  SER A CB   1 
ATOM   1673 O  OG   . SER A 1 91  ? 0.55600   -14.19800 0.86700   1.000 18.26000  ? 91  SER A OG   1 
ATOM   1674 H  H    . SER A 1 91  ? 2.86900   -12.64000 1.73300   1.000 19.12000  ? 91  SER A H    1 
ATOM   1675 H  HA   . SER A 1 91  ? 1.76200   -14.65300 2.97700   1.000 19.02000  ? 91  SER A HA   1 
ATOM   1676 H  HB2  . SER A 1 91  ? 2.41800   -14.29400 0.27700   1.000 20.92000  ? 91  SER A HB2  1 
ATOM   1677 H  HB3  . SER A 1 91  ? 1.82500   -15.68300 0.77100   1.000 20.92000  ? 91  SER A HB3  1 
ATOM   1678 H  HG   . SER A 1 91  ? 0.27900   -14.22600 0.07500   1.000 21.90000  ? 91  SER A HG   1 
ATOM   1679 N  N    . VAL A 1 92  ? 4.78300   -15.16900 1.98400   1.000 15.73000  ? 92  VAL A N    1 
ATOM   1680 C  CA   . VAL A 1 92  ? 5.93400   -16.06300 2.15900   1.000 15.93000  ? 92  VAL A CA   1 
ATOM   1681 C  C    . VAL A 1 92  ? 6.36900   -16.11000 3.61000   1.000 16.41000  ? 92  VAL A C    1 
ATOM   1682 O  O    . VAL A 1 92  ? 6.65000   -17.18100 4.15500   1.000 17.22000  ? 92  VAL A O    1 
ATOM   1683 C  CB   . VAL A 1 92  ? 7.08500   -15.63700 1.23000   1.000 19.25000  ? 92  VAL A CB   1 
ATOM   1684 C  CG1  . VAL A 1 92  ? 8.38200   -16.38000 1.62900   1.000 21.18000  ? 92  VAL A CG1  1 
ATOM   1685 C  CG2  . VAL A 1 92  ? 6.70300   -15.86600 -0.21100  1.000 22.39000  ? 92  VAL A CG2  1 
ATOM   1686 H  H    . VAL A 1 92  ? 4.94100   -14.47300 1.50400   1.000 18.86000  ? 92  VAL A H    1 
ATOM   1687 H  HA   . VAL A 1 92  ? 5.66400   -16.96100 1.91200   1.000 19.10000  ? 92  VAL A HA   1 
ATOM   1688 H  HB   . VAL A 1 92  ? 7.25900   -14.68700 1.32300   1.000 23.08000  ? 92  VAL A HB   1 
ATOM   1689 H  HG11 . VAL A 1 92  ? 8.99100   -16.37900 0.87400   1.000 25.40000  ? 92  VAL A HG11 1 
ATOM   1690 H  HG12 . VAL A 1 92  ? 8.78800   -15.92300 2.38200   1.000 25.40000  ? 92  VAL A HG12 1 
ATOM   1691 H  HG13 . VAL A 1 92  ? 8.16100   -17.29200 1.87400   1.000 25.40000  ? 92  VAL A HG13 1 
ATOM   1692 H  HG21 . VAL A 1 92  ? 7.44700   -15.61400 -0.77900  1.000 26.86000  ? 92  VAL A HG21 1 
ATOM   1693 H  HG22 . VAL A 1 92  ? 6.49400   -16.80500 -0.33700  1.000 26.86000  ? 92  VAL A HG22 1 
ATOM   1694 H  HG23 . VAL A 1 92  ? 5.92700   -15.32400 -0.42300  1.000 26.86000  ? 92  VAL A HG23 1 
ATOM   1695 N  N    . ASN A 1 93  ? 6.49600   -14.94900 4.25600   1.000 16.94000  ? 93  ASN A N    1 
ATOM   1696 C  CA   . ASN A 1 93  ? 6.97800   -14.93800 5.63300   1.000 18.07000  ? 93  ASN A CA   1 
ATOM   1697 C  C    . ASN A 1 93  ? 6.00100   -15.63400 6.56500   1.000 16.33000  ? 93  ASN A C    1 
ATOM   1698 O  O    . ASN A 1 93  ? 6.40100   -16.34500 7.48700   1.000 19.12000  ? 93  ASN A O    1 
ATOM   1699 C  CB   . ASN A 1 93  ? 7.23200   -13.50000 6.08500   1.000 21.53000  ? 93  ASN A CB   1 
ATOM   1700 C  CG   . ASN A 1 93  ? 8.49200   -12.92400 5.47700   1.000 38.57000  ? 93  ASN A CG   1 
ATOM   1701 O  OD1  . ASN A 1 93  ? 9.24700   -13.63300 4.81200   1.000 39.16000  ? 93  ASN A OD1  1 
ATOM   1702 N  ND2  . ASN A 1 93  ? 8.72800   -11.63300 5.70200   1.000 43.26000  ? 93  ASN A ND2  1 
ATOM   1703 H  H    . ASN A 1 93  ? 6.31400   -14.17500 3.92800   1.000 20.31000  ? 93  ASN A H    1 
ATOM   1704 H  HA   . ASN A 1 93  ? 7.82100   -15.41700 5.67600   1.000 21.67000  ? 93  ASN A HA   1 
ATOM   1705 H  HB2  . ASN A 1 93  ? 6.48500   -12.94400 5.81500   1.000 25.82000  ? 93  ASN A HB2  1 
ATOM   1706 H  HB3  . ASN A 1 93  ? 7.32700   -13.48100 7.05100   1.000 25.82000  ? 93  ASN A HB3  1 
ATOM   1707 H  HD21 . ASN A 1 93  ? 8.17700   -11.17100 6.17300   1.000 51.91000  ? 93  ASN A HD21 1 
ATOM   1708 H  HD22 . ASN A 1 93  ? 9.43200   -11.26100 5.37600   1.000 51.91000  ? 93  ASN A HD22 1 
ATOM   1709 N  N    . CYS A 1 94  ? 4.69800   -15.46300 6.33900   1.000 14.73000  ? 94  CYS A N    1 
ATOM   1710 C  CA   . CYS A 1 94  ? 3.72000   -16.18100 7.14900   1.000 15.44000  ? 94  CYS A CA   1 
ATOM   1711 C  C    . CYS A 1 94  ? 3.76700   -17.68300 6.86000   1.000 15.93000  ? 94  CYS A C    1 
ATOM   1712 O  O    . CYS A 1 94  ? 3.70200   -18.50500 7.78700   1.000 16.14000  ? 94  CYS A O    1 
ATOM   1713 C  CB   . CYS A 1 94  ? 2.32200   -15.58800 6.92500   1.000 17.07000  ? 94  CYS A CB   1 
ATOM   1714 S  SG   . CYS A 1 94  ? 1.02400   -16.25100 7.97500   1.000 17.77000  ? 94  CYS A SG   1 
ATOM   1715 H  H    . CYS A 1 94  ? 4.36400   -14.95000 5.73600   1.000 17.67000  ? 94  CYS A H    1 
ATOM   1716 H  HA   . CYS A 1 94  ? 3.92500   -16.06600 8.09000   1.000 18.52000  ? 94  CYS A HA   1 
ATOM   1717 H  HB2  . CYS A 1 94  ? 2.36600   -14.63300 7.08800   1.000 20.47000  ? 94  CYS A HB2  1 
ATOM   1718 H  HB3  . CYS A 1 94  ? 2.06300   -15.75600 6.00500   1.000 20.47000  ? 94  CYS A HB3  1 
ATOM   1719 N  N    . ALA A 1 95  ? 3.92300   -18.05800 5.59100   1.000 14.67000  ? 95  ALA A N    1 
ATOM   1720 C  CA   . ALA A 1 95  ? 4.04500   -19.47600 5.25800   1.000 14.05000  ? 95  ALA A CA   1 
ATOM   1721 C  C    . ALA A 1 95  ? 5.24000   -20.12500 5.94700   1.000 14.75000  ? 95  ALA A C    1 
ATOM   1722 O  O    . ALA A 1 95  ? 5.18200   -21.30400 6.30600   1.000 15.77000  ? 95  ALA A O    1 
ATOM   1723 C  CB   . ALA A 1 95  ? 4.14700   -19.64800 3.74900   1.000 17.45000  ? 95  ALA A CB   1 
ATOM   1724 H  H    . ALA A 1 95  ? 3.96100   -17.52300 4.91800   1.000 17.59000  ? 95  ALA A H    1 
ATOM   1725 H  HA   . ALA A 1 95  ? 3.24600   -19.93300 5.56300   1.000 16.85000  ? 95  ALA A HA   1 
ATOM   1726 H  HB1  . ALA A 1 95  ? 4.21100   -20.59400 3.54300   1.000 20.93000  ? 95  ALA A HB1  1 
ATOM   1727 H  HB2  . ALA A 1 95  ? 3.35500   -19.27300 3.33400   1.000 20.93000  ? 95  ALA A HB2  1 
ATOM   1728 H  HB3  . ALA A 1 95  ? 4.93800   -19.18600 3.43100   1.000 20.93000  ? 95  ALA A HB3  1 
ATOM   1729 N  N    . LYS A 1 96  ? 6.32800   -19.38600 6.14000   1.000 15.33000  ? 96  LYS A N    1 
ATOM   1730 C  CA   . LYS A 1 96  ? 7.47700   -19.95100 6.83700   1.000 15.26000  ? 96  LYS A CA   1 
ATOM   1731 C  C    . LYS A 1 96  ? 7.13000   -20.28800 8.28000   1.000 16.35000  ? 96  LYS A C    1 
ATOM   1732 O  O    . LYS A 1 96  ? 7.59200   -21.30400 8.82400   1.000 18.14000  ? 96  LYS A O    1 
ATOM   1733 C  CB   . LYS A 1 96  ? 8.61500   -18.93800 6.79900   1.000 19.06000  ? 96  LYS A CB   1 
ATOM   1734 C  CG   . LYS A 1 96  ? 9.32400   -18.87000 5.46800   1.000 17.88000  ? 96  LYS A CG   1 
ATOM   1735 C  CD   . LYS A 1 96  ? 10.48200  -17.82800 5.47700   1.000 21.55000  ? 96  LYS A CD   1 
ATOM   1736 C  CE   . LYS A 1 96  ? 11.13800  -17.77100 4.12300   1.000 22.22000  ? 96  LYS A CE   1 
ATOM   1737 N  NZ   . LYS A 1 96  ? 12.13600  -16.65300 4.01900   1.000 30.38000  ? 96  LYS A NZ   1 
ATOM   1738 H  H    . LYS A 1 96  ? 6.42500   -18.57100 5.88200   1.000 18.38000  ? 96  LYS A H    1 
ATOM   1739 H  HA   . LYS A 1 96  ? 7.75800   -20.76800 6.39600   1.000 18.31000  ? 96  LYS A HA   1 
ATOM   1740 H  HB2  . LYS A 1 96  ? 8.25500   -18.05700 6.98900   1.000 22.86000  ? 96  LYS A HB2  1 
ATOM   1741 H  HB3  . LYS A 1 96  ? 9.27100   -19.18000 7.47200   1.000 22.86000  ? 96  LYS A HB3  1 
ATOM   1742 H  HG2  . LYS A 1 96  ? 9.70100   -19.74000 5.26200   1.000 21.45000  ? 96  LYS A HG2  1 
ATOM   1743 H  HG3  . LYS A 1 96  ? 8.69000   -18.61200 4.78100   1.000 21.45000  ? 96  LYS A HG3  1 
ATOM   1744 H  HD2  . LYS A 1 96  ? 10.12900  -16.94900 5.68900   1.000 25.84000  ? 96  LYS A HD2  1 
ATOM   1745 H  HD3  . LYS A 1 96  ? 11.14800  -18.08500 6.13400   1.000 25.84000  ? 96  LYS A HD3  1 
ATOM   1746 H  HE2  . LYS A 1 96  ? 11.60200  -18.60700 3.95900   1.000 26.65000  ? 96  LYS A HE2  1 
ATOM   1747 H  HE3  . LYS A 1 96  ? 10.45700  -17.63200 3.44500   1.000 26.65000  ? 96  LYS A HE3  1 
ATOM   1748 H  HZ1  . LYS A 1 96  ? 12.52400  -16.66500 3.21800   1.000 36.44000  ? 96  LYS A HZ1  1 
ATOM   1749 H  HZ2  . LYS A 1 96  ? 11.72800  -15.87000 4.13100   1.000 36.44000  ? 96  LYS A HZ2  1 
ATOM   1750 H  HZ3  . LYS A 1 96  ? 12.76200  -16.74600 4.64500   1.000 36.44000  ? 96  LYS A HZ3  1 
ATOM   1751 N  N    . LYS A 1 97  ? 6.29400   -19.46100 8.91800   1.000 15.85000  ? 97  LYS A N    1 
ATOM   1752 C  CA   . LYS A 1 97  ? 5.80900   -19.76800 10.26400  1.000 17.00000  ? 97  LYS A CA   1 
ATOM   1753 C  C    . LYS A 1 97  ? 4.88500   -20.98100 10.27400  1.000 16.18000  ? 97  LYS A C    1 
ATOM   1754 O  O    . LYS A 1 97  ? 5.01700   -21.87600 11.12700  1.000 19.39000  ? 97  LYS A O    1 
ATOM   1755 C  CB   . LYS A 1 97  ? 5.15200   -18.53600 10.89500  1.000 20.49000  ? 97  LYS A CB   1 
ATOM   1756 C  CG   . LYS A 1 97  ? 6.05000   -17.28600 10.83900  1.000 33.45000  ? 97  LYS A CG   1 
ATOM   1757 C  CD   . LYS A 1 97  ? 5.38600   -15.98800 11.34000  1.000 47.13000  ? 97  LYS A CD   1 
ATOM   1758 C  CE   . LYS A 1 97  ? 5.65700   -14.81300 10.37400  1.000 69.64000  ? 97  LYS A CE   1 
ATOM   1759 N  NZ   . LYS A 1 97  ? 4.91600   -13.54500 10.69300  1.000 57.48000  ? 97  LYS A NZ   1 
ATOM   1760 H  H    . LYS A 1 97  ? 5.99600   -18.72100 8.59600   1.000 19.00000  ? 97  LYS A H    1 
ATOM   1761 H  HA   . LYS A 1 97  ? 6.57000   -19.99500 10.82100  1.000 20.39000  ? 97  LYS A HA   1 
ATOM   1762 H  HB2  . LYS A 1 97  ? 4.33100   -18.33700 10.41900  1.000 24.57000  ? 97  LYS A HB2  1 
ATOM   1763 H  HB3  . LYS A 1 97  ? 4.95800   -18.72400 11.82700  1.000 24.57000  ? 97  LYS A HB3  1 
ATOM   1764 H  HG2  . LYS A 1 97  ? 6.83300   -17.44300 11.39000  1.000 40.12000  ? 97  LYS A HG2  1 
ATOM   1765 H  HG3  . LYS A 1 97  ? 6.31700   -17.13900 9.91800   1.000 40.12000  ? 97  LYS A HG3  1 
ATOM   1766 H  HD2  . LYS A 1 97  ? 4.42600   -16.11900 11.40000  1.000 56.54000  ? 97  LYS A HD2  1 
ATOM   1767 H  HD3  . LYS A 1 97  ? 5.74400   -15.75700 12.21100  1.000 56.54000  ? 97  LYS A HD3  1 
ATOM   1768 H  HE2  . LYS A 1 97  ? 6.60500   -14.60900 10.39800  1.000 83.56000  ? 97  LYS A HE2  1 
ATOM   1769 H  HE3  . LYS A 1 97  ? 5.39800   -15.08400 9.48000   1.000 83.56000  ? 97  LYS A HE3  1 
ATOM   1770 H  HZ1  . LYS A 1 97  ? 5.10400   -12.92200 10.08600  1.000 68.96000  ? 97  LYS A HZ1  1 
ATOM   1771 H  HZ2  . LYS A 1 97  ? 4.03900   -13.69700 10.69000  1.000 68.96000  ? 97  LYS A HZ2  1 
ATOM   1772 H  HZ3  . LYS A 1 97  ? 5.15500   -13.24700 11.49600  1.000 68.96000  ? 97  LYS A HZ3  1 
ATOM   1773 N  N    . ILE A 1 98  ? 3.98800   -21.07000 9.30400   1.000 15.07000  ? 98  ILE A N    1 
ATOM   1774 C  CA   . ILE A 1 98  ? 3.04200   -22.17300 9.24900   1.000 15.72000  ? 98  ILE A CA   1 
ATOM   1775 C  C    . ILE A 1 98  ? 3.77700   -23.48900 9.06100   1.000 16.92000  ? 98  ILE A C    1 
ATOM   1776 O  O    . ILE A 1 98  ? 3.49300   -24.47900 9.75500   1.000 17.92000  ? 98  ILE A O    1 
ATOM   1777 C  CB   . ILE A 1 98  ? 2.02600   -21.93600 8.11800   1.000 15.32000  ? 98  ILE A CB   1 
ATOM   1778 C  CG1  . ILE A 1 98  ? 1.20700   -20.68000 8.38200   1.000 15.04000  ? 98  ILE A CG1  1 
ATOM   1779 C  CG2  . ILE A 1 98  ? 1.10600   -23.12600 7.95800   1.000 16.80000  ? 98  ILE A CG2  1 
ATOM   1780 C  CD1  . ILE A 1 98  ? 0.33200   -20.26800 7.22400   1.000 18.42000  ? 98  ILE A CD1  1 
ATOM   1781 H  H    . ILE A 1 98  ? 3.90400   -20.50400 8.66200   1.000 18.07000  ? 98  ILE A H    1 
ATOM   1782 H  HA   . ILE A 1 98  ? 2.56300   -22.21500 10.09100  1.000 18.86000  ? 98  ILE A HA   1 
ATOM   1783 H  HB   . ILE A 1 98  ? 2.52700   -21.81600 7.29600   1.000 18.37000  ? 98  ILE A HB   1 
ATOM   1784 H  HG12 . ILE A 1 98  ? 0.63100   -20.83900 9.14600   1.000 18.03000  ? 98  ILE A HG12 1 
ATOM   1785 H  HG13 . ILE A 1 98  ? 1.81300   -19.94600 8.57000   1.000 18.03000  ? 98  ILE A HG13 1 
ATOM   1786 H  HG21 . ILE A 1 98  ? 0.56700   -23.00400 7.16100   1.000 20.15000  ? 98  ILE A HG21 1 
ATOM   1787 H  HG22 . ILE A 1 98  ? 1.64100   -23.93100 7.87600   1.000 20.15000  ? 98  ILE A HG22 1 
ATOM   1788 H  HG23 . ILE A 1 98  ? 0.53200   -23.18900 8.73800   1.000 20.15000  ? 98  ILE A HG23 1 
ATOM   1789 H  HD11 . ILE A 1 98  ? 0.89200   -20.09000 6.45200   1.000 22.09000  ? 98  ILE A HD11 1 
ATOM   1790 H  HD12 . ILE A 1 98  ? -0.28700  -20.98800 7.02400   1.000 22.09000  ? 98  ILE A HD12 1 
ATOM   1791 H  HD13 . ILE A 1 98  ? -0.15900  -19.46800 7.46800   1.000 22.09000  ? 98  ILE A HD13 1 
ATOM   1792 N  N    . VAL A 1 99  ? 4.70600   -23.53900 8.10100   1.000 15.75000  ? 99  VAL A N    1 
ATOM   1793 C  CA   . VAL A 1 99  ? 5.36900   -24.80100 7.75900   1.000 16.23000  ? 99  VAL A CA   1 
ATOM   1794 C  C    . VAL A 1 99  ? 6.26800   -25.25300 8.88100   1.000 18.12000  ? 99  VAL A C    1 
ATOM   1795 O  O    . VAL A 1 99  ? 6.64800   -26.43500 8.92000   1.000 18.99000  ? 99  VAL A O    1 
ATOM   1796 C  CB   . VAL A 1 99  ? 6.08600   -24.66600 6.41200   1.000 15.80000  ? 99  VAL A CB   1 
ATOM   1797 C  CG1  . VAL A 1 99  ? 7.38000   -23.90500 6.51600   1.000 17.38000  ? 99  VAL A CG1  1 
ATOM   1798 C  CG2  . VAL A 1 99  ? 6.35100   -26.03500 5.79600   1.000 19.57000  ? 99  VAL A CG2  1 
ATOM   1799 H  H    . VAL A 1 99  ? 4.96800   -22.86400 7.63800   1.000 18.89000  ? 99  VAL A H    1 
ATOM   1800 H  HA   . VAL A 1 99  ? 4.71100   -25.50400 7.64100   1.000 19.46000  ? 99  VAL A HA   1 
ATOM   1801 H  HB   . VAL A 1 99  ? 5.49400   -24.16000 5.83400   1.000 18.94000  ? 99  VAL A HB   1 
ATOM   1802 H  HG11 . VAL A 1 99  ? 7.74200   -23.77400 5.62500   1.000 20.85000  ? 99  VAL A HG11 1 
ATOM   1803 H  HG12 . VAL A 1 99  ? 7.20900   -23.04600 6.93300   1.000 20.85000  ? 99  VAL A HG12 1 
ATOM   1804 H  HG13 . VAL A 1 99  ? 8.00500   -24.41500 7.05400   1.000 20.85000  ? 99  VAL A HG13 1 
ATOM   1805 H  HG21 . VAL A 1 99  ? 7.00600   -25.94000 5.08600   1.000 23.47000  ? 99  VAL A HG21 1 
ATOM   1806 H  HG22 . VAL A 1 99  ? 6.69100   -26.63000 6.48200   1.000 23.47000  ? 99  VAL A HG22 1 
ATOM   1807 H  HG23 . VAL A 1 99  ? 5.52100   -26.38500 5.43600   1.000 23.47000  ? 99  VAL A HG23 1 
ATOM   1808 N  N    . SER A 1 100 ? 6.61600   -24.35900 9.80900   1.000 18.63000  ? 100 SER A N    1 
ATOM   1809 C  CA   . SER A 1 100 ? 7.42400   -24.66600 10.98000  1.000 18.61000  ? 100 SER A CA   1 
ATOM   1810 C  C    . SER A 1 100 ? 6.59200   -25.07100 12.18000  1.000 21.38000  ? 100 SER A C    1 
ATOM   1811 O  O    . SER A 1 100 ? 7.17700   -25.31700 13.24600  1.000 31.82000  ? 100 SER A O    1 
ATOM   1812 C  CB   . SER A 1 100 ? 8.25200   -23.43100 11.35700  1.000 23.30000  ? 100 SER A CB   1 
ATOM   1813 O  OG   . SER A 1 100 ? 9.11500   -23.03600 10.31300  1.000 25.17000  ? 100 SER A OG   1 
ATOM   1814 H  H    . SER A 1 100 ? 6.38400   -23.53200 9.77700   1.000 22.34000  ? 100 SER A H    1 
ATOM   1815 H  HA   . SER A 1 100 ? 8.02100   -25.39900 10.76400  1.000 22.32000  ? 100 SER A HA   1 
ATOM   1816 H  HB2  . SER A 1 100 ? 7.64700   -22.69900 11.55400  1.000 27.95000  ? 100 SER A HB2  1 
ATOM   1817 H  HB3  . SER A 1 100 ? 8.78600   -23.64100 12.13900  1.000 27.95000  ? 100 SER A HB3  1 
ATOM   1818 H  HG   . SER A 1 100 ? 8.66700   -22.75000 9.66200   1.000 30.20000  ? 100 SER A HG   1 
ATOM   1819 N  N    A ASP A 1 101 ? 5.27600   -25.20500 12.03900  0.550 21.10000  ? 101 ASP A N    1 
ATOM   1820 N  N    B ASP A 1 101 ? 5.27500   -25.19500 12.03600  0.450 21.16000  ? 101 ASP A N    1 
ATOM   1821 C  CA   A ASP A 1 101 ? 4.37600   -25.36700 13.17800  0.550 26.19000  ? 101 ASP A CA   1 
ATOM   1822 C  CA   B ASP A 1 101 ? 4.39000   -25.37100 13.18300  0.450 26.21000  ? 101 ASP A CA   1 
ATOM   1823 C  C    A ASP A 1 101 ? 4.16100   -26.81900 13.58600  0.550 24.46000  ? 101 ASP A C    1 
ATOM   1824 C  C    B ASP A 1 101 ? 4.43800   -26.77700 13.76500  0.450 25.73000  ? 101 ASP A C    1 
ATOM   1825 O  O    A ASP A 1 101 ? 3.28300   -27.09000 14.41500  0.550 26.04000  ? 101 ASP A O    1 
ATOM   1826 O  O    B ASP A 1 101 ? 4.09400   -26.95600 14.93800  0.450 25.21000  ? 101 ASP A O    1 
ATOM   1827 C  CB   A ASP A 1 101 ? 3.02400   -24.67700 12.91600  0.550 33.12000  ? 101 ASP A CB   1 
ATOM   1828 C  CB   B ASP A 1 101 ? 2.94700   -25.04900 12.77800  0.450 30.58000  ? 101 ASP A CB   1 
ATOM   1829 C  CG   A ASP A 1 101 ? 2.01800   -25.55700 12.15200  0.550 27.80000  ? 101 ASP A CG   1 
ATOM   1830 C  CG   B ASP A 1 101 ? 2.11700   -24.51000 13.92300  0.450 40.18000  ? 101 ASP A CG   1 
ATOM   1831 O  OD1  A ASP A 1 101 ? 2.35600   -26.67000 11.67800  0.550 27.82000  ? 101 ASP A OD1  1 
ATOM   1832 O  OD1  B ASP A 1 101 ? 2.67600   -23.82800 14.80800  0.450 50.83000  ? 101 ASP A OD1  1 
ATOM   1833 O  OD2  A ASP A 1 101 ? 0.85900   -25.11300 12.00400  0.550 38.16000  ? 101 ASP A OD2  1 
ATOM   1834 O  OD2  B ASP A 1 101 ? 0.89200   -24.74800 13.92000  0.450 32.67000  ? 101 ASP A OD2  1 
ATOM   1835 H  H    A ASP A 1 101 ? 4.87300   -25.20600 11.27900  0.550 25.31000  ? 101 ASP A H    1 
ATOM   1836 H  H    B ASP A 1 101 ? 4.86600   -25.18000 11.28000  0.450 25.37000  ? 101 ASP A H    1 
ATOM   1837 H  HA   A ASP A 1 101 ? 4.78300   -24.91700 13.93400  0.550 31.42000  ? 101 ASP A HA   1 
ATOM   1838 H  HA   B ASP A 1 101 ? 4.66400   -24.75200 13.87800  0.450 31.44000  ? 101 ASP A HA   1 
ATOM   1839 H  HB2  A ASP A 1 101 ? 2.62400   -24.44200 13.76800  0.550 39.73000  ? 101 ASP A HB2  1 
ATOM   1840 H  HB2  B ASP A 1 101 ? 2.95900   -24.37900 12.07600  0.450 36.68000  ? 101 ASP A HB2  1 
ATOM   1841 H  HB3  A ASP A 1 101 ? 3.17800   -23.87800 12.38900  0.550 39.73000  ? 101 ASP A HB3  1 
ATOM   1842 H  HB3  B ASP A 1 101 ? 2.52200   -25.85900 12.45600  0.450 36.68000  ? 101 ASP A HB3  1 
ATOM   1843 N  N    . GLY A 1 102 ? 4.91000   -27.75800 13.00200  1.000 24.61000  ? 102 GLY A N    1 
ATOM   1844 C  CA   . GLY A 1 102 ? 4.88000   -29.15300 13.41600  1.000 24.49000  ? 102 GLY A CA   1 
ATOM   1845 C  C    . GLY A 1 102 ? 4.44100   -30.10000 12.31800  1.000 24.14000  ? 102 GLY A C    1 
ATOM   1846 O  O    . GLY A 1 102 ? 4.93200   -31.23400 12.26100  1.000 25.81000  ? 102 GLY A O    1 
ATOM   1847 H  H    . GLY A 1 102 ? 5.45000   -27.59700 12.35200  1.000 29.52000  ? 102 GLY A H    1 
ATOM   1848 H  HA2  . GLY A 1 102 ? 5.76800   -29.41600 13.70300  1.000 29.38000  ? 102 GLY A HA2  1 
ATOM   1849 H  HA3  . GLY A 1 102 ? 4.26600   -29.24900 14.16000  1.000 29.38000  ? 102 GLY A HA3  1 
ATOM   1850 N  N    . ASN A 1 103 ? 3.54200   -29.66300 11.43400  1.000 20.26000  ? 103 ASN A N    1 
ATOM   1851 C  CA   . ASN A 1 103 ? 2.94700   -30.54800 10.44700  1.000 18.61000  ? 103 ASN A CA   1 
ATOM   1852 C  C    . ASN A 1 103 ? 3.50200   -30.32900 9.05100   1.000 14.61000  ? 103 ASN A C    1 
ATOM   1853 O  O    . ASN A 1 103 ? 3.04200   -30.95900 8.10300   1.000 17.31000  ? 103 ASN A O    1 
ATOM   1854 C  CB   . ASN A 1 103 ? 1.42400   -30.42700 10.45500  1.000 27.05000  ? 103 ASN A CB   1 
ATOM   1855 C  CG   . ASN A 1 103 ? 0.82700   -30.90600 11.76000  1.000 49.67000  ? 103 ASN A CG   1 
ATOM   1856 O  OD1  . ASN A 1 103 ? 1.05300   -32.04200 12.16600  1.000 40.63000  ? 103 ASN A OD1  1 
ATOM   1857 N  ND2  . ASN A 1 103 ? 0.08800   -30.03600 12.43700  1.000 58.34000  ? 103 ASN A ND2  1 
ATOM   1858 H  H    . ASN A 1 103 ? 3.26300   -28.85100 11.39000  1.000 24.30000  ? 103 ASN A H    1 
ATOM   1859 H  HA   . ASN A 1 103 ? 3.15500   -31.46200 10.69700  1.000 22.32000  ? 103 ASN A HA   1 
ATOM   1860 H  HB2  . ASN A 1 103 ? 1.17700   -29.49700 10.33200  1.000 32.45000  ? 103 ASN A HB2  1 
ATOM   1861 H  HB3  . ASN A 1 103 ? 1.05700   -30.96500 9.73700   1.000 32.45000  ? 103 ASN A HB3  1 
ATOM   1862 H  HD21 . ASN A 1 103 ? -0.03200  -29.24200 12.12800  1.000 69.99000  ? 103 ASN A HD21 1 
ATOM   1863 H  HD22 . ASN A 1 103 ? -0.27100  -30.26600 13.18400  1.000 69.99000  ? 103 ASN A HD22 1 
ATOM   1864 N  N    . GLY A 1 104 ? 4.49500   -29.47700 8.92000   1.000 15.56000  ? 104 GLY A N    1 
ATOM   1865 C  CA   . GLY A 1 104 ? 5.09500   -29.25500 7.62100   1.000 14.67000  ? 104 GLY A CA   1 
ATOM   1866 C  C    . GLY A 1 104 ? 4.07300   -28.74100 6.63200   1.000 14.11000  ? 104 GLY A C    1 
ATOM   1867 O  O    . GLY A 1 104 ? 3.12700   -28.00100 6.97500   1.000 14.81000  ? 104 GLY A O    1 
ATOM   1868 H  H    . GLY A 1 104 ? 4.84000   -29.01600 9.55900   1.000 18.66000  ? 104 GLY A H    1 
ATOM   1869 H  HA2  . GLY A 1 104 ? 5.80900   -28.60300 7.69800   1.000 17.59000  ? 104 GLY A HA2  1 
ATOM   1870 H  HA3  . GLY A 1 104 ? 5.46200   -30.08800 7.28500   1.000 17.59000  ? 104 GLY A HA3  1 
ATOM   1871 N  N    . MET A 1 105 ? 4.21700   -29.16400 5.39800   1.000 12.61000  ? 105 MET A N    1 
ATOM   1872 C  CA   . MET A 1 105 ? 3.29400   -28.65500 4.38500   1.000 12.79000  ? 105 MET A CA   1 
ATOM   1873 C  C    . MET A 1 105 ? 1.95200   -29.36900 4.41500   1.000 12.38000  ? 105 MET A C    1 
ATOM   1874 O  O    . MET A 1 105 ? 1.04200   -28.97900 3.67800   1.000 13.33000  ? 105 MET A O    1 
ATOM   1875 C  CB   . MET A 1 105 ? 3.90900   -28.75600 2.99600   1.000 13.17000  ? 105 MET A CB   1 
ATOM   1876 C  CG   . MET A 1 105 ? 4.92300   -27.63100 2.72600   1.000 15.20000  ? 105 MET A CG   1 
ATOM   1877 S  SD   . MET A 1 105 ? 5.38200   -27.40800 0.98400   1.000 15.91000  ? 105 MET A SD   1 
ATOM   1878 C  CE   . MET A 1 105 ? 3.87900   -26.68800 0.34000   1.000 18.30000  ? 105 MET A CE   1 
ATOM   1879 H  H    . MET A 1 105 ? 4.81100   -29.72100 5.12400   1.000 15.12000  ? 105 MET A H    1 
ATOM   1880 H  HA   . MET A 1 105 ? 3.14800   -27.71100 4.55300   1.000 15.34000  ? 105 MET A HA   1 
ATOM   1881 H  HB2  . MET A 1 105 ? 4.37000   -29.60500 2.91400   1.000 15.80000  ? 105 MET A HB2  1 
ATOM   1882 H  HB3  . MET A 1 105 ? 3.20500   -28.69400 2.33200   1.000 15.80000  ? 105 MET A HB3  1 
ATOM   1883 H  HG2  . MET A 1 105 ? 4.54300   -26.79400 3.03500   1.000 18.23000  ? 105 MET A HG2  1 
ATOM   1884 H  HG3  . MET A 1 105 ? 5.73600   -27.82700 3.21700   1.000 18.23000  ? 105 MET A HG3  1 
ATOM   1885 H  HE1  . MET A 1 105 ? 3.99600   -26.50200 -0.60500  1.000 21.95000  ? 105 MET A HE1  1 
ATOM   1886 H  HE2  . MET A 1 105 ? 3.14900   -27.31500 0.46600   1.000 21.95000  ? 105 MET A HE2  1 
ATOM   1887 H  HE3  . MET A 1 105 ? 3.69300   -25.86500 0.81800   1.000 21.95000  ? 105 MET A HE3  1 
ATOM   1888 N  N    . ASN A 1 106 ? 1.76800   -30.36100 5.29200   1.000 13.91000  ? 106 ASN A N    1 
ATOM   1889 C  CA   . ASN A 1 106 ? 0.45500   -30.96600 5.46600   1.000 13.56000  ? 106 ASN A CA   1 
ATOM   1890 C  C    . ASN A 1 106 ? -0.55300  -29.95700 5.97200   1.000 14.95000  ? 106 ASN A C    1 
ATOM   1891 O  O    . ASN A 1 106 ? -1.75300  -30.22500 5.87900   1.000 16.13000  ? 106 ASN A O    1 
ATOM   1892 C  CB   . ASN A 1 106 ? 0.53800   -32.14700 6.43200   1.000 15.93000  ? 106 ASN A CB   1 
ATOM   1893 C  CG   . ASN A 1 106 ? 1.37300   -33.29000 5.90000   1.000 14.79000  ? 106 ASN A CG   1 
ATOM   1894 O  OD1  . ASN A 1 106 ? 1.02300   -33.96600 4.94400   1.000 15.87000  ? 106 ASN A OD1  1 
ATOM   1895 N  ND2  . ASN A 1 106 ? 2.54000   -33.46200 6.50000   1.000 17.16000  ? 106 ASN A ND2  1 
ATOM   1896 H  H    . ASN A 1 106 ? 2.38300   -30.69600 5.79100   1.000 16.68000  ? 106 ASN A H    1 
ATOM   1897 H  HA   . ASN A 1 106 ? 0.14800   -31.30900 4.61200   1.000 16.26000  ? 106 ASN A HA   1 
ATOM   1898 H  HB2  . ASN A 1 106 ? 0.93800   -31.84700 7.26300   1.000 19.11000  ? 106 ASN A HB2  1 
ATOM   1899 H  HB3  . ASN A 1 106 ? -0.35700  -32.48300 6.59700   1.000 19.11000  ? 106 ASN A HB3  1 
ATOM   1900 H  HD21 . ASN A 1 106 ? 3.06500   -34.09500 6.24700   1.000 20.58000  ? 106 ASN A HD21 1 
ATOM   1901 H  HD22 . ASN A 1 106 ? 2.77400   -32.94100 7.14300   1.000 20.58000  ? 106 ASN A HD22 1 
ATOM   1902 N  N    . ALA A 1 107 ? -0.08900  -28.80500 6.47300   1.000 14.10000  ? 107 ALA A N    1 
ATOM   1903 C  CA   . ALA A 1 107 ? -0.99600  -27.72300 6.86300   1.000 16.16000  ? 107 ALA A CA   1 
ATOM   1904 C  C    . ALA A 1 107 ? -1.85400  -27.25300 5.69600   1.000 16.62000  ? 107 ALA A C    1 
ATOM   1905 O  O    . ALA A 1 107 ? -2.96500  -26.75600 5.90800   1.000 18.12000  ? 107 ALA A O    1 
ATOM   1906 C  CB   . ALA A 1 107 ? -0.19900  -26.53300 7.38900   1.000 18.59000  ? 107 ALA A CB   1 
ATOM   1907 H  H    . ALA A 1 107 ? 0.74300   -28.62600 6.59700   1.000 16.90000  ? 107 ALA A H    1 
ATOM   1908 H  HA   . ALA A 1 107 ? -1.57500  -28.05700 7.56600   1.000 19.37000  ? 107 ALA A HA   1 
ATOM   1909 H  HB1  . ALA A 1 107 ? -0.81500  -25.87600 7.75000   1.000 22.29000  ? 107 ALA A HB1  1 
ATOM   1910 H  HB2  . ALA A 1 107 ? 0.40200   -26.84000 8.08600   1.000 22.29000  ? 107 ALA A HB2  1 
ATOM   1911 H  HB3  . ALA A 1 107 ? 0.30900   -26.14600 6.66000   1.000 22.29000  ? 107 ALA A HB3  1 
ATOM   1912 N  N    . TRP A 1 108 ? -1.36600  -27.37100 4.46900   1.000 13.59000  ? 108 TRP A N    1 
ATOM   1913 C  CA   . TRP A 1 108 ? -2.13400  -27.06500 3.27200   1.000 13.07000  ? 108 TRP A CA   1 
ATOM   1914 C  C    . TRP A 1 108 ? -2.75000  -28.37000 2.76500   1.000 15.72000  ? 108 TRP A C    1 
ATOM   1915 O  O    . TRP A 1 108 ? -2.06000  -29.23700 2.21000   1.000 15.02000  ? 108 TRP A O    1 
ATOM   1916 C  CB   . TRP A 1 108 ? -1.23700  -26.44300 2.21000   1.000 15.52000  ? 108 TRP A CB   1 
ATOM   1917 C  CG   . TRP A 1 108 ? -0.79300  -25.04600 2.50000   1.000 12.63000  ? 108 TRP A CG   1 
ATOM   1918 C  CD1  . TRP A 1 108 ? -1.46400  -23.88900 2.14700   1.000 14.19000  ? 108 TRP A CD1  1 
ATOM   1919 C  CD2  . TRP A 1 108 ? 0.36800   -24.61400 3.20000   1.000 12.03000  ? 108 TRP A CD2  1 
ATOM   1920 N  NE1  . TRP A 1 108 ? -0.78000  -22.80600 2.56200   1.000 14.34000  ? 108 TRP A NE1  1 
ATOM   1921 C  CE2  . TRP A 1 108 ? 0.36000   -23.21000 3.20900   1.000 13.81000  ? 108 TRP A CE2  1 
ATOM   1922 C  CE3  . TRP A 1 108 ? 1.42700   -25.27700 3.81200   1.000 14.09000  ? 108 TRP A CE3  1 
ATOM   1923 C  CZ2  . TRP A 1 108 ? 1.35000   -22.47100 3.82700   1.000 13.67000  ? 108 TRP A CZ2  1 
ATOM   1924 C  CZ3  . TRP A 1 108 ? 2.41300   -24.53500 4.42000   1.000 16.25000  ? 108 TRP A CZ3  1 
ATOM   1925 C  CH2  . TRP A 1 108 ? 2.38000   -23.15000 4.41600   1.000 15.56000  ? 108 TRP A CH2  1 
ATOM   1926 H  H    . TRP A 1 108 ? -0.56600  -27.63400 4.29800   1.000 16.30000  ? 108 TRP A H    1 
ATOM   1927 H  HA   . TRP A 1 108 ? -2.84200  -26.43700 3.48300   1.000 15.67000  ? 108 TRP A HA   1 
ATOM   1928 H  HB2  . TRP A 1 108 ? -0.44000  -26.98900 2.12300   1.000 18.61000  ? 108 TRP A HB2  1 
ATOM   1929 H  HB3  . TRP A 1 108 ? -1.72200  -26.42600 1.37000   1.000 18.61000  ? 108 TRP A HB3  1 
ATOM   1930 H  HD1  . TRP A 1 108 ? -2.27200  -23.86300 1.68900   1.000 17.01000  ? 108 TRP A HD1  1 
ATOM   1931 H  HE1  . TRP A 1 108 ? -1.02000  -21.98900 2.44000   1.000 17.20000  ? 108 TRP A HE1  1 
ATOM   1932 H  HE3  . TRP A 1 108 ? 1.46800   -26.20700 3.81000   1.000 16.89000  ? 108 TRP A HE3  1 
ATOM   1933 H  HZ2  . TRP A 1 108 ? 1.31700   -21.54100 3.84200   1.000 16.39000  ? 108 TRP A HZ2  1 
ATOM   1934 H  HZ3  . TRP A 1 108 ? 3.11700   -24.97200 4.84200   1.000 19.49000  ? 108 TRP A HZ3  1 
ATOM   1935 H  HH2  . TRP A 1 108 ? 3.07000   -22.67500 4.82000   1.000 18.65000  ? 108 TRP A HH2  1 
ATOM   1936 N  N    A VAL A 1 109 ? -4.06400  -28.48000 2.96000   0.490 17.61000  ? 109 VAL A N    1 
ATOM   1937 N  N    B VAL A 1 109 ? -4.05700  -28.53700 2.94700   0.510 17.20000  ? 109 VAL A N    1 
ATOM   1938 C  CA   A VAL A 1 109 ? -4.82700  -29.64900 2.54300   0.490 19.70000  ? 109 VAL A CA   1 
ATOM   1939 C  CA   B VAL A 1 109 ? -4.65700  -29.80300 2.54300   0.510 18.41000  ? 109 VAL A CA   1 
ATOM   1940 C  C    A VAL A 1 109 ? -4.55900  -29.97300 1.08400   0.490 15.52000  ? 109 VAL A C    1 
ATOM   1941 C  C    B VAL A 1 109 ? -4.56000  -30.01500 1.03500   0.510 15.61000  ? 109 VAL A C    1 
ATOM   1942 O  O    A VAL A 1 109 ? -4.34700  -31.13700 0.72500   0.490 16.52000  ? 109 VAL A O    1 
ATOM   1943 O  O    B VAL A 1 109 ? -4.46100  -31.16100 0.58600   0.510 18.79000  ? 109 VAL A O    1 
ATOM   1944 C  CB   A VAL A 1 109 ? -6.32800  -29.41500 2.80200   0.490 18.48000  ? 109 VAL A CB   1 
ATOM   1945 C  CB   B VAL A 1 109 ? -6.09800  -29.94900 3.07100   0.510 24.79000  ? 109 VAL A CB   1 
ATOM   1946 C  CG1  A VAL A 1 109 ? -7.13000  -30.64000 2.39700   0.490 21.36000  ? 109 VAL A CG1  1 
ATOM   1947 C  CG1  B VAL A 1 109 ? -6.13500  -29.73800 4.57100   0.510 28.20000  ? 109 VAL A CG1  1 
ATOM   1948 C  CG2  A VAL A 1 109 ? -6.56600  -29.07400 4.25800   0.490 31.72000  ? 109 VAL A CG2  1 
ATOM   1949 C  CG2  B VAL A 1 109 ? -7.01800  -28.99100 2.34700   0.510 27.63000  ? 109 VAL A CG2  1 
ATOM   1950 H  H    A VAL A 1 109 ? -4.54700  -27.87800 3.34000   0.490 21.12000  ? 109 VAL A H    1 
ATOM   1951 H  H    B VAL A 1 109 ? -4.59500  -27.95800 3.28700   0.510 20.63000  ? 109 VAL A H    1 
ATOM   1952 H  HA   A VAL A 1 109 ? -4.53800  -30.41100 3.06900   0.490 23.63000  ? 109 VAL A HA   1 
ATOM   1953 H  HA   B VAL A 1 109 ? -4.14000  -30.50800 2.96300   0.510 22.08000  ? 109 VAL A HA   1 
ATOM   1954 H  HB   A VAL A 1 109 ? -6.62900  -28.66500 2.26400   0.490 22.16000  ? 109 VAL A HB   1 
ATOM   1955 H  HB   B VAL A 1 109 ? -6.41800  -30.84800 2.89700   0.510 29.74000  ? 109 VAL A HB   1 
ATOM   1956 H  HG11 A VAL A 1 109 ? -8.04600  -30.53100 2.69700   0.490 25.62000  ? 109 VAL A HG11 1 
ATOM   1957 H  HG11 B VAL A 1 109 ? -6.93500  -30.15300 4.92900   0.510 33.83000  ? 109 VAL A HG11 1 
ATOM   1958 H  HG12 A VAL A 1 109 ? -7.10700  -30.72800 1.43100   0.490 25.62000  ? 109 VAL A HG12 1 
ATOM   1959 H  HG12 B VAL A 1 109 ? -5.34700  -30.14300 4.96600   0.510 33.83000  ? 109 VAL A HG12 1 
ATOM   1960 H  HG13 A VAL A 1 109 ? -6.73800  -31.42500 2.81000   0.490 25.62000  ? 109 VAL A HG13 1 
ATOM   1961 H  HG13 B VAL A 1 109 ? -6.14500  -28.78500 4.75600   0.510 33.83000  ? 109 VAL A HG13 1 
ATOM   1962 H  HG21 A VAL A 1 109 ? -7.51300  -29.15800 4.45100   0.490 38.06000  ? 109 VAL A HG21 1 
ATOM   1963 H  HG21 B VAL A 1 109 ? -7.68600  -28.66500 2.97000   0.510 33.14000  ? 109 VAL A HG21 1 
ATOM   1964 H  HG22 A VAL A 1 109 ? -6.06000  -29.68700 4.81300   0.490 38.06000  ? 109 VAL A HG22 1 
ATOM   1965 H  HG22 B VAL A 1 109 ? -6.49500  -28.25000 2.00400   0.510 33.14000  ? 109 VAL A HG22 1 
ATOM   1966 H  HG23 A VAL A 1 109 ? -6.27500  -28.16300 4.42100   0.490 38.06000  ? 109 VAL A HG23 1 
ATOM   1967 H  HG23 B VAL A 1 109 ? -7.44900  -29.46000 1.61500   0.510 33.14000  ? 109 VAL A HG23 1 
ATOM   1968 N  N    . ALA A 1 110 ? -4.56700  -28.95400 0.22900   1.000 15.83000  ? 110 ALA A N    1 
ATOM   1969 C  CA   . ALA A 1 110 ? -4.38500  -29.17300 -1.20800  1.000 15.78000  ? 110 ALA A CA   1 
ATOM   1970 C  C    . ALA A 1 110 ? -3.00300  -29.72500 -1.51900  1.000 17.05000  ? 110 ALA A C    1 
ATOM   1971 O  O    . ALA A 1 110 ? -2.84400  -30.52700 -2.44400  1.000 16.91000  ? 110 ALA A O    1 
ATOM   1972 C  CB   . ALA A 1 110 ? -4.63800  -27.90100 -2.01600  1.000 18.86000  ? 110 ALA A CB   1 
ATOM   1973 H  H    . ALA A 1 110 ? -4.67000  -28.13700 0.47800   1.000 18.98000  ? 110 ALA A H    1 
ATOM   1974 H  HA   . ALA A 1 110 ? -5.04900  -29.82300 -1.48400  1.000 18.92000  ? 110 ALA A HA   1 
ATOM   1975 H  HB1  . ALA A 1 110 ? -4.47800  -28.08600 -2.95500  1.000 22.62000  ? 110 ALA A HB1  1 
ATOM   1976 H  HB2  . ALA A 1 110 ? -5.55800  -27.62300 -1.88600  1.000 22.62000  ? 110 ALA A HB2  1 
ATOM   1977 H  HB3  . ALA A 1 110 ? -4.03600  -27.20600 -1.70800  1.000 22.62000  ? 110 ALA A HB3  1 
ATOM   1978 N  N    . TRP A 1 111 ? -1.98700  -29.30200 -0.77900  1.000 14.02000  ? 111 TRP A N    1 
ATOM   1979 C  CA   . TRP A 1 111 ? -0.65900  -29.89200 -0.99500  1.000 15.03000  ? 111 TRP A CA   1 
ATOM   1980 C  C    . TRP A 1 111 ? -0.68500  -31.37900 -0.67300  1.000 13.58000  ? 111 TRP A C    1 
ATOM   1981 O  O    . TRP A 1 111 ? -0.19800  -32.20200 -1.45900  1.000 13.38000  ? 111 TRP A O    1 
ATOM   1982 C  CB   . TRP A 1 111 ? 0.42700   -29.19400 -0.15700  1.000 13.71000  ? 111 TRP A CB   1 
ATOM   1983 C  CG   . TRP A 1 111 ? 1.76800   -29.83000 -0.33100  1.000 12.80000  ? 111 TRP A CG   1 
ATOM   1984 C  CD1  . TRP A 1 111 ? 2.66400   -29.58700 -1.31600  1.000 12.86000  ? 111 TRP A CD1  1 
ATOM   1985 C  CD2  . TRP A 1 111 ? 2.33400   -30.82500 0.50700   1.000 12.23000  ? 111 TRP A CD2  1 
ATOM   1986 N  NE1  . TRP A 1 111 ? 3.75500   -30.41400 -1.15300  1.000 14.34000  ? 111 TRP A NE1  1 
ATOM   1987 C  CE2  . TRP A 1 111 ? 3.57600   -31.17700 -0.04100  1.000 12.21000  ? 111 TRP A CE2  1 
ATOM   1988 C  CE3  . TRP A 1 111 ? 1.90600   -31.48600 1.65900   1.000 12.10000  ? 111 TRP A CE3  1 
ATOM   1989 C  CZ2  . TRP A 1 111 ? 4.40600   -32.13400 0.55200   1.000 14.68000  ? 111 TRP A CZ2  1 
ATOM   1990 C  CZ3  . TRP A 1 111 ? 2.73700   -32.40800 2.25700   1.000 14.63000  ? 111 TRP A CZ3  1 
ATOM   1991 C  CH2  . TRP A 1 111 ? 3.96900   -32.73600 1.69400   1.000 15.49000  ? 111 TRP A CH2  1 
ATOM   1992 H  H    . TRP A 1 111 ? -2.03000  -28.69900 -0.16800  1.000 16.81000  ? 111 TRP A H    1 
ATOM   1993 H  HA   . TRP A 1 111 ? -0.42500  -29.76000 -1.92700  1.000 18.03000  ? 111 TRP A HA   1 
ATOM   1994 H  HB2  . TRP A 1 111 ? 0.49300   -28.26600 -0.43200  1.000 16.44000  ? 111 TRP A HB2  1 
ATOM   1995 H  HB3  . TRP A 1 111 ? 0.18700   -29.24500 0.78200   1.000 16.44000  ? 111 TRP A HB3  1 
ATOM   1996 H  HD1  . TRP A 1 111 ? 2.56000   -28.96100 -1.99500  1.000 15.42000  ? 111 TRP A HD1  1 
ATOM   1997 H  HE1  . TRP A 1 111 ? 4.44100   -30.44300 -1.67200  1.000 17.19000  ? 111 TRP A HE1  1 
ATOM   1998 H  HE3  . TRP A 1 111 ? 1.06700   -31.30600 2.02000   1.000 14.51000  ? 111 TRP A HE3  1 
ATOM   1999 H  HZ2  . TRP A 1 111 ? 5.23000   -32.35200 0.17900   1.000 17.60000  ? 111 TRP A HZ2  1 
ATOM   2000 H  HZ3  . TRP A 1 111 ? 2.47200   -32.81700 3.04900   1.000 17.54000  ? 111 TRP A HZ3  1 
ATOM   2001 H  HH2  . TRP A 1 111 ? 4.50200   -33.37800 2.10400   1.000 18.58000  ? 111 TRP A HH2  1 
ATOM   2002 N  N    A ARG A 1 112 ? -1.25300  -31.75800 0.47700   0.570 13.49000  ? 112 ARG A N    1 
ATOM   2003 N  N    B ARG A 1 112 ? -1.30000  -31.74000 0.45600   0.430 13.63000  ? 112 ARG A N    1 
ATOM   2004 C  CA   A ARG A 1 112 ? -1.30900  -33.16700 0.84100   0.570 14.95000  ? 112 ARG A CA   1 
ATOM   2005 C  CA   B ARG A 1 112 ? -1.34100  -33.12600 0.89000   0.430 14.74000  ? 112 ARG A CA   1 
ATOM   2006 C  C    A ARG A 1 112 ? -2.04100  -33.97300 -0.23100  0.570 13.80000  ? 112 ARG A C    1 
ATOM   2007 C  C    B ARG A 1 112 ? -2.10100  -33.99700 -0.10600  0.430 14.22000  ? 112 ARG A C    1 
ATOM   2008 O  O    A ARG A 1 112 ? -1.56800  -35.03000 -0.67000  0.570 14.76000  ? 112 ARG A O    1 
ATOM   2009 O  O    B ARG A 1 112 ? -1.72400  -35.15200 -0.33600  0.430 15.77000  ? 112 ARG A O    1 
ATOM   2010 C  CB   A ARG A 1 112 ? -1.96400  -33.33800 2.21700   0.570 18.10000  ? 112 ARG A CB   1 
ATOM   2011 C  CB   B ARG A 1 112 ? -1.97300  -33.20000 2.28200   0.430 17.98000  ? 112 ARG A CB   1 
ATOM   2012 C  CG   A ARG A 1 112 ? -2.27800  -34.80100 2.58100   0.570 23.92000  ? 112 ARG A CG   1 
ATOM   2013 C  CG   B ARG A 1 112 ? -1.89400  -34.56000 2.96100   0.430 21.03000  ? 112 ARG A CG   1 
ATOM   2014 C  CD   A ARG A 1 112 ? -3.01500  -34.95200 3.92500   0.570 30.26000  ? 112 ARG A CD   1 
ATOM   2015 C  CD   B ARG A 1 112 ? -2.34900  -34.44600 4.41600   0.430 26.12000  ? 112 ARG A CD   1 
ATOM   2016 N  NE   A ARG A 1 112 ? -3.25800  -36.35700 4.24100   0.570 38.55000  ? 112 ARG A NE   1 
ATOM   2017 N  NE   B ARG A 1 112 ? -3.50100  -33.56200 4.56200   0.430 32.26000  ? 112 ARG A NE   1 
ATOM   2018 C  CZ   A ARG A 1 112 ? -4.32100  -37.05100 3.85000   0.570 44.38000  ? 112 ARG A CZ   1 
ATOM   2019 C  CZ   B ARG A 1 112 ? -4.75000  -33.89600 4.26300   0.430 35.62000  ? 112 ARG A CZ   1 
ATOM   2020 N  NH1  A ARG A 1 112 ? -5.30700  -36.48900 3.16600   0.570 30.81000  ? 112 ARG A NH1  1 
ATOM   2021 N  NH1  B ARG A 1 112 ? -5.05700  -35.09900 3.80300   0.430 37.37000  ? 112 ARG A NH1  1 
ATOM   2022 N  NH2  A ARG A 1 112 ? -4.39900  -38.34300 4.16000   0.570 44.22000  ? 112 ARG A NH2  1 
ATOM   2023 N  NH2  B ARG A 1 112 ? -5.71800  -33.00200 4.43300   0.430 31.46000  ? 112 ARG A NH2  1 
ATOM   2024 H  H    A ARG A 1 112 ? -1.60500  -31.22400 1.05200   0.570 16.17000  ? 112 ARG A H    1 
ATOM   2025 H  H    B ARG A 1 112 ? -1.70200  -31.19600 0.98700   0.430 16.35000  ? 112 ARG A H    1 
ATOM   2026 H  HA   A ARG A 1 112 ? -0.40500  -33.51200 0.90900   0.570 17.93000  ? 112 ARG A HA   1 
ATOM   2027 H  HA   B ARG A 1 112 ? -0.43700  -33.47300 0.94700   0.430 17.67000  ? 112 ARG A HA   1 
ATOM   2028 H  HB2  A ARG A 1 112 ? -1.36300  -32.98800 2.89400   0.570 21.71000  ? 112 ARG A HB2  1 
ATOM   2029 H  HB2  B ARG A 1 112 ? -1.52200  -32.56200 2.85700   0.430 21.57000  ? 112 ARG A HB2  1 
ATOM   2030 H  HB3  A ARG A 1 112 ? -2.79900  -32.84500 2.22800   0.570 21.71000  ? 112 ARG A HB3  1 
ATOM   2031 H  HB3  B ARG A 1 112 ? -2.91200  -32.96900 2.20400   0.430 21.57000  ? 112 ARG A HB3  1 
ATOM   2032 H  HG2  A ARG A 1 112 ? -2.84100  -35.18200 1.88900   0.570 28.69000  ? 112 ARG A HG2  1 
ATOM   2033 H  HG2  B ARG A 1 112 ? -2.47300  -35.18800 2.50300   0.430 25.22000  ? 112 ARG A HG2  1 
ATOM   2034 H  HG3  A ARG A 1 112 ? -1.44600  -35.29500 2.64200   0.570 28.69000  ? 112 ARG A HG3  1 
ATOM   2035 H  HG3  B ARG A 1 112 ? -0.97900  -34.88000 2.94600   0.430 25.22000  ? 112 ARG A HG3  1 
ATOM   2036 H  HD2  A ARG A 1 112 ? -2.47500  -34.56800 4.63300   0.570 36.30000  ? 112 ARG A HD2  1 
ATOM   2037 H  HD2  B ARG A 1 112 ? -2.59700  -35.32400 4.74300   0.430 31.33000  ? 112 ARG A HD2  1 
ATOM   2038 H  HD3  A ARG A 1 112 ? -3.87100  -34.49700 3.87600   0.570 36.30000  ? 112 ARG A HD3  1 
ATOM   2039 H  HD3  B ARG A 1 112 ? -1.62300  -34.08600 4.95000   0.430 31.33000  ? 112 ARG A HD3  1 
ATOM   2040 H  HE   A ARG A 1 112 ? -2.66800  -36.76500 4.71600   0.570 46.25000  ? 112 ARG A HE   1 
ATOM   2041 H  HE   B ARG A 1 112 ? -3.36100  -32.76900 4.86200   0.430 38.70000  ? 112 ARG A HE   1 
ATOM   2042 H  HH11 A ARG A 1 112 ? -5.26900  -35.65400 2.96300   0.570 36.96000  ? 112 ARG A HH11 1 
ATOM   2043 H  HH11 B ARG A 1 112 ? -4.43900  -35.68700 3.69200   0.430 44.84000  ? 112 ARG A HH11 1 
ATOM   2044 H  HH12 A ARG A 1 112 ? -5.98500  -36.95900 2.92400   0.570 36.96000  ? 112 ARG A HH12 1 
ATOM   2045 H  HH12 B ARG A 1 112 ? -5.87400  -35.29200 3.61700   0.430 44.84000  ? 112 ARG A HH12 1 
ATOM   2046 H  HH21 A ARG A 1 112 ? -3.76700  -38.71800 4.60700   0.570 53.05000  ? 112 ARG A HH21 1 
ATOM   2047 H  HH21 B ARG A 1 112 ? -5.53100  -32.21800 4.73300   0.430 37.74000  ? 112 ARG A HH21 1 
ATOM   2048 H  HH22 A ARG A 1 112 ? -5.08200  -38.80400 3.91300   0.570 53.05000  ? 112 ARG A HH22 1 
ATOM   2049 H  HH22 B ARG A 1 112 ? -6.53100  -33.20800 4.24200   0.430 37.74000  ? 112 ARG A HH22 1 
ATOM   2050 N  N    . ASN A 1 113 ? -3.17800  -33.46800 -0.69700  1.000 13.21000  ? 113 ASN A N    1 
ATOM   2051 C  CA   . ASN A 1 113 ? -4.03800  -34.25000 -1.58100  1.000 14.56000  ? 113 ASN A CA   1 
ATOM   2052 C  C    . ASN A 1 113 ? -3.67200  -34.17700 -3.05600  1.000 17.94000  ? 113 ASN A C    1 
ATOM   2053 O  O    . ASN A 1 113 ? -4.04500  -35.08800 -3.80900  1.000 18.56000  ? 113 ASN A O    1 
ATOM   2054 C  CB   . ASN A 1 113 ? -5.48200  -33.78500 -1.41200  1.000 15.47000  ? 113 ASN A CB   1 
ATOM   2055 C  CG   . ASN A 1 113 ? -6.05900  -34.19000 -0.09300  1.000 16.88000  ? 113 ASN A CG   1 
ATOM   2056 O  OD1  . ASN A 1 113 ? -5.63900  -35.17900 0.50200   1.000 19.73000  ? 113 ASN A OD1  1 
ATOM   2057 N  ND2  . ASN A 1 113 ? -7.07100  -33.47800 0.35400   1.000 17.85000  ? 113 ASN A ND2  1 
ATOM   2058 H  H    . ASN A 1 113 ? -3.47300  -32.68100 -0.51700  1.000 15.84000  ? 113 ASN A H    1 
ATOM   2059 H  HA   . ASN A 1 113 ? -3.96300  -35.18200 -1.32400  1.000 17.46000  ? 113 ASN A HA   1 
ATOM   2060 H  HB2  . ASN A 1 113 ? -5.51200  -32.81800 -1.47000  1.000 18.55000  ? 113 ASN A HB2  1 
ATOM   2061 H  HB3  . ASN A 1 113 ? -6.02600  -34.17700 -2.11300  1.000 18.55000  ? 113 ASN A HB3  1 
ATOM   2062 H  HD21 . ASN A 1 113 ? -7.43500  -33.67400 1.10800   1.000 21.41000  ? 113 ASN A HD21 1 
ATOM   2063 H  HD22 . ASN A 1 113 ? -7.36800  -32.81600 -0.10700  1.000 21.41000  ? 113 ASN A HD22 1 
ATOM   2064 N  N    . ARG A 1 114 ? -2.92900  -33.15400 -3.49800  1.000 15.46000  ? 114 ARG A N    1 
ATOM   2065 C  CA   . ARG A 1 114 ? -2.62800  -32.98500 -4.91100  1.000 16.02000  ? 114 ARG A CA   1 
ATOM   2066 C  C    . ARG A 1 114 ? -1.15700  -32.94700 -5.25900  1.000 16.74000  ? 114 ARG A C    1 
ATOM   2067 O  O    . ARG A 1 114 ? -0.82100  -33.17900 -6.43200  1.000 19.89000  ? 114 ARG A O    1 
ATOM   2068 C  CB   . ARG A 1 114 ? -3.32400  -31.74200 -5.42800  1.000 18.84000  ? 114 ARG A CB   1 
ATOM   2069 C  CG   . ARG A 1 114 ? -4.75700  -31.89000 -4.95400  1.000 23.89000  ? 114 ARG A CG   1 
ATOM   2070 C  CD   . ARG A 1 114 ? -5.63200  -30.94300 -5.56100  1.000 27.90000  ? 114 ARG A CD   1 
ATOM   2071 N  NE   . ARG A 1 114 ? -5.80100  -31.12000 -6.99000  1.000 18.38000  ? 114 ARG A NE   1 
ATOM   2072 C  CZ   . ARG A 1 114 ? -6.52300  -30.25300 -7.67900  1.000 17.61000  ? 114 ARG A CZ   1 
ATOM   2073 N  NH1  . ARG A 1 114 ? -7.14100  -29.25600 -7.07100  1.000 18.96000  ? 114 ARG A NH1  1 
ATOM   2074 N  NH2  . ARG A 1 114 ? -6.64500  -30.40500 -8.98700  1.000 20.06000  ? 114 ARG A NH2  1 
ATOM   2075 H  H    . ARG A 1 114 ? -2.59000  -32.54700 -2.99100  1.000 18.54000  ? 114 ARG A H    1 
ATOM   2076 H  HA   . ARG A 1 114 ? -2.98000  -33.74500 -5.40100  1.000 19.21000  ? 114 ARG A HA   1 
ATOM   2077 H  HB2  . ARG A 1 114 ? -2.92800  -30.94000 -5.05100  1.000 22.60000  ? 114 ARG A HB2  1 
ATOM   2078 H  HB3  . ARG A 1 114 ? -3.29300  -31.70300 -6.39600  1.000 22.60000  ? 114 ARG A HB3  1 
ATOM   2079 H  HG2  . ARG A 1 114 ? -5.07500  -32.77900 -5.17800  1.000 28.65000  ? 114 ARG A HG2  1 
ATOM   2080 H  HG3  . ARG A 1 114 ? -4.79000  -31.75800 -3.99400  1.000 28.65000  ? 114 ARG A HG3  1 
ATOM   2081 H  HD2  . ARG A 1 114 ? -6.50700  -31.02000 -5.15000  1.000 33.47000  ? 114 ARG A HD2  1 
ATOM   2082 H  HD3  . ARG A 1 114 ? -5.27500  -30.05300 -5.41500  1.000 33.47000  ? 114 ARG A HD3  1 
ATOM   2083 H  HE   . ARG A 1 114 ? -5.43200  -31.78700 -7.38800  1.000 22.04000  ? 114 ARG A HE   1 
ATOM   2084 H  HH11 . ARG A 1 114 ? -7.07600  -29.16600 -6.21800  1.000 22.73000  ? 114 ARG A HH11 1 
ATOM   2085 H  HH12 . ARG A 1 114 ? -7.60900  -28.69800 -7.52800  1.000 22.73000  ? 114 ARG A HH12 1 
ATOM   2086 H  HH21 . ARG A 1 114 ? -6.25600  -31.06300 -9.38100  1.000 24.05000  ? 114 ARG A HH21 1 
ATOM   2087 H  HH22 . ARG A 1 114 ? -7.11300  -29.84600 -9.44300  1.000 24.05000  ? 114 ARG A HH22 1 
ATOM   2088 N  N    . CYS A 1 115 ? -0.28200  -32.67900 -4.31800  1.000 13.42000  ? 115 CYS A N    1 
ATOM   2089 C  CA   . CYS A 1 115 ? 1.14400   -32.51900 -4.61000  1.000 13.61000  ? 115 CYS A CA   1 
ATOM   2090 C  C    . CYS A 1 115 ? 2.02100   -33.56700 -3.94400  1.000 15.42000  ? 115 CYS A C    1 
ATOM   2091 O  O    . CYS A 1 115 ? 2.96200   -34.07900 -4.57700  1.000 16.25000  ? 115 CYS A O    1 
ATOM   2092 C  CB   . CYS A 1 115 ? 1.60500   -31.11800 -4.14300  1.000 12.19000  ? 115 CYS A CB   1 
ATOM   2093 S  SG   . CYS A 1 115 ? 0.73500   -29.75400 -4.87500  1.000 14.62000  ? 115 CYS A SG   1 
ATOM   2094 H  H    . CYS A 1 115 ? -0.48100  -32.58000 -3.48800  1.000 16.09000  ? 115 CYS A H    1 
ATOM   2095 H  HA   . CYS A 1 115 ? 1.27600   -32.59400 -5.56800  1.000 16.32000  ? 115 CYS A HA   1 
ATOM   2096 H  HB2  . CYS A 1 115 ? 1.48100   -31.06000 -3.18200  1.000 14.61000  ? 115 CYS A HB2  1 
ATOM   2097 H  HB3  . CYS A 1 115 ? 2.54400   -31.01600 -4.36300  1.000 14.61000  ? 115 CYS A HB3  1 
ATOM   2098 N  N    . LYS A 1 116 ? 1.75300   -33.89700 -2.68600  1.000 14.71000  ? 116 LYS A N    1 
ATOM   2099 C  CA   . LYS A 1 116 ? 2.51700   -34.87800 -1.93300  1.000 15.81000  ? 116 LYS A CA   1 
ATOM   2100 C  C    . LYS A 1 116 ? 2.51400   -36.20700 -2.67000  1.000 16.97000  ? 116 LYS A C    1 
ATOM   2101 O  O    . LYS A 1 116 ? 1.46400   -36.68800 -3.09700  1.000 17.50000  ? 116 LYS A O    1 
ATOM   2102 C  CB   . LYS A 1 116 ? 1.86000   -35.03200 -0.57300  1.000 16.08000  ? 116 LYS A CB   1 
ATOM   2103 C  CG   . LYS A 1 116 ? 2.65300   -35.87500 0.43300   1.000 15.82000  ? 116 LYS A CG   1 
ATOM   2104 C  CD   . LYS A 1 116 ? 1.91500   -35.97100 1.73600   1.000 14.17000  ? 116 LYS A CD   1 
ATOM   2105 C  CE   . LYS A 1 116 ? 2.73000   -36.62900 2.83000   1.000 16.65000  ? 116 LYS A CE   1 
ATOM   2106 N  NZ   . LYS A 1 116 ? 1.99600   -36.67000 4.10500   1.000 18.14000  ? 116 LYS A NZ   1 
ATOM   2107 H  H    . LYS A 1 116 ? 1.10900   -33.55400 -2.23000  1.000 17.64000  ? 116 LYS A H    1 
ATOM   2108 H  HA   . LYS A 1 116 ? 3.43900   -34.59600 -1.82100  1.000 18.96000  ? 116 LYS A HA   1 
ATOM   2109 H  HB2  . LYS A 1 116 ? 1.74200   -34.15000 -0.18600  1.000 19.29000  ? 116 LYS A HB2  1 
ATOM   2110 H  HB3  . LYS A 1 116 ? 0.99700   -35.45900 -0.69500  1.000 19.29000  ? 116 LYS A HB3  1 
ATOM   2111 H  HG2  . LYS A 1 116 ? 2.77600   -36.77100 0.08200   1.000 18.98000  ? 116 LYS A HG2  1 
ATOM   2112 H  HG3  . LYS A 1 116 ? 3.51500   -35.46100 0.59600   1.000 18.98000  ? 116 LYS A HG3  1 
ATOM   2113 H  HD2  . LYS A 1 116 ? 1.68300   -35.07700 2.03400   1.000 16.99000  ? 116 LYS A HD2  1 
ATOM   2114 H  HD3  . LYS A 1 116 ? 1.11100   -36.49600 1.60600   1.000 16.99000  ? 116 LYS A HD3  1 
ATOM   2115 H  HE2  . LYS A 1 116 ? 2.93900   -37.54000 2.57000   1.000 19.97000  ? 116 LYS A HE2  1 
ATOM   2116 H  HE3  . LYS A 1 116 ? 3.54900   -36.12700 2.96600   1.000 19.97000  ? 116 LYS A HE3  1 
ATOM   2117 H  HZ1  . LYS A 1 116 ? 2.41100   -37.20900 4.67800   1.000 21.75000  ? 116 LYS A HZ1  1 
ATOM   2118 H  HZ2  . LYS A 1 116 ? 1.95200   -35.85300 4.45600   1.000 21.75000  ? 116 LYS A HZ2  1 
ATOM   2119 H  HZ3  . LYS A 1 116 ? 1.17000   -36.97200 3.97000   1.000 21.75000  ? 116 LYS A HZ3  1 
ATOM   2120 N  N    . GLY A 1 117 ? 3.70400   -36.79000 -2.82900  1.000 18.62000  ? 117 GLY A N    1 
ATOM   2121 C  CA   . GLY A 1 117 ? 3.83700   -38.06200 -3.52700  1.000 19.69000  ? 117 GLY A CA   1 
ATOM   2122 C  C    . GLY A 1 117 ? 3.87800   -37.97300 -5.03700  1.000 23.52000  ? 117 GLY A C    1 
ATOM   2123 O  O    . GLY A 1 117 ? 3.87800   -39.01400 -5.70500  1.000 27.72000  ? 117 GLY A O    1 
ATOM   2124 H  H    . GLY A 1 117 ? 4.44700   -36.46700 -2.54100  1.000 22.34000  ? 117 GLY A H    1 
ATOM   2125 H  HA2  . GLY A 1 117 ? 4.65700   -38.48900 -3.23600  1.000 23.61000  ? 117 GLY A HA2  1 
ATOM   2126 H  HA3  . GLY A 1 117 ? 3.08400   -38.62500 -3.28700  1.000 23.61000  ? 117 GLY A HA3  1 
ATOM   2127 N  N    . THR A 1 118 ? 3.91500   -36.78100 -5.60800  1.000 18.93000  ? 118 THR A N    1 
ATOM   2128 C  CA   . THR A 1 118 ? 3.98800   -36.59100 -7.04600  1.000 21.36000  ? 118 THR A CA   1 
ATOM   2129 C  C    . THR A 1 118 ? 5.33000   -35.96800 -7.40400  1.000 20.31000  ? 118 THR A C    1 
ATOM   2130 O  O    . THR A 1 118 ? 6.10900   -35.56800 -6.53700  1.000 20.26000  ? 118 THR A O    1 
ATOM   2131 C  CB   . THR A 1 118 ? 2.85100   -35.71000 -7.55300  1.000 21.32000  ? 118 THR A CB   1 
ATOM   2132 O  OG1  . THR A 1 118 ? 3.12700   -34.33000 -7.21000  1.000 19.17000  ? 118 THR A OG1  1 
ATOM   2133 C  CG2  . THR A 1 118 ? 1.52100   -36.12500 -6.95600  1.000 22.82000  ? 118 THR A CG2  1 
ATOM   2134 H  H    . THR A 1 118 ? 3.90000   -36.04300 -5.16800  1.000 22.70000  ? 118 THR A H    1 
ATOM   2135 H  HA   . THR A 1 118 ? 3.90600   -37.45300 -7.48300  1.000 25.62000  ? 118 THR A HA   1 
ATOM   2136 H  HB   . THR A 1 118 ? 2.78100   -35.80100 -8.51600  1.000 25.57000  ? 118 THR A HB   1 
ATOM   2137 H  HG1  . THR A 1 118 ? 3.26200   -34.26100 -6.38400  1.000 22.99000  ? 118 THR A HG1  1 
ATOM   2138 H  HG21 . THR A 1 118 ? 0.79600   -35.66500 -7.40700  1.000 27.37000  ? 118 THR A HG21 1 
ATOM   2139 H  HG22 . THR A 1 118 ? 1.39700   -37.08200 -7.05600  1.000 27.37000  ? 118 THR A HG22 1 
ATOM   2140 H  HG23 . THR A 1 118 ? 1.49700   -35.90100 -6.01200  1.000 27.37000  ? 118 THR A HG23 1 
ATOM   2141 N  N    . ASP A 1 119 ? 5.59200   -35.88600 -8.71000  1.000 21.83000  ? 119 ASP A N    1 
ATOM   2142 C  CA   . ASP A 1 119 ? 6.86200   -35.34000 -9.19900  1.000 23.80000  ? 119 ASP A CA   1 
ATOM   2143 C  C    . ASP A 1 119 ? 6.75400   -33.82300 -9.22100  1.000 20.10000  ? 119 ASP A C    1 
ATOM   2144 O  O    . ASP A 1 119 ? 6.50200   -33.19500 -10.25300 1.000 24.75000  ? 119 ASP A O    1 
ATOM   2145 C  CB   . ASP A 1 119 ? 7.18800   -35.89700 -10.58000 1.000 30.62000  ? 119 ASP A CB   1 
ATOM   2146 C  CG   . ASP A 1 119 ? 8.42900   -35.26100 -11.18600 1.000 37.97000  ? 119 ASP A CG   1 
ATOM   2147 O  OD1  . ASP A 1 119 ? 9.25000   -34.71700 -10.41500 1.000 35.97000  ? 119 ASP A OD1  1 
ATOM   2148 O  OD2  . ASP A 1 119 ? 8.59000   -35.31500 -12.42900 1.000 38.40000  ? 119 ASP A OD2  1 
ATOM   2149 H  H    . ASP A 1 119 ? 5.05300   -36.13800 -9.33100  1.000 26.18000  ? 119 ASP A H    1 
ATOM   2150 H  HA   . ASP A 1 119 ? 7.57400   -35.59100 -8.59100  1.000 28.54000  ? 119 ASP A HA   1 
ATOM   2151 H  HB2  . ASP A 1 119 ? 7.34300   -36.85100 -10.50700 1.000 36.73000  ? 119 ASP A HB2  1 
ATOM   2152 H  HB3  . ASP A 1 119 ? 6.44100   -35.72600 -11.17500 1.000 36.73000  ? 119 ASP A HB3  1 
ATOM   2153 N  N    . VAL A 1 120 ? 6.96800   -33.22500 -8.04100  1.000 21.09000  ? 120 VAL A N    1 
ATOM   2154 C  CA   . VAL A 1 120 ? 6.76800   -31.78000 -7.90000  1.000 18.87000  ? 120 VAL A CA   1 
ATOM   2155 C  C    . VAL A 1 120 ? 7.80400   -30.96500 -8.66700  1.000 20.34000  ? 120 VAL A C    1 
ATOM   2156 O  O    . VAL A 1 120 ? 7.55700   -29.78600 -8.96700  1.000 19.63000  ? 120 VAL A O    1 
ATOM   2157 C  CB   . VAL A 1 120 ? 6.68600   -31.31600 -6.42900  1.000 18.86000  ? 120 VAL A CB   1 
ATOM   2158 C  CG1  . VAL A 1 120 ? 5.46100   -31.90700 -5.74800  1.000 21.67000  ? 120 VAL A CG1  1 
ATOM   2159 C  CG2  . VAL A 1 120 ? 7.94900   -31.64700 -5.69500  1.000 22.55000  ? 120 VAL A CG2  1 
ATOM   2160 H  H    . VAL A 1 120 ? 7.22400   -33.62500 -7.32400  1.000 25.30000  ? 120 VAL A H    1 
ATOM   2161 H  HA   . VAL A 1 120 ? 5.89800   -31.60300 -8.29000  1.000 22.63000  ? 120 VAL A HA   1 
ATOM   2162 H  HB   . VAL A 1 120 ? 6.58900   -30.35100 -6.40500  1.000 22.62000  ? 120 VAL A HB   1 
ATOM   2163 H  HG11 . VAL A 1 120 ? 5.37600   -31.52400 -4.86100  1.000 25.99000  ? 120 VAL A HG11 1 
ATOM   2164 H  HG12 . VAL A 1 120 ? 4.67400   -31.69700 -6.27500  1.000 25.99000  ? 120 VAL A HG12 1 
ATOM   2165 H  HG13 . VAL A 1 120 ? 5.56800   -32.86900 -5.68400  1.000 25.99000  ? 120 VAL A HG13 1 
ATOM   2166 H  HG21 . VAL A 1 120 ? 7.86800   -31.34800 -4.77600  1.000 27.04000  ? 120 VAL A HG21 1 
ATOM   2167 H  HG22 . VAL A 1 120 ? 8.08600   -32.60700 -5.72000  1.000 27.04000  ? 120 VAL A HG22 1 
ATOM   2168 H  HG23 . VAL A 1 120 ? 8.69200   -31.19600 -6.12600  1.000 27.04000  ? 120 VAL A HG23 1 
ATOM   2169 N  N    . GLN A 1 121 ? 8.96800   -31.54200 -8.98000  1.000 20.87000  ? 121 GLN A N    1 
ATOM   2170 C  CA   . GLN A 1 121 ? 9.95400   -30.83500 -9.78600  1.000 20.52000  ? 121 GLN A CA   1 
ATOM   2171 C  C    . GLN A 1 121 ? 9.41200   -30.43700 -11.14700 1.000 20.68000  ? 121 GLN A C    1 
ATOM   2172 O  O    . GLN A 1 121 ? 9.90800   -29.47800 -11.74200 1.000 21.57000  ? 121 GLN A O    1 
ATOM   2173 C  CB   . GLN A 1 121 ? 11.18200  -31.74900 -9.98100  1.000 26.08000  ? 121 GLN A CB   1 
ATOM   2174 C  CG   . GLN A 1 121 ? 12.32400  -31.16600 -10.82200 1.000 63.96000  ? 121 GLN A CG   1 
ATOM   2175 C  CD   . GLN A 1 121 ? 13.16400  -30.11000 -10.10700 1.000 97.46000  ? 121 GLN A CD   1 
ATOM   2176 O  OE1  . GLN A 1 121 ? 14.04000  -29.49700 -10.72000 1.000 101.32000 ? 121 GLN A OE1  1 
ATOM   2177 N  NE2  . GLN A 1 121 ? 12.91100  -29.89700 -8.81600  1.000 101.91000 ? 121 GLN A NE2  1 
ATOM   2178 H  H    . GLN A 1 121 ? 9.20500   -32.33300 -8.74000  1.000 25.04000  ? 121 GLN A H    1 
ATOM   2179 H  HA   . GLN A 1 121 ? 10.22100  -30.02500 -9.32300  1.000 24.61000  ? 121 GLN A HA   1 
ATOM   2180 H  HB2  . GLN A 1 121 ? 11.54700  -31.95800 -9.10700  1.000 31.28000  ? 121 GLN A HB2  1 
ATOM   2181 H  HB3  . GLN A 1 121 ? 10.88900  -32.56200 -10.42100 1.000 31.28000  ? 121 GLN A HB3  1 
ATOM   2182 H  HG2  . GLN A 1 121 ? 12.91900  -31.88800 -11.07800 1.000 76.74000  ? 121 GLN A HG2  1 
ATOM   2183 H  HG3  . GLN A 1 121 ? 11.94500  -30.75200 -11.61300 1.000 76.74000  ? 121 GLN A HG3  1 
ATOM   2184 H  HE21 . GLN A 1 121 ? 12.29500  -30.34700 -8.41900  1.000 122.28000 ? 121 GLN A HE21 1 
ATOM   2185 H  HE22 . GLN A 1 121 ? 13.36400  -29.31000 -8.38000  1.000 122.28000 ? 121 GLN A HE22 1 
ATOM   2186 N  N    . ALA A 1 122 ? 8.39100   -31.13000 -11.63600 1.000 19.13000  ? 122 ALA A N    1 
ATOM   2187 C  CA   . ALA A 1 122 ? 7.78300   -30.77100 -12.90400 1.000 20.50000  ? 122 ALA A CA   1 
ATOM   2188 C  C    . ALA A 1 122 ? 7.29800   -29.33300 -12.90100 1.000 23.45000  ? 122 ALA A C    1 
ATOM   2189 O  O    . ALA A 1 122 ? 7.23200   -28.69200 -13.95600 1.000 21.90000  ? 122 ALA A O    1 
ATOM   2190 C  CB   . ALA A 1 122 ? 6.61700   -31.70500 -13.22100 1.000 28.08000  ? 122 ALA A CB   1 
ATOM   2191 H  H    . ALA A 1 122 ? 8.03200   -31.81100 -11.25200 1.000 22.94000  ? 122 ALA A H    1 
ATOM   2192 H  HA   . ALA A 1 122 ? 8.45000   -30.87200 -13.60100 1.000 24.59000  ? 122 ALA A HA   1 
ATOM   2193 H  HB1  . ALA A 1 122 ? 6.22100   -31.44000 -14.06600 1.000 33.68000  ? 122 ALA A HB1  1 
ATOM   2194 H  HB2  . ALA A 1 122 ? 6.94800   -32.61500 -13.28100 1.000 33.68000  ? 122 ALA A HB2  1 
ATOM   2195 H  HB3  . ALA A 1 122 ? 5.95800   -31.63900 -12.51200 1.000 33.68000  ? 122 ALA A HB3  1 
ATOM   2196 N  N    . TRP A 1 123 ? 6.93200   -28.81000 -11.72300 1.000 19.95000  ? 123 TRP A N    1 
ATOM   2197 C  CA   . TRP A 1 123 ? 6.34900   -27.48000 -11.66100 1.000 19.65000  ? 123 TRP A CA   1 
ATOM   2198 C  C    . TRP A 1 123 ? 7.37000   -26.38300 -11.91700 1.000 20.46000  ? 123 TRP A C    1 
ATOM   2199 O  O    . TRP A 1 123 ? 6.98200   -25.24300 -12.19700 1.000 20.53000  ? 123 TRP A O    1 
ATOM   2200 C  CB   . TRP A 1 123 ? 5.65100   -27.29700 -10.29400 1.000 17.87000  ? 123 TRP A CB   1 
ATOM   2201 C  CG   . TRP A 1 123 ? 4.39200   -28.07600 -10.25000 1.000 18.49000  ? 123 TRP A CG   1 
ATOM   2202 C  CD1  . TRP A 1 123 ? 4.21200   -29.30200 -9.69500  1.000 21.21000  ? 123 TRP A CD1  1 
ATOM   2203 C  CD2  . TRP A 1 123 ? 3.15500   -27.71900 -10.85400 1.000 18.18000  ? 123 TRP A CD2  1 
ATOM   2204 N  NE1  . TRP A 1 123 ? 2.93300   -29.72700 -9.89500  1.000 21.95000  ? 123 TRP A NE1  1 
ATOM   2205 C  CE2  . TRP A 1 123 ? 2.25600   -28.77900 -10.60700 1.000 20.26000  ? 123 TRP A CE2  1 
ATOM   2206 C  CE3  . TRP A 1 123 ? 2.71300   -26.60500 -11.56400 1.000 20.39000  ? 123 TRP A CE3  1 
ATOM   2207 C  CZ2  . TRP A 1 123 ? 0.93500   -28.74800 -11.03600 1.000 26.05000  ? 123 TRP A CZ2  1 
ATOM   2208 C  CZ3  . TRP A 1 123 ? 1.40400   -26.58300 -12.01300 1.000 24.50000  ? 123 TRP A CZ3  1 
ATOM   2209 C  CH2  . TRP A 1 123 ? 0.53500   -27.65700 -11.75600 1.000 26.17000  ? 123 TRP A CH2  1 
ATOM   2210 H  H    . TRP A 1 123 ? 7.01100   -29.20400 -10.96300 1.000 23.92000  ? 123 TRP A H    1 
ATOM   2211 H  HA   . TRP A 1 123 ? 5.67200   -27.38600 -12.34900 1.000 23.56000  ? 123 TRP A HA   1 
ATOM   2212 H  HB2  . TRP A 1 123 ? 6.23500   -27.61100 -9.58600  1.000 21.43000  ? 123 TRP A HB2  1 
ATOM   2213 H  HB3  . TRP A 1 123 ? 5.44100   -26.35900 -10.16000 1.000 21.43000  ? 123 TRP A HB3  1 
ATOM   2214 H  HD1  . TRP A 1 123 ? 4.86800   -29.78300 -9.24300  1.000 25.44000  ? 123 TRP A HD1  1 
ATOM   2215 H  HE1  . TRP A 1 123 ? 2.60500   -30.47200 -9.61700  1.000 26.32000  ? 123 TRP A HE1  1 
ATOM   2216 H  HE3  . TRP A 1 123 ? 3.28600   -25.89200 -11.73300 1.000 24.46000  ? 123 TRP A HE3  1 
ATOM   2217 H  HZ2  . TRP A 1 123 ? 0.34600   -29.44100 -10.84100 1.000 31.25000  ? 123 TRP A HZ2  1 
ATOM   2218 H  HZ3  . TRP A 1 123 ? 1.09500   -25.84700 -12.49100 1.000 29.38000  ? 123 TRP A HZ3  1 
ATOM   2219 H  HH2  . TRP A 1 123 ? -0.33500  -27.62400 -12.08400 1.000 31.39000  ? 123 TRP A HH2  1 
ATOM   2220 N  N    . ILE A 1 124 ? 8.66100   -26.68500 -11.83300 1.000 19.19000  ? 124 ILE A N    1 
ATOM   2221 C  CA   . ILE A 1 124 ? 9.69700   -25.69800 -12.10300 1.000 18.72000  ? 124 ILE A CA   1 
ATOM   2222 C  C    . ILE A 1 124 ? 10.49300  -26.03300 -13.36100 1.000 18.54000  ? 124 ILE A C    1 
ATOM   2223 O  O    . ILE A 1 124 ? 11.46800  -25.33700 -13.67200 1.000 20.49000  ? 124 ILE A O    1 
ATOM   2224 C  CB   . ILE A 1 124 ? 10.57500  -25.43700 -10.86900 1.000 20.58000  ? 124 ILE A CB   1 
ATOM   2225 C  CG1  . ILE A 1 124 ? 11.33300  -26.67700 -10.42500 1.000 24.01000  ? 124 ILE A CG1  1 
ATOM   2226 C  CG2  . ILE A 1 124 ? 9.66600   -24.89900 -9.71500  1.000 22.26000  ? 124 ILE A CG2  1 
ATOM   2227 C  CD1  . ILE A 1 124 ? 12.49300  -26.34300 -9.50400  1.000 33.59000  ? 124 ILE A CD1  1 
ATOM   2228 H  H    . ILE A 1 124 ? 8.96300   -27.46200 -11.61800 1.000 23.01000  ? 124 ILE A H    1 
ATOM   2229 H  HA   . ILE A 1 124 ? 9.26800   -24.84900 -12.29700 1.000 22.46000  ? 124 ILE A HA   1 
ATOM   2230 H  HB   . ILE A 1 124 ? 11.24600  -24.77800 -11.10600 1.000 24.68000  ? 124 ILE A HB   1 
ATOM   2231 H  HG12 . ILE A 1 124 ? 10.72700  -27.26500 -9.94700  1.000 28.80000  ? 124 ILE A HG12 1 
ATOM   2232 H  HG13 . ILE A 1 124 ? 11.68700  -27.13000 -11.20600 1.000 28.80000  ? 124 ILE A HG13 1 
ATOM   2233 H  HG21 . ILE A 1 124 ? 10.21400  -24.73100 -8.93300  1.000 26.70000  ? 124 ILE A HG21 1 
ATOM   2234 H  HG22 . ILE A 1 124 ? 9.24200   -24.07600 -10.00500 1.000 26.70000  ? 124 ILE A HG22 1 
ATOM   2235 H  HG23 . ILE A 1 124 ? 8.99000   -25.56400 -9.50900  1.000 26.70000  ? 124 ILE A HG23 1 
ATOM   2236 H  HD11 . ILE A 1 124 ? 12.98200  -27.15600 -9.30400  1.000 40.29000  ? 124 ILE A HD11 1 
ATOM   2237 H  HD12 . ILE A 1 124 ? 13.07600  -25.70700 -9.94800  1.000 40.29000  ? 124 ILE A HD12 1 
ATOM   2238 H  HD13 . ILE A 1 124 ? 12.14500  -25.95600 -8.68500  1.000 40.29000  ? 124 ILE A HD13 1 
ATOM   2239 N  N    A ARG A 1 125 ? 10.07000  -27.05100 -14.10300 0.390 19.78000  ? 125 ARG A N    1 
ATOM   2240 N  N    B ARG A 1 125 ? 10.07000  -27.04100 -14.11200 0.610 19.67000  ? 125 ARG A N    1 
ATOM   2241 C  CA   A ARG A 1 125 ? 10.73600  -27.42600 -15.34600 0.390 25.04000  ? 125 ARG A CA   1 
ATOM   2242 C  CA   B ARG A 1 125 ? 10.79600  -27.44200 -15.31700 0.610 24.94000  ? 125 ARG A CA   1 
ATOM   2243 C  C    A ARG A 1 125 ? 10.78100  -26.23400 -16.28800 0.390 21.76000  ? 125 ARG A C    1 
ATOM   2244 C  C    B ARG A 1 125 ? 10.77100  -26.31600 -16.33800 0.610 21.67000  ? 125 ARG A C    1 
ATOM   2245 O  O    A ARG A 1 125 ? 9.78900   -25.51400 -16.45100 0.390 24.98000  ? 125 ARG A O    1 
ATOM   2246 O  O    B ARG A 1 125 ? 9.71300   -25.74600 -16.63200 0.610 25.72000  ? 125 ARG A O    1 
ATOM   2247 C  CB   A ARG A 1 125 ? 9.96300   -28.57200 -16.00300 0.390 30.64000  ? 125 ARG A CB   1 
ATOM   2248 C  CB   B ARG A 1 125 ? 10.15200  -28.69200 -15.91600 0.610 30.37000  ? 125 ARG A CB   1 
ATOM   2249 C  CG   A ARG A 1 125 ? 10.80200  -29.49100 -16.88300 0.390 39.60000  ? 125 ARG A CG   1 
ATOM   2250 C  CG   B ARG A 1 125 ? 10.94400  -29.35000 -17.05200 0.610 37.90000  ? 125 ARG A CG   1 
ATOM   2251 C  CD   A ARG A 1 125 ? 9.96700   -30.19000 -17.95800 0.390 37.98000  ? 125 ARG A CD   1 
ATOM   2252 C  CD   B ARG A 1 125 ? 11.10600  -30.85400 -16.80200 0.610 50.07000  ? 125 ARG A CD   1 
ATOM   2253 N  NE   A ARG A 1 125 ? 8.55700   -30.31600 -17.60000 0.390 47.22000  ? 125 ARG A NE   1 
ATOM   2254 N  NE   B ARG A 1 125 ? 12.03800  -31.49700 -17.72300 0.610 64.54000  ? 125 ARG A NE   1 
ATOM   2255 C  CZ   A ARG A 1 125 ? 8.03800   -31.32000 -16.90300 0.390 44.92000  ? 125 ARG A CZ   1 
ATOM   2256 C  CZ   B ARG A 1 125 ? 11.72600  -31.92800 -18.93900 0.610 49.00000  ? 125 ARG A CZ   1 
ATOM   2257 N  NH1  A ARG A 1 125 ? 8.78400   -32.32400 -16.47200 0.390 39.23000  ? 125 ARG A NH1  1 
ATOM   2258 N  NH1  B ARG A 1 125 ? 10.50900  -31.78500 -19.43400 0.610 52.31000  ? 125 ARG A NH1  1 
ATOM   2259 N  NH2  A ARG A 1 125 ? 6.73500   -31.31700 -16.63500 0.390 42.31000  ? 125 ARG A NH2  1 
ATOM   2260 N  NH2  B ARG A 1 125 ? 12.66100  -32.52100 -19.67600 0.610 54.38000  ? 125 ARG A NH2  1 
ATOM   2261 H  H    A ARG A 1 125 ? 9.39400   -27.54600 -13.90800 0.390 23.73000  ? 125 ARG A H    1 
ATOM   2262 H  H    B ARG A 1 125 ? 9.36800   -27.51100 -13.94900 0.610 23.59000  ? 125 ARG A H    1 
ATOM   2263 H  HA   A ARG A 1 125 ? 11.64400  -27.71600 -15.16400 0.390 30.03000  ? 125 ARG A HA   1 
ATOM   2264 H  HA   B ARG A 1 125 ? 11.71800  -27.64100 -15.09000 0.610 29.92000  ? 125 ARG A HA   1 
ATOM   2265 H  HB2  A ARG A 1 125 ? 9.56900   -29.11700 -15.30400 0.390 36.76000  ? 125 ARG A HB2  1 
ATOM   2266 H  HB2  B ARG A 1 125 ? 10.05000  -29.35200 -15.21300 0.610 36.43000  ? 125 ARG A HB2  1 
ATOM   2267 H  HB3  A ARG A 1 125 ? 9.26600   -28.19200 -16.56000 0.390 36.76000  ? 125 ARG A HB3  1 
ATOM   2268 H  HB3  B ARG A 1 125 ? 9.28300   -28.44800 -16.27100 0.610 36.43000  ? 125 ARG A HB3  1 
ATOM   2269 H  HG2  A ARG A 1 125 ? 11.48800  -28.96800 -17.32700 0.390 47.51000  ? 125 ARG A HG2  1 
ATOM   2270 H  HG2  B ARG A 1 125 ? 10.47100  -29.22600 -17.89000 0.610 45.46000  ? 125 ARG A HG2  1 
ATOM   2271 H  HG3  A ARG A 1 125 ? 11.21300  -30.17400 -16.32900 0.390 47.51000  ? 125 ARG A HG3  1 
ATOM   2272 H  HG3  B ARG A 1 125 ? 11.82600  -28.95000 -17.10600 0.610 45.46000  ? 125 ARG A HG3  1 
ATOM   2273 H  HD2  A ARG A 1 125 ? 10.02000  -29.67800 -18.78000 0.390 45.56000  ? 125 ARG A HD2  1 
ATOM   2274 H  HD2  B ARG A 1 125 ? 11.43900  -30.98800 -15.90000 0.610 60.07000  ? 125 ARG A HD2  1 
ATOM   2275 H  HD3  A ARG A 1 125 ? 10.31900  -31.08300 -18.09900 0.390 45.56000  ? 125 ARG A HD3  1 
ATOM   2276 H  HD3  B ARG A 1 125 ? 10.24300  -31.28400 -16.90400 0.610 60.07000  ? 125 ARG A HD3  1 
ATOM   2277 H  HE   A ARG A 1 125 ? 8.02300   -29.69500 -17.86100 0.390 56.65000  ? 125 ARG A HE   1 
ATOM   2278 H  HE   B ARG A 1 125 ? 12.84900  -31.60600 -17.45800 0.610 77.44000  ? 125 ARG A HE   1 
ATOM   2279 H  HH11 A ARG A 1 125 ? 9.62700   -32.33800 -16.64300 0.390 47.06000  ? 125 ARG A HH11 1 
ATOM   2280 H  HH11 B ARG A 1 125 ? 9.89600   -31.40500 -18.96600 0.610 62.75000  ? 125 ARG A HH11 1 
ATOM   2281 H  HH12 A ARG A 1 125 ? 8.42700   -32.96300 -16.02200 0.390 47.06000  ? 125 ARG A HH12 1 
ATOM   2282 H  HH12 B ARG A 1 125 ? 10.33000  -32.07100 -20.22500 0.610 62.75000  ? 125 ARG A HH12 1 
ATOM   2283 H  HH21 A ARG A 1 125 ? 6.24000   -30.67100 -16.91300 0.390 50.76000  ? 125 ARG A HH21 1 
ATOM   2284 H  HH21 B ARG A 1 125 ? 13.45500  -32.62200 -19.36400 0.610 65.24000  ? 125 ARG A HH21 1 
ATOM   2285 H  HH22 A ARG A 1 125 ? 6.38700   -31.96100 -16.18400 0.390 50.76000  ? 125 ARG A HH22 1 
ATOM   2286 H  HH22 B ARG A 1 125 ? 12.47000  -32.80400 -20.46600 0.610 65.24000  ? 125 ARG A HH22 1 
ATOM   2287 N  N    . GLY A 1 126 ? 11.94700  -26.00900 -16.89600 1.000 23.67000  ? 126 GLY A N    1 
ATOM   2288 C  CA   . GLY A 1 126 ? 12.09000  -24.97400 -17.89500 1.000 22.94000  ? 126 GLY A CA   1 
ATOM   2289 C  C    . GLY A 1 126 ? 12.35800  -23.59100 -17.35800 1.000 25.57000  ? 126 GLY A C    1 
ATOM   2290 O  O    . GLY A 1 126 ? 12.68600  -22.69200 -18.14600 1.000 28.79000  ? 126 GLY A O    1 
ATOM   2291 H  H    . GLY A 1 126 ? 12.68800  -26.40100 -16.70100 1.000 28.39000  ? 126 GLY A H    1 
ATOM   2292 H  HA2  . GLY A 1 126 ? 12.82600  -25.21000 -18.48000 1.000 27.51000  ? 126 GLY A HA2  1 
ATOM   2293 H  HA3  . GLY A 1 126 ? 11.27300  -24.93300 -18.41600 1.000 27.51000  ? 126 GLY A HA3  1 
ATOM   2294 N  N    . CYS A 1 127 ? 12.23100  -23.38300 -16.05100 1.000 19.56000  ? 127 CYS A N    1 
ATOM   2295 C  CA   . CYS A 1 127 ? 12.34600  -22.05600 -15.48100 1.000 21.46000  ? 127 CYS A CA   1 
ATOM   2296 C  C    . CYS A 1 127 ? 13.79600  -21.67600 -15.25400 1.000 23.81000  ? 127 CYS A C    1 
ATOM   2297 O  O    . CYS A 1 127 ? 14.61700  -22.49800 -14.80800 1.000 23.33000  ? 127 CYS A O    1 
ATOM   2298 C  CB   . CYS A 1 127 ? 11.66000  -22.01800 -14.12100 1.000 21.28000  ? 127 CYS A CB   1 
ATOM   2299 S  SG   . CYS A 1 127 ? 9.88200   -22.36200 -14.12900 1.000 20.93000  ? 127 CYS A SG   1 
ATOM   2300 H  H    . CYS A 1 127 ? 12.07700  -24.00100 -15.47300 1.000 23.46000  ? 127 CYS A H    1 
ATOM   2301 H  HA   . CYS A 1 127 ? 11.93700  -21.42600 -16.09500 1.000 25.73000  ? 127 CYS A HA   1 
ATOM   2302 H  HB2  . CYS A 1 127 ? 12.07900  -22.68200 -13.55000 1.000 25.52000  ? 127 CYS A HB2  1 
ATOM   2303 H  HB3  . CYS A 1 127 ? 11.78100  -21.13300 -13.74400 1.000 25.52000  ? 127 CYS A HB3  1 
ATOM   2304 N  N    A ARG A 1 128 ? 14.09000  -20.40700 -15.53000 0.390 24.94000  ? 128 ARG A N    1 
ATOM   2305 N  N    B ARG A 1 128 ? 14.11700  -20.42300 -15.55100 0.610 24.93000  ? 128 ARG A N    1 
ATOM   2306 C  CA   A ARG A 1 128 ? 15.39100  -19.80300 -15.27000 0.390 26.01000  ? 128 ARG A CA   1 
ATOM   2307 C  CA   B ARG A 1 128 ? 15.44500  -19.89100 -15.27400 0.610 25.75000  ? 128 ARG A CA   1 
ATOM   2308 C  C    A ARG A 1 128 ? 15.41400  -19.35700 -13.81400 0.390 26.51000  ? 128 ARG A C    1 
ATOM   2309 C  C    B ARG A 1 128 ? 15.44900  -19.37000 -13.84400 0.610 26.34000  ? 128 ARG A C    1 
ATOM   2310 O  O    A ARG A 1 128 ? 14.77300  -18.36200 -13.45600 0.390 33.54000  ? 128 ARG A O    1 
ATOM   2311 O  O    B ARG A 1 128 ? 14.82900  -18.34200 -13.54400 0.610 33.68000  ? 128 ARG A O    1 
ATOM   2312 C  CB   A ARG A 1 128 ? 15.55300  -18.59400 -16.18800 0.390 31.18000  ? 128 ARG A CB   1 
ATOM   2313 C  CB   B ARG A 1 128 ? 15.82100  -18.79700 -16.26700 0.610 31.33000  ? 128 ARG A CB   1 
ATOM   2314 C  CG   A ARG A 1 128 ? 16.78900  -18.59300 -17.06500 0.390 35.31000  ? 128 ARG A CG   1 
ATOM   2315 C  CG   B ARG A 1 128 ? 17.32000  -18.66300 -16.44100 0.610 31.48000  ? 128 ARG A CG   1 
ATOM   2316 C  CD   A ARG A 1 128 ? 16.81900  -17.36600 -17.98900 0.390 29.20000  ? 128 ARG A CD   1 
ATOM   2317 C  CD   B ARG A 1 128 ? 17.68700  -17.53100 -17.38200 0.610 25.96000  ? 128 ARG A CD   1 
ATOM   2318 N  NE   A ARG A 1 128 ? 16.21000  -17.61800 -19.29400 0.390 40.15000  ? 128 ARG A NE   1 
ATOM   2319 N  NE   B ARG A 1 128 ? 19.13300  -17.37100 -17.45600 0.610 33.14000  ? 128 ARG A NE   1 
ATOM   2320 C  CZ   A ARG A 1 128 ? 15.23500  -16.89900 -19.84300 0.390 32.05000  ? 128 ARG A CZ   1 
ATOM   2321 C  CZ   B ARG A 1 128 ? 19.92800  -18.08200 -18.24500 0.610 37.50000  ? 128 ARG A CZ   1 
ATOM   2322 N  NH1  A ARG A 1 128 ? 14.70300  -15.85700 -19.22700 0.390 35.41000  ? 128 ARG A NH1  1 
ATOM   2323 N  NH1  B ARG A 1 128 ? 19.44400  -18.98100 -19.08900 0.610 38.78000  ? 128 ARG A NH1  1 
ATOM   2324 N  NH2  A ARG A 1 128 ? 14.78200  -17.23600 -21.04700 0.390 31.73000  ? 128 ARG A NH2  1 
ATOM   2325 N  NH2  B ARG A 1 128 ? 21.24200  -17.89200 -18.18200 0.610 42.02000  ? 128 ARG A NH2  1 
ATOM   2326 H  H    A ARG A 1 128 ? 13.53200  -19.85600 -15.88100 0.390 29.92000  ? 128 ARG A H    1 
ATOM   2327 H  H    B ARG A 1 128 ? 13.58100  -19.85900 -15.91500 0.610 29.91000  ? 128 ARG A H    1 
ATOM   2328 H  HA   A ARG A 1 128 ? 16.10800  -20.43800 -15.42600 0.390 31.19000  ? 128 ARG A HA   1 
ATOM   2329 H  HA   B ARG A 1 128 ? 16.10400  -20.59800 -15.35600 0.610 30.89000  ? 128 ARG A HA   1 
ATOM   2330 H  HB2  A ARG A 1 128 ? 14.78300  -18.55300 -16.77600 0.390 37.41000  ? 128 ARG A HB2  1 
ATOM   2331 H  HB2  B ARG A 1 128 ? 15.43600  -19.00900 -17.13200 0.610 37.58000  ? 128 ARG A HB2  1 
ATOM   2332 H  HB3  A ARG A 1 128 ? 15.59200  -17.79700 -15.63600 0.390 37.41000  ? 128 ARG A HB3  1 
ATOM   2333 H  HB3  B ARG A 1 128 ? 15.47700  -17.94800 -15.94900 0.610 37.58000  ? 128 ARG A HB3  1 
ATOM   2334 H  HG2  A ARG A 1 128 ? 17.58100  -18.57400 -16.50500 0.390 42.36000  ? 128 ARG A HG2  1 
ATOM   2335 H  HG2  B ARG A 1 128 ? 17.72500  -18.48200 -15.57800 0.610 37.76000  ? 128 ARG A HG2  1 
ATOM   2336 H  HG3  A ARG A 1 128 ? 16.79200  -19.39100 -17.61600 0.390 42.36000  ? 128 ARG A HG3  1 
ATOM   2337 H  HG3  B ARG A 1 128 ? 17.67400  -19.48800 -16.80700 0.610 37.76000  ? 128 ARG A HG3  1 
ATOM   2338 H  HD2  A ARG A 1 128 ? 16.33100  -16.64200 -17.56600 0.390 35.03000  ? 128 ARG A HD2  1 
ATOM   2339 H  HD2  B ARG A 1 128 ? 17.35300  -17.72700 -18.27100 0.610 31.14000  ? 128 ARG A HD2  1 
ATOM   2340 H  HD3  A ARG A 1 128 ? 17.74100  -17.10500 -18.13500 0.390 35.03000  ? 128 ARG A HD3  1 
ATOM   2341 H  HD3  B ARG A 1 128 ? 17.30200  -16.70100 -17.05900 0.610 31.14000  ? 128 ARG A HD3  1 
ATOM   2342 H  HE   A ARG A 1 128 ? 16.50800  -18.28700 -19.74600 0.390 48.16000  ? 128 ARG A HE   1 
ATOM   2343 H  HE   B ARG A 1 128 ? 19.49700  -16.77500 -16.95400 0.610 39.76000  ? 128 ARG A HE   1 
ATOM   2344 H  HH11 A ARG A 1 128 ? 14.98600  -15.62800 -18.44800 0.390 42.48000  ? 128 ARG A HH11 1 
ATOM   2345 H  HH11 B ARG A 1 128 ? 18.59500  -19.11400 -19.13400 0.610 46.52000  ? 128 ARG A HH11 1 
ATOM   2346 H  HH12 A ARG A 1 128 ? 14.07300  -15.41000 -19.60400 0.390 42.48000  ? 128 ARG A HH12 1 
ATOM   2347 H  HH12 B ARG A 1 128 ? 19.97700  -19.43000 -19.59100 0.610 46.52000  ? 128 ARG A HH12 1 
ATOM   2348 H  HH21 A ARG A 1 128 ? 15.11800  -17.91000 -21.46100 0.390 38.06000  ? 128 ARG A HH21 1 
ATOM   2349 H  HH21 B ARG A 1 128 ? 21.56700  -17.31300 -17.63400 0.610 50.41000  ? 128 ARG A HH21 1 
ATOM   2350 H  HH22 A ARG A 1 128 ? 14.15100  -16.77800 -21.41300 0.390 38.06000  ? 128 ARG A HH22 1 
ATOM   2351 H  HH22 B ARG A 1 128 ? 21.76800  -18.34600 -18.68800 0.610 50.41000  ? 128 ARG A HH22 1 
ATOM   2352 N  N    . LEU A 1 129 ? 16.13300  -20.08800 -12.96700 1.000 23.49000  ? 129 LEU A N    1 
ATOM   2353 C  CA   . LEU A 1 129 ? 16.15300  -19.79100 -11.54900 1.000 28.54000  ? 129 LEU A CA   1 
ATOM   2354 C  C    . LEU A 1 129 ? 17.53900  -19.55400 -10.97600 1.000 36.33000  ? 129 LEU A C    1 
ATOM   2355 O  O    . LEU A 1 129 ? 17.67000  -19.23400 -9.79200  1.000 33.19000  ? 129 LEU A O    1 
ATOM   2356 C  CB   . LEU A 1 129 ? 15.50400  -20.94300 -10.77000 1.000 28.75000  ? 129 LEU A CB   1 
ATOM   2357 C  CG   . LEU A 1 129 ? 14.02200  -21.14400 -11.05900 1.000 31.34000  ? 129 LEU A CG   1 
ATOM   2358 C  CD1  . LEU A 1 129 ? 13.57700  -22.51700 -10.60300 1.000 44.39000  ? 129 LEU A CD1  1 
ATOM   2359 C  CD2  . LEU A 1 129 ? 13.19900  -20.03800 -10.38100 1.000 38.16000  ? 129 LEU A CD2  1 
ATOM   2360 O  OXT  . LEU A 1 129 ? 18.54700  -19.70600 -11.65900 1.000 37.50000  ? 129 LEU A OXT  1 
ATOM   2361 H  H    . LEU A 1 129 ? 16.60900  -20.77300 -13.17700 1.000 28.18000  ? 129 LEU A H    1 
ATOM   2362 H  HA   . LEU A 1 129 ? 15.65800  -18.96500 -11.43300 1.000 34.23000  ? 129 LEU A HA   1 
ATOM   2363 H  HB2  . LEU A 1 129 ? 15.96300  -21.76700 -10.99800 1.000 34.48000  ? 129 LEU A HB2  1 
ATOM   2364 H  HB3  . LEU A 1 129 ? 15.59700  -20.76400 -9.82100  1.000 34.48000  ? 129 LEU A HB3  1 
ATOM   2365 H  HG   . LEU A 1 129 ? 13.86500  -21.08900 -12.01500 1.000 37.59000  ? 129 LEU A HG   1 
ATOM   2366 H  HD11 . LEU A 1 129 ? 12.63300  -22.62300 -10.79500 1.000 53.26000  ? 129 LEU A HD11 1 
ATOM   2367 H  HD12 . LEU A 1 129 ? 14.08900  -23.18900 -11.08000 1.000 53.26000  ? 129 LEU A HD12 1 
ATOM   2368 H  HD13 . LEU A 1 129 ? 13.73200  -22.59900 -9.64900  1.000 53.26000  ? 129 LEU A HD13 1 
ATOM   2369 H  HD21 . LEU A 1 129 ? 12.26000  -20.17700 -10.57700 1.000 45.78000  ? 129 LEU A HD21 1 
ATOM   2370 H  HD22 . LEU A 1 129 ? 13.34600  -20.07700 -9.42300  1.000 45.78000  ? 129 LEU A HD22 1 
ATOM   2371 H  HD23 . LEU A 1 129 ? 13.48500  -19.17700 -10.72400 1.000 45.78000  ? 129 LEU A HD23 1 
HETATM 2372 C  C1   . EDO B 2 .   ? 7.82200   -29.01800 10.51600  1.000 32.76000  ? 201 EDO A C1   1 
HETATM 2373 O  O1   . EDO B 2 .   ? 6.63000   -28.26900 10.78900  1.000 21.38000  ? 201 EDO A O1   1 
HETATM 2374 C  C2   . EDO B 2 .   ? 9.02700   -28.40400 11.22600  1.000 46.75000  ? 201 EDO A C2   1 
HETATM 2375 O  O2   . EDO B 2 .   ? 8.80700   -28.42600 12.63900  1.000 61.68000  ? 201 EDO A O2   1 
HETATM 2376 H  H11  . EDO B 2 .   ? 7.68900   -30.04900 10.85000  1.000 39.30000  ? 201 EDO A H11  1 
HETATM 2377 H  H12  . EDO B 2 .   ? 8.00300   -29.03400 9.43900   1.000 39.30000  ? 201 EDO A H12  1 
HETATM 2378 H  HO1  . EDO B 2 .   ? 6.16800   -28.08400 9.96000   1.000 25.64000  ? 201 EDO A HO1  1 
HETATM 2379 H  H21  . EDO B 2 .   ? 9.93000   -28.96700 10.98200  1.000 56.08000  ? 201 EDO A H21  1 
HETATM 2380 H  H22  . EDO B 2 .   ? 9.17200   -27.37500 10.88900  1.000 56.08000  ? 201 EDO A H22  1 
HETATM 2381 H  HO2  . EDO B 2 .   ? 9.52600   -27.95800 13.08400  1.000 74.00000  ? 201 EDO A HO2  1 
HETATM 2382 C  C1   A EDO C 2 .   ? -3.16300  -21.79600 6.42000   0.610 26.94000  ? 202 EDO A C1   1 
HETATM 2383 C  C1   B EDO C 2 .   ? -3.55000  -22.11500 5.40400   0.390 27.63000  ? 202 EDO A C1   1 
HETATM 2384 O  O1   A EDO C 2 .   ? -4.37600  -21.73300 5.68400   0.610 20.62000  ? 202 EDO A O1   1 
HETATM 2385 O  O1   B EDO C 2 .   ? -4.94000  -22.08900 5.02800   0.390 24.99000  ? 202 EDO A O1   1 
HETATM 2386 C  C2   A EDO C 2 .   ? -2.56500  -23.17200 6.18800   0.610 28.28000  ? 202 EDO A C2   1 
HETATM 2387 C  C2   B EDO C 2 .   ? -3.06400  -23.55200 5.52200   0.390 23.08000  ? 202 EDO A C2   1 
HETATM 2388 O  O2   A EDO C 2 .   ? -3.38300  -24.13100 6.86300   0.610 25.92000  ? 202 EDO A O2   1 
HETATM 2389 O  O2   B EDO C 2 .   ? -4.18100  -24.44100 5.49000   0.390 34.26000  ? 202 EDO A O2   1 
HETATM 2390 H  H11  A EDO C 2 .   ? -2.47300  -21.01900 6.08400   0.610 32.31000  ? 202 EDO A H11  1 
HETATM 2391 H  H11  B EDO C 2 .   ? -2.95700  -21.58700 4.65400   0.390 33.15000  ? 202 EDO A H11  1 
HETATM 2392 H  H12  A EDO C 2 .   ? -3.35500  -21.63800 7.48300   0.610 32.31000  ? 202 EDO A H12  1 
HETATM 2393 H  H12  B EDO C 2 .   ? -3.41700  -21.60300 6.35900   0.390 33.15000  ? 202 EDO A H12  1 
HETATM 2394 H  HO1  A EDO C 2 .   ? -4.97900  -22.42100 5.99600   0.610 24.73000  ? 202 EDO A HO1  1 
HETATM 2395 H  HO1  B EDO C 2 .   ? -5.24600  -21.17200 4.99200   0.390 29.97000  ? 202 EDO A HO1  1 
HETATM 2396 H  H21  A EDO C 2 .   ? -2.53000  -23.39200 5.11900   0.610 33.92000  ? 202 EDO A H21  1 
HETATM 2397 H  H21  B EDO C 2 .   ? -2.38400  -23.78200 4.69900   0.390 27.69000  ? 202 EDO A H21  1 
HETATM 2398 H  H22  A EDO C 2 .   ? -1.54400  -23.20900 6.57300   0.610 33.92000  ? 202 EDO A H22  1 
HETATM 2399 H  H22  B EDO C 2 .   ? -2.51600  -23.68200 6.45700   0.390 27.69000  ? 202 EDO A H22  1 
HETATM 2400 H  HO2  A EDO C 2 .   ? -2.94900  -24.99500 6.84200   0.610 31.09000  ? 202 EDO A HO2  1 
HETATM 2401 H  HO2  B EDO C 2 .   ? -3.86900  -25.35400 5.55200   0.390 41.10000  ? 202 EDO A HO2  1 
HETATM 2402 C  C1   . EDO D 2 .   ? -15.25700 -15.16000 0.49900   0.320 14.96000  ? 203 EDO A C1   1 
HETATM 2403 O  O1   . EDO D 2 .   ? -13.96200 -14.75600 0.93800   0.320 21.23000  ? 203 EDO A O1   1 
HETATM 2404 C  C2   . EDO D 2 .   ? -15.44500 -14.66400 -0.91900  0.320 19.63000  ? 203 EDO A C2   1 
HETATM 2405 O  O2   . EDO D 2 .   ? -14.51000 -15.31300 -1.78900  0.320 14.93000  ? 203 EDO A O2   1 
HETATM 2406 H  H11  . EDO D 2 .   ? -15.34600 -16.24800 0.53300   0.320 17.94000  ? 203 EDO A H11  1 
HETATM 2407 H  H12  . EDO D 2 .   ? -16.02600 -14.74000 1.15100   0.320 17.94000  ? 203 EDO A H12  1 
HETATM 2408 H  HO1  . EDO D 2 .   ? -13.84300 -15.00600 1.86400   0.320 25.47000  ? 203 EDO A HO1  1 
HETATM 2409 H  H21  . EDO D 2 .   ? -16.46400 -14.87200 -1.25100  0.320 23.55000  ? 203 EDO A H21  1 
HETATM 2410 H  H22  . EDO D 2 .   ? -15.29300 -13.58300 -0.95500  0.320 23.55000  ? 203 EDO A H22  1 
HETATM 2411 H  HO2  . EDO D 2 .   ? -14.63600 -14.99400 -2.69300  0.320 17.91000  ? 203 EDO A HO2  1 
HETATM 2412 C  C1   . EDO E 2 .   ? 15.70500  -16.50800 -8.98700  0.300 30.09000  ? 204 EDO A C1   1 
HETATM 2413 O  O1   . EDO E 2 .   ? 15.95000  -15.61600 -7.89600  0.300 32.62000  ? 204 EDO A O1   1 
HETATM 2414 C  C2   . EDO E 2 .   ? 16.10600  -15.83500 -10.29300 0.300 25.52000  ? 204 EDO A C2   1 
HETATM 2415 O  O2   . EDO E 2 .   ? 15.24200  -14.72300 -10.55000 0.300 31.11000  ? 204 EDO A O2   1 
HETATM 2416 H  H11  . EDO E 2 .   ? 16.27900  -17.42600 -8.85100  0.300 36.09000  ? 204 EDO A H11  1 
HETATM 2417 H  H12  . EDO E 2 .   ? 14.64600  -16.77500 -9.01600  0.300 36.09000  ? 204 EDO A H12  1 
HETATM 2418 H  HO1  . EDO E 2 .   ? 15.72200  -16.05300 -7.06500  0.300 39.14000  ? 204 EDO A HO1  1 
HETATM 2419 H  H21  . EDO E 2 .   ? 17.14100  -15.49300 -10.23000 0.300 30.61000  ? 204 EDO A H21  1 
HETATM 2420 H  H22  . EDO E 2 .   ? 16.03900  -16.55300 -11.11400 0.300 30.61000  ? 204 EDO A H22  1 
HETATM 2421 H  HO2  . EDO E 2 .   ? 15.50100  -14.29800 -11.37900 0.300 37.32000  ? 204 EDO A HO2  1 
HETATM 2422 C  C1   . EDO F 2 .   ? 6.82300   -35.37900 -3.27000  1.000 43.17000  ? 205 EDO A C1   1 
HETATM 2423 O  O1   . EDO F 2 .   ? 6.28900   -35.99400 -2.09100  1.000 35.61000  ? 205 EDO A O1   1 
HETATM 2424 C  C2   . EDO F 2 .   ? 7.51900   -34.07400 -2.89600  1.000 34.59000  ? 205 EDO A C2   1 
HETATM 2425 O  O2   . EDO F 2 .   ? 6.99700   -33.53900 -1.66700  1.000 28.82000  ? 205 EDO A O2   1 
HETATM 2426 H  H11  . EDO F 2 .   ? 7.53500   -36.05400 -3.75000  1.000 51.79000  ? 205 EDO A H11  1 
HETATM 2427 H  H12  . EDO F 2 .   ? 6.01900   -35.18000 -3.98200  1.000 51.79000  ? 205 EDO A H12  1 
HETATM 2428 H  HO1  . EDO F 2 .   ? 6.16800   -36.94100 -2.24700  1.000 42.72000  ? 205 EDO A HO1  1 
HETATM 2429 H  H21  . EDO F 2 .   ? 8.59100   -34.25200 -2.78800  1.000 41.50000  ? 205 EDO A H21  1 
HETATM 2430 H  H22  . EDO F 2 .   ? 7.37900   -33.34600 -3.69800  1.000 41.50000  ? 205 EDO A H22  1 
HETATM 2431 H  HO2  . EDO F 2 .   ? 7.44800   -32.71000 -1.45900  1.000 34.58000  ? 205 EDO A HO2  1 
HETATM 2432 C  C1   . EDO G 2 .   ? 2.77900   -6.41500  2.18700   1.000 51.36000  ? 206 EDO A C1   1 
HETATM 2433 O  O1   . EDO G 2 .   ? 1.47100   -6.87300  1.82200   1.000 50.72000  ? 206 EDO A O1   1 
HETATM 2434 C  C2   . EDO G 2 .   ? 3.84000   -7.07300  1.31300   1.000 46.94000  ? 206 EDO A C2   1 
HETATM 2435 O  O2   . EDO G 2 .   ? 3.57200   -8.46900  1.14500   1.000 28.98000  ? 206 EDO A O2   1 
HETATM 2436 H  H11  . EDO G 2 .   ? 2.83300   -5.33000  2.07200   1.000 61.62000  ? 206 EDO A H11  1 
HETATM 2437 H  H12  . EDO G 2 .   ? 2.97000   -6.65200  3.23500   1.000 61.62000  ? 206 EDO A H12  1 
HETATM 2438 H  HO1  . EDO G 2 .   ? 0.80600   -6.38300  2.32500   1.000 60.85000  ? 206 EDO A HO1  1 
HETATM 2439 H  H21  . EDO G 2 .   ? 3.86100   -6.58700  0.33600   1.000 56.32000  ? 206 EDO A H21  1 
HETATM 2440 H  H22  . EDO G 2 .   ? 4.82200   -6.94400  1.77300   1.000 56.32000  ? 206 EDO A H22  1 
HETATM 2441 H  HO2  . EDO G 2 .   ? 4.26000   -8.86500  0.59300   1.000 34.76000  ? 206 EDO A HO2  1 
HETATM 2442 CL CL   . CL  H 3 .   ? 8.47300   -31.71800 7.57100   1.000 19.96000  ? 207 CL  A CL   1 
HETATM 2443 CL CL   . CL  I 3 .   ? 11.22400  -31.89000 -1.69200  1.000 25.24000  ? 208 CL  A CL   1 
HETATM 2444 CL CL   . CL  J 3 .   ? 7.33400   -10.35400 -4.32700  1.000 46.29000  ? 209 CL  A CL   1 
HETATM 2445 CL CL   . CL  K 3 .   ? 0.75600   -23.42700 -14.92900 1.000 47.78000  ? 210 CL  A CL   1 
HETATM 2446 NA NA   . NA  L 4 .   ? -7.81000  -14.38400 12.91600  1.000 19.23000  ? 211 NA  A NA   1 
HETATM 2447 NA NA   . NA  M 4 .   ? 11.26700  -29.07600 -6.84700  1.000 24.75000  ? 212 NA  A NA   1 
HETATM 2448 O  O    . HOH N 5 .   ? 14.43200  -31.04900 -0.03000  1.000 29.91000  ? 301 HOH A O    1 
HETATM 2449 O  O    . HOH N 5 .   ? -0.71700  -12.29000 17.37100  1.000 48.00000  ? 302 HOH A O    1 
HETATM 2450 O  O    . HOH N 5 .   ? -7.14000  -24.26400 0.92400   1.000 35.81000  ? 303 HOH A O    1 
HETATM 2451 O  O    . HOH N 5 .   ? -1.76700  -33.77300 -8.66000  1.000 29.78000  ? 304 HOH A O    1 
HETATM 2452 O  O    . HOH N 5 .   ? -0.88800  -13.48700 -2.08200  1.000 25.99000  ? 305 HOH A O    1 
HETATM 2453 O  O    A HOH N 5 .   ? -12.45100 -13.47100 18.54600  0.640 30.64000  ? 306 HOH A O    1 
HETATM 2454 O  O    B HOH N 5 .   ? -12.58100 -11.98100 17.97600  0.360 38.60000  ? 306 HOH A O    1 
HETATM 2455 O  O    . HOH N 5 .   ? -8.04000  -24.28300 -1.27400  1.000 28.88000  ? 307 HOH A O    1 
HETATM 2456 O  O    . HOH N 5 .   ? 0.60700   -11.66300 -1.92400  1.000 33.80000  ? 308 HOH A O    1 
HETATM 2457 O  O    . HOH N 5 .   ? -12.24600 -25.11100 12.40000  1.000 32.81000  ? 309 HOH A O    1 
HETATM 2458 O  O    . HOH N 5 .   ? -3.85000  -23.64700 9.43200   1.000 31.61000  ? 310 HOH A O    1 
HETATM 2459 O  O    . HOH N 5 .   ? -11.25500 -13.10000 -4.11100  1.000 19.03000  ? 311 HOH A O    1 
HETATM 2460 O  O    . HOH N 5 .   ? -0.48600  -18.01200 -14.76500 1.000 30.57000  ? 312 HOH A O    1 
HETATM 2461 O  O    . HOH N 5 .   ? -13.67500 -14.80000 7.78400   1.000 18.28000  ? 313 HOH A O    1 
HETATM 2462 O  O    . HOH N 5 .   ? -1.50700  -24.19900 15.03300  1.000 52.16000  ? 314 HOH A O    1 
HETATM 2463 O  O    . HOH N 5 .   ? 2.15600   -11.69400 -14.16400 1.000 49.09000  ? 315 HOH A O    1 
HETATM 2464 O  O    . HOH N 5 .   ? -3.31900  -7.62600  -5.69400  1.000 39.80000  ? 316 HOH A O    1 
HETATM 2465 O  O    . HOH N 5 .   ? -1.23200  -36.26000 -3.27200  1.000 23.10000  ? 317 HOH A O    1 
HETATM 2466 O  O    . HOH N 5 .   ? -7.36100  -25.93100 -3.24500  1.000 27.43000  ? 318 HOH A O    1 
HETATM 2467 O  O    . HOH N 5 .   ? -5.21300  -10.62500 -9.50100  1.000 18.06000  ? 319 HOH A O    1 
HETATM 2468 O  O    . HOH N 5 .   ? -2.69000  -6.95100  -8.28300  1.000 38.48000  ? 320 HOH A O    1 
HETATM 2469 O  O    . HOH N 5 .   ? -5.69600  -26.14000 1.95400   1.000 21.23000  ? 321 HOH A O    1 
HETATM 2470 O  O    . HOH N 5 .   ? 2.97000   -32.45600 -9.28900  1.000 30.06000  ? 322 HOH A O    1 
HETATM 2471 O  O    B HOH N 5 .   ? 2.60400   -27.13400 9.74700   0.450 20.57000  ? 323 HOH A O    1 
HETATM 2472 O  O    . HOH N 5 .   ? 6.487     -35.130   0.585     1.000 23.54000  ? 324 HOH A O    1 
HETATM 2473 O  O    . HOH N 5 .   ? 12.12400  -12.27000 -8.45700  0.500 38.82000  ? 325 HOH A O    1 
HETATM 2474 O  O    . HOH N 5 .   ? -8.69500  -22.98600 -3.06100  1.000 32.03000  ? 326 HOH A O    1 
HETATM 2475 O  O    . HOH N 5 .   ? 10.71600  -31.78900 5.26300   1.000 21.60000  ? 327 HOH A O    1 
HETATM 2476 O  O    . HOH N 5 .   ? 14.48500  -17.46600 5.39200   1.000 49.89000  ? 328 HOH A O    1 
HETATM 2477 O  O    . HOH N 5 .   ? -1.38300  -16.34400 0.85300   1.000 15.12000  ? 329 HOH A O    1 
HETATM 2478 O  O    . HOH N 5 .   ? 6.65900   -9.69900  6.02400   1.000 46.11000  ? 330 HOH A O    1 
HETATM 2479 O  O    A HOH N 5 .   ? 15.11800  -20.00700 -1.83900  0.490 18.28000  ? 331 HOH A O    1 
HETATM 2480 O  O    B HOH N 5 .   ? 14.46300  -26.11900 -4.27000  0.510 16.05000  ? 331 HOH A O    1 
HETATM 2481 O  O    . HOH N 5 .   ? -8.72700  -22.45000 0.01400   1.000 28.46000  ? 332 HOH A O    1 
HETATM 2482 O  O    . HOH N 5 .   ? -17.190   -21.555   13.979    1.000 45.82000  ? 333 HOH A O    1 
HETATM 2483 O  O    . HOH N 5 .   ? -10.49000 -23.66800 9.59100   1.000 46.79000  ? 334 HOH A O    1 
HETATM 2484 O  O    . HOH N 5 .   ? -7.838    -23.850   -7.526    1.000 41.74000  ? 335 HOH A O    1 
HETATM 2485 O  O    . HOH N 5 .   ? -13.81000 -22.34200 -4.79000  1.000 62.36000  ? 336 HOH A O    1 
HETATM 2486 O  O    A HOH N 5 .   ? 12.09900  -18.38100 -16.29500 0.670 29.38000  ? 337 HOH A O    1 
HETATM 2487 O  O    B HOH N 5 .   ? 12.11500  -18.18700 -13.88200 0.330 19.75000  ? 337 HOH A O    1 
HETATM 2488 O  O    . HOH N 5 .   ? -6.73400  -39.59000 5.45900   1.000 61.28000  ? 338 HOH A O    1 
HETATM 2489 O  O    . HOH N 5 .   ? -8.00300  -17.45500 -8.24800  1.000 25.12000  ? 339 HOH A O    1 
HETATM 2490 O  O    . HOH N 5 .   ? -0.32200  -38.38700 3.44100   1.000 33.93000  ? 340 HOH A O    1 
HETATM 2491 O  O    . HOH N 5 .   ? 7.38100   -10.45600 -10.35200 1.000 53.42000  ? 341 HOH A O    1 
HETATM 2492 O  O    . HOH N 5 .   ? -4.95800  -9.05500  15.95400  1.000 37.16000  ? 342 HOH A O    1 
HETATM 2493 O  O    . HOH N 5 .   ? -19.044   -16.200   0.931     1.000 29.87000  ? 343 HOH A O    1 
HETATM 2494 O  O    . HOH N 5 .   ? 20.93100  -19.83200 -21.54200 1.000 48.68000  ? 344 HOH A O    1 
HETATM 2495 O  O    . HOH N 5 .   ? -2.657    -19.431   23.714    1.000 31.14000  ? 345 HOH A O    1 
HETATM 2496 O  O    . HOH N 5 .   ? 15.98900  -22.11800 2.10100   1.000 46.22000  ? 346 HOH A O    1 
HETATM 2497 O  O    . HOH N 5 .   ? 10.68100  -8.07800  0.39900   1.000 46.11000  ? 347 HOH A O    1 
HETATM 2498 O  O    . HOH N 5 .   ? 15.40500  -24.71200 6.45100   1.000 33.28000  ? 348 HOH A O    1 
HETATM 2499 O  O    . HOH N 5 .   ? 1.40200   -11.36400 0.31700   1.000 23.07000  ? 349 HOH A O    1 
HETATM 2500 O  O    . HOH N 5 .   ? -5.43500  -6.08800  11.64500  1.000 42.04000  ? 350 HOH A O    1 
HETATM 2501 O  O    . HOH N 5 .   ? -16.84700 -7.31200  11.44900  1.000 43.17000  ? 351 HOH A O    1 
HETATM 2502 O  O    . HOH N 5 .   ? -0.46000  -4.47200  -4.34400  1.000 47.10000  ? 352 HOH A O    1 
HETATM 2503 O  O    . HOH N 5 .   ? -9.68600  -12.77600 12.11300  1.000 22.08000  ? 353 HOH A O    1 
HETATM 2504 O  O    . HOH N 5 .   ? 2.92500   -23.15600 -17.13600 1.000 48.69000  ? 354 HOH A O    1 
HETATM 2505 O  O    B HOH N 5 .   ? -17.34600 -15.03200 7.55900   0.510 25.17000  ? 355 HOH A O    1 
HETATM 2506 O  O    . HOH N 5 .   ? -7.57800  -12.31000 14.32100  1.000 27.27000  ? 356 HOH A O    1 
HETATM 2507 O  O    . HOH N 5 .   ? -13.89600 -25.70700 4.94800   1.000 33.62000  ? 357 HOH A O    1 
HETATM 2508 O  O    . HOH N 5 .   ? -2.13100  -9.80100  -13.27800 1.000 32.18000  ? 358 HOH A O    1 
HETATM 2509 O  O    . HOH N 5 .   ? 16.16300  -24.33500 -12.88600 1.000 50.56000  ? 359 HOH A O    1 
HETATM 2510 O  O    . HOH N 5 .   ? -18.737   -9.851    6.109     1.000 20.93000  ? 360 HOH A O    1 
HETATM 2511 O  O    . HOH N 5 .   ? 3.82400   -37.41500 -10.78500 1.000 36.76000  ? 361 HOH A O    1 
HETATM 2512 O  O    . HOH N 5 .   ? -3.09200  -14.08300 18.27300  1.000 27.06000  ? 362 HOH A O    1 
HETATM 2513 O  O    . HOH N 5 .   ? 5.75400   -22.01100 14.20400  1.000 51.53000  ? 363 HOH A O    1 
HETATM 2514 O  O    . HOH N 5 .   ? -9.992    -5.462    12.386    1.000 31.44000  ? 364 HOH A O    1 
HETATM 2515 O  O    . HOH N 5 .   ? 8.93400   -16.01100 9.41900   1.000 57.74000  ? 365 HOH A O    1 
HETATM 2516 O  O    . HOH N 5 .   ? 11.85400  -12.42300 2.61400   1.000 56.36000  ? 366 HOH A O    1 
HETATM 2517 O  O    . HOH N 5 .   ? -11.59400 -11.72300 14.12200  1.000 20.14000  ? 367 HOH A O    1 
HETATM 2518 O  O    . HOH N 5 .   ? 13.30800  -18.09100 8.87700   1.000 49.37000  ? 368 HOH A O    1 
HETATM 2519 O  O    . HOH N 5 .   ? -1.30900  -27.74500 10.65200  1.000 49.68000  ? 369 HOH A O    1 
HETATM 2520 O  O    . HOH N 5 .   ? 12.04800  -35.55800 -11.80900 1.000 61.23000  ? 370 HOH A O    1 
HETATM 2521 O  O    . HOH N 5 .   ? -8.82200  -25.75900 13.02400  1.000 44.97000  ? 371 HOH A O    1 
HETATM 2522 O  O    A HOH N 5 .   ? -2.23400  -7.20900  12.80000  0.560 30.03000  ? 372 HOH A O    1 
HETATM 2523 O  O    B HOH N 5 .   ? -3.56400  -7.10900  12.71500  0.440 31.68000  ? 372 HOH A O    1 
HETATM 2524 O  O    . HOH N 5 .   ? 8.242     -30.169   15.333    1.000 47.33000  ? 373 HOH A O    1 
HETATM 2525 O  O    . HOH N 5 .   ? -8.95300  -20.72900 16.84700  1.000 52.32000  ? 374 HOH A O    1 
HETATM 2526 O  O    . HOH N 5 .   ? 6.30300   -17.32100 -16.10700 1.000 25.03000  ? 375 HOH A O    1 
HETATM 2527 O  O    . HOH N 5 .   ? 10.87800  -32.87700 -13.99900 1.000 54.56000  ? 376 HOH A O    1 
HETATM 2528 O  O    . HOH N 5 .   ? 16.09800  -30.03700 -4.14400  1.000 57.52000  ? 377 HOH A O    1 
HETATM 2529 O  O    . HOH N 5 .   ? 4.60100   -22.56000 -18.52700 1.000 49.64000  ? 378 HOH A O    1 
HETATM 2530 O  O    . HOH N 5 .   ? 0.94700   -34.36600 9.81200   1.000 50.55000  ? 379 HOH A O    1 
HETATM 2531 O  O    . HOH N 5 .   ? 4.06800   -12.11500 7.83000   1.000 46.49000  ? 380 HOH A O    1 
HETATM 2532 O  O    . HOH N 5 .   ? -6.111    -24.848   -10.347   1.000 46.89000  ? 381 HOH A O    1 
HETATM 2533 O  O    . HOH N 5 .   ? 1.86300   -19.70000 -16.57200 1.000 51.68000  ? 382 HOH A O    1 
HETATM 2534 O  O    . HOH N 5 .   ? 11.78600  -30.27500 8.55800   1.000 44.73000  ? 383 HOH A O    1 
HETATM 2535 O  O    . HOH N 5 .   ? -4.89100  -4.89100  0.00000   0.50  49.45000  ? 384 HOH A O    1 
HETATM 2536 O  O    . HOH N 5 .   ? 5.04300   -28.17100 -16.51100 1.000 59.75000  ? 385 HOH A O    1 
HETATM 2537 O  O    . HOH N 5 .   ? 7.71100   -38.34700 -5.37600  1.000 60.27000  ? 386 HOH A O    1 
HETATM 2538 O  O    . HOH N 5 .   ? 20.455    -20.857   -14.283   1.000 58.14000  ? 387 HOH A O    1 
HETATM 2539 O  O    . HOH N 5 .   ? -6.229    -20.851   21.134    1.000 38.76000  ? 388 HOH A O    1 
HETATM 2540 O  O    . HOH N 5 .   ? 0.14000   -14.27100 20.74500  1.000 55.38000  ? 389 HOH A O    1 
HETATM 2541 O  O    . HOH N 5 .   ? -4.36100  -7.78200  -10.92100 1.000 55.48000  ? 390 HOH A O    1 
HETATM 2542 O  O    . HOH N 5 .   ? -13.29800 -24.37400 14.23800  1.000 49.73000  ? 391 HOH A O    1 
HETATM 2543 O  O    . HOH N 5 .   ? 5.53900   -11.12700 13.17900  1.000 52.65000  ? 392 HOH A O    1 
HETATM 2544 O  O    . HOH N 5 .   ? -2.45900  -34.43700 7.82200   1.000 57.59000  ? 393 HOH A O    1 
HETATM 2545 O  O    . HOH N 5 .   ? -11.61800 -23.82900 0.96300   1.000 57.14000  ? 394 HOH A O    1 
HETATM 2546 O  O    . HOH N 5 .   ? -5.81200  -24.93600 -14.45900 1.000 57.74000  ? 395 HOH A O    1 
HETATM 2547 O  O    . HOH N 5 .   ? 9.64100   -21.65500 -19.69700 1.000 58.95000  ? 396 HOH A O    1 
HETATM 2548 O  O    . HOH N 5 .   ? 15.123    -29.352   7.227     1.000 39.50000  ? 397 HOH A O    1 
HETATM 2549 O  O    . HOH N 5 .   ? -14.14400 -11.35600 15.69300  1.000 48.43000  ? 398 HOH A O    1 
HETATM 2550 O  O    . HOH N 5 .   ? -11.00900 -7.41400  15.17900  1.000 65.90000  ? 399 HOH A O    1 
HETATM 2551 O  O    . HOH N 5 .   ? -13.658   -6.603    15.676    1.000 51.03000  ? 400 HOH A O    1 
HETATM 2552 O  O    . HOH N 5 .   ? -9.45900  -19.51600 -10.81600 1.000 53.72000  ? 401 HOH A O    1 
HETATM 2553 O  O    . HOH N 5 .   ? 3.32200   -29.08700 -15.13100 1.000 47.70000  ? 402 HOH A O    1 
HETATM 2554 O  O    . HOH N 5 .   ? 7.83900   -39.52100 -8.02900  1.000 64.19000  ? 403 HOH A O    1 
HETATM 2555 O  O    . HOH N 5 .   ? 0.32600   -39.44100 0.21600   1.000 55.84000  ? 404 HOH A O    1 
# 
