data_9FC8
# 
_entry.id   9FC8 
# 
_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   9FC8         pdb_00009fc8 10.2210/pdb9fc8/pdb 
WWPDB D_1292137234 ?            ?                   
# 
_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                        9FC8 
_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    106 ?        ? ? ? 
# 
_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 25  HOH HOH A . 
N 5 HOH 3   303 37  HOH HOH A . 
N 5 HOH 4   304 131 HOH HOH A . 
N 5 HOH 5   305 99  HOH HOH A . 
N 5 HOH 6   306 100 HOH HOH A . 
N 5 HOH 7   307 109 HOH HOH A . 
N 5 HOH 8   308 5   HOH HOH A . 
N 5 HOH 9   309 71  HOH HOH A . 
N 5 HOH 10  310 43  HOH HOH A . 
N 5 HOH 11  311 105 HOH HOH A . 
N 5 HOH 12  312 1   HOH HOH A . 
N 5 HOH 13  313 130 HOH HOH A . 
N 5 HOH 14  314 124 HOH HOH A . 
N 5 HOH 15  315 3   HOH HOH A . 
N 5 HOH 16  316 49  HOH HOH A . 
N 5 HOH 17  317 121 HOH HOH A . 
N 5 HOH 18  318 106 HOH HOH A . 
N 5 HOH 19  319 7   HOH HOH A . 
N 5 HOH 20  320 97  HOH HOH A . 
N 5 HOH 21  321 128 HOH HOH A . 
N 5 HOH 22  322 4   HOH HOH A . 
N 5 HOH 23  323 15  HOH HOH A . 
N 5 HOH 24  324 2   HOH HOH A . 
N 5 HOH 25  325 118 HOH HOH A . 
N 5 HOH 26  326 144 HOH HOH A . 
N 5 HOH 27  327 6   HOH HOH A . 
N 5 HOH 28  328 41  HOH HOH A . 
N 5 HOH 29  329 11  HOH HOH A . 
N 5 HOH 30  330 81  HOH HOH A . 
N 5 HOH 31  331 9   HOH HOH A . 
N 5 HOH 32  332 47  HOH HOH A . 
N 5 HOH 33  333 122 HOH HOH A . 
N 5 HOH 34  334 57  HOH HOH A . 
N 5 HOH 35  335 14  HOH HOH A . 
N 5 HOH 36  336 127 HOH HOH A . 
N 5 HOH 37  337 59  HOH HOH A . 
N 5 HOH 38  338 28  HOH HOH A . 
N 5 HOH 39  339 138 HOH HOH A . 
N 5 HOH 40  340 16  HOH HOH A . 
N 5 HOH 41  341 141 HOH HOH A . 
N 5 HOH 42  342 33  HOH HOH A . 
N 5 HOH 43  343 8   HOH HOH A . 
N 5 HOH 44  344 145 HOH HOH A . 
N 5 HOH 45  345 17  HOH HOH A . 
N 5 HOH 46  346 12  HOH HOH A . 
N 5 HOH 47  347 36  HOH HOH A . 
N 5 HOH 48  348 115 HOH HOH A . 
N 5 HOH 49  349 55  HOH HOH A . 
N 5 HOH 50  350 78  HOH HOH A . 
N 5 HOH 51  351 20  HOH HOH A . 
N 5 HOH 52  352 45  HOH HOH A . 
N 5 HOH 53  353 10  HOH HOH A . 
N 5 HOH 54  354 46  HOH HOH A . 
N 5 HOH 55  355 50  HOH HOH A . 
N 5 HOH 56  356 34  HOH HOH A . 
N 5 HOH 57  357 126 HOH HOH A . 
N 5 HOH 58  358 75  HOH HOH A . 
N 5 HOH 59  359 30  HOH HOH A . 
N 5 HOH 60  360 13  HOH HOH A . 
N 5 HOH 61  361 79  HOH HOH A . 
N 5 HOH 62  362 93  HOH HOH A . 
N 5 HOH 63  363 117 HOH HOH A . 
N 5 HOH 64  364 108 HOH HOH A . 
N 5 HOH 65  365 22  HOH HOH A . 
N 5 HOH 66  366 61  HOH HOH A . 
N 5 HOH 67  367 23  HOH HOH A . 
N 5 HOH 68  368 86  HOH HOH A . 
N 5 HOH 69  369 66  HOH HOH A . 
N 5 HOH 70  370 29  HOH HOH A . 
N 5 HOH 71  371 134 HOH HOH A . 
N 5 HOH 72  372 111 HOH HOH A . 
N 5 HOH 73  373 96  HOH HOH A . 
N 5 HOH 74  374 24  HOH HOH A . 
N 5 HOH 75  375 143 HOH HOH A . 
N 5 HOH 76  376 63  HOH HOH A . 
N 5 HOH 77  377 116 HOH HOH A . 
N 5 HOH 78  378 142 HOH HOH A . 
N 5 HOH 79  379 18  HOH HOH A . 
N 5 HOH 80  380 146 HOH HOH A . 
N 5 HOH 81  381 129 HOH HOH A . 
N 5 HOH 82  382 56  HOH HOH A . 
N 5 HOH 83  383 52  HOH HOH A . 
N 5 HOH 84  384 60  HOH HOH A . 
N 5 HOH 85  385 112 HOH HOH A . 
N 5 HOH 86  386 74  HOH HOH A . 
N 5 HOH 87  387 44  HOH HOH A . 
N 5 HOH 88  388 62  HOH HOH A . 
N 5 HOH 89  389 87  HOH HOH A . 
N 5 HOH 90  390 58  HOH HOH A . 
N 5 HOH 91  391 53  HOH HOH A . 
N 5 HOH 92  392 67  HOH HOH A . 
N 5 HOH 93  393 107 HOH HOH A . 
N 5 HOH 94  394 139 HOH HOH A . 
N 5 HOH 95  395 132 HOH HOH A . 
N 5 HOH 96  396 77  HOH HOH A . 
N 5 HOH 97  397 101 HOH HOH A . 
N 5 HOH 98  398 120 HOH HOH A . 
N 5 HOH 99  399 91  HOH HOH A . 
N 5 HOH 100 400 133 HOH HOH A . 
N 5 HOH 101 401 125 HOH HOH A . 
N 5 HOH 102 402 72  HOH HOH A . 
N 5 HOH 103 403 73  HOH HOH A . 
N 5 HOH 104 404 110 HOH HOH A . 
N 5 HOH 105 405 137 HOH HOH A . 
N 5 HOH 106 406 135 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                     9FC8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     79.718 
_cell.length_a_esd                 ? 
_cell.length_b                     79.718 
_cell.length_b_esd                 ? 
_cell.length_c                     37.477 
_cell.length_c_esd                 ? 
_cell.volume                       238164.818 
_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                         9FC8 
_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                   9FC8 
_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             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.79 
_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   0.7750 
_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        0.7750 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P09 HiPhaX' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          21.11 
_reflns.entry_id                                       9FC8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.4 
_reflns.d_resolution_low                               21.68 
_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                                     24323 
_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                           99.88 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.4 
_reflns_shell.d_res_low                                     1.45 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.18 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2373 
_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                                  0.677 
_reflns_shell.pdbx_CC_star                                  0.898 
_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                               27.94 
_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                                 9FC8 
_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                             21.68 
_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                     24320 
_refine.ls_number_reflns_R_free                  2015 
_refine.ls_number_reflns_R_work                  22305 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 8.29 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1612 
_refine.ls_R_factor_R_free                       0.1938 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1583 
_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                          1.35 
_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                 19.4546 
_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                            0.1561 
_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                        21.68 
_refine_hist.number_atoms_solvent             106 
_refine_hist.number_atoms_total               1137 
_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' ? 0.0094  ? 1276 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0483  ? 1735 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0827  ? 168  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0111  ? 241  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.3694 ? 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  . . 140 1548 99.59  . . . . 0.3024 . . . . . . . . . . . 0.2907 
'X-RAY DIFFRACTION' 1.44 1.47  . . 143 1560 99.88  . . . . 0.2610 . . . . . . . . . . . 0.2993 
'X-RAY DIFFRACTION' 1.47 1.52  . . 140 1567 100.00 . . . . 0.2325 . . . . . . . . . . . 0.2442 
'X-RAY DIFFRACTION' 1.52 1.57  . . 142 1571 100.00 . . . . 0.2154 . . . . . . . . . . . 0.2428 
'X-RAY DIFFRACTION' 1.57 1.62  . . 139 1564 100.00 . . . . 0.1976 . . . . . . . . . . . 0.2292 
'X-RAY DIFFRACTION' 1.62 1.69  . . 143 1573 100.00 . . . . 0.1920 . . . . . . . . . . . 0.2196 
'X-RAY DIFFRACTION' 1.69 1.76  . . 144 1579 100.00 . . . . 0.1848 . . . . . . . . . . . 0.2336 
'X-RAY DIFFRACTION' 1.76 1.86  . . 140 1583 99.88  . . . . 0.1732 . . . . . . . . . . . 0.1975 
'X-RAY DIFFRACTION' 1.86 1.97  . . 145 1582 100.00 . . . . 0.1606 . . . . . . . . . . . 0.1859 
'X-RAY DIFFRACTION' 1.97 2.13  . . 142 1588 100.00 . . . . 0.1459 . . . . . . . . . . . 0.1830 
'X-RAY DIFFRACTION' 2.13 2.34  . . 148 1608 100.00 . . . . 0.1416 . . . . . . . . . . . 0.1795 
'X-RAY DIFFRACTION' 2.34 2.68  . . 145 1614 100.00 . . . . 0.1401 . . . . . . . . . . . 0.1731 
'X-RAY DIFFRACTION' 2.68 3.37  . . 148 1633 99.72  . . . . 0.1449 . . . . . . . . . . . 0.1922 
'X-RAY DIFFRACTION' 3.37 21.68 . . 156 1735 99.89  . . . . 0.1522 . . . . . . . . . . . 0.1871 
# 
_struct.entry_id                     9FC8 
_struct.title                        'HEN EGG-WHITE Lysozyme incubated at 60% 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        9FC8 
_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              9FC8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 129 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00698 
_struct_ref_seq.db_align_beg                  19 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  147 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       129 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1780 ? 
1 MORE         -41  ? 
1 'SSA (A^2)'  6770 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 4   ? HIS A 15  ? GLY A 4   HIS A 15  1 ? 12 
HELX_P HELX_P2 AA2 ASN A 19  ? TYR A 23  ? ASN A 19  TYR A 23  5 ? 5  
HELX_P HELX_P3 AA3 SER A 24  ? ASN A 37  ? SER A 24  ASN A 37  1 ? 14 
HELX_P HELX_P4 AA4 PRO A 79  ? SER A 85  ? PRO A 79  SER A 85  5 ? 7  
HELX_P HELX_P5 AA5 ILE A 88  ? SER A 100 ? ILE A 88  SER A 100 1 ? 13 
HELX_P HELX_P6 AA6 ASN A 103 ? ALA A 107 ? ASN A 103 ALA A 107 5 ? 5  
HELX_P HELX_P7 AA7 TRP A 108 ? CYS A 115 ? TRP A 108 CYS A 115 1 ? 8  
HELX_P HELX_P8 AA8 ASP A 119 ? ARG A 125 ? ASP A 119 ARG A 125 5 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 6  SG ? ? ? 1_555 A CYS 127 SG ? ? A CYS 6   A CYS 127 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
disulf2 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 115 SG ? ? A CYS 30  A CYS 115 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 80  SG ? ? A CYS 64  A CYS 80  1_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf4 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 94  SG ? ? A CYS 76  A CYS 94  1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc1 metalc ? ? A SER 24 OG ? ? ? 1_555 M NA  .   NA ? ? A SER 24  A NA  212 1_555 ? ? ? ? ? ? ? 2.878 ? ? 
metalc2 metalc ? ? A SER 60 O  ? ? ? 1_555 L NA  .   NA ? ? A SER 60  A NA  211 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc3 metalc ? ? A CYS 64 O  ? ? ? 1_555 L NA  .   NA ? ? A CYS 64  A NA  211 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc4 metalc ? ? A SER 72 OG ? ? ? 1_555 L NA  .   NA ? ? A SER 72  A NA  211 1_555 ? ? ? ? ? ? ? 2.510 ? ? 
metalc5 metalc ? ? A ARG 73 O  ? ? ? 1_555 L NA  .   NA ? ? A ARG 73  A NA  211 1_555 ? ? ? ? ? ? ? 2.418 ? ? 
metalc6 metalc ? ? L NA  .  NA ? ? ? 1_555 N HOH .   O  ? ? A NA  211 A HOH 343 1_555 ? ? ? ? ? ? ? 2.565 ? ? 
metalc7 metalc ? ? L NA  .  NA ? ? ? 1_555 N HOH .   O  ? ? A NA  211 A HOH 374 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
# 
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 87.9  ? 
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_555 167.4 ? 
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 94.5  ? 
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 94.0  ? 
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 98.5  ? 
7  O  ? A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 343 ? 1_555 99.4  ? 
8  O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 343 ? 1_555 86.1  ? 
9  OG ? A SER 72 ? A SER 72  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 343 ? 1_555 82.3  ? 
10 O  ? A ARG 73 ? A ARG 73  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 343 ? 1_555 166.1 ? 
11 O  ? A SER 60 ? A SER 60  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 374 ? 1_555 172.0 ? 
12 O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 374 ? 1_555 98.7  ? 
13 OG ? A SER 72 ? A SER 72  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 374 ? 1_555 83.5  ? 
14 O  ? A ARG 73 ? A ARG 73  ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 374 ? 1_555 89.6  ? 
15 O  ? N HOH .  ? A HOH 343 ? 1_555 NA ? L NA . ? A NA 211 ? 1_555 O  ? N HOH .  ? A HOH 374 ? 1_555 76.7  ? 
# 
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                   9FC8 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TRP A 62 ? B -132.52 -30.89 
2 1 ARG A 68 ? A -143.34 27.37  
3 1 ARG A 68 ? B -142.65 27.27  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     384 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   N 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+3/4  
3 y+1/2,-x+1/2,z+1/4  
4 x+1/2,-y+1/2,-z+1/4 
5 -x+1/2,y+1/2,-z+3/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
NA  NA   NA N N 261 
PHE N    N  N N 262 
PHE CA   C  N S 263 
PHE C    C  N N 264 
PHE O    O  N N 265 
PHE CB   C  N N 266 
PHE CG   C  Y N 267 
PHE CD1  C  Y N 268 
PHE CD2  C  Y N 269 
PHE CE1  C  Y N 270 
PHE CE2  C  Y N 271 
PHE CZ   C  Y N 272 
PHE OXT  O  N N 273 
PHE H    H  N N 274 
PHE H2   H  N N 275 
PHE HA   H  N N 276 
PHE HB2  H  N N 277 
PHE HB3  H  N N 278 
PHE HD1  H  N N 279 
PHE HD2  H  N N 280 
PHE HE1  H  N N 281 
PHE HE2  H  N N 282 
PHE HZ   H  N N 283 
PHE HXT  H  N N 284 
PRO N    N  N N 285 
PRO CA   C  N S 286 
PRO C    C  N N 287 
PRO O    O  N N 288 
PRO CB   C  N N 289 
PRO CG   C  N N 290 
PRO CD   C  N N 291 
PRO OXT  O  N N 292 
PRO H    H  N N 293 
PRO HA   H  N N 294 
PRO HB2  H  N N 295 
PRO HB3  H  N N 296 
PRO HG2  H  N N 297 
PRO HG3  H  N N 298 
PRO HD2  H  N N 299 
PRO HD3  H  N N 300 
PRO HXT  H  N N 301 
SER N    N  N N 302 
SER CA   C  N S 303 
SER C    C  N N 304 
SER O    O  N N 305 
SER CB   C  N N 306 
SER OG   O  N N 307 
SER OXT  O  N N 308 
SER H    H  N N 309 
SER H2   H  N N 310 
SER HA   H  N N 311 
SER HB2  H  N N 312 
SER HB3  H  N N 313 
SER HG   H  N N 314 
SER HXT  H  N N 315 
THR N    N  N N 316 
THR CA   C  N S 317 
THR C    C  N N 318 
THR O    O  N N 319 
THR CB   C  N R 320 
THR OG1  O  N N 321 
THR CG2  C  N N 322 
THR OXT  O  N N 323 
THR H    H  N N 324 
THR H2   H  N N 325 
THR HA   H  N N 326 
THR HB   H  N N 327 
THR HG1  H  N N 328 
THR HG21 H  N N 329 
THR HG22 H  N N 330 
THR HG23 H  N N 331 
THR HXT  H  N N 332 
TRP N    N  N N 333 
TRP CA   C  N S 334 
TRP C    C  N N 335 
TRP O    O  N N 336 
TRP CB   C  N N 337 
TRP CG   C  Y N 338 
TRP CD1  C  Y N 339 
TRP CD2  C  Y N 340 
TRP NE1  N  Y N 341 
TRP CE2  C  Y N 342 
TRP CE3  C  Y N 343 
TRP CZ2  C  Y N 344 
TRP CZ3  C  Y N 345 
TRP CH2  C  Y N 346 
TRP OXT  O  N N 347 
TRP H    H  N N 348 
TRP H2   H  N N 349 
TRP HA   H  N N 350 
TRP HB2  H  N N 351 
TRP HB3  H  N N 352 
TRP HD1  H  N N 353 
TRP HE1  H  N N 354 
TRP HE3  H  N N 355 
TRP HZ2  H  N N 356 
TRP HZ3  H  N N 357 
TRP HH2  H  N N 358 
TRP HXT  H  N N 359 
TYR N    N  N N 360 
TYR CA   C  N S 361 
TYR C    C  N N 362 
TYR O    O  N N 363 
TYR CB   C  N N 364 
TYR CG   C  Y N 365 
TYR CD1  C  Y N 366 
TYR CD2  C  Y N 367 
TYR CE1  C  Y N 368 
TYR CE2  C  Y N 369 
TYR CZ   C  Y N 370 
TYR OH   O  N N 371 
TYR OXT  O  N N 372 
TYR H    H  N N 373 
TYR H2   H  N N 374 
TYR HA   H  N N 375 
TYR HB2  H  N N 376 
TYR HB3  H  N N 377 
TYR HD1  H  N N 378 
TYR HD2  H  N N 379 
TYR HE1  H  N N 380 
TYR HE2  H  N N 381 
TYR HH   H  N N 382 
TYR HXT  H  N N 383 
VAL N    N  N N 384 
VAL CA   C  N S 385 
VAL C    C  N N 386 
VAL O    O  N N 387 
VAL CB   C  N N 388 
VAL CG1  C  N N 389 
VAL CG2  C  N N 390 
VAL OXT  O  N N 391 
VAL H    H  N N 392 
VAL H2   H  N N 393 
VAL HA   H  N N 394 
VAL HB   H  N N 395 
VAL HG11 H  N N 396 
VAL HG12 H  N N 397 
VAL HG13 H  N N 398 
VAL HG21 H  N N 399 
VAL HG22 H  N N 400 
VAL HG23 H  N N 401 
VAL HXT  H  N N 402 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Helmholtz Association' Germany FISCOV 1 
'Helmholtz Association' Germany FRAGX  2 
'Helmholtz Association' Germany HIR3X  3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'intern model of RT lysozyme' 
# 
_space_group.name_H-M_alt     'P 43 21 2' 
_space_group.name_Hall        'P 4nw 2abw' 
_space_group.IT_number        96 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FC8 
_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]   0.012544 
_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]   0.012544 
_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]   0.026683 
_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   ? -3.25400  -10.21300 -8.62200  0.590 21.85000  ? 1   LYS A N    1 
ATOM   2    N  N    B LYS A 1 1   ? -3.23900  -10.16200 -8.66500  0.410 22.09000  ? 1   LYS A N    1 
ATOM   3    C  CA   A LYS A 1 1   ? -2.35000  -10.55300 -9.76800  0.590 22.77000  ? 1   LYS A CA   1 
ATOM   4    C  CA   B LYS A 1 1   ? -2.33000  -10.52400 -9.79700  0.410 22.81000  ? 1   LYS A CA   1 
ATOM   5    C  C    A LYS A 1 1   ? -2.44500  -12.03800 -10.00200 0.590 20.82000  ? 1   LYS A C    1 
ATOM   6    C  C    B LYS A 1 1   ? -2.38000  -12.02100 -10.00300 0.410 20.72000  ? 1   LYS A C    1 
ATOM   7    O  O    A LYS A 1 1   ? -2.53600  -12.80600 -9.04400  0.590 21.57000  ? 1   LYS A O    1 
ATOM   8    O  O    B LYS A 1 1   ? -2.35600  -12.77700 -9.02700  0.410 21.74000  ? 1   LYS A O    1 
ATOM   9    C  CB   A LYS A 1 1   ? -0.91900  -10.16600 -9.42300  0.590 25.74000  ? 1   LYS A CB   1 
ATOM   10   C  CB   B LYS A 1 1   ? -0.90400  -10.09200 -9.47200  0.410 26.03000  ? 1   LYS A CB   1 
ATOM   11   C  CG   A LYS A 1 1   ? 0.13900   -10.59900 -10.43300 0.590 26.34000  ? 1   LYS A CG   1 
ATOM   12   C  CG   B LYS A 1 1   ? 0.16600   -10.62200 -10.41900 0.410 26.25000  ? 1   LYS A CG   1 
ATOM   13   C  CD   A LYS A 1 1   ? 1.51700   -10.13800 -9.98000  0.590 31.10000  ? 1   LYS A CD   1 
ATOM   14   C  CD   B LYS A 1 1   ? 1.52400   -10.02300 -10.08400 0.410 31.05000  ? 1   LYS A CD   1 
ATOM   15   C  CE   A LYS A 1 1   ? 2.60200   -10.80500 -10.81200 0.590 32.04000  ? 1   LYS A CE   1 
ATOM   16   C  CE   B LYS A 1 1   ? 2.62900   -10.68200 -10.89300 0.410 32.22000  ? 1   LYS A CE   1 
ATOM   17   N  NZ   A LYS A 1 1   ? 3.78400   -9.93300  -11.01000 0.590 39.12000  ? 1   LYS A NZ   1 
ATOM   18   N  NZ   B LYS A 1 1   ? 2.48500   -10.42500 -12.34800 0.410 34.16000  ? 1   LYS A NZ   1 
ATOM   19   H  H1   A LYS A 1 1   ? -4.05400  -10.58100 -8.75500  0.590 26.24000  ? 1   LYS A H1   1 
ATOM   20   H  H1   B LYS A 1 1   ? -3.50600  -10.90300 -8.25000  0.410 26.52000  ? 1   LYS A H1   1 
ATOM   21   H  H2   A LYS A 1 1   ? -2.90600  -10.52800 -7.86600  0.590 26.24000  ? 1   LYS A H2   1 
ATOM   22   H  H2   B LYS A 1 1   ? -2.80300  -9.64100  -8.09000  0.410 26.52000  ? 1   LYS A H2   1 
ATOM   23   H  H3   A LYS A 1 1   ? -3.34000  -9.32900  -8.56400  0.590 26.24000  ? 1   LYS A H3   1 
ATOM   24   H  H3   B LYS A 1 1   ? -3.94700  -9.72700  -8.98100  0.410 26.52000  ? 1   LYS A H3   1 
ATOM   25   H  HA   A LYS A 1 1   ? -2.59600  -10.07400 -10.57400 0.590 27.35000  ? 1   LYS A HA   1 
ATOM   26   H  HA   B LYS A 1 1   ? -2.60000  -10.07700 -10.61400 0.410 27.39000  ? 1   LYS A HA   1 
ATOM   27   H  HB2  A LYS A 1 1   ? -0.87300  -9.20000  -9.35200  0.590 30.91000  ? 1   LYS A HB2  1 
ATOM   28   H  HB2  B LYS A 1 1   ? -0.86400  -9.12300  -9.50200  0.410 31.25000  ? 1   LYS A HB2  1 
ATOM   29   H  HB3  A LYS A 1 1   ? -0.69000  -10.57300 -8.57200  0.590 30.91000  ? 1   LYS A HB3  1 
ATOM   30   H  HB3  B LYS A 1 1   ? -0.68400  -10.40500 -8.58100  0.410 31.25000  ? 1   LYS A HB3  1 
ATOM   31   H  HG2  A LYS A 1 1   ? 0.14400   -11.56600 -10.50600 0.590 31.63000  ? 1   LYS A HG2  1 
ATOM   32   H  HG2  B LYS A 1 1   ? 0.22500   -11.58600 -10.33500 0.410 31.52000  ? 1   LYS A HG2  1 
ATOM   33   H  HG3  A LYS A 1 1   ? -0.05300  -10.20100 -11.29600 0.590 31.63000  ? 1   LYS A HG3  1 
ATOM   34   H  HG3  B LYS A 1 1   ? -0.06000  -10.38200 -11.33200 0.410 31.52000  ? 1   LYS A HG3  1 
ATOM   35   H  HD2  A LYS A 1 1   ? 1.59100   -9.17700  -10.09000 0.590 37.34000  ? 1   LYS A HD2  1 
ATOM   36   H  HD2  B LYS A 1 1   ? 1.51800   -9.07500  -10.28800 0.410 37.27000  ? 1   LYS A HD2  1 
ATOM   37   H  HD3  A LYS A 1 1   ? 1.65100   -10.37700 -9.05000  0.590 37.34000  ? 1   LYS A HD3  1 
ATOM   38   H  HD3  B LYS A 1 1   ? 1.71200   -10.15700 -9.14200  0.410 37.27000  ? 1   LYS A HD3  1 
ATOM   39   H  HE2  A LYS A 1 1   ? 2.89600   -11.61200 -10.36100 0.590 38.47000  ? 1   LYS A HE2  1 
ATOM   40   H  HE2  B LYS A 1 1   ? 3.48600   -10.33100 -10.60700 0.410 38.69000  ? 1   LYS A HE2  1 
ATOM   41   H  HE3  A LYS A 1 1   ? 2.24100   -11.02500 -11.68500 0.590 38.47000  ? 1   LYS A HE3  1 
ATOM   42   H  HE3  B LYS A 1 1   ? 2.59900   -11.64100 -10.75100 0.410 38.69000  ? 1   LYS A HE3  1 
ATOM   43   H  HZ1  A LYS A 1 1   ? 4.46800   -10.41200 -11.31600 0.590 46.96000  ? 1   LYS A HZ1  1 
ATOM   44   H  HZ1  B LYS A 1 1   ? 2.43000   -9.54900  -12.49800 0.410 41.01000  ? 1   LYS A HZ1  1 
ATOM   45   H  HZ2  A LYS A 1 1   ? 3.59400   -9.29200  -11.59700 0.590 46.96000  ? 1   LYS A HZ2  1 
ATOM   46   H  HZ2  B LYS A 1 1   ? 3.18900   -10.75000 -12.78500 0.410 41.01000  ? 1   LYS A HZ2  1 
ATOM   47   H  HZ3  A LYS A 1 1   ? 4.01800   -9.55700  -10.23700 0.590 46.96000  ? 1   LYS A HZ3  1 
ATOM   48   H  HZ3  B LYS A 1 1   ? 1.74800   -10.81800 -12.65500 0.410 41.01000  ? 1   LYS A HZ3  1 
ATOM   49   N  N    . VAL A 1 2   ? -2.44300  -12.44700 -11.26400 1.000 22.10000  ? 2   VAL A N    1 
ATOM   50   C  CA   . VAL A 1 2   ? -2.35100  -13.85800 -11.62200 1.000 23.47000  ? 2   VAL A CA   1 
ATOM   51   C  C    . VAL A 1 2   ? -0.92800  -14.07700 -12.12000 1.000 25.02000  ? 2   VAL A C    1 
ATOM   52   O  O    . VAL A 1 2   ? -0.50500  -13.45900 -13.11400 1.000 26.12000  ? 2   VAL A O    1 
ATOM   53   C  CB   . VAL A 1 2   ? -3.40400  -14.25600 -12.66100 1.000 22.54000  ? 2   VAL A CB   1 
ATOM   54   C  CG1  . VAL A 1 2   ? -3.24500  -15.70800 -13.04600 1.000 28.14000  ? 2   VAL A CG1  1 
ATOM   55   C  CG2  . VAL A 1 2   ? -4.81300  -14.01200 -12.10200 1.000 22.26000  ? 2   VAL A CG2  1 
ATOM   56   H  H    . VAL A 1 2   ? -2.49400  -11.92200 -11.94200 1.000 26.54000  ? 2   VAL A H    1 
ATOM   57   H  HA   . VAL A 1 2   ? -2.50500  -14.42000 -10.84700 1.000 28.19000  ? 2   VAL A HA   1 
ATOM   58   H  HB   . VAL A 1 2   ? -3.28300  -13.71400 -13.45700 1.000 27.07000  ? 2   VAL A HB   1 
ATOM   59   H  HG11 . VAL A 1 2   ? -3.94400  -15.94600 -13.67500 1.000 33.79000  ? 2   VAL A HG11 1 
ATOM   60   H  HG12 . VAL A 1 2   ? -2.37500  -15.83300 -13.45500 1.000 33.79000  ? 2   VAL A HG12 1 
ATOM   61   H  HG13 . VAL A 1 2   ? -3.31700  -16.25600 -12.24900 1.000 33.79000  ? 2   VAL A HG13 1 
ATOM   62   H  HG21 . VAL A 1 2   ? -5.46700  -14.26700 -12.77100 1.000 26.73000  ? 2   VAL A HG21 1 
ATOM   63   H  HG22 . VAL A 1 2   ? -4.93200  -14.54700 -11.30100 1.000 26.73000  ? 2   VAL A HG22 1 
ATOM   64   H  HG23 . VAL A 1 2   ? -4.90900  -13.07100 -11.88800 1.000 26.73000  ? 2   VAL A HG23 1 
ATOM   65   N  N    . PHE A 1 3   ? -0.16100  -14.89000 -11.39500 1.000 20.71000  ? 3   PHE A N    1 
ATOM   66   C  CA   . PHE A 1 3   ? 1.22500   -15.15600 -11.76300 1.000 19.46000  ? 3   PHE A CA   1 
ATOM   67   C  C    . PHE A 1 3   ? 1.30600   -16.21500 -12.85000 1.000 23.58000  ? 3   PHE A C    1 
ATOM   68   O  O    . PHE A 1 3   ? 0.47800   -17.11900 -12.92800 1.000 22.36000  ? 3   PHE A O    1 
ATOM   69   C  CB   . PHE A 1 3   ? 2.00000   -15.71500 -10.56100 1.000 20.57000  ? 3   PHE A CB   1 
ATOM   70   C  CG   . PHE A 1 3   ? 2.52000   -14.69000 -9.62000  1.000 19.67000  ? 3   PHE A CG   1 
ATOM   71   C  CD1  . PHE A 1 3   ? 1.69000   -14.12000 -8.65700  1.000 21.07000  ? 3   PHE A CD1  1 
ATOM   72   C  CD2  . PHE A 1 3   ? 3.82900   -14.31600 -9.65500  1.000 23.26000  ? 3   PHE A CD2  1 
ATOM   73   C  CE1  . PHE A 1 3   ? 2.16400   -13.18700 -7.79300  1.000 24.92000  ? 3   PHE A CE1  1 
ATOM   74   C  CE2  . PHE A 1 3   ? 4.31800   -13.38600 -8.77900  1.000 25.13000  ? 3   PHE A CE2  1 
ATOM   75   C  CZ   . PHE A 1 3   ? 3.49000   -12.81500 -7.83800  1.000 30.25000  ? 3   PHE A CZ   1 
ATOM   76   H  H    . PHE A 1 3   ? -0.42100  -15.29900 -10.68500 1.000 24.87000  ? 3   PHE A H    1 
ATOM   77   H  HA   . PHE A 1 3   ? 1.62000   -14.32500 -12.07100 1.000 23.37000  ? 3   PHE A HA   1 
ATOM   78   H  HB2  . PHE A 1 3   ? 1.40900   -16.29800 -10.05800 1.000 24.70000  ? 3   PHE A HB2  1 
ATOM   79   H  HB3  . PHE A 1 3   ? 2.76000   -16.21900 -10.89200 1.000 24.70000  ? 3   PHE A HB3  1 
ATOM   80   H  HD1  . PHE A 1 3   ? 0.79900   -14.38300 -8.60500  1.000 25.31000  ? 3   PHE A HD1  1 
ATOM   81   H  HD2  . PHE A 1 3   ? 4.39800   -14.69700 -10.28400 1.000 27.93000  ? 3   PHE A HD2  1 
ATOM   82   H  HE1  . PHE A 1 3   ? 1.59300   -12.79800 -7.17000  1.000 29.92000  ? 3   PHE A HE1  1 
ATOM   83   H  HE2  . PHE A 1 3   ? 5.21400   -13.13900 -8.81800  1.000 30.18000  ? 3   PHE A HE2  1 
ATOM   84   H  HZ   . PHE A 1 3   ? 3.82200   -12.18500 -7.24000  1.000 36.32000  ? 3   PHE A HZ   1 
ATOM   85   N  N    . GLY A 1 4   ? 2.34200   -16.10200 -13.68900 1.000 24.48000  ? 4   GLY A N    1 
ATOM   86   C  CA   . GLY A 1 4   ? 2.79600   -17.25200 -14.43000 1.000 23.35000  ? 4   GLY A CA   1 
ATOM   87   C  C    . GLY A 1 4   ? 3.52000   -18.24400 -13.54200 1.000 22.30000  ? 4   GLY A C    1 
ATOM   88   O  O    . GLY A 1 4   ? 4.07400   -17.91700 -12.49700 1.000 22.01000  ? 4   GLY A O    1 
ATOM   89   H  H    . GLY A 1 4   ? 2.78300   -15.37900 -13.83500 1.000 29.40000  ? 4   GLY A H    1 
ATOM   90   H  HA2  . GLY A 1 4   ? 2.03500   -17.69700 -14.83400 1.000 28.04000  ? 4   GLY A HA2  1 
ATOM   91   H  HA3  . GLY A 1 4   ? 3.40300   -16.96500 -15.13100 1.000 28.04000  ? 4   GLY A HA3  1 
ATOM   92   N  N    . ARG A 1 5   ? 3.55800   -19.48600 -14.00700 1.000 25.62000  ? 5   ARG A N    1 
ATOM   93   C  CA   . ARG A 1 5   ? 4.21400   -20.54700 -13.25900 1.000 21.52000  ? 5   ARG A CA   1 
ATOM   94   C  C    . ARG A 1 5   ? 5.67500   -20.22800 -12.93400 1.000 20.88000  ? 5   ARG A C    1 
ATOM   95   O  O    . ARG A 1 5   ? 6.11400   -20.32300 -11.78100 1.000 21.62000  ? 5   ARG A O    1 
ATOM   96   C  CB   . ARG A 1 5   ? 4.09800   -21.81800 -14.10900 1.000 28.65000  ? 5   ARG A CB   1 
ATOM   97   C  CG   . ARG A 1 5   ? 4.80400   -23.02000 -13.56800 1.000 25.61000  ? 5   ARG A CG   1 
ATOM   98   C  CD   . ARG A 1 5   ? 4.57000   -24.25300 -14.48700 1.000 24.48000  ? 5   ARG A CD   1 
ATOM   99   N  NE   . ARG A 1 5   ? 5.22600   -24.16700 -15.79600 1.000 33.30000  ? 5   ARG A NE   1 
ATOM   100  C  CZ   . ARG A 1 5   ? 6.45900   -24.59000 -16.04800 1.000 31.08000  ? 5   ARG A CZ   1 
ATOM   101  N  NH1  . ARG A 1 5   ? 7.24200   -25.04600 -15.08800 1.000 29.79000  ? 5   ARG A NH1  1 
ATOM   102  N  NH2  . ARG A 1 5   ? 6.93100   -24.52700 -17.29200 1.000 34.07000  ? 5   ARG A NH2  1 
ATOM   103  H  H    . ARG A 1 5   ? 3.21100   -19.74100 -14.75200 1.000 30.77000  ? 5   ARG A H    1 
ATOM   104  H  HA   . ARG A 1 5   ? 3.78200   -20.66900 -12.39900 1.000 25.84000  ? 5   ARG A HA   1 
ATOM   105  H  HB2  . ARG A 1 5   ? 3.15800   -22.04700 -14.18800 1.000 34.40000  ? 5   ARG A HB2  1 
ATOM   106  H  HB3  . ARG A 1 5   ? 4.47000   -21.63500 -14.98500 1.000 34.40000  ? 5   ARG A HB3  1 
ATOM   107  H  HG2  . ARG A 1 5   ? 5.75700   -22.84400 -13.52400 1.000 30.75000  ? 5   ARG A HG2  1 
ATOM   108  H  HG3  . ARG A 1 5   ? 4.46300   -23.22600 -12.68300 1.000 30.75000  ? 5   ARG A HG3  1 
ATOM   109  H  HD2  . ARG A 1 5   ? 4.91300   -25.04200 -14.04000 1.000 29.39000  ? 5   ARG A HD2  1 
ATOM   110  H  HD3  . ARG A 1 5   ? 3.61700   -24.34700 -14.64300 1.000 29.39000  ? 5   ARG A HD3  1 
ATOM   111  H  HE   . ARG A 1 5   ? 4.78100   -23.81800 -16.44500 1.000 39.98000  ? 5   ARG A HE   1 
ATOM   112  H  HH11 . ARG A 1 5   ? 6.95700   -25.07300 -14.27700 1.000 35.77000  ? 5   ARG A HH11 1 
ATOM   113  H  HH12 . ARG A 1 5   ? 8.03700   -25.31500 -15.27300 1.000 35.77000  ? 5   ARG A HH12 1 
ATOM   114  H  HH21 . ARG A 1 5   ? 6.43800   -24.21400 -17.92400 1.000 40.91000  ? 5   ARG A HH21 1 
ATOM   115  H  HH22 . ARG A 1 5   ? 7.72900   -24.79900 -17.46300 1.000 40.91000  ? 5   ARG A HH22 1 
ATOM   116  N  N    . CYS A 1 6   ? 6.47000   -19.89300 -13.95300 1.000 23.77000  ? 6   CYS A N    1 
ATOM   117  C  CA   . CYS A 1 6   ? 7.87500   -19.63700 -13.66900 1.000 23.71000  ? 6   CYS A CA   1 
ATOM   118  C  C    . CYS A 1 6   ? 8.08900   -18.31600 -12.95800 1.000 21.25000  ? 6   CYS A C    1 
ATOM   119  O  O    . CYS A 1 6   ? 9.03700   -18.18500 -12.18100 1.000 22.04000  ? 6   CYS A O    1 
ATOM   120  C  CB   . CYS A 1 6   ? 8.69700   -19.67900 -14.96600 1.000 23.54000  ? 6   CYS A CB   1 
ATOM   121  S  SG   . CYS A 1 6   ? 8.80100   -21.32400 -15.71900 1.000 26.06000  ? 6   CYS A SG   1 
ATOM   122  H  H    . CYS A 1 6   ? 6.23000   -19.81300 -14.77500 1.000 28.55000  ? 6   CYS A H    1 
ATOM   123  H  HA   . CYS A 1 6   ? 8.19600   -20.34100 -13.08400 1.000 28.48000  ? 6   CYS A HA   1 
ATOM   124  H  HB2  . CYS A 1 6   ? 8.28800   -19.08300 -15.61300 1.000 28.27000  ? 6   CYS A HB2  1 
ATOM   125  H  HB3  . CYS A 1 6   ? 9.60100   -19.38500 -14.77100 1.000 28.27000  ? 6   CYS A HB3  1 
ATOM   126  N  N    . GLU A 1 7   ? 7.22800   -17.33200 -13.20900 1.000 22.29000  ? 7   GLU A N    1 
ATOM   127  C  CA   . GLU A 1 7   ? 7.30500   -16.07400 -12.48800 1.000 21.65000  ? 7   GLU A CA   1 
ATOM   128  C  C    . GLU A 1 7   ? 7.11000   -16.29600 -10.99600 1.000 21.20000  ? 7   GLU A C    1 
ATOM   129  O  O    . GLU A 1 7   ? 7.84900   -15.75300 -10.17900 1.000 22.19000  ? 7   GLU A O    1 
ATOM   130  C  CB   . GLU A 1 7   ? 6.24900   -15.11400 -13.02800 1.000 26.65000  ? 7   GLU A CB   1 
ATOM   131  C  CG   . GLU A 1 7   ? 6.25600   -13.74500 -12.44200 1.000 29.14000  ? 7   GLU A CG   1 
ATOM   132  C  CD   . GLU A 1 7   ? 5.03600   -12.94300 -12.84100 1.000 27.99000  ? 7   GLU A CD   1 
ATOM   133  O  OE1  . GLU A 1 7   ? 4.03200   -13.50900 -13.35700 1.000 28.49000  ? 7   GLU A OE1  1 
ATOM   134  O  OE2  . GLU A 1 7   ? 5.10800   -11.70300 -12.66300 1.000 32.47000  ? 7   GLU A OE2  1 
ATOM   135  H  H    . GLU A 1 7   ? 6.59400   -17.37100 -13.78900 1.000 26.77000  ? 7   GLU A H    1 
ATOM   136  H  HA   . GLU A 1 7   ? 8.17900   -15.67400 -12.62400 1.000 26.00000  ? 7   GLU A HA   1 
ATOM   137  H  HB2  . GLU A 1 7   ? 6.38600   -15.01800 -13.98300 1.000 32.00000  ? 7   GLU A HB2  1 
ATOM   138  H  HB3  . GLU A 1 7   ? 5.37400   -15.49600 -12.85400 1.000 32.00000  ? 7   GLU A HB3  1 
ATOM   139  H  HG2  . GLU A 1 7   ? 6.26900   -13.81400 -11.47500 1.000 34.98000  ? 7   GLU A HG2  1 
ATOM   140  H  HG3  . GLU A 1 7   ? 7.04300   -13.27100 -12.75200 1.000 34.98000  ? 7   GLU A HG3  1 
ATOM   141  N  N    . LEU A 1 8   ? 6.14500   -17.14100 -10.63400 1.000 22.94000  ? 8   LEU A N    1 
ATOM   142  C  CA   . LEU A 1 8   ? 5.91900   -17.41200 -9.21800  1.000 19.51000  ? 8   LEU A CA   1 
ATOM   143  C  C    . LEU A 1 8   ? 7.06300   -18.20200 -8.61000  1.000 18.64000  ? 8   LEU A C    1 
ATOM   144  O  O    . LEU A 1 8   ? 7.49100   -17.93100 -7.47900  1.000 19.46000  ? 8   LEU A O    1 
ATOM   145  C  CB   . LEU A 1 8   ? 4.59500   -18.15700 -9.07100  1.000 23.25000  ? 8   LEU A CB   1 
ATOM   146  C  CG   . LEU A 1 8   ? 4.25300   -18.45800 -7.61700  1.000 19.96000  ? 8   LEU A CG   1 
ATOM   147  C  CD1  . LEU A 1 8   ? 4.00200   -17.20000 -6.86200  1.000 24.86000  ? 8   LEU A CD1  1 
ATOM   148  C  CD2  . LEU A 1 8   ? 3.06200   -19.38900 -7.52700  1.000 22.94000  ? 8   LEU A CD2  1 
ATOM   149  H  H    . LEU A 1 8   ? 5.62200   -17.55800 -11.17400 1.000 27.55000  ? 8   LEU A H    1 
ATOM   150  H  HA   . LEU A 1 8   ? 5.86400   -16.57700 -8.72900  1.000 23.43000  ? 8   LEU A HA   1 
ATOM   151  H  HB2  . LEU A 1 8   ? 3.88300   -17.61300 -9.44200  1.000 27.92000  ? 8   LEU A HB2  1 
ATOM   152  H  HB3  . LEU A 1 8   ? 4.65200   -19.00000 -9.54900  1.000 27.92000  ? 8   LEU A HB3  1 
ATOM   153  H  HG   . LEU A 1 8   ? 5.01000   -18.90400 -7.20500  1.000 23.97000  ? 8   LEU A HG   1 
ATOM   154  H  HD11 . LEU A 1 8   ? 3.60300   -17.42000 -6.00600  1.000 29.85000  ? 8   LEU A HD11 1 
ATOM   155  H  HD12 . LEU A 1 8   ? 4.84400   -16.73900 -6.72700  1.000 29.85000  ? 8   LEU A HD12 1 
ATOM   156  H  HD13 . LEU A 1 8   ? 3.39700   -16.64000 -7.37400  1.000 29.85000  ? 8   LEU A HD13 1 
ATOM   157  H  HD21 . LEU A 1 8   ? 2.86100   -19.55400 -6.59200  1.000 27.55000  ? 8   LEU A HD21 1 
ATOM   158  H  HD22 . LEU A 1 8   ? 2.30100   -18.97100 -7.96000  1.000 27.55000  ? 8   LEU A HD22 1 
ATOM   159  H  HD23 . LEU A 1 8   ? 3.27900   -20.22300 -7.97100  1.000 27.55000  ? 8   LEU A HD23 1 
ATOM   160  N  N    . ALA A 1 9   ? 7.58600   -19.17900 -9.34900  1.000 19.67000  ? 9   ALA A N    1 
ATOM   161  C  CA   . ALA A 1 9   ? 8.71000   -19.92200 -8.83700  1.000 19.97000  ? 9   ALA A CA   1 
ATOM   162  C  C    . ALA A 1 9   ? 9.87600   -19.00100 -8.52100  1.000 19.33000  ? 9   ALA A C    1 
ATOM   163  O  O    . ALA A 1 9   ? 10.51900  -19.16900 -7.49200  1.000 20.98000  ? 9   ALA A O    1 
ATOM   164  C  CB   . ALA A 1 9   ? 9.12300   -20.99800 -9.84700  1.000 22.06000  ? 9   ALA A CB   1 
ATOM   165  H  H    . ALA A 1 9   ? 7.30900   -19.41800 -10.12800 1.000 23.62000  ? 9   ALA A H    1 
ATOM   166  H  HA   . ALA A 1 9   ? 8.45000   -20.36600 -8.01500  1.000 23.99000  ? 9   ALA A HA   1 
ATOM   167  H  HB1  . ALA A 1 9   ? 9.83000   -21.53800 -9.46200  1.000 26.49000  ? 9   ALA A HB1  1 
ATOM   168  H  HB2  . ALA A 1 9   ? 8.35400   -21.55400 -10.04900 1.000 26.49000  ? 9   ALA A HB2  1 
ATOM   169  H  HB3  . ALA A 1 9   ? 9.44000   -20.56600 -10.65600 1.000 26.49000  ? 9   ALA A HB3  1 
ATOM   170  N  N    . ALA A 1 10  ? 10.17600  -18.05100 -9.41000  1.000 21.72000  ? 10  ALA A N    1 
ATOM   171  C  CA   . ALA A 1 10  ? 11.28700  -17.14100 -9.16900  1.000 22.19000  ? 10  ALA A CA   1 
ATOM   172  C  C    . ALA A 1 10  ? 11.03400  -16.25100 -7.96500  1.000 21.46000  ? 10  ALA A C    1 
ATOM   173  O  O    . ALA A 1 10  ? 11.94600  -16.00400 -7.17000  1.000 23.37000  ? 10  ALA A O    1 
ATOM   174  C  CB   . ALA A 1 10  ? 11.51300  -16.28900 -10.41400 1.000 25.33000  ? 10  ALA A CB   1 
ATOM   175  H  H    . ALA A 1 10  ? 9.75600   -17.91700 -10.14900 1.000 26.08000  ? 10  ALA A H    1 
ATOM   176  H  HA   . ALA A 1 10  ? 12.08600  -17.66000 -8.98700  1.000 26.64000  ? 10  ALA A HA   1 
ATOM   177  H  HB1  . ALA A 1 10  ? 12.24800  -15.67700 -10.25000 1.000 30.41000  ? 10  ALA A HB1  1 
ATOM   178  H  HB2  . ALA A 1 10  ? 11.72800  -16.87100 -11.16000 1.000 30.41000  ? 10  ALA A HB2  1 
ATOM   179  H  HB3  . ALA A 1 10  ? 10.70400  -15.79000 -10.60700 1.000 30.41000  ? 10  ALA A HB3  1 
ATOM   180  N  N    . ALA A 1 11  ? 9.81100   -15.73800 -7.82300  1.000 22.31000  ? 11  ALA A N    1 
ATOM   181  C  CA   . ALA A 1 11  ? 9.47900   -14.92800 -6.66500  1.000 22.34000  ? 11  ALA A CA   1 
ATOM   182  C  C    . ALA A 1 11  ? 9.61100   -15.73000 -5.37900  1.000 23.65000  ? 11  ALA A C    1 
ATOM   183  O  O    . ALA A 1 11  ? 10.11800  -15.24000 -4.36800  1.000 23.28000  ? 11  ALA A O    1 
ATOM   184  C  CB   . ALA A 1 11  ? 8.06400   -14.37800 -6.80800  1.000 24.84000  ? 11  ALA A CB   1 
ATOM   185  H  H    . ALA A 1 11  ? 9.16500   -15.84600 -8.38100  1.000 26.80000  ? 11  ALA A H    1 
ATOM   186  H  HA   . ALA A 1 11  ? 10.09400  -14.17900 -6.61600  1.000 26.83000  ? 11  ALA A HA   1 
ATOM   187  H  HB1  . ALA A 1 11  ? 7.83200   -13.88900 -6.00300  1.000 29.82000  ? 11  ALA A HB1  1 
ATOM   188  H  HB2  . ALA A 1 11  ? 8.03100   -13.78600 -7.57600  1.000 29.82000  ? 11  ALA A HB2  1 
ATOM   189  H  HB3  . ALA A 1 11  ? 7.44900   -15.11700 -6.93400  1.000 29.82000  ? 11  ALA A HB3  1 
ATOM   190  N  N    . MET A 1 12  ? 9.19600   -16.98200 -5.40100  1.000 22.05000  ? 12  MET A N    1 
ATOM   191  C  CA   . MET A 1 12  ? 9.27600   -17.78700 -4.20800  1.000 20.39000  ? 12  MET A CA   1 
ATOM   192  C  C    . MET A 1 12  ? 10.71700  -18.12600 -3.83200  1.000 19.13000  ? 12  MET A C    1 
ATOM   193  O  O    . MET A 1 12  ? 11.05700  -18.07300 -2.67700  1.000 23.66000  ? 12  MET A O    1 
ATOM   194  C  CB   . MET A 1 12  ? 8.44500   -19.05800 -4.39800  1.000 21.55000  ? 12  MET A CB   1 
ATOM   195  C  CG   . MET A 1 12  ? 6.94800   -18.83700 -4.32500  1.000 21.94000  ? 12  MET A CG   1 
ATOM   196  S  SD   . MET A 1 12  ? 6.04000   -20.37100 -4.60400  1.000 21.91000  ? 12  MET A SD   1 
ATOM   197  C  CE   . MET A 1 12  ? 4.45800   -19.99600 -3.86000  1.000 24.50000  ? 12  MET A CE   1 
ATOM   198  H  H    . MET A 1 12  ? 8.86100   -17.39100 -6.08300  1.000 26.48000  ? 12  MET A H    1 
ATOM   199  H  HA   . MET A 1 12  ? 8.87000   -17.28800 -3.46900  1.000 24.49000  ? 12  MET A HA   1 
ATOM   200  H  HB2  . MET A 1 12  ? 8.64800   -19.43600 -5.26800  1.000 25.88000  ? 12  MET A HB2  1 
ATOM   201  H  HB3  . MET A 1 12  ? 8.68400   -19.68800 -3.70000  1.000 25.88000  ? 12  MET A HB3  1 
ATOM   202  H  HG2  . MET A 1 12  ? 6.72000   -18.50200 -3.44400  1.000 26.35000  ? 12  MET A HG2  1 
ATOM   203  H  HG3  . MET A 1 12  ? 6.68600   -18.19700 -5.00600  1.000 26.35000  ? 12  MET A HG3  1 
ATOM   204  H  HE1  . MET A 1 12  ? 3.93200   -20.80100 -3.82500  1.000 29.42000  ? 12  MET A HE1  1 
ATOM   205  H  HE2  . MET A 1 12  ? 4.60300   -19.65600 -2.97400  1.000 29.42000  ? 12  MET A HE2  1 
ATOM   206  H  HE3  . MET A 1 12  ? 4.01400   -19.33600 -4.40100  1.000 29.42000  ? 12  MET A HE3  1 
ATOM   207  N  N    A LYS A 1 13  ? 11.53000  -18.34700 -4.85200  0.460 22.13000  ? 13  LYS A N    1 
ATOM   208  N  N    B LYS A 1 13  ? 11.50600  -18.33300 -4.88400  0.540 22.08000  ? 13  LYS A N    1 
ATOM   209  C  CA   A LYS A 1 13  ? 12.94400  -18.56200 -4.55800  0.460 25.10000  ? 13  LYS A CA   1 
ATOM   210  C  CA   B LYS A 1 13  ? 12.92900  -18.60300 -4.70800  0.540 24.99000  ? 13  LYS A CA   1 
ATOM   211  C  C    A LYS A 1 13  ? 13.58700  -17.29500 -4.00900  0.460 24.71000  ? 13  LYS A C    1 
ATOM   212  C  C    B LYS A 1 13  ? 13.62600  -17.42300 -4.05800  0.540 24.42000  ? 13  LYS A C    1 
ATOM   213  O  O    A LYS A 1 13  ? 14.35100  -17.34700 -3.04100  0.460 26.13000  ? 13  LYS A O    1 
ATOM   214  O  O    B LYS A 1 13  ? 14.39000  -17.58900 -3.10300  0.540 27.17000  ? 13  LYS A O    1 
ATOM   215  C  CB   A LYS A 1 13  ? 13.67700  -19.02500 -5.81000  0.460 25.46000  ? 13  LYS A CB   1 
ATOM   216  C  CB   B LYS A 1 13  ? 13.55000  -18.88900 -6.07800  0.540 24.41000  ? 13  LYS A CB   1 
ATOM   217  C  CG   A LYS A 1 13  ? 15.13800  -19.36400 -5.55200  0.460 24.61000  ? 13  LYS A CG   1 
ATOM   218  C  CG   B LYS A 1 13  ? 15.06300  -19.11500 -6.06700  0.540 33.15000  ? 13  LYS A CG   1 
ATOM   219  C  CD   A LYS A 1 13  ? 15.74900  -20.13800 -6.71200  0.460 35.70000  ? 13  LYS A CD   1 
ATOM   220  C  CD   B LYS A 1 13  ? 15.43300  -20.49100 -6.61000  0.540 35.34000  ? 13  LYS A CD   1 
ATOM   221  C  CE   A LYS A 1 13  ? 17.18000  -20.58300 -6.39300  0.460 44.75000  ? 13  LYS A CE   1 
ATOM   222  C  CE   B LYS A 1 13  ? 16.94500  -20.71600 -6.59200  0.540 47.21000  ? 13  LYS A CE   1 
ATOM   223  N  NZ   A LYS A 1 13  ? 17.27000  -21.45900 -5.18500  0.460 46.72000  ? 13  LYS A NZ   1 
ATOM   224  N  NZ   B LYS A 1 13  ? 17.59200  -20.30400 -7.87000  0.540 42.12000  ? 13  LYS A NZ   1 
ATOM   225  H  H    A LYS A 1 13  ? 11.31700  -18.38100 -5.68500  0.460 26.58000  ? 13  LYS A H    1 
ATOM   226  H  H    B LYS A 1 13  ? 11.25700  -18.32700 -5.70700  0.540 26.52000  ? 13  LYS A H    1 
ATOM   227  H  HA   A LYS A 1 13  ? 13.02000  -19.26000 -3.88900  0.460 30.15000  ? 13  LYS A HA   1 
ATOM   228  H  HA   B LYS A 1 13  ? 13.04400  -19.37800 -4.13600  0.540 30.01000  ? 13  LYS A HA   1 
ATOM   229  H  HB2  A LYS A 1 13  ? 13.24100  -19.82100 -6.15400  0.460 30.57000  ? 13  LYS A HB2  1 
ATOM   230  H  HB2  B LYS A 1 13  ? 13.13900  -19.68900 -6.44000  0.540 29.32000  ? 13  LYS A HB2  1 
ATOM   231  H  HB3  A LYS A 1 13  ? 13.64700  -18.31800 -6.47300  0.460 30.57000  ? 13  LYS A HB3  1 
ATOM   232  H  HB3  B LYS A 1 13  ? 13.37300  -18.13300 -6.65900  0.540 29.32000  ? 13  LYS A HB3  1 
ATOM   233  H  HG2  A LYS A 1 13  ? 15.64200  -18.54300 -5.43500  0.460 29.55000  ? 13  LYS A HG2  1 
ATOM   234  H  HG2  B LYS A 1 13  ? 15.49100  -18.44400 -6.62100  0.540 39.80000  ? 13  LYS A HG2  1 
ATOM   235  H  HG3  A LYS A 1 13  ? 15.20400  -19.91000 -4.75300  0.460 29.55000  ? 13  LYS A HG3  1 
ATOM   236  H  HG3  B LYS A 1 13  ? 15.39000  -19.05000 -5.15600  0.540 39.80000  ? 13  LYS A HG3  1 
ATOM   237  H  HD2  A LYS A 1 13  ? 15.21500  -20.92900 -6.88800  0.460 42.87000  ? 13  LYS A HD2  1 
ATOM   238  H  HD2  B LYS A 1 13  ? 15.01700  -21.17400 -6.06100  0.540 42.43000  ? 13  LYS A HD2  1 
ATOM   239  H  HD3  A LYS A 1 13  ? 15.77300  -19.57200 -7.50000  0.460 42.87000  ? 13  LYS A HD3  1 
ATOM   240  H  HD3  B LYS A 1 13  ? 15.12500  -20.56800 -7.52600  0.540 42.43000  ? 13  LYS A HD3  1 
ATOM   241  H  HE2  A LYS A 1 13  ? 17.53000  -21.08100 -7.14800  0.460 53.72000  ? 13  LYS A HE2  1 
ATOM   242  H  HE2  B LYS A 1 13  ? 17.33600  -20.19400 -5.87400  0.540 56.68000  ? 13  LYS A HE2  1 
ATOM   243  H  HE3  A LYS A 1 13  ? 17.72500  -19.79700 -6.23200  0.460 53.72000  ? 13  LYS A HE3  1 
ATOM   244  H  HE3  B LYS A 1 13  ? 17.12400  -21.65900 -6.45300  0.540 56.68000  ? 13  LYS A HE3  1 
ATOM   245  H  HZ1  A LYS A 1 13  ? 18.11100  -21.72200 -5.06200  0.460 56.08000  ? 13  LYS A HZ1  1 
ATOM   246  H  HZ1  B LYS A 1 13  ? 18.46900  -20.45300 -7.82900  0.540 50.56000  ? 13  LYS A HZ1  1 
ATOM   247  H  HZ2  A LYS A 1 13  ? 16.99900  -21.01200 -4.46500  0.460 56.08000  ? 13  LYS A HZ2  1 
ATOM   248  H  HZ2  B LYS A 1 13  ? 17.25100  -20.76900 -8.54700  0.540 50.56000  ? 13  LYS A HZ2  1 
ATOM   249  H  HZ3  A LYS A 1 13  ? 16.75500  -22.17700 -5.29100  0.460 56.08000  ? 13  LYS A HZ3  1 
ATOM   250  H  HZ3  B LYS A 1 13  ? 17.45300  -19.43700 -8.01600  0.540 50.56000  ? 13  LYS A HZ3  1 
ATOM   251  N  N    A ARG A 1 14  ? 13.26700  -16.14400 -4.59600  0.460 25.05000  ? 14  ARG A N    1 
ATOM   252  N  N    B ARG A 1 14  ? 13.36000  -16.21300 -4.54800  0.540 25.19000  ? 14  ARG A N    1 
ATOM   253  C  CA   A ARG A 1 14  ? 13.83200  -14.88900 -4.10800  0.460 24.84000  ? 14  ARG A CA   1 
ATOM   254  C  CA   B ARG A 1 14  ? 14.03000  -15.05700 -3.96900  0.540 25.07000  ? 14  ARG A CA   1 
ATOM   255  C  C    A ARG A 1 14  ? 13.50400  -14.67100 -2.63700  0.460 29.01000  ? 14  ARG A C    1 
ATOM   256  C  C    B ARG A 1 14  ? 13.61000  -14.84600 -2.52400  0.540 28.85000  ? 14  ARG A C    1 
ATOM   257  O  O    A ARG A 1 14  ? 14.27200  -14.03000 -1.91700  0.460 29.83000  ? 14  ARG A O    1 
ATOM   258  O  O    B ARG A 1 14  ? 14.41700  -14.39500 -1.70600  0.540 28.86000  ? 14  ARG A O    1 
ATOM   259  C  CB   A ARG A 1 14  ? 13.33200  -13.74900 -4.99700  0.460 29.55000  ? 14  ARG A CB   1 
ATOM   260  C  CB   B ARG A 1 14  ? 13.77700  -13.79700 -4.79300  0.540 30.63000  ? 14  ARG A CB   1 
ATOM   261  C  CG   A ARG A 1 14  ? 13.47700  -12.35400 -4.43200  0.460 40.86000  ? 14  ARG A CG   1 
ATOM   262  C  CG   B ARG A 1 14  ? 14.58800  -12.59900 -4.27900  0.540 41.65000  ? 14  ARG A CG   1 
ATOM   263  C  CD   A ARG A 1 14  ? 13.15800  -11.31400 -5.50900  0.460 39.35000  ? 14  ARG A CD   1 
ATOM   264  C  CD   B ARG A 1 14  ? 14.44600  -11.36200 -5.15500  0.540 39.05000  ? 14  ARG A CD   1 
ATOM   265  N  NE   A ARG A 1 14  ? 11.77300  -11.42300 -5.95800  0.460 46.90000  ? 14  ARG A NE   1 
ATOM   266  N  NE   B ARG A 1 14  ? 13.49700  -10.41500 -4.58100  0.540 46.41000  ? 14  ARG A NE   1 
ATOM   267  C  CZ   A ARG A 1 14  ? 10.74300  -10.81300 -5.38600  0.460 43.14000  ? 14  ARG A CZ   1 
ATOM   268  C  CZ   B ARG A 1 14  ? 13.77700  -9.55900  -3.60900  0.540 42.70000  ? 14  ARG A CZ   1 
ATOM   269  N  NH1  A ARG A 1 14  ? 10.90800  -9.98200  -4.37000  0.460 47.01000  ? 14  ARG A NH1  1 
ATOM   270  N  NH1  B ARG A 1 14  ? 15.00100  -9.44500  -3.11800  0.540 45.57000  ? 14  ARG A NH1  1 
ATOM   271  N  NH2  A ARG A 1 14  ? 9.51700   -11.04500 -5.84400  0.460 27.99000  ? 14  ARG A NH2  1 
ATOM   272  N  NH2  B ARG A 1 14  ? 12.80400  -8.80200  -3.11300  0.540 43.76000  ? 14  ARG A NH2  1 
ATOM   273  H  H    A ARG A 1 14  ? 12.73500  -16.06300 -5.26700  0.460 30.09000  ? 14  ARG A H    1 
ATOM   274  H  H    B ARG A 1 14  ? 12.81500  -16.04300 -5.19200  0.540 30.25000  ? 14  ARG A H    1 
ATOM   275  H  HA   A ARG A 1 14  ? 14.80000  -14.90100 -4.17000  0.460 29.83000  ? 14  ARG A HA   1 
ATOM   276  H  HA   B ARG A 1 14  ? 14.98600  -15.21600 -3.99100  0.540 30.11000  ? 14  ARG A HA   1 
ATOM   277  H  HB2  A ARG A 1 14  ? 13.83000  -13.77300 -5.82900  0.460 35.48000  ? 14  ARG A HB2  1 
ATOM   278  H  HB2  B ARG A 1 14  ? 14.03200  -13.96300 -5.71500  0.540 36.78000  ? 14  ARG A HB2  1 
ATOM   279  H  HB3  A ARG A 1 14  ? 12.38900  -13.89100 -5.17000  0.460 35.48000  ? 14  ARG A HB3  1 
ATOM   280  H  HB3  B ARG A 1 14  ? 12.83500  -13.56900 -4.74600  0.540 36.78000  ? 14  ARG A HB3  1 
ATOM   281  H  HG2  A ARG A 1 14  ? 12.85900  -12.23500 -3.69300  0.460 49.05000  ? 14  ARG A HG2  1 
ATOM   282  H  HG2  B ARG A 1 14  ? 14.28100  -12.37000 -3.38800  0.540 50.00000  ? 14  ARG A HG2  1 
ATOM   283  H  HG3  A ARG A 1 14  ? 14.38700  -12.21700 -4.12800  0.460 49.05000  ? 14  ARG A HG3  1 
ATOM   284  H  HG3  B ARG A 1 14  ? 15.52700  -12.84100 -4.25400  0.540 50.00000  ? 14  ARG A HG3  1 
ATOM   285  H  HD2  A ARG A 1 14  ? 13.29400  -10.42500 -5.14800  0.460 47.24000  ? 14  ARG A HD2  1 
ATOM   286  H  HD2  B ARG A 1 14  ? 15.30800  -10.92300 -5.23400  0.540 46.88000  ? 14  ARG A HD2  1 
ATOM   287  H  HD3  A ARG A 1 14  ? 13.73900  -11.45500 -6.27300  0.460 47.24000  ? 14  ARG A HD3  1 
ATOM   288  H  HD3  B ARG A 1 14  ? 14.12600  -11.62400 -6.03200  0.540 46.88000  ? 14  ARG A HD3  1 
ATOM   289  H  HE   A ARG A 1 14  ? 11.61400  -11.91700 -6.64300  0.460 56.30000  ? 14  ARG A HE   1 
ATOM   290  H  HE   B ARG A 1 14  ? 12.69700  -10.41200 -4.89700  0.540 55.72000  ? 14  ARG A HE   1 
ATOM   291  H  HH11 A ARG A 1 14  ? 11.69700  -9.82500  -4.06600  0.460 56.44000  ? 14  ARG A HH11 1 
ATOM   292  H  HH11 B ARG A 1 14  ? 15.63700  -9.93300  -3.43000  0.540 54.71000  ? 14  ARG A HH11 1 
ATOM   293  H  HH12 A ARG A 1 14  ? 10.22600  -9.59700  -4.01400  0.460 56.44000  ? 14  ARG A HH12 1 
ATOM   294  H  HH12 B ARG A 1 14  ? 15.16100  -8.88200  -2.48700  0.540 54.71000  ? 14  ARG A HH12 1 
ATOM   295  H  HH21 A ARG A 1 14  ? 9.39900   -11.58500 -6.50300  0.460 33.61000  ? 14  ARG A HH21 1 
ATOM   296  H  HH21 B ARG A 1 14  ? 12.00400  -8.87200  -3.42400  0.540 52.53000  ? 14  ARG A HH21 1 
ATOM   297  H  HH22 A ARG A 1 14  ? 8.84200   -10.65600 -5.48000  0.460 33.61000  ? 14  ARG A HH22 1 
ATOM   298  H  HH22 B ARG A 1 14  ? 12.97300  -8.24300  -2.48300  0.540 52.53000  ? 14  ARG A HH22 1 
ATOM   299  N  N    . HIS A 1 15  ? 12.35500  -15.17000 -2.18100  1.000 25.21000  ? 15  HIS A N    1 
ATOM   300  C  CA   . HIS A 1 15  ? 11.91400  -15.05500 -0.80100  1.000 24.50000  ? 15  HIS A CA   1 
ATOM   301  C  C    . HIS A 1 15  ? 12.28400  -16.25500 0.08600   1.000 26.50000  ? 15  HIS A C    1 
ATOM   302  O  O    . HIS A 1 15  ? 11.81000  -16.30700 1.22600   1.000 33.07000  ? 15  HIS A O    1 
ATOM   303  C  CB   . HIS A 1 15  ? 10.40000  -14.83400 -0.77100  1.000 29.54000  ? 15  HIS A CB   1 
ATOM   304  C  CG   . HIS A 1 15  ? 9.97700   -13.47000 -1.22900  1.000 29.19000  ? 15  HIS A CG   1 
ATOM   305  N  ND1  . HIS A 1 15  ? 9.98500   -12.36700 -0.40000  1.000 40.23000  ? 15  HIS A ND1  1 
ATOM   306  C  CD2  . HIS A 1 15  ? 9.52000   -13.03800 -2.42300  1.000 28.58000  ? 15  HIS A CD2  1 
ATOM   307  C  CE1  . HIS A 1 15  ? 9.55100   -11.31500 -1.07100  1.000 42.11000  ? 15  HIS A CE1  1 
ATOM   308  N  NE2  . HIS A 1 15  ? 9.25600   -11.69500 -2.30000  1.000 38.59000  ? 15  HIS A NE2  1 
ATOM   309  H  H    . HIS A 1 15  ? 11.75400  -15.45500 -2.72600  1.000 30.28000  ? 15  HIS A H    1 
ATOM   310  H  HA   . HIS A 1 15  ? 12.35500  -14.28400 -0.41100  1.000 29.43000  ? 15  HIS A HA   1 
ATOM   311  H  HB2  . HIS A 1 15  ? 9.97800   -15.48500 -1.35400  1.000 35.47000  ? 15  HIS A HB2  1 
ATOM   312  H  HB3  . HIS A 1 15  ? 10.08600  -14.95100 0.13900   1.000 35.47000  ? 15  HIS A HB3  1 
ATOM   313  H  HD1  . HIS A 1 15  ? 10.23400  -12.36500 0.42300   1.000 48.29000  ? 15  HIS A HD1  1 
ATOM   314  H  HD2  . HIS A 1 15  ? 9.40600   -13.55400 -3.18900  1.000 34.31000  ? 15  HIS A HD2  1 
ATOM   315  H  HE1  . HIS A 1 15  ? 9.46700   -10.45200 -0.73300  1.000 50.55000  ? 15  HIS A HE1  1 
ATOM   316  N  N    . GLY A 1 16  ? 13.11500  -17.18100 -0.38500  1.000 24.63000  ? 16  GLY A N    1 
ATOM   317  C  CA   . GLY A 1 16  ? 13.70600  -18.18500 0.47300   1.000 27.67000  ? 16  GLY A CA   1 
ATOM   318  C  C    . GLY A 1 16  ? 12.90500  -19.44800 0.67400   1.000 25.52000  ? 16  GLY A C    1 
ATOM   319  O  O    . GLY A 1 16  ? 13.16500  -20.18400 1.63700   1.000 29.52000  ? 16  GLY A O    1 
ATOM   320  H  H    . GLY A 1 16  ? 13.35200  -17.24400 -1.20900  1.000 29.57000  ? 16  GLY A H    1 
ATOM   321  H  HA2  . GLY A 1 16  ? 14.56300  -18.44200 0.09700   1.000 33.22000  ? 16  GLY A HA2  1 
ATOM   322  H  HA3  . GLY A 1 16  ? 13.85100  -17.79200 1.34800   1.000 33.22000  ? 16  GLY A HA3  1 
ATOM   323  N  N    . LEU A 1 17  ? 11.95100  -19.73900 -0.20300  1.000 25.45000  ? 17  LEU A N    1 
ATOM   324  C  CA   . LEU A 1 17  ? 11.13700  -20.93200 -0.03100  1.000 23.08000  ? 17  LEU A CA   1 
ATOM   325  C  C    . LEU A 1 17  ? 11.75900  -22.19000 -0.60800  1.000 26.31000  ? 17  LEU A C    1 
ATOM   326  O  O    . LEU A 1 17  ? 11.33400  -23.29200 -0.24300  1.000 25.91000  ? 17  LEU A O    1 
ATOM   327  C  CB   . LEU A 1 17  ? 9.77100   -20.74800 -0.68900  1.000 24.89000  ? 17  LEU A CB   1 
ATOM   328  C  CG   . LEU A 1 17  ? 8.77800   -20.02500 0.18200   1.000 25.87000  ? 17  LEU A CG   1 
ATOM   329  C  CD1  . LEU A 1 17  ? 7.42300   -19.99600 -0.51000  1.000 26.62000  ? 17  LEU A CD1  1 
ATOM   330  C  CD2  . LEU A 1 17  ? 8.58600   -20.65500 1.52900   1.000 27.34000  ? 17  LEU A CD2  1 
ATOM   331  H  H    . LEU A 1 17  ? 11.75900  -19.26700 -0.89600  1.000 30.56000  ? 17  LEU A H    1 
ATOM   332  H  HA   . LEU A 1 17  ? 11.01600  -21.06100 0.92300   1.000 27.72000  ? 17  LEU A HA   1 
ATOM   333  H  HB2  . LEU A 1 17  ? 9.88300   -20.23300 -1.50300  1.000 29.89000  ? 17  LEU A HB2  1 
ATOM   334  H  HB3  . LEU A 1 17  ? 9.40400   -21.62100 -0.89700  1.000 29.89000  ? 17  LEU A HB3  1 
ATOM   335  H  HG   . LEU A 1 17  ? 9.13200   -19.13300 0.32400   1.000 31.07000  ? 17  LEU A HG   1 
ATOM   336  H  HD11 . LEU A 1 17  ? 6.81300   -19.45200 0.01200   1.000 31.97000  ? 17  LEU A HD11 1 
ATOM   337  H  HD12 . LEU A 1 17  ? 7.52900   -19.61600 -1.39600  1.000 31.97000  ? 17  LEU A HD12 1 
ATOM   338  H  HD13 . LEU A 1 17  ? 7.08300   -20.90200 -0.57800  1.000 31.97000  ? 17  LEU A HD13 1 
ATOM   339  H  HD21 . LEU A 1 17  ? 7.75400   -20.33500 1.91200   1.000 32.83000  ? 17  LEU A HD21 1 
ATOM   340  H  HD22 . LEU A 1 17  ? 8.55300   -21.61900 1.42500   1.000 32.83000  ? 17  LEU A HD22 1 
ATOM   341  H  HD23 . LEU A 1 17  ? 9.33000   -20.40900 2.10100   1.000 32.83000  ? 17  LEU A HD23 1 
ATOM   342  N  N    A ASP A 1 18  ? 12.71500  -22.07800 -1.53000  0.460 26.84000  ? 18  ASP A N    1 
ATOM   343  N  N    B ASP A 1 18  ? 12.75500  -22.07400 -1.48400  0.540 26.76000  ? 18  ASP A N    1 
ATOM   344  C  CA   A ASP A 1 18  ? 13.33700  -23.27500 -2.07900  0.460 24.29000  ? 18  ASP A CA   1 
ATOM   345  C  CA   B ASP A 1 18  ? 13.33200  -23.24800 -2.12600  0.540 24.35000  ? 18  ASP A CA   1 
ATOM   346  C  C    A ASP A 1 18  ? 13.98700  -24.05800 -0.95100  0.460 29.29000  ? 18  ASP A C    1 
ATOM   347  C  C    B ASP A 1 18  ? 14.09200  -24.08300 -1.10000  0.540 28.84000  ? 18  ASP A C    1 
ATOM   348  O  O    A ASP A 1 18  ? 14.85700  -23.53700 -0.24400  0.460 31.49000  ? 18  ASP A O    1 
ATOM   349  O  O    B ASP A 1 18  ? 15.15300  -23.67500 -0.61800  0.540 28.56000  ? 18  ASP A O    1 
ATOM   350  C  CB   A ASP A 1 18  ? 14.37500  -22.91200 -3.14000  0.460 29.62000  ? 18  ASP A CB   1 
ATOM   351  C  CB   B ASP A 1 18  ? 14.23600  -22.83700 -3.28500  0.540 29.76000  ? 18  ASP A CB   1 
ATOM   352  C  CG   A ASP A 1 18  ? 14.72600  -24.09200 -4.05900  0.460 30.99000  ? 18  ASP A CG   1 
ATOM   353  C  CG   B ASP A 1 18  ? 15.24800  -21.77800 -2.90000  0.540 37.48000  ? 18  ASP A CG   1 
ATOM   354  O  OD1  A ASP A 1 18  ? 14.15500  -25.19800 -3.91800  0.460 23.47000  ? 18  ASP A OD1  1 
ATOM   355  O  OD1  B ASP A 1 18  ? 14.84200  -20.70900 -2.37600  0.540 31.05000  ? 18  ASP A OD1  1 
ATOM   356  O  OD2  A ASP A 1 18  ? 15.58300  -23.90700 -4.94800  0.460 34.59000  ? 18  ASP A OD2  1 
ATOM   357  O  OD2  B ASP A 1 18  ? 16.45400  -22.01600 -3.13500  0.540 34.45000  ? 18  ASP A OD2  1 
ATOM   358  H  H    A ASP A 1 18  ? 13.01300  -21.33600 -1.84500  0.460 32.23000  ? 18  ASP A H    1 
ATOM   359  H  H    B ASP A 1 18  ? 13.11200  -21.32800 -1.72100  0.540 32.13000  ? 18  ASP A H    1 
ATOM   360  H  HA   A ASP A 1 18  ? 12.66200  -23.82200 -2.51000  0.460 29.17000  ? 18  ASP A HA   1 
ATOM   361  H  HA   B ASP A 1 18  ? 12.61400  -23.79200 -2.48500  0.540 29.24000  ? 18  ASP A HA   1 
ATOM   362  H  HB2  A ASP A 1 18  ? 14.02500  -22.19600 -3.69300  0.460 35.57000  ? 18  ASP A HB2  1 
ATOM   363  H  HB2  B ASP A 1 18  ? 14.72300  -23.61500 -3.59700  0.540 35.73000  ? 18  ASP A HB2  1 
ATOM   364  H  HB3  A ASP A 1 18  ? 15.18900  -22.62300 -2.70000  0.460 35.57000  ? 18  ASP A HB3  1 
ATOM   365  H  HB3  B ASP A 1 18  ? 13.68700  -22.47900 -4.00100  0.540 35.73000  ? 18  ASP A HB3  1 
ATOM   366  N  N    A ASN A 1 19  ? 13.53900  -25.30200 -0.76800  0.540 25.12000  ? 19  ASN A N    1 
ATOM   367  N  N    B ASN A 1 19  ? 13.55200  -25.26600 -0.79000  0.460 25.11000  ? 19  ASN A N    1 
ATOM   368  C  CA   A ASN A 1 19  ? 14.02800  -26.21300 0.26500   0.540 24.52000  ? 19  ASN A CA   1 
ATOM   369  C  CA   B ASN A 1 19  ? 14.03000  -26.19300 0.23600   0.460 24.64000  ? 19  ASN A CA   1 
ATOM   370  C  C    A ASN A 1 19  ? 13.84700  -25.66800 1.67500   0.540 23.22000  ? 19  ASN A C    1 
ATOM   371  C  C    B ASN A 1 19  ? 13.83200  -25.68000 1.66100   0.460 23.24000  ? 19  ASN A C    1 
ATOM   372  O  O    A ASN A 1 19  ? 14.51300  -26.11300 2.61500   0.540 24.76000  ? 19  ASN A O    1 
ATOM   373  O  O    B ASN A 1 19  ? 14.49000  -26.15600 2.59200   0.460 24.75000  ? 19  ASN A O    1 
ATOM   374  C  CB   A ASN A 1 19  ? 15.45700  -26.66700 -0.02800  0.540 28.89000  ? 19  ASN A CB   1 
ATOM   375  C  CB   B ASN A 1 19  ? 15.46800  -26.67300 0.02000   0.460 28.87000  ? 19  ASN A CB   1 
ATOM   376  C  CG   A ASN A 1 19  ? 15.50100  -27.70900 -1.12800  0.540 32.53000  ? 19  ASN A CG   1 
ATOM   377  C  CG   B ASN A 1 19  ? 15.63900  -28.15100 0.36400   0.460 30.90000  ? 19  ASN A CG   1 
ATOM   378  O  OD1  A ASN A 1 19  ? 14.92300  -28.79200 -0.99400  0.540 43.75000  ? 19  ASN A OD1  1 
ATOM   379  O  OD1  B ASN A 1 19  ? 14.70000  -28.95000 0.25400   0.460 29.54000  ? 19  ASN A OD1  1 
ATOM   380  N  ND2  A ASN A 1 19  ? 16.14000  -27.37300 -2.24000  0.540 40.00000  ? 19  ASN A ND2  1 
ATOM   381  N  ND2  B ASN A 1 19  ? 16.83100  -28.51100 0.82500   0.460 37.04000  ? 19  ASN A ND2  1 
ATOM   382  H  H    A ASN A 1 19  ? 12.92300  -25.65500 -1.25300  0.540 30.17000  ? 19  ASN A H    1 
ATOM   383  H  H    B ASN A 1 19  ? 12.85600  -25.57300 -1.19000  0.460 30.15000  ? 19  ASN A H    1 
ATOM   384  H  HA   A ASN A 1 19  ? 13.48600  -27.01800 0.24800   0.540 29.45000  ? 19  ASN A HA   1 
ATOM   385  H  HA   B ASN A 1 19  ? 13.47900  -26.98700 0.14700   0.460 29.59000  ? 19  ASN A HA   1 
ATOM   386  H  HB2  A ASN A 1 19  ? 15.98400  -25.90300 -0.31100  0.540 34.69000  ? 19  ASN A HB2  1 
ATOM   387  H  HB2  B ASN A 1 19  ? 15.70900  -26.54900 -0.91100  0.460 34.66000  ? 19  ASN A HB2  1 
ATOM   388  H  HB3  A ASN A 1 19  ? 15.84000  -27.05500 0.77500   0.540 34.69000  ? 19  ASN A HB3  1 
ATOM   389  H  HB3  B ASN A 1 19  ? 16.06400  -26.16000 0.58800   0.460 34.66000  ? 19  ASN A HB3  1 
ATOM   390  H  HD21 A ASN A 1 19  ? 16.19200  -27.93100 -2.89200  0.540 48.02000  ? 19  ASN A HD21 1 
ATOM   391  H  HD21 B ASN A 1 19  ? 16.98100  -29.33100 1.03400   0.460 44.47000  ? 19  ASN A HD21 1 
ATOM   392  H  HD22 A ASN A 1 19  ? 16.50300  -26.59600 -2.30900  0.540 48.02000  ? 19  ASN A HD22 1 
ATOM   393  H  HD22 B ASN A 1 19  ? 17.45300  -27.92300 0.91400   0.460 44.47000  ? 19  ASN A HD22 1 
ATOM   394  N  N    . TYR A 1 20  ? 12.91700  -24.73800 1.87200   1.000 21.99000  ? 20  TYR A N    1 
ATOM   395  C  CA   . TYR A 1 20  ? 12.59400  -24.30100 3.22200   1.000 21.59000  ? 20  TYR A CA   1 
ATOM   396  C  C    . TYR A 1 20  ? 11.96800  -25.46100 3.98200   1.000 25.18000  ? 20  TYR A C    1 
ATOM   397  O  O    . TYR A 1 20  ? 10.98100  -26.05600 3.53300   1.000 23.44000  ? 20  TYR A O    1 
ATOM   398  C  CB   . TYR A 1 20  ? 11.66300  -23.09200 3.20500   1.000 23.94000  ? 20  TYR A CB   1 
ATOM   399  C  CG   . TYR A 1 20  ? 11.51100  -22.45500 4.56100   1.000 21.52000  ? 20  TYR A CG   1 
ATOM   400  C  CD1  . TYR A 1 20  ? 12.44100  -21.52500 5.02300   1.000 27.28000  ? 20  TYR A CD1  1 
ATOM   401  C  CD2  . TYR A 1 20  ? 10.46100  -22.79200 5.39600   1.000 22.47000  ? 20  TYR A CD2  1 
ATOM   402  C  CE1  . TYR A 1 20  ? 12.31200  -20.95700 6.27100   1.000 32.34000  ? 20  TYR A CE1  1 
ATOM   403  C  CE2  . TYR A 1 20  ? 10.33700  -22.23300 6.64200   1.000 25.67000  ? 20  TYR A CE2  1 
ATOM   404  C  CZ   . TYR A 1 20  ? 11.26400  -21.32500 7.07600   1.000 31.30000  ? 20  TYR A CZ   1 
ATOM   405  O  OH   . TYR A 1 20  ? 11.12100  -20.75300 8.32100   1.000 34.37000  ? 20  TYR A OH   1 
ATOM   406  H  H    . TYR A 1 20  ? 12.46800  -24.35300 1.24800   1.000 26.41000  ? 20  TYR A H    1 
ATOM   407  H  HA   . TYR A 1 20  ? 13.40500  -24.02100 3.67400   1.000 25.93000  ? 20  TYR A HA   1 
ATOM   408  H  HB2  . TYR A 1 20  ? 12.02200  -22.42600 2.59800   1.000 28.75000  ? 20  TYR A HB2  1 
ATOM   409  H  HB3  . TYR A 1 20  ? 10.78500  -23.37500 2.90600   1.000 28.75000  ? 20  TYR A HB3  1 
ATOM   410  H  HD1  . TYR A 1 20  ? 13.15800  -21.28500 4.48200   1.000 32.76000  ? 20  TYR A HD1  1 
ATOM   411  H  HD2  . TYR A 1 20  ? 9.82800   -23.41000 5.10700   1.000 26.98000  ? 20  TYR A HD2  1 
ATOM   412  H  HE1  . TYR A 1 20  ? 12.93000  -20.32800 6.56600   1.000 38.83000  ? 20  TYR A HE1  1 
ATOM   413  H  HE2  . TYR A 1 20  ? 9.62400   -22.47000 7.19100   1.000 30.83000  ? 20  TYR A HE2  1 
ATOM   414  H  HH   . TYR A 1 20  ? 10.60700  -21.21900 8.79400   1.000 41.26000  ? 20  TYR A HH   1 
ATOM   415  N  N    A ARG A 1 21  ? 12.55100  -25.80000 5.12900   0.530 24.18000  ? 21  ARG A N    1 
ATOM   416  N  N    B ARG A 1 21  ? 12.57500  -25.80400 5.11700   0.470 24.15000  ? 21  ARG A N    1 
ATOM   417  C  CA   A ARG A 1 21  ? 12.13200  -26.96800 5.89700   0.530 24.91000  ? 21  ARG A CA   1 
ATOM   418  C  CA   B ARG A 1 21  ? 12.17500  -26.96700 5.90100   0.470 24.99000  ? 21  ARG A CA   1 
ATOM   419  C  C    A ARG A 1 21  ? 12.14400  -28.24100 5.06000   0.530 21.14000  ? 21  ARG A C    1 
ATOM   420  C  C    B ARG A 1 21  ? 12.14800  -28.23500 5.06100   0.470 21.18000  ? 21  ARG A C    1 
ATOM   421  O  O    A ARG A 1 21  ? 11.40600  -29.18700 5.34600   0.530 23.63000  ? 21  ARG A O    1 
ATOM   422  O  O    B ARG A 1 21  ? 11.39000  -29.16500 5.34500   0.470 23.56000  ? 21  ARG A O    1 
ATOM   423  C  CB   A ARG A 1 21  ? 10.76400  -26.76200 6.54700   0.530 26.28000  ? 21  ARG A CB   1 
ATOM   424  C  CB   B ARG A 1 21  ? 10.84600  -26.74100 6.61300   0.470 26.36000  ? 21  ARG A CB   1 
ATOM   425  C  CG   A ARG A 1 21  ? 10.78900  -25.86100 7.76400   0.530 36.96000  ? 21  ARG A CG   1 
ATOM   426  C  CG   B ARG A 1 21  ? 10.84700  -25.51700 7.50000   0.470 37.57000  ? 21  ARG A CG   1 
ATOM   427  C  CD   A ARG A 1 21  ? 11.22100  -26.61500 9.00800   0.530 41.60000  ? 21  ARG A CD   1 
ATOM   428  C  CD   B ARG A 1 21  ? 11.40700  -25.83500 8.87700   0.470 39.76000  ? 21  ARG A CD   1 
ATOM   429  N  NE   A ARG A 1 21  ? 11.07300  -25.80200 10.21000  0.530 50.64000  ? 21  ARG A NE   1 
ATOM   430  N  NE   B ARG A 1 21  ? 11.58600  -24.62700 9.67600   0.470 36.83000  ? 21  ARG A NE   1 
ATOM   431  C  CZ   A ARG A 1 21  ? 11.56900  -26.11900 11.39800  0.530 49.93000  ? 21  ARG A CZ   1 
ATOM   432  C  CZ   B ARG A 1 21  ? 12.74100  -24.00400 9.86500   0.470 37.69000  ? 21  ARG A CZ   1 
ATOM   433  N  NH1  A ARG A 1 21  ? 12.23200  -27.24800 11.59200  0.530 72.91000  ? 21  ARG A NH1  1 
ATOM   434  N  NH1  B ARG A 1 21  ? 13.87500  -24.47400 9.36600   0.470 51.52000  ? 21  ARG A NH1  1 
ATOM   435  N  NH2  A ARG A 1 21  ? 11.39600  -25.28400 12.41800  0.530 57.45000  ? 21  ARG A NH2  1 
ATOM   436  N  NH2  B ARG A 1 21  ? 12.76000  -22.87700 10.57100  0.470 45.14000  ? 21  ARG A NH2  1 
ATOM   437  H  H    A ARG A 1 21  ? 13.20000  -25.36400 5.48700   0.530 29.04000  ? 21  ARG A H    1 
ATOM   438  H  H    B ARG A 1 21  ? 13.23300  -25.37000 5.46000   0.470 29.00000  ? 21  ARG A H    1 
ATOM   439  H  HA   A ARG A 1 21  ? 12.77900  -27.08800 6.61000   0.530 29.92000  ? 21  ARG A HA   1 
ATOM   440  H  HA   B ARG A 1 21  ? 12.84600  -27.10200 6.58800   0.470 30.00000  ? 21  ARG A HA   1 
ATOM   441  H  HB2  A ARG A 1 21  ? 10.16800  -26.36100 5.89600   0.530 31.56000  ? 21  ARG A HB2  1 
ATOM   442  H  HB2  B ARG A 1 21  ? 10.14900  -26.62700 5.94800   0.470 31.65000  ? 21  ARG A HB2  1 
ATOM   443  H  HB3  A ARG A 1 21  ? 10.41900  -27.62400 6.82600   0.530 31.56000  ? 21  ARG A HB3  1 
ATOM   444  H  HB3  B ARG A 1 21  ? 10.65200  -27.51200 7.16800   0.470 31.65000  ? 21  ARG A HB3  1 
ATOM   445  H  HG2  A ARG A 1 21  ? 11.41700  -25.13600 7.61400   0.530 44.37000  ? 21  ARG A HG2  1 
ATOM   446  H  HG2  B ARG A 1 21  ? 11.39800  -24.82700 7.09800   0.470 45.10000  ? 21  ARG A HG2  1 
ATOM   447  H  HG3  A ARG A 1 21  ? 9.90100   -25.50400 7.91800   0.530 44.37000  ? 21  ARG A HG3  1 
ATOM   448  H  HG3  B ARG A 1 21  ? 9.93800   -25.19500 7.60700   0.470 45.10000  ? 21  ARG A HG3  1 
ATOM   449  H  HD2  A ARG A 1 21  ? 10.67200  -27.40900 9.10800   0.530 49.94000  ? 21  ARG A HD2  1 
ATOM   450  H  HD2  B ARG A 1 21  ? 10.79300  -26.42200 9.34500   0.470 47.74000  ? 21  ARG A HD2  1 
ATOM   451  H  HD3  A ARG A 1 21  ? 12.15400  -26.86600 8.92300   0.530 49.94000  ? 21  ARG A HD3  1 
ATOM   452  H  HD3  B ARG A 1 21  ? 12.27000  -26.26700 8.78000   0.470 47.74000  ? 21  ARG A HD3  1 
ATOM   453  H  HE   A ARG A 1 21  ? 10.63300  -25.06600 10.14400  0.530 60.78000  ? 21  ARG A HE   1 
ATOM   454  H  HE   B ARG A 1 21  ? 10.88800  -24.29400 10.05300  0.470 44.22000  ? 21  ARG A HE   1 
ATOM   455  H  HH11 A ARG A 1 21  ? 12.34900  -27.79600 10.93900  0.530 87.51000  ? 21  ARG A HH11 1 
ATOM   456  H  HH11 B ARG A 1 21  ? 13.87400  -25.20100 8.90700   0.470 61.84000  ? 21  ARG A HH11 1 
ATOM   457  H  HH12 A ARG A 1 21  ? 12.54600  -27.43500 12.37100  0.530 87.51000  ? 21  ARG A HH12 1 
ATOM   458  H  HH12 B ARG A 1 21  ? 14.61200  -24.05200 9.50200   0.470 61.84000  ? 21  ARG A HH12 1 
ATOM   459  H  HH21 A ARG A 1 21  ? 10.96600  -24.54800 12.30300  0.530 68.96000  ? 21  ARG A HH21 1 
ATOM   460  H  HH21 B ARG A 1 21  ? 12.03000  -22.56300 10.89900  0.470 54.19000  ? 21  ARG A HH21 1 
ATOM   461  H  HH22 A ARG A 1 21  ? 11.71400  -25.47900 13.19300  0.530 68.96000  ? 21  ARG A HH22 1 
ATOM   462  H  HH22 B ARG A 1 21  ? 13.50300  -22.46300 10.70100  0.470 54.19000  ? 21  ARG A HH22 1 
ATOM   463  N  N    . GLY A 1 22  ? 13.00700  -28.28800 4.05300   1.000 21.06000  ? 22  GLY A N    1 
ATOM   464  C  CA   . GLY A 1 22  ? 13.16300  -29.45400 3.22000   1.000 21.79000  ? 22  GLY A CA   1 
ATOM   465  C  C    . GLY A 1 22  ? 12.17300  -29.61500 2.08700   1.000 22.46000  ? 22  GLY A C    1 
ATOM   466  O  O    . GLY A 1 22  ? 12.18900  -30.65400 1.42400   1.000 23.45000  ? 22  GLY A O    1 
ATOM   467  H  H    . GLY A 1 22  ? 13.52400  -27.63600 3.83200   1.000 25.29000  ? 22  GLY A H    1 
ATOM   468  H  HA2  . GLY A 1 22  ? 14.04900  -29.43000 2.82700   1.000 26.16000  ? 22  GLY A HA2  1 
ATOM   469  H  HA3  . GLY A 1 22  ? 13.08800  -30.24100 3.78200   1.000 26.16000  ? 22  GLY A HA3  1 
ATOM   470  N  N    . TYR A 1 23  ? 11.33500  -28.61300 1.82000   1.000 20.65000  ? 23  TYR A N    1 
ATOM   471  C  CA   . TYR A 1 23  ? 10.35600  -28.67400 0.74200   1.000 18.62000  ? 23  TYR A CA   1 
ATOM   472  C  C    . TYR A 1 23  ? 10.91500  -27.94600 -0.46600  1.000 17.63000  ? 23  TYR A C    1 
ATOM   473  O  O    . TYR A 1 23  ? 11.01700  -26.71100 -0.47200  1.000 20.36000  ? 23  TYR A O    1 
ATOM   474  C  CB   . TYR A 1 23  ? 9.03100   -28.05500 1.19400   1.000 17.23000  ? 23  TYR A CB   1 
ATOM   475  C  CG   . TYR A 1 23  ? 8.36800   -28.93300 2.22700   1.000 15.70000  ? 23  TYR A CG   1 
ATOM   476  C  CD1  . TYR A 1 23  ? 7.55000   -29.98100 1.84800   1.000 17.48000  ? 23  TYR A CD1  1 
ATOM   477  C  CD2  . TYR A 1 23  ? 8.54000   -28.69700 3.60100   1.000 17.08000  ? 23  TYR A CD2  1 
ATOM   478  C  CE1  . TYR A 1 23  ? 6.95700   -30.79400 2.78500   1.000 17.33000  ? 23  TYR A CE1  1 
ATOM   479  C  CE2  . TYR A 1 23  ? 7.96000   -29.51900 4.55200   1.000 16.29000  ? 23  TYR A CE2  1 
ATOM   480  C  CZ   . TYR A 1 23  ? 7.14200   -30.54100 4.12100   1.000 15.93000  ? 23  TYR A CZ   1 
ATOM   481  O  OH   . TYR A 1 23  ? 6.49600   -31.40300 5.00700   1.000 18.44000  ? 23  TYR A OH   1 
ATOM   482  H  H    . TYR A 1 23  ? 11.31700  -27.87400 2.25900   1.000 24.80000  ? 23  TYR A H    1 
ATOM   483  H  HA   . TYR A 1 23  ? 10.20100  -29.59900 0.49300   1.000 22.36000  ? 23  TYR A HA   1 
ATOM   484  H  HB2  . TYR A 1 23  ? 9.19700   -27.18400 1.58800   1.000 20.69000  ? 23  TYR A HB2  1 
ATOM   485  H  HB3  . TYR A 1 23  ? 8.43600   -27.96700 0.43300   1.000 20.69000  ? 23  TYR A HB3  1 
ATOM   486  H  HD1  . TYR A 1 23  ? 7.39800   -30.13900 0.94400   1.000 20.99000  ? 23  TYR A HD1  1 
ATOM   487  H  HD2  . TYR A 1 23  ? 9.05500   -27.97300 3.87800   1.000 20.51000  ? 23  TYR A HD2  1 
ATOM   488  H  HE1  . TYR A 1 23  ? 6.43200   -31.51300 2.51500   1.000 20.81000  ? 23  TYR A HE1  1 
ATOM   489  H  HE2  . TYR A 1 23  ? 8.11700   -29.38500 5.45900   1.000 19.57000  ? 23  TYR A HE2  1 
ATOM   490  H  HH   . TYR A 1 23  ? 6.77300   -31.27300 5.78900   1.000 22.15000  ? 23  TYR A HH   1 
ATOM   491  N  N    . SER A 1 24  ? 11.23400  -28.72000 -1.49300  1.000 19.54000  ? 24  SER A N    1 
ATOM   492  C  CA   . SER A 1 24  ? 11.75800  -28.13300 -2.72300  1.000 19.37000  ? 24  SER A CA   1 
ATOM   493  C  C    . SER A 1 24  ? 10.72500  -27.22000 -3.37000  1.000 18.88000  ? 24  SER A C    1 
ATOM   494  O  O    . SER A 1 24  ? 9.51300   -27.31800 -3.13800  1.000 19.25000  ? 24  SER A O    1 
ATOM   495  C  CB   . SER A 1 24  ? 12.16000  -29.22900 -3.71100  1.000 21.21000  ? 24  SER A CB   1 
ATOM   496  O  OG   . SER A 1 24  ? 11.02800  -29.90600 -4.21300  1.000 26.38000  ? 24  SER A OG   1 
ATOM   497  H  H    . SER A 1 24  ? 11.15900  -29.57600 -1.50600  1.000 23.46000  ? 24  SER A H    1 
ATOM   498  H  HA   . SER A 1 24  ? 12.54400  -27.60600 -2.51100  1.000 23.27000  ? 24  SER A HA   1 
ATOM   499  H  HB2  . SER A 1 24  ? 12.63800  -28.82400 -4.45200  1.000 25.47000  ? 24  SER A HB2  1 
ATOM   500  H  HB3  . SER A 1 24  ? 12.73300  -29.86700 -3.25700  1.000 25.47000  ? 24  SER A HB3  1 
ATOM   501  H  HG   . SER A 1 24  ? 10.60900  -30.27000 -3.58200  1.000 31.68000  ? 24  SER A HG   1 
ATOM   502  N  N    . LEU A 1 25  ? 11.22500  -26.31200 -4.21000  1.000 19.07000  ? 25  LEU A N    1 
ATOM   503  C  CA   . LEU A 1 25  ? 10.40300  -25.27400 -4.78700  1.000 17.84000  ? 25  LEU A CA   1 
ATOM   504  C  C    . LEU A 1 25  ? 9.15900   -25.79400 -5.48300  1.000 18.58000  ? 25  LEU A C    1 
ATOM   505  O  O    . LEU A 1 25  ? 8.10200   -25.14800 -5.42500  1.000 18.57000  ? 25  LEU A O    1 
ATOM   506  C  CB   . LEU A 1 25  ? 11.24700  -24.46000 -5.77800  1.000 22.41000  ? 25  LEU A CB   1 
ATOM   507  C  CG   . LEU A 1 25  ? 10.74600  -23.12800 -6.25400  1.000 21.79000  ? 25  LEU A CG   1 
ATOM   508  C  CD1  . LEU A 1 25  ? 10.49500  -22.18900 -5.08600  1.000 26.29000  ? 25  LEU A CD1  1 
ATOM   509  C  CD2  . LEU A 1 25  ? 11.78100  -22.51300 -7.18800  1.000 23.11000  ? 25  LEU A CD2  1 
ATOM   510  H  H    . LEU A 1 25  ? 12.04700  -26.28100 -4.46000  1.000 22.90000  ? 25  LEU A H    1 
ATOM   511  H  HA   . LEU A 1 25  ? 10.09600  -24.70600 -4.06300  1.000 21.42000  ? 25  LEU A HA   1 
ATOM   512  H  HB2  . LEU A 1 25  ? 12.10500  -24.29400 -5.35700  1.000 26.92000  ? 25  LEU A HB2  1 
ATOM   513  H  HB3  . LEU A 1 25  ? 11.36700  -25.00600 -6.57100  1.000 26.92000  ? 25  LEU A HB3  1 
ATOM   514  H  HG   . LEU A 1 25  ? 9.90600   -23.25100 -6.72500  1.000 26.17000  ? 25  LEU A HG   1 
ATOM   515  H  HD11 . LEU A 1 25  ? 10.32800  -21.29600 -5.42800  1.000 31.57000  ? 25  LEU A HD11 1 
ATOM   516  H  HD12 . LEU A 1 25  ? 9.72300   -22.50200 -4.58900  1.000 31.57000  ? 25  LEU A HD12 1 
ATOM   517  H  HD13 . LEU A 1 25  ? 11.27800  -22.18200 -4.51300  1.000 31.57000  ? 25  LEU A HD13 1 
ATOM   518  H  HD21 . LEU A 1 25  ? 11.42100  -21.69500 -7.56400  1.000 27.76000  ? 25  LEU A HD21 1 
ATOM   519  H  HD22 . LEU A 1 25  ? 12.58600  -22.31800 -6.68300  1.000 27.76000  ? 25  LEU A HD22 1 
ATOM   520  H  HD23 . LEU A 1 25  ? 11.98100  -23.14300 -7.89800  1.000 27.76000  ? 25  LEU A HD23 1 
ATOM   521  N  N    . GLY A 1 26  ? 9.25100   -26.90900 -6.19600  1.000 17.79000  ? 26  GLY A N    1 
ATOM   522  C  CA   . GLY A 1 26  ? 8.09700   -27.42700 -6.89600  1.000 18.68000  ? 26  GLY A CA   1 
ATOM   523  C  C    . GLY A 1 26  ? 6.92100   -27.72100 -5.98700  1.000 16.99000  ? 26  GLY A C    1 
ATOM   524  O  O    . GLY A 1 26  ? 5.77200   -27.65700 -6.42500  1.000 17.25000  ? 26  GLY A O    1 
ATOM   525  H  H    . GLY A 1 26  ? 9.96600   -27.37800 -6.28800  1.000 21.37000  ? 26  GLY A H    1 
ATOM   526  H  HA2  . GLY A 1 26  ? 7.81100   -26.77900 -7.55800  1.000 22.44000  ? 26  GLY A HA2  1 
ATOM   527  H  HA3  . GLY A 1 26  ? 8.34300   -28.25100 -7.34600  1.000 22.44000  ? 26  GLY A HA3  1 
ATOM   528  N  N    . ASN A 1 27  ? 7.18400   -28.06500 -4.72800  1.000 16.43000  ? 27  ASN A N    1 
ATOM   529  C  CA   . ASN A 1 27  ? 6.08100   -28.32000 -3.79900  1.000 16.36000  ? 27  ASN A CA   1 
ATOM   530  C  C    . ASN A 1 27  ? 5.25600   -27.05800 -3.59600  1.000 17.36000  ? 27  ASN A C    1 
ATOM   531  O  O    . ASN A 1 27  ? 4.02400   -27.11700 -3.54900  1.000 16.39000  ? 27  ASN A O    1 
ATOM   532  C  CB   . ASN A 1 27  ? 6.59800   -28.74700 -2.43300  1.000 16.97000  ? 27  ASN A CB   1 
ATOM   533  C  CG   . ASN A 1 27  ? 7.08300   -30.14600 -2.41400  1.000 18.76000  ? 27  ASN A CG   1 
ATOM   534  O  OD1  . ASN A 1 27  ? 6.30600   -31.08200 -2.46700  1.000 18.55000  ? 27  ASN A OD1  1 
ATOM   535  N  ND2  . ASN A 1 27  ? 8.41500   -30.29700 -2.40900  1.000 19.52000  ? 27  ASN A ND2  1 
ATOM   536  H  H    . ASN A 1 27  ? 7.97000   -28.15600 -4.39200  1.000 19.74000  ? 27  ASN A H    1 
ATOM   537  H  HA   . ASN A 1 27  ? 5.54400   -29.03400 -4.17500  1.000 19.66000  ? 27  ASN A HA   1 
ATOM   538  H  HB2  . ASN A 1 27  ? 7.33600   -28.17100 -2.17900  1.000 20.38000  ? 27  ASN A HB2  1 
ATOM   539  H  HB3  . ASN A 1 27  ? 5.88000   -28.67100 -1.78500  1.000 20.38000  ? 27  ASN A HB3  1 
ATOM   540  H  HD21 . ASN A 1 27  ? 8.75900   -31.08500 -2.39800  1.000 23.44000  ? 27  ASN A HD21 1 
ATOM   541  H  HD22 . ASN A 1 27  ? 8.92600   -29.60500 -2.41700  1.000 23.44000  ? 27  ASN A HD22 1 
ATOM   542  N  N    . TRP A 1 28  ? 5.92700   -25.91100 -3.47000  1.000 16.88000  ? 28  TRP A N    1 
ATOM   543  C  CA   . TRP A 1 28  ? 5.23900   -24.65400 -3.21600  1.000 16.60000  ? 28  TRP A CA   1 
ATOM   544  C  C    . TRP A 1 28  ? 4.47200   -24.17900 -4.43600  1.000 18.24000  ? 28  TRP A C    1 
ATOM   545  O  O    . TRP A 1 28  ? 3.36400   -23.65900 -4.31600  1.000 18.18000  ? 28  TRP A O    1 
ATOM   546  C  CB   . TRP A 1 28  ? 6.26000   -23.61600 -2.78200  1.000 17.92000  ? 28  TRP A CB   1 
ATOM   547  C  CG   . TRP A 1 28  ? 6.96600   -23.97300 -1.52800  1.000 16.19000  ? 28  TRP A CG   1 
ATOM   548  C  CD1  . TRP A 1 28  ? 8.21100   -24.52000 -1.38500  1.000 18.36000  ? 28  TRP A CD1  1 
ATOM   549  C  CD2  . TRP A 1 28  ? 6.44000   -23.84300 -0.21000  1.000 16.94000  ? 28  TRP A CD2  1 
ATOM   550  N  NE1  . TRP A 1 28  ? 8.49200   -24.71900 -0.05400  1.000 19.88000  ? 28  TRP A NE1  1 
ATOM   551  C  CE2  . TRP A 1 28  ? 7.41600   -24.30200 0.69200   1.000 18.04000  ? 28  TRP A CE2  1 
ATOM   552  C  CE3  . TRP A 1 28  ? 5.23100   -23.36000 0.29700   1.000 19.75000  ? 28  TRP A CE3  1 
ATOM   553  C  CZ2  . TRP A 1 28  ? 7.21300   -24.29700 2.06600   1.000 19.89000  ? 28  TRP A CZ2  1 
ATOM   554  C  CZ3  . TRP A 1 28  ? 5.04700   -23.35400 1.64300   1.000 21.38000  ? 28  TRP A CZ3  1 
ATOM   555  C  CH2  . TRP A 1 28  ? 6.02700   -23.82100 2.51500   1.000 21.62000  ? 28  TRP A CH2  1 
ATOM   556  H  H    . TRP A 1 28  ? 6.78200   -25.83700 -3.52700  1.000 20.27000  ? 28  TRP A H    1 
ATOM   557  H  HA   . TRP A 1 28  ? 4.59300   -24.77800 -2.50300  1.000 19.94000  ? 28  TRP A HA   1 
ATOM   558  H  HB2  . TRP A 1 28  ? 6.92500   -23.52000 -3.48100  1.000 21.52000  ? 28  TRP A HB2  1 
ATOM   559  H  HB3  . TRP A 1 28  ? 5.80600   -22.77100 -2.63800  1.000 21.52000  ? 28  TRP A HB3  1 
ATOM   560  H  HD1  . TRP A 1 28  ? 8.78500   -24.72700 -2.08700  1.000 22.05000  ? 28  TRP A HD1  1 
ATOM   561  H  HE1  . TRP A 1 28  ? 9.22100   -25.05100 0.26000   1.000 23.88000  ? 28  TRP A HE1  1 
ATOM   562  H  HE3  . TRP A 1 28  ? 4.56700   -23.05000 -0.27400  1.000 23.72000  ? 28  TRP A HE3  1 
ATOM   563  H  HZ2  . TRP A 1 28  ? 7.86400   -24.60700 2.65300   1.000 23.88000  ? 28  TRP A HZ2  1 
ATOM   564  H  HZ3  . TRP A 1 28  ? 4.24800   -23.03000 1.99000   1.000 25.68000  ? 28  TRP A HZ3  1 
ATOM   565  H  HH2  . TRP A 1 28  ? 5.86200   -23.80600 3.43000   1.000 25.97000  ? 28  TRP A HH2  1 
ATOM   566  N  N    . VAL A 1 29  ? 5.03500   -24.38800 -5.62700  1.000 16.33000  ? 29  VAL A N    1 
ATOM   567  C  CA   . VAL A 1 29  ? 4.35700   -24.01500 -6.85500  1.000 14.68000  ? 29  VAL A CA   1 
ATOM   568  C  C    . VAL A 1 29  ? 3.12800   -24.88600 -7.05500  1.000 17.24000  ? 29  VAL A C    1 
ATOM   569  O  O    . VAL A 1 29  ? 2.06000   -24.40400 -7.45000  1.000 17.59000  ? 29  VAL A O    1 
ATOM   570  C  CB   . VAL A 1 29  ? 5.31700   -24.06400 -8.06900  1.000 17.26000  ? 29  VAL A CB   1 
ATOM   571  C  CG1  . VAL A 1 29  ? 4.56100   -23.76500 -9.35500  1.000 19.60000  ? 29  VAL A CG1  1 
ATOM   572  C  CG2  . VAL A 1 29  ? 6.44500   -23.06100 -7.83500  1.000 19.70000  ? 29  VAL A CG2  1 
ATOM   573  H  H    . VAL A 1 29  ? 5.80800   -24.74400 -5.74600  1.000 19.62000  ? 29  VAL A H    1 
ATOM   574  H  HA   . VAL A 1 29  ? 4.06600   -23.09400 -6.77400  1.000 17.64000  ? 29  VAL A HA   1 
ATOM   575  H  HB   . VAL A 1 29  ? 5.69900   -24.95000 -8.16700  1.000 20.73000  ? 29  VAL A HB   1 
ATOM   576  H  HG11 . VAL A 1 29  ? 5.19900   -23.63800 -10.07400 1.000 23.54000  ? 29  VAL A HG11 1 
ATOM   577  H  HG12 . VAL A 1 29  ? 3.97700   -24.51200 -9.55900  1.000 23.54000  ? 29  VAL A HG12 1 
ATOM   578  H  HG13 . VAL A 1 29  ? 4.03600   -22.95900 -9.23200  1.000 23.54000  ? 29  VAL A HG13 1 
ATOM   579  H  HG21 . VAL A 1 29  ? 6.97300   -22.98600 -8.64500  1.000 23.66000  ? 29  VAL A HG21 1 
ATOM   580  H  HG22 . VAL A 1 29  ? 6.06000   -22.20000 -7.61000  1.000 23.66000  ? 29  VAL A HG22 1 
ATOM   581  H  HG23 . VAL A 1 29  ? 7.00100   -23.37600 -7.10600  1.000 23.66000  ? 29  VAL A HG23 1 
ATOM   582  N  N    . CYS A 1 30  ? 3.26200   -26.19700 -6.83000  1.000 15.39000  ? 30  CYS A N    1 
ATOM   583  C  CA   . CYS A 1 30  ? 2.13900   -27.10500 -6.95000  1.000 16.31000  ? 30  CYS A CA   1 
ATOM   584  C  C    . CYS A 1 30  ? 1.03000   -26.73000 -5.97000  1.000 17.16000  ? 30  CYS A C    1 
ATOM   585  O  O    . CYS A 1 30  ? -0.14600  -26.70700 -6.33700  1.000 16.28000  ? 30  CYS A O    1 
ATOM   586  C  CB   . CYS A 1 30  ? 2.65800   -28.53400 -6.70300  1.000 17.74000  ? 30  CYS A CB   1 
ATOM   587  S  SG   . CYS A 1 30  ? 1.41100   -29.81400 -6.89400  1.000 17.94000  ? 30  CYS A SG   1 
ATOM   588  H  H    . CYS A 1 30  ? 3.99800   -26.58000 -6.60500  1.000 18.49000  ? 30  CYS A H    1 
ATOM   589  H  HA   . CYS A 1 30  ? 1.75300   -27.06500 -7.83900  1.000 19.59000  ? 30  CYS A HA   1 
ATOM   590  H  HB2  . CYS A 1 30  ? 3.37000   -28.71900 -7.33500  1.000 21.31000  ? 30  CYS A HB2  1 
ATOM   591  H  HB3  . CYS A 1 30  ? 2.99800   -28.58700 -5.79600  1.000 21.31000  ? 30  CYS A HB3  1 
ATOM   592  N  N    . ALA A 1 31  ? 1.39900   -26.43000 -4.73400  1.000 15.35000  ? 31  ALA A N    1 
ATOM   593  C  CA   . ALA A 1 31  ? 0.38200   -26.05100 -3.75400  1.000 15.68000  ? 31  ALA A CA   1 
ATOM   594  C  C    . ALA A 1 31  ? -0.34900  -24.79400 -4.20500  1.000 16.19000  ? 31  ALA A C    1 
ATOM   595  O  O    . ALA A 1 31  ? -1.58900  -24.72800 -4.12900  1.000 17.19000  ? 31  ALA A O    1 
ATOM   596  C  CB   . ALA A 1 31  ? 1.00400   -25.81900 -2.38600  1.000 16.49000  ? 31  ALA A CB   1 
ATOM   597  H  H    . ALA A 1 31  ? 2.20700   -26.43600 -4.44000  1.000 18.44000  ? 31  ALA A H    1 
ATOM   598  H  HA   . ALA A 1 31  ? -0.25100  -26.78200 -3.67200  1.000 18.83000  ? 31  ALA A HA   1 
ATOM   599  H  HB1  . ALA A 1 31  ? 0.30300   -25.59700 -1.75400  1.000 19.81000  ? 31  ALA A HB1  1 
ATOM   600  H  HB2  . ALA A 1 31  ? 1.45900   -26.62800 -2.10500  1.000 19.81000  ? 31  ALA A HB2  1 
ATOM   601  H  HB3  . ALA A 1 31  ? 1.63800   -25.08700 -2.44700  1.000 19.81000  ? 31  ALA A HB3  1 
ATOM   602  N  N    . ALA A 1 32  ? 0.39200   -23.79000 -4.68400  1.000 16.52000  ? 32  ALA A N    1 
ATOM   603  C  CA   . ALA A 1 32  ? -0.24400  -22.54100 -5.10500  1.000 14.72000  ? 32  ALA A CA   1 
ATOM   604  C  C    . ALA A 1 32  ? -1.17100  -22.76600 -6.29300  1.000 16.13000  ? 32  ALA A C    1 
ATOM   605  O  O    . ALA A 1 32  ? -2.23900  -22.13800 -6.39100  1.000 17.92000  ? 32  ALA A O    1 
ATOM   606  C  CB   . ALA A 1 32  ? 0.82800   -21.50400 -5.43500  1.000 16.75000  ? 32  ALA A CB   1 
ATOM   607  H  H    . ALA A 1 32  ? 1.24700   -23.80700 -4.77400  1.000 19.85000  ? 32  ALA A H    1 
ATOM   608  H  HA   . ALA A 1 32  ? -0.78200  -22.19500 -4.37600  1.000 17.68000  ? 32  ALA A HA   1 
ATOM   609  H  HB1  . ALA A 1 32  ? 0.41100   -20.74600 -5.87400  1.000 20.13000  ? 32  ALA A HB1  1 
ATOM   610  H  HB2  . ALA A 1 32  ? 1.25300   -21.21700 -4.61200  1.000 20.13000  ? 32  ALA A HB2  1 
ATOM   611  H  HB3  . ALA A 1 32  ? 1.48600   -21.90600 -6.02400  1.000 20.13000  ? 32  ALA A HB3  1 
ATOM   612  N  N    . LYS A 1 33  ? -0.77400  -23.61200 -7.23100  1.000 16.32000  ? 33  LYS A N    1 
ATOM   613  C  CA   . LYS A 1 33  ? -1.65000  -23.87500 -8.37200  1.000 15.32000  ? 33  LYS A CA   1 
ATOM   614  C  C    . LYS A 1 33  ? -3.00900  -24.40600 -7.92400  1.000 16.24000  ? 33  LYS A C    1 
ATOM   615  O  O    . LYS A 1 33  ? -4.06500  -23.91600 -8.35400  1.000 18.19000  ? 33  LYS A O    1 
ATOM   616  C  CB   . LYS A 1 33  ? -1.01600  -24.91800 -9.29400  1.000 20.84000  ? 33  LYS A CB   1 
ATOM   617  C  CG   . LYS A 1 33  ? -1.92900  -25.40200 -10.45600 1.000 22.38000  ? 33  LYS A CG   1 
ATOM   618  C  CD   . LYS A 1 33  ? -2.09900  -24.34500 -11.50900 1.000 28.00000  ? 33  LYS A CD   1 
ATOM   619  C  CE   . LYS A 1 33  ? -2.97300  -24.83400 -12.66500 1.000 46.24000  ? 33  LYS A CE   1 
ATOM   620  N  NZ   . LYS A 1 33  ? -3.19900  -23.75700 -13.66900 1.000 46.98000  ? 33  LYS A NZ   1 
ATOM   621  H  H    . LYS A 1 33  ? -0.02700  -24.03700 -7.23500  1.000 19.60000  ? 33  LYS A H    1 
ATOM   622  H  HA   . LYS A 1 33  ? -1.76700  -23.03800 -8.84800  1.000 18.41000  ? 33  LYS A HA   1 
ATOM   623  H  HB2  . LYS A 1 33  ? -0.21800  -24.53500 -9.69000  1.000 25.03000  ? 33  LYS A HB2  1 
ATOM   624  H  HB3  . LYS A 1 33  ? -0.78200  -25.69600 -8.76400  1.000 25.03000  ? 33  LYS A HB3  1 
ATOM   625  H  HG2  . LYS A 1 33  ? -1.53100  -26.18300 -10.87200 1.000 26.87000  ? 33  LYS A HG2  1 
ATOM   626  H  HG3  . LYS A 1 33  ? -2.80500  -25.62300 -10.10400 1.000 26.87000  ? 33  LYS A HG3  1 
ATOM   627  H  HD2  . LYS A 1 33  ? -2.52300  -23.56700 -11.11600 1.000 33.62000  ? 33  LYS A HD2  1 
ATOM   628  H  HD3  . LYS A 1 33  ? -1.23000  -24.10500 -11.86600 1.000 33.62000  ? 33  LYS A HD3  1 
ATOM   629  H  HE2  . LYS A 1 33  ? -2.53400  -25.57700 -13.10700 1.000 55.51000  ? 33  LYS A HE2  1 
ATOM   630  H  HE3  . LYS A 1 33  ? -3.83500  -25.11600 -12.31900 1.000 55.51000  ? 33  LYS A HE3  1 
ATOM   631  H  HZ1  . LYS A 1 33  ? -3.75800  -23.14700 -13.34100 1.000 56.39000  ? 33  LYS A HZ1  1 
ATOM   632  H  HZ2  . LYS A 1 33  ? -2.42800  -23.36300 -13.87200 1.000 56.39000  ? 33  LYS A HZ2  1 
ATOM   633  H  HZ3  . LYS A 1 33  ? -3.55100  -24.10200 -14.41100 1.000 56.39000  ? 33  LYS A HZ3  1 
ATOM   634  N  N    . PHE A 1 34  ? -3.01100  -25.40200 -7.04000  1.000 15.28000  ? 34  PHE A N    1 
ATOM   635  C  CA   . PHE A 1 34  ? -4.27300  -26.01100 -6.67700  1.000 16.85000  ? 34  PHE A CA   1 
ATOM   636  C  C    . PHE A 1 34  ? -4.99900  -25.26900 -5.57500  1.000 17.43000  ? 34  PHE A C    1 
ATOM   637  O  O    . PHE A 1 34  ? -6.22400  -25.44200 -5.45700  1.000 22.76000  ? 34  PHE A O    1 
ATOM   638  C  CB   . PHE A 1 34  ? -4.06500  -27.48000 -6.33400  1.000 17.73000  ? 34  PHE A CB   1 
ATOM   639  C  CG   . PHE A 1 34  ? -3.58600  -28.28500 -7.51800  1.000 17.35000  ? 34  PHE A CG   1 
ATOM   640  C  CD1  . PHE A 1 34  ? -4.31900  -28.31300 -8.66800  1.000 19.78000  ? 34  PHE A CD1  1 
ATOM   641  C  CD2  . PHE A 1 34  ? -2.38600  -28.95000 -7.48800  1.000 21.18000  ? 34  PHE A CD2  1 
ATOM   642  C  CE1  . PHE A 1 34  ? -3.88400  -29.03600 -9.75600  1.000 22.66000  ? 34  PHE A CE1  1 
ATOM   643  C  CE2  . PHE A 1 34  ? -1.95300  -29.66200 -8.59000  1.000 28.08000  ? 34  PHE A CE2  1 
ATOM   644  C  CZ   . PHE A 1 34  ? -2.69200  -29.68900 -9.70300  1.000 24.27000  ? 34  PHE A CZ   1 
ATOM   645  H  H    . PHE A 1 34  ? -2.31500  -25.72800 -6.65400  1.000 18.36000  ? 34  PHE A H    1 
ATOM   646  H  HA   . PHE A 1 34  ? -4.86900  -25.99100 -7.44200  1.000 20.25000  ? 34  PHE A HA   1 
ATOM   647  H  HB2  . PHE A 1 34  ? -3.40000  -27.55000 -5.63100  1.000 21.29000  ? 34  PHE A HB2  1 
ATOM   648  H  HB3  . PHE A 1 34  ? -4.90700  -27.85700 -6.03200  1.000 21.29000  ? 34  PHE A HB3  1 
ATOM   649  H  HD1  . PHE A 1 34  ? -5.11900  -27.84100 -8.71700  1.000 23.75000  ? 34  PHE A HD1  1 
ATOM   650  H  HD2  . PHE A 1 34  ? -1.86100  -28.92100 -6.72100  1.000 25.43000  ? 34  PHE A HD2  1 
ATOM   651  H  HE1  . PHE A 1 34  ? -4.40400  -29.07700 -10.52600 1.000 27.21000  ? 34  PHE A HE1  1 
ATOM   652  H  HE2  . PHE A 1 34  ? -1.14600  -30.12400 -8.55700  1.000 33.71000  ? 34  PHE A HE2  1 
ATOM   653  H  HZ   . PHE A 1 34  ? -2.39000  -30.15800 -10.44700 1.000 29.14000  ? 34  PHE A HZ   1 
ATOM   654  N  N    . GLU A 1 35  ? -4.32000  -24.42500 -4.80400  1.000 16.10000  ? 35  GLU A N    1 
ATOM   655  C  CA   . GLU A 1 35  ? -5.03400  -23.61100 -3.81700  1.000 16.20000  ? 35  GLU A CA   1 
ATOM   656  C  C    . GLU A 1 35  ? -5.70300  -22.40200 -4.46000  1.000 17.49000  ? 35  GLU A C    1 
ATOM   657  O  O    . GLU A 1 35  ? -6.83300  -22.05600 -4.10400  1.000 18.91000  ? 35  GLU A O    1 
ATOM   658  C  CB   . GLU A 1 35  ? -4.07100  -23.15100 -2.73600  1.000 16.41000  ? 35  GLU A CB   1 
ATOM   659  C  CG   . GLU A 1 35  ? -3.56900  -24.26100 -1.83900  1.000 15.90000  ? 35  GLU A CG   1 
ATOM   660  C  CD   . GLU A 1 35  ? -4.59700  -24.78300 -0.87200  1.000 19.27000  ? 35  GLU A CD   1 
ATOM   661  O  OE1  . GLU A 1 35  ? -5.75200  -24.29200 -0.88100  1.000 22.13000  ? 35  GLU A OE1  1 
ATOM   662  O  OE2  . GLU A 1 35  ? -4.27700  -25.75600 -0.14700  1.000 21.25000  ? 35  GLU A OE2  1 
ATOM   663  H  H    . GLU A 1 35  ? -3.46900  -24.30500 -4.82900  1.000 19.34000  ? 35  GLU A H    1 
ATOM   664  H  HA   . GLU A 1 35  ? -5.72300  -24.15700 -3.40800  1.000 19.46000  ? 35  GLU A HA   1 
ATOM   665  H  HB2  . GLU A 1 35  ? -3.29900  -22.74400 -3.16100  1.000 19.71000  ? 35  GLU A HB2  1 
ATOM   666  H  HB3  . GLU A 1 35  ? -4.52200  -22.50000 -2.17500  1.000 19.71000  ? 35  GLU A HB3  1 
ATOM   667  H  HG2  . GLU A 1 35  ? -3.28400  -25.00400 -2.39300  1.000 19.11000  ? 35  GLU A HG2  1 
ATOM   668  H  HG3  . GLU A 1 35  ? -2.82100  -23.92700 -1.32000  1.000 19.11000  ? 35  GLU A HG3  1 
ATOM   669  N  N    . SER A 1 36  ? -5.03400  -21.72900 -5.39100  1.000 16.41000  ? 36  SER A N    1 
ATOM   670  C  CA   . SER A 1 36  ? -5.49500  -20.42600 -5.86800  1.000 17.66000  ? 36  SER A CA   1 
ATOM   671  C  C    . SER A 1 36  ? -5.43700  -20.24900 -7.37900  1.000 17.29000  ? 36  SER A C    1 
ATOM   672  O  O    . SER A 1 36  ? -5.79100  -19.16500 -7.85400  1.000 19.16000  ? 36  SER A O    1 
ATOM   673  C  CB   . SER A 1 36  ? -4.62700  -19.32800 -5.23300  1.000 19.43000  ? 36  SER A CB   1 
ATOM   674  O  OG   . SER A 1 36  ? -3.30500  -19.35600 -5.77400  1.000 17.22000  ? 36  SER A OG   1 
ATOM   675  H  H    . SER A 1 36  ? -4.30900  -22.00300 -5.76300  1.000 19.71000  ? 36  SER A H    1 
ATOM   676  H  HA   . SER A 1 36  ? -6.42100  -20.31700 -5.60000  1.000 21.22000  ? 36  SER A HA   1 
ATOM   677  H  HB2  . SER A 1 36  ? -5.02600  -18.46400 -5.41700  1.000 23.34000  ? 36  SER A HB2  1 
ATOM   678  H  HB3  . SER A 1 36  ? -4.58000  -19.47500 -4.27600  1.000 23.34000  ? 36  SER A HB3  1 
ATOM   679  H  HG   . SER A 1 36  ? -2.83600  -19.91400 -5.35700  1.000 20.69000  ? 36  SER A HG   1 
ATOM   680  N  N    . ASN A 1 37  ? -4.96700  -21.23900 -8.13800  1.000 16.72000  ? 37  ASN A N    1 
ATOM   681  C  CA   . ASN A 1 37  ? -4.70500  -21.06900 -9.56600  1.000 20.47000  ? 37  ASN A CA   1 
ATOM   682  C  C    . ASN A 1 37  ? -3.77300  -19.88800 -9.80800  1.000 17.02000  ? 37  ASN A C    1 
ATOM   683  O  O    . ASN A 1 37  ? -3.85700  -19.18900 -10.82100 1.000 20.59000  ? 37  ASN A O    1 
ATOM   684  C  CB   . ASN A 1 37  ? -5.98700  -20.94600 -10.38800 1.000 21.28000  ? 37  ASN A CB   1 
ATOM   685  C  CG   . ASN A 1 37  ? -5.83000  -21.48900 -11.77600 1.000 33.95000  ? 37  ASN A CG   1 
ATOM   686  O  OD1  . ASN A 1 37  ? -4.84400  -22.14300 -12.09100 1.000 30.67000  ? 37  ASN A OD1  1 
ATOM   687  N  ND2  . ASN A 1 37  ? -6.81100  -21.21900 -12.62600 1.000 44.84000  ? 37  ASN A ND2  1 
ATOM   688  H  H    . ASN A 1 37  ? -4.79200  -22.02800 -7.84600  1.000 20.09000  ? 37  ASN A H    1 
ATOM   689  H  HA   . ASN A 1 37  ? -4.25800  -21.86900 -9.88500  1.000 24.59000  ? 37  ASN A HA   1 
ATOM   690  H  HB2  . ASN A 1 37  ? -6.69500  -21.44200 -9.94800  1.000 25.55000  ? 37  ASN A HB2  1 
ATOM   691  H  HB3  . ASN A 1 37  ? -6.23200  -20.01000 -10.45700 1.000 25.55000  ? 37  ASN A HB3  1 
ATOM   692  H  HD21 . ASN A 1 37  ? -7.48800  -20.75500 -12.36900 1.000 53.82000  ? 37  ASN A HD21 1 
ATOM   693  H  HD22 . ASN A 1 37  ? -6.77000  -21.50800 -13.43500 1.000 53.82000  ? 37  ASN A HD22 1 
ATOM   694  N  N    . PHE A 1 38  ? -2.85500  -19.65000 -8.88400  1.000 16.57000  ? 38  PHE A N    1 
ATOM   695  C  CA   . PHE A 1 38  ? -1.82600  -18.61100 -8.96500  1.000 17.37000  ? 38  PHE A CA   1 
ATOM   696  C  C    . PHE A 1 38  ? -2.37700  -17.19300 -8.87900  1.000 16.66000  ? 38  PHE A C    1 
ATOM   697  O  O    . PHE A 1 38  ? -1.71200  -16.24700 -9.27800  1.000 18.52000  ? 38  PHE A O    1 
ATOM   698  C  CB   . PHE A 1 38  ? -0.95300  -18.71000 -10.22900 1.000 18.60000  ? 38  PHE A CB   1 
ATOM   699  C  CG   . PHE A 1 38  ? -0.20800  -20.01900 -10.42300 1.000 18.85000  ? 38  PHE A CG   1 
ATOM   700  C  CD1  . PHE A 1 38  ? 0.33800   -20.72600 -9.37500  1.000 19.11000  ? 38  PHE A CD1  1 
ATOM   701  C  CD2  . PHE A 1 38  ? -0.00700  -20.49200 -11.70200 1.000 22.09000  ? 38  PHE A CD2  1 
ATOM   702  C  CE1  . PHE A 1 38  ? 1.06300   -21.89500 -9.60500  1.000 20.85000  ? 38  PHE A CE1  1 
ATOM   703  C  CE2  . PHE A 1 38  ? 0.69300   -21.67200 -11.93900 1.000 23.19000  ? 38  PHE A CE2  1 
ATOM   704  C  CZ   . PHE A 1 38  ? 1.22800   -22.35700 -10.89000 1.000 20.56000  ? 38  PHE A CZ   1 
ATOM   705  H  H    . PHE A 1 38  ? -2.80100  -20.10200 -8.15500  1.000 19.90000  ? 38  PHE A H    1 
ATOM   706  H  HA   . PHE A 1 38  ? -1.25800  -18.76500 -8.19500  1.000 20.86000  ? 38  PHE A HA   1 
ATOM   707  H  HB2  . PHE A 1 38  ? -1.52600  -18.58900 -11.00300 1.000 22.35000  ? 38  PHE A HB2  1 
ATOM   708  H  HB3  . PHE A 1 38  ? -0.28900  -18.00500 -10.19400 1.000 22.35000  ? 38  PHE A HB3  1 
ATOM   709  H  HD1  . PHE A 1 38  ? 0.22200   -20.42000 -8.50500  1.000 22.95000  ? 38  PHE A HD1  1 
ATOM   710  H  HD2  . PHE A 1 38  ? -0.34700  -20.01200 -12.42300 1.000 26.53000  ? 38  PHE A HD2  1 
ATOM   711  H  HE1  . PHE A 1 38  ? 1.43300   -22.36100 -8.89000  1.000 25.04000  ? 38  PHE A HE1  1 
ATOM   712  H  HE2  . PHE A 1 38  ? 0.79600   -21.99000 -12.80700 1.000 27.85000  ? 38  PHE A HE2  1 
ATOM   713  H  HZ   . PHE A 1 38  ? 1.70600   -23.14000 -11.04300 1.000 24.69000  ? 38  PHE A HZ   1 
ATOM   714  N  N    . ASN A 1 39  ? -3.55900  -17.03000 -8.30900  1.000 17.41000  ? 39  ASN A N    1 
ATOM   715  C  CA   . ASN A 1 39  ? -4.23400  -15.73000 -8.21400  1.000 17.33000  ? 39  ASN A CA   1 
ATOM   716  C  C    . ASN A 1 39  ? -4.11600  -15.19100 -6.79800  1.000 15.99000  ? 39  ASN A C    1 
ATOM   717  O  O    . ASN A 1 39  ? -4.64700  -15.80000 -5.85400  1.000 17.87000  ? 39  ASN A O    1 
ATOM   718  C  CB   . ASN A 1 39  ? -5.68700  -15.91300 -8.60000  1.000 18.01000  ? 39  ASN A CB   1 
ATOM   719  C  CG   . ASN A 1 39  ? -6.48300  -14.63500 -8.57300  1.000 18.09000  ? 39  ASN A CG   1 
ATOM   720  O  OD1  . ASN A 1 39  ? -5.98500  -13.55600 -8.35400  1.000 18.91000  ? 39  ASN A OD1  1 
ATOM   721  N  ND2  . ASN A 1 39  ? -7.75400  -14.78400 -8.83800  1.000 22.88000  ? 39  ASN A ND2  1 
ATOM   722  H  H    . ASN A 1 39  ? -4.01000  -17.67200 -7.95800  1.000 20.91000  ? 39  ASN A H    1 
ATOM   723  H  HA   . ASN A 1 39  ? -3.81300  -15.08400 -8.80200  1.000 20.82000  ? 39  ASN A HA   1 
ATOM   724  H  HB2  . ASN A 1 39  ? -5.72900  -16.27000 -9.50100  1.000 21.63000  ? 39  ASN A HB2  1 
ATOM   725  H  HB3  . ASN A 1 39  ? -6.09900  -16.53300 -7.97800  1.000 21.63000  ? 39  ASN A HB3  1 
ATOM   726  H  HD21 . ASN A 1 39  ? -8.27500  -14.10000 -8.84200  1.000 27.48000  ? 39  ASN A HD21 1 
ATOM   727  H  HD22 . ASN A 1 39  ? -8.06900  -15.56600 -9.00800  1.000 27.48000  ? 39  ASN A HD22 1 
ATOM   728  N  N    . THR A 1 40  ? -3.44400  -14.05000 -6.64100  1.000 16.50000  ? 40  THR A N    1 
ATOM   729  C  CA   . THR A 1 40  ? -3.27200  -13.47900 -5.31300  1.000 17.27000  ? 40  THR A CA   1 
ATOM   730  C  C    . THR A 1 40  ? -4.60500  -13.04700 -4.68700  1.000 17.07000  ? 40  THR A C    1 
ATOM   731  O  O    . THR A 1 40  ? -4.66200  -12.92200 -3.46700  1.000 18.15000  ? 40  THR A O    1 
ATOM   732  C  CB   . THR A 1 40  ? -2.29500  -12.30200 -5.27500  1.000 17.48000  ? 40  THR A CB   1 
ATOM   733  O  OG1  . THR A 1 40  ? -2.87700  -11.22200 -5.99700  1.000 19.48000  ? 40  THR A OG1  1 
ATOM   734  C  CG2  . THR A 1 40  ? -0.90600  -12.65800 -5.84700  1.000 19.77000  ? 40  THR A CG2  1 
ATOM   735  H  H    . THR A 1 40  ? -3.08400  -13.59800 -7.27800  1.000 19.82000  ? 40  THR A H    1 
ATOM   736  H  HA   . THR A 1 40  ? -2.86900  -14.17800 -4.77500  1.000 20.75000  ? 40  THR A HA   1 
ATOM   737  H  HB   . THR A 1 40  ? -2.13400  -12.04500 -4.35300  1.000 20.99000  ? 40  THR A HB   1 
ATOM   738  H  HG1  . THR A 1 40  ? -2.40800  -10.53100 -5.90800  1.000 23.40000  ? 40  THR A HG1  1 
ATOM   739  H  HG21 . THR A 1 40  ? -0.31800  -11.88800 -5.79400  1.000 23.75000  ? 40  THR A HG21 1 
ATOM   740  H  HG22 . THR A 1 40  ? -0.51600  -13.38700 -5.34100  1.000 23.75000  ? 40  THR A HG22 1 
ATOM   741  H  HG23 . THR A 1 40  ? -0.98900  -12.92700 -6.77500  1.000 23.75000  ? 40  THR A HG23 1 
ATOM   742  N  N    A GLN A 1 41  ? -5.63300  -12.81300 -5.48400  0.470 17.04000  ? 41  GLN A N    1 
ATOM   743  N  N    B GLN A 1 41  ? -5.65300  -12.80900 -5.47200  0.530 17.13000  ? 41  GLN A N    1 
ATOM   744  C  CA   A GLN A 1 41  ? -6.88000  -12.28500 -4.95100  0.470 15.14000  ? 41  GLN A CA   1 
ATOM   745  C  CA   B GLN A 1 41  ? -6.92000  -12.30600 -4.93300  0.530 15.04000  ? 41  GLN A CA   1 
ATOM   746  C  C    A GLN A 1 41  ? -7.83000  -13.35500 -4.44400  0.470 17.60000  ? 41  GLN A C    1 
ATOM   747  C  C    B GLN A 1 41  ? -7.92900  -13.40700 -4.64000  0.530 19.02000  ? 41  GLN A C    1 
ATOM   748  O  O    A GLN A 1 41  ? -8.85200  -12.99800 -3.85500  0.470 15.93000  ? 41  GLN A O    1 
ATOM   749  O  O    B GLN A 1 41  ? -9.12700  -13.14200 -4.44600  0.530 18.95000  ? 41  GLN A O    1 
ATOM   750  C  CB   A GLN A 1 41  ? -7.59500  -11.42000 -5.99400  0.470 18.41000  ? 41  GLN A CB   1 
ATOM   751  C  CB   B GLN A 1 41  ? -7.52400  -11.27200 -5.88000  0.530 16.44000  ? 41  GLN A CB   1 
ATOM   752  C  CG   A GLN A 1 41  ? -6.81200  -10.20700 -6.35900  0.470 17.05000  ? 41  GLN A CG   1 
ATOM   753  C  CG   B GLN A 1 41  ? -6.62000  -10.14500 -6.18600  0.530 18.46000  ? 41  GLN A CG   1 
ATOM   754  C  CD   A GLN A 1 41  ? -7.63700  -9.13300  -7.04100  0.470 19.59000  ? 41  GLN A CD   1 
ATOM   755  C  CD   B GLN A 1 41  ? -7.34300  -8.97700  -6.82100  0.530 19.32000  ? 41  GLN A CD   1 
ATOM   756  O  OE1  A GLN A 1 41  ? -8.62600  -8.63100  -6.49400  0.470 15.90000  ? 41  GLN A OE1  1 
ATOM   757  O  OE1  B GLN A 1 41  ? -7.83000  -8.08500  -6.12800  0.530 20.55000  ? 41  GLN A OE1  1 
ATOM   758  N  NE2  A GLN A 1 41  ? -7.21000  -8.75100  -8.23900  0.470 19.54000  ? 41  GLN A NE2  1 
ATOM   759  N  NE2  B GLN A 1 41  ? -7.45400  -9.00200  -8.15500  0.530 20.74000  ? 41  GLN A NE2  1 
ATOM   760  H  H    A GLN A 1 41  ? -5.63500  -12.95100 -6.33300  0.470 20.47000  ? 41  GLN A H    1 
ATOM   761  H  H    B GLN A 1 41  ? -5.65700  -12.93100 -6.32400  0.530 20.58000  ? 41  GLN A H    1 
ATOM   762  H  HA   A GLN A 1 41  ? -6.65700  -11.71500 -4.19900  0.470 18.19000  ? 41  GLN A HA   1 
ATOM   763  H  HA   B GLN A 1 41  ? -6.73200  -11.86200 -4.09100  0.530 18.07000  ? 41  GLN A HA   1 
ATOM   764  H  HB2  A GLN A 1 41  ? -7.73300  -11.94300 -6.79900  0.470 22.11000  ? 41  GLN A HB2  1 
ATOM   765  H  HB2  B GLN A 1 41  ? -7.74600  -11.70900 -6.71800  0.530 19.75000  ? 41  GLN A HB2  1 
ATOM   766  H  HB3  A GLN A 1 41  ? -8.44900  -11.13100 -5.63600  0.470 22.11000  ? 41  GLN A HB3  1 
ATOM   767  H  HB3  B GLN A 1 41  ? -8.32500  -10.90800 -5.47400  0.530 19.75000  ? 41  GLN A HB3  1 
ATOM   768  H  HG2  A GLN A 1 41  ? -6.43500  -9.82300  -5.55200  0.470 20.48000  ? 41  GLN A HG2  1 
ATOM   769  H  HG2  B GLN A 1 41  ? -6.21200  -9.83400  -5.36300  0.530 22.17000  ? 41  GLN A HG2  1 
ATOM   770  H  HG3  A GLN A 1 41  ? -6.10100  -10.46500 -6.96700  0.470 20.48000  ? 41  GLN A HG3  1 
ATOM   771  H  HG3  B GLN A 1 41  ? -5.93500  -10.44600 -6.80300  0.530 22.17000  ? 41  GLN A HG3  1 
ATOM   772  H  HE21 A GLN A 1 41  ? -7.63700  -8.14500  -8.67500  0.470 23.46000  ? 41  GLN A HE21 1 
ATOM   773  H  HE21 B GLN A 1 41  ? -7.85600  -8.36100  -8.56500  0.530 24.91000  ? 41  GLN A HE21 1 
ATOM   774  H  HE22 A GLN A 1 41  ? -6.50500  -9.10900  -8.57900  0.470 23.46000  ? 41  GLN A HE22 1 
ATOM   775  H  HE22 B GLN A 1 41  ? -7.12300  -9.65800  -8.60200  0.530 24.91000  ? 41  GLN A HE22 1 
ATOM   776  N  N    . ALA A 1 42  ? -7.47400  -14.64100 -4.57700  1.000 16.92000  ? 42  ALA A N    1 
ATOM   777  C  CA   . ALA A 1 42  ? -8.38400  -15.74200 -4.31600  1.000 16.17000  ? 42  ALA A CA   1 
ATOM   778  C  C    . ALA A 1 42  ? -8.84900  -15.71100 -2.86100  1.000 16.19000  ? 42  ALA A C    1 
ATOM   779  O  O    . ALA A 1 42  ? -8.05200  -15.55200 -1.93800  1.000 16.69000  ? 42  ALA A O    1 
ATOM   780  C  CB   . ALA A 1 42  ? -7.66000  -17.05300 -4.57800  1.000 19.49000  ? 42  ALA A CB   1 
ATOM   781  H  H    . ALA A 1 42  ? -6.65100  -14.86600 -4.68000  1.000 20.32000  ? 42  ALA A H    1 
ATOM   782  H  HA   . ALA A 1 42  ? -9.16100  -15.67600 -4.89300  1.000 19.42000  ? 42  ALA A HA   1 
ATOM   783  H  HB1  . ALA A 1 42  ? -8.27800  -17.78800 -4.44400  1.000 23.41000  ? 42  ALA A HB1  1 
ATOM   784  H  HB2  . ALA A 1 42  ? -7.33500  -17.05700 -5.49300  1.000 23.41000  ? 42  ALA A HB2  1 
ATOM   785  H  HB3  . ALA A 1 42  ? -6.91400  -17.13100 -3.96300  1.000 23.41000  ? 42  ALA A HB3  1 
ATOM   786  N  N    . THR A 1 43  ? -10.14500 -15.91500 -2.65800  1.000 16.55000  ? 43  THR A N    1 
ATOM   787  C  CA   . THR A 1 43  ? -10.72900 -16.07400 -1.33300  1.000 16.15000  ? 43  THR A CA   1 
ATOM   788  C  C    . THR A 1 43  ? -11.72500 -17.21700 -1.36700  1.000 18.34000  ? 43  THR A C    1 
ATOM   789  O  O    . THR A 1 43  ? -12.39900 -17.44300 -2.37500  1.000 22.38000  ? 43  THR A O    1 
ATOM   790  C  CB   . THR A 1 43  ? -11.42100 -14.82000 -0.82200  1.000 18.41000  ? 43  THR A CB   1 
ATOM   791  O  OG1  . THR A 1 43  ? -12.47200 -14.48200 -1.73200  1.000 19.49000  ? 43  THR A OG1  1 
ATOM   792  C  CG2  . THR A 1 43  ? -10.45300 -13.66600 -0.68200  1.000 20.21000  ? 43  THR A CG2  1 
ATOM   793  H  H    . THR A 1 43  ? -10.72400 -15.96600 -3.29200  1.000 19.88000  ? 43  THR A H    1 
ATOM   794  H  HA   . THR A 1 43  ? -10.01500 -16.28400 -0.71000  1.000 19.40000  ? 43  THR A HA   1 
ATOM   795  H  HB   . THR A 1 43  ? -11.78800 -14.98100 0.06200   1.000 22.11000  ? 43  THR A HB   1 
ATOM   796  H  HG1  . THR A 1 43  ? -12.32300 -13.73100 -2.07700  1.000 23.41000  ? 43  THR A HG1  1 
ATOM   797  H  HG21 . THR A 1 43  ? -10.89300 -12.91400 -0.25500  1.000 24.27000  ? 43  THR A HG21 1 
ATOM   798  H  HG22 . THR A 1 43  ? -9.69300  -13.93400 -0.14200  1.000 24.27000  ? 43  THR A HG22 1 
ATOM   799  H  HG23 . THR A 1 43  ? -10.13700 -13.39100 -1.55600  1.000 24.27000  ? 43  THR A HG23 1 
ATOM   800  N  N    A ASN A 1 44  ? -11.84500 -17.93100 -0.24700  0.500 18.47000  ? 44  ASN A N    1 
ATOM   801  N  N    B ASN A 1 44  ? -11.84300 -17.94500 -0.26000  0.500 18.47000  ? 44  ASN A N    1 
ATOM   802  C  CA   A ASN A 1 44  ? -12.77000 -19.05800 -0.17600  0.500 18.95000  ? 44  ASN A CA   1 
ATOM   803  C  CA   B ASN A 1 44  ? -12.87400 -18.97200 -0.14400  0.500 18.72000  ? 44  ASN A CA   1 
ATOM   804  C  C    A ASN A 1 44  ? -13.21000 -19.29300 1.25500   0.500 16.75000  ? 44  ASN A C    1 
ATOM   805  C  C    B ASN A 1 44  ? -13.34200 -19.02700 1.30000   0.500 16.61000  ? 44  ASN A C    1 
ATOM   806  O  O    A ASN A 1 44  ? -12.37000 -19.45200 2.14200   0.500 16.09000  ? 44  ASN A O    1 
ATOM   807  O  O    B ASN A 1 44  ? -12.56900 -18.76800 2.20500   0.500 16.56000  ? 44  ASN A O    1 
ATOM   808  C  CB   A ASN A 1 44  ? -12.11700 -20.32600 -0.72300  0.500 21.10000  ? 44  ASN A CB   1 
ATOM   809  C  CB   B ASN A 1 44  ? -12.36000 -20.35800 -0.55500  0.500 21.51000  ? 44  ASN A CB   1 
ATOM   810  C  CG   A ASN A 1 44  ? -12.04600 -20.32600 -2.22700  0.500 20.34000  ? 44  ASN A CG   1 
ATOM   811  C  CG   B ASN A 1 44  ? -13.43800 -21.20300 -1.22400  0.500 33.84000  ? 44  ASN A CG   1 
ATOM   812  O  OD1  A ASN A 1 44  ? -13.07200 -20.39000 -2.91900  0.500 20.22000  ? 44  ASN A OD1  1 
ATOM   813  O  OD1  B ASN A 1 44  ? -14.20100 -21.89600 -0.55700  0.500 39.63000  ? 44  ASN A OD1  1 
ATOM   814  N  ND2  A ASN A 1 44  ? -10.83700 -20.20000 -2.74800  0.500 22.13000  ? 44  ASN A ND2  1 
ATOM   815  N  ND2  B ASN A 1 44  ? -13.50500 -21.13700 -2.54800  0.500 35.82000  ? 44  ASN A ND2  1 
ATOM   816  H  H    A ASN A 1 44  ? -11.40600 -17.78300 0.47700   0.500 22.19000  ? 44  ASN A H    1 
ATOM   817  H  H    B ASN A 1 44  ? -11.34100 -17.86300 0.43400   0.500 22.18000  ? 44  ASN A H    1 
ATOM   818  H  HA   A ASN A 1 44  ? -13.55900 -18.84300 -0.69700  0.500 22.76000  ? 44  ASN A HA   1 
ATOM   819  H  HA   B ASN A 1 44  ? -13.61800 -18.73700 -0.71900  0.500 22.49000  ? 44  ASN A HA   1 
ATOM   820  H  HB2  A ASN A 1 44  ? -11.21300 -20.39300 -0.37700  0.500 25.34000  ? 44  ASN A HB2  1 
ATOM   821  H  HB2  B ASN A 1 44  ? -11.62800 -20.25200 -1.18200  0.500 25.83000  ? 44  ASN A HB2  1 
ATOM   822  H  HB3  A ASN A 1 44  ? -12.63700 -21.09700 -0.44400  0.500 25.34000  ? 44  ASN A HB3  1 
ATOM   823  H  HB3  B ASN A 1 44  ? -12.05500 -20.83100 0.23500   0.500 25.83000  ? 44  ASN A HB3  1 
ATOM   824  H  HD21 A ASN A 1 44  ? -10.15300 -20.12400 -2.23300  0.500 26.58000  ? 44  ASN A HD21 1 
ATOM   825  H  HD21 B ASN A 1 44  ? -12.95700 -20.63600 -2.98200  0.500 43.01000  ? 44  ASN A HD21 1 
ATOM   826  H  HD22 A ASN A 1 44  ? -10.73600 -20.19300 -3.60200  0.500 26.58000  ? 44  ASN A HD22 1 
ATOM   827  H  HD22 B ASN A 1 44  ? -14.09700 -21.59600 -2.97200  0.500 43.01000  ? 44  ASN A HD22 1 
ATOM   828  N  N    A ARG A 1 45  ? -14.52700 -19.33400 1.45500   0.500 20.30000  ? 45  ARG A N    1 
ATOM   829  N  N    B ARG A 1 45  ? -14.61400 -19.36200 1.50300   0.500 20.30000  ? 45  ARG A N    1 
ATOM   830  C  CA   A ARG A 1 45  ? -15.11100 -19.51500 2.77100   0.500 22.12000  ? 45  ARG A CA   1 
ATOM   831  C  CA   B ARG A 1 45  ? -15.20900 -19.42700 2.83300   0.500 21.99000  ? 45  ARG A CA   1 
ATOM   832  C  C    A ARG A 1 45  ? -15.05500 -20.97700 3.18100   0.500 24.89000  ? 45  ARG A C    1 
ATOM   833  C  C    B ARG A 1 45  ? -15.33800 -20.88100 3.26000   0.500 24.81000  ? 45  ARG A C    1 
ATOM   834  O  O    A ARG A 1 45  ? -15.11300 -21.89100 2.34800   0.500 23.55000  ? 45  ARG A O    1 
ATOM   835  O  O    B ARG A 1 45  ? -15.87300 -21.70000 2.50100   0.500 20.83000  ? 45  ARG A O    1 
ATOM   836  C  CB   A ARG A 1 45  ? -16.56900 -19.06100 2.78200   0.500 25.01000  ? 45  ARG A CB   1 
ATOM   837  C  CB   B ARG A 1 45  ? -16.59600 -18.78300 2.82700   0.500 24.31000  ? 45  ARG A CB   1 
ATOM   838  C  CG   A ARG A 1 45  ? -17.22600 -19.17800 4.15100   0.500 25.43000  ? 45  ARG A CG   1 
ATOM   839  C  CG   B ARG A 1 45  ? -17.23700 -18.69400 4.20600   0.500 28.61000  ? 45  ARG A CG   1 
ATOM   840  C  CD   A ARG A 1 45  ? -16.72100 -18.07000 5.04800   0.500 27.95000  ? 45  ARG A CD   1 
ATOM   841  C  CD   B ARG A 1 45  ? -16.76900 -17.45100 4.93500   0.500 30.12000  ? 45  ARG A CD   1 
ATOM   842  N  NE   A ARG A 1 45  ? -17.10000 -16.78200 4.48400   0.500 37.08000  ? 45  ARG A NE   1 
ATOM   843  N  NE   B ARG A 1 45  ? -17.03000 -16.25000 4.15200   0.500 40.49000  ? 45  ARG A NE   1 
ATOM   844  C  CZ   A ARG A 1 45  ? -18.01600 -15.96900 4.99300   0.500 43.52000  ? 45  ARG A CZ   1 
ATOM   845  C  CZ   B ARG A 1 45  ? -18.24000 -15.81900 3.82200   0.500 30.98000  ? 45  ARG A CZ   1 
ATOM   846  N  NH1  A ARG A 1 45  ? -18.52300 -16.16400 6.19900   0.500 38.19000  ? 45  ARG A NH1  1 
ATOM   847  N  NH1  B ARG A 1 45  ? -19.33400 -16.43200 4.24700   0.500 44.82000  ? 45  ARG A NH1  1 
ATOM   848  N  NH2  A ARG A 1 45  ? -18.42800 -14.93000 4.27300   0.500 32.96000  ? 45  ARG A NH2  1 
ATOM   849  N  NH2  B ARG A 1 45  ? -18.35700 -14.75500 3.03600   0.500 38.76000  ? 45  ARG A NH2  1 
ATOM   850  H  H    A ARG A 1 45  ? -15.11200 -19.25700 0.82900   0.500 24.38000  ? 45  ARG A H    1 
ATOM   851  H  H    B ARG A 1 45  ? -15.16300 -19.55900 0.87200   0.500 24.38000  ? 45  ARG A H    1 
ATOM   852  H  HA   A ARG A 1 45  ? -14.61300 -18.98400 3.41200   0.500 26.56000  ? 45  ARG A HA   1 
ATOM   853  H  HA   B ARG A 1 45  ? -14.64000 -18.96100 3.46500   0.500 26.41000  ? 45  ARG A HA   1 
ATOM   854  H  HB2  A ARG A 1 45  ? -16.60900 -18.13000 2.51100   0.500 30.04000  ? 45  ARG A HB2  1 
ATOM   855  H  HB2  B ARG A 1 45  ? -16.51900 -17.88100 2.47800   0.500 29.19000  ? 45  ARG A HB2  1 
ATOM   856  H  HB3  A ARG A 1 45  ? -17.07300 -19.61000 2.16100   0.500 30.04000  ? 45  ARG A HB3  1 
ATOM   857  H  HB3  B ARG A 1 45  ? -17.18200 -19.30900 2.26100   0.500 29.19000  ? 45  ARG A HB3  1 
ATOM   858  H  HG2  A ARG A 1 45  ? -18.18800 -19.09600 4.06200   0.500 30.54000  ? 45  ARG A HG2  1 
ATOM   859  H  HG2  B ARG A 1 45  ? -18.20100 -18.65200 4.11300   0.500 34.35000  ? 45  ARG A HG2  1 
ATOM   860  H  HG3  A ARG A 1 45  ? -17.00100 -20.03200 4.55200   0.500 30.54000  ? 45  ARG A HG3  1 
ATOM   861  H  HG3  B ARG A 1 45  ? -16.98700 -19.47100 4.73100   0.500 34.35000  ? 45  ARG A HG3  1 
ATOM   862  H  HD2  A ARG A 1 45  ? -17.11600 -18.15500 5.93000   0.500 33.56000  ? 45  ARG A HD2  1 
ATOM   863  H  HD2  B ARG A 1 45  ? -17.24200 -17.37500 5.77800   0.500 36.16000  ? 45  ARG A HD2  1 
ATOM   864  H  HD3  A ARG A 1 45  ? -15.75500 -18.11300 5.11200   0.500 33.56000  ? 45  ARG A HD3  1 
ATOM   865  H  HD3  B ARG A 1 45  ? -15.81400 -17.51100 5.09500   0.500 36.16000  ? 45  ARG A HD3  1 
ATOM   866  H  HE   A ARG A 1 45  ? -16.70000 -16.53000 3.76700   0.500 44.52000  ? 45  ARG A HE   1 
ATOM   867  H  HE   B ARG A 1 45  ? -16.35300 -15.79000 3.88600   0.500 48.61000  ? 45  ARG A HE   1 
ATOM   868  H  HH11 A ARG A 1 45  ? -18.25900 -16.83100 6.67300   0.500 45.84000  ? 45  ARG A HH11 1 
ATOM   869  H  HH11 B ARG A 1 45  ? -19.27000 -17.12700 4.74900   0.500 53.80000  ? 45  ARG A HH11 1 
ATOM   870  H  HH12 A ARG A 1 45  ? -19.11600 -15.62400 6.50900   0.500 45.84000  ? 45  ARG A HH12 1 
ATOM   871  H  HH12 B ARG A 1 45  ? -20.10900 -16.13500 4.02100   0.500 53.80000  ? 45  ARG A HH12 1 
ATOM   872  H  HH21 A ARG A 1 45  ? -18.10100 -14.79300 3.49000   0.500 39.57000  ? 45  ARG A HH21 1 
ATOM   873  H  HH21 B ARG A 1 45  ? -17.65200 -14.35500 2.74700   0.500 46.53000  ? 45  ARG A HH21 1 
ATOM   874  H  HH22 A ARG A 1 45  ? -19.02200 -14.39500 4.59100   0.500 39.57000  ? 45  ARG A HH22 1 
ATOM   875  H  HH22 B ARG A 1 45  ? -19.13600 -14.46600 2.81600   0.500 46.53000  ? 45  ARG A HH22 1 
ATOM   876  N  N    . ASN A 1 46  ? -14.84900 -21.18900 4.46900   1.000 24.81000  ? 46  ASN A N    1 
ATOM   877  C  CA   . ASN A 1 46  ? -14.89700 -22.53000 5.05300   1.000 25.18000  ? 46  ASN A CA   1 
ATOM   878  C  C    . ASN A 1 46  ? -16.20700 -22.74300 5.80900   1.000 23.42000  ? 46  ASN A C    1 
ATOM   879  O  O    . ASN A 1 46  ? -16.88300 -21.80000 6.20100   1.000 27.98000  ? 46  ASN A O    1 
ATOM   880  C  CB   . ASN A 1 46  ? -13.72900 -22.71200 6.02900   1.000 26.22000  ? 46  ASN A CB   1 
ATOM   881  C  CG   . ASN A 1 46  ? -12.34500 -22.48500 5.38400   1.000 24.82000  ? 46  ASN A CG   1 
ATOM   882  O  OD1  . ASN A 1 46  ? -11.50400 -21.74900 5.93400   1.000 30.65000  ? 46  ASN A OD1  1 
ATOM   883  N  ND2  . ASN A 1 46  ? -12.12500 -23.05500 4.21600   1.000 27.63000  ? 46  ASN A ND2  1 
ATOM   884  H  H    . ASN A 1 46  ? -14.47000 -20.61900 4.99000   1.000 29.80000  ? 46  ASN A H    1 
ATOM   885  H  HA   . ASN A 1 46  ? -14.84000 -23.19000 4.34400   1.000 30.23000  ? 46  ASN A HA   1 
ATOM   886  H  HB2  . ASN A 1 46  ? -13.82600 -22.07500 6.75500   1.000 31.48000  ? 46  ASN A HB2  1 
ATOM   887  H  HB3  . ASN A 1 46  ? -13.75000 -23.61700 6.37700   1.000 31.48000  ? 46  ASN A HB3  1 
ATOM   888  H  HD21 . ASN A 1 46  ? -11.36700 -22.95200 3.82400   1.000 33.17000  ? 46  ASN A HD21 1 
ATOM   889  H  HD22 . ASN A 1 46  ? -12.74000 -23.52800 3.84600   1.000 33.17000  ? 46  ASN A HD22 1 
ATOM   890  N  N    . THR A 1 47  ? -16.52200 -24.01900 6.05000   1.000 34.59000  ? 47  THR A N    1 
ATOM   891  C  CA   . THR A 1 47  ? -17.79200 -24.35800 6.68700   1.000 37.89000  ? 47  THR A CA   1 
ATOM   892  C  C    . THR A 1 47  ? -17.90200 -23.75100 8.07900   1.000 32.91000  ? 47  THR A C    1 
ATOM   893  O  O    . THR A 1 47  ? -19.00600 -23.38900 8.51700   1.000 38.27000  ? 47  THR A O    1 
ATOM   894  C  CB   . THR A 1 47  ? -17.93300 -25.87800 6.77200   1.000 41.78000  ? 47  THR A CB   1 
ATOM   895  O  OG1  . THR A 1 47  ? -16.72800 -26.45200 7.28900   1.000 44.86000  ? 47  THR A OG1  1 
ATOM   896  C  CG2  . THR A 1 47  ? -18.16100 -26.44300 5.38500   1.000 59.67000  ? 47  THR A CG2  1 
ATOM   897  H  H    . THR A 1 47  ? -16.02600 -24.69400 5.85800   1.000 41.53000  ? 47  THR A H    1 
ATOM   898  H  HA   . THR A 1 47  ? -18.51700 -24.00700 6.14700   1.000 45.49000  ? 47  THR A HA   1 
ATOM   899  H  HB   . THR A 1 47  ? -18.67900 -26.10100 7.35000   1.000 50.16000  ? 47  THR A HB   1 
ATOM   900  H  HG1  . THR A 1 47  ? -16.80300 -27.28800 7.33300   1.000 53.85000  ? 47  THR A HG1  1 
ATOM   901  H  HG21 . THR A 1 47  ? -18.25600 -27.40800 5.43100   1.000 71.62000  ? 47  THR A HG21 1 
ATOM   902  H  HG22 . THR A 1 47  ? -18.96700 -26.06500 5.00100   1.000 71.62000  ? 47  THR A HG22 1 
ATOM   903  H  HG23 . THR A 1 47  ? -17.40900 -26.22800 4.81100   1.000 71.62000  ? 47  THR A HG23 1 
ATOM   904  N  N    A ASP A 1 48  ? -16.78100 -23.61400 8.78400   0.660 30.95000  ? 48  ASP A N    1 
ATOM   905  N  N    B ASP A 1 48  ? -16.78300 -23.62000 8.78600   0.340 30.86000  ? 48  ASP A N    1 
ATOM   906  C  CA   A ASP A 1 48  ? -16.78600 -23.09100 10.14600  0.660 32.48000  ? 48  ASP A CA   1 
ATOM   907  C  CA   B ASP A 1 48  ? -16.79400 -23.09800 10.14600  0.340 32.32000  ? 48  ASP A CA   1 
ATOM   908  C  C    A ASP A 1 48  ? -16.90200 -21.57500 10.20600  0.660 30.36000  ? 48  ASP A C    1 
ATOM   909  C  C    B ASP A 1 48  ? -16.85300 -21.57500 10.20300  0.340 30.64000  ? 48  ASP A C    1 
ATOM   910  O  O    A ASP A 1 48  ? -16.89600 -21.01000 11.30500  0.660 34.61000  ? 48  ASP A O    1 
ATOM   911  O  O    B ASP A 1 48  ? -16.74100 -21.00800 11.29500  0.340 34.77000  ? 48  ASP A O    1 
ATOM   912  C  CB   A ASP A 1 48  ? -15.54400 -23.59300 10.89000  0.660 29.08000  ? 48  ASP A CB   1 
ATOM   913  C  CB   B ASP A 1 48  ? -15.57700 -23.61900 10.91600  0.340 29.47000  ? 48  ASP A CB   1 
ATOM   914  C  CG   A ASP A 1 48  ? -14.26800 -22.92600 10.43400  0.660 30.14000  ? 48  ASP A CG   1 
ATOM   915  C  CG   B ASP A 1 48  ? -14.26900 -23.13000 10.34400  0.340 30.27000  ? 48  ASP A CG   1 
ATOM   916  O  OD1  A ASP A 1 48  ? -14.30600 -22.18700 9.42400   0.660 27.24000  ? 48  ASP A OD1  1 
ATOM   917  O  OD1  B ASP A 1 48  ? -13.80500 -23.70000 9.33300   0.340 32.65000  ? 48  ASP A OD1  1 
ATOM   918  O  OD2  A ASP A 1 48  ? -13.22000 -23.17500 11.06800  0.660 31.41000  ? 48  ASP A OD2  1 
ATOM   919  O  OD2  B ASP A 1 48  ? -13.70800 -22.16900 10.90800  0.340 29.07000  ? 48  ASP A OD2  1 
ATOM   920  H  H    A ASP A 1 48  ? -15.99800 -23.81900 8.49200   0.660 37.16000  ? 48  ASP A H    1 
ATOM   921  H  H    B ASP A 1 48  ? -16.00000 -23.82800 8.49600   0.340 37.05000  ? 48  ASP A H    1 
ATOM   922  H  HA   A ASP A 1 48  ? -17.55800 -23.43500 10.62100  0.660 39.00000  ? 48  ASP A HA   1 
ATOM   923  H  HA   B ASP A 1 48  ? -17.58600 -23.42900 10.59700  0.340 38.81000  ? 48  ASP A HA   1 
ATOM   924  H  HB2  A ASP A 1 48  ? -15.65100 -23.41400 11.83800  0.660 34.92000  ? 48  ASP A HB2  1 
ATOM   925  H  HB2  B ASP A 1 48  ? -15.63300 -23.31700 11.83600  0.340 35.38000  ? 48  ASP A HB2  1 
ATOM   926  H  HB3  A ASP A 1 48  ? -15.45100 -24.54700 10.74100  0.660 34.92000  ? 48  ASP A HB3  1 
ATOM   927  H  HB3  B ASP A 1 48  ? -15.57500 -24.58800 10.88500  0.340 35.38000  ? 48  ASP A HB3  1 
ATOM   928  N  N    . GLY A 1 49  ? -17.01600 -20.89400 9.06300   1.000 29.41000  ? 49  GLY A N    1 
ATOM   929  C  CA   . GLY A 1 49  ? -17.10200 -19.45400 9.04100   1.000 29.16000  ? 49  GLY A CA   1 
ATOM   930  C  C    . GLY A 1 49  ? -15.78000 -18.73200 8.83100   1.000 26.01000  ? 49  GLY A C    1 
ATOM   931  O  O    . GLY A 1 49  ? -15.77500 -17.50300 8.66600   1.000 27.18000  ? 49  GLY A O    1 
ATOM   932  H  H    . GLY A 1 49  ? -17.04500 -21.25700 8.28400   1.000 35.31000  ? 49  GLY A H    1 
ATOM   933  H  HA2  . GLY A 1 49  ? -17.69900 -19.19100 8.32300   1.000 35.01000  ? 49  GLY A HA2  1 
ATOM   934  H  HA3  . GLY A 1 49  ? -17.47100 -19.15300 9.88600   1.000 35.01000  ? 49  GLY A HA3  1 
ATOM   935  N  N    . SER A 1 50  ? -14.66000 -19.43800 8.89200   1.000 22.71000  ? 50  SER A N    1 
ATOM   936  C  CA   . SER A 1 50  ? -13.39200 -18.82000 8.56500   1.000 21.34000  ? 50  SER A CA   1 
ATOM   937  C  C    . SER A 1 50  ? -13.25500 -18.69800 7.04700   1.000 18.61000  ? 50  SER A C    1 
ATOM   938  O  O    . SER A 1 50  ? -14.03600 -19.24400 6.29200   1.000 20.51000  ? 50  SER A O    1 
ATOM   939  C  CB   . SER A 1 50  ? -12.25200 -19.60800 9.18300   1.000 20.76000  ? 50  SER A CB   1 
ATOM   940  O  OG   . SER A 1 50  ? -12.18800 -20.88000 8.61000   1.000 21.32000  ? 50  SER A OG   1 
ATOM   941  H  H    . SER A 1 50  ? -14.61100 -20.26700 9.11800   1.000 27.27000  ? 50  SER A H    1 
ATOM   942  H  HA   . SER A 1 50  ? -13.34500 -17.92400 8.93400   1.000 25.63000  ? 50  SER A HA   1 
ATOM   943  H  HB2  . SER A 1 50  ? -11.41600 -19.14300 9.02100   1.000 24.93000  ? 50  SER A HB2  1 
ATOM   944  H  HB3  . SER A 1 50  ? -12.40300 -19.69500 10.13700  1.000 24.93000  ? 50  SER A HB3  1 
ATOM   945  H  HG   . SER A 1 50  ? -12.94200 -21.24900 8.64600   1.000 25.60000  ? 50  SER A HG   1 
ATOM   946  N  N    . THR A 1 51  ? -12.25600 -17.93700 6.62100   1.000 16.97000  ? 51  THR A N    1 
ATOM   947  C  CA   . THR A 1 51  ? -11.99800 -17.68300 5.20100   1.000 15.66000  ? 51  THR A CA   1 
ATOM   948  C  C    . THR A 1 51  ? -10.51600 -17.93400 4.91500   1.000 15.78000  ? 51  THR A C    1 
ATOM   949  O  O    . THR A 1 51  ? -9.65000  -17.64000 5.73700   1.000 15.81000  ? 51  THR A O    1 
ATOM   950  C  CB   . THR A 1 51  ? -12.40600 -16.24200 4.88000   1.000 15.83000  ? 51  THR A CB   1 
ATOM   951  O  OG1  . THR A 1 51  ? -13.80300 -16.07100 5.17300   1.000 19.14000  ? 51  THR A OG1  1 
ATOM   952  C  CG2  . THR A 1 51  ? -12.19000 -15.89500 3.43300   1.000 19.13000  ? 51  THR A CG2  1 
ATOM   953  H  H    . THR A 1 51  ? -11.69700 -17.54500 7.14400   1.000 20.39000  ? 51  THR A H    1 
ATOM   954  H  HA   . THR A 1 51  ? -12.49300 -18.28000 4.61800   1.000 18.81000  ? 51  THR A HA   1 
ATOM   955  H  HB   . THR A 1 51  ? -11.85800 -15.64700 5.41600   1.000 19.02000  ? 51  THR A HB   1 
ATOM   956  H  HG1  . THR A 1 51  ? -13.90700 -15.90700 5.99000   1.000 22.98000  ? 51  THR A HG1  1 
ATOM   957  H  HG21 . THR A 1 51  ? -12.45200 -14.97500 3.27000   1.000 22.97000  ? 51  THR A HG21 1 
ATOM   958  H  HG22 . THR A 1 51  ? -11.25400 -16.00100 3.20200   1.000 22.97000  ? 51  THR A HG22 1 
ATOM   959  H  HG23 . THR A 1 51  ? -12.72200 -16.47800 2.86900   1.000 22.97000  ? 51  THR A HG23 1 
ATOM   960  N  N    A ASP A 1 52  ? -10.22600 -18.42900 3.71400   0.590 16.07000  ? 52  ASP A N    1 
ATOM   961  N  N    B ASP A 1 52  ? -10.24000 -18.44100 3.71600   0.410 16.11000  ? 52  ASP A N    1 
ATOM   962  C  CA   A ASP A 1 52  ? -8.86600  -18.62200 3.22200   0.590 16.55000  ? 52  ASP A CA   1 
ATOM   963  C  CA   B ASP A 1 52  ? -8.89000  -18.62300 3.19700   0.410 16.51000  ? 52  ASP A CA   1 
ATOM   964  C  C    A ASP A 1 52  ? -8.51000  -17.55600 2.20100   0.590 14.69000  ? 52  ASP A C    1 
ATOM   965  C  C    B ASP A 1 52  ? -8.54000  -17.47600 2.25400   0.410 14.88000  ? 52  ASP A C    1 
ATOM   966  O  O    A ASP A 1 52  ? -9.31900  -17.25700 1.30800   0.590 16.14000  ? 52  ASP A O    1 
ATOM   967  O  O    B ASP A 1 52  ? -9.39200  -17.00900 1.49000   0.410 16.67000  ? 52  ASP A O    1 
ATOM   968  C  CB   A ASP A 1 52  ? -8.74400  -19.99100 2.55300   0.590 17.68000  ? 52  ASP A CB   1 
ATOM   969  C  CB   B ASP A 1 52  ? -8.80100  -19.95000 2.43400   0.410 17.29000  ? 52  ASP A CB   1 
ATOM   970  C  CG   A ASP A 1 52  ? -9.44300  -21.06100 3.33100   0.590 16.77000  ? 52  ASP A CG   1 
ATOM   971  C  CG   B ASP A 1 52  ? -8.74000  -21.16400 3.36100   0.410 18.29000  ? 52  ASP A CG   1 
ATOM   972  O  OD1  A ASP A 1 52  ? -9.16600  -21.17600 4.53100   0.590 18.97000  ? 52  ASP A OD1  1 
ATOM   973  O  OD1  B ASP A 1 52  ? -8.48800  -20.98600 4.57800   0.410 19.50000  ? 52  ASP A OD1  1 
ATOM   974  O  OD2  A ASP A 1 52  ? -10.30600 -21.75600 2.76000   0.590 26.20000  ? 52  ASP A OD2  1 
ATOM   975  O  OD2  B ASP A 1 52  ? -8.94500  -22.29200 2.85400   0.410 23.13000  ? 52  ASP A OD2  1 
ATOM   976  H  H    A ASP A 1 52  ? -10.82400 -18.66900 3.14500   0.590 19.31000  ? 52  ASP A H    1 
ATOM   977  H  H    B ASP A 1 52  ? -10.84600 -18.69700 3.16200   0.410 19.36000  ? 52  ASP A H    1 
ATOM   978  H  HA   A ASP A 1 52  ? -8.24700  -18.55800 3.96700   0.590 19.88000  ? 52  ASP A HA   1 
ATOM   979  H  HA   B ASP A 1 52  ? -8.25200  -18.63000 3.92700   0.410 19.84000  ? 52  ASP A HA   1 
ATOM   980  H  HB2  A ASP A 1 52  ? -9.14100  -19.95000 1.66900   0.590 21.23000  ? 52  ASP A HB2  1 
ATOM   981  H  HB2  B ASP A 1 52  ? -9.58500  -20.04300 1.86900   0.410 20.77000  ? 52  ASP A HB2  1 
ATOM   982  H  HB3  A ASP A 1 52  ? -7.80600  -20.22900 2.48500   0.590 21.23000  ? 52  ASP A HB3  1 
ATOM   983  H  HB3  B ASP A 1 52  ? -7.99800  -19.94800 1.88900   0.410 20.77000  ? 52  ASP A HB3  1 
ATOM   984  N  N    . TYR A 1 53  ? -7.29600  -17.00000 2.32600   1.000 14.49000  ? 53  TYR A N    1 
ATOM   985  C  CA   . TYR A 1 53  ? -6.87400  -15.82200 1.56800   1.000 15.82000  ? 53  TYR A CA   1 
ATOM   986  C  C    . TYR A 1 53  ? -5.57800  -16.01000 0.78800   1.000 16.63000  ? 53  TYR A C    1 
ATOM   987  O  O    . TYR A 1 53  ? -4.57200  -16.47200 1.32800   1.000 16.28000  ? 53  TYR A O    1 
ATOM   988  C  CB   . TYR A 1 53  ? -6.65400  -14.66000 2.53800   1.000 17.16000  ? 53  TYR A CB   1 
ATOM   989  C  CG   . TYR A 1 53  ? -7.89600  -14.21300 3.25600   1.000 16.45000  ? 53  TYR A CG   1 
ATOM   990  C  CD1  . TYR A 1 53  ? -8.28400  -14.79200 4.43800   1.000 16.86000  ? 53  TYR A CD1  1 
ATOM   991  C  CD2  . TYR A 1 53  ? -8.64700  -13.18400 2.76800   1.000 17.22000  ? 53  TYR A CD2  1 
ATOM   992  C  CE1  . TYR A 1 53  ? -9.42000  -14.37600 5.08900   1.000 16.05000  ? 53  TYR A CE1  1 
ATOM   993  C  CE2  . TYR A 1 53  ? -9.81000  -12.76000 3.40700   1.000 17.20000  ? 53  TYR A CE2  1 
ATOM   994  C  CZ   . TYR A 1 53  ? -10.15700 -13.34600 4.57500   1.000 17.11000  ? 53  TYR A CZ   1 
ATOM   995  O  OH   . TYR A 1 53  ? -11.30100 -12.91800 5.23300   1.000 18.89000  ? 53  TYR A OH   1 
ATOM   996  H  H    . TYR A 1 53  ? -6.68700  -17.29500 2.85700   1.000 17.41000  ? 53  TYR A H    1 
ATOM   997  H  HA   . TYR A 1 53  ? -7.56500  -15.65400 0.90900   1.000 19.00000  ? 53  TYR A HA   1 
ATOM   998  H  HB2  . TYR A 1 53  ? -6.00900  -14.93400 3.20900   1.000 20.61000  ? 53  TYR A HB2  1 
ATOM   999  H  HB3  . TYR A 1 53  ? -6.31300  -13.90100 2.04000   1.000 20.61000  ? 53  TYR A HB3  1 
ATOM   1000 H  HD1  . TYR A 1 53  ? -7.77100  -15.47700 4.80300   1.000 20.26000  ? 53  TYR A HD1  1 
ATOM   1001 H  HD2  . TYR A 1 53  ? -8.37600  -12.75500 1.98900   1.000 20.69000  ? 53  TYR A HD2  1 
ATOM   1002 H  HE1  . TYR A 1 53  ? -9.68700  -14.79400 5.87600   1.000 19.28000  ? 53  TYR A HE1  1 
ATOM   1003 H  HE2  . TYR A 1 53  ? -10.33700 -12.08800 3.03800   1.000 20.67000  ? 53  TYR A HE2  1 
ATOM   1004 H  HH   . TYR A 1 53  ? -11.67000 -13.56600 5.62000   1.000 22.69000  ? 53  TYR A HH   1 
ATOM   1005 N  N    . GLY A 1 54  ? -5.61400  -15.60100 -0.47500  1.000 16.34000  ? 54  GLY A N    1 
ATOM   1006 C  CA   . GLY A 1 54  ? -4.41800  -15.37100 -1.23400  1.000 16.78000  ? 54  GLY A CA   1 
ATOM   1007 C  C    . GLY A 1 54  ? -3.89800  -16.61000 -1.91600  1.000 15.85000  ? 54  GLY A C    1 
ATOM   1008 O  O    . GLY A 1 54  ? -4.52300  -17.65400 -1.99200  1.000 16.82000  ? 54  GLY A O    1 
ATOM   1009 H  H    . GLY A 1 54  ? -6.33800  -15.45000 -0.91400  1.000 19.63000  ? 54  GLY A H    1 
ATOM   1010 H  HA2  . GLY A 1 54  ? -4.59800  -14.70400 -1.91500  1.000 20.15000  ? 54  GLY A HA2  1 
ATOM   1011 H  HA3  . GLY A 1 54  ? -3.72600  -15.03800 -0.64200  1.000 20.15000  ? 54  GLY A HA3  1 
ATOM   1012 N  N    . ILE A 1 55  ? -2.66700  -16.45800 -2.40000  1.000 16.94000  ? 55  ILE A N    1 
ATOM   1013 C  CA   . ILE A 1 55  ? -2.06500  -17.44000 -3.27700  1.000 17.01000  ? 55  ILE A CA   1 
ATOM   1014 C  C    . ILE A 1 55  ? -1.91500  -18.80100 -2.60500  1.000 16.70000  ? 55  ILE A C    1 
ATOM   1015 O  O    . ILE A 1 55  ? -1.96000  -19.83800 -3.28400  1.000 18.22000  ? 55  ILE A O    1 
ATOM   1016 C  CB   . ILE A 1 55  ? -0.74900  -16.85100 -3.81700  1.000 22.88000  ? 55  ILE A CB   1 
ATOM   1017 C  CG1  . ILE A 1 55  ? -0.32400  -17.59800 -5.07400  1.000 32.07000  ? 55  ILE A CG1  1 
ATOM   1018 C  CG2  . ILE A 1 55  ? 0.31100   -16.81400 -2.73800  1.000 23.51000  ? 55  ILE A CG2  1 
ATOM   1019 C  CD1  . ILE A 1 55  ? 0.18000   -16.70500 -6.13100  1.000 35.99000  ? 55  ILE A CD1  1 
ATOM   1020 H  H    . ILE A 1 55  ? -2.15800  -15.78600 -2.23000  1.000 20.34000  ? 55  ILE A H    1 
ATOM   1021 H  HA   . ILE A 1 55  ? -2.64900  -17.61600 -4.03200  1.000 20.43000  ? 55  ILE A HA   1 
ATOM   1022 H  HB   . ILE A 1 55  ? -0.88800  -15.92700 -4.07700  1.000 27.48000  ? 55  ILE A HB   1 
ATOM   1023 H  HG12 . ILE A 1 55  ? 0.38400   -18.22100 -4.84600  1.000 38.51000  ? 55  ILE A HG12 1 
ATOM   1024 H  HG13 . ILE A 1 55  ? -1.08800  -18.08000 -5.42800  1.000 38.51000  ? 55  ILE A HG13 1 
ATOM   1025 H  HG21 . ILE A 1 55  ? 1.10100   -16.37000 -3.08600  1.000 28.23000  ? 55  ILE A HG21 1 
ATOM   1026 H  HG22 . ILE A 1 55  ? -0.03300  -16.32600 -1.97400  1.000 28.23000  ? 55  ILE A HG22 1 
ATOM   1027 H  HG23 . ILE A 1 55  ? 0.53000   -17.72300 -2.47900  1.000 28.23000  ? 55  ILE A HG23 1 
ATOM   1028 H  HD11 . ILE A 1 55  ? 0.42400   -17.23700 -6.90500  1.000 43.21000  ? 55  ILE A HD11 1 
ATOM   1029 H  HD12 . ILE A 1 55  ? -0.51700  -16.07400 -6.37100  1.000 43.21000  ? 55  ILE A HD12 1 
ATOM   1030 H  HD13 . ILE A 1 55  ? 0.95700   -16.22900 -5.79900  1.000 43.21000  ? 55  ILE A HD13 1 
ATOM   1031 N  N    . LEU A 1 56  ? -1.68300  -18.83200 -1.28700  1.000 17.21000  ? 56  LEU A N    1 
ATOM   1032 C  CA   . LEU A 1 56  ? -1.57900  -20.07000 -0.53400  1.000 15.95000  ? 56  LEU A CA   1 
ATOM   1033 C  C    . LEU A 1 56  ? -2.77000  -20.32200 0.38800   1.000 18.40000  ? 56  LEU A C    1 
ATOM   1034 O  O    . LEU A 1 56  ? -2.71500  -21.22700 1.23000   1.000 18.97000  ? 56  LEU A O    1 
ATOM   1035 C  CB   . LEU A 1 56  ? -0.25600  -20.11700 0.23700   1.000 19.22000  ? 56  LEU A CB   1 
ATOM   1036 C  CG   . LEU A 1 56  ? 0.98800   -20.36800 -0.64700  1.000 22.45000  ? 56  LEU A CG   1 
ATOM   1037 C  CD1  . LEU A 1 56  ? 2.28600   -20.05600 0.09600   1.000 27.43000  ? 56  LEU A CD1  1 
ATOM   1038 C  CD2  . LEU A 1 56  ? 0.96000   -21.81900 -1.13400  1.000 25.39000  ? 56  LEU A CD2  1 
ATOM   1039 H  H    . LEU A 1 56  ? -1.58000  -18.12800 -0.80300  1.000 20.67000  ? 56  LEU A H    1 
ATOM   1040 H  HA   . LEU A 1 56  ? -1.56700  -20.80600 -1.16600  1.000 19.16000  ? 56  LEU A HA   1 
ATOM   1041 H  HB2  . LEU A 1 56  ? -0.13100  -19.26800 0.68800   1.000 23.09000  ? 56  LEU A HB2  1 
ATOM   1042 H  HB3  . LEU A 1 56  ? -0.30400  -20.83500 0.88800   1.000 23.09000  ? 56  LEU A HB3  1 
ATOM   1043 H  HG   . LEU A 1 56  ? 0.96900   -19.77200 -1.41200  1.000 26.96000  ? 56  LEU A HG   1 
ATOM   1044 H  HD11 . LEU A 1 56  ? 3.03100   -20.14700 -0.51800  1.000 32.94000  ? 56  LEU A HD11 1 
ATOM   1045 H  HD12 . LEU A 1 56  ? 2.24500   -19.14800 0.43500   1.000 32.94000  ? 56  LEU A HD12 1 
ATOM   1046 H  HD13 . LEU A 1 56  ? 2.38600   -20.68000 0.83200   1.000 32.94000  ? 56  LEU A HD13 1 
ATOM   1047 H  HD21 . LEU A 1 56  ? 1.80100   -22.02100 -1.57300  1.000 30.49000  ? 56  LEU A HD21 1 
ATOM   1048 H  HD22 . LEU A 1 56  ? 0.83500   -22.40500 -0.37200  1.000 30.49000  ? 56  LEU A HD22 1 
ATOM   1049 H  HD23 . LEU A 1 56  ? 0.22600   -21.92800 -1.75900  1.000 30.49000  ? 56  LEU A HD23 1 
ATOM   1050 N  N    . GLN A 1 57  ? -3.87200  -19.57300 0.23300   1.000 16.18000  ? 57  GLN A N    1 
ATOM   1051 C  CA   . GLN A 1 57  ? -5.14400  -19.87800 0.90500   1.000 16.08000  ? 57  GLN A CA   1 
ATOM   1052 C  C    . GLN A 1 57  ? -4.95800  -20.05300 2.41000   1.000 17.21000  ? 57  GLN A C    1 
ATOM   1053 O  O    . GLN A 1 57  ? -5.40200  -21.03300 3.00500   1.000 19.77000  ? 57  GLN A O    1 
ATOM   1054 C  CB   . GLN A 1 57  ? -5.85800  -21.05800 0.26200   1.000 16.56000  ? 57  GLN A CB   1 
ATOM   1055 C  CG   . GLN A 1 57  ? -6.37400  -20.72600 -1.14500  1.000 16.62000  ? 57  GLN A CG   1 
ATOM   1056 C  CD   . GLN A 1 57  ? -7.54800  -19.77600 -1.08500  1.000 17.02000  ? 57  GLN A CD   1 
ATOM   1057 O  OE1  . GLN A 1 57  ? -8.67300  -20.18800 -0.83000  1.000 18.76000  ? 57  GLN A OE1  1 
ATOM   1058 N  NE2  . GLN A 1 57  ? -7.27800  -18.50500 -1.26700  1.000 18.75000  ? 57  GLN A NE2  1 
ATOM   1059 H  H    . GLN A 1 57  ? -3.90800  -18.87300 -0.26500  1.000 19.43000  ? 57  GLN A H    1 
ATOM   1060 H  HA   . GLN A 1 57  ? -5.72800  -19.11200 0.79100   1.000 19.31000  ? 57  GLN A HA   1 
ATOM   1061 H  HB2  . GLN A 1 57  ? -5.24100  -21.80200 0.19000   1.000 19.89000  ? 57  GLN A HB2  1 
ATOM   1062 H  HB3  . GLN A 1 57  ? -6.61700  -21.30700 0.81200   1.000 19.89000  ? 57  GLN A HB3  1 
ATOM   1063 H  HG2  . GLN A 1 57  ? -5.66600  -20.30700 -1.65800  1.000 19.96000  ? 57  GLN A HG2  1 
ATOM   1064 H  HG3  . GLN A 1 57  ? -6.66200  -21.54200 -1.58300  1.000 19.96000  ? 57  GLN A HG3  1 
ATOM   1065 H  HE21 . GLN A 1 57  ? -6.46800  -18.25400 -1.41000  1.000 22.52000  ? 57  GLN A HE21 1 
ATOM   1066 H  HE22 . GLN A 1 57  ? -7.91100  -17.92300 -1.24200  1.000 22.52000  ? 57  GLN A HE22 1 
ATOM   1067 N  N    . ILE A 1 58  ? -4.35200  -19.04800 3.00600   1.000 16.56000  ? 58  ILE A N    1 
ATOM   1068 C  CA   . ILE A 1 58  ? -4.07600  -19.02100 4.44900   0.930 15.64000  ? 58  ILE A CA   1 
ATOM   1069 C  C    . ILE A 1 58  ? -5.33500  -18.65400 5.21500   0.730 13.60000  ? 58  ILE A C    1 
ATOM   1070 O  O    . ILE A 1 58  ? -6.03000  -17.70800 4.85900   1.000 16.99000  ? 58  ILE A O    1 
ATOM   1071 C  CB   . ILE A 1 58  ? -2.91600  -18.07300 4.71900   0.980 17.84000  ? 58  ILE A CB   1 
ATOM   1072 C  CG1  . ILE A 1 58  ? -1.64500  -18.71300 4.12000   0.990 20.53000  ? 58  ILE A CG1  1 
ATOM   1073 C  CG2  . ILE A 1 58  ? -2.76000  -17.75500 6.22600   0.720 14.17000  ? 58  ILE A CG2  1 
ATOM   1074 C  CD1  . ILE A 1 58  ? -0.49300  -17.80500 4.08400   0.860 23.18000  ? 58  ILE A CD1  1 
ATOM   1075 H  H    . ILE A 1 58  ? -4.07800  -18.34300 2.59600   1.000 19.89000  ? 58  ILE A H    1 
ATOM   1076 H  HA   . ILE A 1 58  ? -3.82800  -19.90500 4.75900   0.990 18.79000  ? 58  ILE A HA   1 
ATOM   1077 H  HB   . ILE A 1 58  ? -3.08400  -17.21600 4.29600   1.000 21.42000  ? 58  ILE A HB   1 
ATOM   1078 H  HG12 . ILE A 1 58  ? -1.40000  -19.48200 4.65700   1.000 24.66000  ? 58  ILE A HG12 1 
ATOM   1079 H  HG13 . ILE A 1 58  ? -1.83400  -18.99000 3.21000   1.000 24.66000  ? 58  ILE A HG13 1 
ATOM   1080 H  HG21 . ILE A 1 58  ? -2.00100  -17.16400 6.34700   1.000 17.02000  ? 58  ILE A HG21 1 
ATOM   1081 H  HG22 . ILE A 1 58  ? -3.56900  -17.32400 6.54200   0.900 17.02000  ? 58  ILE A HG22 1 
ATOM   1082 H  HG23 . ILE A 1 58  ? -2.61600  -18.58300 6.71000   0.950 17.02000  ? 58  ILE A HG23 1 
ATOM   1083 H  HD11 . ILE A 1 58  ? 0.25900   -18.26600 3.67900   0.910 27.84000  ? 58  ILE A HD11 1 
ATOM   1084 H  HD12 . ILE A 1 58  ? -0.72300  -17.02300 3.55900   0.940 27.84000  ? 58  ILE A HD12 1 
ATOM   1085 H  HD13 . ILE A 1 58  ? -0.26900  -17.54200 4.99000   0.910 27.84000  ? 58  ILE A HD13 1 
ATOM   1086 N  N    A ASN A 1 59  ? -5.68400  -19.45700 6.22600   0.400 16.37000  ? 59  ASN A N    1 
ATOM   1087 N  N    B ASN A 1 59  ? -5.60300  -19.40700 6.28900   0.310 16.52000  ? 59  ASN A N    1 
ATOM   1088 N  N    C ASN A 1 59  ? -5.61600  -19.40700 6.28600   0.290 16.50000  ? 59  ASN A N    1 
ATOM   1089 C  CA   A ASN A 1 59  ? -7.00700  -19.35700 6.83400   0.400 19.02000  ? 59  ASN A CA   1 
ATOM   1090 C  CA   B ASN A 1 59  ? -6.88300  -19.42100 6.99100   0.310 18.18000  ? 59  ASN A CA   1 
ATOM   1091 C  CA   C ASN A 1 59  ? -6.92300  -19.41200 6.93700   0.290 18.38000  ? 59  ASN A CA   1 
ATOM   1092 C  C    A ASN A 1 59  ? -7.03600  -18.46900 8.07200   0.400 18.48000  ? 59  ASN A C    1 
ATOM   1093 C  C    B ASN A 1 59  ? -6.94000  -18.31400 8.04000   0.310 18.12000  ? 59  ASN A C    1 
ATOM   1094 C  C    C ASN A 1 59  ? -7.00300  -18.43500 8.10800   0.290 18.40000  ? 59  ASN A C    1 
ATOM   1095 O  O    A ASN A 1 59  ? -6.14500  -18.51600 8.92200   0.400 20.35000  ? 59  ASN A O    1 
ATOM   1096 O  O    B ASN A 1 59  ? -5.92600  -17.95500 8.64600   0.310 16.65000  ? 59  ASN A O    1 
ATOM   1097 O  O    C ASN A 1 59  ? -6.09200  -18.35600 8.93400   0.290 20.29000  ? 59  ASN A O    1 
ATOM   1098 C  CB   A ASN A 1 59  ? -7.54400  -20.73600 7.20300   0.400 19.45000  ? 59  ASN A CB   1 
ATOM   1099 C  CB   B ASN A 1 59  ? -7.06500  -20.80600 7.63700   0.310 21.65000  ? 59  ASN A CB   1 
ATOM   1100 C  CB   C ASN A 1 59  ? -7.23200  -20.82700 7.44300   0.290 21.85000  ? 59  ASN A CB   1 
ATOM   1101 C  CG   A ASN A 1 59  ? -6.86600  -21.29400 8.42500   0.400 20.79000  ? 59  ASN A CG   1 
ATOM   1102 C  CG   B ASN A 1 59  ? -8.52000  -21.14600 7.95600   0.310 18.42000  ? 59  ASN A CG   1 
ATOM   1103 C  CG   C ASN A 1 59  ? -8.61600  -20.94400 8.02400   0.290 20.42000  ? 59  ASN A CG   1 
ATOM   1104 O  OD1  A ASN A 1 59  ? -7.08700  -20.82400 9.54200   0.400 22.53000  ? 59  ASN A OD1  1 
ATOM   1105 O  OD1  B ASN A 1 59  ? -9.37400  -20.27200 8.11000   0.310 17.72000  ? 59  ASN A OD1  1 
ATOM   1106 O  OD1  C ASN A 1 59  ? -8.81000  -20.78200 9.22900   0.290 24.32000  ? 59  ASN A OD1  1 
ATOM   1107 N  ND2  A ASN A 1 59  ? -6.00300  -22.27800 8.22300   0.400 22.99000  ? 59  ASN A ND2  1 
ATOM   1108 N  ND2  B ASN A 1 59  ? -8.80700  -22.43800 8.04500   0.310 22.20000  ? 59  ASN A ND2  1 
ATOM   1109 N  ND2  C ASN A 1 59  ? -9.59100  -21.23600 7.17800   0.290 20.72000  ? 59  ASN A ND2  1 
ATOM   1110 H  H    A ASN A 1 59  ? -5.17600  -20.05900 6.57100   0.370 19.67000  ? 59  ASN A H    1 
ATOM   1111 H  H    B ASN A 1 59  ? -5.03100  -19.94200 6.64300   0.080 19.85000  ? 59  ASN A H    1 
ATOM   1112 H  H    C ASN A 1 59  ? -5.05000  -19.93400 6.66000   0.230 19.82000  ? 59  ASN A H    1 
ATOM   1113 H  HA   A ASN A 1 59  ? -7.58700  -18.94500 6.17400   0.400 22.84000  ? 59  ASN A HA   1 
ATOM   1114 H  HA   B ASN A 1 59  ? -7.61700  -19.25400 6.37900   0.310 21.84000  ? 59  ASN A HA   1 
ATOM   1115 H  HA   C ASN A 1 59  ? -7.58700  -19.12800 6.29000   0.290 22.08000  ? 59  ASN A HA   1 
ATOM   1116 H  HB2  A ASN A 1 59  ? -8.49500  -20.67000 7.38600   0.400 23.36000  ? 59  ASN A HB2  1 
ATOM   1117 H  HB2  B ASN A 1 59  ? -6.73000  -21.48100 7.02700   0.310 26.01000  ? 59  ASN A HB2  1 
ATOM   1118 H  HB2  C ASN A 1 59  ? -7.16400  -21.45000 6.70300   0.290 26.25000  ? 59  ASN A HB2  1 
ATOM   1119 H  HB3  A ASN A 1 59  ? -7.39100  -21.34600 6.46500   0.400 23.36000  ? 59  ASN A HB3  1 
ATOM   1120 H  HB3  B ASN A 1 59  ? -6.56500  -20.83200 8.46800   0.310 26.01000  ? 59  ASN A HB3  1 
ATOM   1121 H  HB3  C ASN A 1 59  ? -6.59500  -21.06200 8.13500   0.290 26.25000  ? 59  ASN A HB3  1 
ATOM   1122 H  HD21 A ASN A 1 59  ? -5.59000  -22.63000 8.89000   0.400 27.61000  ? 59  ASN A HD21 1 
ATOM   1123 H  HD21 B ASN A 1 59  ? -9.61000  -22.68900 8.22200   0.310 26.67000  ? 59  ASN A HD21 1 
ATOM   1124 H  HD21 C ASN A 1 59  ? -10.39900 -21.31300 7.46200   0.290 24.88000  ? 59  ASN A HD21 1 
ATOM   1125 H  HD22 A ASN A 1 59  ? -5.85600  -22.56400 7.42600   0.400 27.61000  ? 59  ASN A HD22 1 
ATOM   1126 H  HD22 B ASN A 1 59  ? -8.18900  -23.02500 7.92400   0.310 26.67000  ? 59  ASN A HD22 1 
ATOM   1127 H  HD22 C ASN A 1 59  ? -9.41700  -21.34700 6.34300   0.290 24.88000  ? 59  ASN A HD22 1 
ATOM   1128 N  N    . SER A 1 60  ? -8.11900  -17.71100 8.18400   1.000 16.26000  ? 60  SER A N    1 
ATOM   1129 C  CA   . SER A 1 60  ? -8.32300  -16.74400 9.25000   1.000 17.07000  ? 60  SER A CA   1 
ATOM   1130 C  C    . SER A 1 60  ? -8.61700  -17.38900 10.59600  1.000 18.55000  ? 60  SER A C    1 
ATOM   1131 O  O    . SER A 1 60  ? -8.61800  -16.66000 11.59500  1.000 22.07000  ? 60  SER A O    1 
ATOM   1132 C  CB   . SER A 1 60  ? -9.51000  -15.83600 8.89000   1.000 17.05000  ? 60  SER A CB   1 
ATOM   1133 O  OG   . SER A 1 60  ? -10.71400 -16.52800 8.81400   1.000 17.87000  ? 60  SER A OG   1 
ATOM   1134 H  H    . SER A 1 60  ? -8.77800  -17.73900 7.63200   0.910 19.53000  ? 60  SER A H    1 
ATOM   1135 H  HA   . SER A 1 60  ? -7.51800  -16.20900 9.33600   1.000 20.51000  ? 60  SER A HA   1 
ATOM   1136 H  HB2  . SER A 1 60  ? -9.59100  -15.15100 9.57100   1.000 20.48000  ? 60  SER A HB2  1 
ATOM   1137 H  HB3  . SER A 1 60  ? -9.33400  -15.42800 8.02700   1.000 20.48000  ? 60  SER A HB3  1 
ATOM   1138 H  HG   . SER A 1 60  ? -10.78700 -17.05100 9.46700   1.000 21.46000  ? 60  SER A HG   1 
ATOM   1139 N  N    A ARG A 1 61  ? -8.85800  -18.69800 10.63700  0.860 18.58000  ? 61  ARG A N    1 
ATOM   1140 N  N    B ARG A 1 61  ? -8.86700  -18.69900 10.63900  0.140 18.76000  ? 61  ARG A N    1 
ATOM   1141 C  CA   A ARG A 1 61  ? -9.11200  -19.38400 11.91100  0.860 21.98000  ? 61  ARG A CA   1 
ATOM   1142 C  CA   B ARG A 1 61  ? -9.11000  -19.37100 11.91100  0.140 22.10000  ? 61  ARG A CA   1 
ATOM   1143 C  C    A ARG A 1 61  ? -7.89100  -19.31300 12.81000  0.860 22.68000  ? 61  ARG A C    1 
ATOM   1144 C  C    B ARG A 1 61  ? -7.89700  -19.28700 12.82400  0.140 23.32000  ? 61  ARG A C    1 
ATOM   1145 O  O    A ARG A 1 61  ? -8.01700  -19.19300 14.04200  0.860 24.54000  ? 61  ARG A O    1 
ATOM   1146 O  O    B ARG A 1 61  ? -8.04900  -19.27700 14.05300  0.140 24.26000  ? 61  ARG A O    1 
ATOM   1147 C  CB   A ARG A 1 61  ? -9.50200  -20.84000 11.63100  0.860 25.68000  ? 61  ARG A CB   1 
ATOM   1148 C  CB   B ARG A 1 61  ? -9.47400  -20.83400 11.64600  0.140 25.78000  ? 61  ARG A CB   1 
ATOM   1149 C  CG   A ARG A 1 61  ? -9.60700  -21.78400 12.83300  0.860 35.45000  ? 61  ARG A CG   1 
ATOM   1150 C  CG   B ARG A 1 61  ? -9.57200  -21.72000 12.88100  0.140 34.98000  ? 61  ARG A CG   1 
ATOM   1151 C  CD   A ARG A 1 61  ? -10.68400 -21.36400 13.79400  0.860 30.01000  ? 61  ARG A CD   1 
ATOM   1152 C  CD   B ARG A 1 61  ? -10.64200 -21.24300 13.84500  0.140 30.70000  ? 61  ARG A CD   1 
ATOM   1153 N  NE   A ARG A 1 61  ? -12.00900 -21.32600 13.18700  0.860 36.22000  ? 61  ARG A NE   1 
ATOM   1154 N  NE   B ARG A 1 61  ? -11.96800 -21.23700 13.23900  0.140 35.96000  ? 61  ARG A NE   1 
ATOM   1155 C  CZ   A ARG A 1 61  ? -13.02400 -20.59700 13.63900  0.860 48.52000  ? 61  ARG A CZ   1 
ATOM   1156 C  CZ   B ARG A 1 61  ? -12.98600 -20.50100 13.66600  0.140 48.63000  ? 61  ARG A CZ   1 
ATOM   1157 N  NH1  A ARG A 1 61  ? -12.92400 -19.87900 14.74900  0.860 40.90000  ? 61  ARG A NH1  1 
ATOM   1158 N  NH1  B ARG A 1 61  ? -12.87700 -19.72200 14.73100  0.140 40.46000  ? 61  ARG A NH1  1 
ATOM   1159 N  NH2  A ARG A 1 61  ? -14.17100 -20.58800 12.95900  0.860 41.24000  ? 61  ARG A NH2  1 
ATOM   1160 N  NH2  B ARG A 1 61  ? -14.14200 -20.54900 13.01000  0.140 41.18000  ? 61  ARG A NH2  1 
ATOM   1161 H  H    A ARG A 1 61  ? -8.88200  -19.21300 9.94900   0.860 22.31000  ? 61  ARG A H    1 
ATOM   1162 H  H    B ARG A 1 61  ? -8.90200  -19.21500 9.95200   0.140 22.53000  ? 61  ARG A H    1 
ATOM   1163 H  HA   A ARG A 1 61  ? -9.84900  -18.95700 12.37400  0.860 26.39000  ? 61  ARG A HA   1 
ATOM   1164 H  HA   B ARG A 1 61  ? -9.85300  -18.94400 12.36400  0.140 26.54000  ? 61  ARG A HA   1 
ATOM   1165 H  HB2  A ARG A 1 61  ? -10.37100 -20.83800 11.19900  0.860 30.84000  ? 61  ARG A HB2  1 
ATOM   1166 H  HB2  B ARG A 1 61  ? -10.33700 -20.85800 11.20400  0.140 30.96000  ? 61  ARG A HB2  1 
ATOM   1167 H  HB3  A ARG A 1 61  ? -8.83700  -21.21700 11.03500  0.860 30.84000  ? 61  ARG A HB3  1 
ATOM   1168 H  HB3  B ARG A 1 61  ? -8.79500  -21.21700 11.06900  0.140 30.96000  ? 61  ARG A HB3  1 
ATOM   1169 H  HG2  A ARG A 1 61  ? -9.81400  -22.67800 12.51900  0.860 42.57000  ? 61  ARG A HG2  1 
ATOM   1170 H  HG2  B ARG A 1 61  ? -9.79400  -22.62400 12.60800  0.140 42.00000  ? 61  ARG A HG2  1 
ATOM   1171 H  HG3  A ARG A 1 61  ? -8.76200  -21.78800 13.31000  0.860 42.57000  ? 61  ARG A HG3  1 
ATOM   1172 H  HG3  B ARG A 1 61  ? -8.72100  -21.71300 13.34700  0.140 42.00000  ? 61  ARG A HG3  1 
ATOM   1173 H  HD2  A ARG A 1 61  ? -10.71100 -21.99400 14.53100  0.860 36.03000  ? 61  ARG A HD2  1 
ATOM   1174 H  HD2  B ARG A 1 61  ? -10.66400 -21.83500 14.61400  0.140 36.87000  ? 61  ARG A HD2  1 
ATOM   1175 H  HD3  A ARG A 1 61  ? -10.48100 -20.47500 14.12400  0.860 36.03000  ? 61  ARG A HD3  1 
ATOM   1176 H  HD3  B ARG A 1 61  ? -10.43500 -20.33900 14.12800  0.140 36.87000  ? 61  ARG A HD3  1 
ATOM   1177 H  HE   A ARG A 1 61  ? -12.14300 -21.80900 12.48800  0.860 43.48000  ? 61  ARG A HE   1 
ATOM   1178 H  HE   B ARG A 1 61  ? -12.10000 -21.74500 12.55700  0.140 43.18000  ? 61  ARG A HE   1 
ATOM   1179 H  HH11 A ARG A 1 61  ? -12.18900 -19.87800 15.19500  0.860 49.11000  ? 61  ARG A HH11 1 
ATOM   1180 H  HH11 B ARG A 1 61  ? -13.55000 -19.25300 14.99100  0.140 48.57000  ? 61  ARG A HH11 1 
ATOM   1181 H  HH12 A ARG A 1 61  ? -13.59500 -19.41500 15.02200  0.860 49.11000  ? 61  ARG A HH12 1 
ATOM   1182 H  HH12 B ARG A 1 61  ? -12.13500 -19.68500 15.16300  0.140 48.57000  ? 61  ARG A HH12 1 
ATOM   1183 H  HH21 A ARG A 1 61  ? -14.24700 -21.04900 12.23800  0.860 49.51000  ? 61  ARG A HH21 1 
ATOM   1184 H  HH21 B ARG A 1 61  ? -14.22300 -21.05300 12.31800  0.140 49.43000  ? 61  ARG A HH21 1 
ATOM   1185 H  HH22 A ARG A 1 61  ? -14.83400 -20.12000 13.24200  0.860 49.51000  ? 61  ARG A HH22 1 
ATOM   1186 H  HH22 B ARG A 1 61  ? -14.80900 -20.07600 13.27900  0.140 49.43000  ? 61  ARG A HH22 1 
ATOM   1187 N  N    A TRP A 1 62  ? -6.69600  -19.36500 12.22600  0.860 20.21000  ? 62  TRP A N    1 
ATOM   1188 N  N    B TRP A 1 62  ? -6.69400  -19.22100 12.25200  0.140 20.16000  ? 62  TRP A N    1 
ATOM   1189 C  CA   A TRP A 1 62  ? -5.46700  -19.37300 12.99800  0.860 21.95000  ? 62  TRP A CA   1 
ATOM   1190 C  CA   B TRP A 1 62  ? -5.48300  -19.26800 13.05600  0.140 22.79000  ? 62  TRP A CA   1 
ATOM   1191 C  C    A TRP A 1 62  ? -4.48900  -18.25700 12.68100  0.860 23.15000  ? 62  TRP A C    1 
ATOM   1192 C  C    B TRP A 1 62  ? -4.46600  -18.19200 12.69900  0.140 23.33000  ? 62  TRP A C    1 
ATOM   1193 O  O    A TRP A 1 62  ? -3.74200  -17.86300 13.56900  0.860 23.03000  ? 62  TRP A O    1 
ATOM   1194 O  O    B TRP A 1 62  ? -3.72000  -17.73900 13.57300  0.140 22.69000  ? 62  TRP A O    1 
ATOM   1195 C  CB   A TRP A 1 62  ? -4.70200  -20.70600 12.81600  0.860 24.88000  ? 62  TRP A CB   1 
ATOM   1196 C  CB   B TRP A 1 62  ? -4.79900  -20.63900 12.91700  0.140 25.25000  ? 62  TRP A CB   1 
ATOM   1197 C  CG   A TRP A 1 62  ? -5.47500  -21.86100 13.26900  0.860 26.48000  ? 62  TRP A CG   1 
ATOM   1198 C  CG   B TRP A 1 62  ? -5.62200  -21.77300 13.41500  0.140 28.14000  ? 62  TRP A CG   1 
ATOM   1199 C  CD1  A TRP A 1 62  ? -6.16000  -22.74400 12.49400  0.860 32.66000  ? 62  TRP A CD1  1 
ATOM   1200 C  CD1  B TRP A 1 62  ? -6.21900  -22.74500 12.66800  0.140 32.36000  ? 62  TRP A CD1  1 
ATOM   1201 C  CD2  A TRP A 1 62  ? -5.68300  -22.26100 14.62100  0.860 33.32000  ? 62  TRP A CD2  1 
ATOM   1202 C  CD2  B TRP A 1 62  ? -5.94700  -22.05600 14.77900  0.140 32.32000  ? 62  TRP A CD2  1 
ATOM   1203 N  NE1  A TRP A 1 62  ? -6.78300  -23.67900 13.28500  0.860 39.12000  ? 62  TRP A NE1  1 
ATOM   1204 N  NE1  B TRP A 1 62  ? -6.89900  -23.61700 13.48500  0.140 37.39000  ? 62  TRP A NE1  1 
ATOM   1205 C  CE2  A TRP A 1 62  ? -6.49700  -23.40500 14.59700  0.860 34.06000  ? 62  TRP A CE2  1 
ATOM   1206 C  CE2  B TRP A 1 62  ? -6.74600  -23.21500 14.78600  0.140 35.71000  ? 62  TRP A CE2  1 
ATOM   1207 C  CE3  A TRP A 1 62  ? -5.24900  -21.76200 15.85100  0.860 35.08000  ? 62  TRP A CE3  1 
ATOM   1208 C  CE3  B TRP A 1 62  ? -5.64000  -21.43900 15.99500  0.140 34.54000  ? 62  TRP A CE3  1 
ATOM   1209 C  CZ2  A TRP A 1 62  ? -6.88800  -24.06600 15.75900  0.860 47.65000  ? 62  TRP A CZ2  1 
ATOM   1210 C  CZ2  B TRP A 1 62  ? -7.24200  -23.77100 15.96300  0.140 44.13000  ? 62  TRP A CZ2  1 
ATOM   1211 C  CZ3  A TRP A 1 62  ? -5.63600  -22.42000 17.00700  0.860 43.60000  ? 62  TRP A CZ3  1 
ATOM   1212 C  CZ3  B TRP A 1 62  ? -6.13200  -21.99300 17.16300  0.140 40.41000  ? 62  TRP A CZ3  1 
ATOM   1213 C  CH2  A TRP A 1 62  ? -6.45300  -23.55700 16.95000  0.860 45.00000  ? 62  TRP A CH2  1 
ATOM   1214 C  CH2  B TRP A 1 62  ? -6.92500  -23.14700 17.13800  0.140 43.23000  ? 62  TRP A CH2  1 
ATOM   1215 H  H    A TRP A 1 62  ? -6.57600  -19.39800 11.37500  0.860 24.27000  ? 62  TRP A H    1 
ATOM   1216 H  H    B TRP A 1 62  ? -6.55700  -19.14800 11.40600  0.140 24.21000  ? 62  TRP A H    1 
ATOM   1217 H  HA   A TRP A 1 62  ? -5.73300  -19.28200 13.92600  0.860 26.36000  ? 62  TRP A HA   1 
ATOM   1218 H  HA   B TRP A 1 62  ? -5.76000  -19.11400 13.97300  0.140 27.36000  ? 62  TRP A HA   1 
ATOM   1219 H  HB2  A TRP A 1 62  ? -4.49900  -20.82900 11.87600  0.860 29.88000  ? 62  TRP A HB2  1 
ATOM   1220 H  HB2  B TRP A 1 62  ? -4.61100  -20.79900 11.97900  0.140 30.32000  ? 62  TRP A HB2  1 
ATOM   1221 H  HB3  A TRP A 1 62  ? -3.88100  -20.67200 13.33200  0.860 29.88000  ? 62  TRP A HB3  1 
ATOM   1222 H  HB3  B TRP A 1 62  ? -3.97300  -20.62800 13.42400  0.140 30.32000  ? 62  TRP A HB3  1 
ATOM   1223 H  HD1  A TRP A 1 62  ? -6.20100  -22.71900 11.56600  0.860 39.21000  ? 62  TRP A HD1  1 
ATOM   1224 H  HD1  B TRP A 1 62  ? -6.17300  -22.80900 11.74200  0.140 38.86000  ? 62  TRP A HD1  1 
ATOM   1225 H  HE1  A TRP A 1 62  ? -7.27100  -24.32800 13.00400  0.860 46.96000  ? 62  TRP A HE1  1 
ATOM   1226 H  HE1  B TRP A 1 62  ? -7.34700  -24.30200 13.22300  0.140 44.89000  ? 62  TRP A HE1  1 
ATOM   1227 H  HE3  A TRP A 1 62  ? -4.71200  -21.00300 15.89400  0.860 42.12000  ? 62  TRP A HE3  1 
ATOM   1228 H  HE3  B TRP A 1 62  ? -5.11500  -20.67200 16.01900  0.140 41.47000  ? 62  TRP A HE3  1 
ATOM   1229 H  HZ2  A TRP A 1 62  ? -7.42500  -24.82500 15.72600  0.860 57.21000  ? 62  TRP A HZ2  1 
ATOM   1230 H  HZ2  B TRP A 1 62  ? -7.76800  -24.53800 15.95100  0.140 52.98000  ? 62  TRP A HZ2  1 
ATOM   1231 H  HZ3  A TRP A 1 62  ? -5.34800  -22.10400 17.83300  0.860 52.34000  ? 62  TRP A HZ3  1 
ATOM   1232 H  HZ3  B TRP A 1 62  ? -5.93400  -21.59200 17.97800  0.140 48.51000  ? 62  TRP A HZ3  1 
ATOM   1233 H  HH2  A TRP A 1 62  ? -6.70600  -23.97500 17.74200  0.860 54.01000  ? 62  TRP A HH2  1 
ATOM   1234 H  HH2  B TRP A 1 62  ? -7.24300  -23.49700 17.93900  0.140 51.89000  ? 62  TRP A HH2  1 
ATOM   1235 N  N    . TRP A 1 63  ? -4.40900  -17.76400 11.43300  1.000 18.86000  ? 63  TRP A N    1 
ATOM   1236 C  CA   . TRP A 1 63  ? -3.20100  -17.12600 10.95300  1.000 18.58000  ? 63  TRP A CA   1 
ATOM   1237 C  C    . TRP A 1 63  ? -3.28100  -15.64400 10.69000  1.000 17.06000  ? 63  TRP A C    1 
ATOM   1238 O  O    . TRP A 1 63  ? -2.24400  -14.99800 10.63000  1.000 19.64000  ? 63  TRP A O    1 
ATOM   1239 C  CB   . TRP A 1 63  ? -2.69400  -17.84000 9.67200   1.000 19.19000  ? 63  TRP A CB   1 
ATOM   1240 C  CG   . TRP A 1 63  ? -2.50500  -19.30600 9.91300   1.000 21.12000  ? 63  TRP A CG   1 
ATOM   1241 C  CD1  . TRP A 1 63  ? -3.29800  -20.30400 9.48400   1.000 22.36000  ? 63  TRP A CD1  1 
ATOM   1242 C  CD2  . TRP A 1 63  ? -1.49100  -19.91700 10.73300  1.000 20.93000  ? 63  TRP A CD2  1 
ATOM   1243 N  NE1  . TRP A 1 63  ? -2.85300  -21.51000 9.95700   1.000 24.20000  ? 63  TRP A NE1  1 
ATOM   1244 C  CE2  . TRP A 1 63  ? -1.74900  -21.29700 10.73600  1.000 19.37000  ? 63  TRP A CE2  1 
ATOM   1245 C  CE3  . TRP A 1 63  ? -0.39600  -19.43000 11.43500  1.000 22.43000  ? 63  TRP A CE3  1 
ATOM   1246 C  CZ2  . TRP A 1 63  ? -0.91900  -22.21600 11.41500  1.000 21.21000  ? 63  TRP A CZ2  1 
ATOM   1247 C  CZ3  . TRP A 1 63  ? 0.42600   -20.35400 12.12300  1.000 23.16000  ? 63  TRP A CZ3  1 
ATOM   1248 C  CH2  . TRP A 1 63  ? 0.14600   -21.71300 12.10100  1.000 25.06000  ? 63  TRP A CH2  1 
ATOM   1249 H  H    . TRP A 1 63  ? -5.04600  -17.79300 10.85600  1.000 22.66000  ? 63  TRP A H    1 
ATOM   1250 H  HA   . TRP A 1 63  ? -2.53500  -17.22400 11.65100  1.000 22.31000  ? 63  TRP A HA   1 
ATOM   1251 H  HB2  . TRP A 1 63  ? -3.34400  -17.72700 8.96100   1.000 23.04000  ? 63  TRP A HB2  1 
ATOM   1252 H  HB3  . TRP A 1 63  ? -1.84300  -17.46000 9.40600   1.000 23.04000  ? 63  TRP A HB3  1 
ATOM   1253 H  HD1  . TRP A 1 63  ? -4.04500  -20.19100 8.94100   1.000 26.86000  ? 63  TRP A HD1  1 
ATOM   1254 H  HE1  . TRP A 1 63  ? -3.21000  -22.27500 9.79200   1.000 29.06000  ? 63  TRP A HE1  1 
ATOM   1255 H  HE3  . TRP A 1 63  ? -0.20700  -18.52000 11.45200  1.000 26.93000  ? 63  TRP A HE3  1 
ATOM   1256 H  HZ2  . TRP A 1 63  ? -1.09200  -23.13000 11.39500  1.000 25.47000  ? 63  TRP A HZ2  1 
ATOM   1257 H  HZ3  . TRP A 1 63  ? 1.16500   -20.04600 12.59700  1.000 27.81000  ? 63  TRP A HZ3  1 
ATOM   1258 H  HH2  . TRP A 1 63  ? 0.70100   -22.29600 12.56700  1.000 30.09000  ? 63  TRP A HH2  1 
ATOM   1259 N  N    . CYS A 1 64  ? -4.47600  -15.10900 10.45000  1.000 17.61000  ? 64  CYS A N    1 
ATOM   1260 C  CA   . CYS A 1 64  ? -4.62400  -13.70000 10.13300  1.000 19.93000  ? 64  CYS A CA   1 
ATOM   1261 C  C    . CYS A 1 64  ? -5.93700  -13.19600 10.70400  1.000 18.59000  ? 64  CYS A C    1 
ATOM   1262 O  O    . CYS A 1 64  ? -6.82900  -13.97100 11.03100  1.000 19.35000  ? 64  CYS A O    1 
ATOM   1263 C  CB   . CYS A 1 64  ? -4.55900  -13.45400 8.61000   1.000 19.02000  ? 64  CYS A CB   1 
ATOM   1264 S  SG   . CYS A 1 64  ? -5.81300  -14.25400 7.60100   1.000 18.14000  ? 64  CYS A SG   1 
ATOM   1265 H  H    . CYS A 1 64  ? -5.21600  -15.54600 10.46500  1.000 21.16000  ? 64  CYS A H    1 
ATOM   1266 H  HA   . CYS A 1 64  ? -3.90600  -13.20000 10.55200  1.000 23.94000  ? 64  CYS A HA   1 
ATOM   1267 H  HB2  . CYS A 1 64  ? -4.64100  -12.49900 8.45800   1.000 22.84000  ? 64  CYS A HB2  1 
ATOM   1268 H  HB3  . CYS A 1 64  ? -3.69800  -13.76800 8.29300   1.000 22.84000  ? 64  CYS A HB3  1 
ATOM   1269 N  N    . ASN A 1 65  ? -6.03800  -11.87500 10.77800  1.000 18.97000  ? 65  ASN A N    1 
ATOM   1270 C  CA   . ASN A 1 65  ? -7.25100  -11.24400 11.27900  1.000 19.54000  ? 65  ASN A CA   1 
ATOM   1271 C  C    . ASN A 1 65  ? -8.08000  -10.64100 10.15200  1.000 17.57000  ? 65  ASN A C    1 
ATOM   1272 O  O    . ASN A 1 65  ? -7.58700  -9.77800  9.43400   1.000 18.67000  ? 65  ASN A O    1 
ATOM   1273 C  CB   . ASN A 1 65  ? -6.91100  -10.13700 12.26700  1.000 22.01000  ? 65  ASN A CB   1 
ATOM   1274 C  CG   . ASN A 1 65  ? -8.14000  -9.43200  12.74900  1.000 30.67000  ? 65  ASN A CG   1 
ATOM   1275 O  OD1  . ASN A 1 65  ? -9.05200  -10.07100 13.23400  1.000 31.32000  ? 65  ASN A OD1  1 
ATOM   1276 N  ND2  . ASN A 1 65  ? -8.20900  -8.13200  12.52600  1.000 35.10000  ? 65  ASN A ND2  1 
ATOM   1277 H  H    . ASN A 1 65  ? -5.41900  -11.32500 10.54400  1.000 22.78000  ? 65  ASN A H    1 
ATOM   1278 H  HA   . ASN A 1 65  ? -7.77800  -11.93900 11.70400  1.000 23.47000  ? 65  ASN A HA   1 
ATOM   1279 H  HB2  . ASN A 1 65  ? -6.45900  -10.52000 13.03400  1.000 26.44000  ? 65  ASN A HB2  1 
ATOM   1280 H  HB3  . ASN A 1 65  ? -6.33700  -9.48700  11.83400  1.000 26.44000  ? 65  ASN A HB3  1 
ATOM   1281 H  HD21 . ASN A 1 65  ? -7.56500  -7.73100  12.12100  1.000 42.15000  ? 65  ASN A HD21 1 
ATOM   1282 H  HD22 . ASN A 1 65  ? -8.89700  -7.68700  12.78600  1.000 42.15000  ? 65  ASN A HD22 1 
ATOM   1283 N  N    . ASP A 1 66  ? -9.33000  -11.09800 10.02800  1.000 18.22000  ? 66  ASP A N    1 
ATOM   1284 C  CA   . ASP A 1 66  ? -10.27300 -10.49400 9.10600   1.000 19.26000  ? 66  ASP A CA   1 
ATOM   1285 C  C    . ASP A 1 66  ? -11.45800 -9.83600  9.79500   1.000 20.76000  ? 66  ASP A C    1 
ATOM   1286 O  O    . ASP A 1 66  ? -12.35300 -9.37600  9.09100   1.000 21.22000  ? 66  ASP A O    1 
ATOM   1287 C  CB   . ASP A 1 66  ? -10.73800 -11.48400 8.03000   1.000 19.65000  ? 66  ASP A CB   1 
ATOM   1288 C  CG   . ASP A 1 66  ? -11.50300 -12.66000 8.55300   1.000 17.96000  ? 66  ASP A CG   1 
ATOM   1289 O  OD1  . ASP A 1 66  ? -11.88500 -12.74300 9.75600   1.000 19.33000  ? 66  ASP A OD1  1 
ATOM   1290 O  OD2  . ASP A 1 66  ? -11.81200 -13.54100 7.74700   1.000 17.78000  ? 66  ASP A OD2  1 
ATOM   1291 H  H    . ASP A 1 66  ? -9.65000  -11.76000 10.47400  1.000 21.89000  ? 66  ASP A H    1 
ATOM   1292 H  HA   . ASP A 1 66  ? -9.80500  -9.79500  8.62300   1.000 23.14000  ? 66  ASP A HA   1 
ATOM   1293 H  HB2  . ASP A 1 66  ? -11.31400 -11.01400 7.40700   1.000 23.60000  ? 66  ASP A HB2  1 
ATOM   1294 H  HB3  . ASP A 1 66  ? -9.95700  -11.82600 7.56700   1.000 23.60000  ? 66  ASP A HB3  1 
ATOM   1295 N  N    . GLY A 1 67  ? -11.49900 -9.79000  11.11800  1.000 20.68000  ? 67  GLY A N    1 
ATOM   1296 C  CA   . GLY A 1 67  ? -12.57300 -9.10000  11.83200  1.000 21.95000  ? 67  GLY A CA   1 
ATOM   1297 C  C    . GLY A 1 67  ? -13.89800 -9.80200  11.86400  1.000 28.04000  ? 67  GLY A C    1 
ATOM   1298 O  O    . GLY A 1 67  ? -14.86600 -9.23600  12.41000  1.000 28.67000  ? 67  GLY A O    1 
ATOM   1299 H  H    . GLY A 1 67  ? -10.91300 -10.15300 11.63300  1.000 24.84000  ? 67  GLY A H    1 
ATOM   1300 H  HA2  . GLY A 1 67  ? -12.29200 -8.96500  12.75100  1.000 26.36000  ? 67  GLY A HA2  1 
ATOM   1301 H  HA3  . GLY A 1 67  ? -12.71100 -8.23500  11.41500  1.000 26.36000  ? 67  GLY A HA3  1 
ATOM   1302 N  N    A ARG A 1 68  ? -13.99700 -11.01400 11.31700  0.630 20.89000  ? 68  ARG A N    1 
ATOM   1303 N  N    B ARG A 1 68  ? -13.99500 -11.01400 11.30900  0.370 21.03000  ? 68  ARG A N    1 
ATOM   1304 C  CA   A ARG A 1 68  ? -15.27000 -11.70700 11.25900  0.630 21.11000  ? 68  ARG A CA   1 
ATOM   1305 C  CA   B ARG A 1 68  ? -15.26600 -11.71400 11.22100  0.370 21.00000  ? 68  ARG A CA   1 
ATOM   1306 C  C    A ARG A 1 68  ? -15.14300 -13.21000 11.46800  0.630 24.87000  ? 68  ARG A C    1 
ATOM   1307 C  C    B ARG A 1 68  ? -15.13000 -13.21600 11.44100  0.370 24.79000  ? 68  ARG A C    1 
ATOM   1308 O  O    A ARG A 1 68  ? -15.97400 -13.97900 10.97300  0.630 27.92000  ? 68  ARG A O    1 
ATOM   1309 O  O    B ARG A 1 68  ? -15.93900 -13.99500 10.92500  0.370 27.64000  ? 68  ARG A O    1 
ATOM   1310 C  CB   A ARG A 1 68  ? -15.94900 -11.41000 9.93900   0.630 22.47000  ? 68  ARG A CB   1 
ATOM   1311 C  CB   B ARG A 1 68  ? -15.93100 -11.43900 9.87600   0.370 22.72000  ? 68  ARG A CB   1 
ATOM   1312 C  CG   A ARG A 1 68  ? -15.15700 -11.91700 8.73600   0.630 21.97000  ? 68  ARG A CG   1 
ATOM   1313 C  CG   B ARG A 1 68  ? -15.11200 -11.91600 8.66800   0.370 21.97000  ? 68  ARG A CG   1 
ATOM   1314 C  CD   A ARG A 1 68  ? -16.09000 -12.02600 7.55000   0.630 28.80000  ? 68  ARG A CD   1 
ATOM   1315 C  CD   B ARG A 1 68  ? -16.03600 -12.43400 7.56300   0.370 29.80000  ? 68  ARG A CD   1 
ATOM   1316 N  NE   A ARG A 1 68  ? -15.69000 -13.02700 6.57500   0.630 20.95000  ? 68  ARG A NE   1 
ATOM   1317 N  NE   B ARG A 1 68  ? -16.48200 -13.79100 7.84800   0.370 30.55000  ? 68  ARG A NE   1 
ATOM   1318 C  CZ   A ARG A 1 68  ? -16.16700 -13.05600 5.33900   0.630 22.01000  ? 68  ARG A CZ   1 
ATOM   1319 C  CZ   B ARG A 1 68  ? -17.61000 -14.32600 7.40200   0.370 35.29000  ? 68  ARG A CZ   1 
ATOM   1320 N  NH1  A ARG A 1 68  ? -17.05900 -12.17400 4.94200   0.630 23.35000  ? 68  ARG A NH1  1 
ATOM   1321 N  NH1  B ARG A 1 68  ? -18.45300 -13.63700 6.65600   0.370 36.69000  ? 68  ARG A NH1  1 
ATOM   1322 N  NH2  A ARG A 1 68  ? -15.73300 -13.98600 4.48100   0.630 19.67000  ? 68  ARG A NH2  1 
ATOM   1323 N  NH2  B ARG A 1 68  ? -17.91100 -15.57500 7.73300   0.370 22.37000  ? 68  ARG A NH2  1 
ATOM   1324 H  H    A ARG A 1 68  ? -13.33900 -11.45000 10.97600  0.630 25.09000  ? 68  ARG A H    1 
ATOM   1325 H  H    B ARG A 1 68  ? -13.33200 -11.44900 10.97600  0.370 25.25000  ? 68  ARG A H    1 
ATOM   1326 H  HA   A ARG A 1 68  ? -15.82600 -11.38800 11.98700  0.630 25.36000  ? 68  ARG A HA   1 
ATOM   1327 H  HA   B ARG A 1 68  ? -15.84000 -11.38400 11.93100  0.370 25.22000  ? 68  ARG A HA   1 
ATOM   1328 H  HB2  A ARG A 1 68  ? -16.81900 -11.84100 9.92800   0.630 26.98000  ? 68  ARG A HB2  1 
ATOM   1329 H  HB2  B ARG A 1 68  ? -16.78600 -11.89500 9.85300   0.370 27.28000  ? 68  ARG A HB2  1 
ATOM   1330 H  HB3  A ARG A 1 68  ? -16.05400 -10.45000 9.84700   0.630 26.98000  ? 68  ARG A HB3  1 
ATOM   1331 H  HB3  B ARG A 1 68  ? -16.06300 -10.48200 9.78500   0.370 27.28000  ? 68  ARG A HB3  1 
ATOM   1332 H  HG2  A ARG A 1 68  ? -14.44500 -11.29300 8.52200   0.630 26.38000  ? 68  ARG A HG2  1 
ATOM   1333 H  HG2  B ARG A 1 68  ? -14.59300 -11.17700 8.31500   0.370 26.39000  ? 68  ARG A HG2  1 
ATOM   1334 H  HG3  A ARG A 1 68  ? -14.78500 -12.79200 8.92800   0.630 26.38000  ? 68  ARG A HG3  1 
ATOM   1335 H  HG3  B ARG A 1 68  ? -14.52200 -12.63700 8.93900   0.370 26.39000  ? 68  ARG A HG3  1 
ATOM   1336 H  HD2  A ARG A 1 68  ? -16.97400 -12.26400 7.87000   0.630 34.58000  ? 68  ARG A HD2  1 
ATOM   1337 H  HD2  B ARG A 1 68  ? -16.81600 -11.86100 7.49900   0.370 35.78000  ? 68  ARG A HD2  1 
ATOM   1338 H  HD3  A ARG A 1 68  ? -16.12100 -11.16900 7.09700   0.630 34.58000  ? 68  ARG A HD3  1 
ATOM   1339 H  HD3  B ARG A 1 68  ? -15.55800 -12.43900 6.71900   0.370 35.78000  ? 68  ARG A HD3  1 
ATOM   1340 H  HE   A ARG A 1 68  ? -15.11900 -13.62500 6.81000   0.630 25.16000  ? 68  ARG A HE   1 
ATOM   1341 H  HE   B ARG A 1 68  ? -15.97700 -14.28100 8.34300   0.370 36.68000  ? 68  ARG A HE   1 
ATOM   1342 H  HH11 A ARG A 1 68  ? -17.33900 -11.57000 5.48600   0.630 28.03000  ? 68  ARG A HH11 1 
ATOM   1343 H  HH11 B ARG A 1 68  ? -18.27700 -12.82100 6.44900   0.370 44.05000  ? 68  ARG A HH11 1 
ATOM   1344 H  HH12 A ARG A 1 68  ? -17.36200 -12.20200 4.13700   0.630 28.03000  ? 68  ARG A HH12 1 
ATOM   1345 H  HH12 B ARG A 1 68  ? -19.17900 -14.00400 6.37700   0.370 44.05000  ? 68  ARG A HH12 1 
ATOM   1346 H  HH21 A ARG A 1 68  ? -15.14700 -14.56300 4.73200   0.630 23.63000  ? 68  ARG A HH21 1 
ATOM   1347 H  HH21 B ARG A 1 68  ? -17.37700 -16.02800 8.23300   0.370 26.87000  ? 68  ARG A HH21 1 
ATOM   1348 H  HH22 A ARG A 1 68  ? -16.04100 -14.00800 3.67800   0.630 23.63000  ? 68  ARG A HH22 1 
ATOM   1349 H  HH22 B ARG A 1 68  ? -18.64000 -15.93200 7.44900   0.370 26.87000  ? 68  ARG A HH22 1 
ATOM   1350 N  N    . THR A 1 69  ? -14.11800 -13.64900 12.19300  1.000 21.50000  ? 69  THR A N    1 
ATOM   1351 C  CA   . THR A 1 69  ? -13.92500 -15.06000 12.50600  1.000 20.91000  ? 69  THR A CA   1 
ATOM   1352 C  C    . THR A 1 69  ? -13.88500 -15.20000 14.02100  1.000 21.40000  ? 69  THR A C    1 
ATOM   1353 O  O    . THR A 1 69  ? -12.81000 -15.18400 14.62300  1.000 24.49000  ? 69  THR A O    1 
ATOM   1354 C  CB   . THR A 1 69  ? -12.65800 -15.62000 11.85000  1.000 20.70000  ? 69  THR A CB   1 
ATOM   1355 O  OG1  . THR A 1 69  ? -12.64900 -15.26300 10.45400  1.000 20.60000  ? 69  THR A OG1  1 
ATOM   1356 C  CG2  . THR A 1 69  ? -12.65100 -17.12600 11.98300  1.000 21.65000  ? 69  THR A CG2  1 
ATOM   1357 H  H    . THR A 1 69  ? -13.50700 -13.14000 12.52100  1.000 25.83000  ? 69  THR A H    1 
ATOM   1358 H  HA   . THR A 1 69  ? -14.67900 -15.57100 12.17200  1.000 25.11000  ? 69  THR A HA   1 
ATOM   1359 H  HB   . THR A 1 69  ? -11.86500 -15.26000 12.27800  1.000 24.86000  ? 69  THR A HB   1 
ATOM   1360 H  HG1  . THR A 1 69  ? -13.34100 -15.55400 10.07800  1.000 24.75000  ? 69  THR A HG1  1 
ATOM   1361 H  HG21 . THR A 1 69  ? -11.80900 -17.48300 11.66000  1.000 26.00000  ? 69  THR A HG21 1 
ATOM   1362 H  HG22 . THR A 1 69  ? -12.76400 -17.37700 12.91400  1.000 26.00000  ? 69  THR A HG22 1 
ATOM   1363 H  HG23 . THR A 1 69  ? -13.37600 -17.50800 11.46400  1.000 26.00000  ? 69  THR A HG23 1 
ATOM   1364 N  N    . PRO A 1 70  ? -15.04300 -15.30200 14.66900  1.000 23.26000  ? 70  PRO A N    1 
ATOM   1365 C  CA   . PRO A 1 70  ? -15.05400 -15.28500 16.13800  1.000 26.38000  ? 70  PRO A CA   1 
ATOM   1366 C  C    . PRO A 1 70  ? -14.27600 -16.43100 16.74400  1.000 25.54000  ? 70  PRO A C    1 
ATOM   1367 O  O    . PRO A 1 70  ? -14.34500 -17.57200 16.28600  1.000 32.33000  ? 70  PRO A O    1 
ATOM   1368 C  CB   . PRO A 1 70  ? -16.54600 -15.36500 16.48200  1.000 29.96000  ? 70  PRO A CB   1 
ATOM   1369 C  CG   . PRO A 1 70  ? -17.23000 -14.79400 15.30600  1.000 33.50000  ? 70  PRO A CG   1 
ATOM   1370 C  CD   . PRO A 1 70  ? -16.40700 -15.27000 14.12000  1.000 26.99000  ? 70  PRO A CD   1 
ATOM   1371 H  HA   . PRO A 1 70  ? -14.68000 -14.45000 16.46100  1.000 31.68000  ? 70  PRO A HA   1 
ATOM   1372 H  HB2  . PRO A 1 70  ? -16.80600 -16.28900 16.62200  1.000 35.97000  ? 70  PRO A HB2  1 
ATOM   1373 H  HB3  . PRO A 1 70  ? -16.73100 -14.84400 17.28000  1.000 35.97000  ? 70  PRO A HB3  1 
ATOM   1374 H  HG2  . PRO A 1 70  ? -18.14000 -15.12700 15.25600  1.000 40.23000  ? 70  PRO A HG2  1 
ATOM   1375 H  HG3  . PRO A 1 70  ? -17.23400 -13.82500 15.36200  1.000 40.23000  ? 70  PRO A HG3  1 
ATOM   1376 H  HD2  . PRO A 1 70  ? -16.68800 -16.15400 13.83400  1.000 32.41000  ? 70  PRO A HD2  1 
ATOM   1377 H  HD3  . PRO A 1 70  ? -16.47000 -14.64600 13.38000  1.000 32.41000  ? 70  PRO A HD3  1 
ATOM   1378 N  N    . GLY A 1 71  ? -13.52700 -16.10000 17.79700  1.000 27.32000  ? 71  GLY A N    1 
ATOM   1379 C  CA   . GLY A 1 71  ? -12.77500 -17.10400 18.51500  1.000 39.40000  ? 71  GLY A CA   1 
ATOM   1380 C  C    . GLY A 1 71  ? -11.56400 -17.59100 17.77100  1.000 45.63000  ? 71  GLY A C    1 
ATOM   1381 O  O    . GLY A 1 71  ? -11.08500 -18.69700 18.03300  1.000 54.18000  ? 71  GLY A O    1 
ATOM   1382 H  H    . GLY A 1 71  ? -13.44200 -15.30200 18.10800  1.000 32.80000  ? 71  GLY A H    1 
ATOM   1383 H  HA2  . GLY A 1 71  ? -12.48100 -16.73300 19.36200  1.000 47.30000  ? 71  GLY A HA2  1 
ATOM   1384 H  HA3  . GLY A 1 71  ? -13.35000 -17.86600 18.68700  1.000 47.30000  ? 71  GLY A HA3  1 
ATOM   1385 N  N    . SER A 1 72  ? -11.06300 -16.80000 16.83200  1.000 28.96000  ? 72  SER A N    1 
ATOM   1386 C  CA   . SER A 1 72  ? -9.90700  -17.19200 16.05000  1.000 24.14000  ? 72  SER A CA   1 
ATOM   1387 C  C    . SER A 1 72  ? -8.64200  -16.53400 16.58900  1.000 33.98000  ? 72  SER A C    1 
ATOM   1388 O  O    . SER A 1 72  ? -8.66800  -15.65800 17.46900  1.000 32.54000  ? 72  SER A O    1 
ATOM   1389 C  CB   . SER A 1 72  ? -10.14200 -16.80400 14.58400  1.000 23.96000  ? 72  SER A CB   1 
ATOM   1390 O  OG   . SER A 1 72  ? -9.97800  -15.41500 14.45100  1.000 25.17000  ? 72  SER A OG   1 
ATOM   1391 H  H    . SER A 1 72  ? -11.38000 -16.02700 16.63000  1.000 34.77000  ? 72  SER A H    1 
ATOM   1392 H  HA   . SER A 1 72  ? -9.77800  -18.15200 16.10500  1.000 28.99000  ? 72  SER A HA   1 
ATOM   1393 H  HB2  . SER A 1 72  ? -9.49800  -17.26100 14.02100  1.000 28.77000  ? 72  SER A HB2  1 
ATOM   1394 H  HB3  . SER A 1 72  ? -11.04400 -17.04900 14.32400  1.000 28.77000  ? 72  SER A HB3  1 
ATOM   1395 H  HG   . SER A 1 72  ? -10.50000 -15.12000 13.86300  1.000 30.22000  ? 72  SER A HG   1 
ATOM   1396 N  N    . ARG A 1 73  ? -7.51200  -16.99200 16.06400  1.000 24.46000  ? 73  ARG A N    1 
ATOM   1397 C  CA   . ARG A 1 73  ? -6.23100  -16.38200 16.34800  1.000 26.64000  ? 73  ARG A CA   1 
ATOM   1398 C  C    . ARG A 1 73  ? -5.70200  -15.67200 15.11000  1.000 27.73000  ? 73  ARG A C    1 
ATOM   1399 O  O    . ARG A 1 73  ? -6.28400  -15.73900 14.01900  1.000 25.34000  ? 73  ARG A O    1 
ATOM   1400 C  CB   . ARG A 1 73  ? -5.22200  -17.43600 16.81800  1.000 27.59000  ? 73  ARG A CB   1 
ATOM   1401 C  CG   . ARG A 1 73  ? -5.73700  -18.29900 17.99000  1.000 36.49000  ? 73  ARG A CG   1 
ATOM   1402 C  CD   . ARG A 1 73  ? -5.82800  -17.48800 19.27600  1.000 44.19000  ? 73  ARG A CD   1 
ATOM   1403 N  NE   . ARG A 1 73  ? -4.52000  -16.97200 19.66300  1.000 70.91000  ? 73  ARG A NE   1 
ATOM   1404 C  CZ   . ARG A 1 73  ? -3.68000  -17.59600 20.48000  1.000 67.03000  ? 73  ARG A CZ   1 
ATOM   1405 N  NH1  . ARG A 1 73  ? -4.00400  -18.73600 21.06700  1.000 57.01000  ? 73  ARG A NH1  1 
ATOM   1406 N  NH2  . ARG A 1 73  ? -2.48200  -17.06600 20.70800  1.000 50.23000  ? 73  ARG A NH2  1 
ATOM   1407 H  H    . ARG A 1 73  ? -7.46800  -17.66600 15.53100  1.000 29.37000  ? 73  ARG A H    1 
ATOM   1408 H  HA   . ARG A 1 73  ? -6.34300  -15.72600 17.05400  1.000 31.99000  ? 73  ARG A HA   1 
ATOM   1409 H  HB2  . ARG A 1 73  ? -5.02100  -18.02900 16.07800  1.000 33.12000  ? 73  ARG A HB2  1 
ATOM   1410 H  HB3  . ARG A 1 73  ? -4.41400  -16.98700 17.11300  1.000 33.12000  ? 73  ARG A HB3  1 
ATOM   1411 H  HG2  . ARG A 1 73  ? -6.62200  -18.63500 17.77700  1.000 43.81000  ? 73  ARG A HG2  1 
ATOM   1412 H  HG3  . ARG A 1 73  ? -5.12700  -19.03800 18.13700  1.000 43.81000  ? 73  ARG A HG3  1 
ATOM   1413 H  HD2  . ARG A 1 73  ? -6.42700  -16.73600 19.14300  1.000 53.05000  ? 73  ARG A HD2  1 
ATOM   1414 H  HD3  . ARG A 1 73  ? -6.15900  -18.05300 19.99200  1.000 53.05000  ? 73  ARG A HD3  1 
ATOM   1415 H  HE   . ARG A 1 73  ? -4.27600  -16.21300 19.34000  1.000 85.11000  ? 73  ARG A HE   1 
ATOM   1416 H  HH11 . ARG A 1 73  ? -4.77400  -19.09000 20.92300  1.000 68.44000  ? 73  ARG A HH11 1 
ATOM   1417 H  HH12 . ARG A 1 73  ? -3.44400  -19.12400 21.59300  1.000 68.44000  ? 73  ARG A HH12 1 
ATOM   1418 H  HH21 . ARG A 1 73  ? -2.25900  -16.32800 20.32700  1.000 60.29000  ? 73  ARG A HH21 1 
ATOM   1419 H  HH22 . ARG A 1 73  ? -1.93000  -17.46200 21.23500  1.000 60.29000  ? 73  ARG A HH22 1 
ATOM   1420 N  N    . ASN A 1 74  ? -4.58300  -14.99000 15.29400  1.000 23.35000  ? 74  ASN A N    1 
ATOM   1421 C  CA   . ASN A 1 74  ? -3.89400  -14.19000 14.29500  1.000 22.10000  ? 74  ASN A CA   1 
ATOM   1422 C  C    . ASN A 1 74  ? -2.38800  -14.42400 14.50800  1.000 23.48000  ? 74  ASN A C    1 
ATOM   1423 O  O    . ASN A 1 74  ? -1.61800  -13.52500 14.79200  1.000 24.31000  ? 74  ASN A O    1 
ATOM   1424 C  CB   . ASN A 1 74  ? -4.25100  -12.70400 14.42800  1.000 24.53000  ? 74  ASN A CB   1 
ATOM   1425 C  CG   . ASN A 1 74  ? -3.53000  -11.82300 13.43600  1.000 26.67000  ? 74  ASN A CG   1 
ATOM   1426 O  OD1  . ASN A 1 74  ? -2.92700  -12.29200 12.47400  1.000 24.21000  ? 74  ASN A OD1  1 
ATOM   1427 N  ND2  . ASN A 1 74  ? -3.59900  -10.51900 13.65200  1.000 29.24000  ? 74  ASN A ND2  1 
ATOM   1428 H  H    . ASN A 1 74  ? -4.17100  -14.97400 16.04900  1.000 28.04000  ? 74  ASN A H    1 
ATOM   1429 H  HA   . ASN A 1 74  ? -4.14400  -14.47600 13.40300  1.000 26.54000  ? 74  ASN A HA   1 
ATOM   1430 H  HB2  . ASN A 1 74  ? -5.20400  -12.59600 14.28300  1.000 29.46000  ? 74  ASN A HB2  1 
ATOM   1431 H  HB3  . ASN A 1 74  ? -4.01500  -12.40300 15.31900  1.000 29.46000  ? 74  ASN A HB3  1 
ATOM   1432 H  HD21 . ASN A 1 74  ? -3.20500  -9.97300  13.11600  1.000 35.11000  ? 74  ASN A HD21 1 
ATOM   1433 H  HD22 . ASN A 1 74  ? -4.03700  -10.21700 14.32800  1.000 35.11000  ? 74  ASN A HD22 1 
ATOM   1434 N  N    . LEU A 1 75  ? -1.94500  -15.66300 14.28000  1.000 24.36000  ? 75  LEU A N    1 
ATOM   1435 C  CA   . LEU A 1 75  ? -0.57000  -16.02500 14.63300  1.000 22.98000  ? 75  LEU A CA   1 
ATOM   1436 C  C    . LEU A 1 75  ? 0.48100   -15.43500 13.69000  1.000 24.73000  ? 75  LEU A C    1 
ATOM   1437 O  O    . LEU A 1 75  ? 1.66200   -15.39000 14.05600  1.000 29.69000  ? 75  LEU A O    1 
ATOM   1438 C  CB   . LEU A 1 75  ? -0.48400  -17.54300 14.62200  1.000 26.92000  ? 75  LEU A CB   1 
ATOM   1439 C  CG   . LEU A 1 75  ? -1.26900  -18.23200 15.72100  1.000 30.66000  ? 75  LEU A CG   1 
ATOM   1440 C  CD1  . LEU A 1 75  ? -1.01700  -19.72100 15.71400  1.000 32.17000  ? 75  LEU A CD1  1 
ATOM   1441 C  CD2  . LEU A 1 75  ? -0.94800  -17.64900 17.12200  1.000 41.16000  ? 75  LEU A CD2  1 
ATOM   1442 H  H    . LEU A 1 75  ? -2.40800  -16.29700 13.93000  1.000 29.25000  ? 75  LEU A H    1 
ATOM   1443 H  HA   . LEU A 1 75  ? -0.35900  -15.68200 15.51500  1.000 27.59000  ? 75  LEU A HA   1 
ATOM   1444 H  HB2  . LEU A 1 75  ? -0.82700  -17.86400 13.77300  1.000 32.33000  ? 75  LEU A HB2  1 
ATOM   1445 H  HB3  . LEU A 1 75  ? 0.44600   -17.79900 14.72300  1.000 32.33000  ? 75  LEU A HB3  1 
ATOM   1446 H  HG   . LEU A 1 75  ? -2.21000  -18.07400 15.54600  1.000 36.81000  ? 75  LEU A HG   1 
ATOM   1447 H  HD11 . LEU A 1 75  ? -1.52900  -20.13100 16.42900  1.000 38.62000  ? 75  LEU A HD11 1 
ATOM   1448 H  HD12 . LEU A 1 75  ? -1.29500  -20.08400 14.85800  1.000 38.62000  ? 75  LEU A HD12 1 
ATOM   1449 H  HD13 . LEU A 1 75  ? -0.07100  -19.88200 15.85000  1.000 38.62000  ? 75  LEU A HD13 1 
ATOM   1450 H  HD21 . LEU A 1 75  ? -1.43900  -18.14900 17.79200  1.000 49.41000  ? 75  LEU A HD21 1 
ATOM   1451 H  HD22 . LEU A 1 75  ? 0.00500   -17.72400 17.28500  1.000 49.41000  ? 75  LEU A HD22 1 
ATOM   1452 H  HD23 . LEU A 1 75  ? -1.21500  -16.71600 17.14400  1.000 49.41000  ? 75  LEU A HD23 1 
ATOM   1453 N  N    . CYS A 1 76  ? 0.12000   -14.99500 12.47200  1.000 21.54000  ? 76  CYS A N    1 
ATOM   1454 C  CA   . CYS A 1 76  ? 1.05300   -14.27600 11.62000  1.000 21.36000  ? 76  CYS A CA   1 
ATOM   1455 C  C    . CYS A 1 76  ? 1.03200   -12.77900 11.86200  1.000 21.42000  ? 76  CYS A C    1 
ATOM   1456 O  O    . CYS A 1 76  ? 1.82800   -12.04600 11.26000  1.000 24.74000  ? 76  CYS A O    1 
ATOM   1457 C  CB   . CYS A 1 76  ? 0.78100   -14.58600 10.13600  1.000 21.57000  ? 76  CYS A CB   1 
ATOM   1458 S  SG   . CYS A 1 76  ? 1.27800   -16.29200 9.75400   1.000 22.49000  ? 76  CYS A SG   1 
ATOM   1459 H  H    . CYS A 1 76  ? -0.66100  -15.10600 12.12800  1.000 25.87000  ? 76  CYS A H    1 
ATOM   1460 H  HA   . CYS A 1 76  ? 1.95100   -14.58800 11.80900  1.000 25.65000  ? 76  CYS A HA   1 
ATOM   1461 H  HB2  . CYS A 1 76  ? -0.16700  -14.48900 9.95200   1.000 25.90000  ? 76  CYS A HB2  1 
ATOM   1462 H  HB3  . CYS A 1 76  ? 1.29100   -13.98000 9.57800   1.000 25.90000  ? 76  CYS A HB3  1 
ATOM   1463 N  N    A ASN A 1 77  ? 0.10700   -12.31300 12.70300  0.590 24.33000  ? 77  ASN A N    1 
ATOM   1464 N  N    B ASN A 1 77  ? 0.12700   -12.31000 12.72200  0.410 24.54000  ? 77  ASN A N    1 
ATOM   1465 C  CA   A ASN A 1 77  ? 0.02800   -10.91300 13.12600  0.590 28.30000  ? 77  ASN A CA   1 
ATOM   1466 C  CA   B ASN A 1 77  ? 0.03900   -10.90200 13.11500  0.410 28.26000  ? 77  ASN A CA   1 
ATOM   1467 C  C    A ASN A 1 77  ? -0.13700  -9.96700  11.93600  0.590 27.33000  ? 77  ASN A C    1 
ATOM   1468 C  C    B ASN A 1 77  ? -0.11600  -9.98000  11.90800  0.410 27.44000  ? 77  ASN A C    1 
ATOM   1469 O  O    A ASN A 1 77  ? 0.59000   -8.98600  11.78000  0.590 28.63000  ? 77  ASN A O    1 
ATOM   1470 O  O    B ASN A 1 77  ? 0.64400   -9.02900  11.71300  0.410 28.80000  ? 77  ASN A O    1 
ATOM   1471 C  CB   A ASN A 1 77  ? 1.22900   -10.52400 13.99800  0.590 30.96000  ? 77  ASN A CB   1 
ATOM   1472 C  CB   B ASN A 1 77  ? 1.22600   -10.47500 13.98000  0.410 31.05000  ? 77  ASN A CB   1 
ATOM   1473 C  CG   A ASN A 1 77  ? 1.38100   -11.41400 15.22600  0.590 37.64000  ? 77  ASN A CG   1 
ATOM   1474 C  CG   B ASN A 1 77  ? 0.98800   -9.14200  14.66500  0.410 34.23000  ? 77  ASN A CG   1 
ATOM   1475 O  OD1  A ASN A 1 77  ? 2.36000   -12.15100 15.35300  0.590 49.23000  ? 77  ASN A OD1  1 
ATOM   1476 O  OD1  B ASN A 1 77  ? -0.08800  -8.89800  15.20900  0.410 42.44000  ? 77  ASN A OD1  1 
ATOM   1477 N  ND2  A ASN A 1 77  ? 0.41300   -11.34500 16.13600  0.590 46.88000  ? 77  ASN A ND2  1 
ATOM   1478 N  ND2  B ASN A 1 77  ? 1.98500   -8.26500  14.62100  0.410 36.27000  ? 77  ASN A ND2  1 
ATOM   1479 H  H    A ASN A 1 77  ? -0.50600  -12.80400 13.05400  0.590 29.22000  ? 77  ASN A H    1 
ATOM   1480 H  H    B ASN A 1 77  ? -0.46500  -12.80300 13.10300  0.410 29.47000  ? 77  ASN A H    1 
ATOM   1481 H  HA   A ASN A 1 77  ? -0.77000  -10.81300 13.67000  0.590 33.98000  ? 77  ASN A HA   1 
ATOM   1482 H  HA   B ASN A 1 77  ? -0.76300  -10.80800 13.65200  0.410 33.93000  ? 77  ASN A HA   1 
ATOM   1483 H  HB2  A ASN A 1 77  ? 2.04000   -10.60100 13.47100  0.590 37.18000  ? 77  ASN A HB2  1 
ATOM   1484 H  HB2  B ASN A 1 77  ? 1.37700   -11.14400 14.66600  0.410 37.28000  ? 77  ASN A HB2  1 
ATOM   1485 H  HB3  A ASN A 1 77  ? 1.11600   -9.61000  14.30200  0.590 37.18000  ? 77  ASN A HB3  1 
ATOM   1486 H  HB3  B ASN A 1 77  ? 2.01400   -10.39000 13.42000  0.410 37.28000  ? 77  ASN A HB3  1 
ATOM   1487 H  HD21 A ASN A 1 77  ? -0.25500  -10.81700 16.01400  0.590 56.28000  ? 77  ASN A HD21 1 
ATOM   1488 H  HD21 B ASN A 1 77  ? 2.71800   -8.46600  14.21900  0.410 43.54000  ? 77  ASN A HD21 1 
ATOM   1489 H  HD22 A ASN A 1 77  ? 0.45500   -11.82800 16.84600  0.590 56.28000  ? 77  ASN A HD22 1 
ATOM   1490 H  HD22 B ASN A 1 77  ? 1.89700   -7.49500  14.99500  0.410 43.54000  ? 77  ASN A HD22 1 
ATOM   1491 N  N    . ILE A 1 78  ? -1.11600  -10.27500 11.08300  1.000 24.43000  ? 78  ILE A N    1 
ATOM   1492 C  CA   . ILE A 1 78  ? -1.36300  -9.49400  9.88300   1.000 24.58000  ? 78  ILE A CA   1 
ATOM   1493 C  C    . ILE A 1 78  ? -2.85500  -9.46200  9.59600   1.000 19.56000  ? 78  ILE A C    1 
ATOM   1494 O  O    . ILE A 1 78  ? -3.56700  -10.42100 9.91000   1.000 21.73000  ? 78  ILE A O    1 
ATOM   1495 C  CB   . ILE A 1 78  ? -0.69300  -10.09400 8.62800   1.000 25.02000  ? 78  ILE A CB   1 
ATOM   1496 C  CG1  . ILE A 1 78  ? -0.96100  -11.59400 8.53500   1.000 25.23000  ? 78  ILE A CG1  1 
ATOM   1497 C  CG2  . ILE A 1 78  ? 0.79300   -9.76200  8.59900   1.000 38.41000  ? 78  ILE A CG2  1 
ATOM   1498 C  CD1  . ILE A 1 78  ? -0.66600  -12.17300 7.14900   1.000 33.34000  ? 78  ILE A CD1  1 
ATOM   1499 H  H    . ILE A 1 78  ? -1.65400  -10.93800 11.18300  1.000 29.34000  ? 78  ILE A H    1 
ATOM   1500 H  HA   . ILE A 1 78  ? -1.01200  -8.60800  10.06600  1.000 29.52000  ? 78  ILE A HA   1 
ATOM   1501 H  HB   . ILE A 1 78  ? -1.09000  -9.68900  7.84200   1.000 30.04000  ? 78  ILE A HB   1 
ATOM   1502 H  HG12 . ILE A 1 78  ? -0.39800  -12.05500 9.17600   1.000 30.30000  ? 78  ILE A HG12 1 
ATOM   1503 H  HG13 . ILE A 1 78  ? -1.89500  -11.76000 8.73400   1.000 30.30000  ? 78  ILE A HG13 1 
ATOM   1504 H  HG21 . ILE A 1 78  ? 1.18600   -10.14200 7.79800   1.000 46.12000  ? 78  ILE A HG21 1 
ATOM   1505 H  HG22 . ILE A 1 78  ? 0.90100   -8.79800  8.59600   1.000 46.12000  ? 78  ILE A HG22 1 
ATOM   1506 H  HG23 . ILE A 1 78  ? 1.21600   -10.13900 9.38600   1.000 46.12000  ? 78  ILE A HG23 1 
ATOM   1507 H  HD11 . ILE A 1 78  ? -0.85700  -13.12400 7.15700   1.000 40.03000  ? 78  ILE A HD11 1 
ATOM   1508 H  HD12 . ILE A 1 78  ? -1.22700  -11.72800 6.49500   1.000 40.03000  ? 78  ILE A HD12 1 
ATOM   1509 H  HD13 . ILE A 1 78  ? 0.26900   -12.02500 6.93800   1.000 40.03000  ? 78  ILE A HD13 1 
ATOM   1510 N  N    . PRO A 1 79  ? -3.34500  -8.39700  8.97500   1.000 21.86000  ? 79  PRO A N    1 
ATOM   1511 C  CA   . PRO A 1 79  ? -4.69400  -8.43100  8.41100   1.000 19.86000  ? 79  PRO A CA   1 
ATOM   1512 C  C    . PRO A 1 79  ? -4.71100  -9.39600  7.24100   1.000 18.84000  ? 79  PRO A C    1 
ATOM   1513 O  O    . PRO A 1 79  ? -3.77600  -9.44600  6.43700   1.000 20.86000  ? 79  PRO A O    1 
ATOM   1514 C  CB   . PRO A 1 79  ? -4.92900  -6.98000  7.96800   1.000 23.22000  ? 79  PRO A CB   1 
ATOM   1515 C  CG   . PRO A 1 79  ? -3.59900  -6.41300  7.77500   1.000 33.36000  ? 79  PRO A CG   1 
ATOM   1516 C  CD   . PRO A 1 79  ? -2.64300  -7.14100  8.67700   1.000 24.23000  ? 79  PRO A CD   1 
ATOM   1517 H  HA   . PRO A 1 79  ? -5.37000  -8.66900  9.06400   1.000 23.85000  ? 79  PRO A HA   1 
ATOM   1518 H  HB2  . PRO A 1 79  ? -5.43400  -6.96800  7.14000   1.000 27.89000  ? 79  PRO A HB2  1 
ATOM   1519 H  HB3  . PRO A 1 79  ? -5.41300  -6.50000  8.65900   1.000 27.89000  ? 79  PRO A HB3  1 
ATOM   1520 H  HG2  . PRO A 1 79  ? -3.33700  -6.52600  6.84800   1.000 40.05000  ? 79  PRO A HG2  1 
ATOM   1521 H  HG3  . PRO A 1 79  ? -3.62000  -5.47000  8.00100   1.000 40.05000  ? 79  PRO A HG3  1 
ATOM   1522 H  HD2  . PRO A 1 79  ? -1.80500  -7.31500  8.22100   1.000 29.10000  ? 79  PRO A HD2  1 
ATOM   1523 H  HD3  . PRO A 1 79  ? -2.48200  -6.63500  9.48800   1.000 29.10000  ? 79  PRO A HD3  1 
ATOM   1524 N  N    . CYS A 1 80  ? -5.80100  -10.13700 7.13800   1.000 17.60000  ? 80  CYS A N    1 
ATOM   1525 C  CA   . CYS A 1 80  ? -5.91500  -11.11200 6.05600   1.000 17.94000  ? 80  CYS A CA   1 
ATOM   1526 C  C    . CYS A 1 80  ? -5.83600  -10.46100 4.68100   1.000 18.50000  ? 80  CYS A C    1 
ATOM   1527 O  O    . CYS A 1 80  ? -5.32500  -11.07900 3.72800   1.000 19.77000  ? 80  CYS A O    1 
ATOM   1528 C  CB   . CYS A 1 80  ? -7.20400  -11.91500 6.18600   1.000 17.34000  ? 80  CYS A CB   1 
ATOM   1529 S  SG   . CYS A 1 80  ? -7.36200  -12.91900 7.71000   1.000 17.81000  ? 80  CYS A SG   1 
ATOM   1530 H  H    . CYS A 1 80  ? -6.47800  -10.10000 7.66700   1.000 21.14000  ? 80  CYS A H    1 
ATOM   1531 H  HA   . CYS A 1 80  ? -5.17100  -11.73000 6.13500   1.000 21.55000  ? 80  CYS A HA   1 
ATOM   1532 H  HB2  . CYS A 1 80  ? -7.95100  -11.29600 6.16900   1.000 20.83000  ? 80  CYS A HB2  1 
ATOM   1533 H  HB3  . CYS A 1 80  ? -7.26100  -12.52300 5.43200   1.000 20.83000  ? 80  CYS A HB3  1 
ATOM   1534 N  N    . SER A 1 81  ? -6.34700  -9.22900  4.54600   1.000 19.30000  ? 81  SER A N    1 
ATOM   1535 C  CA   . SER A 1 81  ? -6.26700  -8.51200  3.28100   1.000 19.73000  ? 81  SER A CA   1 
ATOM   1536 C  C    . SER A 1 81  ? -4.83800  -8.33200  2.77700   1.000 22.00000  ? 81  SER A C    1 
ATOM   1537 O  O    . SER A 1 81  ? -4.63400  -8.22400  1.56900   1.000 24.44000  ? 81  SER A O    1 
ATOM   1538 C  CB   . SER A 1 81  ? -6.95200  -7.14800  3.42300   1.000 23.42000  ? 81  SER A CB   1 
ATOM   1539 O  OG   . SER A 1 81  ? -6.26400  -6.34200  4.35400   1.000 28.19000  ? 81  SER A OG   1 
ATOM   1540 H  H    . SER A 1 81  ? -6.74300  -8.79300  5.17300   1.000 23.19000  ? 81  SER A H    1 
ATOM   1541 H  HA   . SER A 1 81  ? -6.73400  -9.03500  2.61100   1.000 23.70000  ? 81  SER A HA   1 
ATOM   1542 H  HB2  . SER A 1 81  ? -6.95500  -6.70300  2.56100   1.000 28.12000  ? 81  SER A HB2  1 
ATOM   1543 H  HB3  . SER A 1 81  ? -7.86200  -7.28100  3.73100   1.000 28.12000  ? 81  SER A HB3  1 
ATOM   1544 H  HG   . SER A 1 81  ? -6.50300  -6.53700  5.13500   1.000 33.85000  ? 81  SER A HG   1 
ATOM   1545 N  N    . ALA A 1 82  ? -3.84800  -8.31100  3.65800   1.000 20.17000  ? 82  ALA A N    1 
ATOM   1546 C  CA   . ALA A 1 82  ? -2.46100  -8.21600  3.21800   1.000 24.10000  ? 82  ALA A CA   1 
ATOM   1547 C  C    . ALA A 1 82  ? -2.04700  -9.41300  2.38100   1.000 24.20000  ? 82  ALA A C    1 
ATOM   1548 O  O    . ALA A 1 82  ? -1.08900  -9.33300  1.58900   1.000 25.89000  ? 82  ALA A O    1 
ATOM   1549 C  CB   . ALA A 1 82  ? -1.53900  -8.16400  4.43700   1.000 27.08000  ? 82  ALA A CB   1 
ATOM   1550 H  H    . ALA A 1 82  ? -3.94900  -8.34900  4.51200   1.000 24.23000  ? 82  ALA A H    1 
ATOM   1551 H  HA   . ALA A 1 82  ? -2.37000  -7.40700  2.69000   1.000 28.94000  ? 82  ALA A HA   1 
ATOM   1552 H  HB1  . ALA A 1 82  ? -0.62600  -8.03400  4.13700   1.000 32.52000  ? 82  ALA A HB1  1 
ATOM   1553 H  HB2  . ALA A 1 82  ? -1.80900  -7.42600  5.00600   1.000 32.52000  ? 82  ALA A HB2  1 
ATOM   1554 H  HB3  . ALA A 1 82  ? -1.61100  -9.00000  4.92400   1.000 32.52000  ? 82  ALA A HB3  1 
ATOM   1555 N  N    . LEU A 1 83  ? -2.70300  -10.53700 2.56900   1.000 21.19000  ? 83  LEU A N    1 
ATOM   1556 C  CA   . LEU A 1 83  ? -2.39400  -11.74800 1.82500   1.000 20.03000  ? 83  LEU A CA   1 
ATOM   1557 C  C    . LEU A 1 83  ? -2.91000  -11.71700 0.40000   1.000 23.35000  ? 83  LEU A C    1 
ATOM   1558 O  O    . LEU A 1 83  ? -2.68000  -12.67800 -0.34400  1.000 24.90000  ? 83  LEU A O    1 
ATOM   1559 C  CB   . LEU A 1 83  ? -2.98100  -12.94900 2.54200   1.000 20.96000  ? 83  LEU A CB   1 
ATOM   1560 C  CG   . LEU A 1 83  ? -2.48400  -13.14900 3.95600   1.000 22.03000  ? 83  LEU A CG   1 
ATOM   1561 C  CD1  . LEU A 1 83  ? -3.28600  -14.20300 4.68200   1.000 24.67000  ? 83  LEU A CD1  1 
ATOM   1562 C  CD2  . LEU A 1 83  ? -0.99000  -13.53600 3.92300   1.000 30.68000  ? 83  LEU A CD2  1 
ATOM   1563 H  H    . LEU A 1 83  ? -3.34600  -10.63100 3.13200   1.000 25.45000  ? 83  LEU A H    1 
ATOM   1564 H  HA   . LEU A 1 83  ? -1.43000  -11.85200 1.78800   1.000 24.06000  ? 83  LEU A HA   1 
ATOM   1565 H  HB2  . LEU A 1 83  ? -3.94400  -12.84200 2.58300   1.000 25.18000  ? 83  LEU A HB2  1 
ATOM   1566 H  HB3  . LEU A 1 83  ? -2.75700  -13.74800 2.03900   1.000 25.18000  ? 83  LEU A HB3  1 
ATOM   1567 H  HG   . LEU A 1 83  ? -2.59000  -12.32000 4.44900   1.000 26.46000  ? 83  LEU A HG   1 
ATOM   1568 H  HD11 . LEU A 1 83  ? -2.89700  -14.34700 5.55800   1.000 29.63000  ? 83  LEU A HD11 1 
ATOM   1569 H  HD12 . LEU A 1 83  ? -4.20200  -13.89600 4.77300   1.000 29.63000  ? 83  LEU A HD12 1 
ATOM   1570 H  HD13 . LEU A 1 83  ? -3.26200  -15.02600 4.16900   1.000 29.63000  ? 83  LEU A HD13 1 
ATOM   1571 H  HD21 . LEU A 1 83  ? -0.75700  -13.96700 4.76100   1.000 36.83000  ? 83  LEU A HD21 1 
ATOM   1572 H  HD22 . LEU A 1 83  ? -0.83800  -14.14600 3.18400   1.000 36.83000  ? 83  LEU A HD22 1 
ATOM   1573 H  HD23 . LEU A 1 83  ? -0.45800  -12.73400 3.80400   1.000 36.83000  ? 83  LEU A HD23 1 
ATOM   1574 N  N    . LEU A 1 84  ? -3.63400  -10.68100 -0.00600  1.000 20.35000  ? 84  LEU A N    1 
ATOM   1575 C  CA   . LEU A 1 84  ? -4.17400  -10.60300 -1.35800  1.000 21.29000  ? 84  LEU A CA   1 
ATOM   1576 C  C    . LEU A 1 84  ? -3.34200  -9.70400  -2.25800  1.000 23.63000  ? 84  LEU A C    1 
ATOM   1577 O  O    . LEU A 1 84  ? -3.68300  -9.53100  -3.43500  1.000 27.02000  ? 84  LEU A O    1 
ATOM   1578 C  CB   . LEU A 1 84  ? -5.61300  -10.09300 -1.31400  1.000 21.04000  ? 84  LEU A CB   1 
ATOM   1579 C  CG   . LEU A 1 84  ? -6.50700  -10.85900 -0.35400  1.000 22.38000  ? 84  LEU A CG   1 
ATOM   1580 C  CD1  . LEU A 1 84  ? -7.92400  -10.28900 -0.33500  1.000 31.80000  ? 84  LEU A CD1  1 
ATOM   1581 C  CD2  . LEU A 1 84  ? -6.58800  -12.33100 -0.72100  1.000 24.60000  ? 84  LEU A CD2  1 
ATOM   1582 H  H    . LEU A 1 84  ? -3.82900  -10.00500 0.48800   1.000 24.44000  ? 84  LEU A H    1 
ATOM   1583 H  HA   . LEU A 1 84  ? -4.18600  -11.49200 -1.74700  1.000 25.57000  ? 84  LEU A HA   1 
ATOM   1584 H  HB2  . LEU A 1 84  ? -5.60500  -9.16400  -1.03500  1.000 25.27000  ? 84  LEU A HB2  1 
ATOM   1585 H  HB3  . LEU A 1 84  ? -5.99700  -10.17000 -2.20200  1.000 25.27000  ? 84  LEU A HB3  1 
ATOM   1586 H  HG   . LEU A 1 84  ? -6.11400  -10.77100 0.52800   1.000 26.87000  ? 84  LEU A HG   1 
ATOM   1587 H  HD11 . LEU A 1 84  ? -8.46000  -10.79800 0.29200   1.000 38.18000  ? 84  LEU A HD11 1 
ATOM   1588 H  HD12 . LEU A 1 84  ? -7.88600  -9.35900  -0.06100  1.000 38.18000  ? 84  LEU A HD12 1 
ATOM   1589 H  HD13 . LEU A 1 84  ? -8.30300  -10.35600 -1.22600  1.000 38.18000  ? 84  LEU A HD13 1 
ATOM   1590 H  HD21 . LEU A 1 84  ? -7.17500  -12.78100 -0.09300  1.000 29.54000  ? 84  LEU A HD21 1 
ATOM   1591 H  HD22 . LEU A 1 84  ? -6.93900  -12.41400 -1.62100  1.000 29.54000  ? 84  LEU A HD22 1 
ATOM   1592 H  HD23 . LEU A 1 84  ? -5.69900  -12.71700 -0.67600  1.000 29.54000  ? 84  LEU A HD23 1 
ATOM   1593 N  N    A SER A 1 85  ? -2.24700  -9.17300  -1.73800  0.800 23.76000  ? 85  SER A N    1 
ATOM   1594 N  N    B SER A 1 85  ? -2.28300  -9.10000  -1.73500  0.200 23.83000  ? 85  SER A N    1 
ATOM   1595 C  CA   A SER A 1 85  ? -1.40600  -8.23600  -2.46100  0.800 24.25000  ? 85  SER A CA   1 
ATOM   1596 C  CA   B SER A 1 85  ? -1.50400  -8.16000  -2.52200  0.200 25.08000  ? 85  SER A CA   1 
ATOM   1597 C  C    A SER A 1 85  ? -0.69400  -8.89900  -3.63700  0.800 28.07000  ? 85  SER A C    1 
ATOM   1598 C  C    B SER A 1 85  ? -0.76200  -8.87500  -3.64800  0.200 27.84000  ? 85  SER A C    1 
ATOM   1599 O  O    A SER A 1 85  ? -0.39300  -10.09300 -3.62600  0.800 27.08000  ? 85  SER A O    1 
ATOM   1600 O  O    B SER A 1 85  ? -0.54000  -10.08800 -3.62200  0.200 27.65000  ? 85  SER A O    1 
ATOM   1601 C  CB   A SER A 1 85  ? -0.37300  -7.67900  -1.48200  0.800 25.30000  ? 85  SER A CB   1 
ATOM   1602 C  CB   B SER A 1 85  ? -0.49100  -7.44100  -1.63300  0.200 27.76000  ? 85  SER A CB   1 
ATOM   1603 O  OG   A SER A 1 85  ? 0.60800   -6.91800  -2.15000  0.800 26.79000  ? 85  SER A OG   1 
ATOM   1604 O  OG   B SER A 1 85  ? 0.33600   -8.37600  -0.96900  0.200 25.63000  ? 85  SER A OG   1 
ATOM   1605 H  H    A SER A 1 85  ? -1.96100  -9.34400  -0.94600  0.800 28.53000  ? 85  SER A H    1 
ATOM   1606 H  H    B SER A 1 85  ? -1.99800  -9.21700  -0.93200  0.200 28.61000  ? 85  SER A H    1 
ATOM   1607 H  HA   A SER A 1 85  ? -1.94600  -7.51900  -2.82900  0.800 29.12000  ? 85  SER A HA   1 
ATOM   1608 H  HA   B SER A 1 85  ? -2.10200  -7.50600  -2.91600  0.200 30.12000  ? 85  SER A HA   1 
ATOM   1609 H  HB2  A SER A 1 85  ? -0.82500  -7.11200  -0.83800  0.800 30.39000  ? 85  SER A HB2  1 
ATOM   1610 H  HB2  B SER A 1 85  ? 0.06000   -6.86400  -2.18400  0.200 33.33000  ? 85  SER A HB2  1 
ATOM   1611 H  HB3  A SER A 1 85  ? 0.06000   -8.41800  -1.02700  0.800 30.39000  ? 85  SER A HB3  1 
ATOM   1612 H  HB3  B SER A 1 85  ? -0.96700  -6.91300  -0.97300  0.200 33.33000  ? 85  SER A HB3  1 
ATOM   1613 H  HG   A SER A 1 85  ? 1.23300   -6.72800  -1.62200  0.800 32.17000  ? 85  SER A HG   1 
ATOM   1614 H  HG   B SER A 1 85  ? 0.73900   -8.85300  -1.53100  0.200 30.77000  ? 85  SER A HG   1 
ATOM   1615 N  N    . SER A 1 86  ? -0.38100  -8.09400  -4.65800  1.000 27.56000  ? 86  SER A N    1 
ATOM   1616 C  CA   . SER A 1 86  ? 0.45700   -8.61000  -5.73500  1.000 25.67000  ? 86  SER A CA   1 
ATOM   1617 C  C    . SER A 1 86  ? 1.87900   -8.89900  -5.26100  1.000 25.97000  ? 86  SER A C    1 
ATOM   1618 O  O    . SER A 1 86  ? 2.58600   -9.67600  -5.90800  1.000 30.96000  ? 86  SER A O    1 
ATOM   1619 C  CB   . SER A 1 86  ? 0.49600   -7.61800  -6.90000  1.000 33.21000  ? 86  SER A CB   1 
ATOM   1620 O  OG   . SER A 1 86  ? 0.67100   -6.29800  -6.42700  1.000 43.04000  ? 86  SER A OG   1 
ATOM   1621 H  H    . SER A 1 86  ? -0.63500  -7.27700  -4.74300  1.000 33.10000  ? 86  SER A H    1 
ATOM   1622 H  HA   . SER A 1 86  ? 0.06900   -9.43700  -6.06200  1.000 30.83000  ? 86  SER A HA   1 
ATOM   1623 H  HB2  . SER A 1 86  ? 1.23700   -7.84500  -7.48400  1.000 39.87000  ? 86  SER A HB2  1 
ATOM   1624 H  HB3  . SER A 1 86  ? -0.34000  -7.67100  -7.38900  1.000 39.87000  ? 86  SER A HB3  1 
ATOM   1625 H  HG   . SER A 1 86  ? 0.70400   -5.76300  -7.07400  1.000 51.66000  ? 86  SER A HG   1 
ATOM   1626 N  N    . ASP A 1 87  ? 2.29800   -8.29500  -4.15500  1.000 25.23000  ? 87  ASP A N    1 
ATOM   1627 C  CA   . ASP A 1 87  ? 3.55400   -8.58700  -3.47600  1.000 25.58000  ? 87  ASP A CA   1 
ATOM   1628 C  C    . ASP A 1 87  ? 3.29200   -9.75100  -2.52800  1.000 27.89000  ? 87  ASP A C    1 
ATOM   1629 O  O    . ASP A 1 87  ? 2.48900   -9.62500  -1.59600  1.000 26.73000  ? 87  ASP A O    1 
ATOM   1630 C  CB   . ASP A 1 87  ? 3.94000   -7.34100  -2.68200  1.000 30.40000  ? 87  ASP A CB   1 
ATOM   1631 C  CG   . ASP A 1 87  ? 5.24300   -7.48200  -1.90000  1.000 41.02000  ? 87  ASP A CG   1 
ATOM   1632 O  OD1  . ASP A 1 87  ? 5.78300   -8.58700  -1.73800  1.000 32.99000  ? 87  ASP A OD1  1 
ATOM   1633 O  OD2  . ASP A 1 87  ? 5.74500   -6.43800  -1.42900  1.000 58.70000  ? 87  ASP A OD2  1 
ATOM   1634 H  H    . ASP A 1 87  ? 1.84800   -7.67900  -3.75700  1.000 30.30000  ? 87  ASP A H    1 
ATOM   1635 H  HA   . ASP A 1 87  ? 4.26600   -8.82900  -4.08900  1.000 30.72000  ? 87  ASP A HA   1 
ATOM   1636 H  HB2  . ASP A 1 87  ? 4.04500   -6.59900  -3.29800  1.000 36.50000  ? 87  ASP A HB2  1 
ATOM   1637 H  HB3  . ASP A 1 87  ? 3.23300   -7.14600  -2.04600  1.000 36.50000  ? 87  ASP A HB3  1 
ATOM   1638 N  N    . ILE A 1 88  ? 3.96600   -10.87800 -2.76800  1.000 22.71000  ? 88  ILE A N    1 
ATOM   1639 C  CA   . ILE A 1 88  ? 3.68900   -12.10300 -2.01300  1.000 20.94000  ? 88  ILE A CA   1 
ATOM   1640 C  C    . ILE A 1 88  ? 4.46500   -12.20200 -0.71200  1.000 22.97000  ? 88  ILE A C    1 
ATOM   1641 O  O    . ILE A 1 88  ? 4.38900   -13.23100 -0.02900  1.000 21.55000  ? 88  ILE A O    1 
ATOM   1642 C  CB   . ILE A 1 88  ? 3.92700   -13.38400 -2.84800  1.000 20.42000  ? 88  ILE A CB   1 
ATOM   1643 C  CG1  . ILE A 1 88  ? 5.42700   -13.54400 -3.18300  1.000 27.71000  ? 88  ILE A CG1  1 
ATOM   1644 C  CG2  . ILE A 1 88  ? 3.03600   -13.37900 -4.07400  1.000 27.11000  ? 88  ILE A CG2  1 
ATOM   1645 C  CD1  . ILE A 1 88  ? 5.79300   -14.93000 -3.74600  1.000 28.09000  ? 88  ILE A CD1  1 
ATOM   1646 H  H    . ILE A 1 88  ? 4.58500   -10.95900 -3.35900  1.000 27.27000  ? 88  ILE A H    1 
ATOM   1647 H  HA   . ILE A 1 88  ? 2.74500   -12.06400 -1.79500  1.000 25.15000  ? 88  ILE A HA   1 
ATOM   1648 H  HB   . ILE A 1 88  ? 3.68200   -14.16300 -2.32400  1.000 24.52000  ? 88  ILE A HB   1 
ATOM   1649 H  HG12 . ILE A 1 88  ? 5.67000   -12.88100 -3.84700  1.000 33.28000  ? 88  ILE A HG12 1 
ATOM   1650 H  HG13 . ILE A 1 88  ? 5.94400   -13.40700 -2.37300  1.000 33.28000  ? 88  ILE A HG13 1 
ATOM   1651 H  HG21 . ILE A 1 88  ? 3.07200   -14.25300 -4.49400  1.000 32.55000  ? 88  ILE A HG21 1 
ATOM   1652 H  HG22 . ILE A 1 88  ? 2.12600   -13.18100 -3.80200  1.000 32.55000  ? 88  ILE A HG22 1 
ATOM   1653 H  HG23 . ILE A 1 88  ? 3.35200   -12.70100 -4.69100  1.000 32.55000  ? 88  ILE A HG23 1 
ATOM   1654 H  HD11 . ILE A 1 88  ? 6.71900   -14.92000 -4.03400  1.000 33.72000  ? 88  ILE A HD11 1 
ATOM   1655 H  HD12 . ILE A 1 88  ? 5.67000   -15.59600 -3.05100  1.000 33.72000  ? 88  ILE A HD12 1 
ATOM   1656 H  HD13 . ILE A 1 88  ? 5.21400   -15.12800 -4.49900  1.000 33.72000  ? 88  ILE A HD13 1 
ATOM   1657 N  N    . THR A 1 89  ? 5.20900   -11.16500 -0.33000  1.000 23.69000  ? 89  THR A N    1 
ATOM   1658 C  CA   . THR A 1 89  ? 6.02900   -11.24600 0.87100   1.000 23.02000  ? 89  THR A CA   1 
ATOM   1659 C  C    . THR A 1 89  ? 5.23400   -11.72400 2.09000   1.000 23.06000  ? 89  THR A C    1 
ATOM   1660 O  O    . THR A 1 89  ? 5.66200   -12.63100 2.81400   1.000 23.06000  ? 89  THR A O    1 
ATOM   1661 C  CB   . THR A 1 89  ? 6.66900   -9.88400  1.14800   1.000 27.20000  ? 89  THR A CB   1 
ATOM   1662 O  OG1  . THR A 1 89  ? 7.50600   -9.52600  0.04900   1.000 30.31000  ? 89  THR A OG1  1 
ATOM   1663 C  CG2  . THR A 1 89  ? 7.51300   -9.96900  2.39100   1.000 29.93000  ? 89  THR A CG2  1 
ATOM   1664 H  H    . THR A 1 89  ? 5.25500   -10.41300 -0.74400  1.000 28.44000  ? 89  THR A H    1 
ATOM   1665 H  HA   . THR A 1 89  ? 6.73100   -11.89700 0.71500   1.000 27.64000  ? 89  THR A HA   1 
ATOM   1666 H  HB   . THR A 1 89  ? 5.98300   -9.20900  1.27000   1.000 32.67000  ? 89  THR A HB   1 
ATOM   1667 H  HG1  . THR A 1 89  ? 8.30900   -9.50800  0.29300   1.000 36.39000  ? 89  THR A HG1  1 
ATOM   1668 H  HG21 . THR A 1 89  ? 8.08200   -9.18700  2.46100   1.000 35.94000  ? 89  THR A HG21 1 
ATOM   1669 H  HG22 . THR A 1 89  ? 6.94400   -10.01500 3.17600   1.000 35.94000  ? 89  THR A HG22 1 
ATOM   1670 H  HG23 . THR A 1 89  ? 8.07000   -10.76300 2.36000   1.000 35.94000  ? 89  THR A HG23 1 
ATOM   1671 N  N    . ALA A 1 90  ? 4.09000   -11.10700 2.37000   1.000 22.36000  ? 90  ALA A N    1 
ATOM   1672 C  CA   . ALA A 1 90  ? 3.37400   -11.48600 3.58000   1.000 22.20000  ? 90  ALA A CA   1 
ATOM   1673 C  C    . ALA A 1 90  ? 2.89800   -12.93400 3.51800   1.000 20.66000  ? 90  ALA A C    1 
ATOM   1674 O  O    . ALA A 1 90  ? 2.93300   -13.63900 4.53300   1.000 22.24000  ? 90  ALA A O    1 
ATOM   1675 C  CB   . ALA A 1 90  ? 2.21900   -10.52000 3.84300   1.000 26.74000  ? 90  ALA A CB   1 
ATOM   1676 H  H    . ALA A 1 90  ? 3.72200   -10.49100 1.89600   1.000 26.85000  ? 90  ALA A H    1 
ATOM   1677 H  HA   . ALA A 1 90  ? 3.98000   -11.41700 4.33500   1.000 26.66000  ? 90  ALA A HA   1 
ATOM   1678 H  HB1  . ALA A 1 90  ? 1.71400   -10.83300 4.60900   1.000 32.11000  ? 90  ALA A HB1  1 
ATOM   1679 H  HB2  . ALA A 1 90  ? 2.58000   -9.63700  4.02300   1.000 32.11000  ? 90  ALA A HB2  1 
ATOM   1680 H  HB3  . ALA A 1 90  ? 1.64800   -10.49000 3.06000   1.000 32.11000  ? 90  ALA A HB3  1 
ATOM   1681 N  N    . SER A 1 91  ? 2.41400   -13.38200 2.35300   1.000 20.35000  ? 91  SER A N    1 
ATOM   1682 C  CA   . SER A 1 91  ? 2.00600   -14.77400 2.21000   1.000 18.49000  ? 91  SER A CA   1 
ATOM   1683 C  C    . SER A 1 91  ? 3.16400   -15.72400 2.45900   1.000 18.90000  ? 91  SER A C    1 
ATOM   1684 O  O    . SER A 1 91  ? 2.99500   -16.73800 3.13000   1.000 21.01000  ? 91  SER A O    1 
ATOM   1685 C  CB   . SER A 1 91  ? 1.41200   -15.00400 0.82900   1.000 20.41000  ? 91  SER A CB   1 
ATOM   1686 O  OG   . SER A 1 91  ? 0.09400   -14.47800 0.76800   1.000 21.42000  ? 91  SER A OG   1 
ATOM   1687 H  H    . SER A 1 91  ? 2.31500   -12.90500 1.64400   1.000 24.44000  ? 91  SER A H    1 
ATOM   1688 H  HA   . SER A 1 91  ? 1.32000   -14.96400 2.87000   1.000 22.21000  ? 91  SER A HA   1 
ATOM   1689 H  HB2  . SER A 1 91  ? 1.96300   -14.56000 0.16700   1.000 24.51000  ? 91  SER A HB2  1 
ATOM   1690 H  HB3  . SER A 1 91  ? 1.38200   -15.95700 0.65000   1.000 24.51000  ? 91  SER A HB3  1 
ATOM   1691 H  HG   . SER A 1 91  ? -0.20700  -14.54700 -0.01300  1.000 25.72000  ? 91  SER A HG   1 
ATOM   1692 N  N    . VAL A 1 92  ? 4.33500   -15.41600 1.90800   1.000 18.48000  ? 92  VAL A N    1 
ATOM   1693 C  CA   . VAL A 1 92  ? 5.49500   -16.28800 2.06900   1.000 20.19000  ? 92  VAL A CA   1 
ATOM   1694 C  C    . VAL A 1 92  ? 5.96200   -16.31600 3.51000   1.000 22.16000  ? 92  VAL A C    1 
ATOM   1695 O  O    . VAL A 1 92  ? 6.25200   -17.38300 4.06300   1.000 21.61000  ? 92  VAL A O    1 
ATOM   1696 C  CB   . VAL A 1 92  ? 6.62700   -15.87000 1.11500   1.000 23.48000  ? 92  VAL A CB   1 
ATOM   1697 C  CG1  . VAL A 1 92  ? 7.89700   -16.63500 1.46900   1.000 27.77000  ? 92  VAL A CG1  1 
ATOM   1698 C  CG2  . VAL A 1 92  ? 6.22300   -16.13200 -0.29600  1.000 25.60000  ? 92  VAL A CG2  1 
ATOM   1699 H  H    . VAL A 1 92  ? 4.48400   -14.71100 1.43800   1.000 22.20000  ? 92  VAL A H    1 
ATOM   1700 H  HA   . VAL A 1 92  ? 5.22100   -17.18900 1.83200   1.000 24.25000  ? 92  VAL A HA   1 
ATOM   1701 H  HB   . VAL A 1 92  ? 6.80500   -14.92000 1.20500   1.000 28.20000  ? 92  VAL A HB   1 
ATOM   1702 H  HG11 . VAL A 1 92  ? 8.53800   -16.53400 0.74700   1.000 33.34000  ? 92  VAL A HG11 1 
ATOM   1703 H  HG12 . VAL A 1 92  ? 8.26500   -16.27400 2.29000   1.000 33.34000  ? 92  VAL A HG12 1 
ATOM   1704 H  HG13 . VAL A 1 92  ? 7.67800   -17.57200 1.58800   1.000 33.34000  ? 92  VAL A HG13 1 
ATOM   1705 H  HG21 . VAL A 1 92  ? 6.93100   -15.83500 -0.88800  1.000 30.75000  ? 92  VAL A HG21 1 
ATOM   1706 H  HG22 . VAL A 1 92  ? 6.07300   -17.08300 -0.41000  1.000 30.75000  ? 92  VAL A HG22 1 
ATOM   1707 H  HG23 . VAL A 1 92  ? 5.40600   -15.64300 -0.48700  1.000 30.75000  ? 92  VAL A HG23 1 
ATOM   1708 N  N    . ASN A 1 93  ? 6.02900   -15.15100 4.15800   1.000 22.09000  ? 93  ASN A N    1 
ATOM   1709 C  CA   . ASN A 1 93  ? 6.51300   -15.11500 5.53400   1.000 21.96000  ? 93  ASN A CA   1 
ATOM   1710 C  C    . ASN A 1 93  ? 5.55300   -15.84400 6.46200   1.000 19.21000  ? 93  ASN A C    1 
ATOM   1711 O  O    . ASN A 1 93  ? 5.97300   -16.54800 7.38300   1.000 23.83000  ? 93  ASN A O    1 
ATOM   1712 C  CB   . ASN A 1 93  ? 6.69300   -13.66400 5.99700   1.000 27.64000  ? 93  ASN A CB   1 
ATOM   1713 C  CG   . ASN A 1 93  ? 7.95000   -13.03100 5.43400   1.000 41.09000  ? 93  ASN A CG   1 
ATOM   1714 O  OD1  . ASN A 1 93  ? 8.75100   -13.69100 4.76900   1.000 38.88000  ? 93  ASN A OD1  1 
ATOM   1715 N  ND2  . ASN A 1 93  ? 8.14000   -11.74600 5.71600   1.000 51.54000  ? 93  ASN A ND2  1 
ATOM   1716 H  H    . ASN A 1 93  ? 5.80600   -14.38800 3.83100   1.000 26.52000  ? 93  ASN A H    1 
ATOM   1717 H  HA   . ASN A 1 93  ? 7.37800   -15.55200 5.57300   1.000 26.37000  ? 93  ASN A HA   1 
ATOM   1718 H  HB2  . ASN A 1 93  ? 5.93300   -13.14000 5.70100   1.000 33.19000  ? 93  ASN A HB2  1 
ATOM   1719 H  HB3  . ASN A 1 93  ? 6.75300   -13.64500 6.96500   1.000 33.19000  ? 93  ASN A HB3  1 
ATOM   1720 H  HD21 . ASN A 1 93  ? 7.56500   -11.32100 6.19400   1.000 61.87000  ? 93  ASN A HD21 1 
ATOM   1721 H  HD22 . ASN A 1 93  ? 8.83800   -11.33900 5.42100   1.000 61.87000  ? 93  ASN A HD22 1 
ATOM   1722 N  N    . CYS A 1 94  ? 4.24500   -15.70600 6.23600   1.000 19.29000  ? 94  CYS A N    1 
ATOM   1723 C  CA   . CYS A 1 94  ? 3.29000   -16.44600 7.04700   1.000 19.00000  ? 94  CYS A CA   1 
ATOM   1724 C  C    . CYS A 1 94  ? 3.36300   -17.95300 6.76100   1.000 20.29000  ? 94  CYS A C    1 
ATOM   1725 O  O    . CYS A 1 94  ? 3.33500   -18.77300 7.69500   1.000 19.42000  ? 94  CYS A O    1 
ATOM   1726 C  CB   . CYS A 1 94  ? 1.88000   -15.90400 6.79300   1.000 19.41000  ? 94  CYS A CB   1 
ATOM   1727 S  SG   . CYS A 1 94  ? 0.59100   -16.57200 7.86900   1.000 21.77000  ? 94  CYS A SG   1 
ATOM   1728 H  H    . CYS A 1 94  ? 3.89600   -15.20200 5.63200   1.000 23.17000  ? 94  CYS A H    1 
ATOM   1729 H  HA   . CYS A 1 94  ? 3.49800   -16.31900 7.98600   1.000 22.82000  ? 94  CYS A HA   1 
ATOM   1730 H  HB2  . CYS A 1 94  ? 1.89500   -14.94200 6.92000   1.000 23.31000  ? 94  CYS A HB2  1 
ATOM   1731 H  HB3  . CYS A 1 94  ? 1.63200   -16.11400 5.87900   1.000 23.31000  ? 94  CYS A HB3  1 
ATOM   1732 N  N    . ALA A 1 95  ? 3.50700   -18.33600 5.48500   1.000 18.27000  ? 95  ALA A N    1 
ATOM   1733 C  CA   . ALA A 1 95  ? 3.67000   -19.74800 5.12600   1.000 19.08000  ? 95  ALA A CA   1 
ATOM   1734 C  C    . ALA A 1 95  ? 4.87400   -20.37600 5.81400   1.000 18.39000  ? 95  ALA A C    1 
ATOM   1735 O  O    . ALA A 1 95  ? 4.83000   -21.54900 6.16700   1.000 19.80000  ? 95  ALA A O    1 
ATOM   1736 C  CB   . ALA A 1 95  ? 3.79900   -19.90700 3.62000   1.000 20.11000  ? 95  ALA A CB   1 
ATOM   1737 H  H    . ALA A 1 95  ? 3.51400   -17.80000 4.81200   1.000 21.95000  ? 95  ALA A H    1 
ATOM   1738 H  HA   . ALA A 1 95  ? 2.87300   -20.21800 5.41900   1.000 22.92000  ? 95  ALA A HA   1 
ATOM   1739 H  HB1  . ALA A 1 95  ? 3.94200   -20.84400 3.41200   1.000 24.15000  ? 95  ALA A HB1  1 
ATOM   1740 H  HB2  . ALA A 1 95  ? 2.98300   -19.59600 3.19800   1.000 24.15000  ? 95  ALA A HB2  1 
ATOM   1741 H  HB3  . ALA A 1 95  ? 4.55300   -19.38100 3.31000   1.000 24.15000  ? 95  ALA A HB3  1 
ATOM   1742 N  N    . LYS A 1 96  ? 5.96000   -19.62100 6.00000   1.000 18.71000  ? 96  LYS A N    1 
ATOM   1743 C  CA   . LYS A 1 96  ? 7.12900   -20.17100 6.69600   1.000 19.14000  ? 96  LYS A CA   1 
ATOM   1744 C  C    . LYS A 1 96  ? 6.77500   -20.50800 8.13500   1.000 21.32000  ? 96  LYS A C    1 
ATOM   1745 O  O    . LYS A 1 96  ? 7.26000   -21.49700 8.69200   1.000 22.79000  ? 96  LYS A O    1 
ATOM   1746 C  CB   . LYS A 1 96  ? 8.25100   -19.13900 6.65900   1.000 22.06000  ? 96  LYS A CB   1 
ATOM   1747 C  CG   . LYS A 1 96  ? 8.96800   -19.04000 5.33300   1.000 20.93000  ? 96  LYS A CG   1 
ATOM   1748 C  CD   . LYS A 1 96  ? 10.07700  -17.96400 5.36900   1.000 24.50000  ? 96  LYS A CD   1 
ATOM   1749 C  CE   . LYS A 1 96  ? 10.73800  -17.86100 4.01700   1.000 28.87000  ? 96  LYS A CE   1 
ATOM   1750 N  NZ   . LYS A 1 96  ? 11.62700  -16.67000 3.92900   1.000 37.83000  ? 96  LYS A NZ   1 
ATOM   1751 H  H    . LYS A 1 96  ? 6.04500   -18.80600 5.74000   1.000 22.48000  ? 96  LYS A H    1 
ATOM   1752 H  HA   . LYS A 1 96  ? 7.43000   -20.98000 6.25500   1.000 22.99000  ? 96  LYS A HA   1 
ATOM   1753 H  HB2  . LYS A 1 96  ? 7.87500   -18.26700 6.85400   1.000 26.49000  ? 96  LYS A HB2  1 
ATOM   1754 H  HB3  . LYS A 1 96  ? 8.90900   -19.37500 7.33100   1.000 26.49000  ? 96  LYS A HB3  1 
ATOM   1755 H  HG2  . LYS A 1 96  ? 9.37900   -19.89400 5.12600   1.000 25.14000  ? 96  LYS A HG2  1 
ATOM   1756 H  HG3  . LYS A 1 96  ? 8.33300   -18.80100 4.64100   1.000 25.14000  ? 96  LYS A HG3  1 
ATOM   1757 H  HD2  . LYS A 1 96  ? 9.68900   -17.10300 5.59200   1.000 29.43000  ? 96  LYS A HD2  1 
ATOM   1758 H  HD3  . LYS A 1 96  ? 10.74700  -18.20700 6.02600   1.000 29.43000  ? 96  LYS A HD3  1 
ATOM   1759 H  HE2  . LYS A 1 96  ? 11.27500  -18.65300 3.86200   1.000 34.67000  ? 96  LYS A HE2  1 
ATOM   1760 H  HE3  . LYS A 1 96  ? 10.05600  -17.78200 3.33200   1.000 34.67000  ? 96  LYS A HE3  1 
ATOM   1761 H  HZ1  . LYS A 1 96  ? 11.98500  -16.61600 3.11600   1.000 45.41000  ? 96  LYS A HZ1  1 
ATOM   1762 H  HZ2  . LYS A 1 96  ? 11.16100  -15.92900 4.08900   1.000 45.41000  ? 96  LYS A HZ2  1 
ATOM   1763 H  HZ3  . LYS A 1 96  ? 12.28200  -16.73300 4.52900   1.000 45.41000  ? 96  LYS A HZ3  1 
ATOM   1764 N  N    . LYS A 1 97  ? 5.93800   -19.68500 8.77300   1.000 18.49000  ? 97  LYS A N    1 
ATOM   1765 C  CA   . LYS A 1 97  ? 5.48100   -20.01300 10.12300  1.000 19.59000  ? 97  LYS A CA   1 
ATOM   1766 C  C    . LYS A 1 97  ? 4.58600   -21.24900 10.13400  1.000 21.05000  ? 97  LYS A C    1 
ATOM   1767 O  O    . LYS A 1 97  ? 4.71000   -22.11400 11.01700  1.000 24.23000  ? 97  LYS A O    1 
ATOM   1768 C  CB   . LYS A 1 97  ? 4.80400   -18.80100 10.77500  1.000 25.78000  ? 97  LYS A CB   1 
ATOM   1769 C  CG   . LYS A 1 97  ? 5.81000   -17.68200 11.13200  1.000 51.35000  ? 97  LYS A CG   1 
ATOM   1770 C  CD   . LYS A 1 97  ? 5.16000   -16.34300 11.51500  1.000 72.13000  ? 97  LYS A CD   1 
ATOM   1771 C  CE   . LYS A 1 97  ? 5.88400   -15.14200 10.89600  1.000 76.23000  ? 97  LYS A CE   1 
ATOM   1772 N  NZ   . LYS A 1 97  ? 5.14100   -13.85500 11.08300  1.000 59.27000  ? 97  LYS A NZ   1 
ATOM   1773 H  H    . LYS A 1 97  ? 5.62900   -18.94900 8.45500   1.000 22.21000  ? 97  LYS A H    1 
ATOM   1774 H  HA   . LYS A 1 97  ? 6.25500   -20.22500 10.66800  1.000 23.53000  ? 97  LYS A HA   1 
ATOM   1775 H  HB2  . LYS A 1 97  ? 4.15100   -18.43400 10.15900  1.000 30.96000  ? 97  LYS A HB2  1 
ATOM   1776 H  HB3  . LYS A 1 97  ? 4.36600   -19.08500 11.59200  1.000 30.96000  ? 97  LYS A HB3  1 
ATOM   1777 H  HG2  . LYS A 1 97  ? 6.34500   -17.97400 11.88600  1.000 61.64000  ? 97  LYS A HG2  1 
ATOM   1778 H  HG3  . LYS A 1 97  ? 6.38100   -17.52100 10.36400  1.000 61.64000  ? 97  LYS A HG3  1 
ATOM   1779 H  HD2  . LYS A 1 97  ? 4.24200   -16.33500 11.20200  1.000 86.58000  ? 97  LYS A HD2  1 
ATOM   1780 H  HD3  . LYS A 1 97  ? 5.18300   -16.24400 12.48000  1.000 86.58000  ? 97  LYS A HD3  1 
ATOM   1781 H  HE2  . LYS A 1 97  ? 6.75400   -15.04800 11.31400  1.000 91.50000  ? 97  LYS A HE2  1 
ATOM   1782 H  HE3  . LYS A 1 97  ? 5.98700   -15.29200 9.94300   1.000 91.50000  ? 97  LYS A HE3  1 
ATOM   1783 H  HZ1  . LYS A 1 97  ? 5.59200   -13.18500 10.70800  1.000 71.14000  ? 97  LYS A HZ1  1 
ATOM   1784 H  HZ2  . LYS A 1 97  ? 4.33800   -13.90900 10.70400  1.000 71.14000  ? 97  LYS A HZ2  1 
ATOM   1785 H  HZ3  . LYS A 1 97  ? 5.04000   -13.68400 11.95100  1.000 71.14000  ? 97  LYS A HZ3  1 
ATOM   1786 N  N    . ILE A 1 98  ? 3.66700   -21.35300 9.17700   1.000 18.26000  ? 98  ILE A N    1 
ATOM   1787 C  CA   . ILE A 1 98  ? 2.75500   -22.48800 9.12000   1.000 20.07000  ? 98  ILE A CA   1 
ATOM   1788 C  C    . ILE A 1 98  ? 3.52400   -23.79500 8.92200   1.000 20.23000  ? 98  ILE A C    1 
ATOM   1789 O  O    . ILE A 1 98  ? 3.24900   -24.79000 9.59900   1.000 20.55000  ? 98  ILE A O    1 
ATOM   1790 C  CB   . ILE A 1 98  ? 1.71200   -22.27000 8.01000   1.000 18.20000  ? 98  ILE A CB   1 
ATOM   1791 C  CG1  . ILE A 1 98  ? 0.88500   -21.00600 8.30900   1.000 19.48000  ? 98  ILE A CG1  1 
ATOM   1792 C  CG2  . ILE A 1 98  ? 0.81400   -23.48900 7.85300   1.000 19.23000  ? 98  ILE A CG2  1 
ATOM   1793 C  CD1  . ILE A 1 98  ? 0.02100   -20.57500 7.13800   1.000 21.36000  ? 98  ILE A CD1  1 
ATOM   1794 H  H    . ILE A 1 98  ? 3.55100   -20.77800 8.54800   1.000 21.94000  ? 98  ILE A H    1 
ATOM   1795 H  HA   . ILE A 1 98  ? 2.28900   -22.55000 9.96900   1.000 24.11000  ? 98  ILE A HA   1 
ATOM   1796 H  HB   . ILE A 1 98  ? 2.18000   -22.14400 7.16900   1.000 21.86000  ? 98  ILE A HB   1 
ATOM   1797 H  HG12 . ILE A 1 98  ? 0.30200   -21.18200 9.06300   1.000 23.40000  ? 98  ILE A HG12 1 
ATOM   1798 H  HG13 . ILE A 1 98  ? 1.49000   -20.27700 8.51900   1.000 23.40000  ? 98  ILE A HG13 1 
ATOM   1799 H  HG21 . ILE A 1 98  ? 0.23800   -23.36000 7.08400   1.000 23.10000  ? 98  ILE A HG21 1 
ATOM   1800 H  HG22 . ILE A 1 98  ? 1.36700   -24.27500 7.72400   1.000 23.10000  ? 98  ILE A HG22 1 
ATOM   1801 H  HG23 . ILE A 1 98  ? 0.27700   -23.59000 8.65500   1.000 23.10000  ? 98  ILE A HG23 1 
ATOM   1802 H  HD11 . ILE A 1 98  ? 0.59000   -20.40200 6.37200   1.000 25.65000  ? 98  ILE A HD11 1 
ATOM   1803 H  HD12 . ILE A 1 98  ? -0.60600  -21.28600 6.93000   1.000 25.65000  ? 98  ILE A HD12 1 
ATOM   1804 H  HD13 . ILE A 1 98  ? -0.46100  -19.77000 7.38100   1.000 25.65000  ? 98  ILE A HD13 1 
ATOM   1805 N  N    . VAL A 1 99  ? 4.45200   -23.82700 7.96400   1.000 19.39000  ? 99  VAL A N    1 
ATOM   1806 C  CA   . VAL A 1 99  ? 5.13400   -25.06900 7.61700   1.000 20.18000  ? 99  VAL A CA   1 
ATOM   1807 C  C    . VAL A 1 99  ? 6.04300   -25.51500 8.73300   1.000 22.56000  ? 99  VAL A C    1 
ATOM   1808 O  O    . VAL A 1 99  ? 6.40500   -26.70000 8.79300   1.000 22.29000  ? 99  VAL A O    1 
ATOM   1809 C  CB   . VAL A 1 99  ? 5.85700   -24.89700 6.27400   1.000 18.51000  ? 99  VAL A CB   1 
ATOM   1810 C  CG1  . VAL A 1 99  ? 7.12700   -24.10700 6.41000   1.000 19.88000  ? 99  VAL A CG1  1 
ATOM   1811 C  CG2  . VAL A 1 99  ? 6.09900   -26.27400 5.61900   1.000 23.07000  ? 99  VAL A CG2  1 
ATOM   1812 H  H    . VAL A 1 99  ? 4.70300   -23.14500 7.50300   1.000 23.29000  ? 99  VAL A H    1 
ATOM   1813 H  HA   . VAL A 1 99  ? 4.48900   -25.78300 7.49400   1.000 24.24000  ? 99  VAL A HA   1 
ATOM   1814 H  HB   . VAL A 1 99  ? 5.28700   -24.38000 5.68300   1.000 22.24000  ? 99  VAL A HB   1 
ATOM   1815 H  HG11 . VAL A 1 99  ? 7.44300   -23.86400 5.52600   1.000 23.88000  ? 99  VAL A HG11 1 
ATOM   1816 H  HG12 . VAL A 1 99  ? 6.94700   -23.30700 6.92900   1.000 23.88000  ? 99  VAL A HG12 1 
ATOM   1817 H  HG13 . VAL A 1 99  ? 7.79000   -24.65200 6.86100   1.000 23.88000  ? 99  VAL A HG13 1 
ATOM   1818 H  HG21 . VAL A 1 99  ? 6.64300   -26.15600 4.82600   1.000 27.70000  ? 99  VAL A HG21 1 
ATOM   1819 H  HG22 . VAL A 1 99  ? 6.55700   -26.84900 6.25300   1.000 27.70000  ? 99  VAL A HG22 1 
ATOM   1820 H  HG23 . VAL A 1 99  ? 5.24400   -26.66400 5.37800   1.000 27.70000  ? 99  VAL A HG23 1 
ATOM   1821 N  N    . SER A 1 100 ? 6.36500   -24.61800 9.66100   1.000 23.50000  ? 100 SER A N    1 
ATOM   1822 C  CA   . SER A 1 100 ? 7.22800   -24.92500 10.79300  1.000 25.50000  ? 100 SER A CA   1 
ATOM   1823 C  C    . SER A 1 100 ? 6.44100   -25.34300 12.02200  1.000 29.35000  ? 100 SER A C    1 
ATOM   1824 O  O    . SER A 1 100 ? 7.05200   -25.58300 13.07400  1.000 35.42000  ? 100 SER A O    1 
ATOM   1825 C  CB   . SER A 1 100 ? 8.06200   -23.69000 11.14700  1.000 23.83000  ? 100 SER A CB   1 
ATOM   1826 O  OG   . SER A 1 100 ? 8.88300   -23.27300 10.07800  1.000 29.98000  ? 100 SER A OG   1 
ATOM   1827 H  H    . SER A 1 100 ? 6.08700   -23.80400 9.65500   1.000 28.22000  ? 100 SER A H    1 
ATOM   1828 H  HA   . SER A 1 100 ? 7.82600   -25.64800 10.54700  1.000 30.62000  ? 100 SER A HA   1 
ATOM   1829 H  HB2  . SER A 1 100 ? 7.46000   -22.96500 11.37600  1.000 28.62000  ? 100 SER A HB2  1 
ATOM   1830 H  HB3  . SER A 1 100 ? 8.62700   -23.90500 11.90600  1.000 28.62000  ? 100 SER A HB3  1 
ATOM   1831 H  HG   . SER A 1 100 ? 8.41300   -22.92900 9.47200   1.000 35.99000  ? 100 SER A HG   1 
ATOM   1832 N  N    A ASP A 1 101 ? 5.11800   -25.44900 11.92300  0.540 23.92000  ? 101 ASP A N    1 
ATOM   1833 N  N    B ASP A 1 101 ? 5.11500   -25.44700 11.91900  0.460 23.82000  ? 101 ASP A N    1 
ATOM   1834 C  CA   A ASP A 1 101 ? 4.25200   -25.65800 13.08000  0.540 30.25000  ? 101 ASP A CA   1 
ATOM   1835 C  CA   B ASP A 1 101 ? 4.25000   -25.66500 13.07600  0.460 30.33000  ? 101 ASP A CA   1 
ATOM   1836 C  C    A ASP A 1 101 ? 4.08400   -27.12300 13.44400  0.540 32.62000  ? 101 ASP A C    1 
ATOM   1837 C  C    B ASP A 1 101 ? 4.29300   -27.09600 13.58900  0.460 32.86000  ? 101 ASP A C    1 
ATOM   1838 O  O    A ASP A 1 101 ? 3.23000   -27.44700 14.28400  0.540 32.36000  ? 101 ASP A O    1 
ATOM   1839 O  O    B ASP A 1 101 ? 3.87200   -27.34400 14.72200  0.460 30.23000  ? 101 ASP A O    1 
ATOM   1840 C  CB   A ASP A 1 101 ? 2.88600   -24.99800 12.85200  0.540 35.53000  ? 101 ASP A CB   1 
ATOM   1841 C  CB   B ASP A 1 101 ? 2.80500   -25.30300 12.71800  0.460 33.36000  ? 101 ASP A CB   1 
ATOM   1842 C  CG   A ASP A 1 101 ? 1.89400   -25.89300 12.10400  0.540 36.56000  ? 101 ASP A CG   1 
ATOM   1843 C  CG   B ASP A 1 101 ? 2.04100   -24.70300 13.88600  0.460 39.03000  ? 101 ASP A CG   1 
ATOM   1844 O  OD1  A ASP A 1 101 ? 2.27500   -26.96400 11.57600  0.540 31.37000  ? 101 ASP A OD1  1 
ATOM   1845 O  OD1  B ASP A 1 101 ? 2.65600   -23.96800 14.68800  0.460 45.20000  ? 101 ASP A OD1  1 
ATOM   1846 O  OD2  A ASP A 1 101 ? 0.71200   -25.49900 12.02000  0.540 42.37000  ? 101 ASP A OD2  1 
ATOM   1847 O  OD2  B ASP A 1 101 ? 0.81800   -24.93600 13.98100  0.460 44.51000  ? 101 ASP A OD2  1 
ATOM   1848 H  H    A ASP A 1 101 ? 4.68900   -25.40300 11.17900  0.540 28.72000  ? 101 ASP A H    1 
ATOM   1849 H  H    B ASP A 1 101 ? 4.68500   -25.39400 11.17600  0.460 28.60000  ? 101 ASP A H    1 
ATOM   1850 H  HA   A ASP A 1 101 ? 4.65800   -25.22000 13.84400  0.540 36.32000  ? 101 ASP A HA   1 
ATOM   1851 H  HA   B ASP A 1 101 ? 4.54300   -25.08300 13.79400  0.460 36.42000  ? 101 ASP A HA   1 
ATOM   1852 H  HB2  A ASP A 1 101 ? 2.49700   -24.77800 13.71300  0.540 42.66000  ? 101 ASP A HB2  1 
ATOM   1853 H  HB2  B ASP A 1 101 ? 2.81200   -24.65200 11.99800  0.460 40.05000  ? 101 ASP A HB2  1 
ATOM   1854 H  HB3  A ASP A 1 101 ? 3.01100   -24.19100 12.32900  0.540 42.66000  ? 101 ASP A HB3  1 
ATOM   1855 H  HB3  B ASP A 1 101 ? 2.33900   -26.10500 12.43500  0.460 40.05000  ? 101 ASP A HB3  1 
ATOM   1856 N  N    . GLY A 1 102 ? 4.87100   -28.01300 12.83100  1.000 30.17000  ? 102 GLY A N    1 
ATOM   1857 C  CA   . GLY A 1 102 ? 4.87900   -29.42200 13.17300  1.000 30.52000  ? 102 GLY A CA   1 
ATOM   1858 C  C    . GLY A 1 102 ? 4.37100   -30.37400 12.11400  1.000 25.39000  ? 102 GLY A C    1 
ATOM   1859 O  O    . GLY A 1 102 ? 4.85700   -31.50900 12.04300  1.000 25.63000  ? 102 GLY A O    1 
ATOM   1860 H  H    . GLY A 1 102 ? 5.41600   -27.80600 12.19900  1.000 36.23000  ? 102 GLY A H    1 
ATOM   1861 H  HA2  . GLY A 1 102 ? 5.79100   -29.68000 13.38000  1.000 36.64000  ? 102 GLY A HA2  1 
ATOM   1862 H  HA3  . GLY A 1 102 ? 4.32800   -29.54700 13.96200  1.000 36.64000  ? 102 GLY A HA3  1 
ATOM   1863 N  N    . ASN A 1 103 ? 3.42300   -29.94200 11.28400  1.000 23.70000  ? 103 ASN A N    1 
ATOM   1864 C  CA   . ASN A 1 103 ? 2.81600   -30.81300 10.28900  1.000 23.67000  ? 103 ASN A CA   1 
ATOM   1865 C  C    . ASN A 1 103 ? 3.38600   -30.59900 8.89400   1.000 16.53000  ? 103 ASN A C    1 
ATOM   1866 O  O    . ASN A 1 103 ? 2.91300   -31.23700 7.93500   1.000 20.37000  ? 103 ASN A O    1 
ATOM   1867 C  CB   . ASN A 1 103 ? 1.30400   -30.60600 10.25900  1.000 33.09000  ? 103 ASN A CB   1 
ATOM   1868 C  CG   . ASN A 1 103 ? 0.64800   -31.05000 11.53900  1.000 52.57000  ? 103 ASN A CG   1 
ATOM   1869 O  OD1  . ASN A 1 103 ? 0.70700   -32.22500 11.89600  1.000 47.38000  ? 103 ASN A OD1  1 
ATOM   1870 N  ND2  . ASN A 1 103 ? 0.01500   -30.11500 12.23800  1.000 77.64000  ? 103 ASN A ND2  1 
ATOM   1871 H  H    . ASN A 1 103 ? 3.11500   -29.14000 11.28000  1.000 28.46000  ? 103 ASN A H    1 
ATOM   1872 H  HA   . ASN A 1 103 ? 2.98400   -31.73400 10.54200  1.000 28.42000  ? 103 ASN A HA   1 
ATOM   1873 H  HB2  . ASN A 1 103 ? 1.11400   -29.66400 10.13300  1.000 39.73000  ? 103 ASN A HB2  1 
ATOM   1874 H  HB3  . ASN A 1 103 ? 0.92600   -31.12200 9.53000   1.000 39.73000  ? 103 ASN A HB3  1 
ATOM   1875 H  HD21 . ASN A 1 103 ? -0.00400  -29.30400 11.95300  1.000 93.18000  ? 103 ASN A HD21 1 
ATOM   1876 H  HD22 . ASN A 1 103 ? -0.37500  -30.32100 12.97600  1.000 93.18000  ? 103 ASN A HD22 1 
ATOM   1877 N  N    . GLY A 1 104 ? 4.38400   -29.74400 8.75400   1.000 17.91000  ? 104 GLY A N    1 
ATOM   1878 C  CA   . GLY A 1 104 ? 4.94800   -29.48800 7.44700   1.000 18.80000  ? 104 GLY A CA   1 
ATOM   1879 C  C    . GLY A 1 104 ? 3.87700   -29.02300 6.48400   1.000 17.77000  ? 104 GLY A C    1 
ATOM   1880 O  O    . GLY A 1 104 ? 2.93900   -28.30700 6.84500   1.000 18.70000  ? 104 GLY A O    1 
ATOM   1881 H  H    . GLY A 1 104 ? 4.74800   -29.30200 9.39500   1.000 21.51000  ? 104 GLY A H    1 
ATOM   1882 H  HA2  . GLY A 1 104 ? 5.62900   -28.80100 7.51300   1.000 22.59000  ? 104 GLY A HA2  1 
ATOM   1883 H  HA3  . GLY A 1 104 ? 5.35000   -30.30000 7.09900   1.000 22.59000  ? 104 GLY A HA3  1 
ATOM   1884 N  N    . MET A 1 105 ? 3.98600   -29.47300 5.25100   1.000 16.34000  ? 105 MET A N    1 
ATOM   1885 C  CA   . MET A 1 105 ? 3.10300   -28.90100 4.21300   1.000 15.26000  ? 105 MET A CA   1 
ATOM   1886 C  C    . MET A 1 105 ? 1.76900   -29.65700 4.21800   1.000 16.20000  ? 105 MET A C    1 
ATOM   1887 O  O    . MET A 1 105 ? 0.85800   -29.28600 3.47000   1.000 16.30000  ? 105 MET A O    1 
ATOM   1888 C  CB   . MET A 1 105 ? 3.85700   -29.12300 2.92100   1.000 16.06000  ? 105 MET A CB   1 
ATOM   1889 C  CG   . MET A 1 105 ? 4.80700   -27.95400 2.56100   1.000 15.58000  ? 105 MET A CG   1 
ATOM   1890 S  SD   . MET A 1 105 ? 5.16800   -27.64400 0.83300   1.000 19.19000  ? 105 MET A SD   1 
ATOM   1891 C  CE   . MET A 1 105 ? 3.72700   -26.85300 0.36400   1.000 19.99000  ? 105 MET A CE   1 
ATOM   1892 H  H    . MET A 1 105 ? 4.53300   -30.08100 4.98600   1.000 19.63000  ? 105 MET A H    1 
ATOM   1893 H  HA   . MET A 1 105 ? 2.91300   -27.95500 4.31500   1.000 18.34000  ? 105 MET A HA   1 
ATOM   1894 H  HB2  . MET A 1 105 ? 4.39100   -29.92800 3.00300   1.000 19.30000  ? 105 MET A HB2  1 
ATOM   1895 H  HB3  . MET A 1 105 ? 3.21800   -29.22100 2.19800   1.000 19.30000  ? 105 MET A HB3  1 
ATOM   1896 H  HG2  . MET A 1 105 ? 4.41600   -27.13900 2.91100   1.000 18.72000  ? 105 MET A HG2  1 
ATOM   1897 H  HG3  . MET A 1 105 ? 5.65900   -28.12500 2.99300   1.000 18.72000  ? 105 MET A HG3  1 
ATOM   1898 H  HE1  . MET A 1 105 ? 3.77200   -26.65000 -0.58400  1.000 24.01000  ? 105 MET A HE1  1 
ATOM   1899 H  HE2  . MET A 1 105 ? 2.97300   -27.43700 0.54100   1.000 24.01000  ? 105 MET A HE2  1 
ATOM   1900 H  HE3  . MET A 1 105 ? 3.63700   -26.03200 0.87300   1.000 24.01000  ? 105 MET A HE3  1 
ATOM   1901 N  N    . ASN A 1 106 ? 1.60100   -30.67400 5.07500   1.000 16.77000  ? 106 ASN A N    1 
ATOM   1902 C  CA   . ASN A 1 106 ? 0.29200   -31.29800 5.29000   1.000 16.18000  ? 106 ASN A CA   1 
ATOM   1903 C  C    . ASN A 1 106 ? -0.75000  -30.31700 5.80400   1.000 17.73000  ? 106 ASN A C    1 
ATOM   1904 O  O    . ASN A 1 106 ? -1.94100  -30.63000 5.68300   1.000 19.86000  ? 106 ASN A O    1 
ATOM   1905 C  CB   . ASN A 1 106 ? 0.41600   -32.48200 6.25800   1.000 18.98000  ? 106 ASN A CB   1 
ATOM   1906 C  CG   . ASN A 1 106 ? 1.25900   -33.61800 5.70100   1.000 17.36000  ? 106 ASN A CG   1 
ATOM   1907 O  OD1  . ASN A 1 106 ? 0.91100   -34.30100 4.72100   1.000 19.86000  ? 106 ASN A OD1  1 
ATOM   1908 N  ND2  . ASN A 1 106 ? 2.42500   -33.76800 6.27800   1.000 20.72000  ? 106 ASN A ND2  1 
ATOM   1909 H  H    . ASN A 1 106 ? 2.23200   -31.02000 5.54600   1.000 20.14000  ? 106 ASN A H    1 
ATOM   1910 H  HA   . ASN A 1 106 ? -0.02200  -31.64600 4.44000   1.000 19.44000  ? 106 ASN A HA   1 
ATOM   1911 H  HB2  . ASN A 1 106 ? 0.83200   -32.17500 7.07900   1.000 22.80000  ? 106 ASN A HB2  1 
ATOM   1912 H  HB3  . ASN A 1 106 ? -0.47000  -32.83000 6.44500   1.000 22.80000  ? 106 ASN A HB3  1 
ATOM   1913 H  HD21 . ASN A 1 106 ? 2.95700   -34.39100 6.01700   1.000 24.89000  ? 106 ASN A HD21 1 
ATOM   1914 H  HD22 . ASN A 1 106 ? 2.65800   -33.24400 6.91900   1.000 24.89000  ? 106 ASN A HD22 1 
ATOM   1915 N  N    . ALA A 1 107 ? -0.33700  -29.14300 6.27000   1.000 17.31000  ? 107 ALA A N    1 
ATOM   1916 C  CA   . ALA A 1 107 ? -1.27400  -28.09700 6.66000   1.000 18.80000  ? 107 ALA A CA   1 
ATOM   1917 C  C    . ALA A 1 107 ? -2.12700  -27.65100 5.48300   1.000 20.66000  ? 107 ALA A C    1 
ATOM   1918 O  O    . ALA A 1 107 ? -3.24500  -27.16100 5.68200   1.000 21.75000  ? 107 ALA A O    1 
ATOM   1919 C  CB   . ALA A 1 107 ? -0.48700  -26.89200 7.18900   1.000 22.64000  ? 107 ALA A CB   1 
ATOM   1920 H  H    . ALA A 1 107 ? 0.48900   -28.92400 6.37000   1.000 20.79000  ? 107 ALA A H    1 
ATOM   1921 H  HA   . ALA A 1 107 ? -1.85600  -28.43600 7.35800   1.000 22.59000  ? 107 ALA A HA   1 
ATOM   1922 H  HB1  . ALA A 1 107 ? -1.11100  -26.19300 7.44000   1.000 27.19000  ? 107 ALA A HB1  1 
ATOM   1923 H  HB2  . ALA A 1 107 ? 0.03100   -27.16700 7.96100   1.000 27.19000  ? 107 ALA A HB2  1 
ATOM   1924 H  HB3  . ALA A 1 107 ? 0.10500   -26.57100 6.49100   1.000 27.19000  ? 107 ALA A HB3  1 
ATOM   1925 N  N    . TRP A 1 108 ? -1.62300  -27.79700 4.25900   1.000 16.43000  ? 108 TRP A N    1 
ATOM   1926 C  CA   . TRP A 1 108 ? -2.36200  -27.46000 3.04500   1.000 17.31000  ? 108 TRP A CA   1 
ATOM   1927 C  C    . TRP A 1 108 ? -2.96400  -28.75100 2.50800   1.000 18.86000  ? 108 TRP A C    1 
ATOM   1928 O  O    . TRP A 1 108 ? -2.25100  -29.60800 1.96500   1.000 17.55000  ? 108 TRP A O    1 
ATOM   1929 C  CB   . TRP A 1 108 ? -1.44800  -26.83700 2.00200   1.000 16.58000  ? 108 TRP A CB   1 
ATOM   1930 C  CG   . TRP A 1 108 ? -1.07800  -25.43900 2.32800   1.000 17.36000  ? 108 TRP A CG   1 
ATOM   1931 C  CD1  . TRP A 1 108 ? -1.78600  -24.31400 1.99300   1.000 19.73000  ? 108 TRP A CD1  1 
ATOM   1932 C  CD2  . TRP A 1 108 ? 0.08900   -24.98800 3.01800   1.000 15.91000  ? 108 TRP A CD2  1 
ATOM   1933 N  NE1  . TRP A 1 108 ? -1.14700  -23.22200 2.45100   1.000 18.33000  ? 108 TRP A NE1  1 
ATOM   1934 C  CE2  . TRP A 1 108 ? 0.01600   -23.58500 3.08700   1.000 17.84000  ? 108 TRP A CE2  1 
ATOM   1935 C  CE3  . TRP A 1 108 ? 1.18500   -25.63400 3.59300   1.000 17.44000  ? 108 TRP A CE3  1 
ATOM   1936 C  CZ2  . TRP A 1 108 ? 0.98700   -22.81900 3.69600   1.000 17.07000  ? 108 TRP A CZ2  1 
ATOM   1937 C  CZ3  . TRP A 1 108 ? 2.13900   -24.87400 4.23900   1.000 18.90000  ? 108 TRP A CZ3  1 
ATOM   1938 C  CH2  . TRP A 1 108 ? 2.04500   -23.46700 4.27800   1.000 20.52000  ? 108 TRP A CH2  1 
ATOM   1939 H  H    . TRP A 1 108 ? -0.83300  -28.09800 4.10300   1.000 19.74000  ? 108 TRP A H    1 
ATOM   1940 H  HA   . TRP A 1 108 ? -3.06500  -26.82600 3.25600   1.000 20.80000  ? 108 TRP A HA   1 
ATOM   1941 H  HB2  . TRP A 1 108 ? -0.63200  -27.35800 1.94500   1.000 19.92000  ? 108 TRP A HB2  1 
ATOM   1942 H  HB3  . TRP A 1 108 ? -1.90100  -26.83600 1.14400   1.000 19.92000  ? 108 TRP A HB3  1 
ATOM   1943 H  HD1  . TRP A 1 108 ? -2.58800  -24.30700 1.52100   1.000 23.70000  ? 108 TRP A HD1  1 
ATOM   1944 H  HE1  . TRP A 1 108 ? -1.42600  -22.41400 2.35900   1.000 22.02000  ? 108 TRP A HE1  1 
ATOM   1945 H  HE3  . TRP A 1 108 ? 1.27000   -26.55900 3.54100   1.000 20.95000  ? 108 TRP A HE3  1 
ATOM   1946 H  HZ2  . TRP A 1 108 ? 0.92700   -21.89100 3.71000   1.000 20.51000  ? 108 TRP A HZ2  1 
ATOM   1947 H  HZ3  . TRP A 1 108 ? 2.85500   -25.29600 4.65600   1.000 22.70000  ? 108 TRP A HZ3  1 
ATOM   1948 H  HH2  . TRP A 1 108 ? 2.70800   -22.97300 4.70300   1.000 24.65000  ? 108 TRP A HH2  1 
ATOM   1949 N  N    A VAL A 1 109 ? -4.28200  -28.88300 2.67800   0.600 22.86000  ? 109 VAL A N    1 
ATOM   1950 N  N    B VAL A 1 109 ? -4.27400  -28.93200 2.67800   0.400 22.85000  ? 109 VAL A N    1 
ATOM   1951 C  CA   A VAL A 1 109 ? -4.97200  -30.09700 2.27100   0.600 21.36000  ? 109 VAL A CA   1 
ATOM   1952 C  CA   B VAL A 1 109 ? -4.82700  -30.22100 2.28300   0.400 19.49000  ? 109 VAL A CA   1 
ATOM   1953 C  C    A VAL A 1 109 ? -4.70900  -30.39000 0.80400   0.600 18.23000  ? 109 VAL A C    1 
ATOM   1954 C  C    B VAL A 1 109 ? -4.71600  -30.42500 0.76700   0.400 18.43000  ? 109 VAL A C    1 
ATOM   1955 O  O    A VAL A 1 109 ? -4.46000  -31.54300 0.43100   0.600 19.83000  ? 109 VAL A O    1 
ATOM   1956 O  O    B VAL A 1 109 ? -4.58900  -31.56400 0.30800   0.400 20.22000  ? 109 VAL A O    1 
ATOM   1957 C  CB   A VAL A 1 109 ? -6.48100  -29.96300 2.55600   0.600 26.20000  ? 109 VAL A CB   1 
ATOM   1958 C  CB   B VAL A 1 109 ? -6.26700  -30.41600 2.79700   0.400 28.30000  ? 109 VAL A CB   1 
ATOM   1959 C  CG1  A VAL A 1 109 ? -7.21400  -31.24000 2.14700   0.600 24.53000  ? 109 VAL A CG1  1 
ATOM   1960 C  CG1  B VAL A 1 109 ? -6.33500  -30.22400 4.30500   0.400 34.10000  ? 109 VAL A CG1  1 
ATOM   1961 C  CG2  A VAL A 1 109 ? -6.71800  -29.66000 4.02100   0.600 32.30000  ? 109 VAL A CG2  1 
ATOM   1962 C  CG2  B VAL A 1 109 ? -7.20700  -29.47600 2.07400   0.400 32.93000  ? 109 VAL A CG2  1 
ATOM   1963 H  H    A VAL A 1 109 ? -4.79400  -28.28500 3.02500   0.600 27.45000  ? 109 VAL A H    1 
ATOM   1964 H  H    B VAL A 1 109 ? -4.82800  -28.35800 3.00000   0.400 27.44000  ? 109 VAL A H    1 
ATOM   1965 H  HA   A VAL A 1 109 ? -4.62700  -30.84000 2.79100   0.600 25.66000  ? 109 VAL A HA   1 
ATOM   1966 H  HA   B VAL A 1 109 ? -4.29300  -30.90700 2.71200   0.400 23.40000  ? 109 VAL A HA   1 
ATOM   1967 H  HB   A VAL A 1 109 ? -6.83700  -29.22800 2.03400   0.600 31.46000  ? 109 VAL A HB   1 
ATOM   1968 H  HB   B VAL A 1 109 ? -6.55200  -31.32400 2.61200   0.400 33.98000  ? 109 VAL A HB   1 
ATOM   1969 H  HG11 A VAL A 1 109 ? -8.12800  -31.19700 2.46900   0.600 29.46000  ? 109 VAL A HG11 1 
ATOM   1970 H  HG11 B VAL A 1 109 ? -7.13500  -30.65600 4.64300   0.400 40.95000  ? 109 VAL A HG11 1 
ATOM   1971 H  HG12 A VAL A 1 109 ? -7.20700  -31.31200 1.17900   0.600 29.46000  ? 109 VAL A HG12 1 
ATOM   1972 H  HG12 B VAL A 1 109 ? -5.54800  -30.62200 4.71000   0.400 40.95000  ? 109 VAL A HG12 1 
ATOM   1973 H  HG13 A VAL A 1 109 ? -6.76100  -32.00400 2.53800   0.600 29.46000  ? 109 VAL A HG13 1 
ATOM   1974 H  HG13 B VAL A 1 109 ? -6.36300  -29.27500 4.50100   0.400 40.95000  ? 109 VAL A HG13 1 
ATOM   1975 H  HG21 A VAL A 1 109 ? -7.66500  -29.75000 4.21300   0.600 38.78000  ? 109 VAL A HG21 1 
ATOM   1976 H  HG21 B VAL A 1 109 ? -7.83300  -29.10200 2.71400   0.400 39.54000  ? 109 VAL A HG21 1 
ATOM   1977 H  HG22 A VAL A 1 109 ? -6.21100  -30.28700 4.56000   0.600 38.78000  ? 109 VAL A HG22 1 
ATOM   1978 H  HG22 B VAL A 1 109 ? -6.69000  -28.76600 1.66300   0.400 39.54000  ? 109 VAL A HG22 1 
ATOM   1979 H  HG23 A VAL A 1 109 ? -6.42700  -28.75400 4.20700   0.600 38.78000  ? 109 VAL A HG23 1 
ATOM   1980 H  HG23 B VAL A 1 109 ? -7.68800  -29.97300 1.39300   0.400 39.54000  ? 109 VAL A HG23 1 
ATOM   1981 N  N    . ALA A 1 110 ? -4.73100  -29.36400 -0.04000  1.000 19.14000  ? 110 ALA A N    1 
ATOM   1982 C  CA   . ALA A 1 110 ? -4.54000  -29.58000 -1.47600  1.000 18.80000  ? 110 ALA A CA   1 
ATOM   1983 C  C    . ALA A 1 110 ? -3.14800  -30.12100 -1.75800  1.000 20.42000  ? 110 ALA A C    1 
ATOM   1984 O  O    . ALA A 1 110 ? -2.95600  -30.90700 -2.69100  1.000 20.66000  ? 110 ALA A O    1 
ATOM   1985 C  CB   . ALA A 1 110 ? -4.78300  -28.31200 -2.28000  1.000 25.95000  ? 110 ALA A CB   1 
ATOM   1986 H  H    . ALA A 1 110 ? -4.85400  -28.54400 0.18800   1.000 22.99000  ? 110 ALA A H    1 
ATOM   1987 H  HA   . ALA A 1 110 ? -5.20100  -30.22600 -1.76600  1.000 22.58000  ? 110 ALA A HA   1 
ATOM   1988 H  HB1  . ALA A 1 110 ? -4.69000  -28.51500 -3.22400  1.000 31.16000  ? 110 ALA A HB1  1 
ATOM   1989 H  HB2  . ALA A 1 110 ? -5.67900  -27.98900 -2.09800  1.000 31.16000  ? 110 ALA A HB2  1 
ATOM   1990 H  HB3  . ALA A 1 110 ? -4.13100  -27.64300 -2.02000  1.000 31.16000  ? 110 ALA A HB3  1 
ATOM   1991 N  N    . TRP A 1 111 ? -2.13900  -29.65900 -1.00900  1.000 16.92000  ? 111 TRP A N    1 
ATOM   1992 C  CA   . TRP A 1 111 ? -0.80600  -30.22700 -1.18500  1.000 16.58000  ? 111 TRP A CA   1 
ATOM   1993 C  C    . TRP A 1 111 ? -0.82300  -31.71300 -0.87700  1.000 18.19000  ? 111 TRP A C    1 
ATOM   1994 O  O    . TRP A 1 111 ? -0.31400  -32.53400 -1.66300  1.000 16.62000  ? 111 TRP A O    1 
ATOM   1995 C  CB   . TRP A 1 111 ? 0.24000   -29.50600 -0.30700  1.000 16.20000  ? 111 TRP A CB   1 
ATOM   1996 C  CG   . TRP A 1 111 ? 1.60400   -30.11900 -0.47900  1.000 15.74000  ? 111 TRP A CG   1 
ATOM   1997 C  CD1  . TRP A 1 111 ? 2.50900   -29.85200 -1.46900  1.000 18.01000  ? 111 TRP A CD1  1 
ATOM   1998 C  CD2  . TRP A 1 111 ? 2.19100   -31.10800 0.34200   1.000 14.46000  ? 111 TRP A CD2  1 
ATOM   1999 N  NE1  . TRP A 1 111 ? 3.60100   -30.65000 -1.32300  1.000 17.38000  ? 111 TRP A NE1  1 
ATOM   2000 C  CE2  . TRP A 1 111 ? 3.46100   -31.40500 -0.19800  1.000 15.25000  ? 111 TRP A CE2  1 
ATOM   2001 C  CE3  . TRP A 1 111 ? 1.77700   -31.78000 1.49400   1.000 15.37000  ? 111 TRP A CE3  1 
ATOM   2002 C  CZ2  . TRP A 1 111 ? 4.30000   -32.35400 0.36400   1.000 18.00000  ? 111 TRP A CZ2  1 
ATOM   2003 C  CZ3  . TRP A 1 111 ? 2.60700   -32.66800 2.07300   1.000 19.46000  ? 111 TRP A CZ3  1 
ATOM   2004 C  CH2  . TRP A 1 111 ? 3.86100   -32.97300 1.50400   1.000 18.85000  ? 111 TRP A CH2  1 
ATOM   2005 H  H    . TRP A 1 111 ? -2.20100  -29.03900 -0.41600  1.000 20.33000  ? 111 TRP A H    1 
ATOM   2006 H  HA   . TRP A 1 111 ? -0.54000  -30.09400 -2.10800  1.000 19.92000  ? 111 TRP A HA   1 
ATOM   2007 H  HB2  . TRP A 1 111 ? 0.28800   -28.57200 -0.56400  1.000 19.47000  ? 111 TRP A HB2  1 
ATOM   2008 H  HB3  . TRP A 1 111 ? -0.01500  -29.58000 0.62600   1.000 19.47000  ? 111 TRP A HB3  1 
ATOM   2009 H  HD1  . TRP A 1 111 ? 2.39600   -29.22000 -2.14100  1.000 21.63000  ? 111 TRP A HD1  1 
ATOM   2010 H  HE1  . TRP A 1 111 ? 4.27400   -30.67400 -1.85700  1.000 20.88000  ? 111 TRP A HE1  1 
ATOM   2011 H  HE3  . TRP A 1 111 ? 0.93600   -31.61600 1.85800   1.000 18.46000  ? 111 TRP A HE3  1 
ATOM   2012 H  HZ2  . TRP A 1 111 ? 5.12300   -32.56000 -0.01500  1.000 21.62000  ? 111 TRP A HZ2  1 
ATOM   2013 H  HZ3  . TRP A 1 111 ? 2.34900   -33.08800 2.86200   1.000 23.38000  ? 111 TRP A HZ3  1 
ATOM   2014 H  HH2  . TRP A 1 111 ? 4.40300   -33.61000 1.91100   1.000 22.65000  ? 111 TRP A HH2  1 
ATOM   2015 N  N    A ARG A 1 112 ? -1.40700  -32.10300 0.25900   0.590 17.01000  ? 112 ARG A N    1 
ATOM   2016 N  N    B ARG A 1 112 ? -1.44900  -32.07600 0.24300   0.410 17.07000  ? 112 ARG A N    1 
ATOM   2017 C  CA   A ARG A 1 112 ? -1.42000  -33.51800 0.61500   0.590 18.07000  ? 112 ARG A CA   1 
ATOM   2018 C  CA   B ARG A 1 112 ? -1.49100  -33.46100 0.68600   0.410 17.94000  ? 112 ARG A CA   1 
ATOM   2019 C  C    A ARG A 1 112 ? -2.14800  -34.32800 -0.45400  0.590 16.86000  ? 112 ARG A C    1 
ATOM   2020 C  C    B ARG A 1 112 ? -2.20400  -34.33600 -0.33400  0.410 17.25000  ? 112 ARG A C    1 
ATOM   2021 O  O    A ARG A 1 112 ? -1.69400  -35.41100 -0.85200  0.590 18.66000  ? 112 ARG A O    1 
ATOM   2022 O  O    B ARG A 1 112 ? -1.80500  -35.48600 -0.56400  0.410 20.72000  ? 112 ARG A O    1 
ATOM   2023 C  CB   A ARG A 1 112 ? -2.06600  -33.73500 1.99300   0.590 20.14000  ? 112 ARG A CB   1 
ATOM   2024 C  CB   B ARG A 1 112 ? -2.20700  -33.52500 2.04100   0.410 22.43000  ? 112 ARG A CB   1 
ATOM   2025 C  CG   A ARG A 1 112 ? -2.29500  -35.19400 2.35400   0.590 27.93000  ? 112 ARG A CG   1 
ATOM   2026 C  CG   B ARG A 1 112 ? -2.10500  -34.84500 2.77000   0.410 27.40000  ? 112 ARG A CG   1 
ATOM   2027 C  CD   A ARG A 1 112 ? -2.98100  -35.37300 3.72100   0.590 36.92000  ? 112 ARG A CD   1 
ATOM   2028 C  CD   B ARG A 1 112 ? -2.60900  -34.71600 4.21700   0.410 32.11000  ? 112 ARG A CD   1 
ATOM   2029 N  NE   A ARG A 1 112 ? -3.28200  -36.78000 3.96600   0.590 49.07000  ? 112 ARG A NE   1 
ATOM   2030 N  NE   B ARG A 1 112 ? -3.79800  -33.87800 4.35900   0.410 38.67000  ? 112 ARG A NE   1 
ATOM   2031 C  CZ   A ARG A 1 112 ? -4.37600  -37.40100 3.54600   0.590 46.29000  ? 112 ARG A CZ   1 
ATOM   2032 C  CZ   B ARG A 1 112 ? -5.03800  -34.25700 4.07200   0.410 40.68000  ? 112 ARG A CZ   1 
ATOM   2033 N  NH1  A ARG A 1 112 ? -5.32200  -36.76100 2.87700   0.590 32.23000  ? 112 ARG A NH1  1 
ATOM   2034 N  NH1  B ARG A 1 112 ? -5.30100  -35.45400 3.57100   0.410 40.94000  ? 112 ARG A NH1  1 
ATOM   2035 N  NH2  A ARG A 1 112 ? -4.52300  -38.69900 3.80000   0.590 51.57000  ? 112 ARG A NH2  1 
ATOM   2036 N  NH2  B ARG A 1 112 ? -6.04300  -33.41700 4.30200   0.410 37.80000  ? 112 ARG A NH2  1 
ATOM   2037 H  H    A ARG A 1 112 ? -1.79100  -31.58100 0.82400   0.590 20.43000  ? 112 ARG A H    1 
ATOM   2038 H  H    B ARG A 1 112 ? -1.86100  -31.53300 0.76700   0.410 20.50000  ? 112 ARG A H    1 
ATOM   2039 H  HA   A ARG A 1 112 ? -0.50400  -33.83200 0.67800   0.590 21.70000  ? 112 ARG A HA   1 
ATOM   2040 H  HA   B ARG A 1 112 ? -0.58800  -33.79900 0.79200   0.410 21.55000  ? 112 ARG A HA   1 
ATOM   2041 H  HB2  A ARG A 1 112 ? -1.48600  -33.35200 2.67000   0.590 24.19000  ? 112 ARG A HB2  1 
ATOM   2042 H  HB2  B ARG A 1 112 ? -1.82600  -32.84600 2.62000   0.410 26.94000  ? 112 ARG A HB2  1 
ATOM   2043 H  HB3  A ARG A 1 112 ? -2.92800  -33.29000 2.00400   0.590 24.19000  ? 112 ARG A HB3  1 
ATOM   2044 H  HB3  B ARG A 1 112 ? -3.14900  -33.34700 1.89700   0.410 26.94000  ? 112 ARG A HB3  1 
ATOM   2045 H  HG2  A ARG A 1 112 ? -2.86100  -35.60200 1.68000   0.590 33.54000  ? 112 ARG A HG2  1 
ATOM   2046 H  HG2  B ARG A 1 112 ? -2.64700  -35.50800 2.31500   0.410 32.90000  ? 112 ARG A HG2  1 
ATOM   2047 H  HG3  A ARG A 1 112 ? -1.43900  -35.65000 2.38800   0.590 33.54000  ? 112 ARG A HG3  1 
ATOM   2048 H  HG3  B ARG A 1 112 ? -1.17900  -35.13200 2.79200   0.410 32.90000  ? 112 ARG A HG3  1 
ATOM   2049 H  HD2  A ARG A 1 112 ? -2.39200  -35.05600 4.42400   0.590 44.32000  ? 112 ARG A HD2  1 
ATOM   2050 H  HD2  B ARG A 1 112 ? -2.83000  -35.59900 4.55000   0.410 38.55000  ? 112 ARG A HD2  1 
ATOM   2051 H  HD3  A ARG A 1 112 ? -3.81300  -34.87300 3.73500   0.590 44.32000  ? 112 ARG A HD3  1 
ATOM   2052 H  HD3  B ARG A 1 112 ? -1.90600  -34.32300 4.75800   0.410 38.55000  ? 112 ARG A HD3  1 
ATOM   2053 H  HE   A ARG A 1 112 ? -2.70900  -37.23900 4.41500   0.590 58.90000  ? 112 ARG A HE   1 
ATOM   2054 H  HE   B ARG A 1 112 ? -3.68600  -33.07700 4.65100   0.410 46.43000  ? 112 ARG A HE   1 
ATOM   2055 H  HH11 A ARG A 1 112 ? -5.23600  -35.92300 2.70500   0.590 38.70000  ? 112 ARG A HH11 1 
ATOM   2056 H  HH11 B ARG A 1 112 ? -4.66100  -36.00900 3.42300   0.410 49.14000  ? 112 ARG A HH11 1 
ATOM   2057 H  HH12 A ARG A 1 112 ? -6.02400  -37.18400 2.61300   0.590 38.70000  ? 112 ARG A HH12 1 
ATOM   2058 H  HH12 B ARG A 1 112 ? -6.11300  -35.67700 3.39300   0.410 49.14000  ? 112 ARG A HH12 1 
ATOM   2059 H  HH21 A ARG A 1 112 ? -3.91300  -39.12400 4.23200   0.590 61.91000  ? 112 ARG A HH21 1 
ATOM   2060 H  HH21 B ARG A 1 112 ? -5.88500  -32.63800 4.63200   0.410 45.38000  ? 112 ARG A HH21 1 
ATOM   2061 H  HH22 A ARG A 1 112 ? -5.22800  -39.11300 3.53200   0.590 61.91000  ? 112 ARG A HH22 1 
ATOM   2062 H  HH22 B ARG A 1 112 ? -6.85000  -33.65100 4.12000   0.410 45.38000  ? 112 ARG A HH22 1 
ATOM   2063 N  N    . ASN A 1 113 ? -3.27000  -33.81800 -0.93700  1.000 17.30000  ? 113 ASN A N    1 
ATOM   2064 C  CA   . ASN A 1 113 ? -4.11400  -34.62700 -1.82200  1.000 19.91000  ? 113 ASN A CA   1 
ATOM   2065 C  C    . ASN A 1 113 ? -3.72100  -34.58600 -3.29200  1.000 21.42000  ? 113 ASN A C    1 
ATOM   2066 O  O    . ASN A 1 113 ? -4.08500  -35.51300 -4.04300  1.000 21.82000  ? 113 ASN A O    1 
ATOM   2067 C  CB   . ASN A 1 113 ? -5.58100  -34.21300 -1.66600  1.000 19.07000  ? 113 ASN A CB   1 
ATOM   2068 C  CG   . ASN A 1 113 ? -6.14400  -34.62400 -0.34100  1.000 19.84000  ? 113 ASN A CG   1 
ATOM   2069 O  OD1  . ASN A 1 113 ? -5.68500  -35.59100 0.24800   1.000 23.23000  ? 113 ASN A OD1  1 
ATOM   2070 N  ND2  . ASN A 1 113 ? -7.15600  -33.91200 0.13400   1.000 21.33000  ? 113 ASN A ND2  1 
ATOM   2071 H  H    . ASN A 1 113 ? -3.56200  -33.02600 -0.77500  1.000 20.78000  ? 113 ASN A H    1 
ATOM   2072 H  HA   . ASN A 1 113 ? -4.02800  -35.55400 -1.54800  1.000 23.91000  ? 113 ASN A HA   1 
ATOM   2073 H  HB2  . ASN A 1 113 ? -5.64900  -33.24800 -1.73800  1.000 22.90000  ? 113 ASN A HB2  1 
ATOM   2074 H  HB3  . ASN A 1 113 ? -6.10800  -34.63500 -2.36300  1.000 22.90000  ? 113 ASN A HB3  1 
ATOM   2075 H  HD21 . ASN A 1 113 ? -7.50700  -34.11700 0.89200   1.000 25.62000  ? 113 ASN A HD21 1 
ATOM   2076 H  HD22 . ASN A 1 113 ? -7.46200  -33.24600 -0.31600  1.000 25.62000  ? 113 ASN A HD22 1 
ATOM   2077 N  N    . ARG A 1 114 ? -2.97100  -33.57700 -3.72400  1.000 17.83000  ? 114 ARG A N    1 
ATOM   2078 C  CA   . ARG A 1 114 ? -2.69000  -33.35700 -5.14200  1.000 20.48000  ? 114 ARG A CA   1 
ATOM   2079 C  C    . ARG A 1 114 ? -1.23700  -33.23700 -5.48800  1.000 20.16000  ? 114 ARG A C    1 
ATOM   2080 O  O    . ARG A 1 114 ? -0.90500  -33.35400 -6.68000  1.000 22.74000  ? 114 ARG A O    1 
ATOM   2081 C  CB   . ARG A 1 114 ? -3.43900  -32.14100 -5.64600  1.000 21.10000  ? 114 ARG A CB   1 
ATOM   2082 C  CG   . ARG A 1 114 ? -4.89800  -32.39300 -5.26100  1.000 26.36000  ? 114 ARG A CG   1 
ATOM   2083 C  CD   . ARG A 1 114 ? -5.77900  -31.44900 -5.86500  1.000 28.14000  ? 114 ARG A CD   1 
ATOM   2084 N  NE   . ARG A 1 114 ? -5.89900  -31.57100 -7.30400  1.000 21.27000  ? 114 ARG A NE   1 
ATOM   2085 C  CZ   . ARG A 1 114 ? -6.63600  -30.72000 -7.98200  1.000 22.89000  ? 114 ARG A CZ   1 
ATOM   2086 N  NH1  . ARG A 1 114 ? -7.28600  -29.75900 -7.35800  1.000 23.61000  ? 114 ARG A NH1  1 
ATOM   2087 N  NH2  . ARG A 1 114 ? -6.72900  -30.84700 -9.30100  1.000 24.67000  ? 114 ARG A NH2  1 
ATOM   2088 H  H    . ARG A 1 114 ? -2.60700  -32.99400 -3.20700  1.000 21.41000  ? 114 ARG A H    1 
ATOM   2089 H  HA   . ARG A 1 114 ? -3.01900  -34.12200 -5.63800  1.000 24.59000  ? 114 ARG A HA   1 
ATOM   2090 H  HB2  . ARG A 1 114 ? -3.11600  -31.33400 -5.21600  1.000 25.34000  ? 114 ARG A HB2  1 
ATOM   2091 H  HB3  . ARG A 1 114 ? -3.35900  -32.06000 -6.60900  1.000 25.34000  ? 114 ARG A HB3  1 
ATOM   2092 H  HG2  . ARG A 1 114 ? -5.15700  -33.28000 -5.55400  1.000 31.66000  ? 114 ARG A HG2  1 
ATOM   2093 H  HG3  . ARG A 1 114 ? -4.99100  -32.32100 -4.29800  1.000 31.66000  ? 114 ARG A HG3  1 
ATOM   2094 H  HD2  . ARG A 1 114 ? -6.66400  -31.56600 -5.48700  1.000 33.79000  ? 114 ARG A HD2  1 
ATOM   2095 H  HD3  . ARG A 1 114 ? -5.45200  -30.55500 -5.67400  1.000 33.79000  ? 114 ARG A HD3  1 
ATOM   2096 H  HE   . ARG A 1 114 ? -5.48600  -32.20300 -7.71600  1.000 25.54000  ? 114 ARG A HE   1 
ATOM   2097 H  HH11 . ARG A 1 114 ? -7.22800  -29.68700 -6.50300  1.000 28.36000  ? 114 ARG A HH11 1 
ATOM   2098 H  HH12 . ARG A 1 114 ? -7.76700  -29.20400 -7.80500  1.000 28.36000  ? 114 ARG A HH12 1 
ATOM   2099 H  HH21 . ARG A 1 114 ? -6.30900  -31.48100 -9.70200  1.000 29.62000  ? 114 ARG A HH21 1 
ATOM   2100 H  HH22 . ARG A 1 114 ? -7.20900  -30.29500 -9.75300  1.000 29.62000  ? 114 ARG A HH22 1 
ATOM   2101 N  N    . CYS A 1 115 ? -0.35400  -33.00200 -4.52100  1.000 16.80000  ? 115 CYS A N    1 
ATOM   2102 C  CA   . CYS A 1 115 ? 1.05000   -32.79900 -4.81500  1.000 16.88000  ? 115 CYS A CA   1 
ATOM   2103 C  C    . CYS A 1 115 ? 1.93600   -33.82100 -4.15000  1.000 18.54000  ? 115 CYS A C    1 
ATOM   2104 O  O    . CYS A 1 115 ? 2.89800   -34.28200 -4.76300  1.000 20.32000  ? 115 CYS A O    1 
ATOM   2105 C  CB   . CYS A 1 115 ? 1.48200   -31.40700 -4.30900  1.000 15.43000  ? 115 CYS A CB   1 
ATOM   2106 S  SG   . CYS A 1 115 ? 0.57800   -30.04100 -5.03700  1.000 17.80000  ? 115 CYS A SG   1 
ATOM   2107 H  H    . CYS A 1 115 ? -0.55100  -32.95700 -3.68500  1.000 20.18000  ? 115 CYS A H    1 
ATOM   2108 H  HA   . CYS A 1 115 ? 1.17900   -32.84700 -5.77500  1.000 20.28000  ? 115 CYS A HA   1 
ATOM   2109 H  HB2  . CYS A 1 115 ? 1.34600   -31.37100 -3.34900  1.000 18.54000  ? 115 CYS A HB2  1 
ATOM   2110 H  HB3  . CYS A 1 115 ? 2.42100   -31.28100 -4.51600  1.000 18.54000  ? 115 CYS A HB3  1 
ATOM   2111 N  N    . LYS A 1 116 ? 1.65600   -34.18200 -2.90900  1.000 17.95000  ? 116 LYS A N    1 
ATOM   2112 C  CA   . LYS A 1 116 ? 2.48200   -35.10800 -2.15700  1.000 18.53000  ? 116 LYS A CA   1 
ATOM   2113 C  C    . LYS A 1 116 ? 2.55500   -36.43400 -2.89700  1.000 21.41000  ? 116 LYS A C    1 
ATOM   2114 O  O    . LYS A 1 116 ? 1.53100   -36.98100 -3.31100  1.000 21.63000  ? 116 LYS A O    1 
ATOM   2115 C  CB   . LYS A 1 116 ? 1.82400   -35.31000 -0.79900  1.000 19.74000  ? 116 LYS A CB   1 
ATOM   2116 C  CG   . LYS A 1 116 ? 2.60600   -36.16000 0.18400   1.000 19.82000  ? 116 LYS A CG   1 
ATOM   2117 C  CD   . LYS A 1 116 ? 1.84400   -36.26600 1.49900   1.000 20.22000  ? 116 LYS A CD   1 
ATOM   2118 C  CE   . LYS A 1 116 ? 2.67300   -36.90600 2.61400   1.000 19.85000  ? 116 LYS A CE   1 
ATOM   2119 N  NZ   . LYS A 1 116 ? 1.92800   -36.93800 3.91900   1.000 24.25000  ? 116 LYS A NZ   1 
ATOM   2120 H  H    . LYS A 1 116 ? 0.97600   -33.89700 -2.46700  1.000 21.56000  ? 116 LYS A H    1 
ATOM   2121 H  HA   . LYS A 1 116 ? 3.38300   -34.76900 -2.04200  1.000 22.26000  ? 116 LYS A HA   1 
ATOM   2122 H  HB2  . LYS A 1 116 ? 1.69500   -34.44000 -0.39000  1.000 23.70000  ? 116 LYS A HB2  1 
ATOM   2123 H  HB3  . LYS A 1 116 ? 0.96700   -35.74200 -0.93600  1.000 23.70000  ? 116 LYS A HB3  1 
ATOM   2124 H  HG2  . LYS A 1 116 ? 2.72800   -37.05100 -0.17900  1.000 23.80000  ? 116 LYS A HG2  1 
ATOM   2125 H  HG3  . LYS A 1 116 ? 3.46900   -35.75100 0.35600   1.000 23.80000  ? 116 LYS A HG3  1 
ATOM   2126 H  HD2  . LYS A 1 116 ? 1.58800   -35.37700 1.78900   1.000 24.28000  ? 116 LYS A HD2  1 
ATOM   2127 H  HD3  . LYS A 1 116 ? 1.05400   -36.81200 1.36300   1.000 24.28000  ? 116 LYS A HD3  1 
ATOM   2128 H  HE2  . LYS A 1 116 ? 2.89200   -37.81800 2.36700   1.000 23.84000  ? 116 LYS A HE2  1 
ATOM   2129 H  HE3  . LYS A 1 116 ? 3.48700   -36.39300 2.74200   1.000 23.84000  ? 116 LYS A HE3  1 
ATOM   2130 H  HZ1  . LYS A 1 116 ? 2.37600   -37.42500 4.51400   1.000 29.12000  ? 116 LYS A HZ1  1 
ATOM   2131 H  HZ2  . LYS A 1 116 ? 1.83200   -36.11200 4.23500   1.000 29.12000  ? 116 LYS A HZ2  1 
ATOM   2132 H  HZ3  . LYS A 1 116 ? 1.12200   -37.29800 3.80100   1.000 29.12000  ? 116 LYS A HZ3  1 
ATOM   2133 N  N    . GLY A 1 117 ? 3.76900   -36.94100 -3.07300  1.000 22.52000  ? 117 GLY A N    1 
ATOM   2134 C  CA   . GLY A 1 117 ? 3.96300   -38.21400 -3.75400  1.000 24.96000  ? 117 GLY A CA   1 
ATOM   2135 C  C    . GLY A 1 117 ? 3.94500   -38.15000 -5.26200  1.000 25.15000  ? 117 GLY A C    1 
ATOM   2136 O  O    . GLY A 1 117 ? 3.94400   -39.20500 -5.91300  1.000 32.75000  ? 117 GLY A O    1 
ATOM   2137 H  H    . GLY A 1 117 ? 4.49600   -36.56700 -2.80600  1.000 27.04000  ? 117 GLY A H    1 
ATOM   2138 H  HA2  . GLY A 1 117 ? 4.82000   -38.58000 -3.48600  1.000 29.97000  ? 117 GLY A HA2  1 
ATOM   2139 H  HA3  . GLY A 1 117 ? 3.25900   -38.82200 -3.47800  1.000 29.97000  ? 117 GLY A HA3  1 
ATOM   2140 N  N    . THR A 1 118 ? 3.89900   -36.96800 -5.84600  1.000 22.94000  ? 118 THR A N    1 
ATOM   2141 C  CA   . THR A 1 118 ? 3.96200   -36.77600 -7.28300  1.000 21.46000  ? 118 THR A CA   1 
ATOM   2142 C  C    . THR A 1 118 ? 5.29500   -36.13200 -7.64200  1.000 23.12000  ? 118 THR A C    1 
ATOM   2143 O  O    . THR A 1 118 ? 6.07500   -35.74100 -6.77800  1.000 24.70000  ? 118 THR A O    1 
ATOM   2144 C  CB   . THR A 1 118 ? 2.80100   -35.91700 -7.78500  1.000 25.03000  ? 118 THR A CB   1 
ATOM   2145 O  OG1  . THR A 1 118 ? 3.03500   -34.52300 -7.48400  1.000 23.94000  ? 118 THR A OG1  1 
ATOM   2146 C  CG2  . THR A 1 118 ? 1.48200   -36.36000 -7.17300  1.000 25.80000  ? 118 THR A CG2  1 
ATOM   2147 H  H    . THR A 1 118 ? 3.82900   -36.22900 -5.41300  1.000 27.55000  ? 118 THR A H    1 
ATOM   2148 H  HA   . THR A 1 118 ? 3.89600   -37.63600 -7.72500  1.000 25.77000  ? 118 THR A HA   1 
ATOM   2149 H  HB   . THR A 1 118 ? 2.73300   -36.02200 -8.74700  1.000 30.05000  ? 118 THR A HB   1 
ATOM   2150 H  HG1  . THR A 1 118 ? 3.24200   -34.43500 -6.67500  1.000 28.75000  ? 118 THR A HG1  1 
ATOM   2151 H  HG21 . THR A 1 118 ? 0.74800   -35.87100 -7.57600  1.000 30.98000  ? 118 THR A HG21 1 
ATOM   2152 H  HG22 . THR A 1 118 ? 1.34800   -37.30900 -7.32400  1.000 30.98000  ? 118 THR A HG22 1 
ATOM   2153 H  HG23 . THR A 1 118 ? 1.48600   -36.19100 -6.21800  1.000 30.98000  ? 118 THR A HG23 1 
ATOM   2154 N  N    . ASP A 1 119 ? 5.56500   -36.05400 -8.94700  1.000 27.20000  ? 119 ASP A N    1 
ATOM   2155 C  CA   . ASP A 1 119 ? 6.83500   -35.48300 -9.40900  1.000 26.35000  ? 119 ASP A CA   1 
ATOM   2156 C  C    . ASP A 1 119 ? 6.68900   -33.96500 -9.40100  1.000 27.00000  ? 119 ASP A C    1 
ATOM   2157 O  O    . ASP A 1 119 ? 6.36500   -33.33400 -10.41300 1.000 29.40000  ? 119 ASP A O    1 
ATOM   2158 C  CB   . ASP A 1 119 ? 7.18100   -35.99400 -10.80300 1.000 33.63000  ? 119 ASP A CB   1 
ATOM   2159 C  CG   . ASP A 1 119 ? 8.43800   -35.34200 -11.36200 1.000 51.69000  ? 119 ASP A CG   1 
ATOM   2160 O  OD1  . ASP A 1 119 ? 9.27400   -34.87200 -10.55800 1.000 46.55000  ? 119 ASP A OD1  1 
ATOM   2161 O  OD2  . ASP A 1 119 ? 8.58700   -35.30000 -12.60400 1.000 44.74000  ? 119 ASP A OD2  1 
ATOM   2162 H  H    . ASP A 1 119 ? 5.03900   -36.31900 -9.57400  1.000 32.66000  ? 119 ASP A H    1 
ATOM   2163 H  HA   . ASP A 1 119 ? 7.54800   -35.74000 -8.80300  1.000 31.64000  ? 119 ASP A HA   1 
ATOM   2164 H  HB2  . ASP A 1 119 ? 7.33100   -36.95200 -10.76200 1.000 40.37000  ? 119 ASP A HB2  1 
ATOM   2165 H  HB3  . ASP A 1 119 ? 6.44600   -35.79800 -11.40500 1.000 40.37000  ? 119 ASP A HB3  1 
ATOM   2166 N  N    . VAL A 1 120 ? 6.94800   -33.36000 -8.24000  1.000 28.89000  ? 120 VAL A N    1 
ATOM   2167 C  CA   . VAL A 1 120 ? 6.66800   -31.92900 -8.11700  1.000 24.62000  ? 120 VAL A CA   1 
ATOM   2168 C  C    . VAL A 1 120 ? 7.70000   -31.09500 -8.86700  1.000 28.37000  ? 120 VAL A C    1 
ATOM   2169 O  O    . VAL A 1 120 ? 7.44200   -29.92400 -9.16800  1.000 23.32000  ? 120 VAL A O    1 
ATOM   2170 C  CB   . VAL A 1 120 ? 6.52800   -31.47000 -6.65300  1.000 24.07000  ? 120 VAL A CB   1 
ATOM   2171 C  CG1  . VAL A 1 120 ? 5.33700   -32.13700 -5.98400  1.000 25.99000  ? 120 VAL A CG1  1 
ATOM   2172 C  CG2  . VAL A 1 120 ? 7.77200   -31.73600 -5.88300  1.000 25.25000  ? 120 VAL A CG2  1 
ATOM   2173 H  H    . VAL A 1 120 ? 7.27200   -33.73800 -7.53900  1.000 34.69000  ? 120 VAL A H    1 
ATOM   2174 H  HA   . VAL A 1 120 ? 5.80000   -31.77500 -8.52200  1.000 29.56000  ? 120 VAL A HA   1 
ATOM   2175 H  HB   . VAL A 1 120 ? 6.37600   -30.51200 -6.65500  1.000 28.90000  ? 120 VAL A HB   1 
ATOM   2176 H  HG11 . VAL A 1 120 ? 5.25400   -31.80000 -5.07900  1.000 31.20000  ? 120 VAL A HG11 1 
ATOM   2177 H  HG12 . VAL A 1 120 ? 4.53500   -31.93100 -6.48900  1.000 31.20000  ? 120 VAL A HG12 1 
ATOM   2178 H  HG13 . VAL A 1 120 ? 5.48100   -33.09600 -5.96800  1.000 31.20000  ? 120 VAL A HG13 1 
ATOM   2179 H  HG21 . VAL A 1 120 ? 7.63400   -31.47200 -4.96000  1.000 30.33000  ? 120 VAL A HG21 1 
ATOM   2180 H  HG22 . VAL A 1 120 ? 7.97700   -32.68300 -5.93000  1.000 30.33000  ? 120 VAL A HG22 1 
ATOM   2181 H  HG23 . VAL A 1 120 ? 8.49800   -31.22100 -6.26900  1.000 30.33000  ? 120 VAL A HG23 1 
ATOM   2182 N  N    . GLN A 1 121 ? 8.88000   -31.66000 -9.17700  1.000 26.07000  ? 121 GLN A N    1 
ATOM   2183 C  CA   . GLN A 1 121 ? 9.85800   -30.90200 -9.95000  1.000 24.14000  ? 121 GLN A CA   1 
ATOM   2184 C  C    . GLN A 1 121 ? 9.30600   -30.48800 -11.30500 1.000 23.80000  ? 121 GLN A C    1 
ATOM   2185 O  O    . GLN A 1 121 ? 9.78100   -29.50600 -11.89100 1.000 26.87000  ? 121 GLN A O    1 
ATOM   2186 C  CB   . GLN A 1 121 ? 11.13000  -31.72000 -10.21100 1.000 39.15000  ? 121 GLN A CB   1 
ATOM   2187 C  CG   . GLN A 1 121 ? 12.31500  -30.85300 -10.69200 1.000 65.58000  ? 121 GLN A CG   1 
ATOM   2188 C  CD   . GLN A 1 121 ? 12.54200  -30.86800 -12.21700 1.000 92.87000  ? 121 GLN A CD   1 
ATOM   2189 O  OE1  . GLN A 1 121 ? 12.96800  -29.86200 -12.79400 1.000 71.21000  ? 121 GLN A OE1  1 
ATOM   2190 N  NE2  . GLN A 1 121 ? 12.26300  -32.00000 -12.86300 1.000 88.91000  ? 121 GLN A NE2  1 
ATOM   2191 H  H    . GLN A 1 121 ? 9.12400   -32.45400 -8.95500  1.000 31.31000  ? 121 GLN A H    1 
ATOM   2192 H  HA   . GLN A 1 121 ? 10.09200  -30.12300 -9.42300  1.000 28.98000  ? 121 GLN A HA   1 
ATOM   2193 H  HB2  . GLN A 1 121 ? 11.39600  -32.15900 -9.38800  1.000 46.99000  ? 121 GLN A HB2  1 
ATOM   2194 H  HB3  . GLN A 1 121 ? 10.94500  -32.38100 -10.89500 1.000 46.99000  ? 121 GLN A HB3  1 
ATOM   2195 H  HG2  . GLN A 1 121 ? 12.15100  -29.93300 -10.43000 1.000 78.71000  ? 121 GLN A HG2  1 
ATOM   2196 H  HG3  . GLN A 1 121 ? 13.12700  -31.17800 -10.27300 1.000 78.71000  ? 121 GLN A HG3  1 
ATOM   2197 H  HE21 . GLN A 1 121 ? 11.96900  -32.68200 -12.42900 1.000 106.72000 ? 121 GLN A HE21 1 
ATOM   2198 H  HE22 . GLN A 1 121 ? 12.37600  -32.04900 -13.71400 1.000 106.72000 ? 121 GLN A HE22 1 
ATOM   2199 N  N    . ALA A 1 122 ? 8.31300   -31.20700 -11.82900 1.000 23.82000  ? 122 ALA A N    1 
ATOM   2200 C  CA   . ALA A 1 122 ? 7.72600   -30.83200 -13.10700 1.000 27.12000  ? 122 ALA A CA   1 
ATOM   2201 C  C    . ALA A 1 122 ? 7.18900   -29.40900 -13.07400 1.000 26.69000  ? 122 ALA A C    1 
ATOM   2202 O  O    . ALA A 1 122 ? 7.09200   -28.73600 -14.10700 1.000 25.65000  ? 122 ALA A O    1 
ATOM   2203 C  CB   . ALA A 1 122 ? 6.59100   -31.78800 -13.46300 1.000 31.52000  ? 122 ALA A CB   1 
ATOM   2204 H  H    . ALA A 1 122 ? 7.96700   -31.90700 -11.46800 1.000 28.61000  ? 122 ALA A H    1 
ATOM   2205 H  HA   . ALA A 1 122 ? 8.41100   -30.89400 -13.79100 1.000 32.56000  ? 122 ALA A HA   1 
ATOM   2206 H  HB1  . ALA A 1 122 ? 6.23600   -31.54600 -14.33200 1.000 37.85000  ? 122 ALA A HB1  1 
ATOM   2207 H  HB2  . ALA A 1 122 ? 6.93700   -32.69300 -13.48700 1.000 37.85000  ? 122 ALA A HB2  1 
ATOM   2208 H  HB3  . ALA A 1 122 ? 5.89600   -31.71700 -12.79000 1.000 37.85000  ? 122 ALA A HB3  1 
ATOM   2209 N  N    . TRP A 1 123 ? 6.81400   -28.93400 -11.88700 1.000 23.13000  ? 123 TRP A N    1 
ATOM   2210 C  CA   . TRP A 1 123 ? 6.21900   -27.60900 -11.77100 1.000 21.95000  ? 123 TRP A CA   1 
ATOM   2211 C  C    . TRP A 1 123 ? 7.21200   -26.49200 -12.02300 1.000 21.97000  ? 123 TRP A C    1 
ATOM   2212 O  O    . TRP A 1 123 ? 6.78600   -25.37000 -12.30700 1.000 25.59000  ? 123 TRP A O    1 
ATOM   2213 C  CB   . TRP A 1 123 ? 5.54600   -27.45300 -10.38000 1.000 20.51000  ? 123 TRP A CB   1 
ATOM   2214 C  CG   . TRP A 1 123 ? 4.29500   -28.24500 -10.34600 1.000 22.67000  ? 123 TRP A CG   1 
ATOM   2215 C  CD1  . TRP A 1 123 ? 4.12600   -29.46100 -9.77900  1.000 24.87000  ? 123 TRP A CD1  1 
ATOM   2216 C  CD2  . TRP A 1 123 ? 3.04500   -27.88900 -10.92900 1.000 19.53000  ? 123 TRP A CD2  1 
ATOM   2217 N  NE1  . TRP A 1 123 ? 2.85500   -29.90800 -9.99500  1.000 24.79000  ? 123 TRP A NE1  1 
ATOM   2218 C  CE2  . TRP A 1 123 ? 2.16200   -28.96600 -10.69400 1.000 23.31000  ? 123 TRP A CE2  1 
ATOM   2219 C  CE3  . TRP A 1 123 ? 2.59000   -26.79100 -11.65500 1.000 24.25000  ? 123 TRP A CE3  1 
ATOM   2220 C  CZ2  . TRP A 1 123 ? 0.84500   -28.95700 -11.12500 1.000 30.39000  ? 123 TRP A CZ2  1 
ATOM   2221 C  CZ3  . TRP A 1 123 ? 1.27800   -26.80100 -12.11800 1.000 30.65000  ? 123 TRP A CZ3  1 
ATOM   2222 C  CH2  . TRP A 1 123 ? 0.42700   -27.88300 -11.85100 1.000 28.99000  ? 123 TRP A CH2  1 
ATOM   2223 H  H    . TRP A 1 123 ? 6.89300   -29.35600 -11.14200 1.000 27.77000  ? 123 TRP A H    1 
ATOM   2224 H  HA   . TRP A 1 123 ? 5.52500   -27.51800 -12.44300 1.000 26.36000  ? 123 TRP A HA   1 
ATOM   2225 H  HB2  . TRP A 1 123 ? 6.14300   -27.77900 -9.68900  1.000 24.63000  ? 123 TRP A HB2  1 
ATOM   2226 H  HB3  . TRP A 1 123 ? 5.33200   -26.52100 -10.22200 1.000 24.63000  ? 123 TRP A HB3  1 
ATOM   2227 H  HD1  . TRP A 1 123 ? 4.78200   -29.92500 -9.31100  1.000 29.87000  ? 123 TRP A HD1  1 
ATOM   2228 H  HE1  . TRP A 1 123 ? 2.54200   -30.66400 -9.73200  1.000 29.76000  ? 123 TRP A HE1  1 
ATOM   2229 H  HE3  . TRP A 1 123 ? 3.15000   -26.06800 -11.82600 1.000 29.12000  ? 123 TRP A HE3  1 
ATOM   2230 H  HZ2  . TRP A 1 123 ? 0.26700   -29.65900 -10.92700 1.000 36.49000  ? 123 TRP A HZ2  1 
ATOM   2231 H  HZ3  . TRP A 1 123 ? 0.96000   -26.08000 -12.61200 1.000 36.80000  ? 123 TRP A HZ3  1 
ATOM   2232 H  HH2  . TRP A 1 123 ? -0.44400  -27.86600 -12.17800 1.000 34.80000  ? 123 TRP A HH2  1 
ATOM   2233 N  N    . ILE A 1 124 ? 8.51100   -26.77200 -11.93500 1.000 23.47000  ? 124 ILE A N    1 
ATOM   2234 C  CA   . ILE A 1 124 ? 9.52200   -25.76400 -12.20100 1.000 21.67000  ? 124 ILE A CA   1 
ATOM   2235 C  C    . ILE A 1 124 ? 10.33100  -26.08300 -13.45200 1.000 22.53000  ? 124 ILE A C    1 
ATOM   2236 O  O    . ILE A 1 124 ? 11.27300  -25.35400 -13.77300 1.000 23.94000  ? 124 ILE A O    1 
ATOM   2237 C  CB   . ILE A 1 124 ? 10.40700  -25.49300 -10.97700 1.000 23.05000  ? 124 ILE A CB   1 
ATOM   2238 C  CG1  . ILE A 1 124 ? 11.11200  -26.74400 -10.48300 1.000 29.85000  ? 124 ILE A CG1  1 
ATOM   2239 C  CG2  . ILE A 1 124 ? 9.53600   -24.92400 -9.82700  1.000 25.65000  ? 124 ILE A CG2  1 
ATOM   2240 C  CD1  . ILE A 1 124 ? 12.27700  -26.45000 -9.51200  1.000 33.65000  ? 124 ILE A CD1  1 
ATOM   2241 H  H    . ILE A 1 124 ? 8.82700   -27.54300 -11.72100 1.000 28.19000  ? 124 ILE A H    1 
ATOM   2242 H  HA   . ILE A 1 124 ? 9.06600   -24.92900 -12.38700 1.000 26.03000  ? 124 ILE A HA   1 
ATOM   2243 H  HB   . ILE A 1 124 ? 11.08400  -24.85500 -11.25200 1.000 27.68000  ? 124 ILE A HB   1 
ATOM   2244 H  HG12 . ILE A 1 124 ? 10.47000  -27.30200 -10.01600 1.000 35.84000  ? 124 ILE A HG12 1 
ATOM   2245 H  HG13 . ILE A 1 124 ? 11.47300  -27.22200 -11.24600 1.000 35.84000  ? 124 ILE A HG13 1 
ATOM   2246 H  HG21 . ILE A 1 124 ? 10.10500  -24.73700 -9.06400  1.000 30.80000  ? 124 ILE A HG21 1 
ATOM   2247 H  HG22 . ILE A 1 124 ? 9.10900   -24.10700 -10.12900 1.000 30.80000  ? 124 ILE A HG22 1 
ATOM   2248 H  HG23 . ILE A 1 124 ? 8.86400   -25.58000 -9.58600  1.000 30.80000  ? 124 ILE A HG23 1 
ATOM   2249 H  HD11 . ILE A 1 124 ? 12.72100  -27.28400 -9.29100  1.000 40.40000  ? 124 ILE A HD11 1 
ATOM   2250 H  HD12 . ILE A 1 124 ? 12.90200  -25.84600 -9.94300  1.000 40.40000  ? 124 ILE A HD12 1 
ATOM   2251 H  HD13 . ILE A 1 124 ? 11.92200  -26.04100 -8.70800  1.000 40.40000  ? 124 ILE A HD13 1 
ATOM   2252 N  N    A ARG A 1 125 ? 9.95300   -27.13600 -14.17300 0.310 23.02000  ? 125 ARG A N    1 
ATOM   2253 N  N    B ARG A 1 125 ? 9.95800   -27.12100 -14.18200 0.690 22.91000  ? 125 ARG A N    1 
ATOM   2254 C  CA   A ARG A 1 125 ? 10.59700  -27.50600 -15.42800 0.310 29.62000  ? 125 ARG A CA   1 
ATOM   2255 C  CA   B ARG A 1 125 ? 10.70500  -27.52800 -15.37200 0.690 29.33000  ? 125 ARG A CA   1 
ATOM   2256 C  C    A ARG A 1 125 ? 10.64900  -26.31300 -16.36800 0.310 28.52000  ? 125 ARG A C    1 
ATOM   2257 C  C    B ARG A 1 125 ? 10.64300  -26.43800 -16.43100 0.690 28.62000  ? 125 ARG A C    1 
ATOM   2258 O  O    A ARG A 1 125 ? 9.66700   -25.58400 -16.52600 0.310 27.76000  ? 125 ARG A O    1 
ATOM   2259 O  O    B ARG A 1 125 ? 9.57000   -25.92800 -16.76200 0.690 32.69000  ? 125 ARG A O    1 
ATOM   2260 C  CB   A ARG A 1 125 ? 9.78300   -28.63100 -16.07800 0.310 30.71000  ? 125 ARG A CB   1 
ATOM   2261 C  CB   B ARG A 1 125 ? 10.10300  -28.82800 -15.92000 0.690 29.87000  ? 125 ARG A CB   1 
ATOM   2262 C  CG   A ARG A 1 125 ? 10.58100  -29.55800 -16.98000 0.310 44.66000  ? 125 ARG A CG   1 
ATOM   2263 C  CG   B ARG A 1 125 ? 10.83500  -29.44800 -17.11600 0.690 41.78000  ? 125 ARG A CG   1 
ATOM   2264 C  CD   A ARG A 1 125 ? 9.73600   -30.18800 -18.09300 0.310 52.54000  ? 125 ARG A CD   1 
ATOM   2265 C  CD   B ARG A 1 125 ? 11.03500  -30.96500 -16.94300 0.690 61.33000  ? 125 ARG A CD   1 
ATOM   2266 N  NE   A ARG A 1 125 ? 8.32600   -30.36200 -17.75700 0.310 57.57000  ? 125 ARG A NE   1 
ATOM   2267 N  NE   B ARG A 1 125 ? 11.92600  -31.53500 -17.95100 0.690 77.64000  ? 125 ARG A NE   1 
ATOM   2268 C  CZ   A ARG A 1 125 ? 7.81700   -31.43700 -17.16700 0.310 57.74000  ? 125 ARG A CZ   1 
ATOM   2269 C  CZ   B ARG A 1 125 ? 11.54900  -31.96700 -19.14900 0.690 61.56000  ? 125 ARG A CZ   1 
ATOM   2270 N  NH1  A ARG A 1 125 ? 8.58600   -32.43600 -16.76500 0.310 45.59000  ? 125 ARG A NH1  1 
ATOM   2271 N  NH1  B ARG A 1 125 ? 10.27800  -31.97100 -19.51600 0.690 69.33000  ? 125 ARG A NH1  1 
ATOM   2272 N  NH2  A ARG A 1 125 ? 6.50200   -31.51100 -16.97800 0.310 45.38000  ? 125 ARG A NH2  1 
ATOM   2273 N  NH2  B ARG A 1 125 ? 12.47100  -32.41300 -19.99800 0.690 64.41000  ? 125 ARG A NH2  1 
ATOM   2274 H  H    A ARG A 1 125 ? 9.31100   -27.66400 -13.95200 0.310 27.64000  ? 125 ARG A H    1 
ATOM   2275 H  H    B ARG A 1 125 ? 9.27300   -27.61300 -14.01500 0.690 27.52000  ? 125 ARG A H    1 
ATOM   2276 H  HA   A ARG A 1 125 ? 11.50400  -27.80900 -15.26200 0.310 35.57000  ? 125 ARG A HA   1 
ATOM   2277 H  HA   B ARG A 1 125 ? 11.63600  -27.68000 -15.14500 0.690 35.22000  ? 125 ARG A HA   1 
ATOM   2278 H  HB2  A ARG A 1 125 ? 9.39300   -29.17300 -15.37500 0.310 36.87000  ? 125 ARG A HB2  1 
ATOM   2279 H  HB2  B ARG A 1 125 ? 10.10500  -29.48700 -15.20800 0.690 35.86000  ? 125 ARG A HB2  1 
ATOM   2280 H  HB3  A ARG A 1 125 ? 9.08200   -28.23200 -16.61600 0.310 36.87000  ? 125 ARG A HB3  1 
ATOM   2281 H  HB3  B ARG A 1 125 ? 9.19300   -28.64600 -16.20200 0.690 35.86000  ? 125 ARG A HB3  1 
ATOM   2282 H  HG2  A ARG A 1 125 ? 11.29600  -29.05300 -17.39800 0.310 53.61000  ? 125 ARG A HG2  1 
ATOM   2283 H  HG2  B ARG A 1 125 ? 10.31400  -29.30100 -17.92100 0.690 50.16000  ? 125 ARG A HG2  1 
ATOM   2284 H  HG3  A ARG A 1 125 ? 10.95200  -30.27700 -16.44400 0.310 53.61000  ? 125 ARG A HG3  1 
ATOM   2285 H  HG3  B ARG A 1 125 ? 11.70800  -29.03600 -17.20700 0.690 50.16000  ? 125 ARG A HG3  1 
ATOM   2286 H  HD2  A ARG A 1 125 ? 9.78200   -29.61900 -18.87700 0.310 63.07000  ? 125 ARG A HD2  1 
ATOM   2287 H  HD2  B ARG A 1 125 ? 11.42100  -31.13600 -16.07000 0.690 73.62000  ? 125 ARG A HD2  1 
ATOM   2288 H  HD3  A ARG A 1 125 ? 10.09800  -31.06400 -18.29800 0.310 63.07000  ? 125 ARG A HD3  1 
ATOM   2289 H  HD3  B ARG A 1 125 ? 10.17500  -31.40800 -17.01700 0.690 73.62000  ? 125 ARG A HD3  1 
ATOM   2290 H  HE   A ARG A 1 125 ? 7.78600   -29.72300 -17.95700 0.310 69.10000  ? 125 ARG A HE   1 
ATOM   2291 H  HE   B ARG A 1 125 ? 12.76100  -31.59600 -17.75300 0.690 93.19000  ? 125 ARG A HE   1 
ATOM   2292 H  HH11 A ARG A 1 125 ? 9.43700   -32.40000 -16.88400 0.310 54.73000  ? 125 ARG A HH11 1 
ATOM   2293 H  HH11 B ARG A 1 125 ? 9.67200   -31.68900 -18.97300 0.690 83.21000  ? 125 ARG A HH11 1 
ATOM   2294 H  HH12 A ARG A 1 125 ? 8.23400   -33.12300 -16.38400 0.310 54.73000  ? 125 ARG A HH12 1 
ATOM   2295 H  HH12 B ARG A 1 125 ? 10.05700  -32.25500 -20.29700 0.690 83.21000  ? 125 ARG A HH12 1 
ATOM   2296 H  HH21 A ARG A 1 125 ? 5.99300   -30.86800 -17.23800 0.310 54.48000  ? 125 ARG A HH21 1 
ATOM   2297 H  HH21 B ARG A 1 125 ? 13.30000  -32.41900 -19.76800 0.690 77.31000  ? 125 ARG A HH21 1 
ATOM   2298 H  HH22 A ARG A 1 125 ? 6.16000   -32.20200 -16.59700 0.310 54.48000  ? 125 ARG A HH22 1 
ATOM   2299 H  HH22 B ARG A 1 125 ? 12.23800  -32.69500 -20.77600 0.690 77.31000  ? 125 ARG A HH22 1 
ATOM   2300 N  N    . GLY A 1 126 ? 11.81700  -26.08400 -16.96200 1.000 29.11000  ? 126 GLY A N    1 
ATOM   2301 C  CA   . GLY A 1 126 ? 11.93400  -25.06900 -17.96900 1.000 30.79000  ? 126 GLY A CA   1 
ATOM   2302 C  C    . GLY A 1 126 ? 12.18000  -23.67700 -17.44000 1.000 38.38000  ? 126 GLY A C    1 
ATOM   2303 O  O    . GLY A 1 126 ? 12.54300  -22.79100 -18.22300 1.000 37.57000  ? 126 GLY A O    1 
ATOM   2304 H  H    . GLY A 1 126 ? 12.57100  -26.43400 -16.73900 1.000 34.95000  ? 126 GLY A H    1 
ATOM   2305 H  HA2  . GLY A 1 126 ? 12.67200  -25.29800 -18.55600 1.000 36.97000  ? 126 GLY A HA2  1 
ATOM   2306 H  HA3  . GLY A 1 126 ? 11.11300  -25.04900 -18.48600 1.000 36.97000  ? 126 GLY A HA3  1 
ATOM   2307 N  N    . CYS A 1 127 ? 12.03100  -23.44900 -16.14000 1.000 25.86000  ? 127 CYS A N    1 
ATOM   2308 C  CA   . CYS A 1 127 ? 12.10300  -22.09700 -15.61900 1.000 27.47000  ? 127 CYS A CA   1 
ATOM   2309 C  C    . CYS A 1 127 ? 13.54000  -21.62600 -15.40900 1.000 29.37000  ? 127 CYS A C    1 
ATOM   2310 O  O    . CYS A 1 127 ? 14.40300  -22.38800 -14.95500 1.000 30.17000  ? 127 CYS A O    1 
ATOM   2311 C  CB   . CYS A 1 127 ? 11.38000  -22.03400 -14.27000 1.000 27.62000  ? 127 CYS A CB   1 
ATOM   2312 S  SG   . CYS A 1 127 ? 9.63100   -22.48000 -14.30400 1.000 25.14000  ? 127 CYS A SG   1 
ATOM   2313 H  H    . CYS A 1 127 ? 11.88900  -24.05600 -15.54800 1.000 31.05000  ? 127 CYS A H    1 
ATOM   2314 H  HA   . CYS A 1 127 ? 11.68800  -21.50300 -16.26400 1.000 32.99000  ? 127 CYS A HA   1 
ATOM   2315 H  HB2  . CYS A 1 127 ? 11.82200  -22.64300 -13.65800 1.000 33.17000  ? 127 CYS A HB2  1 
ATOM   2316 H  HB3  . CYS A 1 127 ? 11.44000  -21.12600 -13.93400 1.000 33.17000  ? 127 CYS A HB3  1 
ATOM   2317 N  N    A ARG A 1 128 ? 13.76600  -20.34400 -15.70200 0.450 33.19000  ? 128 ARG A N    1 
ATOM   2318 N  N    B ARG A 1 128 ? 13.79000  -20.35600 -15.72200 0.550 33.29000  ? 128 ARG A N    1 
ATOM   2319 C  CA   A ARG A 1 128 ? 15.02800  -19.66200 -15.42600 0.450 38.62000  ? 128 ARG A CA   1 
ATOM   2320 C  CA   B ARG A 1 128 ? 15.08500  -19.74700 -15.43200 0.550 38.56000  ? 128 ARG A CA   1 
ATOM   2321 C  C    A ARG A 1 128 ? 15.03900  -19.23000 -13.96400 0.450 36.05000  ? 128 ARG A C    1 
ATOM   2322 C  C    B ARG A 1 128 ? 15.07800  -19.23900 -13.99600 0.550 36.03000  ? 128 ARG A C    1 
ATOM   2323 O  O    A ARG A 1 128 ? 14.35500  -18.27000 -13.59200 0.450 43.28000  ? 128 ARG A O    1 
ATOM   2324 O  O    B ARG A 1 128 ? 14.42200  -18.23900 -13.68100 0.550 43.30000  ? 128 ARG A O    1 
ATOM   2325 C  CB   A ARG A 1 128 ? 15.13900  -18.44200 -16.34100 0.450 41.27000  ? 128 ARG A CB   1 
ATOM   2326 C  CB   B ARG A 1 128 ? 15.40800  -18.62700 -16.41900 0.550 39.89000  ? 128 ARG A CB   1 
ATOM   2327 C  CG   A ARG A 1 128 ? 16.42600  -18.35400 -17.14900 0.450 46.96000  ? 128 ARG A CG   1 
ATOM   2328 C  CG   B ARG A 1 128 ? 16.91100  -18.38700 -16.54300 0.550 43.11000  ? 128 ARG A CG   1 
ATOM   2329 C  CD   A ARG A 1 128 ? 16.48200  -17.10300 -18.05100 0.450 35.90000  ? 128 ARG A CD   1 
ATOM   2330 C  CD   B ARG A 1 128 ? 17.27200  -17.20200 -17.43400 0.550 27.83000  ? 128 ARG A CD   1 
ATOM   2331 N  NE   A ARG A 1 128 ? 15.92300  -17.35100 -19.37600 0.450 38.28000  ? 128 ARG A NE   1 
ATOM   2332 N  NE   B ARG A 1 128 ? 18.71800  -17.00500 -17.46100 0.550 35.29000  ? 128 ARG A NE   1 
ATOM   2333 C  CZ   A ARG A 1 128 ? 14.96600  -16.63300 -19.95100 0.450 42.46000  ? 128 ARG A CZ   1 
ATOM   2334 C  CZ   B ARG A 1 128 ? 19.56200  -17.74200 -18.17200 0.550 48.72000  ? 128 ARG A CZ   1 
ATOM   2335 N  NH1  A ARG A 1 128 ? 14.48700  -15.53500 -19.38800 0.450 39.70000  ? 128 ARG A NH1  1 
ATOM   2336 N  NH1  B ARG A 1 128 ? 19.13400  -18.69700 -18.98300 0.550 39.55000  ? 128 ARG A NH1  1 
ATOM   2337 N  NH2  A ARG A 1 128 ? 14.47700  -17.02500 -21.12400 0.450 48.30000  ? 128 ARG A NH2  1 
ATOM   2338 N  NH2  B ARG A 1 128 ? 20.86900  -17.51500 -18.06600 0.550 45.90000  ? 128 ARG A NH2  1 
ATOM   2339 H  H    A ARG A 1 128 ? 13.18400  -19.83100 -16.07400 0.450 39.85000  ? 128 ARG A H    1 
ATOM   2340 H  H    B ARG A 1 128 ? 13.22800  -19.82800 -16.10200 0.550 39.97000  ? 128 ARG A H    1 
ATOM   2341 H  HA   A ARG A 1 128 ? 15.77600  -20.25900 -15.58100 0.450 46.37000  ? 128 ARG A HA   1 
ATOM   2342 H  HA   B ARG A 1 128 ? 15.77800  -20.42000 -15.52200 0.550 46.29000  ? 128 ARG A HA   1 
ATOM   2343 H  HB2  A ARG A 1 128 ? 14.40200  -18.46200 -16.97000 0.450 49.55000  ? 128 ARG A HB2  1 
ATOM   2344 H  HB2  B ARG A 1 128 ? 15.06500  -18.86700 -17.29500 0.550 47.89000  ? 128 ARG A HB2  1 
ATOM   2345 H  HB3  A ARG A 1 128 ? 15.08600  -17.64300 -15.79300 0.450 49.55000  ? 128 ARG A HB3  1 
ATOM   2346 H  HB3  B ARG A 1 128 ? 14.99300  -17.80500 -16.11400 0.550 47.89000  ? 128 ARG A HB3  1 
ATOM   2347 H  HG2  A ARG A 1 128 ? 17.18000  -18.31800 -16.54000 0.450 56.37000  ? 128 ARG A HG2  1 
ATOM   2348 H  HG2  B ARG A 1 128 ? 17.27300  -18.21400 -15.66000 0.550 51.75000  ? 128 ARG A HG2  1 
ATOM   2349 H  HG3  A ARG A 1 128 ? 16.49600  -19.13600 -17.71800 0.450 56.37000  ? 128 ARG A HG3  1 
ATOM   2350 H  HG3  B ARG A 1 128 ? 17.32400  -19.17800 -16.92200 0.550 51.75000  ? 128 ARG A HG3  1 
ATOM   2351 H  HD2  A ARG A 1 128 ? 15.97200  -16.38900 -17.63700 0.450 43.10000  ? 128 ARG A HD2  1 
ATOM   2352 H  HD2  B ARG A 1 128 ? 16.96600  -17.37000 -18.33800 0.550 33.42000  ? 128 ARG A HD2  1 
ATOM   2353 H  HD3  A ARG A 1 128 ? 17.40700  -16.83100 -18.16000 0.450 43.10000  ? 128 ARG A HD3  1 
ATOM   2354 H  HD3  B ARG A 1 128 ? 16.85700  -16.39700 -17.08700 0.550 33.42000  ? 128 ARG A HD3  1 
ATOM   2355 H  HE   A ARG A 1 128 ? 16.23900  -18.01600 -19.82100 0.450 45.96000  ? 128 ARG A HE   1 
ATOM   2356 H  HE   B ARG A 1 128 ? 19.04500  -16.36900 -16.98500 0.550 42.36000  ? 128 ARG A HE   1 
ATOM   2357 H  HH11 A ARG A 1 128 ? 14.79700  -15.27000 -18.63000 0.450 47.66000  ? 128 ARG A HH11 1 
ATOM   2358 H  HH11 B ARG A 1 128 ? 18.29100  -18.85200 -19.05800 0.550 47.49000  ? 128 ARG A HH11 1 
ATOM   2359 H  HH12 A ARG A 1 128 ? 13.86700  -15.08600 -19.77900 0.450 47.66000  ? 128 ARG A HH12 1 
ATOM   2360 H  HH12 B ARG A 1 128 ? 19.69800  -19.16300 -19.43500 0.550 47.49000  ? 128 ARG A HH12 1 
ATOM   2361 H  HH21 A ARG A 1 128 ? 14.78100  -17.73600 -21.50100 0.450 57.98000  ? 128 ARG A HH21 1 
ATOM   2362 H  HH21 B ARG A 1 128 ? 21.15700  -16.89800 -17.54200 0.550 55.09000  ? 128 ARG A HH21 1 
ATOM   2363 H  HH22 A ARG A 1 128 ? 13.85700  -16.56800 -21.50600 0.450 57.98000  ? 128 ARG A HH22 1 
ATOM   2364 H  HH22 B ARG A 1 128 ? 21.42500  -17.98700 -18.52200 0.550 55.09000  ? 128 ARG A HH22 1 
ATOM   2365 N  N    . LEU A 1 129 ? 15.80500  -19.93100 -13.12800 1.000 33.43000  ? 129 LEU A N    1 
ATOM   2366 C  CA   . LEU A 1 129 ? 15.87000  -19.59500 -11.71100 1.000 35.95000  ? 129 LEU A CA   1 
ATOM   2367 C  C    . LEU A 1 129 ? 17.28400  -19.36400 -11.20100 1.000 53.44000  ? 129 LEU A C    1 
ATOM   2368 O  O    . LEU A 1 129 ? 17.46300  -19.03700 -10.02600 1.000 45.08000  ? 129 LEU A O    1 
ATOM   2369 C  CB   . LEU A 1 129 ? 15.23000  -20.70100 -10.86400 1.000 36.18000  ? 129 LEU A CB   1 
ATOM   2370 C  CG   . LEU A 1 129 ? 13.82400  -21.10400 -11.28800 1.000 35.05000  ? 129 LEU A CG   1 
ATOM   2371 C  CD1  . LEU A 1 129 ? 13.35300  -22.29900 -10.48300 1.000 40.76000  ? 129 LEU A CD1  1 
ATOM   2372 C  CD2  . LEU A 1 129 ? 12.85500  -19.93400 -11.10300 1.000 41.41000  ? 129 LEU A CD2  1 
ATOM   2373 O  OXT  . LEU A 1 129 ? 18.26000  -19.51700 -11.93200 1.000 60.13000  ? 129 LEU A OXT  1 
ATOM   2374 H  H    . LEU A 1 129 ? 16.28000  -20.61600 -13.33900 1.000 40.14000  ? 129 LEU A H    1 
ATOM   2375 H  HA   . LEU A 1 129 ? 15.38100  -18.76400 -11.60300 1.000 43.16000  ? 129 LEU A HA   1 
ATOM   2376 H  HB2  . LEU A 1 129 ? 15.78900  -21.49200 -10.91900 1.000 43.44000  ? 129 LEU A HB2  1 
ATOM   2377 H  HB3  . LEU A 1 129 ? 15.18100  -20.39400 -9.94500  1.000 43.44000  ? 129 LEU A HB3  1 
ATOM   2378 H  HG   . LEU A 1 129 ? 13.83400  -21.34800 -12.22700 1.000 42.08000  ? 129 LEU A HG   1 
ATOM   2379 H  HD11 . LEU A 1 129 ? 12.46600  -22.55300 -10.78300 1.000 48.94000  ? 129 LEU A HD11 1 
ATOM   2380 H  HD12 . LEU A 1 129 ? 13.97100  -23.03500 -10.61900 1.000 48.94000  ? 129 LEU A HD12 1 
ATOM   2381 H  HD13 . LEU A 1 129 ? 13.32800  -22.05700 -9.54400  1.000 48.94000  ? 129 LEU A HD13 1 
ATOM   2382 H  HD21 . LEU A 1 129 ? 11.96700  -20.21400 -11.37400 1.000 49.71000  ? 129 LEU A HD21 1 
ATOM   2383 H  HD22 . LEU A 1 129 ? 12.84900  -19.67500 -10.16800 1.000 49.71000  ? 129 LEU A HD22 1 
ATOM   2384 H  HD23 . LEU A 1 129 ? 13.15000  -19.19000 -11.65100 1.000 49.71000  ? 129 LEU A HD23 1 
HETATM 2385 C  C1   . EDO B 2 .   ? 7.74500   -29.22600 10.16300  1.000 36.64000  ? 201 EDO A C1   1 
HETATM 2386 O  O1   . EDO B 2 .   ? 6.56200   -28.51200 10.55900  1.000 25.69000  ? 201 EDO A O1   1 
HETATM 2387 C  C2   . EDO B 2 .   ? 8.97800   -28.59400 10.81000  1.000 49.84000  ? 201 EDO A C2   1 
HETATM 2388 O  O2   . EDO B 2 .   ? 8.85400   -28.64900 12.23700  1.000 59.38000  ? 201 EDO A O2   1 
HETATM 2389 H  H11  . EDO B 2 .   ? 7.66400   -30.27200 10.46700  1.000 43.98000  ? 201 EDO A H11  1 
HETATM 2390 H  H12  . EDO B 2 .   ? 7.84600   -29.19900 9.07600   1.000 43.98000  ? 201 EDO A H12  1 
HETATM 2391 H  HO1  . EDO B 2 .   ? 6.06100   -28.25600 9.77300   1.000 30.84000  ? 201 EDO A HO1  1 
HETATM 2392 H  H21  . EDO B 2 .   ? 9.87600   -29.12900 10.49600  1.000 59.83000  ? 201 EDO A H21  1 
HETATM 2393 H  H22  . EDO B 2 .   ? 9.07400   -27.55600 10.48700  1.000 59.83000  ? 201 EDO A H22  1 
HETATM 2394 H  HO2  . EDO B 2 .   ? 9.58600   -28.16600 12.64300  1.000 71.27000  ? 201 EDO A HO2  1 
HETATM 2395 C  C1   A EDO C 2 .   ? -3.64400  -22.44200 5.45300   0.490 28.73000  ? 202 EDO A C1   1 
HETATM 2396 C  C1   B EDO C 2 .   ? -3.04800  -22.34900 6.39900   0.510 30.17000  ? 202 EDO A C1   1 
HETATM 2397 O  O1   A EDO C 2 .   ? -5.04300  -22.40700 5.13600   0.490 33.21000  ? 202 EDO A O1   1 
HETATM 2398 O  O1   B EDO C 2 .   ? -4.41800  -22.09500 6.11700   0.510 23.38000  ? 202 EDO A O1   1 
HETATM 2399 C  C2   A EDO C 2 .   ? -3.20700  -23.89100 5.49800   0.490 25.24000  ? 202 EDO A C2   1 
HETATM 2400 C  C2   B EDO C 2 .   ? -2.75000  -23.81500 6.11900   0.510 33.56000  ? 202 EDO A C2   1 
HETATM 2401 O  O2   A EDO C 2 .   ? -4.33300  -24.72000 5.21100   0.490 34.22000  ? 202 EDO A O2   1 
HETATM 2402 O  O2   B EDO C 2 .   ? -3.70900  -24.62400 6.80100   0.510 27.02000  ? 202 EDO A O2   1 
HETATM 2403 H  H11  A EDO C 2 .   ? -3.07200  -21.89900 4.69800   0.490 34.49000  ? 202 EDO A H11  1 
HETATM 2404 H  H11  B EDO C 2 .   ? -2.41500  -21.71400 5.77500   0.510 36.23000  ? 202 EDO A H11  1 
HETATM 2405 H  H12  A EDO C 2 .   ? -3.46300  -21.96400 6.41800   0.490 34.49000  ? 202 EDO A H12  1 
HETATM 2406 H  H12  B EDO C 2 .   ? -2.83200  -22.11600 7.44300   0.510 36.23000  ? 202 EDO A H12  1 
HETATM 2407 H  HO1  A EDO C 2 .   ? -5.32700  -21.48900 5.03400   0.490 39.87000  ? 202 EDO A HO1  1 
HETATM 2408 H  HO1  B EDO C 2 .   ? -4.82100  -21.63300 6.86600   0.510 28.07000  ? 202 EDO A HO1  1 
HETATM 2409 H  H21  A EDO C 2 .   ? -2.41700  -24.06600 4.76500   0.490 30.31000  ? 202 EDO A H21  1 
HETATM 2410 H  H21  B EDO C 2 .   ? -2.79700  -24.00700 5.04500   0.510 40.29000  ? 202 EDO A H21  1 
HETATM 2411 H  H22  A EDO C 2 .   ? -2.80700  -24.13100 6.48600   0.490 30.31000  ? 202 EDO A H22  1 
HETATM 2412 H  H22  B EDO C 2 .   ? -1.74300  -24.06300 6.46100   0.510 40.29000  ? 202 EDO A H22  1 
HETATM 2413 H  HO2  A EDO C 2 .   ? -4.04900  -25.64300 5.15500   0.490 41.09000  ? 202 EDO A HO2  1 
HETATM 2414 H  HO2  B EDO C 2 .   ? -3.41000  -25.54300 6.80700   0.510 32.45000  ? 202 EDO A HO2  1 
HETATM 2415 C  C1   . EDO D 2 .   ? -15.63000 -15.52500 0.53200   0.280 19.56000  ? 203 EDO A C1   1 
HETATM 2416 O  O1   . EDO D 2 .   ? -14.33600 -15.07900 0.92700   0.280 23.93000  ? 203 EDO A O1   1 
HETATM 2417 C  C2   . EDO D 2 .   ? -15.90000 -14.95000 -0.84500  0.280 21.70000  ? 203 EDO A C2   1 
HETATM 2418 O  O2   . EDO D 2 .   ? -14.96700 -15.52600 -1.77500  0.280 23.68000  ? 203 EDO A O2   1 
HETATM 2419 H  H11  . EDO D 2 .   ? -15.66600 -16.61600 0.50400   0.280 23.49000  ? 203 EDO A H11  1 
HETATM 2420 H  H12  . EDO D 2 .   ? -16.38500 -15.18200 1.24300   0.280 23.49000  ? 203 EDO A H12  1 
HETATM 2421 H  HO1  . EDO D 2 .   ? -14.13200 -15.42200 1.80700   0.280 28.73000  ? 203 EDO A HO1  1 
HETATM 2422 H  H21  . EDO D 2 .   ? -16.92300 -15.17600 -1.15200  0.280 26.07000  ? 203 EDO A H21  1 
HETATM 2423 H  H22  . EDO D 2 .   ? -15.78800 -13.86400 -0.82700  0.280 26.07000  ? 203 EDO A H22  1 
HETATM 2424 H  HO2  . EDO D 2 .   ? -15.09800 -15.13300 -2.64900  0.280 28.43000  ? 203 EDO A HO2  1 
HETATM 2425 C  C1   . EDO E 2 .   ? 15.59800  -16.28400 -8.75800  0.340 39.94000  ? 204 EDO A C1   1 
HETATM 2426 O  O1   . EDO E 2 .   ? 15.85400  -15.45800 -7.61700  0.340 43.15000  ? 204 EDO A O1   1 
HETATM 2427 C  C2   . EDO E 2 .   ? 15.97600  -15.54100 -10.03700 0.340 38.32000  ? 204 EDO A C2   1 
HETATM 2428 O  O2   . EDO E 2 .   ? 15.14300  -14.38700 -10.20300 0.340 39.19000  ? 204 EDO A O2   1 
HETATM 2429 H  H11  . EDO E 2 .   ? 16.17800  -17.20700 -8.68300  0.340 47.95000  ? 204 EDO A H11  1 
HETATM 2430 H  H12  . EDO E 2 .   ? 14.54000  -16.55400 -8.78800  0.340 47.95000  ? 204 EDO A H12  1 
HETATM 2431 H  HO1  . EDO E 2 .   ? 15.68300  -15.96100 -6.81000  0.340 51.79000  ? 204 EDO A HO1  1 
HETATM 2432 H  H21  . EDO E 2 .   ? 17.02300  -15.23500 -9.98800  0.340 46.01000  ? 204 EDO A H21  1 
HETATM 2433 H  H22  . EDO E 2 .   ? 15.86000  -16.20500 -10.89600 0.340 46.01000  ? 204 EDO A H22  1 
HETATM 2434 H  HO2  . EDO E 2 .   ? 15.39000  -13.92500 -11.01600 0.340 47.05000  ? 204 EDO A HO2  1 
HETATM 2435 C  C1   . EDO F 2 .   ? 6.70300   -35.65500 -3.53700  1.000 55.19000  ? 205 EDO A C1   1 
HETATM 2436 O  O1   . EDO F 2 .   ? 6.41300   -36.41700 -2.35500  1.000 60.86000  ? 205 EDO A O1   1 
HETATM 2437 C  C2   . EDO F 2 .   ? 7.35000   -34.33700 -3.12400  1.000 68.50000  ? 205 EDO A C2   1 
HETATM 2438 O  O2   . EDO F 2 .   ? 6.64400   -33.78800 -2.00100  1.000 38.23000  ? 205 EDO A O2   1 
HETATM 2439 H  H11  . EDO F 2 .   ? 7.37700   -36.21600 -4.18800  1.000 66.25000  ? 205 EDO A H11  1 
HETATM 2440 H  H12  . EDO F 2 .   ? 5.78300   -35.46200 -4.09300  1.000 66.25000  ? 205 EDO A H12  1 
HETATM 2441 H  HO1  . EDO F 2 .   ? 6.22300   -37.33300 -2.60100  1.000 73.05000  ? 205 EDO A HO1  1 
HETATM 2442 H  H21  . EDO F 2 .   ? 8.39600   -34.50500 -2.85800  1.000 82.22000  ? 205 EDO A H21  1 
HETATM 2443 H  H22  . EDO F 2 .   ? 7.32500   -33.63400 -3.95900  1.000 82.22000  ? 205 EDO A H22  1 
HETATM 2444 H  HO2  . EDO F 2 .   ? 7.13100   -33.02900 -1.65400  1.000 45.89000  ? 205 EDO A HO2  1 
HETATM 2445 C  C1   . EDO G 2 .   ? 2.40400   -6.64400  2.09700   1.000 76.22000  ? 206 EDO A C1   1 
HETATM 2446 O  O1   . EDO G 2 .   ? 1.04900   -6.98700  1.76600   1.000 51.62000  ? 206 EDO A O1   1 
HETATM 2447 C  C2   . EDO G 2 .   ? 3.38900   -7.33900  1.15900   1.000 69.60000  ? 206 EDO A C2   1 
HETATM 2448 O  O2   . EDO G 2 .   ? 3.05700   -8.72600  1.02700   1.000 32.31000  ? 206 EDO A O2   1 
HETATM 2449 H  H11  . EDO G 2 .   ? 2.53300   -5.56200  2.02500   1.000 91.49000  ? 206 EDO A H11  1 
HETATM 2450 H  H12  . EDO G 2 .   ? 2.61300   -6.93900  3.12700   1.000 91.49000  ? 206 EDO A H12  1 
HETATM 2451 H  HO1  . EDO G 2 .   ? 0.44200   -6.44100  2.28500   1.000 61.97000  ? 206 EDO A HO1  1 
HETATM 2452 H  H21  . EDO G 2 .   ? 3.36200   -6.86100  0.17800   1.000 83.54000  ? 206 EDO A H21  1 
HETATM 2453 H  H22  . EDO G 2 .   ? 4.40300   -7.24000  1.55300   1.000 83.54000  ? 206 EDO A H22  1 
HETATM 2454 H  HO2  . EDO G 2 .   ? 3.70800   -9.16100  0.46000   1.000 38.79000  ? 206 EDO A HO2  1 
HETATM 2455 CL CL   . CL  H 3 .   ? 8.30400   -31.89900 7.37800   1.000 24.14000  ? 207 CL  A CL   1 
HETATM 2456 CL CL   . CL  I 3 .   ? 11.21700  -31.88900 -1.71100  1.000 34.47000  ? 208 CL  A CL   1 
HETATM 2457 CL CL   . CL  J 3 .   ? 6.54900   -10.49200 -4.83100  1.000 60.55000  ? 209 CL  A CL   1 
HETATM 2458 CL CL   . CL  K 3 .   ? 0.22500   -23.78600 -15.02200 1.000 63.79000  ? 210 CL  A CL   1 
HETATM 2459 NA NA   . NA  L 4 .   ? -8.15900  -14.75000 12.85500  1.000 22.52000  ? 211 NA  A NA   1 
HETATM 2460 NA NA   . NA  M 4 .   ? 11.18500  -29.13500 -6.98100  1.000 28.74000  ? 212 NA  A NA   1 
HETATM 2461 O  O    . HOH N 5 .   ? -5.86400  -40.31100 4.51900   1.000 80.28000  ? 301 HOH A O    1 
HETATM 2462 O  O    . HOH N 5 .   ? -4.51300  -23.98600 9.00300   1.000 38.67000  ? 302 HOH A O    1 
HETATM 2463 O  O    . HOH N 5 .   ? 16.05900  -29.61100 -3.31700  1.000 63.41000  ? 303 HOH A O    1 
HETATM 2464 O  O    . HOH N 5 .   ? 15.54300  -22.55800 1.97000   1.000 51.74000  ? 304 HOH A O    1 
HETATM 2465 O  O    . HOH N 5 .   ? 3.96300   -13.07100 8.95700   1.000 47.79000  ? 305 HOH A O    1 
HETATM 2466 O  O    A HOH N 5 .   ? -7.63000  -24.53900 0.84200   0.550 32.53000  ? 306 HOH A O    1 
HETATM 2467 O  O    B HOH N 5 .   ? -6.47600  -24.33700 2.46800   0.450 41.43000  ? 306 HOH A O    1 
HETATM 2468 O  O    . HOH N 5 .   ? -1.41000  -13.93000 -2.19000  1.000 29.62000  ? 307 HOH A O    1 
HETATM 2469 O  O    . HOH N 5 .   ? -1.77800  -33.99900 -9.02400  1.000 32.31000  ? 308 HOH A O    1 
HETATM 2470 O  O    . HOH N 5 .   ? 10.45600  -32.95800 -14.47800 1.000 63.48000  ? 309 HOH A O    1 
HETATM 2471 O  O    . HOH N 5 .   ? 1.31600   -11.94400 -14.20600 1.000 50.88000  ? 310 HOH A O    1 
HETATM 2472 O  O    . HOH N 5 .   ? -5.98600  -26.74700 1.56200   1.000 34.87000  ? 311 HOH A O    1 
HETATM 2473 O  O    . HOH N 5 .   ? -11.69100 -13.52900 -4.11700  1.000 21.21000  ? 312 HOH A O    1 
HETATM 2474 O  O    . HOH N 5 .   ? 0.15600   -12.20200 -2.17200  1.000 33.13000  ? 313 HOH A O    1 
HETATM 2475 O  O    . HOH N 5 .   ? 16.605    -25.554   4.096     1.000 60.08000  ? 314 HOH A O    1 
HETATM 2476 O  O    . HOH N 5 .   ? -0.85300  -18.39700 -14.83800 1.000 34.77000  ? 315 HOH A O    1 
HETATM 2477 O  O    . HOH N 5 .   ? 20.77300  -19.62100 -20.87900 1.000 62.67000  ? 316 HOH A O    1 
HETATM 2478 O  O    . HOH N 5 .   ? -5.93500  -26.45400 3.88300   1.000 38.57000  ? 317 HOH A O    1 
HETATM 2479 O  O    . HOH N 5 .   ? -12.43600 -25.46400 12.29600  1.000 38.81000  ? 318 HOH A O    1 
HETATM 2480 O  O    . HOH N 5 .   ? 2.65300   -32.72600 -9.49900  1.000 33.78000  ? 319 HOH A O    1 
HETATM 2481 O  O    A HOH N 5 .   ? -12.82500 -13.61000 18.66000  0.680 34.90000  ? 320 HOH A O    1 
HETATM 2482 O  O    B HOH N 5 .   ? -13.12900 -11.55700 17.74400  0.320 48.58000  ? 320 HOH A O    1 
HETATM 2483 O  O    . HOH N 5 .   ? 7.02400   -11.12000 -10.80500 1.000 56.40000  ? 321 HOH A O    1 
HETATM 2484 O  O    . HOH N 5 .   ? -14.07600 -15.21500 7.76200   1.000 20.50000  ? 322 HOH A O    1 
HETATM 2485 O  O    . HOH N 5 .   ? 6.384     -35.371   0.229     1.000 26.34000  ? 323 HOH A O    1 
HETATM 2486 O  O    . HOH N 5 .   ? -7.70900  -26.49600 -3.39400  1.000 31.85000  ? 324 HOH A O    1 
HETATM 2487 O  O    . HOH N 5 .   ? -1.37400  -26.90900 10.88500  1.000 63.54000  ? 325 HOH A O    1 
HETATM 2488 O  O    . HOH N 5 .   ? -9.53900  -24.95800 3.30100   1.000 58.72000  ? 326 HOH A O    1 
HETATM 2489 O  O    . HOH N 5 .   ? -5.73800  -11.02000 -9.54100  1.000 21.17000  ? 327 HOH A O    1 
HETATM 2490 O  O    . HOH N 5 .   ? -3.93500  -7.74800  -5.54500  1.000 45.99000  ? 328 HOH A O    1 
HETATM 2491 O  O    . HOH N 5 .   ? -1.19300  -36.52100 -3.59100  1.000 28.23000  ? 329 HOH A O    1 
HETATM 2492 O  O    . HOH N 5 .   ? -1.21800  -12.88000 17.78200  1.000 60.76000  ? 330 HOH A O    1 
HETATM 2493 O  O    . HOH N 5 .   ? -9.33600  -22.82000 -0.13000  1.000 31.42000  ? 331 HOH A O    1 
HETATM 2494 O  O    . HOH N 5 .   ? -3.40200  -7.39000  -8.25200  1.000 36.54000  ? 332 HOH A O    1 
HETATM 2495 O  O    . HOH N 5 .   ? 14.51000  -32.26900 1.34400   1.000 46.56000  ? 333 HOH A O    1 
HETATM 2496 O  O    . HOH N 5 .   ? -1.73100  -24.60300 15.19600  1.000 63.63000  ? 334 HOH A O    1 
HETATM 2497 O  O    . HOH N 5 .   ? -1.74500  -16.65000 0.76200   1.000 19.28000  ? 335 HOH A O    1 
HETATM 2498 O  O    B HOH N 5 .   ? 2.25100   -27.49400 9.57500   0.460 22.12000  ? 336 HOH A O    1 
HETATM 2499 O  O    . HOH N 5 .   ? 0.49100   -34.06400 9.68400   1.000 64.75000  ? 337 HOH A O    1 
HETATM 2500 O  O    . HOH N 5 .   ? -8.99600  -23.56300 -2.89900  1.000 39.47000  ? 338 HOH A O    1 
HETATM 2501 O  O    . HOH N 5 .   ? 12.05700  -12.40900 -8.67100  0.620 43.59000  ? 339 HOH A O    1 
HETATM 2502 O  O    . HOH N 5 .   ? 10.63400  -31.96500 4.99000   1.000 27.50000  ? 340 HOH A O    1 
HETATM 2503 O  O    . HOH N 5 .   ? 16.70100  -31.14100 2.05900   1.000 53.32000  ? 341 HOH A O    1 
HETATM 2504 O  O    . HOH N 5 .   ? 13.63400  -17.30900 5.94700   1.000 57.18000  ? 342 HOH A O    1 
HETATM 2505 O  O    . HOH N 5 .   ? -9.99200  -13.20000 11.95000  1.000 25.50000  ? 343 HOH A O    1 
HETATM 2506 O  O    A HOH N 5 .   ? -7.08400  -24.27700 6.15000   0.590 39.31000  ? 344 HOH A O    1 
HETATM 2507 O  O    B HOH N 5 .   ? -8.33800  -23.99500 4.91300   0.410 36.55000  ? 344 HOH A O    1 
HETATM 2508 O  O    . HOH N 5 .   ? -3.26000  -19.99100 -13.58700 1.000 41.51000  ? 345 HOH A O    1 
HETATM 2509 O  O    . HOH N 5 .   ? -8.43700  -17.96000 -8.32900  1.000 30.11000  ? 346 HOH A O    1 
HETATM 2510 O  O    . HOH N 5 .   ? -17.41500 -8.21900  11.32200  1.000 42.03000  ? 347 HOH A O    1 
HETATM 2511 O  O    A HOH N 5 .   ? 14.90500  -20.09700 -1.85300  0.460 26.14000  ? 348 HOH A O    1 
HETATM 2512 O  O    B HOH N 5 .   ? 14.23300  -26.20300 -4.49900  0.540 23.73000  ? 348 HOH A O    1 
HETATM 2513 O  O    . HOH N 5 .   ? 3.97000   -37.71900 -10.84300 1.000 40.54000  ? 349 HOH A O    1 
HETATM 2514 O  O    A HOH N 5 .   ? 18.10200  -20.30000 -2.55900  1.000 50.07000  ? 350 HOH A O    1 
HETATM 2515 O  O    . HOH N 5 .   ? 13.838    -25.334   14.151    1.000 43.76000  ? 351 HOH A O    1 
HETATM 2516 O  O    . HOH N 5 .   ? -19.362   -16.634   0.924     1.000 30.13000  ? 352 HOH A O    1 
HETATM 2517 O  O    . HOH N 5 .   ? 15.11500  -24.67500 6.25500   1.000 38.63000  ? 353 HOH A O    1 
HETATM 2518 O  O    A HOH N 5 .   ? 11.63100  -18.57000 -16.85200 0.610 33.34000  ? 354 HOH A O    1 
HETATM 2519 O  O    B HOH N 5 .   ? 11.87400  -17.74300 -14.30800 0.390 34.83000  ? 354 HOH A O    1 
HETATM 2520 O  O    . HOH N 5 .   ? -0.34100  -38.80600 3.26800   1.000 36.40000  ? 355 HOH A O    1 
HETATM 2521 O  O    . HOH N 5 .   ? -5.27900  -9.34000  15.85700  1.000 46.09000  ? 356 HOH A O    1 
HETATM 2522 O  O    . HOH N 5 .   ? 11.00100  -30.17700 8.17800   1.000 57.72000  ? 357 HOH A O    1 
HETATM 2523 O  O    . HOH N 5 .   ? 13.700    -31.145   -15.524   1.000 58.43000  ? 358 HOH A O    1 
HETATM 2524 O  O    . HOH N 5 .   ? 5.67600   -10.05400 6.23500   1.000 47.35000  ? 359 HOH A O    1 
HETATM 2525 O  O    . HOH N 5 .   ? -2.74000  -10.28500 -13.39300 1.000 38.49000  ? 360 HOH A O    1 
HETATM 2526 O  O    . HOH N 5 .   ? -9.37100  -21.20200 17.73400  1.000 67.07000  ? 361 HOH A O    1 
HETATM 2527 O  O    . HOH N 5 .   ? 5.22100   -11.52200 13.05300  1.000 69.40000  ? 362 HOH A O    1 
HETATM 2528 O  O    . HOH N 5 .   ? -10.14800 -24.27200 10.08800  1.000 61.85000  ? 363 HOH A O    1 
HETATM 2529 O  O    . HOH N 5 .   ? 1.00600   -11.53000 0.37200   1.000 26.82000  ? 364 HOH A O    1 
HETATM 2530 O  O    . HOH N 5 .   ? -19.163   -10.350   6.251     1.000 28.62000  ? 365 HOH A O    1 
HETATM 2531 O  O    . HOH N 5 .   ? -1.62200  -5.27300  -4.58500  1.000 43.85000  ? 366 HOH A O    1 
HETATM 2532 O  O    . HOH N 5 .   ? -3.50800  -14.44100 18.22200  1.000 30.70000  ? 367 HOH A O    1 
HETATM 2533 O  O    . HOH N 5 .   ? 11.50000  -11.84900 2.25000   1.000 53.78000  ? 368 HOH A O    1 
HETATM 2534 O  O    . HOH N 5 .   ? 5.31500   -22.38300 14.48300  1.000 61.69000  ? 369 HOH A O    1 
HETATM 2535 O  O    . HOH N 5 .   ? -10.502   -6.036    12.443    1.000 31.50000  ? 370 HOH A O    1 
HETATM 2536 O  O    . HOH N 5 .   ? -17.481   -22.312   14.068    1.000 45.23000  ? 371 HOH A O    1 
HETATM 2537 O  O    . HOH N 5 .   ? 2.81500   -22.59100 -16.99600 1.000 78.61000  ? 372 HOH A O    1 
HETATM 2538 O  O    . HOH N 5 .   ? -5.63100  -24.72900 -15.37100 1.000 63.60000  ? 373 HOH A O    1 
HETATM 2539 O  O    . HOH N 5 .   ? -7.99900  -12.82400 14.26900  1.000 30.52000  ? 374 HOH A O    1 
HETATM 2540 O  O    . HOH N 5 .   ? 5.95900   -17.54700 -16.08400 1.000 28.10000  ? 375 HOH A O    1 
HETATM 2541 O  O    . HOH N 5 .   ? 9.55400   -22.81100 -19.33800 1.000 67.04000  ? 376 HOH A O    1 
HETATM 2542 O  O    . HOH N 5 .   ? 15.082    -27.892   10.288    1.000 65.01000  ? 377 HOH A O    1 
HETATM 2543 O  O    . HOH N 5 .   ? 15.17000  -31.79500 -2.13400  1.000 57.85000  ? 378 HOH A O    1 
HETATM 2544 O  O    . HOH N 5 .   ? -11.92900 -12.13600 14.05500  1.000 22.37000  ? 379 HOH A O    1 
HETATM 2545 O  O    . HOH N 5 .   ? 9.78100   -34.64800 -7.21700  1.000 56.03000  ? 380 HOH A O    1 
HETATM 2546 O  O    . HOH N 5 .   ? -5.35500  -6.65100  11.80200  1.000 49.02000  ? 381 HOH A O    1 
HETATM 2547 O  O    . HOH N 5 .   ? -6.369    -25.422   -10.195   1.000 51.03000  ? 382 HOH A O    1 
HETATM 2548 O  O    . HOH N 5 .   ? 1.52500   -19.91500 -16.70900 1.000 54.25000  ? 383 HOH A O    1 
HETATM 2549 O  O    . HOH N 5 .   ? -5.25300  -5.25300  0.00000   0.50  57.87000  ? 384 HOH A O    1 
HETATM 2550 O  O    A HOH N 5 .   ? -2.52500  -7.34100  12.97100  0.530 40.16000  ? 385 HOH A O    1 
HETATM 2551 O  O    B HOH N 5 .   ? -3.66700  -7.66000  12.49400  0.470 33.94000  ? 385 HOH A O    1 
HETATM 2552 O  O    . HOH N 5 .   ? 0.04400   -14.70900 20.56300  1.000 60.69000  ? 386 HOH A O    1 
HETATM 2553 O  O    . HOH N 5 .   ? 12.67600  -17.67400 8.62400   1.000 62.99000  ? 387 HOH A O    1 
HETATM 2554 O  O    . HOH N 5 .   ? 8.81700   -16.46300 9.37400   1.000 60.16000  ? 388 HOH A O    1 
HETATM 2555 O  O    . HOH N 5 .   ? -4.44900  -7.49500  -10.64700 1.000 56.05000  ? 389 HOH A O    1 
HETATM 2556 O  O    . HOH N 5 .   ? -6.37300  -21.49200 -16.13900 1.000 52.65000  ? 390 HOH A O    1 
HETATM 2557 O  O    . HOH N 5 .   ? 4.49500   -22.58800 -19.11200 1.000 63.69000  ? 391 HOH A O    1 
HETATM 2558 O  O    . HOH N 5 .   ? 11.73500  -9.51100  0.97100   1.000 68.90000  ? 392 HOH A O    1 
HETATM 2559 O  O    . HOH N 5 .   ? -13.64900 -24.75700 14.34700  1.000 59.57000  ? 393 HOH A O    1 
HETATM 2560 O  O    . HOH N 5 .   ? 4.47200   -28.20800 -16.63100 1.000 67.22000  ? 394 HOH A O    1 
HETATM 2561 O  O    . HOH N 5 .   ? 8.57200   -38.39400 -5.93800  1.000 72.81000  ? 395 HOH A O    1 
HETATM 2562 O  O    . HOH N 5 .   ? 12.73700  -36.08200 -11.45400 1.000 70.13000  ? 396 HOH A O    1 
HETATM 2563 O  O    . HOH N 5 .   ? 19.845    -29.687   -1.155    1.000 59.02000  ? 397 HOH A O    1 
HETATM 2564 O  O    . HOH N 5 .   ? -8.69700  -26.61900 -0.08800  1.000 68.14000  ? 398 HOH A O    1 
HETATM 2565 O  O    . HOH N 5 .   ? -14.191   -7.143    15.558    1.000 60.72000  ? 399 HOH A O    1 
HETATM 2566 O  O    . HOH N 5 .   ? 7.578     -30.166   15.551    1.000 66.99000  ? 400 HOH A O    1 
HETATM 2567 O  O    . HOH N 5 .   ? -14.50700 -11.53700 15.73100  1.000 50.30000  ? 401 HOH A O    1 
HETATM 2568 O  O    . HOH N 5 .   ? 7.13100   -39.78700 -8.37200  1.000 63.27000  ? 402 HOH A O    1 
HETATM 2569 O  O    . HOH N 5 .   ? 0.39500   -39.70000 -0.48100  1.000 56.23000  ? 403 HOH A O    1 
HETATM 2570 O  O    . HOH N 5 .   ? 3.07200   -29.21500 -15.17100 1.000 48.54000  ? 404 HOH A O    1 
HETATM 2571 O  O    . HOH N 5 .   ? -11.48400 -6.81800  14.91200  1.000 66.76000  ? 405 HOH A O    1 
HETATM 2572 O  O    . HOH N 5 .   ? -2.77400  -33.90000 8.82000   1.000 84.58000  ? 406 HOH A O    1 
# 
