data_9FC9
# 
_entry.id   9FC9 
# 
_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   9FC9         pdb_00009fc9 10.2210/pdb9fc9/pdb 
WWPDB D_1292137235 ?            ?                   
# 
_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                        9FC9 
_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    105 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '1,4-beta-N-acetylmuramidase C,Allergen Gal d IV' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 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 94  HOH HOH A . 
N 5 HOH 2   302 78  HOH HOH A . 
N 5 HOH 3   303 100 HOH HOH A . 
N 5 HOH 4   304 71  HOH HOH A . 
N 5 HOH 5   305 116 HOH HOH A . 
N 5 HOH 6   306 147 HOH HOH A . 
N 5 HOH 7   307 41  HOH HOH A . 
N 5 HOH 8   308 25  HOH HOH A . 
N 5 HOH 9   309 27  HOH HOH A . 
N 5 HOH 10  310 109 HOH HOH A . 
N 5 HOH 11  311 75  HOH HOH A . 
N 5 HOH 12  312 99  HOH HOH A . 
N 5 HOH 13  313 128 HOH HOH A . 
N 5 HOH 14  314 5   HOH HOH A . 
N 5 HOH 15  315 81  HOH HOH A . 
N 5 HOH 16  316 131 HOH HOH A . 
N 5 HOH 17  317 122 HOH HOH A . 
N 5 HOH 18  318 1   HOH HOH A . 
N 5 HOH 19  319 118 HOH HOH A . 
N 5 HOH 20  320 105 HOH HOH A . 
N 5 HOH 21  321 15  HOH HOH A . 
N 5 HOH 22  322 97  HOH HOH A . 
N 5 HOH 23  323 3   HOH HOH A . 
N 5 HOH 24  324 4   HOH HOH A . 
N 5 HOH 25  325 130 HOH HOH A . 
N 5 HOH 26  326 106 HOH HOH A . 
N 5 HOH 27  327 43  HOH HOH A . 
N 5 HOH 28  328 7   HOH HOH A . 
N 5 HOH 29  329 2   HOH HOH A . 
N 5 HOH 30  330 6   HOH HOH A . 
N 5 HOH 31  331 11  HOH HOH A . 
N 5 HOH 32  332 9   HOH HOH A . 
N 5 HOH 33  333 57  HOH HOH A . 
N 5 HOH 34  334 47  HOH HOH A . 
N 5 HOH 35  335 127 HOH HOH A . 
N 5 HOH 36  336 144 HOH HOH A . 
N 5 HOH 37  337 16  HOH HOH A . 
N 5 HOH 38  338 33  HOH HOH A . 
N 5 HOH 39  339 17  HOH HOH A . 
N 5 HOH 40  340 14  HOH HOH A . 
N 5 HOH 41  341 117 HOH HOH A . 
N 5 HOH 42  342 74  HOH HOH A . 
N 5 HOH 43  343 115 HOH HOH A . 
N 5 HOH 44  344 8   HOH HOH A . 
N 5 HOH 45  345 12  HOH HOH A . 
N 5 HOH 46  346 10  HOH HOH A . 
N 5 HOH 47  347 138 HOH HOH A . 
N 5 HOH 48  348 36  HOH HOH A . 
N 5 HOH 49  349 124 HOH HOH A . 
N 5 HOH 50  350 28  HOH HOH A . 
N 5 HOH 51  351 49  HOH HOH A . 
N 5 HOH 52  352 134 HOH HOH A . 
N 5 HOH 53  353 79  HOH HOH A . 
N 5 HOH 54  354 50  HOH HOH A . 
N 5 HOH 55  355 22  HOH HOH A . 
N 5 HOH 56  356 44  HOH HOH A . 
N 5 HOH 57  357 46  HOH HOH A . 
N 5 HOH 58  358 108 HOH HOH A . 
N 5 HOH 59  359 61  HOH HOH A . 
N 5 HOH 60  360 34  HOH HOH A . 
N 5 HOH 61  361 55  HOH HOH A . 
N 5 HOH 62  362 126 HOH HOH A . 
N 5 HOH 63  363 23  HOH HOH A . 
N 5 HOH 64  364 45  HOH HOH A . 
N 5 HOH 65  365 13  HOH HOH A . 
N 5 HOH 66  366 29  HOH HOH A . 
N 5 HOH 67  367 20  HOH HOH A . 
N 5 HOH 68  368 66  HOH HOH A . 
N 5 HOH 69  369 145 HOH HOH A . 
N 5 HOH 70  370 24  HOH HOH A . 
N 5 HOH 71  371 112 HOH HOH A . 
N 5 HOH 72  372 86  HOH HOH A . 
N 5 HOH 73  373 96  HOH HOH A . 
N 5 HOH 74  374 129 HOH HOH A . 
N 5 HOH 75  375 59  HOH HOH A . 
N 5 HOH 76  376 18  HOH HOH A . 
N 5 HOH 77  377 132 HOH HOH A . 
N 5 HOH 78  378 63  HOH HOH A . 
N 5 HOH 79  379 143 HOH HOH A . 
N 5 HOH 80  380 37  HOH HOH A . 
N 5 HOH 81  381 146 HOH HOH A . 
N 5 HOH 82  382 53  HOH HOH A . 
N 5 HOH 83  383 52  HOH HOH A . 
N 5 HOH 84  384 77  HOH HOH A . 
N 5 HOH 85  385 60  HOH HOH A . 
N 5 HOH 86  386 67  HOH HOH A . 
N 5 HOH 87  387 30  HOH HOH A . 
N 5 HOH 88  388 93  HOH HOH A . 
N 5 HOH 89  389 111 HOH HOH A . 
N 5 HOH 90  390 107 HOH HOH A . 
N 5 HOH 91  391 58  HOH HOH A . 
N 5 HOH 92  392 120 HOH HOH A . 
N 5 HOH 93  393 142 HOH HOH A . 
N 5 HOH 94  394 62  HOH HOH A . 
N 5 HOH 95  395 125 HOH HOH A . 
N 5 HOH 96  396 133 HOH HOH A . 
N 5 HOH 97  397 87  HOH HOH A . 
N 5 HOH 98  398 101 HOH HOH A . 
N 5 HOH 99  399 72  HOH HOH A . 
N 5 HOH 100 400 73  HOH HOH A . 
N 5 HOH 101 401 139 HOH HOH A . 
N 5 HOH 102 402 91  HOH HOH A . 
N 5 HOH 103 403 110 HOH HOH A . 
N 5 HOH 104 404 137 HOH HOH A . 
N 5 HOH 105 405 135 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                     9FC9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     79.656 
_cell.length_a_esd                 ? 
_cell.length_b                     79.656 
_cell.length_b_esd                 ? 
_cell.length_c                     37.327 
_cell.length_c_esd                 ? 
_cell.volume                       236842.739 
_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                         9FC9 
_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                   9FC9 
_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             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.46 
_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, SITTING 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                          18.47 
_reflns.entry_id                                       9FC9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.4 
_reflns.d_resolution_low                               28.16 
_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                                     24202 
_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                           99.93 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.64 
_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                                   0.998 
_reflns.pdbx_CC_star                                   0.999 
_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                           1.97 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2354 
_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                                  0.79 
_reflns_shell.pdbx_CC_star                                  0.939 
_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                               24.71 
_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                                 9FC9 
_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                             28.16 
_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                     24202 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  22202 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 8.26 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1604 
_refine.ls_R_factor_R_free                       0.1854 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1580 
_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                 18.5417 
_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                            0.1600 
_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                        28.16 
_refine_hist.number_atoms_solvent             105 
_refine_hist.number_atoms_total               1136 
_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' ? 0.0085  ? 1276 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9969  ? 1735 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0780  ? 168  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0101  ? 241  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.9838 ? 486  ? 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 1.44  . . 139 1543 99.82  . . . . 0.3030 . . . . . . . . . . . 0.3639 
'X-RAY DIFFRACTION' 1.44 1.47  . . 140 1544 100.00 . . . . 0.2533 . . . . . . . . . . . 0.3008 
'X-RAY DIFFRACTION' 1.47 1.52  . . 141 1565 100.00 . . . . 0.2315 . . . . . . . . . . . 0.2173 
'X-RAY DIFFRACTION' 1.52 1.57  . . 139 1560 99.94  . . . . 0.1941 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 1.57 1.62  . . 141 1566 100.00 . . . . 0.1950 . . . . . . . . . . . 0.2140 
'X-RAY DIFFRACTION' 1.62 1.69  . . 141 1561 100.00 . . . . 0.1862 . . . . . . . . . . . 0.1986 
'X-RAY DIFFRACTION' 1.69 1.76  . . 142 1578 100.00 . . . . 0.1906 . . . . . . . . . . . 0.2233 
'X-RAY DIFFRACTION' 1.76 1.86  . . 142 1574 100.00 . . . . 0.1672 . . . . . . . . . . . 0.1937 
'X-RAY DIFFRACTION' 1.86 1.97  . . 140 1559 99.82  . . . . 0.1518 . . . . . . . . . . . 0.1625 
'X-RAY DIFFRACTION' 1.97 2.13  . . 143 1581 99.94  . . . . 0.1416 . . . . . . . . . . . 0.1749 
'X-RAY DIFFRACTION' 2.13 2.34  . . 145 1609 99.94  . . . . 0.1355 . . . . . . . . . . . 0.1601 
'X-RAY DIFFRACTION' 2.34 2.68  . . 145 1604 100.00 . . . . 0.1370 . . . . . . . . . . . 0.1671 
'X-RAY DIFFRACTION' 2.68 3.37  . . 146 1630 100.00 . . . . 0.1417 . . . . . . . . . . . 0.1703 
'X-RAY DIFFRACTION' 3.37 28.16 . . 156 1728 99.84  . . . . 0.1568 . . . . . . . . . . . 0.1853 
# 
_struct.entry_id                     9FC9 
_struct.title                        'HEN EGG-WHITE Lysozyme incubated at 50% 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        9FC9 
_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              9FC9 
_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)' 1790 ? 
1 MORE         -41  ? 
1 'SSA (A^2)'  6830 ? 
# 
_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 ? ? ? ? ? ? ? 1.990 ? ? 
disulf2 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 115 SG ? ? A CYS 30  A CYS 115 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 80  SG ? ? A CYS 64  A CYS 80  1_555 ? ? ? ? ? ? ? 2.058 ? ? 
disulf4 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 94  SG ? ? A CYS 76  A CYS 94  1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc1 metalc ? ? A SER 24 OG ? ? ? 1_555 M NA  .   NA ? ? A SER 24  A NA  212 1_555 ? ? ? ? ? ? ? 2.866 ? ? 
metalc2 metalc ? ? A SER 60 O  ? ? ? 1_555 L NA  .   NA ? ? A SER 60  A NA  211 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc3 metalc ? ? A CYS 64 O  ? ? ? 1_555 L NA  .   NA ? ? A CYS 64  A NA  211 1_555 ? ? ? ? ? ? ? 2.401 ? ? 
metalc4 metalc ? ? A SER 72 OG ? ? ? 1_555 L NA  .   NA ? ? A SER 72  A NA  211 1_555 ? ? ? ? ? ? ? 2.512 ? ? 
metalc5 metalc ? ? A ARG 73 O  ? ? ? 1_555 L NA  .   NA ? ? A ARG 73  A NA  211 1_555 ? ? ? ? ? ? ? 2.355 ? ? 
metalc6 metalc ? ? L NA  .  NA ? ? ? 1_555 N HOH .   O  ? ? A NA  211 A HOH 344 1_555 ? ? ? ? ? ? ? 2.589 ? ? 
metalc7 metalc ? ? L NA  .  NA ? ? ? 1_555 N HOH .   O  ? ? A NA  211 A HOH 370 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
# 
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 SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? A CYS 64 ? A CYS 64  ? 1_555 88.9  ? 
2  O  ? 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 89.1  ? 
3  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_555 166.1 ? 
4  O  ? 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 96.7  ? 
5  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 94.9  ? 
6  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 98.9  ? 
7  O  ? A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 344 ? 1_555 98.9  ? 
8  O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 344 ? 1_555 87.0  ? 
9  OG ? A SER 72 ? A SER 72  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 344 ? 1_555 79.8  ? 
10 O  ? A ARG 73 ? A ARG 73  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 344 ? 1_555 164.4 ? 
11 O  ? A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 370 ? 1_555 170.1 ? 
12 O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 370 ? 1_555 99.4  ? 
13 OG ? A SER 72 ? A SER 72  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 370 ? 1_555 81.6  ? 
14 O  ? A ARG 73 ? A ARG 73  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 370 ? 1_555 88.1  ? 
15 O  ? N HOH .  ? A HOH 344 ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 370 ? 1_555 76.3  ? 
# 
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                   9FC9 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 -137.30 -32.35 
2 1 ARG A 68 ? A -142.96 25.82  
3 1 ARG A 68 ? B -140.10 26.06  
# 
_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     385 
_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                    9FC9 
_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]   0.012554 
_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]   0.012554 
_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]   0.026790 
_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   ? -3.17600  -10.12900 -8.60300  0.520 20.10000 ? 1   LYS A N    1 
ATOM   2    N  N    B LYS A 1 1   ? -3.12700  -10.07300 -8.68300  0.480 20.43000 ? 1   LYS A N    1 
ATOM   3    C  CA   A LYS A 1 1   ? -2.26700  -10.49200 -9.73300  0.520 20.57000 ? 1   LYS A CA   1 
ATOM   4    C  CA   B LYS A 1 1   ? -2.20800  -10.43300 -9.80900  0.480 20.22000 ? 1   LYS A CA   1 
ATOM   5    C  C    A LYS A 1 1   ? -2.39200  -11.97900 -9.98000  0.520 17.31000 ? 1   LYS A C    1 
ATOM   6    C  C    B LYS A 1 1   ? -2.23300  -11.93000 -9.98700  0.480 16.99000 ? 1   LYS A C    1 
ATOM   7    O  O    A LYS A 1 1   ? -2.57500  -12.76600 -9.04800  0.520 17.64000 ? 1   LYS A O    1 
ATOM   8    O  O    B LYS A 1 1   ? -2.14600  -12.66200 -8.98700  0.480 16.57000 ? 1   LYS A O    1 
ATOM   9    C  CB   A LYS A 1 1   ? -0.83500  -10.11700 -9.37200  0.520 22.90000 ? 1   LYS A CB   1 
ATOM   10   C  CB   B LYS A 1 1   ? -0.79400  -9.98500  -9.47600  0.480 22.89000 ? 1   LYS A CB   1 
ATOM   11   C  CG   A LYS A 1 1   ? 0.22400   -10.62400 -10.34100 0.520 24.44000 ? 1   LYS A CG   1 
ATOM   12   C  CG   B LYS A 1 1   ? 0.28900   -10.56300 -10.38300 0.480 24.48000 ? 1   LYS A CG   1 
ATOM   13   C  CD   A LYS A 1 1   ? 1.60500   -10.14000 -9.92800  0.520 28.52000 ? 1   LYS A CD   1 
ATOM   14   C  CD   B LYS A 1 1   ? 1.64600   -9.98200  -10.02100 0.480 28.88000 ? 1   LYS A CD   1 
ATOM   15   C  CE   A LYS A 1 1   ? 2.68500   -10.80500 -10.77300 0.520 27.52000 ? 1   LYS A CE   1 
ATOM   16   C  CE   B LYS A 1 1   ? 2.76900   -10.63700 -10.81500 0.480 27.67000 ? 1   LYS A CE   1 
ATOM   17   N  NZ   A LYS A 1 1   ? 3.83900   -9.90600  -11.05100 0.520 32.98000 ? 1   LYS A NZ   1 
ATOM   18   N  NZ   B LYS A 1 1   ? 2.69300   -10.32100 -12.26500 0.480 28.41000 ? 1   LYS A NZ   1 
ATOM   19   H  H1   A LYS A 1 1   ? -3.99000  -10.45100 -8.76300  0.520 24.14000 ? 1   LYS A H1   1 
ATOM   20   H  H1   B LYS A 1 1   ? -3.36400  -10.81100 -8.24600  0.480 24.54000 ? 1   LYS A H1   1 
ATOM   21   H  H2   A LYS A 1 1   ? -2.86200  -10.47600 -7.84700  0.520 24.14000 ? 1   LYS A H2   1 
ATOM   22   H  H2   B LYS A 1 1   ? -2.70900  -9.52000  -8.12500  0.480 24.54000 ? 1   LYS A H2   1 
ATOM   23   H  H3   A LYS A 1 1   ? -3.21600  -9.24300  -8.52800  0.520 24.14000 ? 1   LYS A H3   1 
ATOM   24   H  H3   B LYS A 1 1   ? -3.85300  -9.67500  -9.00900  0.480 24.54000 ? 1   LYS A H3   1 
ATOM   25   H  HA   A LYS A 1 1   ? -2.49400  -10.01500 -10.54600 0.520 24.70000 ? 1   LYS A HA   1 
ATOM   26   H  HA   B LYS A 1 1   ? -2.47900  -9.99900  -10.63300 0.480 24.29000 ? 1   LYS A HA   1 
ATOM   27   H  HB2  A LYS A 1 1   ? -0.76700  -9.15000  -9.34700  0.520 27.51000 ? 1   LYS A HB2  1 
ATOM   28   H  HB2  B LYS A 1 1   ? -0.75200  -9.01900  -9.55000  0.480 27.49000 ? 1   LYS A HB2  1 
ATOM   29   H  HB3  A LYS A 1 1   ? -0.63100  -10.48700 -8.49800  0.520 27.51000 ? 1   LYS A HB3  1 
ATOM   30   H  HB3  B LYS A 1 1   ? -0.59000  -10.25700 -8.56800  0.480 27.49000 ? 1   LYS A HB3  1 
ATOM   31   H  HG2  A LYS A 1 1   ? 0.22500   -11.59400 -10.34200 0.520 29.36000 ? 1   LYS A HG2  1 
ATOM   32   H  HG2  B LYS A 1 1   ? 0.32500   -11.52600 -10.27400 0.480 29.41000 ? 1   LYS A HG2  1 
ATOM   33   H  HG3  A LYS A 1 1   ? 0.03500   -10.29200 -11.23200 0.520 29.36000 ? 1   LYS A HG3  1 
ATOM   34   H  HG3  B LYS A 1 1   ? 0.09400   -10.34100 -11.30700 0.480 29.41000 ? 1   LYS A HG3  1 
ATOM   35   H  HD2  A LYS A 1 1   ? 1.66300   -9.18000  -10.05400 0.520 34.25000 ? 1   LYS A HD2  1 
ATOM   36   H  HD2  B LYS A 1 1   ? 1.65000   -9.03200  -10.21500 0.480 34.68000 ? 1   LYS A HD2  1 
ATOM   37   H  HD3  A LYS A 1 1   ? 1.76100   -10.36300 -8.99700  0.520 34.25000 ? 1   LYS A HD3  1 
ATOM   38   H  HD3  B LYS A 1 1   ? 1.81600   -10.12800 -9.07700  0.480 34.68000 ? 1   LYS A HD3  1 
ATOM   39   H  HE2  A LYS A 1 1   ? 3.02000   -11.58400 -10.30200 0.520 33.05000 ? 1   LYS A HE2  1 
ATOM   40   H  HE2  B LYS A 1 1   ? 3.62200   -10.31900 -10.48100 0.480 33.23000 ? 1   LYS A HE2  1 
ATOM   41   H  HE3  A LYS A 1 1   ? 2.30200   -11.07100 -11.62400 0.520 33.05000 ? 1   LYS A HE3  1 
ATOM   42   H  HE3  B LYS A 1 1   ? 2.71100   -11.60000 -10.71300 0.480 33.23000 ? 1   LYS A HE3  1 
ATOM   43   H  HZ1  A LYS A 1 1   ? 4.51900   -10.37700 -11.37900 0.520 39.59000 ? 1   LYS A HZ1  1 
ATOM   44   H  HZ1  B LYS A 1 1   ? 2.67500   -9.43900  -12.38400 0.480 34.12000 ? 1   LYS A HZ1  1 
ATOM   45   H  HZ2  A LYS A 1 1   ? 3.60500   -9.28500  -11.64400 0.520 39.59000 ? 1   LYS A HZ2  1 
ATOM   46   H  HZ2  B LYS A 1 1   ? 3.40200   -10.65500 -12.68700 0.480 34.12000 ? 1   LYS A HZ2  1 
ATOM   47   H  HZ3  A LYS A 1 1   ? 4.10000   -9.50500  -10.30100 0.520 39.59000 ? 1   LYS A HZ3  1 
ATOM   48   H  HZ3  B LYS A 1 1   ? 1.95500   -10.67500 -12.61500 0.480 34.12000 ? 1   LYS A HZ3  1 
ATOM   49   N  N    . VAL A 1 2   ? -2.33300  -12.37600 -11.24200 1.000 18.36000 ? 2   VAL A N    1 
ATOM   50   C  CA   . VAL A 1 2   ? -2.23500  -13.78100 -11.61600 1.000 19.98000 ? 2   VAL A CA   1 
ATOM   51   C  C    . VAL A 1 2   ? -0.80700  -13.99100 -12.10700 1.000 22.53000 ? 2   VAL A C    1 
ATOM   52   O  O    . VAL A 1 2   ? -0.38400  -13.40200 -13.11400 1.000 22.59000 ? 2   VAL A O    1 
ATOM   53   C  CB   . VAL A 1 2   ? -3.29200  -14.18000 -12.64700 1.000 20.50000 ? 2   VAL A CB   1 
ATOM   54   C  CG1  . VAL A 1 2   ? -3.15700  -15.63900 -13.02000 1.000 28.06000 ? 2   VAL A CG1  1 
ATOM   55   C  CG2  . VAL A 1 2   ? -4.70400  -13.90100 -12.09400 1.000 20.81000 ? 2   VAL A CG2  1 
ATOM   56   H  H    . VAL A 1 2   ? -2.34900  -11.84200 -11.91500 1.000 22.06000 ? 2   VAL A H    1 
ATOM   57   H  HA   . VAL A 1 2   ? -2.37800  -14.35100 -10.84400 1.000 24.01000 ? 2   VAL A HA   1 
ATOM   58   H  HB   . VAL A 1 2   ? -3.15900  -13.65100 -13.45000 1.000 24.62000 ? 2   VAL A HB   1 
ATOM   59   H  HG11 . VAL A 1 2   ? -3.87100  -15.87600 -13.63300 1.000 33.69000 ? 2   VAL A HG11 1 
ATOM   60   H  HG12 . VAL A 1 2   ? -2.29600  -15.77800 -13.44600 1.000 33.69000 ? 2   VAL A HG12 1 
ATOM   61   H  HG13 . VAL A 1 2   ? -3.21900  -16.17700 -12.21600 1.000 33.69000 ? 2   VAL A HG13 1 
ATOM   62   H  HG21 . VAL A 1 2   ? -5.36000  -14.15200 -12.76300 1.000 24.99000 ? 2   VAL A HG21 1 
ATOM   63   H  HG22 . VAL A 1 2   ? -4.83600  -14.42400 -11.28800 1.000 24.99000 ? 2   VAL A HG22 1 
ATOM   64   H  HG23 . VAL A 1 2   ? -4.78300  -12.95600 -11.89200 1.000 24.99000 ? 2   VAL A HG23 1 
ATOM   65   N  N    . PHE A 1 3   ? -0.04500  -14.79300 -11.37300 1.000 17.55000 ? 3   PHE A N    1 
ATOM   66   C  CA   . PHE A 1 3   ? 1.32900   -15.09400 -11.73200 1.000 17.13000 ? 3   PHE A CA   1 
ATOM   67   C  C    . PHE A 1 3   ? 1.39500   -16.14200 -12.83000 1.000 19.40000 ? 3   PHE A C    1 
ATOM   68   O  O    . PHE A 1 3   ? 0.56500   -17.04500 -12.92000 1.000 19.22000 ? 3   PHE A O    1 
ATOM   69   C  CB   . PHE A 1 3   ? 2.07700   -15.66500 -10.52900 1.000 17.42000 ? 3   PHE A CB   1 
ATOM   70   C  CG   . PHE A 1 3   ? 2.59900   -14.64200 -9.57800  1.000 16.17000 ? 3   PHE A CG   1 
ATOM   71   C  CD1  . PHE A 1 3   ? 1.76600   -14.04900 -8.60600  1.000 18.74000 ? 3   PHE A CD1  1 
ATOM   72   C  CD2  . PHE A 1 3   ? 3.91900   -14.25600 -9.62500  1.000 19.95000 ? 3   PHE A CD2  1 
ATOM   73   C  CE1  . PHE A 1 3   ? 2.27600   -13.10500 -7.73100  1.000 21.63000 ? 3   PHE A CE1  1 
ATOM   74   C  CE2  . PHE A 1 3   ? 4.42500   -13.32700 -8.76300  1.000 22.39000 ? 3   PHE A CE2  1 
ATOM   75   C  CZ   . PHE A 1 3   ? 3.61200   -12.74000 -7.80700  1.000 23.64000 ? 3   PHE A CZ   1 
ATOM   76   H  H    . PHE A 1 3   ? -0.30700  -15.18000 -10.65100 1.000 21.09000 ? 3   PHE A H    1 
ATOM   77   H  HA   . PHE A 1 3   ? 1.74900   -14.27500 -12.03700 1.000 20.58000 ? 3   PHE A HA   1 
ATOM   78   H  HB2  . PHE A 1 3   ? 1.47300   -16.24100 -10.03500 1.000 20.93000 ? 3   PHE A HB2  1 
ATOM   79   H  HB3  . PHE A 1 3   ? 2.83500   -16.17700 -10.85100 1.000 20.93000 ? 3   PHE A HB3  1 
ATOM   80   H  HD1  . PHE A 1 3   ? 0.87000   -14.29300 -8.55200  1.000 22.51000 ? 3   PHE A HD1  1 
ATOM   81   H  HD2  . PHE A 1 3   ? 4.48000   -14.63700 -10.26000 1.000 23.96000 ? 3   PHE A HD2  1 
ATOM   82   H  HE1  . PHE A 1 3   ? 1.72300   -12.71600 -7.09300  1.000 25.98000 ? 3   PHE A HE1  1 
ATOM   83   H  HE2  . PHE A 1 3   ? 5.32200   -13.08600 -8.81700  1.000 26.89000 ? 3   PHE A HE2  1 
ATOM   84   H  HZ   . PHE A 1 3   ? 3.95900   -12.10700 -7.22100  1.000 28.39000 ? 3   PHE A HZ   1 
ATOM   85   N  N    . GLY A 1 4   ? 2.44400   -16.03100 -13.65300 1.000 20.85000 ? 4   GLY A N    1 
ATOM   86   C  CA   . GLY A 1 4   ? 2.88800   -17.17500 -14.40800 1.000 20.95000 ? 4   GLY A CA   1 
ATOM   87   C  C    . GLY A 1 4   ? 3.61300   -18.18200 -13.53100 1.000 18.43000 ? 4   GLY A C    1 
ATOM   88   O  O    . GLY A 1 4   ? 4.15200   -17.88300 -12.46400 1.000 19.38000 ? 4   GLY A O    1 
ATOM   89   H  H    . GLY A 1 4   ? 2.90000   -15.31300 -13.78000 1.000 25.04000 ? 4   GLY A H    1 
ATOM   90   H  HA2  . GLY A 1 4   ? 2.12300   -17.61200 -14.81300 1.000 25.16000 ? 4   GLY A HA2  1 
ATOM   91   H  HA3  . GLY A 1 4   ? 3.49300   -16.88400 -15.10900 1.000 25.16000 ? 4   GLY A HA3  1 
ATOM   92   N  N    . ARG A 1 5   ? 3.64200   -19.41500 -14.01800 1.000 22.61000 ? 5   ARG A N    1 
ATOM   93   C  CA   . ARG A 1 5   ? 4.26900   -20.50000 -13.27300 1.000 20.82000 ? 5   ARG A CA   1 
ATOM   94   C  C    . ARG A 1 5   ? 5.73000   -20.18600 -12.93400 1.000 19.67000 ? 5   ARG A C    1 
ATOM   95   O  O    . ARG A 1 5   ? 6.15700   -20.25600 -11.76900 1.000 19.06000 ? 5   ARG A O    1 
ATOM   96   C  CB   . ARG A 1 5   ? 4.13100   -21.76800 -14.12800 1.000 24.47000 ? 5   ARG A CB   1 
ATOM   97   C  CG   . ARG A 1 5   ? 4.80500   -23.00600 -13.59000 1.000 25.63000 ? 5   ARG A CG   1 
ATOM   98   C  CD   . ARG A 1 5   ? 4.54700   -24.21700 -14.53700 1.000 23.75000 ? 5   ARG A CD   1 
ATOM   99   N  NE   . ARG A 1 5   ? 5.23000   -24.14000 -15.83100 1.000 28.97000 ? 5   ARG A NE   1 
ATOM   100  C  CZ   . ARG A 1 5   ? 6.46300   -24.57500 -16.07200 1.000 29.99000 ? 5   ARG A CZ   1 
ATOM   101  N  NH1  . ARG A 1 5   ? 7.22100   -25.08700 -15.11700 1.000 26.85000 ? 5   ARG A NH1  1 
ATOM   102  N  NH2  . ARG A 1 5   ? 6.95300   -24.49000 -17.30800 1.000 30.21000 ? 5   ARG A NH2  1 
ATOM   103  H  H    . ARG A 1 5   ? 3.30900   -19.65200 -14.77400 1.000 27.16000 ? 5   ARG A H    1 
ATOM   104  H  HA   . ARG A 1 5   ? 3.82700   -20.63600 -12.42100 1.000 25.01000 ? 5   ARG A HA   1 
ATOM   105  H  HB2  . ARG A 1 5   ? 3.18700   -21.97200 -14.21700 1.000 29.39000 ? 5   ARG A HB2  1 
ATOM   106  H  HB3  . ARG A 1 5   ? 4.51600   -21.58800 -15.00000 1.000 29.39000 ? 5   ARG A HB3  1 
ATOM   107  H  HG2  . ARG A 1 5   ? 5.76200   -22.85700 -13.53200 1.000 30.78000 ? 5   ARG A HG2  1 
ATOM   108  H  HG3  . ARG A 1 5   ? 4.44900   -23.21700 -12.71300 1.000 30.78000 ? 5   ARG A HG3  1 
ATOM   109  H  HD2  . ARG A 1 5   ? 4.85100   -25.02500 -14.09500 1.000 28.53000 ? 5   ARG A HD2  1 
ATOM   110  H  HD3  . ARG A 1 5   ? 3.59500   -24.27400 -14.71400 1.000 28.53000 ? 5   ARG A HD3  1 
ATOM   111  H  HE   . ARG A 1 5   ? 4.80000   -23.78500 -16.48500 1.000 34.78000 ? 5   ARG A HE   1 
ATOM   112  H  HH11 . ARG A 1 5   ? 6.91900   -25.14500 -14.31400 1.000 32.25000 ? 5   ARG A HH11 1 
ATOM   113  H  HH12 . ARG A 1 5   ? 8.01500   -25.36100 -15.29900 1.000 32.25000 ? 5   ARG A HH12 1 
ATOM   114  H  HH21 . ARG A 1 5   ? 6.47200   -24.15600 -17.93900 1.000 36.27000 ? 5   ARG A HH21 1 
ATOM   115  H  HH22 . ARG A 1 5   ? 7.74900   -24.76800 -17.47500 1.000 36.27000 ? 5   ARG A HH22 1 
ATOM   116  N  N    . CYS A 1 6   ? 6.54200   -19.86000 -13.95000 1.000 19.72000 ? 6   CYS A N    1 
ATOM   117  C  CA   . CYS A 1 6   ? 7.94500   -19.61600 -13.65800 1.000 22.01000 ? 6   CYS A CA   1 
ATOM   118  C  C    . CYS A 1 6   ? 8.16100   -18.28600 -12.95300 1.000 18.19000 ? 6   CYS A C    1 
ATOM   119  O  O    . CYS A 1 6   ? 9.11500   -18.14900 -12.18600 1.000 20.03000 ? 6   CYS A O    1 
ATOM   120  C  CB   . CYS A 1 6   ? 8.78000   -19.66100 -14.94600 1.000 22.30000 ? 6   CYS A CB   1 
ATOM   121  S  SG   . CYS A 1 6   ? 8.86000   -21.30100 -15.71200 1.000 23.08000 ? 6   CYS A SG   1 
ATOM   122  H  H    . CYS A 1 6   ? 6.31000   -19.77900 -14.77400 1.000 23.69000 ? 6   CYS A H    1 
ATOM   123  H  HA   . CYS A 1 6   ? 8.25300   -20.32400 -13.07000 1.000 26.43000 ? 6   CYS A HA   1 
ATOM   124  H  HB2  . CYS A 1 6   ? 8.38800   -19.05200 -15.59200 1.000 26.78000 ? 6   CYS A HB2  1 
ATOM   125  H  HB3  . CYS A 1 6   ? 9.68700   -19.38800 -14.73900 1.000 26.78000 ? 6   CYS A HB3  1 
ATOM   126  N  N    . GLU A 1 7   ? 7.30600   -17.29400 -13.21100 1.000 19.93000 ? 7   GLU A N    1 
ATOM   127  C  CA   . GLU A 1 7   ? 7.39200   -16.03400 -12.47800 1.000 18.72000 ? 7   GLU A CA   1 
ATOM   128  C  C    . GLU A 1 7   ? 7.18800   -16.25300 -10.98300 1.000 17.66000 ? 7   GLU A C    1 
ATOM   129  O  O    . GLU A 1 7   ? 7.91600   -15.70400 -10.15800 1.000 20.17000 ? 7   GLU A O    1 
ATOM   130  C  CB   . GLU A 1 7   ? 6.34900   -15.06900 -13.02300 1.000 22.39000 ? 7   GLU A CB   1 
ATOM   131  C  CG   . GLU A 1 7   ? 6.35100   -13.69600 -12.41900 1.000 25.91000 ? 7   GLU A CG   1 
ATOM   132  C  CD   . GLU A 1 7   ? 5.11200   -12.89000 -12.80600 1.000 26.14000 ? 7   GLU A CD   1 
ATOM   133  O  OE1  . GLU A 1 7   ? 4.11100   -13.46300 -13.31400 1.000 26.17000 ? 7   GLU A OE1  1 
ATOM   134  O  OE2  . GLU A 1 7   ? 5.15900   -11.65200 -12.61000 1.000 30.64000 ? 7   GLU A OE2  1 
ATOM   135  H  H    . GLU A 1 7   ? 6.67700   -17.32500 -13.79700 1.000 23.94000 ? 7   GLU A H    1 
ATOM   136  H  HA   . GLU A 1 7   ? 8.27200   -15.64600 -12.60400 1.000 22.49000 ? 7   GLU A HA   1 
ATOM   137  H  HB2  . GLU A 1 7   ? 6.49900   -14.96500 -13.97500 1.000 26.90000 ? 7   GLU A HB2  1 
ATOM   138  H  HB3  . GLU A 1 7   ? 5.47100   -15.45100 -12.86500 1.000 26.90000 ? 7   GLU A HB3  1 
ATOM   139  H  HG2  . GLU A 1 7   ? 6.37100   -13.77300 -11.45300 1.000 31.12000 ? 7   GLU A HG2  1 
ATOM   140  H  HG3  . GLU A 1 7   ? 7.13400   -13.21400 -12.73000 1.000 31.12000 ? 7   GLU A HG3  1 
ATOM   141  N  N    . LEU A 1 8   ? 6.23000   -17.10400 -10.63000 1.000 18.81000 ? 8   LEU A N    1 
ATOM   142  C  CA   . LEU A 1 8   ? 5.97500   -17.38300 -9.22300  1.000 17.82000 ? 8   LEU A CA   1 
ATOM   143  C  C    . LEU A 1 8   ? 7.11300   -18.17800 -8.61400  1.000 17.53000 ? 8   LEU A C    1 
ATOM   144  O  O    . LEU A 1 8   ? 7.54000   -17.90300 -7.48600  1.000 17.46000 ? 8   LEU A O    1 
ATOM   145  C  CB   . LEU A 1 8   ? 4.65700   -18.12900 -9.08200  1.000 18.45000 ? 8   LEU A CB   1 
ATOM   146  C  CG   . LEU A 1 8   ? 4.31000   -18.43000 -7.62100  1.000 18.23000 ? 8   LEU A CG   1 
ATOM   147  C  CD1  . LEU A 1 8   ? 4.08400   -17.16400 -6.84700  1.000 21.02000 ? 8   LEU A CD1  1 
ATOM   148  C  CD2  . LEU A 1 8   ? 3.07900   -19.31200 -7.55900  1.000 22.82000 ? 8   LEU A CD2  1 
ATOM   149  H  H    . LEU A 1 8   ? 5.72000   -17.52700 -11.17800 1.000 22.60000 ? 8   LEU A H    1 
ATOM   150  H  HA   . LEU A 1 8   ? 5.90200   -16.54700 -8.73700  1.000 21.41000 ? 8   LEU A HA   1 
ATOM   151  H  HB2  . LEU A 1 8   ? 3.94500   -17.58700 -9.45700  1.000 22.16000 ? 8   LEU A HB2  1 
ATOM   152  H  HB3  . LEU A 1 8   ? 4.71800   -18.97200 -9.55800  1.000 22.16000 ? 8   LEU A HB3  1 
ATOM   153  H  HG   . LEU A 1 8   ? 5.05400   -18.89600 -7.20800  1.000 21.90000 ? 8   LEU A HG   1 
ATOM   154  H  HD11 . LEU A 1 8   ? 3.75000   -17.38800 -5.96500  1.000 25.25000 ? 8   LEU A HD11 1 
ATOM   155  H  HD12 . LEU A 1 8   ? 4.92500   -16.68600 -6.77000  1.000 25.25000 ? 8   LEU A HD12 1 
ATOM   156  H  HD13 . LEU A 1 8   ? 3.43500   -16.61700 -7.31800  1.000 25.25000 ? 8   LEU A HD13 1 
ATOM   157  H  HD21 . LEU A 1 8   ? 2.81300   -19.41900 -6.63200  1.000 27.41000 ? 8   LEU A HD21 1 
ATOM   158  H  HD22 . LEU A 1 8   ? 2.36400   -18.89200 -8.06200  1.000 27.41000 ? 8   LEU A HD22 1 
ATOM   159  H  HD23 . LEU A 1 8   ? 3.29100   -20.17700 -7.94400  1.000 27.41000 ? 8   LEU A HD23 1 
ATOM   160  N  N    . ALA A 1 9   ? 7.64100   -19.15500 -9.35100  1.000 16.96000 ? 9   ALA A N    1 
ATOM   161  C  CA   . ALA A 1 9   ? 8.76500   -19.90700 -8.83300  1.000 16.84000 ? 9   ALA A CA   1 
ATOM   162  C  C    . ALA A 1 9   ? 9.94400   -18.99300 -8.51400  1.000 16.38000 ? 9   ALA A C    1 
ATOM   163  O  O    . ALA A 1 9   ? 10.56900  -19.14000 -7.46800  1.000 18.44000 ? 9   ALA A O    1 
ATOM   164  C  CB   . ALA A 1 9   ? 9.16100   -20.98600 -9.83900  1.000 20.75000 ? 9   ALA A CB   1 
ATOM   165  H  H    . ALA A 1 9   ? 7.37100   -19.39200 -10.13300 1.000 20.37000 ? 9   ALA A H    1 
ATOM   166  H  HA   . ALA A 1 9   ? 8.50600   -20.34500 -8.00700  1.000 20.23000 ? 9   ALA A HA   1 
ATOM   167  H  HB1  . ALA A 1 9   ? 9.87000   -21.52800 -9.45800  1.000 24.92000 ? 9   ALA A HB1  1 
ATOM   168  H  HB2  . ALA A 1 9   ? 8.38800   -21.54000 -10.02900 1.000 24.92000 ? 9   ALA A HB2  1 
ATOM   169  H  HB3  . ALA A 1 9   ? 9.47200   -20.56100 -10.65300 1.000 24.92000 ? 9   ALA A HB3  1 
ATOM   170  N  N    . ALA A 1 10  ? 10.25700  -18.05000 -9.40700  1.000 18.56000 ? 10  ALA A N    1 
ATOM   171  C  CA   . ALA A 1 10  ? 11.35700  -17.12400 -9.15800  1.000 19.97000 ? 10  ALA A CA   1 
ATOM   172  C  C    . ALA A 1 10  ? 11.09900  -16.25600 -7.94200  1.000 17.27000 ? 10  ALA A C    1 
ATOM   173  O  O    . ALA A 1 10  ? 12.00200  -16.03800 -7.12300  1.000 21.08000 ? 10  ALA A O    1 
ATOM   174  C  CB   . ALA A 1 10  ? 11.56600  -16.25600 -10.39600 1.000 21.92000 ? 10  ALA A CB   1 
ATOM   175  H  H    . ALA A 1 10  ? 9.85100   -17.92800 -10.15500 1.000 22.30000 ? 10  ALA A H    1 
ATOM   176  H  HA   . ALA A 1 10  ? 12.16500  -17.63100 -8.98500  1.000 23.98000 ? 10  ALA A HA   1 
ATOM   177  H  HB1  . ALA A 1 10  ? 12.27700  -15.62100 -10.22100 1.000 26.32000 ? 10  ALA A HB1  1 
ATOM   178  H  HB2  . ALA A 1 10  ? 11.80700  -16.82600 -11.14300 1.000 26.32000 ? 10  ALA A HB2  1 
ATOM   179  H  HB3  . ALA A 1 10  ? 10.74200  -15.78400 -10.59300 1.000 26.32000 ? 10  ALA A HB3  1 
ATOM   180  N  N    . ALA A 1 11  ? 9.87900   -15.73700 -7.80900  1.000 20.31000 ? 11  ALA A N    1 
ATOM   181  C  CA   . ALA A 1 11  ? 9.54500   -14.92400 -6.64900  1.000 22.02000 ? 11  ALA A CA   1 
ATOM   182  C  C    . ALA A 1 11  ? 9.68300   -15.72200 -5.35600  1.000 19.16000 ? 11  ALA A C    1 
ATOM   183  O  O    . ALA A 1 11  ? 10.21700  -15.23400 -4.35800  1.000 20.00000 ? 11  ALA A O    1 
ATOM   184  C  CB   . ALA A 1 11  ? 8.12500   -14.37500 -6.79200  1.000 21.14000 ? 11  ALA A CB   1 
ATOM   185  H  H    . ALA A 1 11  ? 9.23500   -15.84100 -8.37100  1.000 24.40000 ? 11  ALA A H    1 
ATOM   186  H  HA   . ALA A 1 11  ? 10.15800  -14.17400 -6.60400  1.000 26.45000 ? 11  ALA A HA   1 
ATOM   187  H  HB1  . ALA A 1 11  ? 7.90400   -13.86100 -6.00000  1.000 25.40000 ? 11  ALA A HB1  1 
ATOM   188  H  HB2  . ALA A 1 11  ? 8.08300   -13.80700 -7.57700  1.000 25.40000 ? 11  ALA A HB2  1 
ATOM   189  H  HB3  . ALA A 1 11  ? 7.50700   -15.11700 -6.88800  1.000 25.40000 ? 11  ALA A HB3  1 
ATOM   190  N  N    . MET A 1 12  ? 9.18100   -16.95500 -5.34500  1.000 18.50000 ? 12  MET A N    1 
ATOM   191  C  CA   . MET A 1 12  ? 9.29200   -17.82000 -4.17600  1.000 17.87000 ? 12  MET A CA   1 
ATOM   192  C  C    . MET A 1 12  ? 10.74100  -18.13600 -3.84400  1.000 16.94000 ? 12  MET A C    1 
ATOM   193  O  O    . MET A 1 12  ? 11.13000  -18.14400 -2.66300  1.000 20.51000 ? 12  MET A O    1 
ATOM   194  C  CB   . MET A 1 12  ? 8.48600   -19.05400 -4.57400  1.000 18.39000 ? 12  MET A CB   1 
ATOM   195  C  CG   . MET A 1 12  ? 6.99000   -18.81600 -4.52900  1.000 18.41000 ? 12  MET A CG   1 
ATOM   196  S  SD   . MET A 1 12  ? 6.10200   -20.36700 -4.55500  1.000 19.70000 ? 12  MET A SD   1 
ATOM   197  C  CE   . MET A 1 12  ? 4.52000   -19.91400 -3.83700  1.000 21.39000 ? 12  MET A CE   1 
ATOM   198  H  H    . MET A 1 12  ? 8.76800   -17.31700 -6.00700  1.000 22.22000 ? 12  MET A H    1 
ATOM   199  H  HA   . MET A 1 12  ? 8.93800   -17.42300 -3.36500  1.000 21.47000 ? 12  MET A HA   1 
ATOM   200  H  HB2  . MET A 1 12  ? 8.72300   -19.30700 -5.48000  1.000 22.10000 ? 12  MET A HB2  1 
ATOM   201  H  HB3  . MET A 1 12  ? 8.69400   -19.77800 -3.96200  1.000 22.10000 ? 12  MET A HB3  1 
ATOM   202  H  HG2  . MET A 1 12  ? 6.76100   -18.34400 -3.71400  1.000 22.12000 ? 12  MET A HG2  1 
ATOM   203  H  HG3  . MET A 1 12  ? 6.72200   -18.29400 -5.30200  1.000 22.12000 ? 12  MET A HG3  1 
ATOM   204  H  HE1  . MET A 1 12  ? 3.95700   -20.70200 -3.79000  1.000 25.69000 ? 12  MET A HE1  1 
ATOM   205  H  HE2  . MET A 1 12  ? 4.66800   -19.55900 -2.94600  1.000 25.69000 ? 12  MET A HE2  1 
ATOM   206  H  HE3  . MET A 1 12  ? 4.10100   -19.24100 -4.39600  1.000 25.69000 ? 12  MET A HE3  1 
ATOM   207  N  N    A LYS A 1 13  ? 11.58700  -18.35100 -4.85500  0.490 20.14000 ? 13  LYS A N    1 
ATOM   208  N  N    B LYS A 1 13  ? 11.55900  -18.36200 -4.88700  0.510 20.06000 ? 13  LYS A N    1 
ATOM   209  C  CA   A LYS A 1 13  ? 13.00600  -18.54400 -4.55400  0.490 21.95000 ? 13  LYS A CA   1 
ATOM   210  C  CA   B LYS A 1 13  ? 12.98500  -18.63800 -4.71800  0.510 21.98000 ? 13  LYS A CA   1 
ATOM   211  C  C    A LYS A 1 13  ? 13.63400  -17.27300 -3.99000  0.490 20.51000 ? 13  LYS A C    1 
ATOM   212  C  C    B LYS A 1 13  ? 13.71400  -17.46200 -4.08300  0.510 20.60000 ? 13  LYS A C    1 
ATOM   213  O  O    A LYS A 1 13  ? 14.38400  -17.32300 -3.01000  0.490 21.40000 ? 13  LYS A O    1 
ATOM   214  O  O    B LYS A 1 13  ? 14.54400  -17.65100 -3.18700  0.510 22.80000 ? 13  LYS A O    1 
ATOM   215  C  CB   A LYS A 1 13  ? 13.76000  -18.99000 -5.79900  0.490 23.35000 ? 13  LYS A CB   1 
ATOM   216  C  CB   B LYS A 1 13  ? 13.59700  -18.95300 -6.08500  0.510 22.69000 ? 13  LYS A CB   1 
ATOM   217  C  CG   A LYS A 1 13  ? 15.22300  -19.34700 -5.51500  0.490 20.86000 ? 13  LYS A CG   1 
ATOM   218  C  CG   B LYS A 1 13  ? 15.11900  -19.16500 -6.08300  0.510 33.69000 ? 13  LYS A CG   1 
ATOM   219  C  CD   A LYS A 1 13  ? 15.84100  -20.09500 -6.68600  0.490 31.30000 ? 13  LYS A CD   1 
ATOM   220  C  CD   B LYS A 1 13  ? 15.50100  -20.54300 -6.61000  0.510 33.14000 ? 13  LYS A CD   1 
ATOM   221  C  CE   A LYS A 1 13  ? 17.25900  -20.56000 -6.35200  0.490 45.51000 ? 13  LYS A CE   1 
ATOM   222  C  CE   B LYS A 1 13  ? 17.01900  -20.75600 -6.62100  0.510 47.03000 ? 13  LYS A CE   1 
ATOM   223  N  NZ   A LYS A 1 13  ? 17.30500  -21.44200 -5.15000  0.490 43.53000 ? 13  LYS A NZ   1 
ATOM   224  N  NZ   B LYS A 1 13  ? 17.66200  -20.36400 -7.91300  0.510 35.35000 ? 13  LYS A NZ   1 
ATOM   225  H  H    A LYS A 1 13  ? 11.37400  -18.38700 -5.68700  0.490 24.19000 ? 13  LYS A H    1 
ATOM   226  H  H    B LYS A 1 13  ? 11.30600  -18.35900 -5.70800  0.510 24.09000 ? 13  LYS A H    1 
ATOM   227  H  HA   A LYS A 1 13  ? 13.08200  -19.24600 -3.88800  0.490 26.37000 ? 13  LYS A HA   1 
ATOM   228  H  HA   B LYS A 1 13  ? 13.09200  -19.40500 -4.13400  0.510 26.40000 ? 13  LYS A HA   1 
ATOM   229  H  HB2  A LYS A 1 13  ? 13.32500  -19.77600 -6.16600  0.490 28.05000 ? 13  LYS A HB2  1 
ATOM   230  H  HB2  B LYS A 1 13  ? 13.19100  -19.76600 -6.42300  0.510 27.25000 ? 13  LYS A HB2  1 
ATOM   231  H  HB3  A LYS A 1 13  ? 13.74800  -18.27100 -6.44900  0.490 28.05000 ? 13  LYS A HB3  1 
ATOM   232  H  HB3  B LYS A 1 13  ? 13.40700  -18.21400 -6.68400  0.510 27.25000 ? 13  LYS A HB3  1 
ATOM   233  H  HG2  A LYS A 1 13  ? 15.73100  -18.53400 -5.36700  0.490 25.06000 ? 13  LYS A HG2  1 
ATOM   234  H  HG2  B LYS A 1 13  ? 15.53500  -18.49700 -6.65000  0.510 40.45000 ? 13  LYS A HG2  1 
ATOM   235  H  HG3  A LYS A 1 13  ? 15.27000  -19.91500 -4.72900  0.490 25.06000 ? 13  LYS A HG3  1 
ATOM   236  H  HG3  B LYS A 1 13  ? 15.45200  -19.08400 -5.17600  0.510 40.45000 ? 13  LYS A HG3  1 
ATOM   237  H  HD2  A LYS A 1 13  ? 15.30300  -20.87500 -6.89200  0.490 37.58000 ? 13  LYS A HD2  1 
ATOM   238  H  HD2  B LYS A 1 13  ? 15.10400  -21.22300 -6.04300  0.510 39.79000 ? 13  LYS A HD2  1 
ATOM   239  H  HD3  A LYS A 1 13  ? 15.88400  -19.50900 -7.45800  0.490 37.58000 ? 13  LYS A HD3  1 
ATOM   240  H  HD3  B LYS A 1 13  ? 15.17600  -20.63800 -7.51900  0.510 39.79000 ? 13  LYS A HD3  1 
ATOM   241  H  HE2  A LYS A 1 13  ? 17.61400  -21.05800 -7.10500  0.490 54.64000 ? 13  LYS A HE2  1 
ATOM   242  H  HE2  B LYS A 1 13  ? 17.41600  -20.22100 -5.91600  0.510 56.46000 ? 13  LYS A HE2  1 
ATOM   243  H  HE3  A LYS A 1 13  ? 17.81400  -19.78400 -6.17700  0.490 54.64000 ? 13  LYS A HE3  1 
ATOM   244  H  HE3  B LYS A 1 13  ? 17.20500  -21.69600 -6.46900  0.510 56.46000 ? 13  LYS A HE3  1 
ATOM   245  H  HZ1  A LYS A 1 13  ? 18.13600  -21.73300 -5.01800  0.490 52.26000 ? 13  LYS A HZ1  1 
ATOM   246  H  HZ1  B LYS A 1 13  ? 18.53700  -20.52300 -7.87800  0.510 42.45000 ? 13  LYS A HZ1  1 
ATOM   247  H  HZ2  A LYS A 1 13  ? 17.03900  -20.99100 -4.43100  0.490 52.26000 ? 13  LYS A HZ2  1 
ATOM   248  H  HZ2  B LYS A 1 13  ? 17.31100  -20.83400 -8.58300  0.510 42.45000 ? 13  LYS A HZ2  1 
ATOM   249  H  HZ3  A LYS A 1 13  ? 16.76900  -22.14300 -5.26600  0.490 52.26000 ? 13  LYS A HZ3  1 
ATOM   250  H  HZ3  B LYS A 1 13  ? 17.53100  -19.49800 -8.06800  0.510 42.45000 ? 13  LYS A HZ3  1 
ATOM   251  N  N    A ARG A 1 14  ? 13.32400  -16.12300 -4.58700  0.490 22.01000 ? 14  ARG A N    1 
ATOM   252  N  N    B ARG A 1 14  ? 13.42400  -16.24200 -4.53800  0.510 22.09000 ? 14  ARG A N    1 
ATOM   253  C  CA   A ARG A 1 14  ? 13.89100  -14.87100 -4.09400  0.490 23.97000 ? 14  ARG A CA   1 
ATOM   254  C  CA   B ARG A 1 14  ? 14.09000  -15.08100 -3.95600  0.510 22.23000 ? 14  ARG A CA   1 
ATOM   255  C  C    A ARG A 1 14  ? 13.56900  -14.66000 -2.62000  0.490 24.63000 ? 14  ARG A C    1 
ATOM   256  C  C    B ARG A 1 14  ? 13.69400  -14.88800 -2.50300  0.510 24.35000 ? 14  ARG A C    1 
ATOM   257  O  O    A ARG A 1 14  ? 14.33300  -14.00400 -1.90400  0.490 25.43000 ? 14  ARG A O    1 
ATOM   258  O  O    B ARG A 1 14  ? 14.52800  -14.48500 -1.68500  0.510 25.05000 ? 14  ARG A O    1 
ATOM   259  C  CB   A ARG A 1 14  ? 13.37500  -13.72000 -4.96300  0.490 24.98000 ? 14  ARG A CB   1 
ATOM   260  C  CB   B ARG A 1 14  ? 13.78400  -13.81300 -4.75500  0.510 26.67000 ? 14  ARG A CB   1 
ATOM   261  C  CG   A ARG A 1 14  ? 13.54300  -12.32900 -4.37700  0.490 35.06000 ? 14  ARG A CG   1 
ATOM   262  C  CG   B ARG A 1 14  ? 14.55200  -12.59300 -4.23600  0.510 36.92000 ? 14  ARG A CG   1 
ATOM   263  C  CD   A ARG A 1 14  ? 13.27400  -11.26300 -5.44400  0.490 33.08000 ? 14  ARG A CD   1 
ATOM   264  C  CD   B ARG A 1 14  ? 14.35800  -11.35200 -5.10300  0.510 30.44000 ? 14  ARG A CD   1 
ATOM   265  N  NE   A ARG A 1 14  ? 11.89500  -11.31700 -5.91700  0.490 39.30000 ? 14  ARG A NE   1 
ATOM   266  N  NE   B ARG A 1 14  ? 13.40100  -10.42300 -4.50900  0.510 40.53000 ? 14  ARG A NE   1 
ATOM   267  C  CZ   A ARG A 1 14  ? 10.87700  -10.67700 -5.35400  0.490 38.47000 ? 14  ARG A CZ   1 
ATOM   268  C  CZ   B ARG A 1 14  ? 13.68300  -9.56400  -3.53800  0.510 31.36000 ? 14  ARG A CZ   1 
ATOM   269  N  NH1  A ARG A 1 14  ? 11.05300  -9.86300  -4.32600  0.490 42.13000 ? 14  ARG A NH1  1 
ATOM   270  N  NH1  B ARG A 1 14  ? 14.90600  -9.45400  -3.04000  0.510 42.69000 ? 14  ARG A NH1  1 
ATOM   271  N  NH2  A ARG A 1 14  ? 9.65000   -10.86300 -5.83400  0.490 26.96000 ? 14  ARG A NH2  1 
ATOM   272  N  NH2  B ARG A 1 14  ? 12.71600  -8.78900  -3.05800  0.510 36.67000 ? 14  ARG A NH2  1 
ATOM   273  H  H    A ARG A 1 14  ? 12.80000  -16.04300 -5.26400  0.490 26.43000 ? 14  ARG A H    1 
ATOM   274  H  H    B ARG A 1 14  ? 12.86200  -16.06500 -5.16400  0.510 26.53000 ? 14  ARG A H    1 
ATOM   275  H  HA   A ARG A 1 14  ? 14.85800  -14.88500 -4.16800  0.490 28.79000 ? 14  ARG A HA   1 
ATOM   276  H  HA   B ARG A 1 14  ? 15.04800  -15.22800 -4.00000  0.510 26.70000 ? 14  ARG A HA   1 
ATOM   277  H  HB2  A ARG A 1 14  ? 13.85300  -13.73700 -5.80600  0.490 30.00000 ? 14  ARG A HB2  1 
ATOM   278  H  HB2  B ARG A 1 14  ? 14.03400  -13.95500 -5.68100  0.510 32.02000 ? 14  ARG A HB2  1 
ATOM   279  H  HB3  A ARG A 1 14  ? 12.42700  -13.85600 -5.11600  0.490 30.00000 ? 14  ARG A HB3  1 
ATOM   280  H  HB3  B ARG A 1 14  ? 12.83500  -13.62100 -4.69300  0.510 32.02000 ? 14  ARG A HB3  1 
ATOM   281  H  HG2  A ARG A 1 14  ? 12.91300  -12.20400 -3.65000  0.490 42.09000 ? 14  ARG A HG2  1 
ATOM   282  H  HG2  B ARG A 1 14  ? 14.24300  -12.38300 -3.34100  0.510 44.33000 ? 14  ARG A HG2  1 
ATOM   283  H  HG3  A ARG A 1 14  ? 14.45000  -12.22000 -4.05300  0.490 42.09000 ? 14  ARG A HG3  1 
ATOM   284  H  HG3  B ARG A 1 14  ? 15.50000  -12.80000 -4.22000  0.510 44.33000 ? 14  ARG A HG3  1 
ATOM   285  H  HD2  A ARG A 1 14  ? 13.43300  -10.38300 -5.06700  0.490 39.72000 ? 14  ARG A HD2  1 
ATOM   286  H  HD2  B ARG A 1 14  ? 15.20700  -10.89300 -5.20000  0.510 36.55000 ? 14  ARG A HD2  1 
ATOM   287  H  HD3  A ARG A 1 14  ? 13.86200  -11.41000 -6.20100  0.490 39.72000 ? 14  ARG A HD3  1 
ATOM   288  H  HD3  B ARG A 1 14  ? 14.02300  -11.61800 -5.97300  0.510 36.55000 ? 14  ARG A HD3  1 
ATOM   289  H  HE   A ARG A 1 14  ? 11.72900  -11.79800 -6.61000  0.490 47.19000 ? 14  ARG A HE   1 
ATOM   290  H  HE   B ARG A 1 14  ? 12.59500  -10.43400 -4.80900  0.510 48.66000 ? 14  ARG A HE   1 
ATOM   291  H  HH11 A ARG A 1 14  ? 11.84200  -9.73800  -4.00600  0.490 50.58000 ? 14  ARG A HH11 1 
ATOM   292  H  HH11 B ARG A 1 14  ? 15.54000  -9.94800  -3.34600  0.510 51.26000 ? 14  ARG A HH11 1 
ATOM   293  H  HH12 A ARG A 1 14  ? 10.37900  -9.45900  -3.97700  0.490 50.58000 ? 14  ARG A HH12 1 
ATOM   294  H  HH12 B ARG A 1 14  ? 15.06500  -8.89000  -2.41100  0.510 51.26000 ? 14  ARG A HH12 1 
ATOM   295  H  HH21 A ARG A 1 14  ? 9.52400   -11.39300 -6.50000  0.490 32.37000 ? 14  ARG A HH21 1 
ATOM   296  H  HH21 B ARG A 1 14  ? 11.91900  -8.84800  -3.37600  0.510 44.03000 ? 14  ARG A HH21 1 
ATOM   297  H  HH22 A ARG A 1 14  ? 8.98200   -10.45500 -5.47800  0.490 32.37000 ? 14  ARG A HH22 1 
ATOM   298  H  HH22 B ARG A 1 14  ? 12.88700  -8.22700  -2.42900  0.510 44.03000 ? 14  ARG A HH22 1 
ATOM   299  N  N    . HIS A 1 15  ? 12.43800  -15.19000 -2.15300  1.000 23.79000 ? 15  HIS A N    1 
ATOM   300  C  CA   . HIS A 1 15  ? 12.00200  -15.05800 -0.77200  1.000 22.29000 ? 15  HIS A CA   1 
ATOM   301  C  C    . HIS A 1 15  ? 12.38900  -16.24100 0.10700   1.000 24.65000 ? 15  HIS A C    1 
ATOM   302  O  O    . HIS A 1 15  ? 11.92700  -16.30500 1.25400   1.000 28.28000 ? 15  HIS A O    1 
ATOM   303  C  CB   . HIS A 1 15  ? 10.49300  -14.85200 -0.72100  1.000 26.36000 ? 15  HIS A CB   1 
ATOM   304  C  CG   . HIS A 1 15  ? 10.05800  -13.49300 -1.16700  1.000 25.84000 ? 15  HIS A CG   1 
ATOM   305  N  ND1  . HIS A 1 15  ? 10.07500  -12.39800 -0.32800  1.000 35.28000 ? 15  HIS A ND1  1 
ATOM   306  C  CD2  . HIS A 1 15  ? 9.61200   -13.04500 -2.36100  1.000 24.56000 ? 15  HIS A CD2  1 
ATOM   307  C  CE1  . HIS A 1 15  ? 9.64200   -11.33800 -0.98500  1.000 31.29000 ? 15  HIS A CE1  1 
ATOM   308  N  NE2  . HIS A 1 15  ? 9.35400   -11.70100 -2.22100  1.000 36.17000 ? 15  HIS A NE2  1 
ATOM   309  H  H    . HIS A 1 15  ? 11.83000  -15.47000 -2.69400  1.000 28.57000 ? 15  HIS A H    1 
ATOM   310  H  HA   . HIS A 1 15  ? 12.43100  -14.27300 -0.39700  1.000 26.77000 ? 15  HIS A HA   1 
ATOM   311  H  HB2  . HIS A 1 15  ? 10.06900  -15.50300 -1.30100  1.000 31.66000 ? 15  HIS A HB2  1 
ATOM   312  H  HB3  . HIS A 1 15  ? 10.19100  -14.97500 0.19200   1.000 31.66000 ? 15  HIS A HB3  1 
ATOM   313  H  HD1  . HIS A 1 15  ? 10.32800  -12.40500 0.49400   1.000 42.35000 ? 15  HIS A HD1  1 
ATOM   314  H  HD2  . HIS A 1 15  ? 9.50100   -13.55100 -3.13300  1.000 29.49000 ? 15  HIS A HD2  1 
ATOM   315  H  HE1  . HIS A 1 15  ? 9.55500   -10.48000 -0.63600  1.000 37.57000 ? 15  HIS A HE1  1 
ATOM   316  N  N    . GLY A 1 16  ? 13.19000  -17.17100 -0.40300  1.000 21.98000 ? 16  GLY A N    1 
ATOM   317  C  CA   . GLY A 1 16  ? 13.78400  -18.21300 0.41000   1.000 24.26000 ? 16  GLY A CA   1 
ATOM   318  C  C    . GLY A 1 16  ? 12.94700  -19.45100 0.63300   1.000 26.27000 ? 16  GLY A C    1 
ATOM   319  O  O    . GLY A 1 16  ? 13.21700  -20.19800 1.58100   1.000 25.98000 ? 16  GLY A O    1 
ATOM   320  H  H    . GLY A 1 16  ? 13.40700  -17.21700 -1.23400  1.000 26.40000 ? 16  GLY A H    1 
ATOM   321  H  HA2  . GLY A 1 16  ? 14.61000  -18.49500 -0.01200  1.000 29.14000 ? 16  GLY A HA2  1 
ATOM   322  H  HA3  . GLY A 1 16  ? 13.98600  -17.84000 1.28300   1.000 29.14000 ? 16  GLY A HA3  1 
ATOM   323  N  N    . LEU A 1 17  ? 11.96300  -19.72300 -0.22100  1.000 23.91000 ? 17  LEU A N    1 
ATOM   324  C  CA   . LEU A 1 17  ? 11.14200  -20.91400 -0.03200  1.000 21.20000 ? 17  LEU A CA   1 
ATOM   325  C  C    . LEU A 1 17  ? 11.75400  -22.17600 -0.60600  1.000 24.80000 ? 17  LEU A C    1 
ATOM   326  O  O    . LEU A 1 17  ? 11.34000  -23.27600 -0.22300  1.000 26.15000 ? 17  LEU A O    1 
ATOM   327  C  CB   . LEU A 1 17  ? 9.76900   -20.74200 -0.67900  1.000 21.46000 ? 17  LEU A CB   1 
ATOM   328  C  CG   . LEU A 1 17  ? 8.77400   -20.00200 0.18400   1.000 25.81000 ? 17  LEU A CG   1 
ATOM   329  C  CD1  . LEU A 1 17  ? 7.44600   -20.02900 -0.50300  1.000 24.59000 ? 17  LEU A CD1  1 
ATOM   330  C  CD2  . LEU A 1 17  ? 8.61500   -20.59300 1.58600   1.000 22.09000 ? 17  LEU A CD2  1 
ATOM   331  H  H    . LEU A 1 17  ? 11.75600  -19.24400 -0.90500  1.000 28.71000 ? 17  LEU A H    1 
ATOM   332  H  HA   . LEU A 1 17  ? 11.03400  -21.02200 0.92600   1.000 25.47000 ? 17  LEU A HA   1 
ATOM   333  H  HB2  . LEU A 1 17  ? 9.87400   -20.24300 -1.50400  1.000 25.77000 ? 17  LEU A HB2  1 
ATOM   334  H  HB3  . LEU A 1 17  ? 9.40200   -21.62000 -0.86700  1.000 25.77000 ? 17  LEU A HB3  1 
ATOM   335  H  HG   . LEU A 1 17  ? 9.10300   -19.09800 0.30500   1.000 31.00000 ? 17  LEU A HG   1 
ATOM   336  H  HD11 . LEU A 1 17  ? 6.79800   -19.55800 0.04400   1.000 29.53000 ? 17  LEU A HD11 1 
ATOM   337  H  HD12 . LEU A 1 17  ? 7.52800   -19.59300 -1.36600  1.000 29.53000 ? 17  LEU A HD12 1 
ATOM   338  H  HD13 . LEU A 1 17  ? 7.17000   -20.95100 -0.62300  1.000 29.53000 ? 17  LEU A HD13 1 
ATOM   339  H  HD21 . LEU A 1 17  ? 7.80500   -20.24000 1.98700   1.000 26.53000 ? 17  LEU A HD21 1 
ATOM   340  H  HD22 . LEU A 1 17  ? 8.55600   -21.55800 1.51700   1.000 26.53000 ? 17  LEU A HD22 1 
ATOM   341  H  HD23 . LEU A 1 17  ? 9.38500   -20.34600 2.12200   1.000 26.53000 ? 17  LEU A HD23 1 
ATOM   342  N  N    A ASP A 1 18  ? 12.70200  -22.07500 -1.53500  0.420 23.79000 ? 18  ASP A N    1 
ATOM   343  N  N    B ASP A 1 18  ? 12.74500  -22.05700 -1.48600  0.580 23.81000 ? 18  ASP A N    1 
ATOM   344  C  CA   A ASP A 1 18  ? 13.32100  -23.28500 -2.04800  0.420 22.02000 ? 18  ASP A CA   1 
ATOM   345  C  CA   B ASP A 1 18  ? 13.31400  -23.22700 -2.13600  0.580 22.10000 ? 18  ASP A CA   1 
ATOM   346  C  C    A ASP A 1 18  ? 13.93700  -24.05500 -0.89100  0.420 25.39000 ? 18  ASP A C    1 
ATOM   347  C  C    B ASP A 1 18  ? 14.08300  -24.06300 -1.11900  0.580 24.03000 ? 18  ASP A C    1 
ATOM   348  O  O    A ASP A 1 18  ? 14.72000  -23.50100 -0.10600  0.420 26.37000 ? 18  ASP A O    1 
ATOM   349  O  O    B ASP A 1 18  ? 15.14800  -23.65500 -0.63900  0.580 21.57000 ? 18  ASP A O    1 
ATOM   350  C  CB   A ASP A 1 18  ? 14.39200  -22.95800 -3.09000  0.420 21.54000 ? 18  ASP A CB   1 
ATOM   351  C  CB   B ASP A 1 18  ? 14.21600  -22.81000 -3.29500  0.580 23.87000 ? 18  ASP A CB   1 
ATOM   352  C  CG   A ASP A 1 18  ? 14.73200  -24.14700 -3.99500  0.420 22.69000 ? 18  ASP A CG   1 
ATOM   353  C  CG   B ASP A 1 18  ? 15.26300  -21.77900 -2.89900  0.580 29.32000 ? 18  ASP A CG   1 
ATOM   354  O  OD1  A ASP A 1 18  ? 14.16000  -25.25300 -3.82800  0.420 20.79000 ? 18  ASP A OD1  1 
ATOM   355  O  OD1  B ASP A 1 18  ? 14.90500  -20.72800 -2.31700  0.580 26.09000 ? 18  ASP A OD1  1 
ATOM   356  O  OD2  A ASP A 1 18  ? 15.57500  -23.96800 -4.90700  0.420 31.00000 ? 18  ASP A OD2  1 
ATOM   357  O  OD2  B ASP A 1 18  ? 16.45400  -22.02100 -3.19300  0.580 30.20000 ? 18  ASP A OD2  1 
ATOM   358  H  H    A ASP A 1 18  ? 12.99300  -21.33900 -1.87300  0.420 28.57000 ? 18  ASP A H    1 
ATOM   359  H  H    B ASP A 1 18  ? 13.10200  -21.31100 -1.72200  0.580 28.59000 ? 18  ASP A H    1 
ATOM   360  H  HA   A ASP A 1 18  ? 12.65000  -23.83200 -2.48700  0.420 26.45000 ? 18  ASP A HA   1 
ATOM   361  H  HA   B ASP A 1 18  ? 12.59300  -23.76700 -2.49300  0.580 26.55000 ? 18  ASP A HA   1 
ATOM   362  H  HB2  A ASP A 1 18  ? 14.07300  -22.23500 -3.65400  0.420 25.88000 ? 18  ASP A HB2  1 
ATOM   363  H  HB2  B ASP A 1 18  ? 14.68000  -23.59300 -3.63100  0.580 28.67000 ? 18  ASP A HB2  1 
ATOM   364  H  HB3  A ASP A 1 18  ? 15.20400  -22.68800 -2.63300  0.420 25.88000 ? 18  ASP A HB3  1 
ATOM   365  H  HB3  B ASP A 1 18  ? 13.66800  -22.42300 -3.99700  0.580 28.67000 ? 18  ASP A HB3  1 
ATOM   366  N  N    A ASN A 1 19  ? 13.54900  -25.32700 -0.77000  0.470 20.48000 ? 19  ASN A N    1 
ATOM   367  N  N    B ASN A 1 19  ? 13.53900  -25.24100 -0.79700  0.530 20.68000 ? 19  ASN A N    1 
ATOM   368  C  CA   A ASN A 1 19  ? 14.04700  -26.23600 0.25900   0.470 19.09000 ? 19  ASN A CA   1 
ATOM   369  C  CA   B ASN A 1 19  ? 14.05800  -26.16800 0.20600   0.530 19.11000 ? 19  ASN A CA   1 
ATOM   370  C  C    A ASN A 1 19  ? 13.87000  -25.68400 1.67000   0.470 20.35000 ? 19  ASN A C    1 
ATOM   371  C  C    B ASN A 1 19  ? 13.84600  -25.69800 1.64100   0.530 20.27000 ? 19  ASN A C    1 
ATOM   372  O  O    A ASN A 1 19  ? 14.53400  -26.13100 2.61600   0.470 21.97000 ? 19  ASN A O    1 
ATOM   373  O  O    B ASN A 1 19  ? 14.46700  -26.23300 2.57200   0.530 21.82000 ? 19  ASN A O    1 
ATOM   374  C  CB   A ASN A 1 19  ? 15.48200  -26.68100 -0.03600  0.470 23.46000 ? 19  ASN A CB   1 
ATOM   375  C  CB   B ASN A 1 19  ? 15.51300  -26.58600 -0.03400  0.530 23.36000 ? 19  ASN A CB   1 
ATOM   376  C  CG   A ASN A 1 19  ? 15.53000  -27.71200 -1.14300  0.470 26.88000 ? 19  ASN A CG   1 
ATOM   377  C  CG   B ASN A 1 19  ? 15.72700  -28.05700 0.25500   0.530 24.08000 ? 19  ASN A CG   1 
ATOM   378  O  OD1  A ASN A 1 19  ? 14.90000  -28.76900 -1.04300  0.470 35.33000 ? 19  ASN A OD1  1 
ATOM   379  O  OD1  B ASN A 1 19  ? 14.80600  -28.86600 0.11600   0.530 26.77000 ? 19  ASN A OD1  1 
ATOM   380  N  ND2  A ASN A 1 19  ? 16.24100  -27.40000 -2.21900  0.470 38.79000 ? 19  ASN A ND2  1 
ATOM   381  N  ND2  B ASN A 1 19  ? 16.93600  -28.41100 0.68400   0.530 34.88000 ? 19  ASN A ND2  1 
ATOM   382  H  H    A ASN A 1 19  ? 12.97700  -25.69800 -1.29400  0.470 24.60000 ? 19  ASN A H    1 
ATOM   383  H  H    B ASN A 1 19  ? 12.82500  -25.54000 -1.17200  0.530 24.83000 ? 19  ASN A H    1 
ATOM   384  H  HA   A ASN A 1 19  ? 13.50800  -27.04200 0.24300   0.470 22.94000 ? 19  ASN A HA   1 
ATOM   385  H  HA   B ASN A 1 19  ? 13.53900  -26.98200 0.10900   0.530 22.95000 ? 19  ASN A HA   1 
ATOM   386  H  HB2  A ASN A 1 19  ? 16.00500  -25.91300 -0.31300  0.470 28.17000 ? 19  ASN A HB2  1 
ATOM   387  H  HB2  B ASN A 1 19  ? 15.74400  -26.42100 -0.96200  0.530 28.06000 ? 19  ASN A HB2  1 
ATOM   388  H  HB3  A ASN A 1 19  ? 15.86600  -27.07400 0.76300   0.470 28.17000 ? 19  ASN A HB3  1 
ATOM   389  H  HB3  B ASN A 1 19  ? 16.09400  -26.07300 0.54900   0.530 28.06000 ? 19  ASN A HB3  1 
ATOM   390  H  HD21 A ASN A 1 19  ? 16.29700  -27.95600 -2.87300  0.470 46.57000 ? 19  ASN A HD21 1 
ATOM   391  H  HD21 B ASN A 1 19  ? 17.10400  -29.23600 0.86100   0.530 41.88000 ? 19  ASN A HD21 1 
ATOM   392  H  HD22 A ASN A 1 19  ? 16.64600  -26.64300 -2.26200  0.470 46.57000 ? 19  ASN A HD22 1 
ATOM   393  H  HD22 B ASN A 1 19  ? 17.54800  -27.81600 0.78300   0.530 41.88000 ? 19  ASN A HD22 1 
ATOM   394  N  N    . TYR A 1 20  ? 12.95100  -24.74000 1.85900   1.000 19.77000 ? 20  TYR A N    1 
ATOM   395  C  CA   . TYR A 1 20  ? 12.62600  -24.30600 3.20600   1.000 20.29000 ? 20  TYR A CA   1 
ATOM   396  C  C    . TYR A 1 20  ? 12.00000  -25.47100 3.96800   1.000 23.75000 ? 20  TYR A C    1 
ATOM   397  O  O    . TYR A 1 20  ? 11.00400  -26.05600 3.52300   1.000 20.17000 ? 20  TYR A O    1 
ATOM   398  C  CB   . TYR A 1 20  ? 11.69000  -23.09900 3.17200   1.000 21.14000 ? 20  TYR A CB   1 
ATOM   399  C  CG   . TYR A 1 20  ? 11.54200  -22.45900 4.52400   1.000 19.93000 ? 20  TYR A CG   1 
ATOM   400  C  CD1  . TYR A 1 20  ? 12.47400  -21.53200 4.97800   1.000 24.10000 ? 20  TYR A CD1  1 
ATOM   401  C  CD2  . TYR A 1 20  ? 10.51400  -22.81600 5.37600   1.000 19.01000 ? 20  TYR A CD2  1 
ATOM   402  C  CE1  . TYR A 1 20  ? 12.35800  -20.97100 6.23100   1.000 26.14000 ? 20  TYR A CE1  1 
ATOM   403  C  CE2  . TYR A 1 20  ? 10.39700  -22.25800 6.63500   1.000 23.71000 ? 20  TYR A CE2  1 
ATOM   404  C  CZ   . TYR A 1 20  ? 11.32600  -21.34200 7.05200   1.000 27.65000 ? 20  TYR A CZ   1 
ATOM   405  O  OH   . TYR A 1 20  ? 11.21700  -20.75600 8.30000   1.000 31.75000 ? 20  TYR A OH   1 
ATOM   406  H  H    . TYR A 1 20  ? 12.52000  -24.32700 1.24000   1.000 23.75000 ? 20  TYR A H    1 
ATOM   407  H  HA   . TYR A 1 20  ? 13.43200  -24.02400 3.66800   1.000 24.38000 ? 20  TYR A HA   1 
ATOM   408  H  HB2  . TYR A 1 20  ? 12.04700  -22.43600 2.56000   1.000 25.39000 ? 20  TYR A HB2  1 
ATOM   409  H  HB3  . TYR A 1 20  ? 10.81200  -23.38500 2.87400   1.000 25.39000 ? 20  TYR A HB3  1 
ATOM   410  H  HD1  . TYR A 1 20  ? 13.18400  -21.28700 4.42900   1.000 28.95000 ? 20  TYR A HD1  1 
ATOM   411  H  HD2  . TYR A 1 20  ? 9.88800   -23.44500 5.09700   1.000 22.83000 ? 20  TYR A HD2  1 
ATOM   412  H  HE1  . TYR A 1 20  ? 12.97900  -20.34200 6.51900   1.000 31.39000 ? 20  TYR A HE1  1 
ATOM   413  H  HE2  . TYR A 1 20  ? 9.69500   -22.50200 7.19400   1.000 28.48000 ? 20  TYR A HE2  1 
ATOM   414  H  HH   . TYR A 1 20  ? 10.77500  -21.25300 8.81300   1.000 38.12000 ? 20  TYR A HH   1 
ATOM   415  N  N    A ARG A 1 21  ? 12.59700  -25.83100 5.10500   0.520 21.92000 ? 21  ARG A N    1 
ATOM   416  N  N    B ARG A 1 21  ? 12.62100  -25.82800 5.09400   0.480 21.99000 ? 21  ARG A N    1 
ATOM   417  C  CA   A ARG A 1 21  ? 12.17200  -26.99500 5.87900   0.520 21.83000 ? 21  ARG A CA   1 
ATOM   418  C  CA   B ARG A 1 21  ? 12.22800  -26.98900 5.88800   0.480 21.90000 ? 21  ARG A CA   1 
ATOM   419  C  C    A ARG A 1 21  ? 12.18900  -28.27300 5.04400   0.520 20.23000 ? 21  ARG A C    1 
ATOM   420  C  C    B ARG A 1 21  ? 12.18800  -28.26000 5.04400   0.480 20.23000 ? 21  ARG A C    1 
ATOM   421  O  O    A ARG A 1 21  ? 11.46100  -29.22800 5.33200   0.520 21.49000 ? 21  ARG A O    1 
ATOM   422  O  O    B ARG A 1 21  ? 11.42600  -29.18900 5.32400   0.480 21.54000 ? 21  ARG A O    1 
ATOM   423  C  CB   A ARG A 1 21  ? 10.80000  -26.78300 6.52600   0.520 23.96000 ? 21  ARG A CB   1 
ATOM   424  C  CB   B ARG A 1 21  ? 10.91000  -26.75000 6.62300   0.480 23.96000 ? 21  ARG A CB   1 
ATOM   425  C  CG   A ARG A 1 21  ? 10.82200  -25.87300 7.73900   0.520 34.16000 ? 21  ARG A CG   1 
ATOM   426  C  CG   B ARG A 1 21  ? 10.92000  -25.50500 7.50500   0.480 35.70000 ? 21  ARG A CG   1 
ATOM   427  C  CD   A ARG A 1 21  ? 11.23200  -26.61300 8.99500   0.520 36.94000 ? 21  ARG A CD   1 
ATOM   428  C  CD   B ARG A 1 21  ? 11.45200  -25.79600 8.90000   0.480 40.57000 ? 21  ARG A CD   1 
ATOM   429  N  NE   A ARG A 1 21  ? 11.02600  -25.79400 10.18700  0.520 44.60000 ? 21  ARG A NE   1 
ATOM   430  N  NE   B ARG A 1 21  ? 11.58800  -24.57600 9.69100   0.480 34.75000 ? 21  ARG A NE   1 
ATOM   431  C  CZ   A ARG A 1 21  ? 11.46800  -26.10500 11.39900  0.520 42.38000 ? 21  ARG A CZ   1 
ATOM   432  C  CZ   B ARG A 1 21  ? 12.72700  -23.92400 9.90100   0.480 40.69000 ? 21  ARG A CZ   1 
ATOM   433  N  NH1  A ARG A 1 21  ? 12.12500  -27.23100 11.62900  0.520 54.41000 ? 21  ARG A NH1  1 
ATOM   434  N  NH1  B ARG A 1 21  ? 13.87900  -24.35900 9.41400   0.480 42.93000 ? 21  ARG A NH1  1 
ATOM   435  N  NH2  A ARG A 1 21  ? 11.24500  -25.26500 12.40500  0.520 52.79000 ? 21  ARG A NH2  1 
ATOM   436  N  NH2  B ARG A 1 21  ? 12.70700  -22.80300 10.61800  0.480 39.31000 ? 21  ARG A NH2  1 
ATOM   437  H  H    A ARG A 1 21  ? 13.26200  -25.41000 5.45200   0.520 26.33000 ? 21  ARG A H    1 
ATOM   438  H  H    B ARG A 1 21  ? 13.29100  -25.40200 5.42600   0.480 26.42000 ? 21  ARG A H    1 
ATOM   439  H  HA   A ARG A 1 21  ? 12.81000  -27.11700 6.60000   0.520 26.22000 ? 21  ARG A HA   1 
ATOM   440  H  HA   B ARG A 1 21  ? 12.90400  -27.13200 6.56900   0.480 26.30000 ? 21  ARG A HA   1 
ATOM   441  H  HB2  A ARG A 1 21  ? 10.20600  -26.38500 5.87000   0.520 28.78000 ? 21  ARG A HB2  1 
ATOM   442  H  HB2  B ARG A 1 21  ? 10.20200  -26.64400 5.96900   0.480 28.78000 ? 21  ARG A HB2  1 
ATOM   443  H  HB3  A ARG A 1 21  ? 10.45400  -27.64300 6.80900   0.520 28.78000 ? 21  ARG A HB3  1 
ATOM   444  H  HB3  B ARG A 1 21  ? 10.72600  -27.51500 7.19100   0.480 28.78000 ? 21  ARG A HB3  1 
ATOM   445  H  HG2  A ARG A 1 21  ? 11.45800  -25.15600 7.58900   0.520 41.02000 ? 21  ARG A HG2  1 
ATOM   446  H  HG2  B ARG A 1 21  ? 11.48800  -24.83200 7.09900   0.480 42.86000 ? 21  ARG A HG2  1 
ATOM   447  H  HG3  A ARG A 1 21  ? 9.93500   -25.50600 7.87900   0.520 41.02000 ? 21  ARG A HG3  1 
ATOM   448  H  HG3  B ARG A 1 21  ? 10.01400  -25.16800 7.59100   0.480 42.86000 ? 21  ARG A HG3  1 
ATOM   449  H  HD2  A ARG A 1 21  ? 10.69800  -27.41900 9.08300   0.520 44.35000 ? 21  ARG A HD2  1 
ATOM   450  H  HD2  B ARG A 1 21  ? 10.83900  -26.39000 9.36000   0.480 48.71000 ? 21  ARG A HD2  1 
ATOM   451  H  HD3  A ARG A 1 21  ? 12.17300  -26.84300 8.94100   0.520 44.35000 ? 21  ARG A HD3  1 
ATOM   452  H  HD3  B ARG A 1 21  ? 12.32600  -26.21200 8.83000   0.480 48.71000 ? 21  ARG A HD3  1 
ATOM   453  H  HE   A ARG A 1 21  ? 10.58800  -25.06000 10.09700  0.520 53.55000 ? 21  ARG A HE   1 
ATOM   454  H  HE   B ARG A 1 21  ? 10.87500  -24.25500 10.04900  0.480 41.73000 ? 21  ARG A HE   1 
ATOM   455  H  HH11 A ARG A 1 21  ? 12.27300  -27.78100 10.98600  0.520 65.31000 ? 21  ARG A HH11 1 
ATOM   456  H  HH11 B ARG A 1 21  ? 13.90300  -25.08100 8.94900   0.480 51.55000 ? 21  ARG A HH11 1 
ATOM   457  H  HH12 A ARG A 1 21  ? 12.40200  -27.41200 12.42300  0.520 65.31000 ? 21  ARG A HH12 1 
ATOM   458  H  HH12 B ARG A 1 21  ? 14.60200  -23.91900 9.56400   0.480 51.55000 ? 21  ARG A HH12 1 
ATOM   459  H  HH21 A ARG A 1 21  ? 10.81800  -24.53100 12.26600  0.520 63.38000 ? 21  ARG A HH21 1 
ATOM   460  H  HH21 B ARG A 1 21  ? 11.96500  -22.51000 10.93800  0.480 47.19000 ? 21  ARG A HH21 1 
ATOM   461  H  HH22 A ARG A 1 21  ? 11.52700  -25.45500 13.19500  0.520 63.38000 ? 21  ARG A HH22 1 
ATOM   462  H  HH22 B ARG A 1 21  ? 13.43700  -22.37100 10.76100  0.480 47.19000 ? 21  ARG A HH22 1 
ATOM   463  N  N    . GLY A 1 22  ? 13.02700  -28.31000 4.01700   1.000 19.34000 ? 22  GLY A N    1 
ATOM   464  C  CA   . GLY A 1 22  ? 13.17700  -29.48600 3.19200   1.000 19.42000 ? 22  GLY A CA   1 
ATOM   465  C  C    . GLY A 1 22  ? 12.20100  -29.63100 2.05000   1.000 19.36000 ? 22  GLY A C    1 
ATOM   466  O  O    . GLY A 1 22  ? 12.22700  -30.65400 1.36400   1.000 20.31000 ? 22  GLY A O    1 
ATOM   467  H  H    . GLY A 1 22  ? 13.52700  -27.65200 3.77700   1.000 23.24000 ? 22  GLY A H    1 
ATOM   468  H  HA2  . GLY A 1 22  ? 14.06900  -29.47900 2.81100   1.000 23.33000 ? 22  GLY A HA2  1 
ATOM   469  H  HA3  . GLY A 1 22  ? 13.08100  -30.26900 3.75600   1.000 23.33000 ? 22  GLY A HA3  1 
ATOM   470  N  N    . TYR A 1 23  ? 11.35900  -28.63600 1.80600   1.000 16.60000 ? 23  TYR A N    1 
ATOM   471  C  CA   . TYR A 1 23  ? 10.38200  -28.68200 0.73000   1.000 15.23000 ? 23  TYR A CA   1 
ATOM   472  C  C    . TYR A 1 23  ? 10.93600  -27.94600 -0.47700  1.000 15.09000 ? 23  TYR A C    1 
ATOM   473  O  O    . TYR A 1 23  ? 11.02500  -26.70700 -0.47700  1.000 16.89000 ? 23  TYR A O    1 
ATOM   474  C  CB   . TYR A 1 23  ? 9.06900   -28.07800 1.21500   1.000 14.97000 ? 23  TYR A CB   1 
ATOM   475  C  CG   . TYR A 1 23  ? 8.40200   -28.95100 2.22700   1.000 12.48000 ? 23  TYR A CG   1 
ATOM   476  C  CD1  . TYR A 1 23  ? 7.59300   -29.97400 1.83800   1.000 13.57000 ? 23  TYR A CD1  1 
ATOM   477  C  CD2  . TYR A 1 23  ? 8.58600   -28.73800 3.57500   1.000 15.31000 ? 23  TYR A CD2  1 
ATOM   478  C  CE1  . TYR A 1 23  ? 6.96200   -30.79100 2.77400   1.000 13.47000 ? 23  TYR A CE1  1 
ATOM   479  C  CE2  . TYR A 1 23  ? 7.97800   -29.54200 4.52000   1.000 14.68000 ? 23  TYR A CE2  1 
ATOM   480  C  CZ   . TYR A 1 23  ? 7.15400   -30.56500 4.10000   1.000 14.21000 ? 23  TYR A CZ   1 
ATOM   481  O  OH   . TYR A 1 23  ? 6.49200   -31.38500 4.99700   1.000 16.03000 ? 23  TYR A OH   1 
ATOM   482  H  H    . TYR A 1 23  ? 11.33500  -27.90700 2.26100   1.000 19.94000 ? 23  TYR A H    1 
ATOM   483  H  HA   . TYR A 1 23  ? 10.22600  -29.59900 0.45500   1.000 18.30000 ? 23  TYR A HA   1 
ATOM   484  H  HB2  . TYR A 1 23  ? 9.24500   -27.21700 1.62400   1.000 17.99000 ? 23  TYR A HB2  1 
ATOM   485  H  HB3  . TYR A 1 23  ? 8.46800   -27.97100 0.46100   1.000 17.99000 ? 23  TYR A HB3  1 
ATOM   486  H  HD1  . TYR A 1 23  ? 7.45900   -30.13100 0.93100   1.000 16.30000 ? 23  TYR A HD1  1 
ATOM   487  H  HD2  . TYR A 1 23  ? 9.13100   -28.03800 3.85600   1.000 18.40000 ? 23  TYR A HD2  1 
ATOM   488  H  HE1  . TYR A 1 23  ? 6.41300   -31.48700 2.49300   1.000 16.19000 ? 23  TYR A HE1  1 
ATOM   489  H  HE2  . TYR A 1 23  ? 8.12200   -29.39600 5.42700   1.000 17.64000 ? 23  TYR A HE2  1 
ATOM   490  H  HH   . TYR A 1 23  ? 6.81100   -31.28400 5.76800   1.000 19.26000 ? 23  TYR A HH   1 
ATOM   491  N  N    . SER A 1 24  ? 11.26400  -28.71400 -1.51400  1.000 16.39000 ? 24  SER A N    1 
ATOM   492  C  CA   . SER A 1 24  ? 11.80000  -28.12600 -2.73300  1.000 16.57000 ? 24  SER A CA   1 
ATOM   493  C  C    . SER A 1 24  ? 10.75800  -27.22600 -3.37800  1.000 15.83000 ? 24  SER A C    1 
ATOM   494  O  O    . SER A 1 24  ? 9.55000   -27.34200 -3.14300  1.000 15.32000 ? 24  SER A O    1 
ATOM   495  C  CB   . SER A 1 24  ? 12.23000  -29.20100 -3.72600  1.000 18.45000 ? 24  SER A CB   1 
ATOM   496  O  OG   . SER A 1 24  ? 11.12600  -29.91400 -4.23900  1.000 23.32000 ? 24  SER A OG   1 
ATOM   497  H  H    . SER A 1 24  ? 11.18600  -29.57000 -1.53500  1.000 19.69000 ? 24  SER A H    1 
ATOM   498  H  HA   . SER A 1 24  ? 12.58500  -27.60000 -2.51100  1.000 19.91000 ? 24  SER A HA   1 
ATOM   499  H  HB2  . SER A 1 24  ? 12.69600  -28.77600 -4.46300  1.000 22.17000 ? 24  SER A HB2  1 
ATOM   500  H  HB3  . SER A 1 24  ? 12.82100  -29.82400 -3.27500  1.000 22.17000 ? 24  SER A HB3  1 
ATOM   501  H  HG   . SER A 1 24  ? 10.75600  -30.35100 -3.62500  1.000 28.01000 ? 24  SER A HG   1 
ATOM   502  N  N    . LEU A 1 25  ? 11.24600  -26.30800 -4.21200  1.000 16.40000 ? 25  LEU A N    1 
ATOM   503  C  CA   . LEU A 1 25  ? 10.41400  -25.26600 -4.78000  1.000 14.44000 ? 25  LEU A CA   1 
ATOM   504  C  C    . LEU A 1 25  ? 9.17600   -25.79800 -5.48400  1.000 15.85000 ? 25  LEU A C    1 
ATOM   505  O  O    . LEU A 1 25  ? 8.11500   -25.16800 -5.42800  1.000 15.44000 ? 25  LEU A O    1 
ATOM   506  C  CB   . LEU A 1 25  ? 11.26600  -24.45000 -5.76500  1.000 17.85000 ? 25  LEU A CB   1 
ATOM   507  C  CG   . LEU A 1 25  ? 10.73700  -23.12900 -6.27700  1.000 19.34000 ? 25  LEU A CG   1 
ATOM   508  C  CD1  . LEU A 1 25  ? 10.43600  -22.18600 -5.14100  1.000 22.48000 ? 25  LEU A CD1  1 
ATOM   509  C  CD2  . LEU A 1 25  ? 11.78800  -22.48700 -7.18500  1.000 22.01000 ? 25  LEU A CD2  1 
ATOM   510  H  H    . LEU A 1 25  ? 12.06700  -26.27000 -4.46400  1.000 19.70000 ? 25  LEU A H    1 
ATOM   511  H  HA   . LEU A 1 25  ? 10.09600  -24.70100 -4.05800  1.000 17.35000 ? 25  LEU A HA   1 
ATOM   512  H  HB2  . LEU A 1 25  ? 12.11000  -24.25600 -5.32700  1.000 21.45000 ? 25  LEU A HB2  1 
ATOM   513  H  HB3  . LEU A 1 25  ? 11.41800  -25.00500 -6.54600  1.000 21.45000 ? 25  LEU A HB3  1 
ATOM   514  H  HG   . LEU A 1 25  ? 9.91500   -23.28900 -6.76700  1.000 23.23000 ? 25  LEU A HG   1 
ATOM   515  H  HD11 . LEU A 1 25  ? 10.24700  -21.30600 -5.50300  1.000 27.00000 ? 25  LEU A HD11 1 
ATOM   516  H  HD12 . LEU A 1 25  ? 9.66500   -22.51600 -4.65300  1.000 27.00000 ? 25  LEU A HD12 1 
ATOM   517  H  HD13 . LEU A 1 25  ? 11.20700  -22.14300 -4.55400  1.000 27.00000 ? 25  LEU A HD13 1 
ATOM   518  H  HD21 . LEU A 1 25  ? 11.41700  -21.68100 -7.57700  1.000 26.44000 ? 25  LEU A HD21 1 
ATOM   519  H  HD22 . LEU A 1 25  ? 12.57100  -22.26800 -6.65600  1.000 26.44000 ? 25  LEU A HD22 1 
ATOM   520  H  HD23 . LEU A 1 25  ? 12.02700  -23.11500 -7.88400  1.000 26.44000 ? 25  LEU A HD23 1 
ATOM   521  N  N    . GLY A 1 26  ? 9.27400   -26.90700 -6.20400  1.000 14.66000 ? 26  GLY A N    1 
ATOM   522  C  CA   . GLY A 1 26  ? 8.11300   -27.42400 -6.89900  1.000 15.46000 ? 26  GLY A CA   1 
ATOM   523  C  C    . GLY A 1 26  ? 6.92700   -27.70200 -5.99300  1.000 14.40000 ? 26  GLY A C    1 
ATOM   524  O  O    . GLY A 1 26  ? 5.77900   -27.62900 -6.43600  1.000 14.28000 ? 26  GLY A O    1 
ATOM   525  H  H    . GLY A 1 26  ? 9.99200   -27.37100 -6.30300  1.000 17.62000 ? 26  GLY A H    1 
ATOM   526  H  HA2  . GLY A 1 26  ? 7.83400   -26.78000 -7.56800  1.000 18.58000 ? 26  GLY A HA2  1 
ATOM   527  H  HA3  . GLY A 1 26  ? 8.35400   -28.25400 -7.34000  1.000 18.58000 ? 26  GLY A HA3  1 
ATOM   528  N  N    . ASN A 1 27  ? 7.18200   -28.06600 -4.73700  1.000 13.69000 ? 27  ASN A N    1 
ATOM   529  C  CA   . ASN A 1 27  ? 6.08300   -28.30100 -3.79400  1.000 13.63000 ? 27  ASN A CA   1 
ATOM   530  C  C    . ASN A 1 27  ? 5.26200   -27.03700 -3.60700  1.000 13.90000 ? 27  ASN A C    1 
ATOM   531  O  O    . ASN A 1 27  ? 4.02300   -27.08100 -3.54200  1.000 13.46000 ? 27  ASN A O    1 
ATOM   532  C  CB   . ASN A 1 27  ? 6.62100   -28.70800 -2.43400  1.000 13.76000 ? 27  ASN A CB   1 
ATOM   533  C  CG   . ASN A 1 27  ? 7.10900   -30.11600 -2.41000  1.000 15.60000 ? 27  ASN A CG   1 
ATOM   534  O  OD1  . ASN A 1 27  ? 6.32400   -31.05800 -2.45500  1.000 15.88000 ? 27  ASN A OD1  1 
ATOM   535  N  ND2  . ASN A 1 27  ? 8.44200   -30.27200 -2.42000  1.000 15.70000 ? 27  ASN A ND2  1 
ATOM   536  H  H    . ASN A 1 27  ? 7.96800   -28.18300 -4.40800  1.000 16.45000 ? 27  ASN A H    1 
ATOM   537  H  HA   . ASN A 1 27  ? 5.53300   -29.01700 -4.14900  1.000 16.38000 ? 27  ASN A HA   1 
ATOM   538  H  HB2  . ASN A 1 27  ? 7.36300   -28.12800 -2.20100  1.000 16.54000 ? 27  ASN A HB2  1 
ATOM   539  H  HB3  . ASN A 1 27  ? 5.91500   -28.62300 -1.77500  1.000 16.54000 ? 27  ASN A HB3  1 
ATOM   540  H  HD21 . ASN A 1 27  ? 8.78300   -31.06100 -2.40700  1.000 18.86000 ? 27  ASN A HD21 1 
ATOM   541  H  HD22 . ASN A 1 27  ? 8.95500   -29.58200 -2.43900  1.000 18.86000 ? 27  ASN A HD22 1 
ATOM   542  N  N    . TRP A 1 28  ? 5.94300   -25.90100 -3.48500  1.000 13.26000 ? 28  TRP A N    1 
ATOM   543  C  CA   . TRP A 1 28  ? 5.26700   -24.64400 -3.22800  1.000 12.71000 ? 28  TRP A CA   1 
ATOM   544  C  C    . TRP A 1 28  ? 4.49200   -24.16900 -4.44000  1.000 13.81000 ? 28  TRP A C    1 
ATOM   545  O  O    . TRP A 1 28  ? 3.39400   -23.63100 -4.30900  1.000 14.73000 ? 28  TRP A O    1 
ATOM   546  C  CB   . TRP A 1 28  ? 6.28700   -23.59000 -2.77300  1.000 14.50000 ? 28  TRP A CB   1 
ATOM   547  C  CG   . TRP A 1 28  ? 7.00200   -23.96200 -1.50000  1.000 15.91000 ? 28  TRP A CG   1 
ATOM   548  C  CD1  . TRP A 1 28  ? 8.24900   -24.51500 -1.36200  1.000 15.31000 ? 28  TRP A CD1  1 
ATOM   549  C  CD2  . TRP A 1 28  ? 6.47800   -23.83600 -0.17500  1.000 14.95000 ? 28  TRP A CD2  1 
ATOM   550  N  NE1  . TRP A 1 28  ? 8.52700   -24.73400 -0.03400  1.000 17.06000 ? 28  TRP A NE1  1 
ATOM   551  C  CE2  . TRP A 1 28  ? 7.45600   -24.31800 0.71400   1.000 15.24000 ? 28  TRP A CE2  1 
ATOM   552  C  CE3  . TRP A 1 28  ? 5.27000   -23.34600 0.33800   1.000 17.00000 ? 28  TRP A CE3  1 
ATOM   553  C  CZ2  . TRP A 1 28  ? 7.26800   -24.31000 2.09400   1.000 17.81000 ? 28  TRP A CZ2  1 
ATOM   554  C  CZ3  . TRP A 1 28  ? 5.08800   -23.34400 1.69200   1.000 18.30000 ? 28  TRP A CZ3  1 
ATOM   555  C  CH2  . TRP A 1 28  ? 6.07500   -23.82900 2.55800   1.000 19.42000 ? 28  TRP A CH2  1 
ATOM   556  H  H    . TRP A 1 28  ? 6.79800   -25.83400 -3.54900  1.000 15.94000 ? 28  TRP A H    1 
ATOM   557  H  HA   . TRP A 1 28  ? 4.62800   -24.77000 -2.50900  1.000 15.28000 ? 28  TRP A HA   1 
ATOM   558  H  HB2  . TRP A 1 28  ? 6.95500   -23.47900 -3.46900  1.000 17.43000 ? 28  TRP A HB2  1 
ATOM   559  H  HB3  . TRP A 1 28  ? 5.82500   -22.75100 -2.62100  1.000 17.43000 ? 28  TRP A HB3  1 
ATOM   560  H  HD1  . TRP A 1 28  ? 8.82400   -24.71400 -2.06600  1.000 18.40000 ? 28  TRP A HD1  1 
ATOM   561  H  HE1  . TRP A 1 28  ? 9.25200   -25.07500 0.27600   1.000 20.49000 ? 28  TRP A HE1  1 
ATOM   562  H  HE3  . TRP A 1 28  ? 4.60600   -23.02900 -0.23100  1.000 20.42000 ? 28  TRP A HE3  1 
ATOM   563  H  HZ2  . TRP A 1 28  ? 7.92500   -24.61900 2.67500   1.000 21.39000 ? 28  TRP A HZ2  1 
ATOM   564  H  HZ3  . TRP A 1 28  ? 4.29300   -23.01500 2.04500   1.000 21.99000 ? 28  TRP A HZ3  1 
ATOM   565  H  HH2  . TRP A 1 28  ? 5.91500   -23.82400 3.47500   1.000 23.33000 ? 28  TRP A HH2  1 
ATOM   566  N  N    . VAL A 1 29  ? 5.05300   -24.35600 -5.62800  1.000 14.10000 ? 29  VAL A N    1 
ATOM   567  C  CA   . VAL A 1 29  ? 4.37000   -23.98300 -6.85900  1.000 11.98000 ? 29  VAL A CA   1 
ATOM   568  C  C    . VAL A 1 29  ? 3.14600   -24.85800 -7.07000  1.000 14.22000 ? 29  VAL A C    1 
ATOM   569  O  O    . VAL A 1 29  ? 2.07200   -24.37500 -7.43900  1.000 14.66000 ? 29  VAL A O    1 
ATOM   570  C  CB   . VAL A 1 29  ? 5.34400   -24.04600 -8.05100  1.000 14.59000 ? 29  VAL A CB   1 
ATOM   571  C  CG1  . VAL A 1 29  ? 4.62500   -23.72300 -9.35800  1.000 16.30000 ? 29  VAL A CG1  1 
ATOM   572  C  CG2  . VAL A 1 29  ? 6.50300   -23.06600 -7.85500  1.000 17.13000 ? 29  VAL A CG2  1 
ATOM   573  H  H    . VAL A 1 29  ? 5.83200   -24.70000 -5.75000  1.000 16.95000 ? 29  VAL A H    1 
ATOM   574  H  HA   . VAL A 1 29  ? 4.06500   -23.06500 -6.78000  1.000 14.40000 ? 29  VAL A HA   1 
ATOM   575  H  HB   . VAL A 1 29  ? 5.69700   -24.94800 -8.10300  1.000 17.54000 ? 29  VAL A HB   1 
ATOM   576  H  HG11 . VAL A 1 29  ? 5.28500   -23.58300 -10.05500 1.000 19.58000 ? 29  VAL A HG11 1 
ATOM   577  H  HG12 . VAL A 1 29  ? 4.04800   -24.46600 -9.59300  1.000 19.58000 ? 29  VAL A HG12 1 
ATOM   578  H  HG13 . VAL A 1 29  ? 4.09600   -22.91900 -9.23700  1.000 19.58000 ? 29  VAL A HG13 1 
ATOM   579  H  HG21 . VAL A 1 29  ? 6.95100   -22.93300 -8.70500  1.000 20.57000 ? 29  VAL A HG21 1 
ATOM   580  H  HG22 . VAL A 1 29  ? 6.15100   -22.22200 -7.53100  1.000 20.57000 ? 29  VAL A HG22 1 
ATOM   581  H  HG23 . VAL A 1 29  ? 7.12300   -23.43700 -7.20800  1.000 20.57000 ? 29  VAL A HG23 1 
ATOM   582  N  N    . CYS A 1 30  ? 3.28300   -26.16900 -6.82800  1.000 13.23000 ? 30  CYS A N    1 
ATOM   583  C  CA   . CYS A 1 30  ? 2.16100   -27.08500 -6.93200  1.000 13.05000 ? 30  CYS A CA   1 
ATOM   584  C  C    . CYS A 1 30  ? 1.04700   -26.69200 -5.97000  1.000 13.72000 ? 30  CYS A C    1 
ATOM   585  O  O    . CYS A 1 30  ? -0.13300  -26.65100 -6.34300  1.000 13.89000 ? 30  CYS A O    1 
ATOM   586  C  CB   . CYS A 1 30  ? 2.66700   -28.51300 -6.67500  1.000 14.29000 ? 30  CYS A CB   1 
ATOM   587  S  SG   . CYS A 1 30  ? 1.40800   -29.78400 -6.87200  1.000 14.61000 ? 30  CYS A SG   1 
ATOM   588  H  H    . CYS A 1 30  ? 4.02200   -26.54700 -6.60100  1.000 15.90000 ? 30  CYS A H    1 
ATOM   589  H  HA   . CYS A 1 30  ? 1.78400   -27.05600 -7.82500  1.000 15.69000 ? 30  CYS A HA   1 
ATOM   590  H  HB2  . CYS A 1 30  ? 3.38200   -28.70700 -7.30100  1.000 17.17000 ? 30  CYS A HB2  1 
ATOM   591  H  HB3  . CYS A 1 30  ? 3.00000   -28.56600 -5.76500  1.000 17.17000 ? 30  CYS A HB3  1 
ATOM   592  N  N    . ALA A 1 31  ? 1.40900   -26.38200 -4.74300  1.000 12.44000 ? 31  ALA A N    1 
ATOM   593  C  CA   . ALA A 1 31  ? 0.38300   -26.00600 -3.76700  1.000 13.37000 ? 31  ALA A CA   1 
ATOM   594  C  C    . ALA A 1 31  ? -0.32900  -24.73500 -4.20800  1.000 14.25000 ? 31  ALA A C    1 
ATOM   595  O  O    . ALA A 1 31  ? -1.55800  -24.65000 -4.13500  1.000 14.59000 ? 31  ALA A O    1 
ATOM   596  C  CB   . ALA A 1 31  ? 1.03100   -25.79900 -2.40000  1.000 14.33000 ? 31  ALA A CB   1 
ATOM   597  H  H    . ALA A 1 31  ? 2.21600   -26.37700 -4.44800  1.000 14.95000 ? 31  ALA A H    1 
ATOM   598  H  HA   . ALA A 1 31  ? -0.27100  -26.71900 -3.69200  1.000 16.07000 ? 31  ALA A HA   1 
ATOM   599  H  HB1  . ALA A 1 31  ? 0.34400   -25.56200 -1.75800  1.000 17.22000 ? 31  ALA A HB1  1 
ATOM   600  H  HB2  . ALA A 1 31  ? 1.46800   -26.62200 -2.13000  1.000 17.22000 ? 31  ALA A HB2  1 
ATOM   601  H  HB3  . ALA A 1 31  ? 1.68400   -25.08400 -2.46500  1.000 17.22000 ? 31  ALA A HB3  1 
ATOM   602  N  N    . ALA A 1 32  ? 0.42600   -23.73500 -4.67200  1.000 13.56000 ? 32  ALA A N    1 
ATOM   603  C  CA   . ALA A 1 32  ? -0.19300  -22.49400 -5.11800  1.000 12.34000 ? 32  ALA A CA   1 
ATOM   604  C  C    . ALA A 1 32  ? -1.12800  -22.72400 -6.30100  1.000 13.06000 ? 32  ALA A C    1 
ATOM   605  O  O    . ALA A 1 32  ? -2.19000  -22.08400 -6.39700  1.000 14.48000 ? 32  ALA A O    1 
ATOM   606  C  CB   . ALA A 1 32  ? 0.87800   -21.46400 -5.46100  1.000 13.80000 ? 32  ALA A CB   1 
ATOM   607  H  H    . ALA A 1 32  ? 1.28400   -23.75300 -4.73600  1.000 16.29000 ? 32  ALA A H    1 
ATOM   608  H  HA   . ALA A 1 32  ? -0.72600  -22.13800 -4.39000  1.000 14.83000 ? 32  ALA A HA   1 
ATOM   609  H  HB1  . ALA A 1 32  ? 0.46300   -20.71900 -5.92400  1.000 16.58000 ? 32  ALA A HB1  1 
ATOM   610  H  HB2  . ALA A 1 32  ? 1.29300   -21.15400 -4.64100  1.000 16.58000 ? 32  ALA A HB2  1 
ATOM   611  H  HB3  . ALA A 1 32  ? 1.54300   -21.87800 -6.03200  1.000 16.58000 ? 32  ALA A HB3  1 
ATOM   612  N  N    . LYS A 1 33  ? -0.74400  -23.59300 -7.23500  1.000 12.84000 ? 33  LYS A N    1 
ATOM   613  C  CA   . LYS A 1 33  ? -1.61800  -23.84100 -8.36900  1.000 13.79000 ? 33  LYS A CA   1 
ATOM   614  C  C    . LYS A 1 33  ? -2.97700  -24.34700 -7.91500  1.000 13.51000 ? 33  LYS A C    1 
ATOM   615  O  O    . LYS A 1 33  ? -4.01800  -23.87200 -8.37700  1.000 14.33000 ? 33  LYS A O    1 
ATOM   616  C  CB   . LYS A 1 33  ? -0.98200  -24.89200 -9.28200  1.000 17.27000 ? 33  LYS A CB   1 
ATOM   617  C  CG   . LYS A 1 33  ? -1.88300  -25.35700 -10.45700 1.000 18.01000 ? 33  LYS A CG   1 
ATOM   618  C  CD   . LYS A 1 33  ? -2.01900  -24.27400 -11.49100 1.000 26.75000 ? 33  LYS A CD   1 
ATOM   619  C  CE   . LYS A 1 33  ? -2.86600  -24.72600 -12.67700 1.000 38.23000 ? 33  LYS A CE   1 
ATOM   620  N  NZ   . LYS A 1 33  ? -3.05600  -23.61800 -13.64500 1.000 44.49000 ? 33  LYS A NZ   1 
ATOM   621  H  H    . LYS A 1 33  ? -0.00700  -24.03700 -7.23200  1.000 15.43000 ? 33  LYS A H    1 
ATOM   622  H  HA   . LYS A 1 33  ? -1.73400  -23.01000 -8.85600  1.000 16.57000 ? 33  LYS A HA   1 
ATOM   623  H  HB2  . LYS A 1 33  ? -0.17200  -24.51900 -9.66400  1.000 20.75000 ? 33  LYS A HB2  1 
ATOM   624  H  HB3  . LYS A 1 33  ? -0.76800  -25.67400 -8.74900  1.000 20.75000 ? 33  LYS A HB3  1 
ATOM   625  H  HG2  . LYS A 1 33  ? -1.48900  -26.13700 -10.87800 1.000 21.64000 ? 33  LYS A HG2  1 
ATOM   626  H  HG3  . LYS A 1 33  ? -2.76700  -25.57300 -10.12100 1.000 21.64000 ? 33  LYS A HG3  1 
ATOM   627  H  HD2  . LYS A 1 33  ? -2.44600  -23.50100 -11.09100 1.000 32.13000 ? 33  LYS A HD2  1 
ATOM   628  H  HD3  . LYS A 1 33  ? -1.13900  -24.03400 -11.82100 1.000 32.13000 ? 33  LYS A HD3  1 
ATOM   629  H  HE2  . LYS A 1 33  ? -2.42100  -25.45900 -13.13100 1.000 45.90000 ? 33  LYS A HE2  1 
ATOM   630  H  HE3  . LYS A 1 33  ? -3.73700  -25.01200 -12.36100 1.000 45.90000 ? 33  LYS A HE3  1 
ATOM   631  H  HZ1  . LYS A 1 33  ? -3.58700  -22.99500 -13.29400 1.000 53.41000 ? 33  LYS A HZ1  1 
ATOM   632  H  HZ2  . LYS A 1 33  ? -2.27100  -23.25000 -13.84400 1.000 53.41000 ? 33  LYS A HZ2  1 
ATOM   633  H  HZ3  . LYS A 1 33  ? -3.42800  -23.92700 -14.39200 1.000 53.41000 ? 33  LYS A HZ3  1 
ATOM   634  N  N    . PHE A 1 34  ? -2.99500  -25.34200 -7.03600  1.000 13.10000 ? 34  PHE A N    1 
ATOM   635  C  CA   . PHE A 1 34  ? -4.26600  -25.94600 -6.67700  1.000 14.08000 ? 34  PHE A CA   1 
ATOM   636  C  C    . PHE A 1 34  ? -5.00300  -25.17800 -5.59500  1.000 15.18000 ? 34  PHE A C    1 
ATOM   637  O  O    . PHE A 1 34  ? -6.22700  -25.30000 -5.51500  1.000 18.99000 ? 34  PHE A O    1 
ATOM   638  C  CB   . PHE A 1 34  ? -4.05400  -27.42500 -6.32300  1.000 15.19000 ? 34  PHE A CB   1 
ATOM   639  C  CG   . PHE A 1 34  ? -3.58100  -28.23900 -7.50200  1.000 14.86000 ? 34  PHE A CG   1 
ATOM   640  C  CD1  . PHE A 1 34  ? -4.33600  -28.28400 -8.64600  1.000 18.26000 ? 34  PHE A CD1  1 
ATOM   641  C  CD2  . PHE A 1 34  ? -2.37200  -28.89400 -7.48700  1.000 19.71000 ? 34  PHE A CD2  1 
ATOM   642  C  CE1  . PHE A 1 34  ? -3.91700  -28.99200 -9.74100  1.000 19.77000 ? 34  PHE A CE1  1 
ATOM   643  C  CE2  . PHE A 1 34  ? -1.95400  -29.61100 -8.60000  1.000 25.14000 ? 34  PHE A CE2  1 
ATOM   644  C  CZ   . PHE A 1 34  ? -2.74200  -29.64200 -9.71100  1.000 20.67000 ? 34  PHE A CZ   1 
ATOM   645  H  H    . PHE A 1 34  ? -2.30500  -25.67400 -6.64600  1.000 15.75000 ? 34  PHE A H    1 
ATOM   646  H  HA   . PHE A 1 34  ? -4.86400  -25.93900 -7.44100  1.000 16.92000 ? 34  PHE A HA   1 
ATOM   647  H  HB2  . PHE A 1 34  ? -3.38600  -27.49100 -5.62400  1.000 18.25000 ? 34  PHE A HB2  1 
ATOM   648  H  HB3  . PHE A 1 34  ? -4.89400  -27.80100 -6.01600  1.000 18.25000 ? 34  PHE A HB3  1 
ATOM   649  H  HD1  . PHE A 1 34  ? -5.14500  -27.82600 -8.67900  1.000 21.93000 ? 34  PHE A HD1  1 
ATOM   650  H  HD2  . PHE A 1 34  ? -1.83300  -28.85600 -6.73000  1.000 23.68000 ? 34  PHE A HD2  1 
ATOM   651  H  HE1  . PHE A 1 34  ? -4.44600  -29.02300 -10.50600 1.000 23.75000 ? 34  PHE A HE1  1 
ATOM   652  H  HE2  . PHE A 1 34  ? -1.14300  -30.06600 -8.58700  1.000 30.20000 ? 34  PHE A HE2  1 
ATOM   653  H  HZ   . PHE A 1 34  ? -2.46200  -30.12000 -10.45900 1.000 24.82000 ? 34  PHE A HZ   1 
ATOM   654  N  N    . GLU A 1 35  ? -4.31600  -24.36800 -4.80900  1.000 13.22000 ? 35  GLU A N    1 
ATOM   655  C  CA   . GLU A 1 35  ? -5.01900  -23.54000 -3.83600  1.000 13.97000 ? 35  GLU A CA   1 
ATOM   656  C  C    . GLU A 1 35  ? -5.66600  -22.31800 -4.48400  1.000 15.14000 ? 35  GLU A C    1 
ATOM   657  O  O    . GLU A 1 35  ? -6.78100  -21.95300 -4.11600  1.000 15.90000 ? 35  GLU A O    1 
ATOM   658  C  CB   . GLU A 1 35  ? -4.05100  -23.06500 -2.76100  1.000 14.22000 ? 35  GLU A CB   1 
ATOM   659  C  CG   . GLU A 1 35  ? -3.53800  -24.14100 -1.85700  1.000 13.49000 ? 35  GLU A CG   1 
ATOM   660  C  CD   . GLU A 1 35  ? -4.57900  -24.67100 -0.88100  1.000 18.49000 ? 35  GLU A CD   1 
ATOM   661  O  OE1  . GLU A 1 35  ? -5.74600  -24.22400 -0.91400  1.000 18.07000 ? 35  GLU A OE1  1 
ATOM   662  O  OE2  . GLU A 1 35  ? -4.23500  -25.60300 -0.09700  1.000 18.62000 ? 35  GLU A OE2  1 
ATOM   663  H  H    . GLU A 1 35  ? -3.46100  -24.27900 -4.81500  1.000 15.88000 ? 35  GLU A H    1 
ATOM   664  H  HA   . GLU A 1 35  ? -5.71200  -24.08200 -3.43000  1.000 16.79000 ? 35  GLU A HA   1 
ATOM   665  H  HB2  . GLU A 1 35  ? -3.28500  -22.65900 -3.19500  1.000 17.08000 ? 35  GLU A HB2  1 
ATOM   666  H  HB3  . GLU A 1 35  ? -4.50500  -22.41000 -2.20700  1.000 17.08000 ? 35  GLU A HB3  1 
ATOM   667  H  HG2  . GLU A 1 35  ? -3.23500  -24.88600 -2.40000  1.000 16.21000 ? 35  GLU A HG2  1 
ATOM   668  H  HG3  . GLU A 1 35  ? -2.80000  -23.78600 -1.33800  1.000 16.21000 ? 35  GLU A HG3  1 
ATOM   669  N  N    . SER A 1 36  ? -4.96600  -21.63400 -5.39800  1.000 14.04000 ? 36  SER A N    1 
ATOM   670  C  CA   . SER A 1 36  ? -5.40700  -20.32900 -5.87400  1.000 14.39000 ? 36  SER A CA   1 
ATOM   671  C  C    . SER A 1 36  ? -5.34300  -20.15700 -7.38800  1.000 15.18000 ? 36  SER A C    1 
ATOM   672  O  O    . SER A 1 36  ? -5.68200  -19.06900 -7.88400  1.000 16.86000 ? 36  SER A O    1 
ATOM   673  C  CB   . SER A 1 36  ? -4.53700  -19.25200 -5.24500  1.000 14.87000 ? 36  SER A CB   1 
ATOM   674  O  OG   . SER A 1 36  ? -3.22400  -19.30400 -5.77300  1.000 15.25000 ? 36  SER A OG   1 
ATOM   675  H  H    . SER A 1 36  ? -4.23300  -21.90900 -5.75500  1.000 16.87000 ? 36  SER A H    1 
ATOM   676  H  HA   . SER A 1 36  ? -6.33200  -20.20600 -5.60800  1.000 17.29000 ? 36  SER A HA   1 
ATOM   677  H  HB2  . SER A 1 36  ? -4.92200  -18.38300 -5.43600  1.000 17.87000 ? 36  SER A HB2  1 
ATOM   678  H  HB3  . SER A 1 36  ? -4.49900  -19.39500 -4.28700  1.000 17.87000 ? 36  SER A HB3  1 
ATOM   679  H  HG   . SER A 1 36  ? -2.71900  -19.72000 -5.24700  1.000 18.33000 ? 36  SER A HG   1 
ATOM   680  N  N    . ASN A 1 37  ? -4.89900  -21.16900 -8.13900  1.000 14.29000 ? 37  ASN A N    1 
ATOM   681  C  CA   . ASN A 1 37  ? -4.59300  -21.01000 -9.56800  1.000 18.29000 ? 37  ASN A CA   1 
ATOM   682  C  C    . ASN A 1 37  ? -3.67000  -19.81700 -9.80300  1.000 14.61000 ? 37  ASN A C    1 
ATOM   683  O  O    . ASN A 1 37  ? -3.74800  -19.12800 -10.83000 1.000 18.08000 ? 37  ASN A O    1 
ATOM   684  C  CB   . ASN A 1 37  ? -5.85800  -20.89600 -10.40800 1.000 18.70000 ? 37  ASN A CB   1 
ATOM   685  C  CG   . ASN A 1 37  ? -5.67500  -21.42500 -11.79700 1.000 27.97000 ? 37  ASN A CG   1 
ATOM   686  O  OD1  . ASN A 1 37  ? -4.71000  -22.10700 -12.09300 1.000 27.49000 ? 37  ASN A OD1  1 
ATOM   687  N  ND2  . ASN A 1 37  ? -6.60200  -21.07500 -12.67600 1.000 37.57000 ? 37  ASN A ND2  1 
ATOM   688  H  H    . ASN A 1 37  ? -4.76600  -21.96600 -7.84300  1.000 17.18000 ? 37  ASN A H    1 
ATOM   689  H  HA   . ASN A 1 37  ? -4.12500  -21.80600 -9.86700  1.000 21.98000 ? 37  ASN A HA   1 
ATOM   690  H  HB2  . ASN A 1 37  ? -6.56700  -21.40400 -9.98300  1.000 22.47000 ? 37  ASN A HB2  1 
ATOM   691  H  HB3  . ASN A 1 37  ? -6.11200  -19.96200 -10.47300 1.000 22.47000 ? 37  ASN A HB3  1 
ATOM   692  H  HD21 . ASN A 1 37  ? -7.25600  -20.57300 -12.43400 1.000 45.11000 ? 37  ASN A HD21 1 
ATOM   693  H  HD22 . ASN A 1 37  ? -6.54800  -21.35000 -13.48900 1.000 45.11000 ? 37  ASN A HD22 1 
ATOM   694  N  N    . PHE A 1 38  ? -2.75400  -19.55500 -8.87200  1.000 14.36000 ? 38  PHE A N    1 
ATOM   695  C  CA   . PHE A 1 38  ? -1.72100  -18.53000 -8.96300  1.000 14.49000 ? 38  PHE A CA   1 
ATOM   696  C  C    . PHE A 1 38  ? -2.27800  -17.11200 -8.87900  1.000 14.09000 ? 38  PHE A C    1 
ATOM   697  O  O    . PHE A 1 38  ? -1.61200  -16.15400 -9.26800  1.000 16.91000 ? 38  PHE A O    1 
ATOM   698  C  CB   . PHE A 1 38  ? -0.84000  -18.63300 -10.22100 1.000 16.40000 ? 38  PHE A CB   1 
ATOM   699  C  CG   . PHE A 1 38  ? -0.11100  -19.95800 -10.41900 1.000 16.52000 ? 38  PHE A CG   1 
ATOM   700  C  CD1  . PHE A 1 38  ? 0.39400   -20.71000 -9.36400  1.000 17.18000 ? 38  PHE A CD1  1 
ATOM   701  C  CD2  . PHE A 1 38  ? 0.12400   -20.39100 -11.71700 1.000 19.29000 ? 38  PHE A CD2  1 
ATOM   702  C  CE1  . PHE A 1 38  ? 1.09800   -21.89200 -9.61500  1.000 18.17000 ? 38  PHE A CE1  1 
ATOM   703  C  CE2  . PHE A 1 38  ? 0.82600   -21.58000 -11.96300 1.000 20.56000 ? 38  PHE A CE2  1 
ATOM   704  C  CZ   . PHE A 1 38  ? 1.31200   -22.31200 -10.92300 1.000 17.59000 ? 38  PHE A CZ   1 
ATOM   705  H  H    . PHE A 1 38  ? -2.71000  -19.98800 -8.13100  1.000 17.26000 ? 38  PHE A H    1 
ATOM   706  H  HA   . PHE A 1 38  ? -1.14500  -18.68700 -8.19900  1.000 17.41000 ? 38  PHE A HA   1 
ATOM   707  H  HB2  . PHE A 1 38  ? -1.40400  -18.49700 -10.99800 1.000 19.70000 ? 38  PHE A HB2  1 
ATOM   708  H  HB3  . PHE A 1 38  ? -0.16500  -17.93800 -10.17500 1.000 19.70000 ? 38  PHE A HB3  1 
ATOM   709  H  HD1  . PHE A 1 38  ? 0.26300   -20.42600 -8.48800  1.000 20.64000 ? 38  PHE A HD1  1 
ATOM   710  H  HD2  . PHE A 1 38  ? -0.18700  -19.88600 -12.43300 1.000 23.17000 ? 38  PHE A HD2  1 
ATOM   711  H  HE1  . PHE A 1 38  ? 1.42400   -22.39800 -8.90600  1.000 21.83000 ? 38  PHE A HE1  1 
ATOM   712  H  HE2  . PHE A 1 38  ? 0.95900   -21.86800 -12.83700 1.000 24.70000 ? 38  PHE A HE2  1 
ATOM   713  H  HZ   . PHE A 1 38  ? 1.78700   -23.09400 -11.08800 1.000 21.13000 ? 38  PHE A HZ   1 
ATOM   714  N  N    . ASN A 1 39  ? -3.47400  -16.96500 -8.33200  1.000 14.50000 ? 39  ASN A N    1 
ATOM   715  C  CA   . ASN A 1 39  ? -4.14100  -15.66300 -8.22000  1.000 14.53000 ? 39  ASN A CA   1 
ATOM   716  C  C    . ASN A 1 39  ? -4.00500  -15.12900 -6.80300  1.000 12.79000 ? 39  ASN A C    1 
ATOM   717  O  O    . ASN A 1 39  ? -4.58000  -15.71500 -5.86200  1.000 15.73000 ? 39  ASN A O    1 
ATOM   718  C  CB   . ASN A 1 39  ? -5.60900  -15.82500 -8.57100  1.000 14.38000 ? 39  ASN A CB   1 
ATOM   719  C  CG   . ASN A 1 39  ? -6.39700  -14.53100 -8.55000  1.000 15.19000 ? 39  ASN A CG   1 
ATOM   720  O  OD1  . ASN A 1 39  ? -5.87900  -13.46300 -8.34600  1.000 16.42000 ? 39  ASN A OD1  1 
ATOM   721  N  ND2  . ASN A 1 39  ? -7.68200  -14.66300 -8.80500  1.000 21.29000 ? 39  ASN A ND2  1 
ATOM   722  H  H    . ASN A 1 39  ? -3.93500  -17.61500 -8.00800  1.000 17.43000 ? 39  ASN A H    1 
ATOM   723  H  HA   . ASN A 1 39  ? -3.72000  -15.02500 -8.81800  1.000 17.46000 ? 39  ASN A HA   1 
ATOM   724  H  HB2  . ASN A 1 39  ? -5.67600  -16.19500 -9.46500  1.000 17.28000 ? 39  ASN A HB2  1 
ATOM   725  H  HB3  . ASN A 1 39  ? -6.01700  -16.42900 -7.93100  1.000 17.28000 ? 39  ASN A HB3  1 
ATOM   726  H  HD21 . ASN A 1 39  ? -8.19200  -13.97100 -8.80900  1.000 25.57000 ? 39  ASN A HD21 1 
ATOM   727  H  HD22 . ASN A 1 39  ? -8.01100  -15.44100 -8.96600  1.000 25.57000 ? 39  ASN A HD22 1 
ATOM   728  N  N    . THR A 1 40  ? -3.32600  -13.99700 -6.63900  1.000 14.29000 ? 40  THR A N    1 
ATOM   729  C  CA   . THR A 1 40  ? -3.18000  -13.43600 -5.30100  1.000 15.98000 ? 40  THR A CA   1 
ATOM   730  C  C    . THR A 1 40  ? -4.50500  -12.98500 -4.68900  1.000 15.06000 ? 40  THR A C    1 
ATOM   731  O  O    . THR A 1 40  ? -4.57500  -12.87200 -3.46000  1.000 16.08000 ? 40  THR A O    1 
ATOM   732  C  CB   . THR A 1 40  ? -2.21300  -12.25900 -5.23500  1.000 16.43000 ? 40  THR A CB   1 
ATOM   733  O  OG1  . THR A 1 40  ? -2.77900  -11.15900 -5.96700  1.000 17.22000 ? 40  THR A OG1  1 
ATOM   734  C  CG2  . THR A 1 40  ? -0.82500  -12.61300 -5.82400  1.000 16.05000 ? 40  THR A CG2  1 
ATOM   735  H  H    . THR A 1 40  ? -2.95000  -13.54800 -7.26800  1.000 17.18000 ? 40  THR A H    1 
ATOM   736  H  HA   . THR A 1 40  ? -2.79600  -14.15300 -4.77200  1.000 19.20000 ? 40  THR A HA   1 
ATOM   737  H  HB   . THR A 1 40  ? -2.07200  -12.01400 -4.30700  1.000 19.73000 ? 40  THR A HB   1 
ATOM   738  H  HG1  . THR A 1 40  ? -2.33300  -10.46100 -5.82600  1.000 20.69000 ? 40  THR A HG1  1 
ATOM   739  H  HG21 . THR A 1 40  ? -0.23800  -11.84200 -5.77500  1.000 19.29000 ? 40  THR A HG21 1 
ATOM   740  H  HG22 . THR A 1 40  ? -0.42800  -13.34300 -5.32200  1.000 19.29000 ? 40  THR A HG22 1 
ATOM   741  H  HG23 . THR A 1 40  ? -0.91600  -12.88100 -6.75100  1.000 19.29000 ? 40  THR A HG23 1 
ATOM   742  N  N    A GLN A 1 41  ? -5.52900  -12.72700 -5.49500  0.480 14.03000 ? 41  GLN A N    1 
ATOM   743  N  N    B GLN A 1 41  ? -5.54500  -12.72500 -5.48700  0.520 14.05000 ? 41  GLN A N    1 
ATOM   744  C  CA   A GLN A 1 41  ? -6.77300  -12.20000 -4.95200  0.480 12.90000 ? 41  GLN A CA   1 
ATOM   745  C  CA   B GLN A 1 41  ? -6.80800  -12.21600 -4.94500  0.520 12.73000 ? 41  GLN A CA   1 
ATOM   746  C  C    A GLN A 1 41  ? -7.72000  -13.26800 -4.45500  0.480 13.19000 ? 41  GLN A C    1 
ATOM   747  C  C    B GLN A 1 41  ? -7.81200  -13.31000 -4.62900  0.520 15.47000 ? 41  GLN A C    1 
ATOM   748  O  O    A GLN A 1 41  ? -8.76800  -12.90600 -3.90600  0.480 13.11000 ? 41  GLN A O    1 
ATOM   749  O  O    B GLN A 1 41  ? -9.00200  -13.02500 -4.41000  0.520 17.01000 ? 41  GLN A O    1 
ATOM   750  C  CB   A GLN A 1 41  ? -7.49800  -11.32400 -5.97900  0.480 14.59000 ? 41  GLN A CB   1 
ATOM   751  C  CB   B GLN A 1 41  ? -7.43400  -11.20200 -5.90400  0.520 13.89000 ? 41  GLN A CB   1 
ATOM   752  C  CG   A GLN A 1 41  ? -6.74500  -10.07300 -6.29600  0.480 17.82000 ? 41  GLN A CG   1 
ATOM   753  C  CG   B GLN A 1 41  ? -6.55800  -10.02600 -6.22500  0.520 18.27000 ? 41  GLN A CG   1 
ATOM   754  C  CD   A GLN A 1 41  ? -7.59400  -9.02600  -6.97800  0.480 17.80000 ? 41  GLN A CD   1 
ATOM   755  C  CD   B GLN A 1 41  ? -7.33600  -8.92300  -6.89700  0.520 17.76000 ? 41  GLN A CD   1 
ATOM   756  O  OE1  A GLN A 1 41  ? -8.65800  -8.63100  -6.47500  0.480 15.32000 ? 41  GLN A OE1  1 
ATOM   757  O  OE1  B GLN A 1 41  ? -7.93400  -8.08200  -6.21600  0.520 16.92000 ? 41  GLN A OE1  1 
ATOM   758  N  NE2  A GLN A 1 41  ? -7.11200  -8.54300  -8.11800  0.480 17.02000 ? 41  GLN A NE2  1 
ATOM   759  N  NE2  B GLN A 1 41  ? -7.37200  -8.94200  -8.24000  0.520 16.51000 ? 41  GLN A NE2  1 
ATOM   760  H  H    A GLN A 1 41  ? -5.52600  -12.84700 -6.34700  0.480 16.86000 ? 41  GLN A H    1 
ATOM   761  H  H    B GLN A 1 41  ? -5.54200  -12.83400 -6.34000  0.520 16.89000 ? 41  GLN A H    1 
ATOM   762  H  HA   A GLN A 1 41  ? -6.53900  -11.63800 -4.19700  0.480 15.50000 ? 41  GLN A HA   1 
ATOM   763  H  HA   B GLN A 1 41  ? -6.60800  -11.75600 -4.11400  0.520 15.30000 ? 41  GLN A HA   1 
ATOM   764  H  HB2  A GLN A 1 41  ? -7.60800  -11.82600 -6.80200  0.480 17.54000 ? 41  GLN A HB2  1 
ATOM   765  H  HB2  B GLN A 1 41  ? -7.63900  -11.65100 -6.73900  0.520 16.69000 ? 41  GLN A HB2  1 
ATOM   766  H  HB3  A GLN A 1 41  ? -8.36500  -11.07200 -5.62500  0.480 17.54000 ? 41  GLN A HB3  1 
ATOM   767  H  HB3  B GLN A 1 41  ? -8.24800  -10.85900 -5.50300  0.520 16.69000 ? 41  GLN A HB3  1 
ATOM   768  H  HG2  A GLN A 1 41  ? -6.40700  -9.69100  -5.47100  0.480 21.40000 ? 41  GLN A HG2  1 
ATOM   769  H  HG2  B GLN A 1 41  ? -6.17800  -9.67600  -5.40500  0.520 21.95000 ? 41  GLN A HG2  1 
ATOM   770  H  HG3  A GLN A 1 41  ? -6.00700  -10.29000 -6.88700  0.480 21.40000 ? 41  GLN A HG3  1 
ATOM   771  H  HG3  B GLN A 1 41  ? -5.85000  -10.30900 -6.82500  0.520 21.95000 ? 41  GLN A HG3  1 
ATOM   772  H  HE21 A GLN A 1 41  ? -7.55100  -7.94500  -8.55200  0.480 20.45000 ? 41  GLN A HE21 1 
ATOM   773  H  HE21 B GLN A 1 41  ? -7.80400  -8.33300  -8.66700  0.520 19.84000 ? 41  GLN A HE21 1 
ATOM   774  H  HE22 A GLN A 1 41  ? -6.36000  -8.83000  -8.42200  0.480 20.45000 ? 41  GLN A HE22 1 
ATOM   775  H  HE22 B GLN A 1 41  ? -6.96400  -9.56400  -8.67200  0.520 19.84000 ? 41  GLN A HE22 1 
ATOM   776  N  N    . ALA A 1 42  ? -7.38300  -14.56100 -4.61900  1.000 13.83000 ? 42  ALA A N    1 
ATOM   777  C  CA   . ALA A 1 42  ? -8.29300  -15.65100 -4.30500  1.000 14.18000 ? 42  ALA A CA   1 
ATOM   778  C  C    . ALA A 1 42  ? -8.73600  -15.62000 -2.83800  1.000 12.37000 ? 42  ALA A C    1 
ATOM   779  O  O    . ALA A 1 42  ? -7.92100  -15.45000 -1.93700  1.000 14.62000 ? 42  ALA A O    1 
ATOM   780  C  CB   . ALA A 1 42  ? -7.60200  -16.97500 -4.57400  1.000 16.09000 ? 42  ALA A CB   1 
ATOM   781  H  H    . ALA A 1 42  ? -6.57500  -14.80200 -4.78900  1.000 16.62000 ? 42  ALA A H    1 
ATOM   782  H  HA   . ALA A 1 42  ? -9.08300  -15.56400 -4.86000  1.000 17.05000 ? 42  ALA A HA   1 
ATOM   783  H  HB1  . ALA A 1 42  ? -8.23500  -17.69600 -4.43600  1.000 19.33000 ? 42  ALA A HB1  1 
ATOM   784  H  HB2  . ALA A 1 42  ? -7.28500  -16.98500 -5.49100  1.000 19.33000 ? 42  ALA A HB2  1 
ATOM   785  H  HB3  . ALA A 1 42  ? -6.85300  -17.07100 -3.96500  1.000 19.33000 ? 42  ALA A HB3  1 
ATOM   786  N  N    . THR A 1 43  ? -10.03200 -15.81600 -2.62700  1.000 14.08000 ? 43  THR A N    1 
ATOM   787  C  CA   . THR A 1 43  ? -10.63300 -15.98500 -1.30300  1.000 14.26000 ? 43  THR A CA   1 
ATOM   788  C  C    . THR A 1 43  ? -11.63500 -17.11500 -1.34100  1.000 15.27000 ? 43  THR A C    1 
ATOM   789  O  O    . THR A 1 43  ? -12.31800 -17.32700 -2.34900  1.000 19.32000 ? 43  THR A O    1 
ATOM   790  C  CB   . THR A 1 43  ? -11.33600 -14.74200 -0.78800  1.000 16.18000 ? 43  THR A CB   1 
ATOM   791  O  OG1  . THR A 1 43  ? -12.41500 -14.41500 -1.68800  1.000 16.83000 ? 43  THR A OG1  1 
ATOM   792  C  CG2  . THR A 1 43  ? -10.35900 -13.56800 -0.66500  1.000 19.30000 ? 43  THR A CG2  1 
ATOM   793  H  H    . THR A 1 43  ? -10.61300 -15.85700 -3.26000  1.000 16.92000 ? 43  THR A H    1 
ATOM   794  H  HA   . THR A 1 43  ? -9.91600  -16.20000 -0.68600  1.000 17.14000 ? 43  THR A HA   1 
ATOM   795  H  HB   . THR A 1 43  ? -11.69400 -14.90300 0.09900   1.000 19.44000 ? 43  THR A HB   1 
ATOM   796  H  HG1  . THR A 1 43  ? -12.16200 -13.83600 -2.24200  1.000 20.22000 ? 43  THR A HG1  1 
ATOM   797  H  HG21 . THR A 1 43  ? -10.81300 -12.79600 -0.29200  1.000 23.18000 ? 43  THR A HG21 1 
ATOM   798  H  HG22 . THR A 1 43  ? -9.62100  -13.81000 -0.08400  1.000 23.18000 ? 43  THR A HG22 1 
ATOM   799  H  HG23 . THR A 1 43  ? -10.00800 -13.33500 -1.53800  1.000 23.18000 ? 43  THR A HG23 1 
ATOM   800  N  N    A ASN A 1 44  ? -11.76400 -17.84500 -0.22900  0.530 15.55000 ? 44  ASN A N    1 
ATOM   801  N  N    B ASN A 1 44  ? -11.75300 -17.84200 -0.23100  0.470 15.59000 ? 44  ASN A N    1 
ATOM   802  C  CA   A ASN A 1 44  ? -12.70500 -18.96000 -0.20000  0.530 17.08000 ? 44  ASN A CA   1 
ATOM   803  C  CA   B ASN A 1 44  ? -12.77800 -18.86900 -0.12700  0.470 17.53000 ? 44  ASN A CA   1 
ATOM   804  C  C    A ASN A 1 44  ? -13.17200 -19.21700 1.22000   0.530 14.68000 ? 44  ASN A C    1 
ATOM   805  C  C    B ASN A 1 44  ? -13.26100 -18.91400 1.31400   0.470 13.22000 ? 44  ASN A C    1 
ATOM   806  O  O    A ASN A 1 44  ? -12.34300 -19.39500 2.11400   0.530 15.10000 ? 44  ASN A O    1 
ATOM   807  O  O    B ASN A 1 44  ? -12.46800 -18.73500 2.22900   0.470 12.46000 ? 44  ASN A O    1 
ATOM   808  C  CB   A ASN A 1 44  ? -12.06900 -20.21700 -0.77800  0.530 19.37000 ? 44  ASN A CB   1 
ATOM   809  C  CB   B ASN A 1 44  ? -12.24500 -20.24000 -0.53900  0.470 18.80000 ? 44  ASN A CB   1 
ATOM   810  C  CG   A ASN A 1 44  ? -11.99300 -20.16700 -2.28300  0.530 16.75000 ? 44  ASN A CG   1 
ATOM   811  C  CG   B ASN A 1 44  ? -13.28800 -21.06900 -1.27600  0.470 27.18000 ? 44  ASN A CG   1 
ATOM   812  O  OD1  A ASN A 1 44  ? -13.02300 -20.21400 -2.98400  0.530 18.60000 ? 44  ASN A OD1  1 
ATOM   813  O  OD1  B ASN A 1 44  ? -14.08600 -21.76100 -0.65800  0.470 27.85000 ? 44  ASN A OD1  1 
ATOM   814  N  ND2  A ASN A 1 44  ? -10.78000 -20.00700 -2.79400  0.530 18.82000 ? 44  ASN A ND2  1 
ATOM   815  N  ND2  B ASN A 1 44  ? -13.30000 -20.97400 -2.60200  0.470 35.89000 ? 44  ASN A ND2  1 
ATOM   816  H  H    A ASN A 1 44  ? -11.32800 -17.71500 0.50100   0.530 18.68000 ? 44  ASN A H    1 
ATOM   817  H  H    B ASN A 1 44  ? -11.25500 -17.75800 0.46500   0.470 18.73000 ? 44  ASN A H    1 
ATOM   818  H  HA   A ASN A 1 44  ? -13.48500 -18.72400 -0.72500  0.530 20.52000 ? 44  ASN A HA   1 
ATOM   819  H  HA   B ASN A 1 44  ? -13.52400 -18.64900 -0.70700  0.470 21.06000 ? 44  ASN A HA   1 
ATOM   820  H  HB2  A ASN A 1 44  ? -11.16800 -20.30800 -0.43100  0.530 23.27000 ? 44  ASN A HB2  1 
ATOM   821  H  HB2  B ASN A 1 44  ? -11.48300 -20.12100 -1.12800  0.470 22.58000 ? 44  ASN A HB2  1 
ATOM   822  H  HB3  A ASN A 1 44  ? -12.60000 -20.98800 -0.52700  0.530 23.27000 ? 44  ASN A HB3  1 
ATOM   823  H  HB3  B ASN A 1 44  ? -11.97700 -20.72900 0.25500   0.470 22.58000 ? 44  ASN A HB3  1 
ATOM   824  H  HD21 A ASN A 1 44  ? -10.10000 -19.93900 -2.27300  0.530 22.61000 ? 44  ASN A HD21 1 
ATOM   825  H  HD21 B ASN A 1 44  ? -12.73600 -20.46200 -3.00100  0.470 43.10000 ? 44  ASN A HD21 1 
ATOM   826  H  HD22 A ASN A 1 44  ? -10.67400 -19.97100 -3.64700  0.530 22.61000 ? 44  ASN A HD22 1 
ATOM   827  H  HD22 B ASN A 1 44  ? -13.87200 -21.42400 -3.06000  0.470 43.10000 ? 44  ASN A HD22 1 
ATOM   828  N  N    A ARG A 1 45  ? -14.49400 -19.23800 1.39700   0.530 18.83000 ? 45  ARG A N    1 
ATOM   829  N  N    B ARG A 1 45  ? -14.55300 -19.16400 1.50100   0.470 18.52000 ? 45  ARG A N    1 
ATOM   830  C  CA   A ARG A 1 45  ? -15.11000 -19.42600 2.70000   0.530 20.04000 ? 45  ARG A CA   1 
ATOM   831  C  CA   B ARG A 1 45  ? -15.15000 -19.27000 2.82700   0.470 19.40000 ? 45  ARG A CA   1 
ATOM   832  C  C    A ARG A 1 45  ? -15.01000 -20.87500 3.12200   0.530 20.66000 ? 45  ARG A C    1 
ATOM   833  C  C    B ARG A 1 45  ? -15.28900 -20.73900 3.20800   0.470 19.63000 ? 45  ARG A C    1 
ATOM   834  O  O    A ARG A 1 45  ? -15.08900 -21.79900 2.30100   0.530 21.64000 ? 45  ARG A O    1 
ATOM   835  O  O    B ARG A 1 45  ? -15.85000 -21.53600 2.44400   0.470 16.65000 ? 45  ARG A O    1 
ATOM   836  C  CB   A ARG A 1 45  ? -16.59000 -19.03800 2.65700   0.530 19.89000 ? 45  ARG A CB   1 
ATOM   837  C  CB   B ARG A 1 45  ? -16.52200 -18.59000 2.85200   0.470 20.96000 ? 45  ARG A CB   1 
ATOM   838  C  CG   A ARG A 1 45  ? -17.28200 -19.17800 4.01800   0.530 19.56000 ? 45  ARG A CG   1 
ATOM   839  C  CG   B ARG A 1 45  ? -17.13400 -18.49800 4.25400   0.470 21.39000 ? 45  ARG A CG   1 
ATOM   840  C  CD   A ARG A 1 45  ? -16.78300 -18.09400 4.94800   0.530 23.66000 ? 45  ARG A CD   1 
ATOM   841  C  CD   B ARG A 1 45  ? -16.63400 -17.28400 5.01800   0.470 25.96000 ? 45  ARG A CD   1 
ATOM   842  N  NE   A ARG A 1 45  ? -17.08900 -16.78100 4.40200   0.530 32.70000 ? 45  ARG A NE   1 
ATOM   843  N  NE   B ARG A 1 45  ? -16.84000 -16.06200 4.25600   0.470 33.09000 ? 45  ARG A NE   1 
ATOM   844  C  CZ   A ARG A 1 45  ? -17.91300 -15.89600 4.95100   0.530 40.32000 ? 45  ARG A CZ   1 
ATOM   845  C  CZ   B ARG A 1 45  ? -18.03200 -15.60600 3.89800   0.470 25.03000 ? 45  ARG A CZ   1 
ATOM   846  N  NH1  A ARG A 1 45  ? -18.36000 -16.03400 6.19100   0.530 34.63000 ? 45  ARG A NH1  1 
ATOM   847  N  NH1  B ARG A 1 45  ? -19.14900 -16.20000 4.29200   0.470 40.66000 ? 45  ARG A NH1  1 
ATOM   848  N  NH2  A ARG A 1 45  ? -18.27300 -14.82600 4.24700   0.530 33.25000 ? 45  ARG A NH2  1 
ATOM   849  N  NH2  B ARG A 1 45  ? -18.10800 -14.53200 3.12300   0.470 31.68000 ? 45  ARG A NH2  1 
ATOM   850  H  H    A ARG A 1 45  ? -15.06500 -19.14200 0.76100   0.530 22.62000 ? 45  ARG A H    1 
ATOM   851  H  H    B ARG A 1 45  ? -15.11500 -19.27900 0.86100   0.470 22.25000 ? 45  ARG A H    1 
ATOM   852  H  HA   A ARG A 1 45  ? -14.65200 -18.86600 3.34600   0.530 24.07000 ? 45  ARG A HA   1 
ATOM   853  H  HA   B ARG A 1 45  ? -14.57700 -18.83700 3.47900   0.470 23.30000 ? 45  ARG A HA   1 
ATOM   854  H  HB2  A ARG A 1 45  ? -16.66600 -18.11300 2.37500   0.530 23.90000 ? 45  ARG A HB2  1 
ATOM   855  H  HB2  B ARG A 1 45  ? -16.43100 -17.68800 2.50800   0.470 25.17000 ? 45  ARG A HB2  1 
ATOM   856  H  HB3  A ARG A 1 45  ? -17.04900 -19.61600 2.02700   0.530 23.90000 ? 45  ARG A HB3  1 
ATOM   857  H  HB3  B ARG A 1 45  ? -17.13300 -19.09700 2.29400   0.470 25.17000 ? 45  ARG A HB3  1 
ATOM   858  H  HG2  A ARG A 1 45  ? -18.24100 -19.08200 3.91100   0.530 23.50000 ? 45  ARG A HG2  1 
ATOM   859  H  HG2  B ARG A 1 45  ? -18.09800 -18.43100 4.17800   0.470 25.70000 ? 45  ARG A HG2  1 
ATOM   860  H  HG3  A ARG A 1 45  ? -17.07500 -20.04300 4.40500   0.530 23.50000 ? 45  ARG A HG3  1 
ATOM   861  H  HG3  B ARG A 1 45  ? -16.89600 -19.29100 4.75900   0.470 25.70000 ? 45  ARG A HG3  1 
ATOM   862  H  HD2  A ARG A 1 45  ? -17.21700 -18.18000 5.81100   0.530 28.41000 ? 45  ARG A HD2  1 
ATOM   863  H  HD2  B ARG A 1 45  ? -17.11800 -17.20800 5.85500   0.470 31.17000 ? 45  ARG A HD2  1 
ATOM   864  H  HD3  A ARG A 1 45  ? -15.82100 -18.17000 5.05100   0.530 28.41000 ? 45  ARG A HD3  1 
ATOM   865  H  HD3  B ARG A 1 45  ? -15.68400 -17.38100 5.19100   0.470 31.17000 ? 45  ARG A HD3  1 
ATOM   866  H  HE   A ARG A 1 45  ? -16.70500 -16.55900 3.66500   0.530 39.27000 ? 45  ARG A HE   1 
ATOM   867  H  HE   B ARG A 1 45  ? -16.14700 -15.60800 4.02500   0.470 39.73000 ? 45  ARG A HE   1 
ATOM   868  H  HH11 A ARG A 1 45  ? -18.11600 -16.71100 6.66200   0.530 41.58000 ? 45  ARG A HH11 1 
ATOM   869  H  HH11 B ARG A 1 45  ? -19.11200 -16.89800 4.79200   0.470 48.81000 ? 45  ARG A HH11 1 
ATOM   870  H  HH12 A ARG A 1 45  ? -18.89300 -15.44800 6.52400   0.530 41.58000 ? 45  ARG A HH12 1 
ATOM   871  H  HH12 B ARG A 1 45  ? -19.91200 -15.88700 4.04700   0.470 48.81000 ? 45  ARG A HH12 1 
ATOM   872  H  HH21 A ARG A 1 45  ? -17.97300 -14.71500 3.44900   0.530 39.93000 ? 45  ARG A HH21 1 
ATOM   873  H  HH21 B ARG A 1 45  ? -17.38800 -14.14100 2.85900   0.470 38.04000 ? 45  ARG A HH21 1 
ATOM   874  H  HH22 A ARG A 1 45  ? -18.80700 -14.24500 4.59000   0.530 39.93000 ? 45  ARG A HH22 1 
ATOM   875  H  HH22 B ARG A 1 45  ? -18.87500 -14.22700 2.88400   0.470 38.04000 ? 45  ARG A HH22 1 
ATOM   876  N  N    . ASN A 1 46  ? -14.83400 -21.06600 4.41900   1.000 21.18000 ? 46  ASN A N    1 
ATOM   877  C  CA   . ASN A 1 46  ? -14.85200 -22.40800 4.99600   1.000 26.22000 ? 46  ASN A CA   1 
ATOM   878  C  C    . ASN A 1 46  ? -16.16000 -22.61700 5.76300   1.000 20.55000 ? 46  ASN A C    1 
ATOM   879  O  O    . ASN A 1 46  ? -16.83700 -21.67500 6.16900   1.000 26.27000 ? 46  ASN A O    1 
ATOM   880  C  CB   . ASN A 1 46  ? -13.65800 -22.62000 5.94000   1.000 25.33000 ? 46  ASN A CB   1 
ATOM   881  C  CG   . ASN A 1 46  ? -12.30000 -22.38200 5.26300   1.000 23.40000 ? 46  ASN A CG   1 
ATOM   882  O  OD1  . ASN A 1 46  ? -11.44300 -21.66000 5.78300   1.000 27.56000 ? 46  ASN A OD1  1 
ATOM   883  N  ND2  . ASN A 1 46  ? -12.09100 -23.01800 4.13000   1.000 29.95000 ? 46  ASN A ND2  1 
ATOM   884  H  H    . ASN A 1 46  ? -14.70200 -20.43500 4.98800   1.000 25.44000 ? 46  ASN A H    1 
ATOM   885  H  HA   . ASN A 1 46  ? -14.79000 -23.06600 4.28600   1.000 31.49000 ? 46  ASN A HA   1 
ATOM   886  H  HB2  . ASN A 1 46  ? -13.73300 -22.00200 6.68400   1.000 30.41000 ? 46  ASN A HB2  1 
ATOM   887  H  HB3  . ASN A 1 46  ? -13.67300 -23.53400 6.26400   1.000 30.41000 ? 46  ASN A HB3  1 
ATOM   888  H  HD21 . ASN A 1 46  ? -11.34600 -22.91900 3.71200   1.000 35.96000 ? 46  ASN A HD21 1 
ATOM   889  H  HD22 . ASN A 1 46  ? -12.69900 -23.53400 3.80800   1.000 35.96000 ? 46  ASN A HD22 1 
ATOM   890  N  N    . THR A 1 47  ? -16.48000 -23.89300 5.98800   1.000 33.72000 ? 47  THR A N    1 
ATOM   891  C  CA   . THR A 1 47  ? -17.74600 -24.23100 6.62700   1.000 37.01000 ? 47  THR A CA   1 
ATOM   892  C  C    . THR A 1 47  ? -17.83600 -23.66300 8.04000   1.000 32.69000 ? 47  THR A C    1 
ATOM   893  O  O    . THR A 1 47  ? -18.93400 -23.32800 8.50400   1.000 39.59000 ? 47  THR A O    1 
ATOM   894  C  CB   . THR A 1 47  ? -17.93900 -25.75300 6.62100   1.000 42.96000 ? 47  THR A CB   1 
ATOM   895  O  OG1  . THR A 1 47  ? -17.06000 -26.35500 7.57600   1.000 50.20000 ? 47  THR A OG1  1 
ATOM   896  C  CG2  . THR A 1 47  ? -17.64200 -26.34300 5.23700   1.000 42.19000 ? 47  THR A CG2  1 
ATOM   897  H  H    . THR A 1 47  ? -15.98900 -24.56900 5.78300   1.000 40.49000 ? 47  THR A H    1 
ATOM   898  H  HA   . THR A 1 47  ? -18.47500 -23.84100 6.11800   1.000 44.44000 ? 47  THR A HA   1 
ATOM   899  H  HB   . THR A 1 47  ? -18.86100 -25.95200 6.84900   1.000 51.58000 ? 47  THR A HB   1 
ATOM   900  H  HG1  . THR A 1 47  ? -17.16500 -27.18900 7.57700   1.000 60.26000 ? 47  THR A HG1  1 
ATOM   901  H  HG21 . THR A 1 47  ? -17.81700 -27.29700 5.23900   1.000 50.66000 ? 47  THR A HG21 1 
ATOM   902  H  HG22 . THR A 1 47  ? -18.20500 -25.92100 4.56900   1.000 50.66000 ? 47  THR A HG22 1 
ATOM   903  H  HG23 . THR A 1 47  ? -16.71200 -26.19300 5.00500   1.000 50.66000 ? 47  THR A HG23 1 
ATOM   904  N  N    A ASP A 1 48  ? -16.70100 -23.52300 8.72500   0.680 31.52000 ? 48  ASP A N    1 
ATOM   905  N  N    B ASP A 1 48  ? -16.70500 -23.52900 8.73000   0.320 31.44000 ? 48  ASP A N    1 
ATOM   906  C  CA   A ASP A 1 48  ? -16.66800 -23.02600 10.09800  0.680 29.96000 ? 48  ASP A CA   1 
ATOM   907  C  CA   B ASP A 1 48  ? -16.69100 -23.03100 10.10100  0.320 29.93000 ? 48  ASP A CA   1 
ATOM   908  C  C    A ASP A 1 48  ? -16.73700 -21.51300 10.19200  0.680 30.44000 ? 48  ASP A C    1 
ATOM   909  C  C    B ASP A 1 48  ? -16.75800 -21.51400 10.19300  0.320 30.37000 ? 48  ASP A C    1 
ATOM   910  O  O    A ASP A 1 48  ? -16.61000 -20.96500 11.29400  0.680 34.32000 ? 48  ASP A O    1 
ATOM   911  O  O    B ASP A 1 48  ? -16.64900 -20.97200 11.29800  0.320 34.10000 ? 48  ASP A O    1 
ATOM   912  C  CB   A ASP A 1 48  ? -15.42400 -23.55600 10.82700  0.680 24.73000 ? 48  ASP A CB   1 
ATOM   913  C  CB   B ASP A 1 48  ? -15.44200 -23.52800 10.83700  0.320 24.91000 ? 48  ASP A CB   1 
ATOM   914  C  CG   A ASP A 1 48  ? -14.12800 -22.89800 10.37300  0.680 28.28000 ? 48  ASP A CG   1 
ATOM   915  C  CG   B ASP A 1 48  ? -14.15800 -22.98100 10.24700  0.320 28.30000 ? 48  ASP A CG   1 
ATOM   916  O  OD1  A ASP A 1 48  ? -14.13900 -22.16600 9.36100   0.680 23.94000 ? 48  ASP A OD1  1 
ATOM   917  O  OD1  B ASP A 1 48  ? -13.69000 -23.53800 9.23300   0.320 31.40000 ? 48  ASP A OD1  1 
ATOM   918  O  OD2  A ASP A 1 48  ? -13.08700 -23.11700 11.04000  0.680 27.44000 ? 48  ASP A OD2  1 
ATOM   919  O  OD2  B ASP A 1 48  ? -13.62200 -21.99000 10.79300  0.320 29.69000 ? 48  ASP A OD2  1 
ATOM   920  H  H    A ASP A 1 48  ? -15.92400 -23.71200 8.40900   0.680 37.85000 ? 48  ASP A H    1 
ATOM   921  H  H    B ASP A 1 48  ? -15.92600 -23.72100 8.42100   0.320 37.75000 ? 48  ASP A H    1 
ATOM   922  H  HA   A ASP A 1 48  ? -17.44500 -23.37400 10.56300  0.680 35.98000 ? 48  ASP A HA   1 
ATOM   923  H  HA   B ASP A 1 48  ? -17.47100 -23.39100 10.55200  0.320 35.95000 ? 48  ASP A HA   1 
ATOM   924  H  HB2  A ASP A 1 48  ? -15.52400 -23.39000 11.77800  0.680 29.70000 ? 48  ASP A HB2  1 
ATOM   925  H  HB2  B ASP A 1 48  ? -15.48900 -23.24700 11.76400  0.320 29.92000 ? 48  ASP A HB2  1 
ATOM   926  H  HB3  A ASP A 1 48  ? -15.34600 -24.50900 10.66300  0.680 29.70000 ? 48  ASP A HB3  1 
ATOM   927  H  HB3  B ASP A 1 48  ? -15.40800 -24.49500 10.78400  0.320 29.92000 ? 48  ASP A HB3  1 
ATOM   928  N  N    . GLY A 1 49  ? -16.92600 -20.80800 9.07400   1.000 28.55000 ? 49  GLY A N    1 
ATOM   929  C  CA   . GLY A 1 49  ? -16.98600 -19.37100 9.09800   1.000 26.67000 ? 49  GLY A CA   1 
ATOM   930  C  C    . GLY A 1 49  ? -15.66900 -18.66200 8.85500   1.000 24.35000 ? 49  GLY A C    1 
ATOM   931  O  O    . GLY A 1 49  ? -15.66300 -17.43600 8.68100   1.000 24.94000 ? 49  GLY A O    1 
ATOM   932  H  H    . GLY A 1 49  ? -17.02000 -21.15200 8.29200   1.000 34.28000 ? 49  GLY A H    1 
ATOM   933  H  HA2  . GLY A 1 49  ? -17.60900 -19.07700 8.41500   1.000 32.03000 ? 49  GLY A HA2  1 
ATOM   934  H  HA3  . GLY A 1 49  ? -17.31500 -19.09100 9.96700   1.000 32.03000 ? 49  GLY A HA3  1 
ATOM   935  N  N    . SER A 1 50  ? -14.55300 -19.38200 8.85400   1.000 19.42000 ? 50  SER A N    1 
ATOM   936  C  CA   . SER A 1 50  ? -13.28100 -18.76800 8.53800   1.000 18.63000 ? 50  SER A CA   1 
ATOM   937  C  C    . SER A 1 50  ? -13.14500 -18.64700 7.01800   1.000 15.50000 ? 50  SER A C    1 
ATOM   938  O  O    . SER A 1 50  ? -13.95300 -19.17300 6.25700   1.000 18.55000 ? 50  SER A O    1 
ATOM   939  C  CB   . SER A 1 50  ? -12.13300 -19.56900 9.14400   1.000 17.00000 ? 50  SER A CB   1 
ATOM   940  O  OG   . SER A 1 50  ? -12.01500 -20.81100 8.52400   1.000 18.16000 ? 50  SER A OG   1 
ATOM   941  H  H    . SER A 1 50  ? -14.51100 -20.22300 9.03300   1.000 23.32000 ? 50  SER A H    1 
ATOM   942  H  HA   . SER A 1 50  ? -13.23200 -17.87800 8.91900   1.000 22.38000 ? 50  SER A HA   1 
ATOM   943  H  HB2  . SER A 1 50  ? -11.30700 -19.07600 9.02500   1.000 20.42000 ? 50  SER A HB2  1 
ATOM   944  H  HB3  . SER A 1 50  ? -12.30600 -19.70200 10.08900  1.000 20.42000 ? 50  SER A HB3  1 
ATOM   945  H  HG   . SER A 1 50  ? -12.77300 -21.16400 8.44000   1.000 21.81000 ? 50  SER A HG   1 
ATOM   946  N  N    . THR A 1 51  ? -12.15100 -17.87700 6.60700   1.000 14.53000 ? 51  THR A N    1 
ATOM   947  C  CA   . THR A 1 51  ? -11.90700 -17.59900 5.18800   1.000 13.35000 ? 51  THR A CA   1 
ATOM   948  C  C    . THR A 1 51  ? -10.42700 -17.83400 4.89900   1.000 13.36000 ? 51  THR A C    1 
ATOM   949  O  O    . THR A 1 51  ? -9.56500  -17.55300 5.73700   1.000 13.96000 ? 51  THR A O    1 
ATOM   950  C  CB   . THR A 1 51  ? -12.30700 -16.16600 4.86400   1.000 14.44000 ? 51  THR A CB   1 
ATOM   951  O  OG1  . THR A 1 51  ? -13.69100 -15.99500 5.16800   1.000 16.95000 ? 51  THR A OG1  1 
ATOM   952  C  CG2  . THR A 1 51  ? -12.10700 -15.82200 3.38200   1.000 16.62000 ? 51  THR A CG2  1 
ATOM   953  H  H    . THR A 1 51  ? -11.59000 -17.49500 7.13500   1.000 17.46000 ? 51  THR A H    1 
ATOM   954  H  HA   . THR A 1 51  ? -12.42000 -18.19100 4.61500   1.000 16.05000 ? 51  THR A HA   1 
ATOM   955  H  HB   . THR A 1 51  ? -11.74700 -15.57000 5.38600   1.000 17.35000 ? 51  THR A HB   1 
ATOM   956  H  HG1  . THR A 1 51  ? -13.78300 -15.42400 5.77700   1.000 20.36000 ? 51  THR A HG1  1 
ATOM   957  H  HG21 . THR A 1 51  ? -12.49400 -14.95300 3.18800   1.000 19.97000 ? 51  THR A HG21 1 
ATOM   958  H  HG22 . THR A 1 51  ? -11.16100 -15.79900 3.17100   1.000 19.97000 ? 51  THR A HG22 1 
ATOM   959  H  HG23 . THR A 1 51  ? -12.53800 -16.48900 2.82600   1.000 19.97000 ? 51  THR A HG23 1 
ATOM   960  N  N    A ASP A 1 52  ? -10.12700 -18.35800 3.70400   0.580 13.47000 ? 52  ASP A N    1 
ATOM   961  N  N    B ASP A 1 52  ? -10.14400 -18.35300 3.69900   0.420 13.61000 ? 52  ASP A N    1 
ATOM   962  C  CA   A ASP A 1 52  ? -8.76800  -18.55200 3.22100   0.580 13.29000 ? 52  ASP A CA   1 
ATOM   963  C  CA   B ASP A 1 52  ? -8.79800  -18.55000 3.18300   0.420 13.20000 ? 52  ASP A CA   1 
ATOM   964  C  C    A ASP A 1 52  ? -8.42700  -17.47000 2.21600   0.580 12.14000 ? 52  ASP A C    1 
ATOM   965  C  C    B ASP A 1 52  ? -8.44900  -17.40700 2.24200   0.420 12.24000 ? 52  ASP A C    1 
ATOM   966  O  O    A ASP A 1 52  ? -9.24400  -17.15900 1.34000   0.580 13.47000 ? 52  ASP A O    1 
ATOM   967  O  O    B ASP A 1 52  ? -9.28800  -16.96300 1.45000   0.420 14.37000 ? 52  ASP A O    1 
ATOM   968  C  CB   A ASP A 1 52  ? -8.65600  -19.90600 2.53300   0.580 14.41000 ? 52  ASP A CB   1 
ATOM   969  C  CB   B ASP A 1 52  ? -8.74400  -19.85900 2.39900   0.420 14.81000 ? 52  ASP A CB   1 
ATOM   970  C  CG   A ASP A 1 52  ? -9.31500  -21.00200 3.31200   0.580 16.02000 ? 52  ASP A CG   1 
ATOM   971  C  CG   B ASP A 1 52  ? -8.64000  -21.09000 3.28800   0.420 16.88000 ? 52  ASP A CG   1 
ATOM   972  O  OD1  A ASP A 1 52  ? -8.99600  -21.11800 4.50100   0.580 15.94000 ? 52  ASP A OD1  1 
ATOM   973  O  OD1  B ASP A 1 52  ? -8.21200  -20.99800 4.45900   0.420 15.50000 ? 52  ASP A OD1  1 
ATOM   974  O  OD2  A ASP A 1 52  ? -10.15700 -21.72300 2.74400   0.580 25.55000 ? 52  ASP A OD2  1 
ATOM   975  O  OD2  B ASP A 1 52  ? -9.00800  -22.17600 2.80400   0.420 19.68000 ? 52  ASP A OD2  1 
ATOM   976  H  H    A ASP A 1 52  ? -10.72100 -18.61700 3.13900   0.580 16.19000 ? 52  ASP A H    1 
ATOM   977  H  H    B ASP A 1 52  ? -10.74900 -18.60900 3.14400   0.420 16.35000 ? 52  ASP A H    1 
ATOM   978  H  HA   A ASP A 1 52  ? -8.14200  -18.50600 3.96100   0.580 15.97000 ? 52  ASP A HA   1 
ATOM   979  H  HA   B ASP A 1 52  ? -8.15600  -18.57400 3.90900   0.420 15.87000 ? 52  ASP A HA   1 
ATOM   980  H  HB2  A ASP A 1 52  ? -9.08400  -19.85600 1.66400   0.580 17.32000 ? 52  ASP A HB2  1 
ATOM   981  H  HB2  B ASP A 1 52  ? -9.55300  -19.94200 1.86900   0.420 17.80000 ? 52  ASP A HB2  1 
ATOM   982  H  HB3  A ASP A 1 52  ? -7.71900  -20.13300 2.43000   0.580 17.32000 ? 52  ASP A HB3  1 
ATOM   983  H  HB3  B ASP A 1 52  ? -7.96700  -19.84500 1.81800   0.420 17.80000 ? 52  ASP A HB3  1 
ATOM   984  N  N    . TYR A 1 53  ? -7.21300  -16.93300 2.32300   1.000 12.47000 ? 53  TYR A N    1 
ATOM   985  C  CA   . TYR A 1 53  ? -6.79200  -15.75400 1.57900   1.000 11.95000 ? 53  TYR A CA   1 
ATOM   986  C  C    . TYR A 1 53  ? -5.49400  -15.96100 0.81200   1.000 13.58000 ? 53  TYR A C    1 
ATOM   987  O  O    . TYR A 1 53  ? -4.49400  -16.41500 1.36000   1.000 13.24000 ? 53  TYR A O    1 
ATOM   988  C  CB   . TYR A 1 53  ? -6.58100  -14.58700 2.55100   1.000 13.15000 ? 53  TYR A CB   1 
ATOM   989  C  CG   . TYR A 1 53  ? -7.82100  -14.13000 3.26300   1.000 13.06000 ? 53  TYR A CG   1 
ATOM   990  C  CD1  . TYR A 1 53  ? -8.21800  -14.69700 4.47100   1.000 14.10000 ? 53  TYR A CD1  1 
ATOM   991  C  CD2  . TYR A 1 53  ? -8.60200  -13.11100 2.74700   1.000 14.72000 ? 53  TYR A CD2  1 
ATOM   992  C  CE1  . TYR A 1 53  ? -9.35200  -14.26100 5.10800   1.000 12.88000 ? 53  TYR A CE1  1 
ATOM   993  C  CE2  . TYR A 1 53  ? -9.74400  -12.68000 3.40200   1.000 15.61000 ? 53  TYR A CE2  1 
ATOM   994  C  CZ   . TYR A 1 53  ? -10.10300 -13.27200 4.57000   1.000 13.62000 ? 53  TYR A CZ   1 
ATOM   995  O  OH   . TYR A 1 53  ? -11.23400 -12.82200 5.23900   1.000 15.74000 ? 53  TYR A OH   1 
ATOM   996  H  H    . TYR A 1 53  ? -6.59700  -17.24300 2.83600   1.000 14.99000 ? 53  TYR A H    1 
ATOM   997  H  HA   . TYR A 1 53  ? -7.47800  -15.57100 0.91900   1.000 14.37000 ? 53  TYR A HA   1 
ATOM   998  H  HB2  . TYR A 1 53  ? -5.94100  -14.86000 3.22700   1.000 15.81000 ? 53  TYR A HB2  1 
ATOM   999  H  HB3  . TYR A 1 53  ? -6.23400  -13.83000 2.05300   1.000 15.81000 ? 53  TYR A HB3  1 
ATOM   1000 H  HD1  . TYR A 1 53  ? -7.70900  -15.37700 4.85000   1.000 16.95000 ? 53  TYR A HD1  1 
ATOM   1001 H  HD2  . TYR A 1 53  ? -8.35500  -12.70800 1.94500   1.000 17.69000 ? 53  TYR A HD2  1 
ATOM   1002 H  HE1  . TYR A 1 53  ? -9.60600  -14.64700 5.91400   1.000 15.48000 ? 53  TYR A HE1  1 
ATOM   1003 H  HE2  . TYR A 1 53  ? -10.25900 -11.99200 3.04600   1.000 18.75000 ? 53  TYR A HE2  1 
ATOM   1004 H  HH   . TYR A 1 53  ? -11.72500 -13.47200 5.44200   1.000 18.92000 ? 53  TYR A HH   1 
ATOM   1005 N  N    . GLY A 1 54  ? -5.50800  -15.52000 -0.44200  1.000 13.38000 ? 54  GLY A N    1 
ATOM   1006 C  CA   . GLY A 1 54  ? -4.31600  -15.29800 -1.22000  1.000 14.04000 ? 54  GLY A CA   1 
ATOM   1007 C  C    . GLY A 1 54  ? -3.79800  -16.53700 -1.91400  1.000 13.27000 ? 54  GLY A C    1 
ATOM   1008 O  O    . GLY A 1 54  ? -4.42700  -17.58100 -1.99500  1.000 14.21000 ? 54  GLY A O    1 
ATOM   1009 H  H    . GLY A 1 54  ? -6.22900  -15.33600 -0.87500  1.000 16.08000 ? 54  GLY A H    1 
ATOM   1010 H  HA2  . GLY A 1 54  ? -4.50200  -14.63000 -1.89800  1.000 16.87000 ? 54  GLY A HA2  1 
ATOM   1011 H  HA3  . GLY A 1 54  ? -3.61600  -14.96700 -0.63600  1.000 16.87000 ? 54  GLY A HA3  1 
ATOM   1012 N  N    . ILE A 1 55  ? -2.56400  -16.38200 -2.39400  1.000 14.76000 ? 55  ILE A N    1 
ATOM   1013 C  CA   . ILE A 1 55  ? -1.96300  -17.36500 -3.28000  1.000 14.48000 ? 55  ILE A CA   1 
ATOM   1014 C  C    . ILE A 1 55  ? -1.79300  -18.72300 -2.62000  1.000 13.51000 ? 55  ILE A C    1 
ATOM   1015 O  O    . ILE A 1 55  ? -1.83200  -19.75900 -3.30300  1.000 15.73000 ? 55  ILE A O    1 
ATOM   1016 C  CB   . ILE A 1 55  ? -0.64700  -16.78000 -3.82800  1.000 20.13000 ? 55  ILE A CB   1 
ATOM   1017 C  CG1  . ILE A 1 55  ? -0.24100  -17.50600 -5.10900  1.000 28.06000 ? 55  ILE A CG1  1 
ATOM   1018 C  CG2  . ILE A 1 55  ? 0.45500   -16.77300 -2.78700  1.000 19.69000 ? 55  ILE A CG2  1 
ATOM   1019 C  CD1  . ILE A 1 55  ? 0.28500   -16.62400 -6.17100  1.000 31.78000 ? 55  ILE A CD1  1 
ATOM   1020 H  H    . ILE A 1 55  ? -2.05400  -15.71200 -2.22000  1.000 17.74000 ? 55  ILE A H    1 
ATOM   1021 H  HA   . ILE A 1 55  ? -2.56100  -17.53300 -4.02400  1.000 17.39000 ? 55  ILE A HA   1 
ATOM   1022 H  HB   . ILE A 1 55  ? -0.80200  -15.84800 -4.05200  1.000 24.18000 ? 55  ILE A HB   1 
ATOM   1023 H  HG12 . ILE A 1 55  ? 0.45100   -18.15100 -4.89400  1.000 33.69000 ? 55  ILE A HG12 1 
ATOM   1024 H  HG13 . ILE A 1 55  ? -1.02000  -17.96200 -5.46600  1.000 33.69000 ? 55  ILE A HG13 1 
ATOM   1025 H  HG21 . ILE A 1 55  ? 1.25700   -16.39300 -3.17900  1.000 23.66000 ? 55  ILE A HG21 1 
ATOM   1026 H  HG22 . ILE A 1 55  ? 0.17200   -16.23700 -2.03000  1.000 23.66000 ? 55  ILE A HG22 1 
ATOM   1027 H  HG23 . ILE A 1 55  ? 0.62600   -17.68400 -2.50200  1.000 23.66000 ? 55  ILE A HG23 1 
ATOM   1028 H  HD11 . ILE A 1 55  ? 0.54400   -17.16500 -6.93300  1.000 38.16000 ? 55  ILE A HD11 1 
ATOM   1029 H  HD12 . ILE A 1 55  ? -0.40700  -15.99500 -6.43200  1.000 38.16000 ? 55  ILE A HD12 1 
ATOM   1030 H  HD13 . ILE A 1 55  ? 1.05600   -16.14400 -5.83000  1.000 38.16000 ? 55  ILE A HD13 1 
ATOM   1031 N  N    . LEU A 1 56  ? -1.60200  -18.76400 -1.29200  1.000 13.93000 ? 56  LEU A N    1 
ATOM   1032 C  CA   . LEU A 1 56  ? -1.47200  -19.99900 -0.54600  1.000 14.62000 ? 56  LEU A CA   1 
ATOM   1033 C  C    . LEU A 1 56  ? -2.65700  -20.24000 0.38800   1.000 15.84000 ? 56  LEU A C    1 
ATOM   1034 O  O    . LEU A 1 56  ? -2.61400  -21.12800 1.23700   1.000 15.86000 ? 56  LEU A O    1 
ATOM   1035 C  CB   . LEU A 1 56  ? -0.15200  -20.05000 0.20900   1.000 15.75000 ? 56  LEU A CB   1 
ATOM   1036 C  CG   . LEU A 1 56  ? 1.07200   -20.26300 -0.68400  1.000 18.33000 ? 56  LEU A CG   1 
ATOM   1037 C  CD1  . LEU A 1 56  ? 2.35600   -19.95800 0.10500   1.000 23.27000 ? 56  LEU A CD1  1 
ATOM   1038 C  CD2  . LEU A 1 56  ? 1.05300   -21.69800 -1.18500  1.000 25.14000 ? 56  LEU A CD2  1 
ATOM   1039 H  H    . LEU A 1 56  ? -1.54400  -18.06300 -0.79800  1.000 16.74000 ? 56  LEU A H    1 
ATOM   1040 H  HA   . LEU A 1 56  ? -1.44900  -20.73500 -1.17700  1.000 17.57000 ? 56  LEU A HA   1 
ATOM   1041 H  HB2  . LEU A 1 56  ? -0.03100  -19.21000 0.67900   1.000 18.93000 ? 56  LEU A HB2  1 
ATOM   1042 H  HB3  . LEU A 1 56  ? -0.18600  -20.78300 0.84400   1.000 18.93000 ? 56  LEU A HB3  1 
ATOM   1043 H  HG   . LEU A 1 56  ? 1.05900   -19.66500 -1.44800  1.000 22.03000 ? 56  LEU A HG   1 
ATOM   1044 H  HD11 . LEU A 1 56  ? 3.11700   -20.02500 -0.49200  1.000 27.95000 ? 56  LEU A HD11 1 
ATOM   1045 H  HD12 . LEU A 1 56  ? 2.29800   -19.06100 0.46800   1.000 27.95000 ? 56  LEU A HD12 1 
ATOM   1046 H  HD13 . LEU A 1 56  ? 2.44300   -20.60200 0.82600   1.000 27.95000 ? 56  LEU A HD13 1 
ATOM   1047 H  HD21 . LEU A 1 56  ? 1.89600   -21.89000 -1.62500  1.000 30.19000 ? 56  LEU A HD21 1 
ATOM   1048 H  HD22 . LEU A 1 56  ? 0.93100   -22.29400 -0.43000  1.000 30.19000 ? 56  LEU A HD22 1 
ATOM   1049 H  HD23 . LEU A 1 56  ? 0.32100   -21.80400 -1.81200  1.000 30.19000 ? 56  LEU A HD23 1 
ATOM   1050 N  N    . GLN A 1 57  ? -3.74400  -19.48300 0.23900   1.000 13.68000 ? 57  GLN A N    1 
ATOM   1051 C  CA   . GLN A 1 57  ? -5.01200  -19.77800 0.89700   1.000 13.17000 ? 57  GLN A CA   1 
ATOM   1052 C  C    . GLN A 1 57  ? -4.84900  -19.96300 2.40300   1.000 14.16000 ? 57  GLN A C    1 
ATOM   1053 O  O    . GLN A 1 57  ? -5.28800  -20.95800 2.98600   1.000 15.94000 ? 57  GLN A O    1 
ATOM   1054 C  CB   . GLN A 1 57  ? -5.72200  -20.95600 0.25000   1.000 13.69000 ? 57  GLN A CB   1 
ATOM   1055 C  CG   . GLN A 1 57  ? -6.28000  -20.62300 -1.16900  1.000 13.50000 ? 57  GLN A CG   1 
ATOM   1056 C  CD   . GLN A 1 57  ? -7.48200  -19.69600 -1.11700  1.000 13.34000 ? 57  GLN A CD   1 
ATOM   1057 O  OE1  . GLN A 1 57  ? -8.61200  -20.11600 -0.88100  1.000 15.43000 ? 57  GLN A OE1  1 
ATOM   1058 N  NE2  . GLN A 1 57  ? -7.21800  -18.41500 -1.28100  1.000 15.75000 ? 57  GLN A NE2  1 
ATOM   1059 H  H    . GLN A 1 57  ? -3.77000  -18.77700 -0.25100  1.000 16.44000 ? 57  GLN A H    1 
ATOM   1060 H  HA   . GLN A 1 57  ? -5.58200  -19.00200 0.77800   1.000 15.83000 ? 57  GLN A HA   1 
ATOM   1061 H  HB2  . GLN A 1 57  ? -5.09500  -21.69200 0.16100   1.000 16.45000 ? 57  GLN A HB2  1 
ATOM   1062 H  HB3  . GLN A 1 57  ? -6.46700  -21.22200 0.81000   1.000 16.45000 ? 57  GLN A HB3  1 
ATOM   1063 H  HG2  . GLN A 1 57  ? -5.58600  -20.18800 -1.68900  1.000 16.22000 ? 57  GLN A HG2  1 
ATOM   1064 H  HG3  . GLN A 1 57  ? -6.55200  -21.44700 -1.60400  1.000 16.22000 ? 57  GLN A HG3  1 
ATOM   1065 H  HE21 . GLN A 1 57  ? -6.40800  -18.15600 -1.40700  1.000 18.93000 ? 57  GLN A HE21 1 
ATOM   1066 H  HE22 . GLN A 1 57  ? -7.85600  -17.83900 -1.26200  1.000 18.93000 ? 57  GLN A HE22 1 
ATOM   1067 N  N    . ILE A 1 58  ? -4.28400  -18.96000 2.99400   0.850 10.91000 ? 58  ILE A N    1 
ATOM   1068 C  CA   . ILE A 1 58  ? -3.99100  -18.94800 4.43100   0.940 13.19000 ? 58  ILE A CA   1 
ATOM   1069 C  C    . ILE A 1 58  ? -5.24200  -18.55300 5.19900   0.710 9.63000  ? 58  ILE A C    1 
ATOM   1070 O  O    . ILE A 1 58  ? -5.92300  -17.58600 4.85400   0.890 13.23000 ? 58  ILE A O    1 
ATOM   1071 C  CB   . ILE A 1 58  ? -2.81500  -18.01000 4.69600   0.880 14.16000 ? 58  ILE A CB   1 
ATOM   1072 C  CG1  . ILE A 1 58  ? -1.53300  -18.62800 4.11900   0.910 17.68000 ? 58  ILE A CG1  1 
ATOM   1073 C  CG2  . ILE A 1 58  ? -2.68000  -17.69200 6.20800   0.770 13.66000 ? 58  ILE A CG2  1 
ATOM   1074 C  CD1  . ILE A 1 58  ? -0.35600  -17.70000 4.07800   0.730 18.80000 ? 58  ILE A CD1  1 
ATOM   1075 H  H    . ILE A 1 58  ? -4.04300  -18.24000 2.59100   1.000 13.12000 ? 58  ILE A H    1 
ATOM   1076 H  HA   . ILE A 1 58  ? -3.74700  -19.83600 4.73400   0.980 15.86000 ? 58  ILE A HA   1 
ATOM   1077 H  HB   . ILE A 1 58  ? -2.97500  -17.16300 4.25000   1.000 17.01000 ? 58  ILE A HB   1 
ATOM   1078 H  HG12 . ILE A 1 58  ? -1.28600  -19.39100 4.66500   1.000 21.23000 ? 58  ILE A HG12 1 
ATOM   1079 H  HG13 . ILE A 1 58  ? -1.71100  -18.91400 3.21000   0.990 21.23000 ? 58  ILE A HG13 1 
ATOM   1080 H  HG21 . ILE A 1 58  ? -1.87600  -17.16900 6.35000   1.000 16.41000 ? 58  ILE A HG21 1 
ATOM   1081 H  HG22 . ILE A 1 58  ? -3.45800  -17.18900 6.49500   0.950 16.41000 ? 58  ILE A HG22 1 
ATOM   1082 H  HG23 . ILE A 1 58  ? -2.62400  -18.52500 6.70200   0.990 16.41000 ? 58  ILE A HG23 1 
ATOM   1083 H  HD11 . ILE A 1 58  ? 0.39400   -18.16000 3.67100   0.920 22.59000 ? 58  ILE A HD11 1 
ATOM   1084 H  HD12 . ILE A 1 58  ? -0.58900  -16.91800 3.55500   0.970 22.59000 ? 58  ILE A HD12 1 
ATOM   1085 H  HD13 . ILE A 1 58  ? -0.13000  -17.43700 4.98400   0.930 22.59000 ? 58  ILE A HD13 1 
ATOM   1086 N  N    A ASN A 1 59  ? -5.62400  -19.38300 6.18600   0.430 13.53000 ? 59  ASN A N    1 
ATOM   1087 N  N    B ASN A 1 59  ? -5.51400  -19.29300 6.27500   0.180 14.33000 ? 59  ASN A N    1 
ATOM   1088 N  N    C ASN A 1 59  ? -5.51300  -19.29000 6.27700   0.390 14.35000 ? 59  ASN A N    1 
ATOM   1089 C  CA   A ASN A 1 59  ? -6.93300  -19.25200 6.81700   0.430 14.96000 ? 59  ASN A CA   1 
ATOM   1090 C  CA   B ASN A 1 59  ? -6.79900  -19.30300 6.96000   0.180 14.75000 ? 59  ASN A CA   1 
ATOM   1091 C  CA   C ASN A 1 59  ? -6.81100  -19.29100 6.93200   0.390 14.69000 ? 59  ASN A CA   1 
ATOM   1092 C  C    A ASN A 1 59  ? -6.93100  -18.35300 8.05200   0.430 15.40000 ? 59  ASN A C    1 
ATOM   1093 C  C    B ASN A 1 59  ? -6.86100  -18.23600 8.04800   0.180 15.33000 ? 59  ASN A C    1 
ATOM   1094 C  C    C ASN A 1 59  ? -6.88900  -18.29600 8.08700   0.390 15.33000 ? 59  ASN A C    1 
ATOM   1095 O  O    A ASN A 1 59  ? -5.99100  -18.32700 8.84700   0.430 17.38000 ? 59  ASN A O    1 
ATOM   1096 O  O    B ASN A 1 59  ? -5.85900  -17.91100 8.69100   0.180 16.12000 ? 59  ASN A O    1 
ATOM   1097 O  O    C ASN A 1 59  ? -5.92700  -18.10300 8.83300   0.390 16.84000 ? 59  ASN A O    1 
ATOM   1098 C  CB   A ASN A 1 59  ? -7.50600  -20.61800 7.19500   0.430 16.51000 ? 59  ASN A CB   1 
ATOM   1099 C  CB   B ASN A 1 59  ? -7.00800  -20.69100 7.57800   0.180 18.12000 ? 59  ASN A CB   1 
ATOM   1100 C  CB   C ASN A 1 59  ? -7.09300  -20.70600 7.43500   0.390 18.49000 ? 59  ASN A CB   1 
ATOM   1101 C  CG   A ASN A 1 59  ? -6.82600  -21.20800 8.40800   0.430 16.37000 ? 59  ASN A CG   1 
ATOM   1102 C  CG   B ASN A 1 59  ? -8.46600  -21.00400 7.87400   0.180 16.01000 ? 59  ASN A CG   1 
ATOM   1103 C  CG   C ASN A 1 59  ? -8.47000  -20.85200 8.01200   0.390 16.40000 ? 59  ASN A CG   1 
ATOM   1104 O  OD1  A ASN A 1 59  ? -7.01300  -20.73400 9.53000   0.430 19.88000 ? 59  ASN A OD1  1 
ATOM   1105 O  OD1  B ASN A 1 59  ? -9.30200  -20.11300 7.99600   0.180 16.94000 ? 59  ASN A OD1  1 
ATOM   1106 O  OD1  C ASN A 1 59  ? -8.66400  -20.67100 9.21000   0.390 21.44000 ? 59  ASN A OD1  1 
ATOM   1107 N  ND2  A ASN A 1 59  ? -6.01700  -22.22300 8.19000   0.430 15.49000 ? 59  ASN A ND2  1 
ATOM   1108 N  ND2  B ASN A 1 59  ? -8.77300  -22.29100 8.00000   0.180 21.23000 ? 59  ASN A ND2  1 
ATOM   1109 N  ND2  C ASN A 1 59  ? -9.43500  -21.19400 7.17400   0.390 17.86000 ? 59  ASN A ND2  1 
ATOM   1110 H  H    A ASN A 1 59  ? -5.14100  -20.02200 6.50000   0.390 16.25000 ? 59  ASN A H    1 
ATOM   1111 H  H    B ASN A 1 59  ? -4.94200  -19.82000 6.64200   0.040 17.22000 ? 59  ASN A H    1 
ATOM   1112 H  H    C ASN A 1 59  ? -4.94200  -19.81000 6.65600   0.220 17.25000 ? 59  ASN A H    1 
ATOM   1113 H  HA   A ASN A 1 59  ? -7.51200  -18.82800 6.16400   0.430 17.97000 ? 59  ASN A HA   1 
ATOM   1114 H  HA   B ASN A 1 59  ? -7.51400  -19.10700 6.33400   0.180 17.72000 ? 59  ASN A HA   1 
ATOM   1115 H  HA   C ASN A 1 59  ? -7.49200  -19.01200 6.30000   0.390 17.65000 ? 59  ASN A HA   1 
ATOM   1116 H  HB2  A ASN A 1 59  ? -8.45100  -20.52200 7.39500   0.430 19.84000 ? 59  ASN A HB2  1 
ATOM   1117 H  HB2  B ASN A 1 59  ? -6.67900  -21.36300 6.96000   0.180 21.77000 ? 59  ASN A HB2  1 
ATOM   1118 H  HB2  C ASN A 1 59  ? -7.01100  -21.32700 6.69400   0.390 22.22000 ? 59  ASN A HB2  1 
ATOM   1119 H  HB3  A ASN A 1 59  ? -7.38500  -21.23000 6.45300   0.430 19.84000 ? 59  ASN A HB3  1 
ATOM   1120 H  HB3  B ASN A 1 59  ? -6.51800  -20.74000 8.41300   0.180 21.77000 ? 59  ASN A HB3  1 
ATOM   1121 H  HB3  C ASN A 1 59  ? -6.45200  -20.92900 8.12700   0.390 22.22000 ? 59  ASN A HB3  1 
ATOM   1122 H  HD21 A ASN A 1 59  ? -5.60500  -22.59400 8.84800   0.430 18.61000 ? 59  ASN A HD21 1 
ATOM   1123 H  HD21 B ASN A 1 59  ? -9.58400  -22.52500 8.16800   0.180 25.50000 ? 59  ASN A HD21 1 
ATOM   1124 H  HD21 C ASN A 1 59  ? -10.24000 -21.28800 7.46200   0.390 21.45000 ? 59  ASN A HD21 1 
ATOM   1125 H  HD22 A ASN A 1 59  ? -5.89900  -22.51500 7.39000   0.430 18.61000 ? 59  ASN A HD22 1 
ATOM   1126 H  HD22 B ASN A 1 59  ? -8.16200  -22.88900 7.91400   0.180 25.50000 ? 59  ASN A HD22 1 
ATOM   1127 H  HD22 C ASN A 1 59  ? -9.25800  -21.32100 6.34300   0.390 21.45000 ? 59  ASN A HD22 1 
ATOM   1128 N  N    . SER A 1 60  ? -8.05700  -17.66700 8.23300   1.000 14.71000 ? 60  SER A N    1 
ATOM   1129 C  CA   . SER A 1 60  ? -8.28100  -16.68500 9.28500   1.000 15.29000 ? 60  SER A CA   1 
ATOM   1130 C  C    . SER A 1 60  ? -8.58000  -17.30800 10.64000  1.000 15.83000 ? 60  SER A C    1 
ATOM   1131 O  O    . SER A 1 60  ? -8.58100  -16.56100 11.62900  1.000 18.54000 ? 60  SER A O    1 
ATOM   1132 C  CB   . SER A 1 60  ? -9.46400  -15.77700 8.87700   1.000 13.71000 ? 60  SER A CB   1 
ATOM   1133 O  OG   . SER A 1 60  ? -10.67100 -16.47800 8.80400   1.000 15.19000 ? 60  SER A OG   1 
ATOM   1134 H  H    . SER A 1 60  ? -8.74700  -17.76000 7.72900   0.970 17.67000 ? 60  SER A H    1 
ATOM   1135 H  HA   . SER A 1 60  ? -7.48200  -16.14500 9.38400   1.000 18.37000 ? 60  SER A HA   1 
ATOM   1136 H  HB2  . SER A 1 60  ? -9.55500  -15.07100 9.53600   1.000 16.48000 ? 60  SER A HB2  1 
ATOM   1137 H  HB3  . SER A 1 60  ? -9.27500  -15.39400 8.00500   1.000 16.48000 ? 60  SER A HB3  1 
ATOM   1138 H  HG   . SER A 1 60  ? -10.63300 -17.16600 9.28400   1.000 18.25000 ? 60  SER A HG   1 
ATOM   1139 N  N    A ARG A 1 61  ? -8.77900  -18.61000 10.74000  0.610 17.05000 ? 61  ARG A N    1 
ATOM   1140 N  N    B ARG A 1 61  ? -8.88200  -18.61200 10.66800  0.390 17.24000 ? 61  ARG A N    1 
ATOM   1141 C  CA   A ARG A 1 61  ? -8.98000  -19.21800 12.06200  0.610 18.54000 ? 61  ARG A CA   1 
ATOM   1142 C  CA   B ARG A 1 61  ? -9.15800  -19.32700 11.91000  0.390 18.53000 ? 61  ARG A CA   1 
ATOM   1143 C  C    A ARG A 1 61  ? -7.71500  -19.08200 12.89700  0.610 20.82000 ? 61  ARG A C    1 
ATOM   1144 C  C    B ARG A 1 61  ? -7.94900  -19.33800 12.81700  0.390 14.74000 ? 61  ARG A C    1 
ATOM   1145 O  O    A ARG A 1 61  ? -7.75300  -18.74300 14.09900  0.610 17.11000 ? 61  ARG A O    1 
ATOM   1146 O  O    B ARG A 1 61  ? -8.11800  -19.46800 14.03600  0.390 15.54000 ? 61  ARG A O    1 
ATOM   1147 C  CB   A ARG A 1 61  ? -9.34000  -20.68500 11.83900  0.610 21.44000 ? 61  ARG A CB   1 
ATOM   1148 C  CB   B ARG A 1 61  ? -9.55800  -20.77400 11.60200  0.390 24.14000 ? 61  ARG A CB   1 
ATOM   1149 C  CG   A ARG A 1 61  ? -9.48200  -21.58600 13.06400  0.610 28.96000 ? 61  ARG A CG   1 
ATOM   1150 C  CG   B ARG A 1 61  ? -9.65800  -21.70500 12.82200  0.390 28.60000 ? 61  ARG A CG   1 
ATOM   1151 C  CD   A ARG A 1 61  ? -10.64200 -21.18100 13.92300  0.610 28.00000 ? 61  ARG A CD   1 
ATOM   1152 C  CD   B ARG A 1 61  ? -10.69900 -21.22300 13.80000  0.390 27.42000 ? 61  ARG A CD   1 
ATOM   1153 N  NE   A ARG A 1 61  ? -11.92200 -21.20600 13.22600  0.610 34.03000 ? 61  ARG A NE   1 
ATOM   1154 N  NE   B ARG A 1 61  ? -12.02800 -21.17600 13.20300  0.390 33.88000 ? 61  ARG A NE   1 
ATOM   1155 C  CZ   A ARG A 1 61  ? -12.98700 -20.51000 13.60500  0.610 41.00000 ? 61  ARG A CZ   1 
ATOM   1156 C  CZ   B ARG A 1 61  ? -13.02200 -20.41700 13.64500  0.390 40.90000 ? 61  ARG A CZ   1 
ATOM   1157 N  NH1  A ARG A 1 61  ? -12.96800 -19.76000 14.69800  0.610 38.60000 ? 61  ARG A NH1  1 
ATOM   1158 N  NH1  B ARG A 1 61  ? -12.88400 -19.64500 14.71300  0.390 38.45000 ? 61  ARG A NH1  1 
ATOM   1159 N  NH2  A ARG A 1 61  ? -14.10000 -20.57300 12.87500  0.610 38.57000 ? 61  ARG A NH2  1 
ATOM   1160 N  NH2  B ARG A 1 61  ? -14.18700 -20.43500 13.00000  0.390 38.32000 ? 61  ARG A NH2  1 
ATOM   1161 H  H    A ARG A 1 61  ? -8.80500  -19.16000 10.07900  0.610 20.48000 ? 61  ARG A H    1 
ATOM   1162 H  H    B ARG A 1 61  ? -8.93400  -19.10900 9.96900   0.390 20.71000 ? 61  ARG A H    1 
ATOM   1163 H  HA   A ARG A 1 61  ? -9.69900  -18.78500 12.54800  0.610 22.27000 ? 61  ARG A HA   1 
ATOM   1164 H  HA   B ARG A 1 61  ? -9.89700  -18.89400 12.36700  0.390 22.26000 ? 61  ARG A HA   1 
ATOM   1165 H  HB2  A ARG A 1 61  ? -10.19100 -20.71200 11.37500  0.610 25.75000 ? 61  ARG A HB2  1 
ATOM   1166 H  HB2  B ARG A 1 61  ? -10.42700 -20.76500 11.17200  0.390 28.99000 ? 61  ARG A HB2  1 
ATOM   1167 H  HB3  A ARG A 1 61  ? -8.64700  -21.07700 11.28500  0.610 25.75000 ? 61  ARG A HB3  1 
ATOM   1168 H  HB3  B ARG A 1 61  ? -8.89500  -21.15300 11.00300  0.390 28.99000 ? 61  ARG A HB3  1 
ATOM   1169 H  HG2  A ARG A 1 61  ? -9.62300  -22.50100 12.77400  0.610 34.78000 ? 61  ARG A HG2  1 
ATOM   1170 H  HG2  B ARG A 1 61  ? -9.90600  -22.59500 12.52700  0.390 34.35000 ? 61  ARG A HG2  1 
ATOM   1171 H  HG3  A ARG A 1 61  ? -8.67400  -21.52900 13.59800  0.610 34.78000 ? 61  ARG A HG3  1 
ATOM   1172 H  HG3  B ARG A 1 61  ? -8.80200  -21.73200 13.27700  0.390 34.35000 ? 61  ARG A HG3  1 
ATOM   1173 H  HD2  A ARG A 1 61  ? -10.70300 -21.79100 14.67500  0.610 33.62000 ? 61  ARG A HD2  1 
ATOM   1174 H  HD2  B ARG A 1 61  ? -10.72800 -21.82800 14.55800  0.390 32.93000 ? 61  ARG A HD2  1 
ATOM   1175 H  HD3  A ARG A 1 61  ? -10.49600 -20.27700 14.24100  0.610 33.62000 ? 61  ARG A HD3  1 
ATOM   1176 H  HD3  B ARG A 1 61  ? -10.46800 -20.32900 14.09700  0.390 32.93000 ? 61  ARG A HD3  1 
ATOM   1177 H  HE   A ARG A 1 61  ? -11.99200 -21.70200 12.52600  0.610 40.86000 ? 61  ARG A HE   1 
ATOM   1178 H  HE   B ARG A 1 61  ? -12.17700 -21.67400 12.51800  0.390 40.68000 ? 61  ARG A HE   1 
ATOM   1179 H  HH11 A ARG A 1 61  ? -12.25600 -19.71800 15.17800  0.610 46.34000 ? 61  ARG A HH11 1 
ATOM   1180 H  HH11 B ARG A 1 61  ? -13.54200 -19.16100 14.98200  0.390 46.16000 ? 61  ARG A HH11 1 
ATOM   1181 H  HH12 A ARG A 1 61  ? -13.66800 -19.31700 14.92800  0.610 46.34000 ? 61  ARG A HH12 1 
ATOM   1182 H  HH12 B ARG A 1 61  ? -12.13600 -19.62800 15.13700  0.390 46.16000 ? 61  ARG A HH12 1 
ATOM   1183 H  HH21 A ARG A 1 61  ? -14.12300 -21.06000 12.16700  0.610 46.30000 ? 61  ARG A HH21 1 
ATOM   1184 H  HH21 B ARG A 1 61  ? -14.28600 -20.93400 12.30600  0.390 46.01000 ? 61  ARG A HH21 1 
ATOM   1185 H  HH22 A ARG A 1 61  ? -14.79600 -20.12600 13.11200  0.610 46.30000 ? 61  ARG A HH22 1 
ATOM   1186 H  HH22 B ARG A 1 61  ? -14.83900 -19.94800 13.27600  0.390 46.01000 ? 61  ARG A HH22 1 
ATOM   1187 N  N    A TRP A 1 62  ? -6.56700  -19.31700 12.27900  0.610 17.50000 ? 62  TRP A N    1 
ATOM   1188 N  N    B TRP A 1 62  ? -6.73200  -19.17900 12.25500  0.390 18.87000 ? 62  TRP A N    1 
ATOM   1189 C  CA   A TRP A 1 62  ? -5.32900  -19.30900 13.02500  0.610 19.75000 ? 62  TRP A CA   1 
ATOM   1190 C  CA   B TRP A 1 62  ? -5.49400  -19.23900 13.02500  0.390 18.28000 ? 62  TRP A CA   1 
ATOM   1191 C  C    A TRP A 1 62  ? -4.38400  -18.18100 12.67700  0.610 20.90000 ? 62  TRP A C    1 
ATOM   1192 C  C    B TRP A 1 62  ? -4.45600  -18.17800 12.67900  0.390 20.53000 ? 62  TRP A C    1 
ATOM   1193 O  O    A TRP A 1 62  ? -3.64100  -17.73300 13.54400  0.610 21.45000 ? 62  TRP A O    1 
ATOM   1194 O  O    B TRP A 1 62  ? -3.70900  -17.77700 13.57200  0.390 21.41000 ? 62  TRP A O    1 
ATOM   1195 C  CB   A TRP A 1 62  ? -4.58400  -20.64200 12.84300  0.610 20.57000 ? 62  TRP A CB   1 
ATOM   1196 C  CB   B TRP A 1 62  ? -4.81600  -20.61800 12.87900  0.390 22.56000 ? 62  TRP A CB   1 
ATOM   1197 C  CG   A TRP A 1 62  ? -5.37300  -21.80700 13.33100  0.610 22.52000 ? 62  TRP A CG   1 
ATOM   1198 C  CG   B TRP A 1 62  ? -5.62700  -21.75100 13.39400  0.390 23.52000 ? 62  TRP A CG   1 
ATOM   1199 C  CD1  A TRP A 1 62  ? -6.09400  -22.68800 12.57500  0.610 26.60000 ? 62  TRP A CD1  1 
ATOM   1200 C  CD1  B TRP A 1 62  ? -6.26500  -22.70200 12.65700  0.390 26.30000 ? 62  TRP A CD1  1 
ATOM   1201 C  CD2  A TRP A 1 62  ? -5.53700  -22.22000 14.69200  0.610 31.64000 ? 62  TRP A CD2  1 
ATOM   1202 C  CD2  B TRP A 1 62  ? -5.89600  -22.05600 14.76600  0.390 28.64000 ? 62  TRP A CD2  1 
ATOM   1203 N  NE1  A TRP A 1 62  ? -6.69100  -23.62600 13.38100  0.610 33.49000 ? 62  TRP A NE1  1 
ATOM   1204 N  NE1  B TRP A 1 62  ? -6.91500  -23.58400 13.48600  0.390 32.48000 ? 62  TRP A NE1  1 
ATOM   1205 C  CE2  A TRP A 1 62  ? -6.36200  -23.36200 14.68400  0.610 33.89000 ? 62  TRP A CE2  1 
ATOM   1206 C  CE2  B TRP A 1 62  ? -6.70400  -23.20900 14.78600  0.390 34.43000 ? 62  TRP A CE2  1 
ATOM   1207 C  CE3  A TRP A 1 62  ? -5.06000  -21.73800 15.91200  0.610 31.34000 ? 62  TRP A CE3  1 
ATOM   1208 C  CE3  B TRP A 1 62  ? -5.53200  -21.46500 15.97800  0.390 32.95000 ? 62  TRP A CE3  1 
ATOM   1209 C  CZ2  A TRP A 1 62  ? -6.72300  -24.03100 15.85300  0.610 44.62000 ? 62  TRP A CZ2  1 
ATOM   1210 C  CZ2  B TRP A 1 62  ? -7.15400  -23.78500 15.97200  0.390 42.88000 ? 62  TRP A CZ2  1 
ATOM   1211 C  CZ3  A TRP A 1 62  ? -5.42200  -22.40900 17.07900  0.610 40.39000 ? 62  TRP A CZ3  1 
ATOM   1212 C  CZ3  B TRP A 1 62  ? -5.98100  -22.04100 17.15900  0.390 38.25000 ? 62  TRP A CZ3  1 
ATOM   1213 C  CH2  A TRP A 1 62  ? -6.24600  -23.53800 17.03600  0.610 39.07000 ? 62  TRP A CH2  1 
ATOM   1214 C  CH2  B TRP A 1 62  ? -6.78400  -23.18700 17.14400  0.390 36.73000 ? 62  TRP A CH2  1 
ATOM   1215 H  H    A TRP A 1 62  ? -6.48500  -19.48200 11.43900  0.610 21.02000 ? 62  TRP A H    1 
ATOM   1216 H  H    B TRP A 1 62  ? -6.60600  -19.03400 11.41600  0.390 22.67000 ? 62  TRP A H    1 
ATOM   1217 H  HA   A TRP A 1 62  ? -5.55400  -19.21000 13.96400  0.610 23.72000 ? 62  TRP A HA   1 
ATOM   1218 H  HA   B TRP A 1 62  ? -5.74000  -19.11300 13.95500  0.390 21.96000 ? 62  TRP A HA   1 
ATOM   1219 H  HB2  A TRP A 1 62  ? -4.40100  -20.77600 11.90000  0.610 24.71000 ? 62  TRP A HB2  1 
ATOM   1220 H  HB2  B TRP A 1 62  ? -4.64600  -20.78100 11.93800  0.390 27.10000 ? 62  TRP A HB2  1 
ATOM   1221 H  HB3  A TRP A 1 62  ? -3.75300  -20.61100 13.34100  0.610 24.71000 ? 62  TRP A HB3  1 
ATOM   1222 H  HB3  B TRP A 1 62  ? -3.98000  -20.60600 13.37100  0.390 27.10000 ? 62  TRP A HB3  1 
ATOM   1223 H  HD1  A TRP A 1 62  ? -6.17000  -22.65600 11.64800  0.610 31.95000 ? 62  TRP A HD1  1 
ATOM   1224 H  HD1  B TRP A 1 62  ? -6.26200  -22.74800 11.72900  0.390 31.59000 ? 62  TRP A HD1  1 
ATOM   1225 H  HE1  A TRP A 1 62  ? -7.18900  -24.27300 13.11200  0.610 40.21000 ? 62  TRP A HE1  1 
ATOM   1226 H  HE1  B TRP A 1 62  ? -7.38000  -24.26100 13.23000  0.390 39.00000 ? 62  TRP A HE1  1 
ATOM   1227 H  HE3  A TRP A 1 62  ? -4.51300  -20.98700 15.94600  0.610 37.63000 ? 62  TRP A HE3  1 
ATOM   1228 H  HE3  B TRP A 1 62  ? -5.00100  -20.70200 15.99300  0.390 39.57000 ? 62  TRP A HE3  1 
ATOM   1229 H  HZ2  A TRP A 1 62  ? -7.26900  -24.78400 15.83000  0.610 53.57000 ? 62  TRP A HZ2  1 
ATOM   1230 H  HZ2  B TRP A 1 62  ? -7.68700  -24.54700 15.96700  0.390 51.48000 ? 62  TRP A HZ2  1 
ATOM   1231 H  HZ3  A TRP A 1 62  ? -5.11100  -22.10100 17.90000  0.610 48.49000 ? 62  TRP A HZ3  1 
ATOM   1232 H  HZ3  B TRP A 1 62  ? -5.74400  -21.65900 17.97300  0.390 45.92000 ? 62  TRP A HZ3  1 
ATOM   1233 H  HH2  A TRP A 1 62  ? -6.47400  -23.96400 17.83100  0.610 46.91000 ? 62  TRP A HH2  1 
ATOM   1234 H  HH2  B TRP A 1 62  ? -7.07200  -23.55000 17.95100  0.390 44.10000 ? 62  TRP A HH2  1 
ATOM   1235 N  N    . TRP A 1 63  ? -4.34600  -17.71200 11.42400  1.000 15.38000 ? 63  TRP A N    1 
ATOM   1236 C  CA   . TRP A 1 63  ? -3.14300  -17.06000 10.95300  1.000 15.17000 ? 63  TRP A CA   1 
ATOM   1237 C  C    . TRP A 1 63  ? -3.21500  -15.57100 10.68800  1.000 15.85000 ? 63  TRP A C    1 
ATOM   1238 O  O    . TRP A 1 63  ? -2.18100  -14.92100 10.60700  1.000 17.82000 ? 63  TRP A O    1 
ATOM   1239 C  CB   . TRP A 1 63  ? -2.63400  -17.77200 9.67300   1.000 15.39000 ? 63  TRP A CB   1 
ATOM   1240 C  CG   . TRP A 1 63  ? -2.45100  -19.21800 9.90900   1.000 17.93000 ? 63  TRP A CG   1 
ATOM   1241 C  CD1  . TRP A 1 63  ? -3.25600  -20.22200 9.48600   1.000 18.81000 ? 63  TRP A CD1  1 
ATOM   1242 C  CD2  . TRP A 1 63  ? -1.44800  -19.82300 10.74500  1.000 19.17000 ? 63  TRP A CD2  1 
ATOM   1243 N  NE1  . TRP A 1 63  ? -2.80100  -21.43300 9.97600   1.000 20.43000 ? 63  TRP A NE1  1 
ATOM   1244 C  CE2  . TRP A 1 63  ? -1.69900  -21.20300 10.75400  1.000 18.61000 ? 63  TRP A CE2  1 
ATOM   1245 C  CE3  . TRP A 1 63  ? -0.35800  -19.32400 11.45800  1.000 21.10000 ? 63  TRP A CE3  1 
ATOM   1246 C  CZ2  . TRP A 1 63  ? -0.87400  -22.10700 11.45500  1.000 20.62000 ? 63  TRP A CZ2  1 
ATOM   1247 C  CZ3  . TRP A 1 63  ? 0.46200   -20.22200 12.14800  1.000 21.11000 ? 63  TRP A CZ3  1 
ATOM   1248 C  CH2  . TRP A 1 63  ? 0.19200   -21.58700 12.13600  1.000 22.06000 ? 63  TRP A CH2  1 
ATOM   1249 H  H    . TRP A 1 63  ? -4.98800  -17.76200 10.85400  1.000 18.48000 ? 63  TRP A H    1 
ATOM   1250 H  HA   . TRP A 1 63  ? -2.48600  -17.15000 11.66100  1.000 18.23000 ? 63  TRP A HA   1 
ATOM   1251 H  HB2  . TRP A 1 63  ? -3.28200  -17.65600 8.96000   1.000 18.50000 ? 63  TRP A HB2  1 
ATOM   1252 H  HB3  . TRP A 1 63  ? -1.78100  -17.39300 9.41100   1.000 18.50000 ? 63  TRP A HB3  1 
ATOM   1253 H  HD1  . TRP A 1 63  ? -4.00500  -20.11200 8.94600   1.000 22.59000 ? 63  TRP A HD1  1 
ATOM   1254 H  HE1  . TRP A 1 63  ? -3.15200  -22.20200 9.81800   1.000 24.55000 ? 63  TRP A HE1  1 
ATOM   1255 H  HE3  . TRP A 1 63  ? -0.18000  -18.41200 11.47500  1.000 25.35000 ? 63  TRP A HE3  1 
ATOM   1256 H  HZ2  . TRP A 1 63  ? -1.04700  -23.02100 11.45500  1.000 24.77000 ? 63  TRP A HZ2  1 
ATOM   1257 H  HZ3  . TRP A 1 63  ? 1.19700   -19.90300 12.62000  1.000 25.35000 ? 63  TRP A HZ3  1 
ATOM   1258 H  HH2  . TRP A 1 63  ? 0.75300   -22.16300 12.60500  1.000 26.50000 ? 63  TRP A HH2  1 
ATOM   1259 N  N    . CYS A 1 64  ? -4.41000  -15.03700 10.44600  1.000 15.33000 ? 64  CYS A N    1 
ATOM   1260 C  CA   . CYS A 1 64  ? -4.53800  -13.62600 10.12800  1.000 15.91000 ? 64  CYS A CA   1 
ATOM   1261 C  C    . CYS A 1 64  ? -5.84500  -13.11200 10.70700  1.000 14.04000 ? 64  CYS A C    1 
ATOM   1262 O  O    . CYS A 1 64  ? -6.76300  -13.88500 11.01300  1.000 16.61000 ? 64  CYS A O    1 
ATOM   1263 C  CB   . CYS A 1 64  ? -4.47200  -13.38100 8.60200   1.000 16.21000 ? 64  CYS A CB   1 
ATOM   1264 S  SG   . CYS A 1 64  ? -5.71200  -14.16800 7.58600   1.000 15.67000 ? 64  CYS A SG   1 
ATOM   1265 H  H    . CYS A 1 64  ? -5.15200  -15.47100 10.46100  1.000 18.42000 ? 64  CYS A H    1 
ATOM   1266 H  HA   . CYS A 1 64  ? -3.81300  -13.13100 10.54000  1.000 19.12000 ? 64  CYS A HA   1 
ATOM   1267 H  HB2  . CYS A 1 64  ? -4.55100  -12.42600 8.45100   1.000 19.48000 ? 64  CYS A HB2  1 
ATOM   1268 H  HB3  . CYS A 1 64  ? -3.61100  -13.69600 8.28800   1.000 19.48000 ? 64  CYS A HB3  1 
ATOM   1269 N  N    . ASN A 1 65  ? -5.93300  -11.78200 10.77800  1.000 16.03000 ? 65  ASN A N    1 
ATOM   1270 C  CA   . ASN A 1 65  ? -7.14800  -11.15400 11.28100  1.000 18.42000 ? 65  ASN A CA   1 
ATOM   1271 C  C    . ASN A 1 65  ? -7.98500  -10.57100 10.15100  1.000 14.77000 ? 65  ASN A C    1 
ATOM   1272 O  O    . ASN A 1 65  ? -7.50400  -9.69900  9.42300   1.000 15.55000 ? 65  ASN A O    1 
ATOM   1273 C  CB   . ASN A 1 65  ? -6.82800  -10.04300 12.27000  1.000 20.20000 ? 65  ASN A CB   1 
ATOM   1274 C  CG   . ASN A 1 65  ? -8.08200  -9.34700  12.72800  1.000 25.21000 ? 65  ASN A CG   1 
ATOM   1275 O  OD1  . ASN A 1 65  ? -9.02100  -10.01800 13.16000  1.000 26.08000 ? 65  ASN A OD1  1 
ATOM   1276 N  ND2  . ASN A 1 65  ? -8.14800  -8.03700  12.54700  1.000 36.40000 ? 65  ASN A ND2  1 
ATOM   1277 H  H    . ASN A 1 65  ? -5.31200  -11.23600 10.54400  1.000 19.26000 ? 65  ASN A H    1 
ATOM   1278 H  HA   . ASN A 1 65  ? -7.66400  -11.85200 11.71500  1.000 22.12000 ? 65  ASN A HA   1 
ATOM   1279 H  HB2  . ASN A 1 65  ? -6.38500  -10.41900 13.04600  1.000 24.26000 ? 65  ASN A HB2  1 
ATOM   1280 H  HB3  . ASN A 1 65  ? -6.25200  -9.38900  11.84400  1.000 24.26000 ? 65  ASN A HB3  1 
ATOM   1281 H  HD21 . ASN A 1 65  ? -7.49100  -7.62000  12.18100  1.000 43.71000 ? 65  ASN A HD21 1 
ATOM   1282 H  HD22 . ASN A 1 65  ? -8.84800  -7.60300  12.79500  1.000 43.71000 ? 65  ASN A HD22 1 
ATOM   1283 N  N    . ASP A 1 66  ? -9.24000  -11.00800 10.06100  1.000 15.46000 ? 66  ASP A N    1 
ATOM   1284 C  CA   . ASP A 1 66  ? -10.18000 -10.40300 9.12000   1.000 16.77000 ? 66  ASP A CA   1 
ATOM   1285 C  C    . ASP A 1 66  ? -11.38000 -9.75100  9.79000   1.000 19.49000 ? 66  ASP A C    1 
ATOM   1286 O  O    . ASP A 1 66  ? -12.27800 -9.29900  9.07500   1.000 19.44000 ? 66  ASP A O    1 
ATOM   1287 C  CB   . ASP A 1 66  ? -10.63800 -11.38600 8.03700   1.000 17.45000 ? 66  ASP A CB   1 
ATOM   1288 C  CG   . ASP A 1 66  ? -11.42100 -12.56500 8.55100   1.000 15.55000 ? 66  ASP A CG   1 
ATOM   1289 O  OD1  . ASP A 1 66  ? -11.80000 -12.63700 9.75900   1.000 16.93000 ? 66  ASP A OD1  1 
ATOM   1290 O  OD2  . ASP A 1 66  ? -11.73100 -13.46700 7.74500   1.000 14.77000 ? 66  ASP A OD2  1 
ATOM   1291 H  H    . ASP A 1 66  ? -9.56700  -11.64900 10.53100  1.000 18.58000 ? 66  ASP A H    1 
ATOM   1292 H  HA   . ASP A 1 66  ? -9.69200  -9.70100  8.66200   1.000 20.14000 ? 66  ASP A HA   1 
ATOM   1293 H  HB2  . ASP A 1 66  ? -11.20400 -10.91100 7.40900   1.000 20.97000 ? 66  ASP A HB2  1 
ATOM   1294 H  HB3  . ASP A 1 66  ? -9.85400  -11.73100 7.58200   1.000 20.97000 ? 66  ASP A HB3  1 
ATOM   1295 N  N    . GLY A 1 67  ? -11.41000 -9.68600  11.11300  1.000 17.49000 ? 67  GLY A N    1 
ATOM   1296 C  CA   . GLY A 1 67  ? -12.48100 -9.01900  11.85600  1.000 18.49000 ? 67  GLY A CA   1 
ATOM   1297 C  C    . GLY A 1 67  ? -13.80200 -9.72900  11.87300  1.000 23.56000 ? 67  GLY A C    1 
ATOM   1298 O  O    . GLY A 1 67  ? -14.77400 -9.17900  12.43100  1.000 25.49000 ? 67  GLY A O    1 
ATOM   1299 H  H    . GLY A 1 67  ? -10.80700 -10.02800 11.62200  1.000 21.01000 ? 67  GLY A H    1 
ATOM   1300 H  HA2  . GLY A 1 67  ? -12.19500 -8.91200  12.77700  1.000 22.21000 ? 67  GLY A HA2  1 
ATOM   1301 H  HA3  . GLY A 1 67  ? -12.62500 -8.14300  11.46600  1.000 22.21000 ? 67  GLY A HA3  1 
ATOM   1302 N  N    A ARG A 1 68  ? -13.89900 -10.93500 11.30700  0.590 19.51000 ? 68  ARG A N    1 
ATOM   1303 N  N    B ARG A 1 68  ? -13.90200 -10.92500 11.27200  0.410 19.49000 ? 68  ARG A N    1 
ATOM   1304 C  CA   A ARG A 1 68  ? -15.18000 -11.61800 11.24500  0.590 20.30000 ? 68  ARG A CA   1 
ATOM   1305 C  CA   B ARG A 1 68  ? -15.17400 -11.63000 11.17600  0.410 20.12000 ? 68  ARG A CA   1 
ATOM   1306 C  C    A ARG A 1 68  ? -15.06300 -13.12500 11.44400  0.590 20.32000 ? 68  ARG A C    1 
ATOM   1307 C  C    B ARG A 1 68  ? -15.04200 -13.13600 11.39900  0.410 20.44000 ? 68  ARG A C    1 
ATOM   1308 O  O    A ARG A 1 68  ? -15.89900 -13.89200 10.94800  0.590 24.33000 ? 68  ARG A O    1 
ATOM   1309 O  O    B ARG A 1 68  ? -15.85200 -13.91700 10.88400  0.410 24.04000 ? 68  ARG A O    1 
ATOM   1310 C  CB   A ARG A 1 68  ? -15.86600 -11.32100 9.92700   0.590 19.08000 ? 68  ARG A CB   1 
ATOM   1311 C  CB   B ARG A 1 68  ? -15.84900 -11.36300 9.83000   0.410 19.40000 ? 68  ARG A CB   1 
ATOM   1312 C  CG   A ARG A 1 68  ? -15.08400 -11.81500 8.72600   0.590 20.22000 ? 68  ARG A CG   1 
ATOM   1313 C  CG   B ARG A 1 68  ? -15.03400 -11.81000 8.60700   0.410 20.20000 ? 68  ARG A CG   1 
ATOM   1314 C  CD   A ARG A 1 68  ? -15.99400 -11.88700 7.54500   0.590 25.12000 ? 68  ARG A CD   1 
ATOM   1315 C  CD   B ARG A 1 68  ? -15.94600 -12.32400 7.49300   0.410 24.08000 ? 68  ARG A CD   1 
ATOM   1316 N  NE   A ARG A 1 68  ? -15.60400 -12.89400 6.57500   0.590 18.21000 ? 68  ARG A NE   1 
ATOM   1317 N  NE   B ARG A 1 68  ? -16.37400 -13.68900 7.76700   0.410 25.81000 ? 68  ARG A NE   1 
ATOM   1318 C  CZ   A ARG A 1 68  ? -16.09300 -12.94100 5.34200   0.590 21.01000 ? 68  ARG A CZ   1 
ATOM   1319 C  CZ   B ARG A 1 68  ? -17.51600 -14.23000 7.36800   0.410 29.34000 ? 68  ARG A CZ   1 
ATOM   1320 N  NH1  A ARG A 1 68  ? -17.01200 -12.08400 4.94700   0.590 21.27000 ? 68  ARG A NH1  1 
ATOM   1321 N  NH1  B ARG A 1 68  ? -18.38900 -13.55000 6.64300   0.410 36.20000 ? 68  ARG A NH1  1 
ATOM   1322 N  NH2  A ARG A 1 68  ? -15.65600 -13.87300 4.49300   0.590 16.43000 ? 68  ARG A NH2  1 
ATOM   1323 N  NH2  B ARG A 1 68  ? -17.80700 -15.47500 7.73600   0.410 19.65000 ? 68  ARG A NH2  1 
ATOM   1324 H  H    A ARG A 1 68  ? -13.24300 -11.36700 10.95700  0.590 23.44000 ? 68  ARG A H    1 
ATOM   1325 H  H    B ARG A 1 68  ? -13.24200 -11.34400 10.91400  0.410 23.41000 ? 68  ARG A H    1 
ATOM   1326 H  HA   A ARG A 1 68  ? -15.73000 -11.29100 11.97400  0.590 24.39000 ? 68  ARG A HA   1 
ATOM   1327 H  HA   B ARG A 1 68  ? -15.74400 -11.29200 11.88400  0.410 24.17000 ? 68  ARG A HA   1 
ATOM   1328 H  HB2  A ARG A 1 68  ? -16.73300 -11.75500 9.91900   0.590 22.92000 ? 68  ARG A HB2  1 
ATOM   1329 H  HB2  B ARG A 1 68  ? -16.69400 -11.84000 9.80900   0.410 23.30000 ? 68  ARG A HB2  1 
ATOM   1330 H  HB3  A ARG A 1 68  ? -15.97500 -10.36100 9.83900   0.590 22.92000 ? 68  ARG A HB3  1 
ATOM   1331 H  HB3  B ARG A 1 68  ? -16.00500 -10.41000 9.74600   0.410 23.30000 ? 68  ARG A HB3  1 
ATOM   1332 H  HG2  A ARG A 1 68  ? -14.36000 -11.20100 8.52800   0.590 24.29000 ? 68  ARG A HG2  1 
ATOM   1333 H  HG2  B ARG A 1 68  ? -14.52700 -11.05700 8.26500   0.410 24.26000 ? 68  ARG A HG2  1 
ATOM   1334 H  HG3  A ARG A 1 68  ? -14.72900 -12.70000 8.90400   0.590 24.29000 ? 68  ARG A HG3  1 
ATOM   1335 H  HG3  B ARG A 1 68  ? -14.43200 -12.52500 8.86400   0.410 24.26000 ? 68  ARG A HG3  1 
ATOM   1336 H  HD2  A ARG A 1 68  ? -16.88900 -12.10200 7.85100   0.590 30.17000 ? 68  ARG A HD2  1 
ATOM   1337 H  HD2  B ARG A 1 68  ? -16.73300 -11.76000 7.43200   0.410 28.91000 ? 68  ARG A HD2  1 
ATOM   1338 H  HD3  A ARG A 1 68  ? -15.99500 -11.02700 7.09600   0.590 30.17000 ? 68  ARG A HD3  1 
ATOM   1339 H  HD3  B ARG A 1 68  ? -15.46500 -12.31500 6.65000   0.410 28.91000 ? 68  ARG A HD3  1 
ATOM   1340 H  HE   A ARG A 1 68  ? -15.02800 -13.48800 6.81000   0.590 21.88000 ? 68  ARG A HE   1 
ATOM   1341 H  HE   B ARG A 1 68  ? -15.84200 -14.18500 8.22600   0.410 30.99000 ? 68  ARG A HE   1 
ATOM   1342 H  HH11 A ARG A 1 68  ? -17.30200 -11.48400 5.49100   0.590 25.55000 ? 68  ARG A HH11 1 
ATOM   1343 H  HH11 B ARG A 1 68  ? -18.22100 -12.73700 6.42000   0.410 43.46000 ? 68  ARG A HH11 1 
ATOM   1344 H  HH12 A ARG A 1 68  ? -17.32100 -12.12400 4.14600   0.590 25.55000 ? 68  ARG A HH12 1 
ATOM   1345 H  HH12 B ARG A 1 68  ? -19.12400 -13.92100 6.39500   0.410 43.46000 ? 68  ARG A HH12 1 
ATOM   1346 H  HH21 A ARG A 1 68  ? -15.06000 -14.44000 4.74500   0.590 19.75000 ? 68  ARG A HH21 1 
ATOM   1347 H  HH21 B ARG A 1 68  ? -17.25700 -15.91700 8.22700   0.410 23.61000 ? 68  ARG A HH21 1 
ATOM   1348 H  HH22 A ARG A 1 68  ? -15.97000 -13.90700 3.69300   0.590 19.75000 ? 68  ARG A HH22 1 
ATOM   1349 H  HH22 B ARG A 1 68  ? -18.54500 -15.83700 7.48300   0.410 23.61000 ? 68  ARG A HH22 1 
ATOM   1350 N  N    . THR A 1 69  ? -14.02000 -13.57100 12.14000  1.000 18.87000 ? 69  THR A N    1 
ATOM   1351 C  CA   . THR A 1 69  ? -13.85200 -14.98200 12.47600  1.000 17.06000 ? 69  THR A CA   1 
ATOM   1352 C  C    . THR A 1 69  ? -13.83000 -15.12700 13.99400  1.000 19.39000 ? 69  THR A C    1 
ATOM   1353 O  O    . THR A 1 69  ? -12.76300 -15.08700 14.61600  1.000 21.78000 ? 69  THR A O    1 
ATOM   1354 C  CB   . THR A 1 69  ? -12.58600 -15.54700 11.83700  1.000 19.44000 ? 69  THR A CB   1 
ATOM   1355 O  OG1  . THR A 1 69  ? -12.58500 -15.19000 10.43900  1.000 18.40000 ? 69  THR A OG1  1 
ATOM   1356 C  CG2  . THR A 1 69  ? -12.57800 -17.04700 11.96100  1.000 20.07000 ? 69  THR A CG2  1 
ATOM   1357 H  H    . THR A 1 69  ? -13.38700 -13.06900 12.43500  1.000 22.67000 ? 69  THR A H    1 
ATOM   1358 H  HA   . THR A 1 69  ? -14.61000 -15.48600 12.14200  1.000 20.50000 ? 69  THR A HA   1 
ATOM   1359 H  HB   . THR A 1 69  ? -11.79400 -15.19600 12.27400  1.000 23.35000 ? 69  THR A HB   1 
ATOM   1360 H  HG1  . THR A 1 69  ? -13.23400 -15.55300 10.04900  1.000 22.10000 ? 69  THR A HG1  1 
ATOM   1361 H  HG21 . THR A 1 69  ? -11.75700 -17.40700 11.59000  1.000 24.11000 ? 69  THR A HG21 1 
ATOM   1362 H  HG22 . THR A 1 69  ? -12.64000 -17.30300 12.89500  1.000 24.11000 ? 69  THR A HG22 1 
ATOM   1363 H  HG23 . THR A 1 69  ? -13.33200 -17.42400 11.48100  1.000 24.11000 ? 69  THR A HG23 1 
ATOM   1364 N  N    . PRO A 1 70  ? -14.98700 -15.27400 14.62500  1.000 21.13000 ? 70  PRO A N    1 
ATOM   1365 C  CA   . PRO A 1 70  ? -15.02500 -15.22300 16.09400  1.000 21.03000 ? 70  PRO A CA   1 
ATOM   1366 C  C    . PRO A 1 70  ? -14.22300 -16.35000 16.71100  1.000 26.12000 ? 70  PRO A C    1 
ATOM   1367 O  O    . PRO A 1 70  ? -14.23300 -17.48800 16.23400  1.000 29.43000 ? 70  PRO A O    1 
ATOM   1368 C  CB   . PRO A 1 70  ? -16.51500 -15.34700 16.41400  1.000 24.32000 ? 70  PRO A CB   1 
ATOM   1369 C  CG   . PRO A 1 70  ? -17.20800 -14.85600 15.19900  1.000 33.73000 ? 70  PRO A CG   1 
ATOM   1370 C  CD   . PRO A 1 70  ? -16.34000 -15.33500 14.05300  1.000 26.31000 ? 70  PRO A CD   1 
ATOM   1371 H  HA   . PRO A 1 70  ? -14.68800 -14.37200 16.41600  1.000 25.26000 ? 70  PRO A HA   1 
ATOM   1372 H  HB2  . PRO A 1 70  ? -16.73900 -16.27500 16.59100  1.000 29.20000 ? 70  PRO A HB2  1 
ATOM   1373 H  HB3  . PRO A 1 70  ? -16.73500 -14.80100 17.18500  1.000 29.20000 ? 70  PRO A HB3  1 
ATOM   1374 H  HG2  . PRO A 1 70  ? -18.09900 -15.23700 15.14600  1.000 40.50000 ? 70  PRO A HG2  1 
ATOM   1375 H  HG3  . PRO A 1 70  ? -17.26200 -13.88800 15.21500  1.000 40.50000 ? 70  PRO A HG3  1 
ATOM   1376 H  HD2  . PRO A 1 70  ? -16.57000 -16.24300 13.79900  1.000 31.60000 ? 70  PRO A HD2  1 
ATOM   1377 H  HD3  . PRO A 1 70  ? -16.42100 -14.74600 13.28600  1.000 31.60000 ? 70  PRO A HD3  1 
ATOM   1378 N  N    . GLY A 1 71  ? -13.50400 -16.00700 17.77500  1.000 24.83000 ? 71  GLY A N    1 
ATOM   1379 C  CA   . GLY A 1 71  ? -12.75500 -17.00800 18.49800  1.000 32.09000 ? 71  GLY A CA   1 
ATOM   1380 C  C    . GLY A 1 71  ? -11.53600 -17.48500 17.76000  1.000 41.61000 ? 71  GLY A C    1 
ATOM   1381 O  O    . GLY A 1 71  ? -11.02400 -18.56700 18.05500  1.000 47.07000 ? 71  GLY A O    1 
ATOM   1382 H  H    . GLY A 1 71  ? -13.43800 -15.20900 18.08900  1.000 29.82000 ? 71  GLY A H    1 
ATOM   1383 H  HA2  . GLY A 1 71  ? -12.46900 -16.63800 19.34800  1.000 38.53000 ? 71  GLY A HA2  1 
ATOM   1384 H  HA3  . GLY A 1 71  ? -13.32700 -17.77400 18.66300  1.000 38.53000 ? 71  GLY A HA3  1 
ATOM   1385 N  N    . SER A 1 72  ? -11.05900 -16.70600 16.79800  1.000 25.08000 ? 72  SER A N    1 
ATOM   1386 C  CA   . SER A 1 72  ? -9.87500  -17.07700 16.04000  1.000 21.34000 ? 72  SER A CA   1 
ATOM   1387 C  C    . SER A 1 72  ? -8.60900  -16.42800 16.60000  1.000 31.71000 ? 72  SER A C    1 
ATOM   1388 O  O    . SER A 1 72  ? -8.63000  -15.56900 17.49500  1.000 27.62000 ? 72  SER A O    1 
ATOM   1389 C  CB   . SER A 1 72  ? -10.07500 -16.67200 14.57400  1.000 21.34000 ? 72  SER A CB   1 
ATOM   1390 O  OG   . SER A 1 72  ? -9.91700  -15.28700 14.46000  1.000 24.50000 ? 72  SER A OG   1 
ATOM   1391 H  H    . SER A 1 72  ? -11.40600 -15.95400 16.56500  1.000 30.11000 ? 72  SER A H    1 
ATOM   1392 H  HA   . SER A 1 72  ? -9.74900  -18.03600 16.10400  1.000 25.63000 ? 72  SER A HA   1 
ATOM   1393 H  HB2  . SER A 1 72  ? -9.41300  -17.11900 14.02300  1.000 25.63000 ? 72  SER A HB2  1 
ATOM   1394 H  HB3  . SER A 1 72  ? -10.96800 -16.92100 14.28900  1.000 25.63000 ? 72  SER A HB3  1 
ATOM   1395 H  HG   . SER A 1 72  ? -10.50300 -14.97300 13.94500  1.000 29.42000 ? 72  SER A HG   1 
ATOM   1396 N  N    . ARG A 1 73  ? -7.47600  -16.87000 16.06400  1.000 23.50000 ? 73  ARG A N    1 
ATOM   1397 C  CA   . ARG A 1 73  ? -6.19200  -16.26600 16.35100  1.000 24.37000 ? 73  ARG A CA   1 
ATOM   1398 C  C    . ARG A 1 73  ? -5.66100  -15.54600 15.11700  1.000 24.88000 ? 73  ARG A C    1 
ATOM   1399 O  O    . ARG A 1 73  ? -6.25400  -15.59600 14.02900  1.000 24.46000 ? 73  ARG A O    1 
ATOM   1400 C  CB   . ARG A 1 73  ? -5.19900  -17.34100 16.82300  1.000 26.79000 ? 73  ARG A CB   1 
ATOM   1401 C  CG   . ARG A 1 73  ? -5.69900  -18.17000 18.02000  1.000 33.80000 ? 73  ARG A CG   1 
ATOM   1402 C  CD   . ARG A 1 73  ? -5.71200  -17.34900 19.30500  1.000 37.54000 ? 73  ARG A CD   1 
ATOM   1403 N  NE   . ARG A 1 73  ? -4.37100  -16.89400 19.64900  1.000 56.08000 ? 73  ARG A NE   1 
ATOM   1404 C  CZ   . ARG A 1 73  ? -3.57900  -17.46900 20.54600  1.000 59.28000 ? 73  ARG A CZ   1 
ATOM   1405 N  NH1  . ARG A 1 73  ? -3.97300  -18.51800 21.25200  1.000 54.65000 ? 73  ARG A NH1  1 
ATOM   1406 N  NH2  . ARG A 1 73  ? -2.35600  -16.98300 20.73300  1.000 45.59000 ? 73  ARG A NH2  1 
ATOM   1407 H  H    . ARG A 1 73  ? -7.43100  -17.53300 15.51800  1.000 28.23000 ? 73  ARG A H    1 
ATOM   1408 H  HA   . ARG A 1 73  ? -6.29100  -15.60900 17.05800  1.000 29.27000 ? 73  ARG A HA   1 
ATOM   1409 H  HB2  . ARG A 1 73  ? -5.03100  -17.95300 16.08900  1.000 32.17000 ? 73  ARG A HB2  1 
ATOM   1410 H  HB3  . ARG A 1 73  ? -4.37300  -16.90700 17.08800  1.000 32.17000 ? 73  ARG A HB3  1 
ATOM   1411 H  HG2  . ARG A 1 73  ? -6.60200  -18.47500 17.84400  1.000 40.58000 ? 73  ARG A HG2  1 
ATOM   1412 H  HG3  . ARG A 1 73  ? -5.11100  -18.93100 18.15100  1.000 40.58000 ? 73  ARG A HG3  1 
ATOM   1413 H  HD2  . ARG A 1 73  ? -6.27900  -16.57100 19.18500  1.000 45.08000 ? 73  ARG A HD2  1 
ATOM   1414 H  HD3  . ARG A 1 73  ? -6.04800  -17.89500 20.03300  1.000 45.08000 ? 73  ARG A HD3  1 
ATOM   1415 H  HE   . ARG A 1 73  ? -4.07000  -16.19900 19.24100  1.000 67.32000 ? 73  ARG A HE   1 
ATOM   1416 H  HH11 . ARG A 1 73  ? -4.76000  -18.84400 21.13500  1.000 65.60000 ? 73  ARG A HH11 1 
ATOM   1417 H  HH12 . ARG A 1 73  ? -3.44100  -18.87400 21.82700  1.000 65.60000 ? 73  ARG A HH12 1 
ATOM   1418 H  HH21 . ARG A 1 73  ? -2.08800  -16.30500 20.27600  1.000 54.73000 ? 73  ARG A HH21 1 
ATOM   1419 H  HH22 . ARG A 1 73  ? -1.83200  -17.34600 21.31100  1.000 54.73000 ? 73  ARG A HH22 1 
ATOM   1420 N  N    . ASN A 1 74  ? -4.54100  -14.86900 15.30200  1.000 21.03000 ? 74  ASN A N    1 
ATOM   1421 C  CA   . ASN A 1 74  ? -3.83400  -14.09500 14.30300  1.000 19.58000 ? 74  ASN A CA   1 
ATOM   1422 C  C    . ASN A 1 74  ? -2.32700  -14.33300 14.49900  1.000 21.89000 ? 74  ASN A C    1 
ATOM   1423 O  O    . ASN A 1 74  ? -1.54300  -13.43200 14.77700  1.000 22.79000 ? 74  ASN A O    1 
ATOM   1424 C  CB   . ASN A 1 74  ? -4.20000  -12.61000 14.42200  1.000 22.34000 ? 74  ASN A CB   1 
ATOM   1425 C  CG   . ASN A 1 74  ? -3.46800  -11.72600 13.43100  1.000 22.88000 ? 74  ASN A CG   1 
ATOM   1426 O  OD1  . ASN A 1 74  ? -2.85400  -12.20400 12.48000  1.000 21.27000 ? 74  ASN A OD1  1 
ATOM   1427 N  ND2  . ASN A 1 74  ? -3.54600  -10.41400 13.62600  1.000 26.48000 ? 74  ASN A ND2  1 
ATOM   1428 H  H    . ASN A 1 74  ? -4.13800  -14.84300 16.06200  1.000 25.26000 ? 74  ASN A H    1 
ATOM   1429 H  HA   . ASN A 1 74  ? -4.06900  -14.39900 13.41300  1.000 23.52000 ? 74  ASN A HA   1 
ATOM   1430 H  HB2  . ASN A 1 74  ? -5.15200  -12.50800 14.26300  1.000 26.83000 ? 74  ASN A HB2  1 
ATOM   1431 H  HB3  . ASN A 1 74  ? -3.97800  -12.30200 15.31500  1.000 26.83000 ? 74  ASN A HB3  1 
ATOM   1432 H  HD21 . ASN A 1 74  ? -3.14600  -9.87500  13.08800  1.000 31.80000 ? 74  ASN A HD21 1 
ATOM   1433 H  HD22 . ASN A 1 74  ? -3.99700  -10.10400 14.28900  1.000 31.80000 ? 74  ASN A HD22 1 
ATOM   1434 N  N    . LEU A 1 75  ? -1.90000  -15.57500 14.27400  1.000 20.56000 ? 75  LEU A N    1 
ATOM   1435 C  CA   . LEU A 1 75  ? -0.52600  -15.94600 14.62900  1.000 20.33000 ? 75  LEU A CA   1 
ATOM   1436 C  C    . LEU A 1 75  ? 0.53300   -15.34000 13.71300  1.000 22.05000 ? 75  LEU A C    1 
ATOM   1437 O  O    . LEU A 1 75  ? 1.71100   -15.28400 14.10000  1.000 28.41000 ? 75  LEU A O    1 
ATOM   1438 C  CB   . LEU A 1 75  ? -0.41500  -17.46300 14.66800  1.000 23.82000 ? 75  LEU A CB   1 
ATOM   1439 C  CG   . LEU A 1 75  ? -1.19200  -18.14900 15.77100  1.000 25.48000 ? 75  LEU A CG   1 
ATOM   1440 C  CD1  . LEU A 1 75  ? -1.06000  -19.66500 15.67800  1.000 29.86000 ? 75  LEU A CD1  1 
ATOM   1441 C  CD2  . LEU A 1 75  ? -0.75300  -17.60400 17.15200  1.000 37.22000 ? 75  LEU A CD2  1 
ATOM   1442 H  H    . LEU A 1 75  ? -2.37100  -16.20600 13.92800  1.000 24.70000 ? 75  LEU A H    1 
ATOM   1443 H  HA   . LEU A 1 75  ? -0.33000  -15.60300 15.51500  1.000 24.42000 ? 75  LEU A HA   1 
ATOM   1444 H  HB2  . LEU A 1 75  ? -0.74100  -17.81300 13.82400  1.000 28.61000 ? 75  LEU A HB2  1 
ATOM   1445 H  HB3  . LEU A 1 75  ? 0.51900   -17.69600 14.78500  1.000 28.61000 ? 75  LEU A HB3  1 
ATOM   1446 H  HG   . LEU A 1 75  ? -2.13700  -17.95200 15.67000  1.000 30.60000 ? 75  LEU A HG   1 
ATOM   1447 H  HD11 . LEU A 1 75  ? -1.57300  -20.07100 16.39500  1.000 35.86000 ? 75  LEU A HD11 1 
ATOM   1448 H  HD12 . LEU A 1 75  ? -1.40200  -19.96000 14.82000  1.000 35.86000 ? 75  LEU A HD12 1 
ATOM   1449 H  HD13 . LEU A 1 75  ? -0.12500  -19.90700 15.76300  1.000 35.86000 ? 75  LEU A HD13 1 
ATOM   1450 H  HD21 . LEU A 1 75  ? -1.05300  -18.21500 17.84300  1.000 44.69000 ? 75  LEU A HD21 1 
ATOM   1451 H  HD22 . LEU A 1 75  ? 0.21500   -17.53500 17.17000  1.000 44.69000 ? 75  LEU A HD22 1 
ATOM   1452 H  HD23 . LEU A 1 75  ? -1.15000  -16.73000 17.28800  1.000 44.69000 ? 75  LEU A HD23 1 
ATOM   1453 N  N    . CYS A 1 76  ? 0.17800   -14.90100 12.49600  1.000 18.68000 ? 76  CYS A N    1 
ATOM   1454 C  CA   . CYS A 1 76  ? 1.10700   -14.18500 11.63800  1.000 18.96000 ? 76  CYS A CA   1 
ATOM   1455 C  C    . CYS A 1 76  ? 1.08500   -12.68100 11.85600  1.000 19.79000 ? 76  CYS A C    1 
ATOM   1456 O  O    . CYS A 1 76  ? 1.86500   -11.96500 11.22900  1.000 21.72000 ? 76  CYS A O    1 
ATOM   1457 C  CB   . CYS A 1 76  ? 0.86200   -14.50200 10.14700  1.000 19.60000 ? 76  CYS A CB   1 
ATOM   1458 S  SG   . CYS A 1 76  ? 1.37900   -16.22000 9.76500   1.000 19.38000 ? 76  CYS A SG   1 
ATOM   1459 H  H    . CYS A 1 76  ? -0.60200  -15.01100 12.15200  1.000 22.44000 ? 76  CYS A H    1 
ATOM   1460 H  HA   . CYS A 1 76  ? 2.00000   -14.50300 11.84600  1.000 22.78000 ? 76  CYS A HA   1 
ATOM   1461 H  HB2  . CYS A 1 76  ? -0.08200  -14.41100 9.94700   1.000 23.55000 ? 76  CYS A HB2  1 
ATOM   1462 H  HB3  . CYS A 1 76  ? 1.37900   -13.89300 9.59600   1.000 23.55000 ? 76  CYS A HB3  1 
ATOM   1463 N  N    A ASN A 1 77  ? 0.19800   -12.19800 12.72500  0.540 20.87000 ? 77  ASN A N    1 
ATOM   1464 N  N    B ASN A 1 77  ? 0.21000   -12.20400 12.73900  0.460 20.89000 ? 77  ASN A N    1 
ATOM   1465 C  CA   A ASN A 1 77  ? 0.14300   -10.78900 13.11400  0.540 25.69000 ? 77  ASN A CA   1 
ATOM   1466 C  CA   B ASN A 1 77  ? 0.10800   -10.79400 13.11400  0.460 25.59000 ? 77  ASN A CA   1 
ATOM   1467 C  C    A ASN A 1 77  ? -0.01500  -9.87400  11.90100  0.540 24.61000 ? 77  ASN A C    1 
ATOM   1468 C  C    B ASN A 1 77  ? 0.00200   -9.89400  11.88500  0.460 24.62000 ? 77  ASN A C    1 
ATOM   1469 O  O    A ASN A 1 77  ? 0.72100   -8.90300  11.72500  0.540 26.21000 ? 77  ASN A O    1 
ATOM   1470 O  O    B ASN A 1 77  ? 0.78600   -8.96700  11.68000  0.460 26.24000 ? 77  ASN A O    1 
ATOM   1471 C  CB   A ASN A 1 77  ? 1.36900   -10.39200 13.94900  0.540 27.29000 ? 77  ASN A CB   1 
ATOM   1472 C  CB   B ASN A 1 77  ? 1.26800   -10.36500 14.01900  0.460 27.25000 ? 77  ASN A CB   1 
ATOM   1473 C  CG   A ASN A 1 77  ? 1.58100   -11.29800 15.14600  0.540 28.21000 ? 77  ASN A CG   1 
ATOM   1474 C  CG   B ASN A 1 77  ? 1.03000   -9.01000  14.66100  0.460 30.64000 ? 77  ASN A CG   1 
ATOM   1475 O  OD1  A ASN A 1 77  ? 2.60300   -11.98200 15.24700  0.540 41.61000 ? 77  ASN A OD1  1 
ATOM   1476 O  OD1  B ASN A 1 77  ? -0.07100  -8.71600  15.12500  0.460 38.09000 ? 77  ASN A OD1  1 
ATOM   1477 N  ND2  A ASN A 1 77  ? 0.61400   -11.31100 16.06000  0.540 34.84000 ? 77  ASN A ND2  1 
ATOM   1478 N  ND2  B ASN A 1 77  ? 2.06100   -8.17300  14.67900  0.460 37.61000 ? 77  ASN A ND2  1 
ATOM   1479 H  H    A ASN A 1 77  ? -0.39900  -12.68000 13.11300  0.540 25.07000 ? 77  ASN A H    1 
ATOM   1480 H  H    B ASN A 1 77  ? -0.35900  -12.69800 13.15200  0.460 25.10000 ? 77  ASN A H    1 
ATOM   1481 H  HA   A ASN A 1 77  ? -0.64600  -10.66600 13.66600  0.540 30.86000 ? 77  ASN A HA   1 
ATOM   1482 H  HA   B ASN A 1 77  ? -0.71400  -10.68800 13.61900  0.460 30.73000 ? 77  ASN A HA   1 
ATOM   1483 H  HB2  A ASN A 1 77  ? 2.16100   -10.44200 13.39100  0.540 32.77000 ? 77  ASN A HB2  1 
ATOM   1484 H  HB2  B ASN A 1 77  ? 1.37700   -11.01900 14.72700  0.460 32.73000 ? 77  ASN A HB2  1 
ATOM   1485 H  HB3  A ASN A 1 77  ? 1.24900   -9.48700  14.27500  0.540 32.77000 ? 77  ASN A HB3  1 
ATOM   1486 H  HB3  B ASN A 1 77  ? 2.08000   -10.31000 13.49100  0.460 32.73000 ? 77  ASN A HB3  1 
ATOM   1487 H  HD21 A ASN A 1 77  ? -0.08500  -10.82200 15.95400  0.540 41.83000 ? 77  ASN A HD21 1 
ATOM   1488 H  HD21 B ASN A 1 77  ? 2.81400   -8.41100  14.33800  0.460 45.15000 ? 77  ASN A HD21 1 
ATOM   1489 H  HD22 A ASN A 1 77  ? 0.68900   -11.80900 16.75800  0.540 41.83000 ? 77  ASN A HD22 1 
ATOM   1490 H  HD22 B ASN A 1 77  ? 1.97600   -7.39300  15.03200  0.460 45.15000 ? 77  ASN A HD22 1 
ATOM   1491 N  N    . ILE A 1 78  ? -1.00000  -10.18400 11.05700  1.000 20.64000 ? 78  ILE A N    1 
ATOM   1492 C  CA   . ILE A 1 78  ? -1.24900  -9.42000  9.84600   1.000 21.45000 ? 78  ILE A CA   1 
ATOM   1493 C  C    . ILE A 1 78  ? -2.74500  -9.37800  9.57300   1.000 18.43000 ? 78  ILE A C    1 
ATOM   1494 O  O    . ILE A 1 78  ? -3.47300  -10.32500 9.89700   1.000 18.35000 ? 78  ILE A O    1 
ATOM   1495 C  CB   . ILE A 1 78  ? -0.57900  -10.02600 8.59300   1.000 25.09000 ? 78  ILE A CB   1 
ATOM   1496 C  CG1  . ILE A 1 78  ? -0.80300  -11.53500 8.53400   1.000 23.76000 ? 78  ILE A CG1  1 
ATOM   1497 C  CG2  . ILE A 1 78  ? 0.90000   -9.65100  8.50400   1.000 33.12000 ? 78  ILE A CG2  1 
ATOM   1498 C  CD1  . ILE A 1 78  ? -0.99200  -12.05500 7.12100   1.000 37.44000 ? 78  ILE A CD1  1 
ATOM   1499 H  H    . ILE A 1 78  ? -1.54200  -10.84300 11.16800  1.000 24.79000 ? 78  ILE A H    1 
ATOM   1500 H  HA   . ILE A 1 78  ? -0.89300  -8.53400  10.01500  1.000 25.77000 ? 78  ILE A HA   1 
ATOM   1501 H  HB   . ILE A 1 78  ? -1.00600  -9.64000  7.81200   1.000 30.13000 ? 78  ILE A HB   1 
ATOM   1502 H  HG12 . ILE A 1 78  ? -0.03100  -11.98200 8.91600   1.000 28.54000 ? 78  ILE A HG12 1 
ATOM   1503 H  HG13 . ILE A 1 78  ? -1.59900  -11.75400 9.04200   1.000 28.54000 ? 78  ILE A HG13 1 
ATOM   1504 H  HG21 . ILE A 1 78  ? 1.27800   -10.04500 7.70200   1.000 39.77000 ? 78  ILE A HG21 1 
ATOM   1505 H  HG22 . ILE A 1 78  ? 0.97900   -8.68500  8.46600   1.000 39.77000 ? 78  ILE A HG22 1 
ATOM   1506 H  HG23 . ILE A 1 78  ? 1.35900   -9.99000  9.28800   1.000 39.77000 ? 78  ILE A HG23 1 
ATOM   1507 H  HD11 . ILE A 1 78  ? -1.12500  -13.01600 7.15300   1.000 44.95000 ? 78  ILE A HD11 1 
ATOM   1508 H  HD12 . ILE A 1 78  ? -1.76900  -11.62700 6.72800   1.000 44.95000 ? 78  ILE A HD12 1 
ATOM   1509 H  HD13 . ILE A 1 78  ? -0.20100  -11.84800 6.59900   1.000 44.95000 ? 78  ILE A HD13 1 
ATOM   1510 N  N    . PRO A 1 79  ? -3.23000  -8.32900  8.93700   1.000 19.41000 ? 79  PRO A N    1 
ATOM   1511 C  CA   . PRO A 1 79  ? -4.59100  -8.39600  8.40600   1.000 18.01000 ? 79  PRO A CA   1 
ATOM   1512 C  C    . PRO A 1 79  ? -4.61400  -9.35400  7.23800   1.000 16.49000 ? 79  PRO A C    1 
ATOM   1513 O  O    . PRO A 1 79  ? -3.68500  -9.39000  6.41600   1.000 17.98000 ? 79  PRO A O    1 
ATOM   1514 C  CB   . PRO A 1 79  ? -4.88500  -6.96000  7.96300   1.000 21.55000 ? 79  PRO A CB   1 
ATOM   1515 C  CG   . PRO A 1 79  ? -3.54100  -6.34300  7.72900   1.000 29.12000 ? 79  PRO A CG   1 
ATOM   1516 C  CD   . PRO A 1 79  ? -2.55300  -7.06000  8.62100   1.000 24.00000 ? 79  PRO A CD   1 
ATOM   1517 H  HA   . PRO A 1 79  ? -5.23800  -8.65000  9.08300   1.000 21.64000 ? 79  PRO A HA   1 
ATOM   1518 H  HB2  . PRO A 1 79  ? -5.41000  -6.96700  7.14800   1.000 25.89000 ? 79  PRO A HB2  1 
ATOM   1519 H  HB3  . PRO A 1 79  ? -5.36500  -6.49100  8.66300   1.000 25.89000 ? 79  PRO A HB3  1 
ATOM   1520 H  HG2  . PRO A 1 79  ? -3.29600  -6.45200  6.79700   1.000 34.97000 ? 79  PRO A HG2  1 
ATOM   1521 H  HG3  . PRO A 1 79  ? -3.57800  -5.40000  7.95400   1.000 34.97000 ? 79  PRO A HG3  1 
ATOM   1522 H  HD2  . PRO A 1 79  ? -1.72000  -7.22200  8.15000   1.000 28.82000 ? 79  PRO A HD2  1 
ATOM   1523 H  HD3  . PRO A 1 79  ? -2.38500  -6.54900  9.42800   1.000 28.82000 ? 79  PRO A HD3  1 
ATOM   1524 N  N    . CYS A 1 80  ? -5.70400  -10.09000 7.14700   1.000 14.52000 ? 80  CYS A N    1 
ATOM   1525 C  CA   . CYS A 1 80  ? -5.84300  -11.06000 6.05200   1.000 14.93000 ? 80  CYS A CA   1 
ATOM   1526 C  C    . CYS A 1 80  ? -5.75400  -10.39500 4.68100   1.000 15.89000 ? 80  CYS A C    1 
ATOM   1527 O  O    . CYS A 1 80  ? -5.23500  -11.00100 3.73000   1.000 16.87000 ? 80  CYS A O    1 
ATOM   1528 C  CB   . CYS A 1 80  ? -7.15000  -11.85000 6.17600   1.000 14.13000 ? 80  CYS A CB   1 
ATOM   1529 S  SG   . CYS A 1 80  ? -7.28300  -12.84300 7.70300   1.000 14.94000 ? 80  CYS A SG   1 
ATOM   1530 H  H    . CYS A 1 80  ? -6.37100  -10.05700 7.68900   1.000 17.45000 ? 80  CYS A H    1 
ATOM   1531 H  HA   . CYS A 1 80  ? -5.11200  -11.69400 6.12700   1.000 17.94000 ? 80  CYS A HA   1 
ATOM   1532 H  HB2  . CYS A 1 80  ? -7.89200  -11.22600 6.16600   1.000 16.98000 ? 80  CYS A HB2  1 
ATOM   1533 H  HB3  . CYS A 1 80  ? -7.21700  -12.45800 5.42300   1.000 16.98000 ? 80  CYS A HB3  1 
ATOM   1534 N  N    . SER A 1 81  ? -6.25300  -9.16600  4.54200   1.000 16.95000 ? 81  SER A N    1 
ATOM   1535 C  CA   . SER A 1 81  ? -6.17900  -8.48200  3.25600   1.000 17.19000 ? 81  SER A CA   1 
ATOM   1536 C  C    . SER A 1 81  ? -4.75700  -8.26200  2.75900   1.000 19.54000 ? 81  SER A C    1 
ATOM   1537 O  O    . SER A 1 81  ? -4.56400  -8.15200  1.54200   1.000 22.28000 ? 81  SER A O    1 
ATOM   1538 C  CB   . SER A 1 81  ? -6.91400  -7.14300  3.34700   1.000 23.64000 ? 81  SER A CB   1 
ATOM   1539 O  OG   . SER A 1 81  ? -6.24600  -6.29800  4.27400   1.000 26.00000 ? 81  SER A OG   1 
ATOM   1540 H  H    . SER A 1 81  ? -6.63300  -8.71500  5.16800   1.000 20.37000 ? 81  SER A H    1 
ATOM   1541 H  HA   . SER A 1 81  ? -6.62000  -9.04000  2.59600   1.000 20.65000 ? 81  SER A HA   1 
ATOM   1542 H  HB2  . SER A 1 81  ? -6.92000  -6.72100  2.47400   1.000 28.39000 ? 81  SER A HB2  1 
ATOM   1543 H  HB3  . SER A 1 81  ? -7.82400  -7.29600  3.64800   1.000 28.39000 ? 81  SER A HB3  1 
ATOM   1544 H  HG   . SER A 1 81  ? -6.42300  -6.53700  5.06000   1.000 31.23000 ? 81  SER A HG   1 
ATOM   1545 N  N    . ALA A 1 82  ? -3.76000  -8.21800  3.64300   1.000 18.07000 ? 82  ALA A N    1 
ATOM   1546 C  CA   . ALA A 1 82  ? -2.36800  -8.13100  3.20800   1.000 23.01000 ? 82  ALA A CA   1 
ATOM   1547 C  C    . ALA A 1 82  ? -1.95900  -9.32900  2.36800   1.000 21.72000 ? 82  ALA A C    1 
ATOM   1548 O  O    . ALA A 1 82  ? -1.01000  -9.24200  1.56900   1.000 25.50000 ? 82  ALA A O    1 
ATOM   1549 C  CB   . ALA A 1 82  ? -1.44100  -8.06100  4.42100   1.000 25.70000 ? 82  ALA A CB   1 
ATOM   1550 H  H    . ALA A 1 82  ? -3.86200  -8.23700  4.49700   1.000 21.71000 ? 82  ALA A H    1 
ATOM   1551 H  HA   . ALA A 1 82  ? -2.27400  -7.32300  2.68000   1.000 27.64000 ? 82  ALA A HA   1 
ATOM   1552 H  HB1  . ALA A 1 82  ? -0.53300  -7.90200  4.11700   1.000 30.87000 ? 82  ALA A HB1  1 
ATOM   1553 H  HB2  . ALA A 1 82  ? -1.72800  -7.33400  4.99700   1.000 30.87000 ? 82  ALA A HB2  1 
ATOM   1554 H  HB3  . ALA A 1 82  ? -1.48600  -8.90200  4.90300   1.000 30.87000 ? 82  ALA A HB3  1 
ATOM   1555 N  N    . LEU A 1 83  ? -2.62000  -10.45800 2.55500   1.000 18.64000 ? 83  LEU A N    1 
ATOM   1556 C  CA   . LEU A 1 83  ? -2.32300  -11.67900 1.82100   1.000 17.96000 ? 83  LEU A CA   1 
ATOM   1557 C  C    . LEU A 1 83  ? -2.84500  -11.66100 0.39300   1.000 20.06000 ? 83  LEU A C    1 
ATOM   1558 O  O    . LEU A 1 83  ? -2.61800  -12.63700 -0.33800  1.000 21.24000 ? 83  LEU A O    1 
ATOM   1559 C  CB   . LEU A 1 83  ? -2.92900  -12.86900 2.55200   1.000 18.70000 ? 83  LEU A CB   1 
ATOM   1560 C  CG   . LEU A 1 83  ? -2.41000  -13.09100 3.96800   1.000 19.25000 ? 83  LEU A CG   1 
ATOM   1561 C  CD1  . LEU A 1 83  ? -3.22500  -14.09900 4.75200   1.000 23.72000 ? 83  LEU A CD1  1 
ATOM   1562 C  CD2  . LEU A 1 83  ? -0.92900  -13.53100 3.87900   1.000 27.69000 ? 83  LEU A CD2  1 
ATOM   1563 H  H    . LEU A 1 83  ? -3.26400  -10.54800 3.11700   1.000 22.39000 ? 83  LEU A H    1 
ATOM   1564 H  HA   . LEU A 1 83  ? -1.35900  -11.78800 1.78400   1.000 21.58000 ? 83  LEU A HA   1 
ATOM   1565 H  HB2  . LEU A 1 83  ? -3.88800  -12.73600 2.61100   1.000 22.46000 ? 83  LEU A HB2  1 
ATOM   1566 H  HB3  . LEU A 1 83  ? -2.73700  -13.67200 2.04200   1.000 22.46000 ? 83  LEU A HB3  1 
ATOM   1567 H  HG   . LEU A 1 83  ? -2.48600  -12.26000 4.46300   1.000 23.12000 ? 83  LEU A HG   1 
ATOM   1568 H  HD11 . LEU A 1 83  ? -2.82000  -14.22300 5.62400   1.000 28.49000 ? 83  LEU A HD11 1 
ATOM   1569 H  HD12 . LEU A 1 83  ? -4.13000  -13.76300 4.85200   1.000 28.49000 ? 83  LEU A HD12 1 
ATOM   1570 H  HD13 . LEU A 1 83  ? -3.23700  -14.94000 4.26900   1.000 28.49000 ? 83  LEU A HD13 1 
ATOM   1571 H  HD21 . LEU A 1 83  ? -0.67100  -13.94200 4.71900   1.000 33.25000 ? 83  LEU A HD21 1 
ATOM   1572 H  HD22 . LEU A 1 83  ? -0.83200  -14.16900 3.15500   1.000 33.25000 ? 83  LEU A HD22 1 
ATOM   1573 H  HD23 . LEU A 1 83  ? -0.37800  -12.75100 3.70900   1.000 33.25000 ? 83  LEU A HD23 1 
ATOM   1574 N  N    . LEU A 1 84  ? -3.56800  -10.62100 -0.01800  1.000 17.63000 ? 84  LEU A N    1 
ATOM   1575 C  CA   . LEU A 1 84  ? -4.10400  -10.53500 -1.37300  1.000 18.66000 ? 84  LEU A CA   1 
ATOM   1576 C  C    . LEU A 1 84  ? -3.26400  -9.63300  -2.27100  1.000 23.27000 ? 84  LEU A C    1 
ATOM   1577 O  O    . LEU A 1 84  ? -3.59800  -9.46700  -3.45800  1.000 24.64000 ? 84  LEU A O    1 
ATOM   1578 C  CB   . LEU A 1 84  ? -5.55000  -10.04500 -1.33800  1.000 19.44000 ? 84  LEU A CB   1 
ATOM   1579 C  CG   . LEU A 1 84  ? -6.46500  -10.79000 -0.36900  1.000 20.39000 ? 84  LEU A CG   1 
ATOM   1580 C  CD1  . LEU A 1 84  ? -7.86400  -10.19500 -0.39600  1.000 26.40000 ? 84  LEU A CD1  1 
ATOM   1581 C  CD2  . LEU A 1 84  ? -6.52900  -12.25400 -0.76600  1.000 19.32000 ? 84  LEU A CD2  1 
ATOM   1582 H  H    . LEU A 1 84  ? -3.76400  -9.94500  0.47600   1.000 21.18000 ? 84  LEU A H    1 
ATOM   1583 H  HA   . LEU A 1 84  ? -4.11100  -11.42100 -1.76700  1.000 22.41000 ? 84  LEU A HA   1 
ATOM   1584 H  HB2  . LEU A 1 84  ? -5.55000  -9.11000  -1.07800  1.000 23.35000 ? 84  LEU A HB2  1 
ATOM   1585 H  HB3  . LEU A 1 84  ? -5.92700  -10.14100 -2.22700  1.000 23.35000 ? 84  LEU A HB3  1 
ATOM   1586 H  HG   . LEU A 1 84  ? -6.11600  -10.71200 0.53300   1.000 24.50000 ? 84  LEU A HG   1 
ATOM   1587 H  HD11 . LEU A 1 84  ? -8.42200  -10.67100 0.24000   1.000 31.70000 ? 84  LEU A HD11 1 
ATOM   1588 H  HD12 . LEU A 1 84  ? -7.81300  -9.25700  -0.15400  1.000 31.70000 ? 84  LEU A HD12 1 
ATOM   1589 H  HD13 . LEU A 1 84  ? -8.22900  -10.28700 -1.29000  1.000 31.70000 ? 84  LEU A HD13 1 
ATOM   1590 H  HD21 . LEU A 1 84  ? -7.11200  -12.72300 -0.15000  1.000 23.20000 ? 84  LEU A HD21 1 
ATOM   1591 H  HD22 . LEU A 1 84  ? -6.87800  -12.32100 -1.66900  1.000 23.20000 ? 84  LEU A HD22 1 
ATOM   1592 H  HD23 . LEU A 1 84  ? -5.63600  -12.63100 -0.72800  1.000 23.20000 ? 84  LEU A HD23 1 
ATOM   1593 N  N    A SER A 1 85  ? -2.16700  -9.10200  -1.74400  0.700 21.66000 ? 85  SER A N    1 
ATOM   1594 N  N    B SER A 1 85  ? -2.21400  -9.01400  -1.74200  0.300 21.66000 ? 85  SER A N    1 
ATOM   1595 C  CA   A SER A 1 85  ? -1.33300  -8.14400  -2.45600  0.700 21.66000 ? 85  SER A CA   1 
ATOM   1596 C  CA   B SER A 1 85  ? -1.45500  -8.06800  -2.54400  0.300 22.63000 ? 85  SER A CA   1 
ATOM   1597 C  C    A SER A 1 85  ? -0.59300  -8.79100  -3.62400  0.700 25.50000 ? 85  SER A C    1 
ATOM   1598 C  C    B SER A 1 85  ? -0.76700  -8.78200  -3.70800  0.300 24.27000 ? 85  SER A C    1 
ATOM   1599 O  O    A SER A 1 85  ? -0.25400  -9.97700  -3.58800  0.700 21.33000 ? 85  SER A O    1 
ATOM   1600 O  O    B SER A 1 85  ? -0.70700  -10.00900 -3.78300  0.300 22.27000 ? 85  SER A O    1 
ATOM   1601 C  CB   A SER A 1 85  ? -0.31300  -7.57900  -1.47000  0.700 20.51000 ? 85  SER A CB   1 
ATOM   1602 C  CB   B SER A 1 85  ? -0.42800  -7.33200  -1.68500  0.300 23.63000 ? 85  SER A CB   1 
ATOM   1603 O  OG   A SER A 1 85  ? 0.63900   -6.77800  -2.12800  0.700 23.62000 ? 85  SER A OG   1 
ATOM   1604 O  OG   B SER A 1 85  ? 0.43800   -8.23900  -1.03300  0.300 26.52000 ? 85  SER A OG   1 
ATOM   1605 H  H    A SER A 1 85  ? -1.87600  -9.28600  -0.95600  0.700 26.02000 ? 85  SER A H    1 
ATOM   1606 H  H    B SER A 1 85  ? -1.92800  -9.12300  -0.93800  0.300 26.02000 ? 85  SER A H    1 
ATOM   1607 H  HA   A SER A 1 85  ? -1.88400  -7.43500  -2.82300  0.700 26.02000 ? 85  SER A HA   1 
ATOM   1608 H  HA   B SER A 1 85  ? -2.06300  -7.40900  -2.91300  0.300 27.18000 ? 85  SER A HA   1 
ATOM   1609 H  HB2  A SER A 1 85  ? -0.77700  -7.03900  -0.81200  0.700 24.64000 ? 85  SER A HB2  1 
ATOM   1610 H  HB2  B SER A 1 85  ? 0.09900   -6.75000  -2.25500  0.300 28.38000 ? 85  SER A HB2  1 
ATOM   1611 H  HB3  A SER A 1 85  ? 0.14400   -8.31500  -1.03400  0.700 24.64000 ? 85  SER A HB3  1 
ATOM   1612 H  HB3  B SER A 1 85  ? -0.89600  -6.80800  -1.01700  0.300 28.38000 ? 85  SER A HB3  1 
ATOM   1613 H  HG   A SER A 1 85  ? 1.32500   -6.69600  -1.65100  0.700 28.36000 ? 85  SER A HG   1 
ATOM   1614 H  HG   B SER A 1 85  ? 0.79900   -8.74800  -1.59600  0.300 31.85000 ? 85  SER A HG   1 
ATOM   1615 N  N    . SER A 1 86  ? -0.28300  -7.98200  -4.65600  1.000 23.93000 ? 86  SER A N    1 
ATOM   1616 C  CA   . SER A 1 86  ? 0.56000   -8.49400  -5.73500  1.000 24.58000 ? 86  SER A CA   1 
ATOM   1617 C  C    . SER A 1 86  ? 1.96400   -8.83400  -5.24400  1.000 23.64000 ? 86  SER A C    1 
ATOM   1618 O  O    . SER A 1 86  ? 2.66400   -9.63200  -5.87900  1.000 32.02000 ? 86  SER A O    1 
ATOM   1619 C  CB   . SER A 1 86  ? 0.65500   -7.45800  -6.86500  1.000 27.82000 ? 86  SER A CB   1 
ATOM   1620 O  OG   . SER A 1 86  ? 0.98300   -6.19100  -6.33100  1.000 35.73000 ? 86  SER A OG   1 
ATOM   1621 H  H    . SER A 1 86  ? -0.54300  -7.16600  -4.74200  1.000 28.74000 ? 86  SER A H    1 
ATOM   1622 H  HA   . SER A 1 86  ? 0.15400   -9.29900  -6.09300  1.000 29.52000 ? 86  SER A HA   1 
ATOM   1623 H  HB2  . SER A 1 86  ? 1.34500   -7.73000  -7.49000  1.000 33.41000 ? 86  SER A HB2  1 
ATOM   1624 H  HB3  . SER A 1 86  ? -0.20000  -7.40200  -7.31900  1.000 33.41000 ? 86  SER A HB3  1 
ATOM   1625 H  HG   . SER A 1 86  ? 1.02200   -5.62100  -6.94700  1.000 42.90000 ? 86  SER A HG   1 
ATOM   1626 N  N    . ASP A 1 87  ? 2.38400   -8.22500  -4.14300  1.000 21.88000 ? 87  ASP A N    1 
ATOM   1627 C  CA   . ASP A 1 87  ? 3.62600   -8.53600  -3.44400  1.000 23.77000 ? 87  ASP A CA   1 
ATOM   1628 C  C    . ASP A 1 87  ? 3.37200   -9.70800  -2.50400  1.000 23.80000 ? 87  ASP A C    1 
ATOM   1629 O  O    . ASP A 1 87  ? 2.56900   -9.58400  -1.57500  1.000 24.38000 ? 87  ASP A O    1 
ATOM   1630 C  CB   . ASP A 1 87  ? 4.01300   -7.29100  -2.64500  1.000 31.78000 ? 87  ASP A CB   1 
ATOM   1631 C  CG   . ASP A 1 87  ? 5.39500   -7.38200  -1.99800  1.000 44.10000 ? 87  ASP A CG   1 
ATOM   1632 O  OD1  . ASP A 1 87  ? 5.88900   -8.49200  -1.72600  1.000 32.00000 ? 87  ASP A OD1  1 
ATOM   1633 O  OD2  . ASP A 1 87  ? 6.00200   -6.31400  -1.76300  1.000 66.16000 ? 87  ASP A OD2  1 
ATOM   1634 H  H    . ASP A 1 87  ? 1.94500   -7.59400  -3.75900  1.000 26.28000 ? 87  ASP A H    1 
ATOM   1635 H  HA   . ASP A 1 87  ? 4.33700   -8.78100  -4.05600  1.000 28.54000 ? 87  ASP A HA   1 
ATOM   1636 H  HB2  . ASP A 1 87  ? 4.01600   -6.52600  -3.24000  1.000 38.16000 ? 87  ASP A HB2  1 
ATOM   1637 H  HB3  . ASP A 1 87  ? 3.36300   -7.15900  -1.93700  1.000 38.16000 ? 87  ASP A HB3  1 
ATOM   1638 N  N    . ILE A 1 88  ? 4.04600   -10.83800 -2.74500  1.000 18.98000 ? 88  ILE A N    1 
ATOM   1639 C  CA   . ILE A 1 88  ? 3.77000   -12.06000 -1.98200  1.000 18.71000 ? 88  ILE A CA   1 
ATOM   1640 C  C    . ILE A 1 88  ? 4.55100   -12.16900 -0.68200  1.000 20.39000 ? 88  ILE A C    1 
ATOM   1641 O  O    . ILE A 1 88  ? 4.47300   -13.19700 0.00800   1.000 19.33000 ? 88  ILE A O    1 
ATOM   1642 C  CB   . ILE A 1 88  ? 3.97500   -13.33400 -2.82700  1.000 17.25000 ? 88  ILE A CB   1 
ATOM   1643 C  CG1  . ILE A 1 88  ? 5.45800   -13.53000 -3.18900  1.000 23.26000 ? 88  ILE A CG1  1 
ATOM   1644 C  CG2  . ILE A 1 88  ? 3.08200   -13.30100 -4.03600  1.000 23.24000 ? 88  ILE A CG2  1 
ATOM   1645 C  CD1  . ILE A 1 88  ? 5.75200   -14.91600 -3.77900  1.000 28.80000 ? 88  ILE A CD1  1 
ATOM   1646 H  H    . ILE A 1 88  ? 4.66100   -10.92200 -3.34000  1.000 22.80000 ? 88  ILE A H    1 
ATOM   1647 H  HA   . ILE A 1 88  ? 2.83900   -11.97600 -1.72500  1.000 22.48000 ? 88  ILE A HA   1 
ATOM   1648 H  HB   . ILE A 1 88  ? 3.72000   -14.10600 -2.29800  1.000 20.72000 ? 88  ILE A HB   1 
ATOM   1649 H  HG12 . ILE A 1 88  ? 5.71200   -12.86500 -3.84700  1.000 27.93000 ? 88  ILE A HG12 1 
ATOM   1650 H  HG13 . ILE A 1 88  ? 5.99400   -13.42600 -2.38800  1.000 27.93000 ? 88  ILE A HG13 1 
ATOM   1651 H  HG21 . ILE A 1 88  ? 3.15500   -14.14600 -4.50600  1.000 27.91000 ? 88  ILE A HG21 1 
ATOM   1652 H  HG22 . ILE A 1 88  ? 2.16600   -13.16000 -3.74900  1.000 27.91000 ? 88  ILE A HG22 1 
ATOM   1653 H  HG23 . ILE A 1 88  ? 3.36200   -12.57500 -4.61600  1.000 27.91000 ? 88  ILE A HG23 1 
ATOM   1654 H  HD11 . ILE A 1 88  ? 6.68300   -14.95300 -4.05000  1.000 34.58000 ? 88  ILE A HD11 1 
ATOM   1655 H  HD12 . ILE A 1 88  ? 5.57700   -15.59000 -3.10300  1.000 34.58000 ? 88  ILE A HD12 1 
ATOM   1656 H  HD13 . ILE A 1 88  ? 5.17800   -15.06100 -4.54700  1.000 34.58000 ? 88  ILE A HD13 1 
ATOM   1657 N  N    . THR A 1 89  ? 5.29600   -11.12400 -0.29900  1.000 21.44000 ? 89  THR A N    1 
ATOM   1658 C  CA   . THR A 1 89  ? 6.11900   -11.20400 0.90500   1.000 20.12000 ? 89  THR A CA   1 
ATOM   1659 C  C    . THR A 1 89  ? 5.32300   -11.69400 2.11700   1.000 19.92000 ? 89  THR A C    1 
ATOM   1660 O  O    . THR A 1 89  ? 5.75700   -12.60100 2.84000   1.000 21.44000 ? 89  THR A O    1 
ATOM   1661 C  CB   . THR A 1 89  ? 6.73000   -9.82800  1.18500   1.000 25.40000 ? 89  THR A CB   1 
ATOM   1662 O  OG1  . THR A 1 89  ? 7.53900   -9.44400  0.07300   1.000 27.19000 ? 89  THR A OG1  1 
ATOM   1663 C  CG2  . THR A 1 89  ? 7.60000   -9.87300  2.39200   1.000 28.82000 ? 89  THR A CG2  1 
ATOM   1664 H  H    . THR A 1 89  ? 5.34000   -10.37200 -0.71300  1.000 25.75000 ? 89  THR A H    1 
ATOM   1665 H  HA   . THR A 1 89  ? 6.83100   -11.84400 0.75300   1.000 24.17000 ? 89  THR A HA   1 
ATOM   1666 H  HB   . THR A 1 89  ? 6.01900   -9.18600  1.33300   1.000 30.50000 ? 89  THR A HB   1 
ATOM   1667 H  HG1  . THR A 1 89  ? 8.35200   -9.50800  0.27300   1.000 32.65000 ? 89  THR A HG1  1 
ATOM   1668 H  HG21 . THR A 1 89  ? 8.10200   -9.04700  2.46900   1.000 34.60000 ? 89  THR A HG21 1 
ATOM   1669 H  HG22 . THR A 1 89  ? 7.05700   -9.98700  3.18800   1.000 34.60000 ? 89  THR A HG22 1 
ATOM   1670 H  HG23 . THR A 1 89  ? 8.22200   -10.61400 2.32500   1.000 34.60000 ? 89  THR A HG23 1 
ATOM   1671 N  N    . ALA A 1 90  ? 4.16800   -11.08900 2.39100   1.000 19.68000 ? 90  ALA A N    1 
ATOM   1672 C  CA   . ALA A 1 90  ? 3.44700   -11.46200 3.60000   1.000 19.84000 ? 90  ALA A CA   1 
ATOM   1673 C  C    . ALA A 1 90  ? 2.97600   -12.90800 3.54400   1.000 18.55000 ? 90  ALA A C    1 
ATOM   1674 O  O    . ALA A 1 90  ? 3.00700   -13.61900 4.56000   1.000 19.79000 ? 90  ALA A O    1 
ATOM   1675 C  CB   . ALA A 1 90  ? 2.27800   -10.50500 3.81600   1.000 23.44000 ? 90  ALA A CB   1 
ATOM   1676 H  H    . ALA A 1 90  ? 3.79600   -10.48200 1.90900   1.000 23.64000 ? 90  ALA A H    1 
ATOM   1677 H  HA   . ALA A 1 90  ? 4.04100   -11.38200 4.36200   1.000 23.83000 ? 90  ALA A HA   1 
ATOM   1678 H  HB1  . ALA A 1 90  ? 1.72600   -10.84000 4.54000   1.000 28.15000 ? 90  ALA A HB1  1 
ATOM   1679 H  HB2  . ALA A 1 90  ? 2.62500   -9.62800  4.04300   1.000 28.15000 ? 90  ALA A HB2  1 
ATOM   1680 H  HB3  . ALA A 1 90  ? 1.75700   -10.45400 2.99900   1.000 28.15000 ? 90  ALA A HB3  1 
ATOM   1681 N  N    . SER A 1 91  ? 2.50900   -13.35500 2.37800   1.000 18.11000 ? 91  SER A N    1 
ATOM   1682 C  CA   . SER A 1 91  ? 2.09300   -14.74700 2.22800   1.000 16.03000 ? 91  SER A CA   1 
ATOM   1683 C  C    . SER A 1 91  ? 3.25400   -15.70100 2.47000   1.000 15.88000 ? 91  SER A C    1 
ATOM   1684 O  O    . SER A 1 91  ? 3.10200   -16.71300 3.16900   1.000 17.80000 ? 91  SER A O    1 
ATOM   1685 C  CB   . SER A 1 91  ? 1.50000   -14.96900 0.84600   1.000 18.03000 ? 91  SER A CB   1 
ATOM   1686 O  OG   . SER A 1 91  ? 0.19300   -14.43700 0.78800   1.000 18.60000 ? 91  SER A OG   1 
ATOM   1687 H  H    . SER A 1 91  ? 2.42400   -12.87900 1.66700   1.000 21.76000 ? 91  SER A H    1 
ATOM   1688 H  HA   . SER A 1 91  ? 1.40600   -14.93500 2.88700   1.000 19.26000 ? 91  SER A HA   1 
ATOM   1689 H  HB2  . SER A 1 91  ? 2.05500   -14.52500 0.18600   1.000 21.66000 ? 91  SER A HB2  1 
ATOM   1690 H  HB3  . SER A 1 91  ? 1.46500   -15.92100 0.66400   1.000 21.66000 ? 91  SER A HB3  1 
ATOM   1691 H  HG   . SER A 1 91  ? -0.09400  -14.46800 -0.00100  1.000 22.34000 ? 91  SER A HG   1 
ATOM   1692 N  N    . VAL A 1 92  ? 4.41700   -15.40000 1.89100   1.000 16.67000 ? 92  VAL A N    1 
ATOM   1693 C  CA   . VAL A 1 92  ? 5.58900   -16.26100 2.05000   1.000 17.67000 ? 92  VAL A CA   1 
ATOM   1694 C  C    . VAL A 1 92  ? 6.04400   -16.30700 3.49800   1.000 19.83000 ? 92  VAL A C    1 
ATOM   1695 O  O    . VAL A 1 92  ? 6.32700   -17.38200 4.04500   1.000 18.29000 ? 92  VAL A O    1 
ATOM   1696 C  CB   . VAL A 1 92  ? 6.72200   -15.80900 1.10800   1.000 19.65000 ? 92  VAL A CB   1 
ATOM   1697 C  CG1  . VAL A 1 92  ? 8.00000   -16.59700 1.39100   1.000 26.68000 ? 92  VAL A CG1  1 
ATOM   1698 C  CG2  . VAL A 1 92  ? 6.32500   -16.02600 -0.31100  1.000 23.94000 ? 92  VAL A CG2  1 
ATOM   1699 H  H    . VAL A 1 92  ? 4.55400   -14.70600 1.40200   1.000 20.03000 ? 92  VAL A H    1 
ATOM   1700 H  HA   . VAL A 1 92  ? 5.33300   -17.16300 1.80200   1.000 21.22000 ? 92  VAL A HA   1 
ATOM   1701 H  HB   . VAL A 1 92  ? 6.88900   -14.86600 1.25700   1.000 23.60000 ? 92  VAL A HB   1 
ATOM   1702 H  HG11 . VAL A 1 92  ? 8.67400   -16.35100 0.73800   1.000 32.04000 ? 92  VAL A HG11 1 
ATOM   1703 H  HG12 . VAL A 1 92  ? 8.31100   -16.38200 2.28500   1.000 32.04000 ? 92  VAL A HG12 1 
ATOM   1704 H  HG13 . VAL A 1 92  ? 7.80800   -17.54500 1.32700   1.000 32.04000 ? 92  VAL A HG13 1 
ATOM   1705 H  HG21 . VAL A 1 92  ? 7.03700   -15.71100 -0.88900  1.000 28.75000 ? 92  VAL A HG21 1 
ATOM   1706 H  HG22 . VAL A 1 92  ? 6.17500   -16.97300 -0.45600  1.000 28.75000 ? 92  VAL A HG22 1 
ATOM   1707 H  HG23 . VAL A 1 92  ? 5.51100   -15.53000 -0.49000  1.000 28.75000 ? 92  VAL A HG23 1 
ATOM   1708 N  N    . ASN A 1 93  ? 6.11400   -15.14800 4.15700   1.000 18.17000 ? 93  ASN A N    1 
ATOM   1709 C  CA   . ASN A 1 93  ? 6.60400   -15.11300 5.53200   1.000 19.40000 ? 93  ASN A CA   1 
ATOM   1710 C  C    . ASN A 1 93  ? 5.64100   -15.82000 6.46900   1.000 16.78000 ? 93  ASN A C    1 
ATOM   1711 O  O    . ASN A 1 93  ? 6.05600   -16.53900 7.38300   1.000 21.44000 ? 93  ASN A O    1 
ATOM   1712 C  CB   . ASN A 1 93  ? 6.81000   -13.66700 5.98700   1.000 27.67000 ? 93  ASN A CB   1 
ATOM   1713 C  CG   . ASN A 1 93  ? 8.06100   -13.05000 5.40000   1.000 39.62000 ? 93  ASN A CG   1 
ATOM   1714 O  OD1  . ASN A 1 93  ? 8.85500   -13.72900 4.74500   1.000 39.79000 ? 93  ASN A OD1  1 
ATOM   1715 N  ND2  . ASN A 1 93  ? 8.24000   -11.75100 5.62700   1.000 46.40000 ? 93  ASN A ND2  1 
ATOM   1716 H  H    . ASN A 1 93  ? 5.88700   -14.38300 3.83600   1.000 21.83000 ? 93  ASN A H    1 
ATOM   1717 H  HA   . ASN A 1 93  ? 7.46200   -15.56500 5.56600   1.000 23.31000 ? 93  ASN A HA   1 
ATOM   1718 H  HB2  . ASN A 1 93  ? 6.05000   -13.13500 5.70500   1.000 33.23000 ? 93  ASN A HB2  1 
ATOM   1719 H  HB3  . ASN A 1 93  ? 6.88900   -13.64700 6.95300   1.000 33.23000 ? 93  ASN A HB3  1 
ATOM   1720 H  HD21 . ASN A 1 93  ? 7.66100   -11.31100 6.08600   1.000 55.71000 ? 93  ASN A HD21 1 
ATOM   1721 H  HD22 . ASN A 1 93  ? 8.93500   -11.35200 5.31500   1.000 55.71000 ? 93  ASN A HD22 1 
ATOM   1722 N  N    . CYS A 1 94  ? 4.33900   -15.67800 6.22900   1.000 17.02000 ? 94  CYS A N    1 
ATOM   1723 C  CA   . CYS A 1 94  ? 3.37600   -16.40000 7.04500   1.000 16.16000 ? 94  CYS A CA   1 
ATOM   1724 C  C    . CYS A 1 94  ? 3.44500   -17.89900 6.76100   1.000 17.23000 ? 94  CYS A C    1 
ATOM   1725 O  O    . CYS A 1 94  ? 3.38000   -18.71700 7.68400   1.000 16.34000 ? 94  CYS A O    1 
ATOM   1726 C  CB   . CYS A 1 94  ? 1.95800   -15.84700 6.81000   1.000 17.37000 ? 94  CYS A CB   1 
ATOM   1727 S  SG   . CYS A 1 94  ? 0.69200   -16.50500 7.88700   1.000 18.82000 ? 94  CYS A SG   1 
ATOM   1728 H  H    . CYS A 1 94  ? 3.99800   -15.18200 5.61400   1.000 20.45000 ? 94  CYS A H    1 
ATOM   1729 H  HA   . CYS A 1 94  ? 3.58300   -16.26500 7.98300   1.000 19.42000 ? 94  CYS A HA   1 
ATOM   1730 H  HB2  . CYS A 1 94  ? 1.97900   -14.88600 6.94200   1.000 20.87000 ? 94  CYS A HB2  1 
ATOM   1731 H  HB3  . CYS A 1 94  ? 1.69800   -16.05000 5.89800   1.000 20.87000 ? 94  CYS A HB3  1 
ATOM   1732 N  N    . ALA A 1 95  ? 3.59200   -18.28000 5.49000   1.000 16.47000 ? 95  ALA A N    1 
ATOM   1733 C  CA   . ALA A 1 95  ? 3.72400   -19.70200 5.15000   1.000 16.75000 ? 95  ALA A CA   1 
ATOM   1734 C  C    . ALA A 1 95  ? 4.93200   -20.34900 5.82900   1.000 15.19000 ? 95  ALA A C    1 
ATOM   1735 O  O    . ALA A 1 95  ? 4.88200   -21.53900 6.15800   1.000 16.66000 ? 95  ALA A O    1 
ATOM   1736 C  CB   . ALA A 1 95  ? 3.82500   -19.86500 3.64200   1.000 16.00000 ? 95  ALA A CB   1 
ATOM   1737 H  H    . ALA A 1 95  ? 3.61900   -17.74700 4.81500   1.000 19.79000 ? 95  ALA A H    1 
ATOM   1738 H  HA   . ALA A 1 95  ? 2.92900   -20.16400 5.46000   1.000 20.12000 ? 95  ALA A HA   1 
ATOM   1739 H  HB1  . ALA A 1 95  ? 3.87200   -20.81000 3.42900   1.000 19.23000 ? 95  ALA A HB1  1 
ATOM   1740 H  HB2  . ALA A 1 95  ? 3.04000   -19.47300 3.22800   1.000 19.23000 ? 95  ALA A HB2  1 
ATOM   1741 H  HB3  . ALA A 1 95  ? 4.62400   -19.41500 3.32800   1.000 19.23000 ? 95  ALA A HB3  1 
ATOM   1742 N  N    . LYS A 1 96  ? 6.02900   -19.60700 6.02900   1.000 14.92000 ? 96  LYS A N    1 
ATOM   1743 C  CA   . LYS A 1 96  ? 7.17600   -20.17900 6.73000   1.000 15.73000 ? 96  LYS A CA   1 
ATOM   1744 C  C    . LYS A 1 96  ? 6.82200   -20.50600 8.16600   1.000 18.97000 ? 96  LYS A C    1 
ATOM   1745 O  O    . LYS A 1 96  ? 7.30100   -21.50000 8.72100   1.000 20.28000 ? 96  LYS A O    1 
ATOM   1746 C  CB   . LYS A 1 96  ? 8.32400   -19.18200 6.69600   1.000 17.70000 ? 96  LYS A CB   1 
ATOM   1747 C  CG   . LYS A 1 96  ? 9.00900   -19.06500 5.35100   1.000 20.07000 ? 96  LYS A CG   1 
ATOM   1748 C  CD   . LYS A 1 96  ? 10.11000  -18.00300 5.39200   1.000 23.32000 ? 96  LYS A CD   1 
ATOM   1749 C  CE   . LYS A 1 96  ? 10.77500  -17.89700 4.04400   1.000 26.70000 ? 96  LYS A CE   1 
ATOM   1750 N  NZ   . LYS A 1 96  ? 11.68000  -16.71900 3.93300   1.000 35.00000 ? 96  LYS A NZ   1 
ATOM   1751 H  H    . LYS A 1 96  ? 6.12900   -18.79200 5.77400   1.000 17.92000 ? 96  LYS A H    1 
ATOM   1752 H  HA   . LYS A 1 96  ? 7.45200   -20.99700 6.28800   1.000 18.90000 ? 96  LYS A HA   1 
ATOM   1753 H  HB2  . LYS A 1 96  ? 7.98000   -18.30500 6.92700   1.000 21.27000 ? 96  LYS A HB2  1 
ATOM   1754 H  HB3  . LYS A 1 96  ? 8.99300   -19.45700 7.34200   1.000 21.27000 ? 96  LYS A HB3  1 
ATOM   1755 H  HG2  . LYS A 1 96  ? 9.41100   -19.91600 5.11700   1.000 24.11000 ? 96  LYS A HG2  1 
ATOM   1756 H  HG3  . LYS A 1 96  ? 8.35900   -18.80900 4.67800   1.000 24.11000 ? 96  LYS A HG3  1 
ATOM   1757 H  HD2  . LYS A 1 96  ? 9.72500   -17.14200 5.61800   1.000 28.00000 ? 96  LYS A HD2  1 
ATOM   1758 H  HD3  . LYS A 1 96  ? 10.77800  -18.25000 6.05000   1.000 28.00000 ? 96  LYS A HD3  1 
ATOM   1759 H  HE2  . LYS A 1 96  ? 11.30300  -18.69500 3.88900   1.000 32.06000 ? 96  LYS A HE2  1 
ATOM   1760 H  HE3  . LYS A 1 96  ? 10.09100  -17.81300 3.36100   1.000 32.06000 ? 96  LYS A HE3  1 
ATOM   1761 H  HZ1  . LYS A 1 96  ? 12.04200  -16.68800 3.12100   1.000 42.02000 ? 96  LYS A HZ1  1 
ATOM   1762 H  HZ2  . LYS A 1 96  ? 11.22200  -15.96900 4.07400   1.000 42.02000 ? 96  LYS A HZ2  1 
ATOM   1763 H  HZ3  . LYS A 1 96  ? 12.33100  -16.77700 4.53800   1.000 42.02000 ? 96  LYS A HZ3  1 
ATOM   1764 N  N    . LYS A 1 97  ? 5.98200   -19.67900 8.79700   1.000 15.95000 ? 97  LYS A N    1 
ATOM   1765 C  CA   . LYS A 1 97  ? 5.52500   -20.00100 10.14800  1.000 17.68000 ? 97  LYS A CA   1 
ATOM   1766 C  C    . LYS A 1 97  ? 4.61200   -21.22800 10.15700  1.000 20.00000 ? 97  LYS A C    1 
ATOM   1767 O  O    . LYS A 1 97  ? 4.72500   -22.09100 11.03400  1.000 20.81000 ? 97  LYS A O    1 
ATOM   1768 C  CB   . LYS A 1 97  ? 4.82700   -18.79100 10.78800  1.000 20.21000 ? 97  LYS A CB   1 
ATOM   1769 C  CG   . LYS A 1 97  ? 5.76700   -17.60500 11.02800  1.000 39.80000 ? 97  LYS A CG   1 
ATOM   1770 C  CD   . LYS A 1 97  ? 5.03900   -16.36700 11.57800  1.000 73.36000 ? 97  LYS A CD   1 
ATOM   1771 C  CE   . LYS A 1 97  ? 5.99600   -15.18300 11.79800  1.000 75.17000 ? 97  LYS A CE   1 
ATOM   1772 N  NZ   . LYS A 1 97  ? 5.59400   -13.94300 11.06200  1.000 59.56000 ? 97  LYS A NZ   1 
ATOM   1773 H  H    . LYS A 1 97  ? 5.67200   -18.94600 8.47300   1.000 19.17000 ? 97  LYS A H    1 
ATOM   1774 H  HA   . LYS A 1 97  ? 6.30200   -20.20800 10.69000  1.000 21.24000 ? 97  LYS A HA   1 
ATOM   1775 H  HB2  . LYS A 1 97  ? 4.11500   -18.49200 10.20100  1.000 24.28000 ? 97  LYS A HB2  1 
ATOM   1776 H  HB3  . LYS A 1 97  ? 4.46000   -19.05800 11.64500  1.000 24.28000 ? 97  LYS A HB3  1 
ATOM   1777 H  HG2  . LYS A 1 97  ? 6.44500   -17.86400 11.67200  1.000 47.78000 ? 97  LYS A HG2  1 
ATOM   1778 H  HG3  . LYS A 1 97  ? 6.18500   -17.35800 10.18800  1.000 47.78000 ? 97  LYS A HG3  1 
ATOM   1779 H  HD2  . LYS A 1 97  ? 4.35800   -16.09100 10.94500  1.000 88.06000 ? 97  LYS A HD2  1 
ATOM   1780 H  HD3  . LYS A 1 97  ? 4.63100   -16.58800 12.42900  1.000 88.06000 ? 97  LYS A HD3  1 
ATOM   1781 H  HE2  . LYS A 1 97  ? 6.01900   -14.97100 12.74500  1.000 90.23000 ? 97  LYS A HE2  1 
ATOM   1782 H  HE3  . LYS A 1 97  ? 6.88200   -15.43500 11.49300  1.000 90.23000 ? 97  LYS A HE3  1 
ATOM   1783 H  HZ1  . LYS A 1 97  ? 6.18100   -13.29200 11.21800  1.000 71.50000 ? 97  LYS A HZ1  1 
ATOM   1784 H  HZ2  . LYS A 1 97  ? 5.56700   -14.10300 10.18700  1.000 71.50000 ? 97  LYS A HZ2  1 
ATOM   1785 H  HZ3  . LYS A 1 97  ? 4.78900   -13.67600 11.33200  1.000 71.50000 ? 97  LYS A HZ3  1 
ATOM   1786 N  N    . ILE A 1 98  ? 3.71000   -21.33000 9.18600   1.000 16.64000 ? 98  ILE A N    1 
ATOM   1787 C  CA   . ILE A 1 98  ? 2.78100   -22.44900 9.11200   1.000 16.16000 ? 98  ILE A CA   1 
ATOM   1788 C  C    . ILE A 1 98  ? 3.52700   -23.76300 8.91400   1.000 16.66000 ? 98  ILE A C    1 
ATOM   1789 O  O    . ILE A 1 98  ? 3.24400   -24.75800 9.58300   1.000 17.62000 ? 98  ILE A O    1 
ATOM   1790 C  CB   . ILE A 1 98  ? 1.76400   -22.21800 7.98600   1.000 15.89000 ? 98  ILE A CB   1 
ATOM   1791 C  CG1  . ILE A 1 98  ? 0.92600   -20.97100 8.28100   1.000 16.26000 ? 98  ILE A CG1  1 
ATOM   1792 C  CG2  . ILE A 1 98  ? 0.85600   -23.42000 7.81100   1.000 19.58000 ? 98  ILE A CG2  1 
ATOM   1793 C  CD1  . ILE A 1 98  ? 0.04400   -20.52700 7.13000   1.000 19.49000 ? 98  ILE A CD1  1 
ATOM   1794 H  H    . ILE A 1 98  ? 3.61400   -20.75800 8.55100   1.000 19.99000 ? 98  ILE A H    1 
ATOM   1795 H  HA   . ILE A 1 98  ? 2.30500   -22.50400 9.95600   1.000 19.42000 ? 98  ILE A HA   1 
ATOM   1796 H  HB   . ILE A 1 98  ? 2.25900   -22.08600 7.16200   1.000 19.09000 ? 98  ILE A HB   1 
ATOM   1797 H  HG12 . ILE A 1 98  ? 0.34900   -21.15700 9.03800   1.000 19.54000 ? 98  ILE A HG12 1 
ATOM   1798 H  HG13 . ILE A 1 98  ? 1.52500   -20.23800 8.49200   1.000 19.54000 ? 98  ILE A HG13 1 
ATOM   1799 H  HG21 . ILE A 1 98  ? 0.30100   -23.28400 7.02800   1.000 23.52000 ? 98  ILE A HG21 1 
ATOM   1800 H  HG22 . ILE A 1 98  ? 1.40200   -24.21400 7.69700   1.000 23.52000 ? 98  ILE A HG22 1 
ATOM   1801 H  HG23 . ILE A 1 98  ? 0.30000   -23.51200 8.60000   1.000 23.52000 ? 98  ILE A HG23 1 
ATOM   1802 H  HD11 . ILE A 1 98  ? 0.59100   -20.41500 6.33700   1.000 23.41000 ? 98  ILE A HD11 1 
ATOM   1803 H  HD12 . ILE A 1 98  ? -0.63300  -21.20300 6.97200   1.000 23.41000 ? 98  ILE A HD12 1 
ATOM   1804 H  HD13 . ILE A 1 98  ? -0.37800  -19.68500 7.36200   1.000 23.41000 ? 98  ILE A HD13 1 
ATOM   1805 N  N    . VAL A 1 99  ? 4.45600   -23.79700 7.95900   1.000 15.89000 ? 99  VAL A N    1 
ATOM   1806 C  CA   . VAL A 1 99  ? 5.14100   -25.04000 7.61800   1.000 18.05000 ? 99  VAL A CA   1 
ATOM   1807 C  C    . VAL A 1 99  ? 6.04100   -25.48800 8.74200   1.000 19.11000 ? 99  VAL A C    1 
ATOM   1808 O  O    . VAL A 1 99  ? 6.39900   -26.66700 8.80200   1.000 19.38000 ? 99  VAL A O    1 
ATOM   1809 C  CB   . VAL A 1 99  ? 5.88000   -24.86300 6.28200   1.000 15.08000 ? 99  VAL A CB   1 
ATOM   1810 C  CG1  . VAL A 1 99  ? 7.16300   -24.06500 6.40500   1.000 17.37000 ? 99  VAL A CG1  1 
ATOM   1811 C  CG2  . VAL A 1 99  ? 6.12100   -26.21100 5.61400   1.000 19.63000 ? 99  VAL A CG2  1 
ATOM   1812 H  H    . VAL A 1 99  ? 4.70700   -23.11700 7.49600   1.000 19.09000 ? 99  VAL A H    1 
ATOM   1813 H  HA   . VAL A 1 99  ? 4.49800   -25.75500 7.49100   1.000 21.68000 ? 99  VAL A HA   1 
ATOM   1814 H  HB   . VAL A 1 99  ? 5.30300   -24.33600 5.70700   1.000 18.12000 ? 99  VAL A HB   1 
ATOM   1815 H  HG11 . VAL A 1 99  ? 7.46900   -23.82100 5.51800   1.000 20.86000 ? 99  VAL A HG11 1 
ATOM   1816 H  HG12 . VAL A 1 99  ? 6.98900   -23.26600 6.92700   1.000 20.86000 ? 99  VAL A HG12 1 
ATOM   1817 H  HG13 . VAL A 1 99  ? 7.83200   -24.61000 6.84800   1.000 20.86000 ? 99  VAL A HG13 1 
ATOM   1818 H  HG21 . VAL A 1 99  ? 6.56000   -26.06700 4.76100   1.000 23.58000 ? 99  VAL A HG21 1 
ATOM   1819 H  HG22 . VAL A 1 99  ? 6.68400   -26.75200 6.18900   1.000 23.58000 ? 99  VAL A HG22 1 
ATOM   1820 H  HG23 . VAL A 1 99  ? 5.26800   -26.65200 5.47600   1.000 23.58000 ? 99  VAL A HG23 1 
ATOM   1821 N  N    . SER A 1 100 ? 6.38400   -24.58600 9.65600   1.000 18.11000 ? 100 SER A N    1 
ATOM   1822 C  CA   . SER A 1 100 ? 7.21100   -24.90100 10.81100  1.000 22.12000 ? 100 SER A CA   1 
ATOM   1823 C  C    . SER A 1 100 ? 6.39700   -25.31500 12.03600  1.000 24.39000 ? 100 SER A C    1 
ATOM   1824 O  O    . SER A 1 100 ? 6.99400   -25.57300 13.09100  1.000 27.81000 ? 100 SER A O    1 
ATOM   1825 C  CB   . SER A 1 100 ? 8.06100   -23.67200 11.16900  1.000 23.26000 ? 100 SER A CB   1 
ATOM   1826 O  OG   . SER A 1 100 ? 8.90500   -23.25600 10.10400  1.000 25.33000 ? 100 SER A OG   1 
ATOM   1827 H  H    . SER A 1 100 ? 6.14100   -23.76200 9.62700   1.000 21.76000 ? 100 SER A H    1 
ATOM   1828 H  HA   . SER A 1 100 ? 7.79900   -25.63900 10.58500  1.000 26.57000 ? 100 SER A HA   1 
ATOM   1829 H  HB2  . SER A 1 100 ? 7.46500   -22.94100 11.39400  1.000 27.93000 ? 100 SER A HB2  1 
ATOM   1830 H  HB3  . SER A 1 100 ? 8.61600   -23.89400 11.93300  1.000 27.93000 ? 100 SER A HB3  1 
ATOM   1831 H  HG   . SER A 1 100 ? 8.46900   -22.78900 9.55800   1.000 30.41000 ? 100 SER A HG   1 
ATOM   1832 N  N    A ASP A 1 101 ? 5.07000   -25.42200 11.91200  0.440 22.41000 ? 101 ASP A N    1 
ATOM   1833 N  N    B ASP A 1 101 ? 5.06700   -25.40200 11.93100  0.560 22.37000 ? 101 ASP A N    1 
ATOM   1834 C  CA   A ASP A 1 101 ? 4.16700   -25.62500 13.04100  0.440 28.84000 ? 101 ASP A CA   1 
ATOM   1835 C  CA   B ASP A 1 101 ? 4.20300   -25.62200 13.09300  0.560 28.80000 ? 101 ASP A CA   1 
ATOM   1836 C  C    A ASP A 1 101 ? 3.97500   -27.08800 13.40800  0.440 26.85000 ? 101 ASP A C    1 
ATOM   1837 C  C    B ASP A 1 101 ? 4.24400   -27.05600 13.60700  0.560 28.59000 ? 101 ASP A C    1 
ATOM   1838 O  O    A ASP A 1 101 ? 3.06300   -27.40500 14.18300  0.440 25.68000 ? 101 ASP A O    1 
ATOM   1839 O  O    B ASP A 1 101 ? 3.83900   -27.30000 14.74800  0.560 26.05000 ? 101 ASP A O    1 
ATOM   1840 C  CB   A ASP A 1 101 ? 2.80000   -24.97700 12.76000  0.440 29.64000 ? 101 ASP A CB   1 
ATOM   1841 C  CB   B ASP A 1 101 ? 2.75300   -25.25600 12.74400  0.560 28.50000 ? 101 ASP A CB   1 
ATOM   1842 C  CG   A ASP A 1 101 ? 1.83900   -25.89000 11.97900  0.440 32.87000 ? 101 ASP A CG   1 
ATOM   1843 C  CG   B ASP A 1 101 ? 1.95500   -24.76800 13.94600  0.560 33.05000 ? 101 ASP A CG   1 
ATOM   1844 O  OD1  A ASP A 1 101 ? 2.24600   -26.95800 11.46100  0.440 29.13000 ? 101 ASP A OD1  1 
ATOM   1845 O  OD1  B ASP A 1 101 ? 2.53100   -24.10200 14.83300  0.560 40.73000 ? 101 ASP A OD1  1 
ATOM   1846 O  OD2  A ASP A 1 101 ? 0.64800   -25.52400 11.87100  0.440 37.57000 ? 101 ASP A OD2  1 
ATOM   1847 O  OD2  B ASP A 1 101 ? 0.73800   -25.04400 13.99200  0.560 39.91000 ? 101 ASP A OD2  1 
ATOM   1848 H  H    A ASP A 1 101 ? 4.65900   -25.37900 11.15700  0.440 26.92000 ? 101 ASP A H    1 
ATOM   1849 H  H    B ASP A 1 101 ? 4.63500   -25.33700 11.19000  0.560 26.87000 ? 101 ASP A H    1 
ATOM   1850 H  HA   A ASP A 1 101 ? 4.55400   -25.18000 13.81100  0.440 34.63000 ? 101 ASP A HA   1 
ATOM   1851 H  HA   B ASP A 1 101 ? 4.51200   -25.04200 13.80700  0.560 34.59000 ? 101 ASP A HA   1 
ATOM   1852 H  HB2  A ASP A 1 101 ? 2.37900   -24.75500 13.60500  0.440 35.60000 ? 101 ASP A HB2  1 
ATOM   1853 H  HB2  B ASP A 1 101 ? 2.75800   -24.54800 12.08100  0.560 34.22000 ? 101 ASP A HB2  1 
ATOM   1854 H  HB3  A ASP A 1 101 ? 2.93700   -24.17200 12.23600  0.440 35.60000 ? 101 ASP A HB3  1 
ATOM   1855 H  HB3  B ASP A 1 101 ? 2.30700   -26.04100 12.38800  0.560 34.22000 ? 101 ASP A HB3  1 
ATOM   1856 N  N    . GLY A 1 102 ? 4.75000   -27.99800 12.81800  1.000 25.48000 ? 102 GLY A N    1 
ATOM   1857 C  CA   . GLY A 1 102 ? 4.76700   -29.39200 13.21900  1.000 25.43000 ? 102 GLY A CA   1 
ATOM   1858 C  C    . GLY A 1 102 ? 4.31700   -30.35500 12.13600  1.000 25.60000 ? 102 GLY A C    1 
ATOM   1859 O  O    . GLY A 1 102 ? 4.84100   -31.47300 12.08400  1.000 23.71000 ? 102 GLY A O    1 
ATOM   1860 H  H    . GLY A 1 102 ? 5.09200   -27.86000 12.04100  1.000 30.60000 ? 102 GLY A H    1 
ATOM   1861 H  HA2  . GLY A 1 102 ? 5.67100   -29.63300 13.47700  1.000 30.54000 ? 102 GLY A HA2  1 
ATOM   1862 H  HA3  . GLY A 1 102 ? 4.18000   -29.50600 13.98300  1.000 30.54000 ? 102 GLY A HA3  1 
ATOM   1863 N  N    . ASN A 1 103 ? 3.37900   -29.96300 11.26900  1.000 21.98000 ? 103 ASN A N    1 
ATOM   1864 C  CA   . ASN A 1 103 ? 2.82800   -30.87700 10.27600  1.000 19.60000 ? 103 ASN A CA   1 
ATOM   1865 C  C    . ASN A 1 103 ? 3.37600   -30.61500 8.87600   1.000 14.98000 ? 103 ASN A C    1 
ATOM   1866 O  O    . ASN A 1 103 ? 2.94000   -31.26300 7.91200   1.000 17.47000 ? 103 ASN A O    1 
ATOM   1867 C  CB   . ASN A 1 103 ? 1.30200   -30.82200 10.25900  1.000 25.86000 ? 103 ASN A CB   1 
ATOM   1868 C  CG   . ASN A 1 103 ? 0.67200   -31.48000 11.48400  1.000 39.18000 ? 103 ASN A CG   1 
ATOM   1869 O  OD1  . ASN A 1 103 ? 1.33200   -32.20500 12.22600  1.000 41.33000 ? 103 ASN A OD1  1 
ATOM   1870 N  ND2  . ASN A 1 103 ? -0.61900  -31.23600 11.68200  1.000 83.11000 ? 103 ASN A ND2  1 
ATOM   1871 H  H    . ASN A 1 103 ? 3.04700   -29.17000 11.24100  1.000 26.39000 ? 103 ASN A H    1 
ATOM   1872 H  HA   . ASN A 1 103 ? 3.07500   -31.77900 10.53400  1.000 23.55000 ? 103 ASN A HA   1 
ATOM   1873 H  HB2  . ASN A 1 103 ? 1.02000   -29.89400 10.23900  1.000 31.05000 ? 103 ASN A HB2  1 
ATOM   1874 H  HB3  . ASN A 1 103 ? 0.97800   -31.28400 9.47000   1.000 31.05000 ? 103 ASN A HB3  1 
ATOM   1875 H  HD21 . ASN A 1 103 ? -1.05000  -30.73100 11.13500  1.000 99.76000 ? 103 ASN A HD21 1 
ATOM   1876 H  HD22 . ASN A 1 103 ? -1.02300  -31.58200 12.35800  1.000 99.76000 ? 103 ASN A HD22 1 
ATOM   1877 N  N    . GLY A 1 104 ? 4.35600   -29.74300 8.75900   1.000 14.86000 ? 104 GLY A N    1 
ATOM   1878 C  CA   . GLY A 1 104 ? 4.97600   -29.46500 7.47300   1.000 14.41000 ? 104 GLY A CA   1 
ATOM   1879 C  C    . GLY A 1 104 ? 3.92300   -28.99100 6.50000   1.000 15.25000 ? 104 GLY A C    1 
ATOM   1880 O  O    . GLY A 1 104 ? 2.98400   -28.27800 6.86400   1.000 15.46000 ? 104 GLY A O    1 
ATOM   1881 H  H    . GLY A 1 104 ? 4.68800   -29.29200 9.41200   1.000 17.85000 ? 104 GLY A H    1 
ATOM   1882 H  HA2  . GLY A 1 104 ? 5.65200   -28.77600 7.57200   1.000 17.31000 ? 104 GLY A HA2  1 
ATOM   1883 H  HA3  . GLY A 1 104 ? 5.39400   -30.26800 7.12400   1.000 17.31000 ? 104 GLY A HA3  1 
ATOM   1884 N  N    . MET A 1 105 ? 4.06000   -29.41600 5.25100   1.000 13.25000 ? 105 MET A N    1 
ATOM   1885 C  CA   . MET A 1 105 ? 3.13800   -28.94300 4.21300   1.000 13.77000 ? 105 MET A CA   1 
ATOM   1886 C  C    . MET A 1 105 ? 1.80100   -29.65500 4.24800   1.000 13.61000 ? 105 MET A C    1 
ATOM   1887 O  O    . MET A 1 105 ? 0.88900   -29.26100 3.51700   1.000 13.79000 ? 105 MET A O    1 
ATOM   1888 C  CB   . MET A 1 105 ? 3.77900   -29.03200 2.82800   1.000 13.37000 ? 105 MET A CB   1 
ATOM   1889 C  CG   . MET A 1 105 ? 4.79100   -27.90100 2.59200   1.000 13.29000 ? 105 MET A CG   1 
ATOM   1890 S  SD   . MET A 1 105 ? 5.21800   -27.61900 0.85100   1.000 16.45000 ? 105 MET A SD   1 
ATOM   1891 C  CE   . MET A 1 105 ? 3.74100   -26.76300 0.31000   1.000 17.39000 ? 105 MET A CE   1 
ATOM   1892 H  H    . MET A 1 105 ? 4.66400   -29.96500 4.98000   1.000 15.92000 ? 105 MET A H    1 
ATOM   1893 H  HA   . MET A 1 105 ? 2.97200   -27.99800 4.36100   1.000 16.54000 ? 105 MET A HA   1 
ATOM   1894 H  HB2  . MET A 1 105 ? 4.24400   -29.87900 2.74500   1.000 16.07000 ? 105 MET A HB2  1 
ATOM   1895 H  HB3  . MET A 1 105 ? 3.08700   -28.96600 2.15100   1.000 16.07000 ? 105 MET A HB3  1 
ATOM   1896 H  HG2  . MET A 1 105 ? 4.41800   -27.07500 2.93800   1.000 15.98000 ? 105 MET A HG2  1 
ATOM   1897 H  HG3  . MET A 1 105 ? 5.61100   -28.11800 3.06200   1.000 15.98000 ? 105 MET A HG3  1 
ATOM   1898 H  HE1  . MET A 1 105 ? 3.84600   -26.50900 -0.62000  1.000 20.89000 ? 105 MET A HE1  1 
ATOM   1899 H  HE2  . MET A 1 105 ? 2.97900   -27.35500 0.40700   1.000 20.89000 ? 105 MET A HE2  1 
ATOM   1900 H  HE3  . MET A 1 105 ? 3.61600   -25.97200 0.85700   1.000 20.89000 ? 105 MET A HE3  1 
ATOM   1901 N  N    . ASN A 1 106 ? 1.63800   -30.65900 5.11600   1.000 13.49000 ? 106 ASN A N    1 
ATOM   1902 C  CA   . ASN A 1 106 ? 0.32100   -31.26700 5.27400   1.000 12.94000 ? 106 ASN A CA   1 
ATOM   1903 C  C    . ASN A 1 106 ? -0.70900  -30.28300 5.81400   1.000 14.05000 ? 106 ASN A C    1 
ATOM   1904 O  O    . ASN A 1 106 ? -1.90200  -30.56800 5.69900   1.000 17.08000 ? 106 ASN A O    1 
ATOM   1905 C  CB   . ASN A 1 106 ? 0.43000   -32.45500 6.23200   1.000 14.99000 ? 106 ASN A CB   1 
ATOM   1906 C  CG   . ASN A 1 106 ? 1.27600   -33.58200 5.68400   1.000 13.44000 ? 106 ASN A CG   1 
ATOM   1907 O  OD1  . ASN A 1 106 ? 0.94400   -34.26200 4.69800   1.000 16.99000 ? 106 ASN A OD1  1 
ATOM   1908 N  ND2  . ASN A 1 106 ? 2.43000   -33.76300 6.29500   1.000 17.15000 ? 106 ASN A ND2  1 
ATOM   1909 H  H    . ASN A 1 106 ? 2.25700   -30.99400 5.61000   1.000 16.21000 ? 106 ASN A H    1 
ATOM   1910 H  HA   . ASN A 1 106 ? 0.01200   -31.58600 4.41200   1.000 15.55000 ? 106 ASN A HA   1 
ATOM   1911 H  HB2  . ASN A 1 106 ? 0.83300   -32.15500 7.06100   1.000 18.01000 ? 106 ASN A HB2  1 
ATOM   1912 H  HB3  . ASN A 1 106 ? -0.45900  -32.80500 6.40200   1.000 18.01000 ? 106 ASN A HB3  1 
ATOM   1913 H  HD21 . ASN A 1 106 ? 2.96100   -34.38800 6.03400   1.000 20.60000 ? 106 ASN A HD21 1 
ATOM   1914 H  HD22 . ASN A 1 106 ? 2.65200   -33.25700 6.95300   1.000 20.60000 ? 106 ASN A HD22 1 
ATOM   1915 N  N    . ALA A 1 107 ? -0.27300  -29.11800 6.29800   1.000 14.21000 ? 107 ALA A N    1 
ATOM   1916 C  CA   . ALA A 1 107 ? -1.19900  -28.06200 6.68700   1.000 15.98000 ? 107 ALA A CA   1 
ATOM   1917 C  C    . ALA A 1 107 ? -2.05800  -27.62700 5.51600   1.000 16.86000 ? 107 ALA A C    1 
ATOM   1918 O  O    . ALA A 1 107 ? -3.17800  -27.14500 5.71500   1.000 19.31000 ? 107 ALA A O    1 
ATOM   1919 C  CB   . ALA A 1 107 ? -0.40300  -26.86500 7.20700   1.000 19.05000 ? 107 ALA A CB   1 
ATOM   1920 H  H    . ALA A 1 107 ? 0.55600   -28.91600 6.41000   1.000 17.07000 ? 107 ALA A H    1 
ATOM   1921 H  HA   . ALA A 1 107 ? -1.78100  -28.38800 7.39100   1.000 19.20000 ? 107 ALA A HA   1 
ATOM   1922 H  HB1  . ALA A 1 107 ? -1.02200  -26.17600 7.49700   1.000 22.88000 ? 107 ALA A HB1  1 
ATOM   1923 H  HB2  . ALA A 1 107 ? 0.14600   -27.15100 7.95300   1.000 22.88000 ? 107 ALA A HB2  1 
ATOM   1924 H  HB3  . ALA A 1 107 ? 0.15900   -26.52500 6.49300   1.000 22.88000 ? 107 ALA A HB3  1 
ATOM   1925 N  N    . TRP A 1 108 ? -1.55600  -27.75300 4.28600   1.000 14.11000 ? 108 TRP A N    1 
ATOM   1926 C  CA   . TRP A 1 108 ? -2.30700  -27.41300 3.08500   1.000 14.86000 ? 108 TRP A CA   1 
ATOM   1927 C  C    . TRP A 1 108 ? -2.90400  -28.71700 2.56000   1.000 16.71000 ? 108 TRP A C    1 
ATOM   1928 O  O    . TRP A 1 108 ? -2.19200  -29.57300 2.01100   1.000 15.03000 ? 108 TRP A O    1 
ATOM   1929 C  CB   . TRP A 1 108 ? -1.40300  -26.79200 2.03600   1.000 13.45000 ? 108 TRP A CB   1 
ATOM   1930 C  CG   . TRP A 1 108 ? -1.02400  -25.40000 2.34500   1.000 14.01000 ? 108 TRP A CG   1 
ATOM   1931 C  CD1  . TRP A 1 108 ? -1.71600  -24.26400 2.00400   1.000 16.63000 ? 108 TRP A CD1  1 
ATOM   1932 C  CD2  . TRP A 1 108 ? 0.15600   -24.93500 3.04000   1.000 12.88000 ? 108 TRP A CD2  1 
ATOM   1933 N  NE1  . TRP A 1 108 ? -1.06000  -23.16400 2.44800   1.000 15.23000 ? 108 TRP A NE1  1 
ATOM   1934 C  CE2  . TRP A 1 108 ? 0.09400   -23.53000 3.09500   1.000 13.76000 ? 108 TRP A CE2  1 
ATOM   1935 C  CE3  . TRP A 1 108 ? 1.23600   -25.57400 3.63500   1.000 15.01000 ? 108 TRP A CE3  1 
ATOM   1936 C  CZ2  . TRP A 1 108 ? 1.06000   -22.77000 3.69400   1.000 14.21000 ? 108 TRP A CZ2  1 
ATOM   1937 C  CZ3  . TRP A 1 108 ? 2.21100   -24.81700 4.22800   1.000 17.05000 ? 108 TRP A CZ3  1 
ATOM   1938 C  CH2  . TRP A 1 108 ? 2.11900   -23.41100 4.26500   1.000 15.13000 ? 108 TRP A CH2  1 
ATOM   1939 H  H    . TRP A 1 108 ? -0.76300  -28.04200 4.12100   1.000 16.96000 ? 108 TRP A H    1 
ATOM   1940 H  HA   . TRP A 1 108 ? -3.00900  -26.77800 3.29600   1.000 17.86000 ? 108 TRP A HA   1 
ATOM   1941 H  HB2  . TRP A 1 108 ? -0.58900  -27.31500 1.97300   1.000 16.17000 ? 108 TRP A HB2  1 
ATOM   1942 H  HB3  . TRP A 1 108 ? -1.86400  -26.79300 1.18300   1.000 16.17000 ? 108 TRP A HB3  1 
ATOM   1943 H  HD1  . TRP A 1 108 ? -2.52000  -24.25100 1.53600   1.000 19.98000 ? 108 TRP A HD1  1 
ATOM   1944 H  HE1  . TRP A 1 108 ? -1.32800  -22.35400 2.33900   1.000 18.30000 ? 108 TRP A HE1  1 
ATOM   1945 H  HE3  . TRP A 1 108 ? 1.29700   -26.50200 3.63000   1.000 18.04000 ? 108 TRP A HE3  1 
ATOM   1946 H  HZ2  . TRP A 1 108 ? 0.99700   -21.84200 3.71200   1.000 17.08000 ? 108 TRP A HZ2  1 
ATOM   1947 H  HZ3  . TRP A 1 108 ? 2.94700   -25.23700 4.61200   1.000 20.48000 ? 108 TRP A HZ3  1 
ATOM   1948 H  HH2  . TRP A 1 108 ? 2.78700   -22.91600 4.68300   1.000 18.17000 ? 108 TRP A HH2  1 
ATOM   1949 N  N    A VAL A 1 109 ? -4.21700  -28.85400 2.75300   0.620 19.74000 ? 109 VAL A N    1 
ATOM   1950 N  N    B VAL A 1 109 ? -4.21500  -28.89900 2.73600   0.380 19.66000 ? 109 VAL A N    1 
ATOM   1951 C  CA   A VAL A 1 109 ? -4.93400  -30.05100 2.33900   0.620 19.12000 ? 109 VAL A CA   1 
ATOM   1952 C  CA   B VAL A 1 109 ? -4.79900  -30.17700 2.33500   0.380 17.78000 ? 109 VAL A CA   1 
ATOM   1953 C  C    A VAL A 1 109 ? -4.67100  -30.36000 0.87500   0.620 18.37000 ? 109 VAL A C    1 
ATOM   1954 C  C    B VAL A 1 109 ? -4.67800  -30.39600 0.82800   0.380 18.31000 ? 109 VAL A C    1 
ATOM   1955 O  O    A VAL A 1 109 ? -4.41700  -31.52000 0.51600   0.620 16.33000 ? 109 VAL A O    1 
ATOM   1956 O  O    B VAL A 1 109 ? -4.55300  -31.54100 0.38000   0.380 18.54000 ? 109 VAL A O    1 
ATOM   1957 C  CB   A VAL A 1 109 ? -6.43700  -29.86800 2.62900   0.620 23.52000 ? 109 VAL A CB   1 
ATOM   1958 C  CB   B VAL A 1 109 ? -6.25200  -30.32400 2.83300   0.380 24.74000 ? 109 VAL A CB   1 
ATOM   1959 C  CG1  A VAL A 1 109 ? -7.22100  -31.07800 2.16400   0.620 22.26000 ? 109 VAL A CG1  1 
ATOM   1960 C  CG1  B VAL A 1 109 ? -6.32400  -30.16500 4.35200   0.380 25.30000 ? 109 VAL A CG1  1 
ATOM   1961 C  CG2  A VAL A 1 109 ? -6.66100  -29.62500 4.11600   0.620 32.40000 ? 109 VAL A CG2  1 
ATOM   1962 C  CG2  B VAL A 1 109 ? -7.15300  -29.32800 2.11900   0.380 32.18000 ? 109 VAL A CG2  1 
ATOM   1963 H  H    A VAL A 1 109 ? -4.71700  -28.26200 3.12500   0.620 23.71000 ? 109 VAL A H    1 
ATOM   1964 H  H    B VAL A 1 109 ? -4.76100  -28.32500 3.07000   0.380 23.61000 ? 109 VAL A H    1 
ATOM   1965 H  HA   A VAL A 1 109 ? -4.61000  -30.80900 2.85100   0.620 22.96000 ? 109 VAL A HA   1 
ATOM   1966 H  HA   B VAL A 1 109 ? -4.28600  -30.87500 2.77100   0.380 21.37000 ? 109 VAL A HA   1 
ATOM   1967 H  HB   A VAL A 1 109 ? -6.75900  -29.09400 2.14000   0.620 28.24000 ? 109 VAL A HB   1 
ATOM   1968 H  HB   B VAL A 1 109 ? -6.57400  -31.21500 2.62500   0.380 29.71000 ? 109 VAL A HB   1 
ATOM   1969 H  HG11 A VAL A 1 109 ? -8.13500  -31.00100 2.47900   0.620 26.74000 ? 109 VAL A HG11 1 
ATOM   1970 H  HG11 B VAL A 1 109 ? -7.15800  -30.54700 4.67000   0.380 30.39000 ? 109 VAL A HG11 1 
ATOM   1971 H  HG12 A VAL A 1 109 ? -7.20600  -31.11000 1.19500   0.620 26.74000 ? 109 VAL A HG12 1 
ATOM   1972 H  HG12 B VAL A 1 109 ? -5.57300  -30.63000 4.75400   0.380 30.39000 ? 109 VAL A HG12 1 
ATOM   1973 H  HG13 A VAL A 1 109 ? -6.81100  -31.87800 2.52900   0.620 26.74000 ? 109 VAL A HG13 1 
ATOM   1974 H  HG13 B VAL A 1 109 ? -6.28600  -29.22200 4.57300   0.380 30.39000 ? 109 VAL A HG13 1 
ATOM   1975 H  HG21 A VAL A 1 109 ? -7.61100  -29.68200 4.30600   0.620 38.91000 ? 109 VAL A HG21 1 
ATOM   1976 H  HG21 B VAL A 1 109 ? -7.78400  -28.95900 2.75700   0.380 38.64000 ? 109 VAL A HG21 1 
ATOM   1977 H  HG22 A VAL A 1 109 ? -6.18200  -30.30000 4.62200   0.620 38.91000 ? 109 VAL A HG22 1 
ATOM   1978 H  HG22 B VAL A 1 109 ? -6.60700  -28.61900 1.74600   0.380 38.64000 ? 109 VAL A HG22 1 
ATOM   1979 H  HG23 A VAL A 1 109 ? -6.33100  -28.74300 4.34600   0.620 38.91000 ? 109 VAL A HG23 1 
ATOM   1980 H  HG23 B VAL A 1 109 ? -7.63000  -29.78600 1.41000   0.380 38.64000 ? 109 VAL A HG23 1 
ATOM   1981 N  N    . ALA A 1 110 ? -4.68900  -29.33300 0.02500   1.000 16.44000 ? 110 ALA A N    1 
ATOM   1982 C  CA   . ALA A 1 110 ? -4.50100  -29.52900 -1.41200  1.000 16.39000 ? 110 ALA A CA   1 
ATOM   1983 C  C    . ALA A 1 110 ? -3.10600  -30.06200 -1.71800  1.000 17.82000 ? 110 ALA A C    1 
ATOM   1984 O  O    . ALA A 1 110 ? -2.93000  -30.86400 -2.64300  1.000 16.88000 ? 110 ALA A O    1 
ATOM   1985 C  CB   . ALA A 1 110 ? -4.75600  -28.24900 -2.19100  1.000 22.56000 ? 110 ALA A CB   1 
ATOM   1986 H  H    . ALA A 1 110 ? -4.80900  -28.51400 0.25700   1.000 19.75000 ? 110 ALA A H    1 
ATOM   1987 H  HA   . ALA A 1 110 ? -5.15800  -30.17900 -1.70600  1.000 19.69000 ? 110 ALA A HA   1 
ATOM   1988 H  HB1  . ALA A 1 110 ? -4.72100  -28.44500 -3.14000  1.000 27.10000 ? 110 ALA A HB1  1 
ATOM   1989 H  HB2  . ALA A 1 110 ? -5.63100  -27.90400 -1.95600  1.000 27.10000 ? 110 ALA A HB2  1 
ATOM   1990 H  HB3  . ALA A 1 110 ? -4.07300  -27.59900 -1.96300  1.000 27.10000 ? 110 ALA A HB3  1 
ATOM   1991 N  N    . TRP A 1 111 ? -2.08600  -29.62100 -0.97600  1.000 14.72000 ? 111 TRP A N    1 
ATOM   1992 C  CA   . TRP A 1 111 ? -0.75300  -30.20900 -1.17100  1.000 13.37000 ? 111 TRP A CA   1 
ATOM   1993 C  C    . TRP A 1 111 ? -0.77100  -31.69000 -0.83200  1.000 14.21000 ? 111 TRP A C    1 
ATOM   1994 O  O    . TRP A 1 111 ? -0.26900  -32.51900 -1.61100  1.000 13.37000 ? 111 TRP A O    1 
ATOM   1995 C  CB   . TRP A 1 111 ? 0.28600   -29.48200 -0.31500  1.000 14.01000 ? 111 TRP A CB   1 
ATOM   1996 C  CG   . TRP A 1 111 ? 1.64100   -30.09700 -0.47100  1.000 13.30000 ? 111 TRP A CG   1 
ATOM   1997 C  CD1  . TRP A 1 111 ? 2.55400   -29.82800 -1.45600  1.000 15.86000 ? 111 TRP A CD1  1 
ATOM   1998 C  CD2  . TRP A 1 111 ? 2.23000   -31.08800 0.36400   1.000 11.92000 ? 111 TRP A CD2  1 
ATOM   1999 N  NE1  . TRP A 1 111 ? 3.65100   -30.62500 -1.29500  1.000 14.97000 ? 111 TRP A NE1  1 
ATOM   2000 C  CE2  . TRP A 1 111 ? 3.48900   -31.40100 -0.18500  1.000 12.08000 ? 111 TRP A CE2  1 
ATOM   2001 C  CE3  . TRP A 1 111 ? 1.79600   -31.77800 1.50600   1.000 13.14000 ? 111 TRP A CE3  1 
ATOM   2002 C  CZ2  . TRP A 1 111 ? 4.34000   -32.33100 0.39900   1.000 15.60000 ? 111 TRP A CZ2  1 
ATOM   2003 C  CZ3  . TRP A 1 111 ? 2.65100   -32.67500 2.09100   1.000 16.96000 ? 111 TRP A CZ3  1 
ATOM   2004 C  CH2  . TRP A 1 111 ? 3.90600   -32.95600 1.52400   1.000 15.47000 ? 111 TRP A CH2  1 
ATOM   2005 H  H    . TRP A 1 111 ? -2.13400  -29.00700 -0.37600  1.000 17.69000 ? 111 TRP A H    1 
ATOM   2006 H  HA   . TRP A 1 111 ? -0.49800  -30.10100 -2.10000  1.000 16.07000 ? 111 TRP A HA   1 
ATOM   2007 H  HB2  . TRP A 1 111 ? 0.33700   -28.55300 -0.59100  1.000 16.83000 ? 111 TRP A HB2  1 
ATOM   2008 H  HB3  . TRP A 1 111 ? 0.02900   -29.53800 0.61900   1.000 16.83000 ? 111 TRP A HB3  1 
ATOM   2009 H  HD1  . TRP A 1 111 ? 2.44300   -29.19900 -2.13200  1.000 19.05000 ? 111 TRP A HD1  1 
ATOM   2010 H  HE1  . TRP A 1 111 ? 4.33700   -30.63500 -1.81300  1.000 17.99000 ? 111 TRP A HE1  1 
ATOM   2011 H  HE3  . TRP A 1 111 ? 0.94700   -31.63100 1.85800   1.000 15.79000 ? 111 TRP A HE3  1 
ATOM   2012 H  HZ2  . TRP A 1 111 ? 5.17400   -32.51800 0.03400   1.000 18.74000 ? 111 TRP A HZ2  1 
ATOM   2013 H  HZ3  . TRP A 1 111 ? 2.39700   -33.10400 2.87600   1.000 20.37000 ? 111 TRP A HZ3  1 
ATOM   2014 H  HH2  . TRP A 1 111 ? 4.45500   -33.58800 1.93000   1.000 18.59000 ? 111 TRP A HH2  1 
ATOM   2015 N  N    A ARG A 1 112 ? -1.35100  -32.07200 0.31000   0.580 14.74000 ? 112 ARG A N    1 
ATOM   2016 N  N    B ARG A 1 112 ? -1.39600  -32.04500 0.29400   0.420 14.91000 ? 112 ARG A N    1 
ATOM   2017 C  CA   A ARG A 1 112 ? -1.37600  -33.48900 0.65200   0.580 16.29000 ? 112 ARG A CA   1 
ATOM   2018 C  CA   B ARG A 1 112 ? -1.45400  -33.43100 0.72900   0.420 16.25000 ? 112 ARG A CA   1 
ATOM   2019 C  C    A ARG A 1 112 ? -2.10500  -34.28700 -0.42300  0.580 14.12000 ? 112 ARG A C    1 
ATOM   2020 C  C    B ARG A 1 112 ? -2.16900  -34.30000 -0.29500  0.420 14.43000 ? 112 ARG A C    1 
ATOM   2021 O  O    A ARG A 1 112 ? -1.63700  -35.35200 -0.84700  0.580 15.96000 ? 112 ARG A O    1 
ATOM   2022 O  O    B ARG A 1 112 ? -1.77700  -35.45200 -0.52500  0.420 16.71000 ? 112 ARG A O    1 
ATOM   2023 C  CB   A ARG A 1 112 ? -2.02700  -33.71600 2.02400   0.580 18.86000 ? 112 ARG A CB   1 
ATOM   2024 C  CB   B ARG A 1 112 ? -2.18800  -33.50500 2.07200   0.420 19.47000 ? 112 ARG A CB   1 
ATOM   2025 C  CG   A ARG A 1 112 ? -2.23400  -35.18700 2.37600   0.580 22.09000 ? 112 ARG A CG   1 
ATOM   2026 C  CG   B ARG A 1 112 ? -2.08300  -34.83800 2.77800   0.420 22.84000 ? 112 ARG A CG   1 
ATOM   2027 C  CD   A ARG A 1 112 ? -2.95700  -35.38500 3.71300   0.580 33.05000 ? 112 ARG A CD   1 
ATOM   2028 C  CD   B ARG A 1 112 ? -2.60800  -34.75200 4.22300   0.420 26.32000 ? 112 ARG A CD   1 
ATOM   2029 N  NE   A ARG A 1 112 ? -3.25400  -36.79600 3.93700   0.580 42.44000 ? 112 ARG A NE   1 
ATOM   2030 N  NE   B ARG A 1 112 ? -3.81300  -33.93900 4.36500   0.420 33.43000 ? 112 ARG A NE   1 
ATOM   2031 C  CZ   A ARG A 1 112 ? -4.33200  -37.42300 3.48200   0.580 41.42000 ? 112 ARG A CZ   1 
ATOM   2032 C  CZ   B ARG A 1 112 ? -5.04000  -34.33400 4.04600   0.420 37.23000 ? 112 ARG A CZ   1 
ATOM   2033 N  NH1  A ARG A 1 112 ? -5.27000  -36.78500 2.79800   0.580 33.95000 ? 112 ARG A NH1  1 
ATOM   2034 N  NH1  B ARG A 1 112 ? -5.27300  -35.52900 3.52500   0.420 35.20000 ? 112 ARG A NH1  1 
ATOM   2035 N  NH2  A ARG A 1 112 ? -4.47600  -38.72300 3.72200   0.580 51.42000 ? 112 ARG A NH2  1 
ATOM   2036 N  NH2  B ARG A 1 112 ? -6.06100  -33.51000 4.26000   0.420 33.96000 ? 112 ARG A NH2  1 
ATOM   2037 H  H    A ARG A 1 112 ? -1.72200  -31.54800 0.88100   0.580 17.72000 ? 112 ARG A H    1 
ATOM   2038 H  H    B ARG A 1 112 ? -1.79500  -31.49600 0.82300   0.420 17.92000 ? 112 ARG A H    1 
ATOM   2039 H  HA   A ARG A 1 112 ? -0.46100  -33.80600 0.71400   0.580 19.57000 ? 112 ARG A HA   1 
ATOM   2040 H  HA   B ARG A 1 112 ? -0.55100  -33.76800 0.83700   0.420 19.52000 ? 112 ARG A HA   1 
ATOM   2041 H  HB2  A ARG A 1 112 ? -1.45900  -33.32700 2.70700   0.580 22.65000 ? 112 ARG A HB2  1 
ATOM   2042 H  HB2  B ARG A 1 112 ? -1.81700  -32.83100 2.66300   0.420 23.39000 ? 112 ARG A HB2  1 
ATOM   2043 H  HB3  A ARG A 1 112 ? -2.89600  -33.28600 2.03100   0.580 22.65000 ? 112 ARG A HB3  1 
ATOM   2044 H  HB3  B ARG A 1 112 ? -3.13000  -33.32900 1.91800   0.420 23.39000 ? 112 ARG A HB3  1 
ATOM   2045 H  HG2  A ARG A 1 112 ? -2.76800  -35.60600 1.68200   0.580 26.54000 ? 112 ARG A HG2  1 
ATOM   2046 H  HG2  B ARG A 1 112 ? -2.61000  -35.49800 2.30100   0.420 27.43000 ? 112 ARG A HG2  1 
ATOM   2047 H  HG3  A ARG A 1 112 ? -1.36900  -35.62300 2.43600   0.580 26.54000 ? 112 ARG A HG3  1 
ATOM   2048 H  HG3  B ARG A 1 112 ? -1.15300  -35.11400 2.80800   0.420 27.43000 ? 112 ARG A HG3  1 
ATOM   2049 H  HD2  A ARG A 1 112 ? -2.39200  -35.07100 4.43600   0.580 39.68000 ? 112 ARG A HD2  1 
ATOM   2050 H  HD2  B ARG A 1 112 ? -2.81800  -35.64700 4.53300   0.420 31.60000 ? 112 ARG A HD2  1 
ATOM   2051 H  HD3  A ARG A 1 112 ? -3.79200  -34.89200 3.70600   0.580 39.68000 ? 112 ARG A HD3  1 
ATOM   2052 H  HD3  B ARG A 1 112 ? -1.92000  -34.36000 4.78300   0.420 31.60000 ? 112 ARG A HD3  1 
ATOM   2053 H  HE   A ARG A 1 112 ? -2.69100  -37.25500 4.39700   0.580 50.95000 ? 112 ARG A HE   1 
ATOM   2054 H  HE   B ARG A 1 112 ? -3.72100  -33.14400 4.68000   0.420 40.14000 ? 112 ARG A HE   1 
ATOM   2055 H  HH11 A ARG A 1 112 ? -5.18900  -35.94300 2.64000   0.580 40.76000 ? 112 ARG A HH11 1 
ATOM   2056 H  HH11 B ARG A 1 112 ? -4.62100  -36.07100 3.38500   0.420 42.27000 ? 112 ARG A HH11 1 
ATOM   2057 H  HH12 A ARG A 1 112 ? -5.96000  -37.21200 2.51300   0.580 40.76000 ? 112 ARG A HH12 1 
ATOM   2058 H  HH12 B ARG A 1 112 ? -6.07700  -35.76200 3.32600   0.420 42.27000 ? 112 ARG A HH12 1 
ATOM   2059 H  HH21 A ARG A 1 112 ? -3.87400  -39.14700 4.16700   0.580 61.73000 ? 112 ARG A HH21 1 
ATOM   2060 H  HH21 B ARG A 1 112 ? -5.92300  -32.73200 4.60000   0.420 40.78000 ? 112 ARG A HH21 1 
ATOM   2061 H  HH22 A ARG A 1 112 ? -5.17000  -39.14000 3.43200   0.580 61.73000 ? 112 ARG A HH22 1 
ATOM   2062 H  HH22 B ARG A 1 112 ? -6.86100  -33.75400 4.05700   0.420 40.78000 ? 112 ARG A HH22 1 
ATOM   2063 N  N    . ASN A 1 113 ? -3.23700  -33.77600 -0.89600  1.000 14.89000 ? 113 ASN A N    1 
ATOM   2064 C  CA   . ASN A 1 113 ? -4.09600  -34.57400 -1.78000  1.000 16.99000 ? 113 ASN A CA   1 
ATOM   2065 C  C    . ASN A 1 113 ? -3.70800  -34.53100 -3.24700  1.000 17.63000 ? 113 ASN A C    1 
ATOM   2066 O  O    . ASN A 1 113 ? -4.07900  -35.45800 -4.00800  1.000 18.81000 ? 113 ASN A O    1 
ATOM   2067 C  CB   . ASN A 1 113 ? -5.57100  -34.15900 -1.60700  1.000 16.63000 ? 113 ASN A CB   1 
ATOM   2068 C  CG   . ASN A 1 113 ? -6.12700  -34.57400 -0.27200  1.000 17.08000 ? 113 ASN A CG   1 
ATOM   2069 O  OD1  . ASN A 1 113 ? -5.66200  -35.52500 0.31400   1.000 20.94000 ? 113 ASN A OD1  1 
ATOM   2070 N  ND2  . ASN A 1 113 ? -7.13000  -33.86700 0.20600   1.000 18.91000 ? 113 ASN A ND2  1 
ATOM   2071 H  H    . ASN A 1 113 ? -3.52800  -32.98500 -0.72600  1.000 17.89000 ? 113 ASN A H    1 
ATOM   2072 H  HA   . ASN A 1 113 ? -4.01800  -35.50300 -1.51100  1.000 20.41000 ? 113 ASN A HA   1 
ATOM   2073 H  HB2  . ASN A 1 113 ? -5.64000  -33.19400 -1.67600  1.000 19.98000 ? 113 ASN A HB2  1 
ATOM   2074 H  HB3  . ASN A 1 113 ? -6.10300  -34.58000 -2.30000  1.000 19.98000 ? 113 ASN A HB3  1 
ATOM   2075 H  HD21 . ASN A 1 113 ? -7.47700  -34.07200 0.96600   1.000 22.72000 ? 113 ASN A HD21 1 
ATOM   2076 H  HD22 . ASN A 1 113 ? -7.43800  -33.20100 -0.24200  1.000 22.72000 ? 113 ASN A HD22 1 
ATOM   2077 N  N    . ARG A 1 114 ? -2.95900  -33.51300 -3.68200  1.000 16.20000 ? 114 ARG A N    1 
ATOM   2078 C  CA   . ARG A 1 114 ? -2.67400  -33.32600 -5.10600  1.000 18.02000 ? 114 ARG A CA   1 
ATOM   2079 C  C    . ARG A 1 114 ? -1.21400  -33.20800 -5.46000  1.000 18.48000 ? 114 ARG A C    1 
ATOM   2080 O  O    . ARG A 1 114 ? -0.88200  -33.36600 -6.64800  1.000 20.57000 ? 114 ARG A O    1 
ATOM   2081 C  CB   . ARG A 1 114 ? -3.43400  -32.12100 -5.61600  1.000 17.55000 ? 114 ARG A CB   1 
ATOM   2082 C  CG   . ARG A 1 114 ? -4.89500  -32.38700 -5.25100  1.000 21.16000 ? 114 ARG A CG   1 
ATOM   2083 C  CD   . ARG A 1 114 ? -5.78700  -31.43200 -5.80700  1.000 22.52000 ? 114 ARG A CD   1 
ATOM   2084 N  NE   . ARG A 1 114 ? -5.91400  -31.51900 -7.24600  1.000 19.59000 ? 114 ARG A NE   1 
ATOM   2085 C  CZ   . ARG A 1 114 ? -6.64800  -30.65500 -7.91700  1.000 20.04000 ? 114 ARG A CZ   1 
ATOM   2086 N  NH1  . ARG A 1 114 ? -7.27400  -29.67100 -7.29300  1.000 21.03000 ? 114 ARG A NH1  1 
ATOM   2087 N  NH2  . ARG A 1 114 ? -6.77200  -30.80200 -9.23100  1.000 21.93000 ? 114 ARG A NH2  1 
ATOM   2088 H  H    . ARG A 1 114 ? -2.60500  -32.91800 -3.17200  1.000 19.46000 ? 114 ARG A H    1 
ATOM   2089 H  HA   . ARG A 1 114 ? -2.99100  -34.10200 -5.59400  1.000 21.64000 ? 114 ARG A HA   1 
ATOM   2090 H  HB2  . ARG A 1 114 ? -3.12600  -31.31000 -5.18200  1.000 21.08000 ? 114 ARG A HB2  1 
ATOM   2091 H  HB3  . ARG A 1 114 ? -3.34300  -32.03700 -6.57800  1.000 21.08000 ? 114 ARG A HB3  1 
ATOM   2092 H  HG2  . ARG A 1 114 ? -5.14900  -33.26200 -5.58300  1.000 25.41000 ? 114 ARG A HG2  1 
ATOM   2093 H  HG3  . ARG A 1 114 ? -4.99000  -32.35900 -4.28600  1.000 25.41000 ? 114 ARG A HG3  1 
ATOM   2094 H  HD2  . ARG A 1 114 ? -6.66700  -31.56700 -5.42400  1.000 27.05000 ? 114 ARG A HD2  1 
ATOM   2095 H  HD3  . ARG A 1 114 ? -5.46500  -30.54300 -5.59200  1.000 27.05000 ? 114 ARG A HD3  1 
ATOM   2096 H  HE   . ARG A 1 114 ? -5.50500  -32.14500 -7.67000  1.000 23.53000 ? 114 ARG A HE   1 
ATOM   2097 H  HH11 . ARG A 1 114 ? -7.20600  -29.58900 -6.44000  1.000 25.26000 ? 114 ARG A HH11 1 
ATOM   2098 H  HH12 . ARG A 1 114 ? -7.75100  -29.11200 -7.74100  1.000 25.26000 ? 114 ARG A HH12 1 
ATOM   2099 H  HH21 . ARG A 1 114 ? -6.37700  -31.45400 -9.63000  1.000 26.34000 ? 114 ARG A HH21 1 
ATOM   2100 H  HH22 . ARG A 1 114 ? -7.24800  -30.24600 -9.68300  1.000 26.34000 ? 114 ARG A HH22 1 
ATOM   2101 N  N    . CYS A 1 115 ? -0.32700  -32.95800 -4.50200  1.000 14.27000 ? 115 CYS A N    1 
ATOM   2102 C  CA   . CYS A 1 115 ? 1.08400   -32.76800 -4.77600  1.000 14.04000 ? 115 CYS A CA   1 
ATOM   2103 C  C    . CYS A 1 115 ? 1.97100   -33.80200 -4.11600  1.000 15.36000 ? 115 CYS A C    1 
ATOM   2104 O  O    . CYS A 1 115 ? 2.93900   -34.26600 -4.73500  1.000 16.67000 ? 115 CYS A O    1 
ATOM   2105 C  CB   . CYS A 1 115 ? 1.52000   -31.36700 -4.28200  1.000 13.50000 ? 115 CYS A CB   1 
ATOM   2106 S  SG   . CYS A 1 115 ? 0.59700   -30.00300 -5.03600  1.000 14.69000 ? 115 CYS A SG   1 
ATOM   2107 H  H    . CYS A 1 115 ? -0.52700  -32.89300 -3.66800  1.000 17.15000 ? 115 CYS A H    1 
ATOM   2108 H  HA   . CYS A 1 115 ? 1.22200   -32.82500 -5.73400  1.000 16.87000 ? 115 CYS A HA   1 
ATOM   2109 H  HB2  . CYS A 1 115 ? 1.38600   -31.32000 -3.32200  1.000 16.23000 ? 115 CYS A HB2  1 
ATOM   2110 H  HB3  . CYS A 1 115 ? 2.45800   -31.24100 -4.49200  1.000 16.23000 ? 115 CYS A HB3  1 
ATOM   2111 N  N    . LYS A 1 116 ? 1.69800   -34.14700 -2.86100  1.000 15.00000 ? 116 LYS A N    1 
ATOM   2112 C  CA   . LYS A 1 116 ? 2.49400   -35.10600 -2.10900  1.000 16.70000 ? 116 LYS A CA   1 
ATOM   2113 C  C    . LYS A 1 116 ? 2.53500   -36.42900 -2.86200  1.000 16.84000 ? 116 LYS A C    1 
ATOM   2114 O  O    . LYS A 1 116 ? 1.50200   -36.93900 -3.30000  1.000 17.49000 ? 116 LYS A O    1 
ATOM   2115 C  CB   . LYS A 1 116 ? 1.85900   -35.28100 -0.73100  1.000 17.05000 ? 116 LYS A CB   1 
ATOM   2116 C  CG   . LYS A 1 116 ? 2.64000   -36.14500 0.23600   1.000 15.65000 ? 116 LYS A CG   1 
ATOM   2117 C  CD   . LYS A 1 116 ? 1.88900   -36.24200 1.52700   1.000 16.01000 ? 116 LYS A CD   1 
ATOM   2118 C  CE   . LYS A 1 116 ? 2.70200   -36.87500 2.62400   1.000 17.23000 ? 116 LYS A CE   1 
ATOM   2119 N  NZ   . LYS A 1 116 ? 1.92600   -36.91800 3.90000   1.000 19.88000 ? 116 LYS A NZ   1 
ATOM   2120 H  H    . LYS A 1 116 ? 1.03700   -33.83000 -2.41100  1.000 18.03000 ? 116 LYS A H    1 
ATOM   2121 H  HA   . LYS A 1 116 ? 3.40700   -34.79800 -1.99400  1.000 20.06000 ? 116 LYS A HA   1 
ATOM   2122 H  HB2  . LYS A 1 116 ? 1.76300   -34.40600 -0.32500  1.000 20.48000 ? 116 LYS A HB2  1 
ATOM   2123 H  HB3  . LYS A 1 116 ? 0.98700   -35.69100 -0.84600  1.000 20.48000 ? 116 LYS A HB3  1 
ATOM   2124 H  HG2  . LYS A 1 116 ? 2.75000   -37.03500 -0.13200  1.000 18.80000 ? 116 LYS A HG2  1 
ATOM   2125 H  HG3  . LYS A 1 116 ? 3.50800   -35.74600 0.40700   1.000 18.80000 ? 116 LYS A HG3  1 
ATOM   2126 H  HD2  . LYS A 1 116 ? 1.63800   -35.35100 1.81600   1.000 19.23000 ? 116 LYS A HD2  1 
ATOM   2127 H  HD3  . LYS A 1 116 ? 1.09500   -36.78300 1.39200   1.000 19.23000 ? 116 LYS A HD3  1 
ATOM   2128 H  HE2  . LYS A 1 116 ? 2.93300   -37.78400 2.37300   1.000 20.70000 ? 116 LYS A HE2  1 
ATOM   2129 H  HE3  . LYS A 1 116 ? 3.50800   -36.35600 2.77100   1.000 20.70000 ? 116 LYS A HE3  1 
ATOM   2130 H  HZ1  . LYS A 1 116 ? 2.36000   -37.40700 4.50400   1.000 23.88000 ? 116 LYS A HZ1  1 
ATOM   2131 H  HZ2  . LYS A 1 116 ? 1.81800   -36.09400 4.21800   1.000 23.88000 ? 116 LYS A HZ2  1 
ATOM   2132 H  HZ3  . LYS A 1 116 ? 1.12500   -37.28000 3.75700   1.000 23.88000 ? 116 LYS A HZ3  1 
ATOM   2133 N  N    . GLY A 1 117 ? 3.74500   -36.94600 -3.05800  1.000 19.66000 ? 117 GLY A N    1 
ATOM   2134 C  CA   . GLY A 1 117 ? 3.92700   -38.21800 -3.73300  1.000 21.36000 ? 117 GLY A CA   1 
ATOM   2135 C  C    . GLY A 1 117 ? 3.92900   -38.15100 -5.23900  1.000 23.75000 ? 117 GLY A C    1 
ATOM   2136 O  O    . GLY A 1 117 ? 3.91900   -39.20300 -5.89400  1.000 29.64000 ? 117 GLY A O    1 
ATOM   2137 H  H    . GLY A 1 117 ? 4.47900   -36.57500 -2.80600  1.000 23.61000 ? 117 GLY A H    1 
ATOM   2138 H  HA2  . GLY A 1 117 ? 4.77400   -38.59800 -3.45400  1.000 25.66000 ? 117 GLY A HA2  1 
ATOM   2139 H  HA3  . GLY A 1 117 ? 3.21000   -38.81500 -3.46600  1.000 25.66000 ? 117 GLY A HA3  1 
ATOM   2140 N  N    . THR A 1 118 ? 3.91300   -36.96200 -5.81900  1.000 19.18000 ? 118 THR A N    1 
ATOM   2141 C  CA   . THR A 1 118 ? 3.95600   -36.75800 -7.25900  1.000 19.20000 ? 118 THR A CA   1 
ATOM   2142 C  C    . THR A 1 118 ? 5.28300   -36.11400 -7.63700  1.000 20.75000 ? 118 THR A C    1 
ATOM   2143 O  O    . THR A 1 118 ? 6.07800   -35.71300 -6.78700  1.000 21.80000 ? 118 THR A O    1 
ATOM   2144 C  CB   . THR A 1 118 ? 2.78800   -35.89100 -7.74400  1.000 22.07000 ? 118 THR A CB   1 
ATOM   2145 O  OG1  . THR A 1 118 ? 3.03800   -34.49700 -7.43400  1.000 20.85000 ? 118 THR A OG1  1 
ATOM   2146 C  CG2  . THR A 1 118 ? 1.48500   -36.34200 -7.13300  1.000 21.50000 ? 118 THR A CG2  1 
ATOM   2147 H  H    . THR A 1 118 ? 3.87700   -36.22300 -5.37900  1.000 23.04000 ? 118 THR A H    1 
ATOM   2148 H  HA   . THR A 1 118 ? 3.88000   -37.61700 -7.70200  1.000 23.07000 ? 118 THR A HA   1 
ATOM   2149 H  HB   . THR A 1 118 ? 2.70400   -35.98200 -8.70600  1.000 26.50000 ? 118 THR A HB   1 
ATOM   2150 H  HG1  . THR A 1 118 ? 3.43200   -34.43400 -6.69500  1.000 25.04000 ? 118 THR A HG1  1 
ATOM   2151 H  HG21 . THR A 1 118 ? 0.75300   -35.81000 -7.48200  1.000 25.82000 ? 118 THR A HG21 1 
ATOM   2152 H  HG22 . THR A 1 118 ? 1.32500   -37.27500 -7.34500  1.000 25.82000 ? 118 THR A HG22 1 
ATOM   2153 H  HG23 . THR A 1 118 ? 1.51800   -36.24000 -6.16900  1.000 25.82000 ? 118 THR A HG23 1 
ATOM   2154 N  N    . ASP A 1 119 ? 5.53300   -36.02400 -8.94700  1.000 25.21000 ? 119 ASP A N    1 
ATOM   2155 C  CA   . ASP A 1 119 ? 6.79500   -35.46100 -9.43000  1.000 25.19000 ? 119 ASP A CA   1 
ATOM   2156 C  C    . ASP A 1 119 ? 6.67700   -33.93800 -9.42400  1.000 24.72000 ? 119 ASP A C    1 
ATOM   2157 O  O    . ASP A 1 119 ? 6.41600   -33.28700 -10.44100 1.000 28.19000 ? 119 ASP A O    1 
ATOM   2158 C  CB   . ASP A 1 119 ? 7.11200   -35.99300 -10.82300 1.000 32.98000 ? 119 ASP A CB   1 
ATOM   2159 C  CG   . ASP A 1 119 ? 8.35200   -35.35700 -11.42000 1.000 45.41000 ? 119 ASP A CG   1 
ATOM   2160 O  OD1  . ASP A 1 119 ? 9.19400   -34.85300 -10.64300 1.000 39.02000 ? 119 ASP A OD1  1 
ATOM   2161 O  OD2  . ASP A 1 119 ? 8.48900   -35.37100 -12.66500 1.000 42.84000 ? 119 ASP A OD2  1 
ATOM   2162 H  H    . ASP A 1 119 ? 4.99400   -36.28000 -9.56600  1.000 30.27000 ? 119 ASP A H    1 
ATOM   2163 H  HA   . ASP A 1 119 ? 7.51400   -35.71600 -8.83100  1.000 30.25000 ? 119 ASP A HA   1 
ATOM   2164 H  HB2  . ASP A 1 119 ? 7.26000   -36.95000 -10.77000 1.000 39.60000 ? 119 ASP A HB2  1 
ATOM   2165 H  HB3  . ASP A 1 119 ? 6.36400   -35.80500 -11.41100 1.000 39.60000 ? 119 ASP A HB3  1 
ATOM   2166 N  N    . VAL A 1 120 ? 6.87100   -33.35800 -8.23800  1.000 25.77000 ? 120 VAL A N    1 
ATOM   2167 C  CA   . VAL A 1 120 ? 6.63400   -31.92400 -8.09700  1.000 21.18000 ? 120 VAL A CA   1 
ATOM   2168 C  C    . VAL A 1 120 ? 7.66800   -31.09600 -8.84300  1.000 25.27000 ? 120 VAL A C    1 
ATOM   2169 O  O    . VAL A 1 120 ? 7.42600   -29.92100 -9.10900  1.000 19.61000 ? 120 VAL A O    1 
ATOM   2170 C  CB   . VAL A 1 120 ? 6.54500   -31.49100 -6.62200  1.000 20.55000 ? 120 VAL A CB   1 
ATOM   2171 C  CG1  . VAL A 1 120 ? 5.36500   -32.15800 -5.95500  1.000 22.87000 ? 120 VAL A CG1  1 
ATOM   2172 C  CG2  . VAL A 1 120 ? 7.81300   -31.79000 -5.88700  1.000 23.30000 ? 120 VAL A CG2  1 
ATOM   2173 H  H    . VAL A 1 120 ? 7.13000   -33.76000 -7.52300  1.000 30.95000 ? 120 VAL A H    1 
ATOM   2174 H  HA   . VAL A 1 120 ? 5.76700   -31.74700 -8.49500  1.000 25.44000 ? 120 VAL A HA   1 
ATOM   2175 H  HB   . VAL A 1 120 ? 6.41400   -30.53000 -6.59000  1.000 24.68000 ? 120 VAL A HB   1 
ATOM   2176 H  HG11 . VAL A 1 120 ? 5.29000   -31.83000 -5.04500  1.000 27.47000 ? 120 VAL A HG11 1 
ATOM   2177 H  HG12 . VAL A 1 120 ? 4.55900   -31.94500 -6.45100  1.000 27.47000 ? 120 VAL A HG12 1 
ATOM   2178 H  HG13 . VAL A 1 120 ? 5.50700   -33.11800 -5.94900  1.000 27.47000 ? 120 VAL A HG13 1 
ATOM   2179 H  HG21 . VAL A 1 120 ? 7.71800   -31.50500 -4.96500  1.000 27.99000 ? 120 VAL A HG21 1 
ATOM   2180 H  HG22 . VAL A 1 120 ? 7.98100   -32.74500 -5.92300  1.000 27.99000 ? 120 VAL A HG22 1 
ATOM   2181 H  HG23 . VAL A 1 120 ? 8.54300   -31.31000 -6.30900  1.000 27.99000 ? 120 VAL A HG23 1 
ATOM   2182 N  N    . GLN A 1 121 ? 8.83400   -31.66200 -9.16900  1.000 23.62000 ? 121 GLN A N    1 
ATOM   2183 C  CA   . GLN A 1 121 ? 9.82600   -30.90900 -9.93400  1.000 22.72000 ? 121 GLN A CA   1 
ATOM   2184 C  C    . GLN A 1 121 ? 9.28200   -30.50500 -11.29300 1.000 21.38000 ? 121 GLN A C    1 
ATOM   2185 O  O    . GLN A 1 121 ? 9.76300   -29.52300 -11.88100 1.000 22.94000 ? 121 GLN A O    1 
ATOM   2186 C  CB   . GLN A 1 121 ? 11.10900  -31.73700 -10.10800 1.000 30.54000 ? 121 GLN A CB   1 
ATOM   2187 C  CG   . GLN A 1 121 ? 12.23900  -30.99700 -10.83900 1.000 55.45000 ? 121 GLN A CG   1 
ATOM   2188 C  CD   . GLN A 1 121 ? 12.25500  -31.25000 -12.34700 1.000 89.42000 ? 121 GLN A CD   1 
ATOM   2189 O  OE1  . GLN A 1 121 ? 11.66000  -32.21300 -12.83800 1.000 76.88000 ? 121 GLN A OE1  1 
ATOM   2190 N  NE2  . GLN A 1 121 ? 12.94600  -30.38100 -13.08700 1.000 72.88000 ? 121 GLN A NE2  1 
ATOM   2191 H  H    . GLN A 1 121 ? 9.06800   -32.46300 -8.96300  1.000 28.37000 ? 121 GLN A H    1 
ATOM   2192 H  HA   . GLN A 1 121 ? 10.06200  -30.10600 -9.44400  1.000 27.29000 ? 121 GLN A HA   1 
ATOM   2193 H  HB2  . GLN A 1 121 ? 11.43800  -31.98600 -9.23100  1.000 36.68000 ? 121 GLN A HB2  1 
ATOM   2194 H  HB3  . GLN A 1 121 ? 10.89700  -32.53200 -10.62200 1.000 36.68000 ? 121 GLN A HB3  1 
ATOM   2195 H  HG2  . GLN A 1 121 ? 12.13200  -30.04300 -10.69800 1.000 66.57000 ? 121 GLN A HG2  1 
ATOM   2196 H  HG3  . GLN A 1 121 ? 13.09100  -31.29200 -10.47900 1.000 66.57000 ? 121 GLN A HG3  1 
ATOM   2197 H  HE21 . GLN A 1 121 ? 13.35100  -29.72200 -12.71000 1.000 87.49000 ? 121 GLN A HE21 1 
ATOM   2198 H  HE22 . GLN A 1 121 ? 12.98500  -30.47900 -13.94000 1.000 87.49000 ? 121 GLN A HE22 1 
ATOM   2199 N  N    . ALA A 1 122 ? 8.28200   -31.22000 -11.81100 1.000 20.41000 ? 122 ALA A N    1 
ATOM   2200 C  CA   . ALA A 1 122 ? 7.67000   -30.84300 -13.07900 1.000 24.45000 ? 122 ALA A CA   1 
ATOM   2201 C  C    . ALA A 1 122 ? 7.15100   -29.41500 -13.04200 1.000 22.78000 ? 122 ALA A C    1 
ATOM   2202 O  O    . ALA A 1 122 ? 7.08100   -28.73300 -14.07200 1.000 22.91000 ? 122 ALA A O    1 
ATOM   2203 C  CB   . ALA A 1 122 ? 6.51000   -31.78600 -13.40100 1.000 29.69000 ? 122 ALA A CB   1 
ATOM   2204 H  H    . ALA A 1 122 ? 7.94400   -31.92300 -11.44800 1.000 24.51000 ? 122 ALA A H    1 
ATOM   2205 H  HA   . ALA A 1 122 ? 8.34000   -30.91900 -13.77700 1.000 29.36000 ? 122 ALA A HA   1 
ATOM   2206 H  HB1  . ALA A 1 122 ? 6.13300   -31.54100 -14.26100 1.000 35.65000 ? 122 ALA A HB1  1 
ATOM   2207 H  HB2  . ALA A 1 122 ? 6.84200   -32.69700 -13.43400 1.000 35.65000 ? 122 ALA A HB2  1 
ATOM   2208 H  HB3  . ALA A 1 122 ? 5.83500   -31.70500 -12.70900 1.000 35.65000 ? 122 ALA A HB3  1 
ATOM   2209 N  N    . TRP A 1 123 ? 6.79800   -28.92900 -11.85100 1.000 20.88000 ? 123 TRP A N    1 
ATOM   2210 C  CA   . TRP A 1 123 ? 6.21200   -27.59800 -11.76400 1.000 18.80000 ? 123 TRP A CA   1 
ATOM   2211 C  C    . TRP A 1 123 ? 7.20800   -26.48100 -12.01800 1.000 19.75000 ? 123 TRP A C    1 
ATOM   2212 O  O    . TRP A 1 123 ? 6.78400   -25.35300 -12.29500 1.000 22.79000 ? 123 TRP A O    1 
ATOM   2213 C  CB   . TRP A 1 123 ? 5.53600   -27.43000 -10.39000 1.000 17.39000 ? 123 TRP A CB   1 
ATOM   2214 C  CG   . TRP A 1 123 ? 4.28500   -28.21100 -10.34700 1.000 20.04000 ? 123 TRP A CG   1 
ATOM   2215 C  CD1  . TRP A 1 123 ? 4.10600   -29.43900 -9.79400  1.000 21.69000 ? 123 TRP A CD1  1 
ATOM   2216 C  CD2  . TRP A 1 123 ? 3.04900   -27.85100 -10.94500 1.000 17.36000 ? 123 TRP A CD2  1 
ATOM   2217 N  NE1  . TRP A 1 123 ? 2.81900   -29.86700 -10.00600 1.000 21.77000 ? 123 TRP A NE1  1 
ATOM   2218 C  CE2  . TRP A 1 123 ? 2.14900   -28.91900 -10.71400 1.000 20.72000 ? 123 TRP A CE2  1 
ATOM   2219 C  CE3  . TRP A 1 123 ? 2.61200   -26.74800 -11.68000 1.000 21.35000 ? 123 TRP A CE3  1 
ATOM   2220 C  CZ2  . TRP A 1 123 ? 0.83200   -28.89000 -11.16500 1.000 25.82000 ? 123 TRP A CZ2  1 
ATOM   2221 C  CZ3  . TRP A 1 123 ? 1.30500   -26.73200 -12.14300 1.000 29.21000 ? 123 TRP A CZ3  1 
ATOM   2222 C  CH2  . TRP A 1 123 ? 0.43600   -27.79800 -11.88200 1.000 27.19000 ? 123 TRP A CH2  1 
ATOM   2223 H  H    . TRP A 1 123 ? 6.88600   -29.34000 -11.10100 1.000 25.08000 ? 123 TRP A H    1 
ATOM   2224 H  HA   . TRP A 1 123 ? 5.53200   -27.51100 -12.45000 1.000 22.58000 ? 123 TRP A HA   1 
ATOM   2225 H  HB2  . TRP A 1 123 ? 6.12900   -27.75100 -9.69300  1.000 20.90000 ? 123 TRP A HB2  1 
ATOM   2226 H  HB3  . TRP A 1 123 ? 5.32500   -26.49500 -10.24200 1.000 20.90000 ? 123 TRP A HB3  1 
ATOM   2227 H  HD1  . TRP A 1 123 ? 4.75900   -29.92000 -9.33900  1.000 26.05000 ? 123 TRP A HD1  1 
ATOM   2228 H  HE1  . TRP A 1 123 ? 2.49000   -30.61400 -9.73500  1.000 26.15000 ? 123 TRP A HE1  1 
ATOM   2229 H  HE3  . TRP A 1 123 ? 3.18600   -26.03700 -11.85500 1.000 25.65000 ? 123 TRP A HE3  1 
ATOM   2230 H  HZ2  . TRP A 1 123 ? 0.24500   -29.58800 -10.98600 1.000 31.01000 ? 123 TRP A HZ2  1 
ATOM   2231 H  HZ3  . TRP A 1 123 ? 1.00100   -26.00300 -12.63500 1.000 35.08000 ? 123 TRP A HZ3  1 
ATOM   2232 H  HH2  . TRP A 1 123 ? -0.43500  -27.76100 -12.20600 1.000 32.65000 ? 123 TRP A HH2  1 
ATOM   2233 N  N    . ILE A 1 124 ? 8.50400   -26.75900 -11.93100 1.000 19.51000 ? 124 ILE A N    1 
ATOM   2234 C  CA   . ILE A 1 124 ? 9.52200   -25.76100 -12.21300 1.000 19.06000 ? 124 ILE A CA   1 
ATOM   2235 C  C    . ILE A 1 124 ? 10.32200  -26.09800 -13.46000 1.000 20.38000 ? 124 ILE A C    1 
ATOM   2236 O  O    . ILE A 1 124 ? 11.26400  -25.37100 -13.79600 1.000 23.09000 ? 124 ILE A O    1 
ATOM   2237 C  CB   . ILE A 1 124 ? 10.41200  -25.49500 -10.98800 1.000 20.31000 ? 124 ILE A CB   1 
ATOM   2238 C  CG1  . ILE A 1 124 ? 11.09600  -26.75500 -10.48500 1.000 27.01000 ? 124 ILE A CG1  1 
ATOM   2239 C  CG2  . ILE A 1 124 ? 9.56000   -24.86400 -9.86100  1.000 23.17000 ? 124 ILE A CG2  1 
ATOM   2240 C  CD1  . ILE A 1 124 ? 12.25600  -26.46900 -9.53800  1.000 29.16000 ? 124 ILE A CD1  1 
ATOM   2241 H  H    . ILE A 1 124 ? 8.81900   -27.52800 -11.70800 1.000 23.43000 ? 124 ILE A H    1 
ATOM   2242 H  HA   . ILE A 1 124 ? 9.08700   -24.91500 -12.40200 1.000 22.89000 ? 124 ILE A HA   1 
ATOM   2243 H  HB   . ILE A 1 124 ? 11.11200  -24.88200 -11.26200 1.000 24.39000 ? 124 ILE A HB   1 
ATOM   2244 H  HG12 . ILE A 1 124 ? 10.44800  -27.29600 -10.00800 1.000 32.44000 ? 124 ILE A HG12 1 
ATOM   2245 H  HG13 . ILE A 1 124 ? 11.44500  -27.24800 -11.24400 1.000 32.44000 ? 124 ILE A HG13 1 
ATOM   2246 H  HG21 . ILE A 1 124 ? 10.10900  -24.76600 -9.06700  1.000 27.83000 ? 124 ILE A HG21 1 
ATOM   2247 H  HG22 . ILE A 1 124 ? 9.24300   -23.99500 -10.15300 1.000 27.83000 ? 124 ILE A HG22 1 
ATOM   2248 H  HG23 . ILE A 1 124 ? 8.80600   -25.44500 -9.67300  1.000 27.83000 ? 124 ILE A HG23 1 
ATOM   2249 H  HD11 . ILE A 1 124 ? 12.69300  -27.30500 -9.31100  1.000 35.02000 ? 124 ILE A HD11 1 
ATOM   2250 H  HD12 . ILE A 1 124 ? 12.88500  -25.87600 -9.97800  1.000 35.02000 ? 124 ILE A HD12 1 
ATOM   2251 H  HD13 . ILE A 1 124 ? 11.91100  -26.04800 -8.73500  1.000 35.02000 ? 124 ILE A HD13 1 
ATOM   2252 N  N    A ARG A 1 125 ? 9.94900   -27.16600 -14.16300 0.360 20.87000 ? 125 ARG A N    1 
ATOM   2253 N  N    B ARG A 1 125 ? 9.95100   -27.15500 -14.17200 0.640 20.75000 ? 125 ARG A N    1 
ATOM   2254 C  CA   A ARG A 1 125 ? 10.58500  -27.53400 -15.42100 0.360 29.97000 ? 125 ARG A CA   1 
ATOM   2255 C  CA   B ARG A 1 125 ? 10.69200  -27.57100 -15.36200 0.640 29.74000 ? 125 ARG A CA   1 
ATOM   2256 C  C    A ARG A 1 125 ? 10.65400  -26.33100 -16.34700 0.360 24.79000 ? 125 ARG A C    1 
ATOM   2257 C  C    B ARG A 1 125 ? 10.63200  -26.49100 -16.43300 0.640 25.37000 ? 125 ARG A C    1 
ATOM   2258 O  O    A ARG A 1 125 ? 9.70200   -25.55700 -16.46600 0.360 25.22000 ? 125 ARG A O    1 
ATOM   2259 O  O    B ARG A 1 125 ? 9.55300   -26.00700 -16.78900 0.640 25.52000 ? 125 ARG A O    1 
ATOM   2260 C  CB   A ARG A 1 125 ? 9.76000   -28.64100 -16.08800 0.360 33.46000 ? 125 ARG A CB   1 
ATOM   2261 C  CB   B ARG A 1 125 ? 10.08500  -28.87300 -15.89700 0.640 32.86000 ? 125 ARG A CB   1 
ATOM   2262 C  CG   A ARG A 1 125 ? 10.55300  -29.55900 -17.00700 0.360 44.26000 ? 125 ARG A CG   1 
ATOM   2263 C  CG   B ARG A 1 125 ? 10.78700  -29.47000 -17.12300 0.640 43.25000 ? 125 ARG A CG   1 
ATOM   2264 C  CD   A ARG A 1 125 ? 9.69600   -30.19100 -18.11000 0.360 51.22000 ? 125 ARG A CD   1 
ATOM   2265 C  CD   B ARG A 1 125 ? 10.98100  -30.99000 -16.99000 0.640 58.22000 ? 125 ARG A CD   1 
ATOM   2266 N  NE   A ARG A 1 125 ? 8.29700   -30.39500 -17.74400 0.360 53.83000 ? 125 ARG A NE   1 
ATOM   2267 N  NE   B ARG A 1 125 ? 11.83500  -31.53900 -18.04100 0.640 67.04000 ? 125 ARG A NE   1 
ATOM   2268 C  CZ   A ARG A 1 125 ? 7.82300   -31.47900 -17.14100 0.360 54.11000 ? 125 ARG A CZ   1 
ATOM   2269 C  CZ   B ARG A 1 125 ? 11.41300  -31.93900 -19.23500 0.640 51.42000 ? 125 ARG A CZ   1 
ATOM   2270 N  NH1  A ARG A 1 125 ? 8.62100   -32.45900 -16.74900 0.360 39.77000 ? 125 ARG A NH1  1 
ATOM   2271 N  NH1  B ARG A 1 125 ? 10.13100  -31.91300 -19.56200 0.640 59.92000 ? 125 ARG A NH1  1 
ATOM   2272 N  NH2  A ARG A 1 125 ? 6.51200   -31.58600 -16.93300 0.360 39.90000 ? 125 ARG A NH2  1 
ATOM   2273 N  NH2  B ARG A 1 125 ? 12.30000  -32.38500 -20.12100 0.640 52.34000 ? 125 ARG A NH2  1 
ATOM   2274 H  H    A ARG A 1 125 ? 9.31900   -27.70200 -13.92900 0.360 25.07000 ? 125 ARG A H    1 
ATOM   2275 H  H    B ARG A 1 125 ? 9.27300   -27.65200 -13.99000 0.640 24.92000 ? 125 ARG A H    1 
ATOM   2276 H  HA   A ARG A 1 125 ? 11.48700  -27.85300 -15.25800 0.360 35.98000 ? 125 ARG A HA   1 
ATOM   2277 H  HA   B ARG A 1 125 ? 11.62300  -27.72000 -15.13500 0.640 35.71000 ? 125 ARG A HA   1 
ATOM   2278 H  HB2  A ARG A 1 125 ? 9.36600   -29.19200 -15.39400 0.360 40.17000 ? 125 ARG A HB2  1 
ATOM   2279 H  HB2  B ARG A 1 125 ? 10.11800  -29.53800 -15.19200 0.640 39.46000 ? 125 ARG A HB2  1 
ATOM   2280 H  HB3  A ARG A 1 125 ? 9.06200   -28.22700 -16.61900 0.360 40.17000 ? 125 ARG A HB3  1 
ATOM   2281 H  HB3  B ARG A 1 125 ? 9.16400   -28.70000 -16.14700 0.640 39.46000 ? 125 ARG A HB3  1 
ATOM   2282 H  HG2  A ARG A 1 125 ? 11.25800  -29.04600 -17.43300 0.360 53.14000 ? 125 ARG A HG2  1 
ATOM   2283 H  HG2  B ARG A 1 125 ? 10.25000  -29.30000 -17.91300 0.640 51.92000 ? 125 ARG A HG2  1 
ATOM   2284 H  HG3  A ARG A 1 125 ? 10.93800  -30.27700 -16.48000 0.360 53.14000 ? 125 ARG A HG3  1 
ATOM   2285 H  HG3  B ARG A 1 125 ? 11.66100  -29.06000 -17.22200 0.640 51.92000 ? 125 ARG A HG3  1 
ATOM   2286 H  HD2  A ARG A 1 125 ? 9.71400   -29.61000 -18.88700 0.360 61.48000 ? 125 ARG A HD2  1 
ATOM   2287 H  HD2  B ARG A 1 125 ? 11.39400  -31.18400 -16.13400 0.640 69.89000 ? 125 ARG A HD2  1 
ATOM   2288 H  HD3  A ARG A 1 125 ? 10.07000  -31.05700 -18.33500 0.360 61.48000 ? 125 ARG A HD3  1 
ATOM   2289 H  HD3  B ARG A 1 125 ? 10.11600  -31.42600 -17.04700 0.640 69.89000 ? 125 ARG A HD3  1 
ATOM   2290 H  HE   A ARG A 1 125 ? 7.74000   -29.76800 -17.93300 0.360 64.63000 ? 125 ARG A HE   1 
ATOM   2291 H  HE   B ARG A 1 125 ? 12.67600  -31.60900 -17.87400 0.640 80.47000 ? 125 ARG A HE   1 
ATOM   2292 H  HH11 A ARG A 1 125 ? 9.46900   -32.40200 -16.88300 0.360 47.75000 ? 125 ARG A HH11 1 
ATOM   2293 H  HH11 B ARG A 1 125 ? 9.54800   -31.63300 -18.99600 0.640 71.93000 ? 125 ARG A HH11 1 
ATOM   2294 H  HH12 A ARG A 1 125 ? 8.29300   -33.15200 -16.36000 0.360 47.75000 ? 125 ARG A HH12 1 
ATOM   2295 H  HH12 B ARG A 1 125 ? 9.88100   -32.17700 -20.34200 0.640 71.93000 ? 125 ARG A HH12 1 
ATOM   2296 H  HH21 A ARG A 1 125 ? 5.98400   -30.95800 -17.18800 0.360 47.90000 ? 125 ARG A HH21 1 
ATOM   2297 H  HH21 B ARG A 1 125 ? 13.13500  -32.41200 -19.91700 0.640 62.83000 ? 125 ARG A HH21 1 
ATOM   2298 H  HH22 A ARG A 1 125 ? 6.19500   -32.28400 -16.54300 0.360 47.90000 ? 125 ARG A HH22 1 
ATOM   2299 H  HH22 B ARG A 1 125 ? 12.03800  -32.64700 -20.89700 0.640 62.83000 ? 125 ARG A HH22 1 
ATOM   2300 N  N    . GLY A 1 126 ? 11.80600  -26.15400 -16.98800 1.000 26.73000 ? 126 GLY A N    1 
ATOM   2301 C  CA   . GLY A 1 126 ? 11.93000  -25.12400 -17.98400 1.000 29.34000 ? 126 GLY A CA   1 
ATOM   2302 C  C    . GLY A 1 126 ? 12.16300  -23.73000 -17.44900 1.000 32.39000 ? 126 GLY A C    1 
ATOM   2303 O  O    . GLY A 1 126 ? 12.48000  -22.82700 -18.23700 1.000 33.43000 ? 126 GLY A O    1 
ATOM   2304 H  H    . GLY A 1 126 ? 12.55500  -26.52700 -16.78900 1.000 32.10000 ? 126 GLY A H    1 
ATOM   2305 H  HA2  . GLY A 1 126 ? 12.67600  -25.34400 -18.56400 1.000 35.23000 ? 126 GLY A HA2  1 
ATOM   2306 H  HA3  . GLY A 1 126 ? 11.11600  -25.10400 -18.51000 1.000 35.23000 ? 126 GLY A HA3  1 
ATOM   2307 N  N    . CYS A 1 127 ? 12.04100  -23.50700 -16.14400 1.000 23.14000 ? 127 CYS A N    1 
ATOM   2308 C  CA   . CYS A 1 127 ? 12.13600  -22.15100 -15.63600 1.000 22.21000 ? 127 CYS A CA   1 
ATOM   2309 C  C    . CYS A 1 127 ? 13.58500  -21.71700 -15.43700 1.000 26.94000 ? 127 CYS A C    1 
ATOM   2310 O  O    . CYS A 1 127 ? 14.42400  -22.49000 -14.96500 1.000 28.13000 ? 127 CYS A O    1 
ATOM   2311 C  CB   . CYS A 1 127 ? 11.42300  -22.05500 -14.28600 1.000 22.86000 ? 127 CYS A CB   1 
ATOM   2312 S  SG   . CYS A 1 127 ? 9.65300   -22.45900 -14.30100 1.000 22.31000 ? 127 CYS A SG   1 
ATOM   2313 H  H    . CYS A 1 127 ? 11.90600  -24.11300 -15.54900 1.000 27.79000 ? 127 CYS A H    1 
ATOM   2314 H  HA   . CYS A 1 127 ? 11.72400  -21.55500 -16.28100 1.000 26.68000 ? 127 CYS A HA   1 
ATOM   2315 H  HB2  . CYS A 1 127 ? 11.85300  -22.66900 -13.67100 1.000 27.45000 ? 127 CYS A HB2  1 
ATOM   2316 H  HB3  . CYS A 1 127 ? 11.50800  -21.14500 -13.96100 1.000 27.45000 ? 127 CYS A HB3  1 
ATOM   2317 N  N    A ARG A 1 128 ? 13.85300  -20.45300 -15.76400 0.360 28.05000 ? 128 ARG A N    1 
ATOM   2318 N  N    B ARG A 1 128 ? 13.87900  -20.46900 -15.79600 0.640 27.99000 ? 128 ARG A N    1 
ATOM   2319 C  CA   A ARG A 1 128 ? 15.13600  -19.80400 -15.49400 0.360 31.39000 ? 128 ARG A CA   1 
ATOM   2320 C  CA   B ARG A 1 128 ? 15.19000  -19.89400 -15.50200 0.640 31.35000 ? 128 ARG A CA   1 
ATOM   2321 C  C    A ARG A 1 128 ? 15.15900  -19.38100 -14.03100 0.360 29.86000 ? 128 ARG A C    1 
ATOM   2322 C  C    B ARG A 1 128 ? 15.19800  -19.39200 -14.06400 0.640 29.68000 ? 128 ARG A C    1 
ATOM   2323 O  O    A ARG A 1 128 ? 14.52900  -18.38900 -13.65100 0.360 36.49000 ? 128 ARG A O    1 
ATOM   2324 O  O    B ARG A 1 128 ? 14.59900  -18.35500 -13.75000 0.640 36.83000 ? 128 ARG A O    1 
ATOM   2325 C  CB   A ARG A 1 128 ? 15.28700  -18.58500 -16.40000 0.360 34.08000 ? 128 ARG A CB   1 
ATOM   2326 C  CB   B ARG A 1 128 ? 15.53700  -18.77300 -16.47900 0.640 34.98000 ? 128 ARG A CB   1 
ATOM   2327 C  CG   A ARG A 1 128 ? 16.57000  -18.54000 -17.20500 0.360 39.94000 ? 128 ARG A CG   1 
ATOM   2328 C  CG   B ARG A 1 128 ? 17.03900  -18.52000 -16.55900 0.640 35.26000 ? 128 ARG A CG   1 
ATOM   2329 C  CD   A ARG A 1 128 ? 16.63500  -17.28200 -18.07600 0.360 33.94000 ? 128 ARG A CD   1 
ATOM   2330 C  CD   B ARG A 1 128 ? 17.38200  -17.28200 -17.39000 0.640 28.59000 ? 128 ARG A CD   1 
ATOM   2331 N  NE   A ARG A 1 128 ? 15.98200  -17.48600 -19.36400 0.360 37.46000 ? 128 ARG A NE   1 
ATOM   2332 N  NE   B ARG A 1 128 ? 18.82400  -17.05800 -17.43100 0.640 32.39000 ? 128 ARG A NE   1 
ATOM   2333 C  CZ   A ARG A 1 128 ? 15.01500  -16.72500 -19.86200 0.360 35.88000 ? 128 ARG A CZ   1 
ATOM   2334 C  CZ   B ARG A 1 128 ? 19.66600  -17.76500 -18.17200 0.640 45.66000 ? 128 ARG A CZ   1 
ATOM   2335 N  NH1  A ARG A 1 128 ? 14.59000  -15.64000 -19.23400 0.360 36.15000 ? 128 ARG A NH1  1 
ATOM   2336 N  NH1  B ARG A 1 128 ? 19.24300  -18.74200 -18.95900 0.640 40.04000 ? 128 ARG A NH1  1 
ATOM   2337 N  NH2  A ARG A 1 128 ? 14.46100  -17.05900 -21.02300 0.360 34.58000 ? 128 ARG A NH2  1 
ATOM   2338 N  NH2  B ARG A 1 128 ? 20.96700  -17.49100 -18.11600 0.640 45.10000 ? 128 ARG A NH2  1 
ATOM   2339 H  H    A ARG A 1 128 ? 13.29000  -19.93300 -16.15400 0.360 33.69000 ? 128 ARG A H    1 
ATOM   2340 H  H    B ARG A 1 128 ? 13.34000  -19.93900 -16.20700 0.640 33.61000 ? 128 ARG A H    1 
ATOM   2341 H  HA   A ARG A 1 128 ? 15.86300  -20.42500 -15.65500 0.360 37.69000 ? 128 ARG A HA   1 
ATOM   2342 H  HA   B ARG A 1 128 ? 15.86300  -20.58500 -15.59700 0.640 37.64000 ? 128 ARG A HA   1 
ATOM   2343 H  HB2  A ARG A 1 128 ? 14.54900  -18.57700 -17.02900 0.360 40.92000 ? 128 ARG A HB2  1 
ATOM   2344 H  HB2  B ARG A 1 128 ? 15.22300  -19.01500 -17.36400 0.640 42.01000 ? 128 ARG A HB2  1 
ATOM   2345 H  HB3  A ARG A 1 128 ? 15.26100  -17.78800 -15.84900 0.360 40.92000 ? 128 ARG A HB3  1 
ATOM   2346 H  HB3  B ARG A 1 128 ? 15.10700  -17.95400 -16.18800 0.640 42.01000 ? 128 ARG A HB3  1 
ATOM   2347 H  HG2  A ARG A 1 128 ? 17.32900  -18.53400 -16.60100 0.360 47.95000 ? 128 ARG A HG2  1 
ATOM   2348 H  HG2  B ARG A 1 128 ? 17.38700  -18.38700 -15.66300 0.640 42.34000 ? 128 ARG A HG2  1 
ATOM   2349 H  HG3  A ARG A 1 128 ? 16.61400  -19.31700 -17.78500 0.360 47.95000 ? 128 ARG A HG3  1 
ATOM   2350 H  HG3  B ARG A 1 128 ? 17.46800  -19.28700 -16.97100 0.640 42.34000 ? 128 ARG A HG3  1 
ATOM   2351 H  HD2  A ARG A 1 128 ? 16.18700  -16.55300 -17.61900 0.360 40.75000 ? 128 ARG A HD2  1 
ATOM   2352 H  HD2  B ARG A 1 128 ? 17.06600  -17.40500 -18.29900 0.640 34.33000 ? 128 ARG A HD2  1 
ATOM   2353 H  HD3  A ARG A 1 128 ? 17.56300  -17.05200 -18.23800 0.360 40.75000 ? 128 ARG A HD3  1 
ATOM   2354 H  HD3  B ARG A 1 128 ? 16.96200  -16.50200 -16.99500 0.640 34.33000 ? 128 ARG A HD3  1 
ATOM   2355 H  HE   A ARG A 1 128 ? 16.24500  -18.15300 -19.84000 0.360 44.98000 ? 128 ARG A HE   1 
ATOM   2356 H  HE   B ARG A 1 128 ? 19.14700  -16.42700 -16.94400 0.640 38.89000 ? 128 ARG A HE   1 
ATOM   2357 H  HH11 A ARG A 1 128 ? 14.94200  -15.41200 -18.48300 0.360 43.41000 ? 128 ARG A HH11 1 
ATOM   2358 H  HH11 B ARG A 1 128 ? 18.40400  -18.92900 -18.99900 0.640 48.07000 ? 128 ARG A HH11 1 
ATOM   2359 H  HH12 A ARG A 1 128 ? 13.96200  -15.16300 -19.57700 0.360 43.41000 ? 128 ARG A HH12 1 
ATOM   2360 H  HH12 B ARG A 1 128 ? 19.80600  -19.18800 -19.43100 0.640 48.07000 ? 128 ARG A HH12 1 
ATOM   2361 H  HH21 A ARG A 1 128 ? 14.73000  -17.76100 -21.44200 0.360 41.52000 ? 128 ARG A HH21 1 
ATOM   2362 H  HH21 B ARG A 1 128 ? 21.25200  -16.86200 -17.60400 0.640 54.15000 ? 128 ARG A HH21 1 
ATOM   2363 H  HH22 A ARG A 1 128 ? 13.83300  -16.57400 -21.35600 0.360 41.52000 ? 128 ARG A HH22 1 
ATOM   2364 H  HH22 B ARG A 1 128 ? 21.52200  -17.94400 -18.59100 0.640 54.15000 ? 128 ARG A HH22 1 
ATOM   2365 N  N    . LEU A 1 129 ? 15.88600  -20.12400 -13.19600 1.000 28.01000 ? 129 LEU A N    1 
ATOM   2366 C  CA   . LEU A 1 129 ? 15.93000  -19.81500 -11.77100 1.000 31.87000 ? 129 LEU A CA   1 
ATOM   2367 C  C    . LEU A 1 129 ? 17.34500  -19.68300 -11.23500 1.000 51.27000 ? 129 LEU A C    1 
ATOM   2368 O  O    . LEU A 1 129 ? 17.52500  -19.23600 -10.09800 1.000 43.51000 ? 129 LEU A O    1 
ATOM   2369 C  CB   . LEU A 1 129 ? 15.20700  -20.89400 -10.96100 1.000 33.51000 ? 129 LEU A CB   1 
ATOM   2370 C  CG   . LEU A 1 129 ? 13.74500  -21.13100 -11.32300 1.000 36.69000 ? 129 LEU A CG   1 
ATOM   2371 C  CD1  . LEU A 1 129 ? 13.22200  -22.34700 -10.57700 1.000 39.41000 ? 129 LEU A CD1  1 
ATOM   2372 C  CD2  . LEU A 1 129 ? 12.89000  -19.90500 -11.01600 1.000 36.47000 ? 129 LEU A CD2  1 
ATOM   2373 O  OXT  . LEU A 1 129 ? 18.31200  -20.03400 -11.91200 1.000 45.66000 ? 129 LEU A OXT  1 
ATOM   2374 H  H    . LEU A 1 129 ? 16.34500  -20.81900 -13.41100 1.000 33.63000 ? 129 LEU A H    1 
ATOM   2375 H  HA   . LEU A 1 129 ? 15.48500  -18.96100 -11.65400 1.000 38.27000 ? 129 LEU A HA   1 
ATOM   2376 H  HB2  . LEU A 1 129 ? 15.67500  -21.73400 -11.09100 1.000 40.24000 ? 129 LEU A HB2  1 
ATOM   2377 H  HB3  . LEU A 1 129 ? 15.23500  -20.64000 -10.02600 1.000 40.24000 ? 129 LEU A HB3  1 
ATOM   2378 H  HG   . LEU A 1 129 ? 13.67800  -21.29500 -12.27700 1.000 44.06000 ? 129 LEU A HG   1 
ATOM   2379 H  HD11 . LEU A 1 129 ? 12.33900  -22.56700 -10.91200 1.000 47.32000 ? 129 LEU A HD11 1 
ATOM   2380 H  HD12 . LEU A 1 129 ? 13.82700  -23.09100 -10.72400 1.000 47.32000 ? 129 LEU A HD12 1 
ATOM   2381 H  HD13 . LEU A 1 129 ? 13.17500  -22.14000 -9.63100  1.000 47.32000 ? 129 LEU A HD13 1 
ATOM   2382 H  HD21 . LEU A 1 129 ? 11.96000  -20.11500 -11.19400 1.000 43.79000 ? 129 LEU A HD21 1 
ATOM   2383 H  HD22 . LEU A 1 129 ? 13.00400  -19.66700 -10.08300 1.000 43.79000 ? 129 LEU A HD22 1 
ATOM   2384 H  HD23 . LEU A 1 129 ? 13.17700  -19.17100 -11.58200 1.000 43.79000 ? 129 LEU A HD23 1 
HETATM 2385 C  C1   . EDO B 2 .   ? 7.69000   -29.23400 10.16300  1.000 40.93000 ? 201 EDO A C1   1 
HETATM 2386 O  O1   . EDO B 2 .   ? 6.51700   -28.53900 10.62000  1.000 23.27000 ? 201 EDO A O1   1 
HETATM 2387 C  C2   . EDO B 2 .   ? 8.94500   -28.56800 10.71800  1.000 45.04000 ? 201 EDO A C2   1 
HETATM 2388 O  O2   . EDO B 2 .   ? 8.91600   -28.58800 12.14800  1.000 58.49000 ? 201 EDO A O2   1 
HETATM 2389 H  H11  . EDO B 2 .   ? 7.65100   -30.27500 10.48900  1.000 49.14000 ? 201 EDO A H11  1 
HETATM 2390 H  H12  . EDO B 2 .   ? 7.72000   -29.22500 9.07100   1.000 49.14000 ? 201 EDO A H12  1 
HETATM 2391 H  HO1  . EDO B 2 .   ? 5.98500   -28.26800 9.85900   1.000 27.95000 ? 201 EDO A HO1  1 
HETATM 2392 H  H21  . EDO B 2 .   ? 9.83200   -29.09400 10.35900  1.000 54.07000 ? 201 EDO A H21  1 
HETATM 2393 H  H22  . EDO B 2 .   ? 9.00200   -27.53600 10.36500  1.000 54.07000 ? 201 EDO A H22  1 
HETATM 2394 H  HO2  . EDO B 2 .   ? 9.70500   -28.14800 12.49300  1.000 70.21000 ? 201 EDO A HO2  1 
HETATM 2395 C  C1   A EDO C 2 .   ? -3.38400  -22.31600 5.50100   0.510 23.72000 ? 202 EDO A C1   1 
HETATM 2396 C  C1   B EDO C 2 .   ? -2.94600  -22.29700 6.35900   0.490 30.45000 ? 202 EDO A C1   1 
HETATM 2397 O  O1   A EDO C 2 .   ? -4.80600  -22.23100 5.34500   0.510 24.20000 ? 202 EDO A O1   1 
HETATM 2398 O  O1   B EDO C 2 .   ? -4.30200  -22.00300 6.06600   0.490 19.84000 ? 202 EDO A O1   1 
HETATM 2399 C  C2   A EDO C 2 .   ? -3.00900  -23.77800 5.44400   0.510 24.51000 ? 202 EDO A C2   1 
HETATM 2400 C  C2   B EDO C 2 .   ? -2.70900  -23.77500 6.10300   0.490 31.39000 ? 202 EDO A C2   1 
HETATM 2401 O  O2   A EDO C 2 .   ? -4.03000  -24.46200 4.71800   0.510 33.17000 ? 202 EDO A O2   1 
HETATM 2402 O  O2   B EDO C 2 .   ? -3.74100  -24.53200 6.74500   0.490 23.65000 ? 202 EDO A O2   1 
HETATM 2403 H  H11  A EDO C 2 .   ? -2.88000  -21.76200 4.70600   0.510 28.48000 ? 202 EDO A H11  1 
HETATM 2404 H  H11  B EDO C 2 .   ? -2.28700  -21.69600 5.72800   0.490 36.57000 ? 202 EDO A H11  1 
HETATM 2405 H  H12  A EDO C 2 .   ? -3.08000  -21.88200 6.45600   0.510 28.48000 ? 202 EDO A H12  1 
HETATM 2406 H  H12  B EDO C 2 .   ? -2.72600  -22.05600 7.40100   0.490 36.57000 ? 202 EDO A H12  1 
HETATM 2407 H  HO1  A EDO C 2 .   ? -5.04700  -21.33700 5.06700   0.510 29.07000 ? 202 EDO A HO1  1 
HETATM 2408 H  HO1  B EDO C 2 .   ? -4.69600  -21.52700 6.81000   0.490 23.84000 ? 202 EDO A HO1  1 
HETATM 2409 H  H21  A EDO C 2 .   ? -2.04400  -23.90200 4.94800   0.510 29.43000 ? 202 EDO A H21  1 
HETATM 2410 H  H21  B EDO C 2 .   ? -2.71300  -23.97300 5.02900   0.490 37.69000 ? 202 EDO A H21  1 
HETATM 2411 H  H22  A EDO C 2 .   ? -2.92200  -24.18700 6.45300   0.510 29.43000 ? 202 EDO A H22  1 
HETATM 2412 H  H22  B EDO C 2 .   ? -1.73200  -24.06900 6.49400   0.490 37.69000 ? 202 EDO A H22  1 
HETATM 2413 H  HO2  A EDO C 2 .   ? -3.90200  -25.41600 4.80300   0.510 39.83000 ? 202 EDO A HO2  1 
HETATM 2414 H  HO2  B EDO C 2 .   ? -3.49700  -25.46800 6.75400   0.490 28.41000 ? 202 EDO A HO2  1 
HETATM 2415 C  C1   . EDO D 2 .   ? -15.56200 -15.48300 0.54900   0.320 15.81000 ? 203 EDO A C1   1 
HETATM 2416 O  O1   . EDO D 2 .   ? -14.27300 -15.13100 1.04600   0.320 27.24000 ? 203 EDO A O1   1 
HETATM 2417 C  C2   . EDO D 2 .   ? -15.75300 -14.88600 -0.83000  0.320 20.43000 ? 203 EDO A C2   1 
HETATM 2418 O  O2   . EDO D 2 .   ? -14.88000 -15.52400 -1.76800  0.320 19.18000 ? 203 EDO A O2   1 
HETATM 2419 H  H11  . EDO D 2 .   ? -15.65600 -16.57000 0.49900   0.320 19.00000 ? 203 EDO A H11  1 
HETATM 2420 H  H12  . EDO D 2 .   ? -16.33500 -15.11000 1.22500   0.320 19.00000 ? 203 EDO A H12  1 
HETATM 2421 H  HO1  . EDO D 2 .   ? -14.16800 -15.47800 1.94300   0.320 32.72000 ? 203 EDO A HO1  1 
HETATM 2422 H  H21  . EDO D 2 .   ? -16.79100 -15.01600 -1.14600  0.320 24.54000 ? 203 EDO A H21  1 
HETATM 2423 H  H22  . EDO D 2 .   ? -15.54300 -13.81500 -0.80000  0.320 24.54000 ? 203 EDO A H22  1 
HETATM 2424 H  HO2  . EDO D 2 .   ? -15.02600 -15.15200 -2.64800  0.320 23.04000 ? 203 EDO A HO2  1 
HETATM 2425 C  C1   . EDO E 2 .   ? 15.62300  -16.39300 -8.69900  0.310 34.50000 ? 204 EDO A C1   1 
HETATM 2426 O  O1   . EDO E 2 .   ? 15.75900  -15.55000 -7.54900  0.310 36.85000 ? 204 EDO A O1   1 
HETATM 2427 C  C2   . EDO E 2 .   ? 15.95400  -15.60600 -9.96200  0.310 33.53000 ? 204 EDO A C2   1 
HETATM 2428 O  O2   . EDO E 2 .   ? 15.05800  -14.49600 -10.10000 0.310 27.21000 ? 204 EDO A O2   1 
HETATM 2429 H  H11  . EDO E 2 .   ? 16.29500  -17.24900 -8.61000  0.310 41.43000 ? 204 EDO A H11  1 
HETATM 2430 H  H12  . EDO E 2 .   ? 14.60100  -16.77400 -8.75800  0.310 41.43000 ? 204 EDO A H12  1 
HETATM 2431 H  HO1  . EDO E 2 .   ? 15.61000  -16.07000 -6.74800  0.310 44.25000 ? 204 EDO A HO1  1 
HETATM 2432 H  H21  . EDO E 2 .   ? 16.98300  -15.24400 -9.91200  0.310 40.26000 ? 204 EDO A H21  1 
HETATM 2433 H  H22  . EDO E 2 .   ? 15.87000  -16.25700 -10.83500 0.310 40.26000 ? 204 EDO A H22  1 
HETATM 2434 H  HO2  . EDO E 2 .   ? 15.30000  -13.98100 -10.88100 0.310 32.68000 ? 204 EDO A HO2  1 
HETATM 2435 C  C1   . EDO F 2 .   ? 6.60600   -35.51900 -3.52100  1.000 45.46000 ? 205 EDO A C1   1 
HETATM 2436 O  O1   . EDO F 2 .   ? 6.43600   -36.32000 -2.34300  1.000 48.41000 ? 205 EDO A O1   1 
HETATM 2437 C  C2   . EDO F 2 .   ? 7.33900   -34.23500 -3.14800  1.000 53.55000 ? 205 EDO A C2   1 
HETATM 2438 O  O2   . EDO F 2 .   ? 6.90200   -33.76500 -1.86500  1.000 30.30000 ? 205 EDO A O2   1 
HETATM 2439 H  H11  . EDO F 2 .   ? 7.17800   -36.07100 -4.26900  1.000 54.57000 ? 205 EDO A H11  1 
HETATM 2440 H  H12  . EDO F 2 .   ? 5.63100   -35.28000 -3.95300  1.000 54.57000 ? 205 EDO A H12  1 
HETATM 2441 H  HO1  . EDO F 2 .   ? 6.20900   -37.22500 -2.59800  1.000 58.12000 ? 205 EDO A HO1  1 
HETATM 2442 H  H21  . EDO F 2 .   ? 8.41500   -34.42100 -3.12300  1.000 64.29000 ? 205 EDO A H21  1 
HETATM 2443 H  H22  . EDO F 2 .   ? 7.14800   -33.47000 -3.90300  1.000 64.29000 ? 205 EDO A H22  1 
HETATM 2444 H  HO2  . EDO F 2 .   ? 7.32600   -32.91800 -1.67000  1.000 36.39000 ? 205 EDO A HO2  1 
HETATM 2445 C  C1   . EDO G 2 .   ? 2.37000   -6.63700  2.12900   1.000 55.24000 ? 206 EDO A C1   1 
HETATM 2446 O  O1   . EDO G 2 .   ? 1.02300   -6.99500  1.79000   1.000 49.48000 ? 206 EDO A O1   1 
HETATM 2447 C  C2   . EDO G 2 .   ? 3.36200   -7.32300  1.19200   1.000 57.76000 ? 206 EDO A C2   1 
HETATM 2448 O  O2   . EDO G 2 .   ? 3.07600   -8.72500  1.05400   1.000 31.24000 ? 206 EDO A O2   1 
HETATM 2449 H  H11  . EDO G 2 .   ? 2.48900   -5.55400  2.05900   1.000 66.31000 ? 206 EDO A H11  1 
HETATM 2450 H  H12  . EDO G 2 .   ? 2.57800   -6.93200  3.16000   1.000 66.31000 ? 206 EDO A H12  1 
HETATM 2451 H  HO1  . EDO G 2 .   ? 0.40700   -6.48100  2.33000   1.000 59.40000 ? 206 EDO A HO1  1 
HETATM 2452 H  H21  . EDO G 2 .   ? 3.31900   -6.84700  0.20900   1.000 69.34000 ? 206 EDO A H21  1 
HETATM 2453 H  H22  . EDO G 2 .   ? 4.37400   -7.19700  1.58200   1.000 69.34000 ? 206 EDO A H22  1 
HETATM 2454 H  HO2  . EDO G 2 .   ? 3.74900   -9.13700  0.49500   1.000 37.51000 ? 206 EDO A HO2  1 
HETATM 2455 CL CL   . CL  H 3 .   ? 8.34500   -31.88200 7.38600   1.000 20.89000 ? 207 CL  A CL   1 
HETATM 2456 CL CL   . CL  I 3 .   ? 11.20000  -31.97400 -1.81500  1.000 28.84000 ? 208 CL  A CL   1 
HETATM 2457 CL CL   . CL  J 3 .   ? 6.90800   -10.46100 -4.46700  1.000 54.86000 ? 209 CL  A CL   1 
HETATM 2458 CL CL   . CL  K 3 .   ? 0.50700   -23.68300 -14.94100 1.000 48.38000 ? 210 CL  A CL   1 
HETATM 2459 NA NA   . NA  L 4 .   ? -8.08000  -14.68000 12.85700  1.000 20.15000 ? 211 NA  A NA   1 
HETATM 2460 NA NA   . NA  M 4 .   ? 11.17900  -29.12400 -6.99300  1.000 26.93000 ? 212 NA  A NA   1 
HETATM 2461 O  O    . HOH N 5 .   ? -5.96400  -40.31800 4.37800   1.000 65.13000 ? 301 HOH A O    1 
HETATM 2462 O  O    B HOH N 5 .   ? 18.35200  -20.56800 -3.00400  1.000 51.74000 ? 302 HOH A O    1 
HETATM 2463 O  O    A HOH N 5 .   ? -7.51500  -24.50500 0.71400   0.520 29.51000 ? 303 HOH A O    1 
HETATM 2464 O  O    B HOH N 5 .   ? -6.36300  -24.09100 2.36500   0.480 35.45000 ? 303 HOH A O    1 
HETATM 2465 O  O    . HOH N 5 .   ? 10.11500  -33.25900 -14.38200 1.000 56.29000 ? 304 HOH A O    1 
HETATM 2466 O  O    . HOH N 5 .   ? -11.37100 -23.38000 1.39700   1.000 49.13000 ? 305 HOH A O    1 
HETATM 2467 O  O    . HOH N 5 .   ? 14.26200  -31.22700 -0.32800  1.000 30.00000 ? 306 HOH A O    1 
HETATM 2468 O  O    . HOH N 5 .   ? -3.79100  -8.33000  -5.67200  1.000 41.40000 ? 307 HOH A O    1 
HETATM 2469 O  O    . HOH N 5 .   ? -4.35500  -23.90700 9.08800   1.000 34.89000 ? 308 HOH A O    1 
HETATM 2470 O  O    . HOH N 5 .   ? -8.19600  -24.72500 -1.18200  1.000 33.63000 ? 309 HOH A O    1 
HETATM 2471 O  O    . HOH N 5 .   ? -1.32700  -13.83100 -2.20300  1.000 27.96000 ? 310 HOH A O    1 
HETATM 2472 O  O    . HOH N 5 .   ? 13.664    -31.426   -15.315   1.000 57.50000 ? 311 HOH A O    1 
HETATM 2473 O  O    . HOH N 5 .   ? 4.08500   -13.10400 9.13700   1.000 47.94000 ? 312 HOH A O    1 
HETATM 2474 O  O    . HOH N 5 .   ? 6.93200   -11.08000 -10.81200 1.000 59.31000 ? 313 HOH A O    1 
HETATM 2475 O  O    . HOH N 5 .   ? -1.75700  -33.95900 -9.01900  1.000 31.90000 ? 314 HOH A O    1 
HETATM 2476 O  O    . HOH N 5 .   ? -1.22900  -12.59300 17.41800  1.000 54.72000 ? 315 HOH A O    1 
HETATM 2477 O  O    . HOH N 5 .   ? 15.56300  -22.36900 2.10900   1.000 43.15000 ? 316 HOH A O    1 
HETATM 2478 O  O    . HOH N 5 .   ? -7.768    -24.831   -7.619    1.000 43.61000 ? 317 HOH A O    1 
HETATM 2479 O  O    . HOH N 5 .   ? -11.60200 -13.44400 -4.11600  1.000 18.78000 ? 318 HOH A O    1 
HETATM 2480 O  O    . HOH N 5 .   ? -1.34400  -26.89700 10.76700  1.000 59.91000 ? 319 HOH A O    1 
HETATM 2481 O  O    . HOH N 5 .   ? -5.81500  -26.47200 1.88000   1.000 27.84000 ? 320 HOH A O    1 
HETATM 2482 O  O    . HOH N 5 .   ? 6.448     -35.314   0.276     1.000 24.79000 ? 321 HOH A O    1 
HETATM 2483 O  O    A HOH N 5 .   ? -12.63300 -13.59700 18.56500  0.700 32.93000 ? 322 HOH A O    1 
HETATM 2484 O  O    B HOH N 5 .   ? -12.94200 -11.34500 18.06300  0.300 36.67000 ? 322 HOH A O    1 
HETATM 2485 O  O    . HOH N 5 .   ? -0.69400  -18.33500 -14.92700 1.000 32.80000 ? 323 HOH A O    1 
HETATM 2486 O  O    . HOH N 5 .   ? -14.01000 -15.14200 7.72400   1.000 18.06000 ? 324 HOH A O    1 
HETATM 2487 O  O    . HOH N 5 .   ? 0.19800   -12.21900 -2.11800  1.000 31.57000 ? 325 HOH A O    1 
HETATM 2488 O  O    . HOH N 5 .   ? -12.40300 -25.43400 12.28900  1.000 41.34000 ? 326 HOH A O    1 
HETATM 2489 O  O    . HOH N 5 .   ? 1.75000   -12.18600 -14.28600 1.000 41.58000 ? 327 HOH A O    1 
HETATM 2490 O  O    . HOH N 5 .   ? 2.77500   -32.67700 -9.47700  1.000 31.33000 ? 328 HOH A O    1 
HETATM 2491 O  O    . HOH N 5 .   ? -7.62700  -26.39600 -3.38600  1.000 30.17000 ? 329 HOH A O    1 
HETATM 2492 O  O    . HOH N 5 .   ? -5.65700  -10.95400 -9.53300  1.000 18.47000 ? 330 HOH A O    1 
HETATM 2493 O  O    . HOH N 5 .   ? -1.23500  -36.52100 -3.50300  1.000 24.38000 ? 331 HOH A O    1 
HETATM 2494 O  O    . HOH N 5 .   ? -9.22500  -22.70700 -0.08100  1.000 27.61000 ? 332 HOH A O    1 
HETATM 2495 O  O    . HOH N 5 .   ? -1.84200  -24.34000 14.80200  1.000 58.96000 ? 333 HOH A O    1 
HETATM 2496 O  O    . HOH N 5 .   ? -3.31500  -7.31600  -8.23500  1.000 35.99000 ? 334 HOH A O    1 
HETATM 2497 O  O    B HOH N 5 .   ? 2.50400   -27.47600 9.61600   0.560 18.86000 ? 335 HOH A O    1 
HETATM 2498 O  O    . HOH N 5 .   ? -9.77900  -24.89900 2.94700   1.000 53.02000 ? 336 HOH A O    1 
HETATM 2499 O  O    . HOH N 5 .   ? 10.65500  -31.97100 5.08000   1.000 25.53000 ? 337 HOH A O    1 
HETATM 2500 O  O    . HOH N 5 .   ? 13.59300  -17.16600 6.03300   1.000 54.90000 ? 338 HOH A O    1 
HETATM 2501 O  O    . HOH N 5 .   ? -2.995    -19.720   23.678    1.000 31.78000 ? 339 HOH A O    1 
HETATM 2502 O  O    . HOH N 5 .   ? -1.67400  -16.63400 0.75400   1.000 16.34000 ? 340 HOH A O    1 
HETATM 2503 O  O    . HOH N 5 .   ? -9.98500  -23.96300 10.02600  1.000 54.70000 ? 341 HOH A O    1 
HETATM 2504 O  O    . HOH N 5 .   ? -0.25700  -14.99900 20.51200  1.000 55.90000 ? 342 HOH A O    1 
HETATM 2505 O  O    A HOH N 5 .   ? 14.81600  -20.12400 -1.88300  0.420 21.50000 ? 343 HOH A O    1 
HETATM 2506 O  O    B HOH N 5 .   ? 14.31000  -26.19200 -4.43000  0.580 18.02000 ? 343 HOH A O    1 
HETATM 2507 O  O    . HOH N 5 .   ? -9.96700  -13.12900 12.00000  1.000 22.60000 ? 344 HOH A O    1 
HETATM 2508 O  O    . HOH N 5 .   ? -8.34400  -17.86800 -8.25800  1.000 26.81000 ? 345 HOH A O    1 
HETATM 2509 O  O    . HOH N 5 .   ? 15.03400  -24.68900 6.34500   1.000 36.15000 ? 346 HOH A O    1 
HETATM 2510 O  O    . HOH N 5 .   ? 12.12100  -12.45600 -8.63000  0.720 40.66000 ? 347 HOH A O    1 
HETATM 2511 O  O    . HOH N 5 .   ? -17.33600 -8.21400  11.32200  1.000 38.02000 ? 348 HOH A O    1 
HETATM 2512 O  O    . HOH N 5 .   ? 17.222    -26.320   3.899     1.000 50.69000 ? 349 HOH A O    1 
HETATM 2513 O  O    . HOH N 5 .   ? -9.00100  -23.48800 -2.81400  1.000 38.07000 ? 350 HOH A O    1 
HETATM 2514 O  O    . HOH N 5 .   ? -19.980   -18.245   7.403     1.000 48.19000 ? 351 HOH A O    1 
HETATM 2515 O  O    . HOH N 5 .   ? 17.45700  -22.53400 -14.05600 1.000 43.98000 ? 352 HOH A O    1 
HETATM 2516 O  O    . HOH N 5 .   ? -8.84700  -20.64200 18.34400  1.000 61.97000 ? 353 HOH A O    1 
HETATM 2517 O  O    . HOH N 5 .   ? -0.37600  -38.74800 3.19200   1.000 35.76000 ? 354 HOH A O    1 
HETATM 2518 O  O    . HOH N 5 .   ? -19.077   -10.232   6.224     1.000 24.13000 ? 355 HOH A O    1 
HETATM 2519 O  O    . HOH N 5 .   ? 13.03700  -18.34100 8.72600   1.000 56.75000 ? 356 HOH A O    1 
HETATM 2520 O  O    A HOH N 5 .   ? 11.70900  -18.48400 -16.69900 0.570 32.17000 ? 357 HOH A O    1 
HETATM 2521 O  O    B HOH N 5 .   ? 11.99700  -17.76900 -14.29900 0.430 33.26000 ? 357 HOH A O    1 
HETATM 2522 O  O    . HOH N 5 .   ? 1.12100   -11.52000 0.34500   1.000 23.47000 ? 358 HOH A O    1 
HETATM 2523 O  O    . HOH N 5 .   ? -1.56700  -5.18800  -4.63200  1.000 42.46000 ? 359 HOH A O    1 
HETATM 2524 O  O    . HOH N 5 .   ? -5.23200  -9.29000  15.94300  1.000 42.16000 ? 360 HOH A O    1 
HETATM 2525 O  O    . HOH N 5 .   ? 3.81100   -37.70500 -10.87000 1.000 40.55000 ? 361 HOH A O    1 
HETATM 2526 O  O    . HOH N 5 .   ? 10.65900  -30.08500 8.18800   1.000 50.93000 ? 362 HOH A O    1 
HETATM 2527 O  O    . HOH N 5 .   ? -3.32200  -14.37300 18.19200  1.000 28.22000 ? 363 HOH A O    1 
HETATM 2528 O  O    . HOH N 5 .   ? -16.54100 -19.29300 -0.93900  1.000 27.15000 ? 364 HOH A O    1 
HETATM 2529 O  O    . HOH N 5 .   ? -2.52000  -10.10400 -13.35900 1.000 34.83000 ? 365 HOH A O    1 
HETATM 2530 O  O    . HOH N 5 .   ? -10.472   -5.958    12.489    1.000 27.31000 ? 366 HOH A O    1 
HETATM 2531 O  O    . HOH N 5 .   ? 13.865    -25.717   14.067    1.000 40.28000 ? 367 HOH A O    1 
HETATM 2532 O  O    . HOH N 5 .   ? 5.78400   -22.41100 13.96800  1.000 50.84000 ? 368 HOH A O    1 
HETATM 2533 O  O    A HOH N 5 .   ? -7.19900  -24.22000 6.07600   0.490 31.43000 ? 369 HOH A O    1 
HETATM 2534 O  O    B HOH N 5 .   ? -8.21200  -23.61700 5.10300   0.510 32.48000 ? 369 HOH A O    1 
HETATM 2535 O  O    . HOH N 5 .   ? -7.93600  -12.73500 14.31800  1.000 28.99000 ? 370 HOH A O    1 
HETATM 2536 O  O    A HOH N 5 .   ? -2.83000  -7.47300  12.73600  0.620 34.30000 ? 371 HOH A O    1 
HETATM 2537 O  O    B HOH N 5 .   ? -4.02200  -7.33800  12.34200  0.380 28.15000 ? 371 HOH A O    1 
HETATM 2538 O  O    . HOH N 5 .   ? 11.34600  -12.07200 2.54900   1.000 49.32000 ? 372 HOH A O    1 
HETATM 2539 O  O    . HOH N 5 .   ? -5.69600  -24.22700 -15.29900 1.000 70.78000 ? 373 HOH A O    1 
HETATM 2540 O  O    . HOH N 5 .   ? -5.58200  -6.42700  11.57400  1.000 41.91000 ? 374 HOH A O    1 
HETATM 2541 O  O    . HOH N 5 .   ? 0.98300   -34.14400 9.72700   1.000 57.83000 ? 375 HOH A O    1 
HETATM 2542 O  O    . HOH N 5 .   ? -11.89700 -12.07600 14.04600  1.000 19.16000 ? 376 HOH A O    1 
HETATM 2543 O  O    . HOH N 5 .   ? 7.58100   -38.22200 -5.49400  1.000 69.25000 ? 377 HOH A O    1 
HETATM 2544 O  O    . HOH N 5 .   ? 9.67100   -23.44500 -19.67200 1.000 69.47000 ? 378 HOH A O    1 
HETATM 2545 O  O    . HOH N 5 .   ? 5.98700   -17.47900 -16.14200 1.000 25.89000 ? 379 HOH A O    1 
HETATM 2546 O  O    . HOH N 5 .   ? 16.00600  -29.98100 -4.13100  1.000 58.77000 ? 380 HOH A O    1 
HETATM 2547 O  O    . HOH N 5 .   ? 9.87800   -34.38000 -7.49600  1.000 55.47000 ? 381 HOH A O    1 
HETATM 2548 O  O    . HOH N 5 .   ? 4.05500   -22.80300 -18.58800 1.000 53.51000 ? 382 HOH A O    1 
HETATM 2549 O  O    . HOH N 5 .   ? 1.77300   -19.90900 -16.68000 1.000 45.55000 ? 383 HOH A O    1 
HETATM 2550 O  O    . HOH N 5 .   ? 12.27700  -35.45200 -11.70100 1.000 55.23000 ? 384 HOH A O    1 
HETATM 2551 O  O    . HOH N 5 .   ? -5.23300  -5.23300  0.00000   0.50  60.14000 ? 385 HOH A O    1 
HETATM 2552 O  O    . HOH N 5 .   ? 10.77000  -8.41800  0.55300   1.000 54.20000 ? 386 HOH A O    1 
HETATM 2553 O  O    . HOH N 5 .   ? 5.38700   -10.05000 6.58900   1.000 50.72000 ? 387 HOH A O    1 
HETATM 2554 O  O    . HOH N 5 .   ? 5.98600   -11.25200 13.23700  1.000 71.26000 ? 388 HOH A O    1 
HETATM 2555 O  O    . HOH N 5 .   ? 2.40300   -22.38300 -16.90600 1.000 80.66000 ? 389 HOH A O    1 
HETATM 2556 O  O    . HOH N 5 .   ? -13.36500 -24.70100 14.15600  1.000 53.35000 ? 390 HOH A O    1 
HETATM 2557 O  O    . HOH N 5 .   ? -6.47700  -21.20300 -16.22400 1.000 45.93000 ? 391 HOH A O    1 
HETATM 2558 O  O    . HOH N 5 .   ? -8.08300  -26.85900 -0.31500  1.000 50.03000 ? 392 HOH A O    1 
HETATM 2559 O  O    . HOH N 5 .   ? 15.24400  -32.18100 -2.20800  1.000 48.94000 ? 393 HOH A O    1 
HETATM 2560 O  O    . HOH N 5 .   ? 9.00200   -16.65600 9.54000   1.000 55.07000 ? 394 HOH A O    1 
HETATM 2561 O  O    . HOH N 5 .   ? -14.91700 -11.48400 15.28900  1.000 47.76000 ? 395 HOH A O    1 
HETATM 2562 O  O    . HOH N 5 .   ? 7.50600   -30.61500 -21.78300 1.000 56.98000 ? 396 HOH A O    1 
HETATM 2563 O  O    . HOH N 5 .   ? -4.34000  -7.35200  -10.83600 1.000 60.81000 ? 397 HOH A O    1 
HETATM 2564 O  O    . HOH N 5 .   ? 19.968    -30.044   -1.104    1.000 58.53000 ? 398 HOH A O    1 
HETATM 2565 O  O    . HOH N 5 .   ? 6.98100   -39.59700 -8.29500  1.000 63.07000 ? 399 HOH A O    1 
HETATM 2566 O  O    . HOH N 5 .   ? 0.77400   -39.79200 -0.71700  1.000 53.42000 ? 400 HOH A O    1 
HETATM 2567 O  O    . HOH N 5 .   ? 4.01400   -27.86400 -16.61900 1.000 61.66000 ? 401 HOH A O    1 
HETATM 2568 O  O    . HOH N 5 .   ? -13.702   -6.911    15.618    1.000 60.55000 ? 402 HOH A O    1 
HETATM 2569 O  O    . HOH N 5 .   ? 3.09700   -29.20900 -15.07800 1.000 48.18000 ? 403 HOH A O    1 
HETATM 2570 O  O    . HOH N 5 .   ? -11.50000 -7.20200  15.07700  1.000 61.85000 ? 404 HOH A O    1 
HETATM 2571 O  O    . HOH N 5 .   ? -2.63900  -34.18200 8.50000   1.000 71.93000 ? 405 HOH A O    1 
# 
