data_9FCB
# 
_entry.id   9FCB 
# 
_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   9FCB         pdb_00009fcb 10.2210/pdb9fcb/pdb 
WWPDB D_1292137237 ?            ?                   
# 
_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                        9FCB 
_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    7  ?        ? ? ? 
3 non-polymer syn 'CHLORIDE ION' 35.453    4  ?        ? ? ? 
4 non-polymer syn 'SODIUM ION'   22.990    2  ?        ? ? ? 
5 water       nat water          18.015    96 ?        ? ? ? 
# 
_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 2 EDO 1  207 217 EDO EDO A . 
I 3 CL  1  208 2   CL  CL  A . 
J 3 CL  1  209 3   CL  CL  A . 
K 3 CL  1  210 4   CL  CL  A . 
L 3 CL  1  211 5   CL  CL  A . 
M 4 NA  1  212 1   NA  NA  A . 
N 4 NA  1  213 2   NA  NA  A . 
O 5 HOH 1  301 43  HOH HOH A . 
O 5 HOH 2  302 81  HOH HOH A . 
O 5 HOH 3  303 35  HOH HOH A . 
O 5 HOH 4  304 5   HOH HOH A . 
O 5 HOH 5  305 57  HOH HOH A . 
O 5 HOH 6  306 109 HOH HOH A . 
O 5 HOH 7  307 106 HOH HOH A . 
O 5 HOH 8  308 27  HOH HOH A . 
O 5 HOH 9  309 41  HOH HOH A . 
O 5 HOH 10 310 1   HOH HOH A . 
O 5 HOH 11 311 28  HOH HOH A . 
O 5 HOH 12 312 4   HOH HOH A . 
O 5 HOH 13 313 25  HOH HOH A . 
O 5 HOH 14 314 124 HOH HOH A . 
O 5 HOH 15 315 37  HOH HOH A . 
O 5 HOH 16 316 97  HOH HOH A . 
O 5 HOH 17 317 33  HOH HOH A . 
O 5 HOH 18 318 100 HOH HOH A . 
O 5 HOH 19 319 15  HOH HOH A . 
O 5 HOH 20 320 11  HOH HOH A . 
O 5 HOH 21 321 3   HOH HOH A . 
O 5 HOH 22 322 16  HOH HOH A . 
O 5 HOH 23 323 9   HOH HOH A . 
O 5 HOH 24 324 30  HOH HOH A . 
O 5 HOH 25 325 6   HOH HOH A . 
O 5 HOH 26 326 67  HOH HOH A . 
O 5 HOH 27 327 20  HOH HOH A . 
O 5 HOH 28 328 47  HOH HOH A . 
O 5 HOH 29 329 117 HOH HOH A . 
O 5 HOH 30 330 7   HOH HOH A . 
O 5 HOH 31 331 2   HOH HOH A . 
O 5 HOH 32 332 98  HOH HOH A . 
O 5 HOH 33 333 115 HOH HOH A . 
O 5 HOH 34 334 105 HOH HOH A . 
O 5 HOH 35 335 127 HOH HOH A . 
O 5 HOH 36 336 49  HOH HOH A . 
O 5 HOH 37 337 53  HOH HOH A . 
O 5 HOH 38 338 14  HOH HOH A . 
O 5 HOH 39 339 93  HOH HOH A . 
O 5 HOH 40 340 122 HOH HOH A . 
O 5 HOH 41 341 12  HOH HOH A . 
O 5 HOH 42 342 17  HOH HOH A . 
O 5 HOH 43 343 36  HOH HOH A . 
O 5 HOH 44 344 50  HOH HOH A . 
O 5 HOH 45 345 45  HOH HOH A . 
O 5 HOH 46 346 108 HOH HOH A . 
O 5 HOH 47 347 24  HOH HOH A . 
O 5 HOH 48 348 79  HOH HOH A . 
O 5 HOH 49 349 10  HOH HOH A . 
O 5 HOH 50 350 34  HOH HOH A . 
O 5 HOH 51 351 46  HOH HOH A . 
O 5 HOH 52 352 13  HOH HOH A . 
O 5 HOH 53 353 39  HOH HOH A . 
O 5 HOH 54 354 8   HOH HOH A . 
O 5 HOH 55 355 118 HOH HOH A . 
O 5 HOH 56 356 77  HOH HOH A . 
O 5 HOH 57 357 69  HOH HOH A . 
O 5 HOH 58 358 23  HOH HOH A . 
O 5 HOH 59 359 94  HOH HOH A . 
O 5 HOH 60 360 44  HOH HOH A . 
O 5 HOH 61 361 22  HOH HOH A . 
O 5 HOH 62 362 55  HOH HOH A . 
O 5 HOH 63 363 66  HOH HOH A . 
O 5 HOH 64 364 111 HOH HOH A . 
O 5 HOH 65 365 18  HOH HOH A . 
O 5 HOH 66 366 112 HOH HOH A . 
O 5 HOH 67 367 29  HOH HOH A . 
O 5 HOH 68 368 86  HOH HOH A . 
O 5 HOH 69 369 52  HOH HOH A . 
O 5 HOH 70 370 59  HOH HOH A . 
O 5 HOH 71 371 116 HOH HOH A . 
O 5 HOH 72 372 82  HOH HOH A . 
O 5 HOH 73 373 61  HOH HOH A . 
O 5 HOH 74 374 74  HOH HOH A . 
O 5 HOH 75 375 58  HOH HOH A . 
O 5 HOH 76 376 87  HOH HOH A . 
O 5 HOH 77 377 60  HOH HOH A . 
O 5 HOH 78 378 63  HOH HOH A . 
O 5 HOH 79 379 56  HOH HOH A . 
O 5 HOH 80 380 75  HOH HOH A . 
O 5 HOH 81 381 78  HOH HOH A . 
O 5 HOH 82 382 89  HOH HOH A . 
O 5 HOH 83 383 120 HOH HOH A . 
O 5 HOH 84 384 26  HOH HOH A . 
O 5 HOH 85 385 95  HOH HOH A . 
O 5 HOH 86 386 68  HOH HOH A . 
O 5 HOH 87 387 96  HOH HOH A . 
O 5 HOH 88 388 125 HOH HOH A . 
O 5 HOH 89 389 84  HOH HOH A . 
O 5 HOH 90 390 71  HOH HOH A . 
O 5 HOH 91 391 101 HOH HOH A . 
O 5 HOH 92 392 91  HOH HOH A . 
O 5 HOH 93 393 110 HOH HOH A . 
O 5 HOH 94 394 62  HOH HOH A . 
O 5 HOH 95 395 72  HOH HOH A . 
O 5 HOH 96 396 73  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FCB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.466 
_cell.length_a_esd                 ? 
_cell.length_b                     78.466 
_cell.length_b_esd                 ? 
_cell.length_c                     37.154 
_cell.length_c_esd                 ? 
_cell.volume                       228753.951 
_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                         9FCB 
_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                   9FCB 
_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             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.35 
_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                        p09 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.7750 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          18.57 
_reflns.entry_id                                       9FCB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.4 
_reflns.d_resolution_low                               21.39 
_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                                     23400 
_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                           99.89 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.28 
_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                           1.07 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2287 
_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                                  0.508 
_reflns_shell.pdbx_CC_star                                  0.821 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.88 
_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                                 9FCB 
_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                             21.39 
_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                     23394 
_refine.ls_number_reflns_R_free                  1941 
_refine.ls_number_reflns_R_work                  21453 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 8.30 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1635 
_refine.ls_R_factor_R_free                       0.1895 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1612 
_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                 19.3207 
_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                            0.1559 
_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                        21.39 
_refine_hist.number_atoms_solvent             96 
_refine_hist.number_atoms_total               1131 
_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         34 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0085  ? 1267 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.5083  ? 1720 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0796  ? 168  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0173  ? 237  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.1472 ? 479  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.40 1.44  . . 137 1489 99.21  . . . . 0.3130 . . . . . . . . . . . 0.3289 
'X-RAY DIFFRACTION' 1.44 1.47  . . 128 1507 100.00 . . . . 0.2591 . . . . . . . . . . . 0.3187 
'X-RAY DIFFRACTION' 1.47 1.52  . . 142 1485 100.00 . . . . 0.2451 . . . . . . . . . . . 0.2600 
'X-RAY DIFFRACTION' 1.52 1.57  . . 134 1526 99.94  . . . . 0.2242 . . . . . . . . . . . 0.2576 
'X-RAY DIFFRACTION' 1.57 1.62  . . 137 1501 100.00 . . . . 0.1985 . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 1.62 1.69  . . 141 1518 100.00 . . . . 0.1819 . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 1.69 1.76  . . 130 1518 100.00 . . . . 0.1717 . . . . . . . . . . . 0.2145 
'X-RAY DIFFRACTION' 1.76 1.86  . . 142 1514 100.00 . . . . 0.1636 . . . . . . . . . . . 0.2106 
'X-RAY DIFFRACTION' 1.86 1.97  . . 139 1528 100.00 . . . . 0.1483 . . . . . . . . . . . 0.1678 
'X-RAY DIFFRACTION' 1.97 2.12  . . 139 1525 100.00 . . . . 0.1367 . . . . . . . . . . . 0.1545 
'X-RAY DIFFRACTION' 2.13 2.34  . . 139 1543 100.00 . . . . 0.1334 . . . . . . . . . . . 0.1695 
'X-RAY DIFFRACTION' 2.34 2.68  . . 139 1551 100.00 . . . . 0.1342 . . . . . . . . . . . 0.1727 
'X-RAY DIFFRACTION' 2.68 3.37  . . 144 1581 100.00 . . . . 0.1380 . . . . . . . . . . . 0.1613 
'X-RAY DIFFRACTION' 3.37 21.39 . . 150 1667 99.94  . . . . 0.1712 . . . . . . . . . . . 0.1947 
# 
_struct.entry_id                     9FCB 
_struct.title                        'HEN EGG-WHITE Lysozyme incubated at 34% 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        9FCB 
_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 2 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
O 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              9FCB 
_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)' 1950 ? 
1 MORE         -41  ? 
1 'SSA (A^2)'  6730 ? 
# 
_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,O 
# 
_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 ? ? ? ? ? ? ? 2.009 ? ? 
disulf2 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 115 SG ? ? A CYS 30  A CYS 115 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 80  SG ? ? A CYS 64  A CYS 80  1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf4 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 94  SG ? ? A CYS 76  A CYS 94  1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc1 metalc ? ? A SER 24 OG ? ? ? 1_555 N NA  .   NA ? ? A SER 24  A NA  213 1_555 ? ? ? ? ? ? ? 2.808 ? ? 
metalc2 metalc ? ? A SER 60 O  B ? ? 1_555 M NA  .   NA ? ? A SER 60  A NA  212 1_555 ? ? ? ? ? ? ? 2.241 ? ? 
metalc3 metalc ? ? A SER 60 O  C ? ? 1_555 M NA  .   NA ? ? A SER 60  A NA  212 1_555 ? ? ? ? ? ? ? 2.821 ? ? 
metalc4 metalc ? ? A CYS 64 O  ? ? ? 1_555 M NA  .   NA ? ? A CYS 64  A NA  212 1_555 ? ? ? ? ? ? ? 2.445 ? ? 
metalc5 metalc ? ? A SER 72 OG ? ? ? 1_555 M NA  .   NA ? ? A SER 72  A NA  212 1_555 ? ? ? ? ? ? ? 2.493 ? ? 
metalc6 metalc ? ? A ARG 73 O  ? ? ? 1_555 M NA  .   NA ? ? A ARG 73  A NA  212 1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc7 metalc ? ? M NA  .  NA ? ? ? 1_555 O HOH .   O  ? ? A NA  212 A HOH 347 1_555 ? ? ? ? ? ? ? 2.482 ? ? 
metalc8 metalc ? ? M NA  .  NA ? ? ? 1_555 O HOH .   O  ? ? A NA  212 A HOH 354 1_555 ? ? ? ? ? ? ? 2.602 ? ? 
# 
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  B A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  C A SER 60 ? A SER 60  ? 1_555 10.8  ? 
2  O  B A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? A CYS 64 ? A CYS 64  ? 1_555 88.3  ? 
3  O  C A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? A CYS 64 ? A CYS 64  ? 1_555 95.5  ? 
4  O  B A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 OG ? A SER 72 ? A SER 72  ? 1_555 90.6  ? 
5  O  C A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 OG ? A SER 72 ? A SER 72  ? 1_555 81.6  ? 
6  O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 OG ? A SER 72 ? A SER 72  ? 1_555 165.5 ? 
7  O  B A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? A ARG 73 ? A ARG 73  ? 1_555 95.7  ? 
8  O  C A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? A ARG 73 ? A ARG 73  ? 1_555 103.4 ? 
9  O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? A ARG 73 ? A ARG 73  ? 1_555 92.2  ? 
10 OG ? A SER 72 ? A SER 72  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? A ARG 73 ? A ARG 73  ? 1_555 102.2 ? 
11 O  B A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 347 ? 1_555 173.1 ? 
12 O  C A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 347 ? 1_555 162.3 ? 
13 O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 347 ? 1_555 95.5  ? 
14 OG ? A SER 72 ? A SER 72  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 347 ? 1_555 84.3  ? 
15 O  ? A ARG 73 ? A ARG 73  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 347 ? 1_555 89.9  ? 
16 O  B A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 354 ? 1_555 102.0 ? 
17 O  C A SER 60 ? A SER 60  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 354 ? 1_555 94.4  ? 
18 O  ? A CYS 64 ? A CYS 64  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 354 ? 1_555 87.4  ? 
19 OG ? A SER 72 ? A SER 72  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 354 ? 1_555 78.8  ? 
20 O  ? A ARG 73 ? A ARG 73  ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 354 ? 1_555 162.2 ? 
21 O  ? O HOH .  ? A HOH 347 ? 1_555 NA ? M NA . ? A NA 212 ? 1_555 O  ? O HOH .  ? A HOH 354 ? 1_555 72.4  ? 
# 
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                   9FCB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    318 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    383 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.10 
# 
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 ASN A 19 ? B 80.83   16.22  
2 1 TRP A 62 ? B -138.80 -33.59 
3 1 ARG A 68 ? ? -142.73 23.01  
# 
_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     377 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   O 
_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                    9FCB 
_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]   0.012744 
_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]   0.012744 
_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]   0.026915 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A LYS A 1 1   ? -2.49400  -9.45800  -8.58800  0.620 19.19000  ? 1   LYS A N    1 
ATOM   2    N  N    B LYS A 1 1   ? -2.39700  -9.45300  -8.48800  0.380 19.35000  ? 1   LYS A N    1 
ATOM   3    C  CA   A LYS A 1 1   ? -1.50600  -9.83700  -9.61500  0.620 20.84000  ? 1   LYS A CA   1 
ATOM   4    C  CA   B LYS A 1 1   ? -1.48800  -9.83500  -9.59600  0.380 20.93000  ? 1   LYS A CA   1 
ATOM   5    C  C    A LYS A 1 1   ? -1.61100  -11.32500 -9.84100  0.620 19.99000  ? 1   LYS A C    1 
ATOM   6    C  C    B LYS A 1 1   ? -1.59700  -11.32900 -9.83600  0.380 20.02000  ? 1   LYS A C    1 
ATOM   7    O  O    A LYS A 1 1   ? -1.72000  -12.08400 -8.88900  0.620 18.78000  ? 1   LYS A O    1 
ATOM   8    O  O    B LYS A 1 1   ? -1.69200  -12.09800 -8.88500  0.380 18.91000  ? 1   LYS A O    1 
ATOM   9    C  CB   A LYS A 1 1   ? -0.09700  -9.48800  -9.13800  0.620 22.16000  ? 1   LYS A CB   1 
ATOM   10   C  CB   B LYS A 1 1   ? -0.05200  -9.46900  -9.22400  0.380 22.54000  ? 1   LYS A CB   1 
ATOM   11   C  CG   A LYS A 1 1   ? 0.97400   -10.02100 -10.06900 0.620 26.57000  ? 1   LYS A CG   1 
ATOM   12   C  CG   B LYS A 1 1   ? 0.99900   -10.06300 -10.14800 0.380 26.52000  ? 1   LYS A CG   1 
ATOM   13   C  CD   A LYS A 1 1   ? 2.33400   -9.44800  -9.76600  0.620 29.50000  ? 1   LYS A CD   1 
ATOM   14   C  CD   B LYS A 1 1   ? 2.35400   -9.42700  -9.90600  0.380 29.90000  ? 1   LYS A CD   1 
ATOM   15   C  CE   A LYS A 1 1   ? 3.39200   -10.23700 -10.52700 0.620 30.86000  ? 1   LYS A CE   1 
ATOM   16   C  CE   B LYS A 1 1   ? 3.46200   -10.18300 -10.62800 0.380 30.66000  ? 1   LYS A CE   1 
ATOM   17   N  NZ   A LYS A 1 1   ? 4.43300   -9.37600  -11.12200 0.620 31.55000  ? 1   LYS A NZ   1 
ATOM   18   N  NZ   B LYS A 1 1   ? 3.28000   -10.21500 -12.10400 0.380 23.97000  ? 1   LYS A NZ   1 
ATOM   19   H  H1   A LYS A 1 1   ? -3.20100  -9.99600  -8.64300  0.620 23.01000  ? 1   LYS A H1   1 
ATOM   20   H  H1   B LYS A 1 1   ? -2.78800  -10.18200 -8.16000  0.380 23.20000  ? 1   LYS A H1   1 
ATOM   21   H  H2   A LYS A 1 1   ? -2.12700  -9.53300  -7.78100  0.620 23.01000  ? 1   LYS A H2   1 
ATOM   22   H  H2   B LYS A 1 1   ? -1.93000  -9.05200  -7.84600  0.380 23.20000  ? 1   LYS A H2   1 
ATOM   23   H  H3   A LYS A 1 1   ? -2.75100  -8.61600  -8.72000  0.620 23.01000  ? 1   LYS A H3   1 
ATOM   24   H  H3   B LYS A 1 1   ? -3.02000  -8.89600  -8.79400  0.380 23.20000  ? 1   LYS A H3   1 
ATOM   25   H  HA   A LYS A 1 1   ? -1.66500  -9.36100  -10.44500 0.620 25.00000  ? 1   LYS A HA   1 
ATOM   26   H  HA   B LYS A 1 1   ? -1.72100  -9.36500  -10.41200 0.380 25.11000  ? 1   LYS A HA   1 
ATOM   27   H  HB2  A LYS A 1 1   ? -0.00700  -8.52400  -9.09300  0.620 26.58000  ? 1   LYS A HB2  1 
ATOM   28   H  HB2  B LYS A 1 1   ? 0.04100   -8.50400  -9.25500  0.380 27.03000  ? 1   LYS A HB2  1 
ATOM   29   H  HB3  A LYS A 1 1   ? 0.04600   -9.87600  -8.26000  0.620 26.58000  ? 1   LYS A HB3  1 
ATOM   30   H  HB3  B LYS A 1 1   ? 0.12900   -9.79100  -8.32700  0.380 27.03000  ? 1   LYS A HB3  1 
ATOM   31   H  HG2  A LYS A 1 1   ? 1.02600   -10.98500 -9.97500  0.620 31.87000  ? 1   LYS A HG2  1 
ATOM   32   H  HG2  B LYS A 1 1   ? 1.07200   -11.01600 -9.98300  0.380 31.82000  ? 1   LYS A HG2  1 
ATOM   33   H  HG3  A LYS A 1 1   ? 0.74600   -9.78800  -10.98200 0.620 31.87000  ? 1   LYS A HG3  1 
ATOM   34   H  HG3  B LYS A 1 1   ? 0.74500   -9.90500  -11.07100 0.380 31.82000  ? 1   LYS A HG3  1 
ATOM   35   H  HD2  A LYS A 1 1   ? 2.37100   -8.52100  -10.04700 0.620 35.39000  ? 1   LYS A HD2  1 
ATOM   36   H  HD2  B LYS A 1 1   ? 2.34400   -8.51400  -10.23300 0.380 35.87000  ? 1   LYS A HD2  1 
ATOM   37   H  HD3  A LYS A 1 1   ? 2.51600   -9.51500  -8.81600  0.620 35.39000  ? 1   LYS A HD3  1 
ATOM   38   H  HD3  B LYS A 1 1   ? 2.54800   -9.43600  -8.95500  0.380 35.87000  ? 1   LYS A HD3  1 
ATOM   39   H  HE2  A LYS A 1 1   ? 3.82600   -10.85300 -9.91600  0.620 37.02000  ? 1   LYS A HE2  1 
ATOM   40   H  HE2  B LYS A 1 1   ? 4.31100   -9.75300  -10.44100 0.380 36.78000  ? 1   LYS A HE2  1 
ATOM   41   H  HE3  A LYS A 1 1   ? 2.96400   -10.72900 -11.24500 0.620 37.02000  ? 1   LYS A HE3  1 
ATOM   42   H  HE3  B LYS A 1 1   ? 3.47700   -11.09900 -10.31000 0.380 36.78000  ? 1   LYS A HE3  1 
ATOM   43   H  HZ1  A LYS A 1 1   ? 5.13800   -9.86800  -11.35500 0.620 37.84000  ? 1   LYS A HZ1  1 
ATOM   44   H  HZ1  B LYS A 1 1   ? 3.17500   -9.38700  -12.41500 0.380 28.75000  ? 1   LYS A HZ1  1 
ATOM   45   H  HZ2  A LYS A 1 1   ? 4.11300   -8.96800  -11.84500 0.620 37.84000  ? 1   LYS A HZ2  1 
ATOM   46   H  HZ2  B LYS A 1 1   ? 3.99200   -10.58100 -12.49000 0.380 28.75000  ? 1   LYS A HZ2  1 
ATOM   47   H  HZ3  A LYS A 1 1   ? 4.69200   -8.76100  -10.53300 0.620 37.84000  ? 1   LYS A HZ3  1 
ATOM   48   H  HZ3  B LYS A 1 1   ? 2.55900   -10.69400 -12.31100 0.380 28.75000  ? 1   LYS A HZ3  1 
ATOM   49   N  N    . VAL A 1 2   ? -1.59900  -11.74300 -11.09900 1.000 18.91000  ? 2   VAL A N    1 
ATOM   50   C  CA   . VAL A 1 2   ? -1.54400  -13.14600 -11.46600 1.000 16.50000  ? 2   VAL A CA   1 
ATOM   51   C  C    . VAL A 1 2   ? -0.13000  -13.39100 -11.95900 1.000 22.36000  ? 2   VAL A C    1 
ATOM   52   O  O    . VAL A 1 2   ? 0.29700   -12.78200 -12.94500 1.000 21.79000  ? 2   VAL A O    1 
ATOM   53   C  CB   . VAL A 1 2   ? -2.57800  -13.48000 -12.54300 1.000 20.54000  ? 2   VAL A CB   1 
ATOM   54   C  CG1  . VAL A 1 2   ? -2.41500  -14.89500 -13.01600 1.000 29.77000  ? 2   VAL A CG1  1 
ATOM   55   C  CG2  . VAL A 1 2   ? -3.96000  -13.27800 -11.97900 1.000 20.24000  ? 2   VAL A CG2  1 
ATOM   56   H  H    . VAL A 1 2   ? -1.62200  -11.21700 -11.77900 1.000 22.68000  ? 2   VAL A H    1 
ATOM   57   H  HA   . VAL A 1 2   ? -1.72200  -13.71300 -10.70000 1.000 19.78000  ? 2   VAL A HA   1 
ATOM   58   H  HB   . VAL A 1 2   ? -2.45100  -12.89400 -13.30600 1.000 24.63000  ? 2   VAL A HB   1 
ATOM   59   H  HG11 . VAL A 1 2   ? -3.16900  -15.12900 -13.57900 1.000 35.71000  ? 2   VAL A HG11 1 
ATOM   60   H  HG12 . VAL A 1 2   ? -1.59000  -14.96500 -13.52300 1.000 35.71000  ? 2   VAL A HG12 1 
ATOM   61   H  HG13 . VAL A 1 2   ? -2.38100  -15.48400 -12.24600 1.000 35.71000  ? 2   VAL A HG13 1 
ATOM   62   H  HG21 . VAL A 1 2   ? -4.61300  -13.59600 -12.62200 1.000 24.28000  ? 2   VAL A HG21 1 
ATOM   63   H  HG22 . VAL A 1 2   ? -4.04000  -13.77800 -11.15200 1.000 24.28000  ? 2   VAL A HG22 1 
ATOM   64   H  HG23 . VAL A 1 2   ? -4.09700  -12.33300 -11.80900 1.000 24.28000  ? 2   VAL A HG23 1 
ATOM   65   N  N    . PHE A 1 3   ? 0.60300   -14.24600 -11.25100 1.000 21.08000  ? 3   PHE A N    1 
ATOM   66   C  CA   . PHE A 1 3   ? 1.98400   -14.56300 -11.59000 1.000 18.61000  ? 3   PHE A CA   1 
ATOM   67   C  C    . PHE A 1 3   ? 2.03600   -15.62900 -12.66900 1.000 20.49000  ? 3   PHE A C    1 
ATOM   68   O  O    . PHE A 1 3   ? 1.16700   -16.49500 -12.77900 1.000 21.07000  ? 3   PHE A O    1 
ATOM   69   C  CB   . PHE A 1 3   ? 2.71500   -15.14100 -10.37900 1.000 19.93000  ? 3   PHE A CB   1 
ATOM   70   C  CG   . PHE A 1 3   ? 3.24300   -14.13400 -9.42400  1.000 19.15000  ? 3   PHE A CG   1 
ATOM   71   C  CD1  . PHE A 1 3   ? 2.40800   -13.56100 -8.48700  1.000 22.10000  ? 3   PHE A CD1  1 
ATOM   72   C  CD2  . PHE A 1 3   ? 4.58300   -13.76300 -9.41400  1.000 19.33000  ? 3   PHE A CD2  1 
ATOM   73   C  CE1  . PHE A 1 3   ? 2.87400   -12.65700 -7.59100  1.000 21.88000  ? 3   PHE A CE1  1 
ATOM   74   C  CE2  . PHE A 1 3   ? 5.05100   -12.86700 -8.49300  1.000 20.97000  ? 3   PHE A CE2  1 
ATOM   75   C  CZ   . PHE A 1 3   ? 4.19800   -12.29500 -7.59400  1.000 25.98000  ? 3   PHE A CZ   1 
ATOM   76   H  H    . PHE A 1 3   ? 0.31700   -14.66400 -10.55600 1.000 25.29000  ? 3   PHE A H    1 
ATOM   77   H  HA   . PHE A 1 3   ? 2.41700   -13.74900 -11.89100 1.000 22.31000  ? 3   PHE A HA   1 
ATOM   78   H  HB2  . PHE A 1 3   ? 2.09800   -15.71000 -9.89100  1.000 23.91000  ? 3   PHE A HB2  1 
ATOM   79   H  HB3  . PHE A 1 3   ? 3.46800   -15.66400 -10.69700 1.000 23.91000  ? 3   PHE A HB3  1 
ATOM   80   H  HD1  . PHE A 1 3   ? 1.50900   -13.79900 -8.47000  1.000 26.50000  ? 3   PHE A HD1  1 
ATOM   81   H  HD2  . PHE A 1 3   ? 5.16600   -14.12700 -10.04000 1.000 23.18000  ? 3   PHE A HD2  1 
ATOM   82   H  HE1  . PHE A 1 3   ? 2.29300   -12.28000 -6.97100  1.000 26.25000  ? 3   PHE A HE1  1 
ATOM   83   H  HE2  . PHE A 1 3   ? 5.95500   -12.64700 -8.47900  1.000 25.16000  ? 3   PHE A HE2  1 
ATOM   84   H  HZ   . PHE A 1 3   ? 4.51200   -11.66400 -6.98800  1.000 31.17000  ? 3   PHE A HZ   1 
ATOM   85   N  N    . GLY A 1 4   ? 3.10000   -15.56500 -13.47300 1.000 23.68000  ? 4   GLY A N    1 
ATOM   86   C  CA   . GLY A 1 4   ? 3.48100   -16.71800 -14.24900 1.000 23.98000  ? 4   GLY A CA   1 
ATOM   87   C  C    . GLY A 1 4   ? 4.13600   -17.76300 -13.36500 1.000 18.85000  ? 4   GLY A C    1 
ATOM   88   O  O    . GLY A 1 4   ? 4.69300   -17.45200 -12.31500 1.000 20.84000  ? 4   GLY A O    1 
ATOM   89   H  H    . GLY A 1 4   ? 3.60100   -14.87400 -13.57800 1.000 28.40000  ? 4   GLY A H    1 
ATOM   90   H  HA2  . GLY A 1 4   ? 2.69600   -17.10700 -14.66600 1.000 28.76000  ? 4   GLY A HA2  1 
ATOM   91   H  HA3  . GLY A 1 4   ? 4.10800   -16.45500 -14.94100 1.000 28.76000  ? 4   GLY A HA3  1 
ATOM   92   N  N    . ARG A 1 5   ? 4.11700   -19.00000 -13.84500 1.000 22.42000  ? 5   ARG A N    1 
ATOM   93   C  CA   . ARG A 1 5   ? 4.69800   -20.10700 -13.10400 1.000 21.16000  ? 5   ARG A CA   1 
ATOM   94   C  C    . ARG A 1 5   ? 6.15900   -19.84200 -12.75500 1.000 21.86000  ? 5   ARG A C    1 
ATOM   95   O  O    . ARG A 1 5   ? 6.56300   -19.93400 -11.58500 1.000 19.75000  ? 5   ARG A O    1 
ATOM   96   C  CB   . ARG A 1 5   ? 4.54400   -21.36800 -13.94100 1.000 25.55000  ? 5   ARG A CB   1 
ATOM   97   C  CG   . ARG A 1 5   ? 5.20500   -22.56000 -13.36200 1.000 26.13000  ? 5   ARG A CG   1 
ATOM   98   C  CD   . ARG A 1 5   ? 4.91100   -23.79100 -14.17500 1.000 24.42000  ? 5   ARG A CD   1 
ATOM   99   N  NE   . ARG A 1 5   ? 5.52400   -23.76900 -15.49800 1.000 28.03000  ? 5   ARG A NE   1 
ATOM   100  C  CZ   . ARG A 1 5   ? 6.72100   -24.26700 -15.79000 1.000 26.93000  ? 5   ARG A CZ   1 
ATOM   101  N  NH1  . ARG A 1 5   ? 7.51900   -24.74400 -14.85400 1.000 27.38000  ? 5   ARG A NH1  1 
ATOM   102  N  NH2  . ARG A 1 5   ? 7.12800   -24.27600 -17.05500 1.000 34.06000  ? 5   ARG A NH2  1 
ATOM   103  H  H    . ARG A 1 5   ? 3.77100   -19.22600 -14.60000 1.000 26.89000  ? 5   ARG A H    1 
ATOM   104  H  HA   . ARG A 1 5   ? 4.23100   -20.22700 -12.26200 1.000 25.39000  ? 5   ARG A HA   1 
ATOM   105  H  HB2  . ARG A 1 5   ? 3.59900   -21.56900 -14.03000 1.000 30.65000  ? 5   ARG A HB2  1 
ATOM   106  H  HB3  . ARG A 1 5   ? 4.93300   -21.21000 -14.81500 1.000 30.65000  ? 5   ARG A HB3  1 
ATOM   107  H  HG2  . ARG A 1 5   ? 6.16500   -22.42200 -13.35100 1.000 31.35000  ? 5   ARG A HG2  1 
ATOM   108  H  HG3  . ARG A 1 5   ? 4.88000   -22.70300 -12.46000 1.000 31.35000  ? 5   ARG A HG3  1 
ATOM   109  H  HD2  . ARG A 1 5   ? 5.25000   -24.56700 -13.70300 1.000 29.29000  ? 5   ARG A HD2  1 
ATOM   110  H  HD3  . ARG A 1 5   ? 3.95100   -23.86700 -14.29400 1.000 29.29000  ? 5   ARG A HD3  1 
ATOM   111  H  HE   . ARG A 1 5   ? 5.07800   -23.40600 -16.13700 1.000 33.62000  ? 5   ARG A HE   1 
ATOM   112  H  HH11 . ARG A 1 5   ? 7.26900   -24.73800 -14.03100 1.000 32.84000  ? 5   ARG A HH11 1 
ATOM   113  H  HH12 . ARG A 1 5   ? 8.28900   -25.06200 -15.06600 1.000 32.84000  ? 5   ARG A HH12 1 
ATOM   114  H  HH21 . ARG A 1 5   ? 6.61800   -23.96200 -17.67300 1.000 40.86000  ? 5   ARG A HH21 1 
ATOM   115  H  HH22 . ARG A 1 5   ? 7.90000   -24.59600 -17.25600 1.000 40.86000  ? 5   ARG A HH22 1 
ATOM   116  N  N    . CYS A 1 6   ? 6.98100   -19.52400 -13.75900 1.000 20.43000  ? 6   CYS A N    1 
ATOM   117  C  CA   . CYS A 1 6   ? 8.40100   -19.32900 -13.48900 1.000 21.49000  ? 6   CYS A CA   1 
ATOM   118  C  C    . CYS A 1 6   ? 8.67000   -18.00400 -12.79700 1.000 20.29000  ? 6   CYS A C    1 
ATOM   119  O  O    . CYS A 1 6   ? 9.63600   -17.86700 -12.05200 1.000 20.92000  ? 6   CYS A O    1 
ATOM   120  C  CB   . CYS A 1 6   ? 9.21300   -19.42900 -14.79300 1.000 24.26000  ? 6   CYS A CB   1 
ATOM   121  S  SG   . CYS A 1 6   ? 9.19800   -21.08100 -15.49300 1.000 25.00000  ? 6   CYS A SG   1 
ATOM   122  H  H    . CYS A 1 6   ? 6.74700   -19.41900 -14.57900 1.000 24.50000  ? 6   CYS A H    1 
ATOM   123  H  HA   . CYS A 1 6   ? 8.69900   -20.03800 -12.89800 1.000 25.77000  ? 6   CYS A HA   1 
ATOM   124  H  HB2  . CYS A 1 6   ? 8.83500   -18.82100 -15.44700 1.000 29.10000  ? 6   CYS A HB2  1 
ATOM   125  H  HB3  . CYS A 1 6   ? 10.13400  -19.18800 -14.61000 1.000 29.10000  ? 6   CYS A HB3  1 
ATOM   126  N  N    . GLU A 1 7   ? 7.81300   -17.00500 -13.01100 1.000 21.87000  ? 7   GLU A N    1 
ATOM   127  C  CA   . GLU A 1 7   ? 7.96800   -15.74500 -12.30400 1.000 19.02000  ? 7   GLU A CA   1 
ATOM   128  C  C    . GLU A 1 7   ? 7.74700   -15.93800 -10.81000 1.000 16.30000  ? 7   GLU A C    1 
ATOM   129  O  O    . GLU A 1 7   ? 8.48500   -15.40400 -9.97200  1.000 18.58000  ? 7   GLU A O    1 
ATOM   130  C  CB   . GLU A 1 7   ? 6.90300   -14.77800 -12.82500 1.000 23.82000  ? 7   GLU A CB   1 
ATOM   131  C  CG   . GLU A 1 7   ? 6.98500   -13.40100 -12.23700 1.000 22.54000  ? 7   GLU A CG   1 
ATOM   132  C  CD   . GLU A 1 7   ? 5.76300   -12.53000 -12.56600 1.000 23.66000  ? 7   GLU A CD   1 
ATOM   133  O  OE1  . GLU A 1 7   ? 4.74800   -13.05200 -13.07200 1.000 24.55000  ? 7   GLU A OE1  1 
ATOM   134  O  OE2  . GLU A 1 7   ? 5.85600   -11.31400 -12.31200 1.000 32.36000  ? 7   GLU A OE2  1 
ATOM   135  H  H    . GLU A 1 7   ? 7.14600   -17.03400 -13.55200 1.000 26.23000  ? 7   GLU A H    1 
ATOM   136  H  HA   . GLU A 1 7   ? 8.85900   -15.39100 -12.45300 1.000 22.81000  ? 7   GLU A HA   1 
ATOM   137  H  HB2  . GLU A 1 7   ? 7.00400   -14.69400 -13.78600 1.000 28.57000  ? 7   GLU A HB2  1 
ATOM   138  H  HB3  . GLU A 1 7   ? 6.02800   -15.13700 -12.61300 1.000 28.57000  ? 7   GLU A HB3  1 
ATOM   139  H  HG2  . GLU A 1 7   ? 7.04800   -13.47400 -11.27200 1.000 27.03000  ? 7   GLU A HG2  1 
ATOM   140  H  HG3  . GLU A 1 7   ? 7.77200   -12.95600 -12.58700 1.000 27.03000  ? 7   GLU A HG3  1 
ATOM   141  N  N    . LEU A 1 8   ? 6.74000   -16.73700 -10.47400 1.000 19.10000  ? 8   LEU A N    1 
ATOM   142  C  CA   . LEU A 1 8   ? 6.48600   -17.00000 -9.07200  1.000 16.91000  ? 8   LEU A CA   1 
ATOM   143  C  C    . LEU A 1 8   ? 7.59800   -17.83500 -8.47100  1.000 16.87000  ? 8   LEU A C    1 
ATOM   144  O  O    . LEU A 1 8   ? 8.04200   -17.57300 -7.35000  1.000 17.89000  ? 8   LEU A O    1 
ATOM   145  C  CB   . LEU A 1 8   ? 5.14100   -17.68700 -8.91400  1.000 17.11000  ? 8   LEU A CB   1 
ATOM   146  C  CG   . LEU A 1 8   ? 4.80100   -18.00800 -7.46900  1.000 18.09000  ? 8   LEU A CG   1 
ATOM   147  C  CD1  . LEU A 1 8   ? 4.62600   -16.79900 -6.60600  1.000 21.29000  ? 8   LEU A CD1  1 
ATOM   148  C  CD2  . LEU A 1 8   ? 3.54100   -18.88500 -7.46200  1.000 21.88000  ? 8   LEU A CD2  1 
ATOM   149  H  H    . LEU A 1 8   ? 6.20600   -17.12600 -11.02500 1.000 22.91000  ? 8   LEU A H    1 
ATOM   150  H  HA   . LEU A 1 8   ? 6.44900   -16.16100 -8.58800  1.000 20.29000  ? 8   LEU A HA   1 
ATOM   151  H  HB2  . LEU A 1 8   ? 4.44800   -17.10400 -9.26100  1.000 20.52000  ? 8   LEU A HB2  1 
ATOM   152  H  HB3  . LEU A 1 8   ? 5.15300   -18.52000 -9.41000  1.000 20.52000  ? 8   LEU A HB3  1 
ATOM   153  H  HG   . LEU A 1 8   ? 5.54900   -18.48100 -7.07000  1.000 21.69000  ? 8   LEU A HG   1 
ATOM   154  H  HD11 . LEU A 1 8   ? 4.33200   -17.07900 -5.72500  1.000 25.53000  ? 8   LEU A HD11 1 
ATOM   155  H  HD12 . LEU A 1 8   ? 5.47400   -16.33300 -6.53900  1.000 25.53000  ? 8   LEU A HD12 1 
ATOM   156  H  HD13 . LEU A 1 8   ? 3.96000   -16.21800 -7.00700  1.000 25.53000  ? 8   LEU A HD13 1 
ATOM   157  H  HD21 . LEU A 1 8   ? 3.19100   -18.92900 -6.55800  1.000 26.25000  ? 8   LEU A HD21 1 
ATOM   158  H  HD22 . LEU A 1 8   ? 2.88000   -18.49200 -8.05300  1.000 26.25000  ? 8   LEU A HD22 1 
ATOM   159  H  HD23 . LEU A 1 8   ? 3.77300   -19.77500 -7.77000  1.000 26.25000  ? 8   LEU A HD23 1 
ATOM   160  N  N    . ALA A 1 9   ? 8.07200   -18.84200 -9.19600  1.000 18.91000  ? 9   ALA A N    1 
ATOM   161  C  CA   . ALA A 1 9   ? 9.17200   -19.64000 -8.66800  1.000 18.43000  ? 9   ALA A CA   1 
ATOM   162  C  C    . ALA A 1 9   ? 10.38000  -18.76200 -8.36100  1.000 17.90000  ? 9   ALA A C    1 
ATOM   163  O  O    . ALA A 1 9   ? 11.03800  -18.92900 -7.32500  1.000 18.79000  ? 9   ALA A O    1 
ATOM   164  C  CB   . ALA A 1 9   ? 9.54200   -20.73300 -9.67000  1.000 19.87000  ? 9   ALA A CB   1 
ATOM   165  H  H    . ALA A 1 9   ? 7.78400   -19.07800 -9.97200  1.000 22.68000  ? 9   ALA A H    1 
ATOM   166  H  HA   . ALA A 1 9   ? 8.89100   -20.06800 -7.84400  1.000 22.10000  ? 9   ALA A HA   1 
ATOM   167  H  HB1  . ALA A 1 9   ? 10.25100  -21.27900 -9.29500  1.000 23.83000  ? 9   ALA A HB1  1 
ATOM   168  H  HB2  . ALA A 1 9   ? 8.76100   -21.28000 -9.84500  1.000 23.83000  ? 9   ALA A HB2  1 
ATOM   169  H  HB3  . ALA A 1 9   ? 9.84600   -20.31800 -10.49300 1.000 23.83000  ? 9   ALA A HB3  1 
ATOM   170  N  N    . ALA A 1 10  ? 10.69900  -17.82000 -9.26100  1.000 19.81000  ? 10  ALA A N    1 
ATOM   171  C  CA   . ALA A 1 10  ? 11.83400  -16.93000 -9.04200  1.000 20.49000  ? 10  ALA A CA   1 
ATOM   172  C  C    . ALA A 1 10  ? 11.62200  -16.05900 -7.81700  1.000 19.09000  ? 10  ALA A C    1 
ATOM   173  O  O    . ALA A 1 10  ? 12.54400  -15.85800 -7.01600  1.000 20.70000  ? 10  ALA A O    1 
ATOM   174  C  CB   . ALA A 1 10  ? 12.07900  -16.05600 -10.27800 1.000 21.49000  ? 10  ALA A CB   1 
ATOM   175  H  H    . ALA A 1 10  ? 10.27600  -17.68100 -9.99700  1.000 23.76000  ? 10  ALA A H    1 
ATOM   176  H  HA   . ALA A 1 10  ? 12.62400  -17.47400 -8.89800  1.000 24.57000  ? 10  ALA A HA   1 
ATOM   177  H  HB1  . ALA A 1 10  ? 12.77000  -15.40700 -10.07400 1.000 25.78000  ? 10  ALA A HB1  1 
ATOM   178  H  HB2  . ALA A 1 10  ? 12.36300  -16.62200 -11.01300 1.000 25.78000  ? 10  ALA A HB2  1 
ATOM   179  H  HB3  . ALA A 1 10  ? 11.25500  -15.60000 -10.51100 1.000 25.78000  ? 10  ALA A HB3  1 
ATOM   180  N  N    . ALA A 1 11  ? 10.40700  -15.53500 -7.63600  1.000 18.11000  ? 11  ALA A N    1 
ATOM   181  C  CA   . ALA A 1 11  ? 10.16100  -14.70200 -6.47000  1.000 18.32000  ? 11  ALA A CA   1 
ATOM   182  C  C    . ALA A 1 11  ? 10.24400  -15.50800 -5.18700  1.000 19.26000  ? 11  ALA A C    1 
ATOM   183  O  O    . ALA A 1 11  ? 10.78200  -15.04100 -4.18800  1.000 20.81000  ? 11  ALA A O    1 
ATOM   184  C  CB   . ALA A 1 11  ? 8.80400   -14.02500 -6.58200  1.000 22.11000  ? 11  ALA A CB   1 
ATOM   185  H  H    . ALA A 1 11  ? 9.73400   -15.64600 -8.15900  1.000 21.71000  ? 11  ALA A H    1 
ATOM   186  H  HA   . ALA A 1 11  ? 10.84100  -14.01100 -6.43900  1.000 21.97000  ? 11  ALA A HA   1 
ATOM   187  H  HB1  . ALA A 1 11  ? 8.62700   -13.53500 -5.76300  1.000 26.52000  ? 11  ALA A HB1  1 
ATOM   188  H  HB2  . ALA A 1 11  ? 8.81600   -13.41500 -7.33600  1.000 26.52000  ? 11  ALA A HB2  1 
ATOM   189  H  HB3  . ALA A 1 11  ? 8.12200   -14.70200 -6.71600  1.000 26.52000  ? 11  ALA A HB3  1 
ATOM   190  N  N    . MET A 1 12  ? 9.72200   -16.73200 -5.20300  1.000 18.23000  ? 12  MET A N    1 
ATOM   191  C  CA   . MET A 1 12  ? 9.83500   -17.57600 -4.01200  1.000 17.72000  ? 12  MET A CA   1 
ATOM   192  C  C    . MET A 1 12  ? 11.27900  -17.94600 -3.70300  1.000 19.76000  ? 12  MET A C    1 
ATOM   193  O  O    . MET A 1 12  ? 11.66400  -18.01000 -2.53000  1.000 21.64000  ? 12  MET A O    1 
ATOM   194  C  CB   . MET A 1 12  ? 8.98500   -18.82300 -4.12300  1.000 18.67000  ? 12  MET A CB   1 
ATOM   195  C  CG   . MET A 1 12  ? 7.50100   -18.51500 -4.14000  1.000 19.13000  ? 12  MET A CG   1 
ATOM   196  S  SD   . MET A 1 12  ? 6.53700   -20.01400 -4.45600  1.000 20.04000  ? 12  MET A SD   1 
ATOM   197  C  CE   . MET A 1 12  ? 4.93600   -19.62000 -3.77100  1.000 24.24000  ? 12  MET A CE   1 
ATOM   198  H  H    . MET A 1 12  ? 9.31100   -17.08900 -5.86900  1.000 21.87000  ? 12  MET A H    1 
ATOM   199  H  HA   . MET A 1 12  ? 9.48100   -17.05600 -3.27400  1.000 21.26000  ? 12  MET A HA   1 
ATOM   200  H  HB2  . MET A 1 12  ? 9.20600   -19.28600 -4.94600  1.000 22.39000  ? 12  MET A HB2  1 
ATOM   201  H  HB3  . MET A 1 12  ? 9.16400   -19.39700 -3.36200  1.000 22.39000  ? 12  MET A HB3  1 
ATOM   202  H  HG2  . MET A 1 12  ? 7.23500   -18.15300 -3.28000  1.000 22.94000  ? 12  MET A HG2  1 
ATOM   203  H  HG3  . MET A 1 12  ? 7.31200   -17.87300 -4.84300  1.000 22.94000  ? 12  MET A HG3  1 
ATOM   204  H  HE1  . MET A 1 12  ? 4.34300   -20.37700 -3.89700  1.000 29.08000  ? 12  MET A HE1  1 
ATOM   205  H  HE2  . MET A 1 12  ? 5.03500   -19.43200 -2.82400  1.000 29.08000  ? 12  MET A HE2  1 
ATOM   206  H  HE3  . MET A 1 12  ? 4.58000   -18.84200 -4.22700  1.000 29.08000  ? 12  MET A HE3  1 
ATOM   207  N  N    A LYS A 1 13  ? 12.08600  -18.23100 -4.72600  0.560 19.04000  ? 13  LYS A N    1 
ATOM   208  N  N    B LYS A 1 13  ? 12.07900  -18.20100 -4.74200  0.440 19.12000  ? 13  LYS A N    1 
ATOM   209  C  CA   A LYS A 1 13  ? 13.49700  -18.50700 -4.47300  0.560 20.04000  ? 13  LYS A CA   1 
ATOM   210  C  CA   B LYS A 1 13  ? 13.49900  -18.48400 -4.55400  0.440 20.10000  ? 13  LYS A CA   1 
ATOM   211  C  C    A LYS A 1 13  ? 14.20700  -17.29200 -3.88600  0.560 19.18000  ? 13  LYS A C    1 
ATOM   212  C  C    B LYS A 1 13  ? 14.22000  -17.31300 -3.89100  0.440 19.19000  ? 13  LYS A C    1 
ATOM   213  O  O    A LYS A 1 13  ? 14.99200  -17.41600 -2.93600  0.560 22.62000  ? 13  LYS A O    1 
ATOM   214  O  O    B LYS A 1 13  ? 14.95000  -17.49600 -2.90900  0.440 22.84000  ? 13  LYS A O    1 
ATOM   215  C  CB   A LYS A 1 13  ? 14.18400  -18.94800 -5.76000  0.560 20.95000  ? 13  LYS A CB   1 
ATOM   216  C  CB   B LYS A 1 13  ? 14.13100  -18.82300 -5.90500  0.440 19.72000  ? 13  LYS A CB   1 
ATOM   217  C  CG   A LYS A 1 13  ? 15.61000  -19.45200 -5.51400  0.560 20.67000  ? 13  LYS A CG   1 
ATOM   218  C  CG   B LYS A 1 13  ? 15.62700  -19.16000 -5.83400  0.440 23.81000  ? 13  LYS A CG   1 
ATOM   219  C  CD   A LYS A 1 13  ? 16.15300  -20.25200 -6.67300  0.560 29.37000  ? 13  LYS A CD   1 
ATOM   220  C  CD   B LYS A 1 13  ? 15.90400  -20.62300 -6.12900  0.440 33.75000  ? 13  LYS A CD   1 
ATOM   221  C  CE   A LYS A 1 13  ? 17.52300  -20.85100 -6.32800  0.560 36.98000  ? 13  LYS A CE   1 
ATOM   222  C  CE   B LYS A 1 13  ? 17.39400  -20.93800 -6.02600  0.440 37.04000  ? 13  LYS A CE   1 
ATOM   223  N  NZ   A LYS A 1 13  ? 17.49300  -21.81100 -5.18100  0.560 37.61000  ? 13  LYS A NZ   1 
ATOM   224  N  NZ   B LYS A 1 13  ? 18.14900  -20.57700 -7.26100  0.440 35.79000  ? 13  LYS A NZ   1 
ATOM   225  H  H    A LYS A 1 13  ? 11.84800  -18.27000 -5.55200  0.560 22.83000  ? 13  LYS A H    1 
ATOM   226  H  H    B LYS A 1 13  ? 11.82400  -18.21600 -5.56300  0.440 22.93000  ? 13  LYS A H    1 
ATOM   227  H  HA   A LYS A 1 13  ? 13.55900  -19.23100 -3.83000  0.560 24.03000  ? 13  LYS A HA   1 
ATOM   228  H  HA   B LYS A 1 13  ? 13.59600  -19.25100 -3.96700  0.440 24.10000  ? 13  LYS A HA   1 
ATOM   229  H  HB2  A LYS A 1 13  ? 13.67400  -19.66900 -6.16100  0.560 25.13000  ? 13  LYS A HB2  1 
ATOM   230  H  HB2  B LYS A 1 13  ? 13.67300  -19.59400 -6.27600  0.440 23.66000  ? 13  LYS A HB2  1 
ATOM   231  H  HB3  A LYS A 1 13  ? 14.23000  -18.19500 -6.37000  0.560 25.13000  ? 13  LYS A HB3  1 
ATOM   232  H  HB3  B LYS A 1 13  ? 14.02800  -18.06100 -6.49600  0.440 23.66000  ? 13  LYS A HB3  1 
ATOM   233  H  HG2  A LYS A 1 13  ? 16.19500  -18.69000 -5.37600  0.560 24.79000  ? 13  LYS A HG2  1 
ATOM   234  H  HG2  B LYS A 1 13  ? 16.10500  -18.62500 -6.48700  0.440 28.56000  ? 13  LYS A HG2  1 
ATOM   235  H  HG3  A LYS A 1 13  ? 15.61500  -20.02100 -4.72900  0.560 24.79000  ? 13  LYS A HG3  1 
ATOM   236  H  HG3  B LYS A 1 13  ? 15.95500  -18.96500 -4.94200  0.440 28.56000  ? 13  LYS A HG3  1 
ATOM   237  H  HD2  A LYS A 1 13  ? 15.54300  -20.97700 -6.87900  0.560 35.24000  ? 13  LYS A HD2  1 
ATOM   238  H  HD2  B LYS A 1 13  ? 15.42900  -21.17600 -5.48900  0.440 40.49000  ? 13  LYS A HD2  1 
ATOM   239  H  HD3  A LYS A 1 13  ? 16.25500  -19.67400 -7.44600  0.560 35.24000  ? 13  LYS A HD3  1 
ATOM   240  H  HD3  B LYS A 1 13  ? 15.60900  -20.83100 -7.03000  0.440 40.49000  ? 13  LYS A HD3  1 
ATOM   241  H  HE2  A LYS A 1 13  ? 17.85900  -21.32800 -7.10300  0.560 44.37000  ? 13  LYS A HE2  1 
ATOM   242  H  HE2  B LYS A 1 13  ? 17.77200  -20.43600 -5.28600  0.440 44.44000  ? 13  LYS A HE2  1 
ATOM   243  H  HE3  A LYS A 1 13  ? 18.12900  -20.13100 -6.09400  0.560 44.37000  ? 13  LYS A HE3  1 
ATOM   244  H  HE3  B LYS A 1 13  ? 17.50600  -21.88900 -5.87400  0.440 44.44000  ? 13  LYS A HE3  1 
ATOM   245  H  HZ1  A LYS A 1 13  ? 18.30700  -22.14000 -5.03700  0.560 45.12000  ? 13  LYS A HZ1  1 
ATOM   246  H  HZ1  B LYS A 1 13  ? 19.02100  -20.70000 -7.13200  0.440 42.94000  ? 13  LYS A HZ1  1 
ATOM   247  H  HZ2  A LYS A 1 13  ? 17.21500  -21.39600 -4.44400  0.560 45.12000  ? 13  LYS A HZ2  1 
ATOM   248  H  HZ2  B LYS A 1 13  ? 17.88300  -21.08600 -7.94000  0.440 42.94000  ? 13  LYS A HZ2  1 
ATOM   249  H  HZ3  A LYS A 1 13  ? 16.93700  -22.48300 -5.36100  0.560 45.12000  ? 13  LYS A HZ3  1 
ATOM   250  H  HZ3  B LYS A 1 13  ? 18.00600  -19.72300 -7.46700  0.440 42.94000  ? 13  LYS A HZ3  1 
ATOM   251  N  N    A ARG A 1 14  ? 13.93100  -16.10200 -4.42900  0.560 19.96000  ? 14  ARG A N    1 
ATOM   252  N  N    B ARG A 1 14  ? 14.02200  -16.09100 -4.40300  0.440 20.22000  ? 14  ARG A N    1 
ATOM   253  C  CA   A ARG A 1 14  ? 14.58300  -14.89600 -3.92900  0.560 20.00000  ? 14  ARG A CA   1 
ATOM   254  C  CA   B ARG A 1 14  ? 14.72900  -14.95600 -3.81500  0.440 21.43000  ? 14  ARG A CA   1 
ATOM   255  C  C    A ARG A 1 14  ? 14.28400  -14.67500 -2.45100  0.560 21.66000  ? 14  ARG A C    1 
ATOM   256  C  C    B ARG A 1 14  ? 14.33900  -14.75500 -2.35900  0.440 21.85000  ? 14  ARG A C    1 
ATOM   257  O  O    A ARG A 1 14  ? 15.13000  -14.17200 -1.70800  0.560 24.83000  ? 14  ARG A O    1 
ATOM   258  O  O    B ARG A 1 14  ? 15.16400  -14.32400 -1.54800  0.440 23.92000  ? 14  ARG A O    1 
ATOM   259  C  CB   A ARG A 1 14  ? 14.15000  -13.70000 -4.78400  0.560 21.77000  ? 14  ARG A CB   1 
ATOM   260  C  CB   B ARG A 1 14  ? 14.49500  -13.66300 -4.60000  0.440 24.83000  ? 14  ARG A CB   1 
ATOM   261  C  CG   A ARG A 1 14  ? 14.20700  -12.35700 -4.08100  0.560 34.39000  ? 14  ARG A CG   1 
ATOM   262  C  CG   B ARG A 1 14  ? 15.16100  -12.45500 -3.91900  0.440 29.90000  ? 14  ARG A CG   1 
ATOM   263  C  CD   A ARG A 1 14  ? 14.02500  -11.23200 -5.08600  0.560 26.74000  ? 14  ARG A CD   1 
ATOM   264  C  CD   B ARG A 1 14  ? 14.95800  -11.15100 -4.67600  0.440 33.00000  ? 14  ARG A CD   1 
ATOM   265  N  NE   A ARG A 1 14  ? 12.68100  -11.21600 -5.64700  0.560 32.03000  ? 14  ARG A NE   1 
ATOM   266  N  NE   B ARG A 1 14  ? 13.78400  -10.41600 -4.21200  0.440 32.28000  ? 14  ARG A NE   1 
ATOM   267  C  CZ   A ARG A 1 14  ? 11.65000  -10.57800 -5.11100  0.560 29.31000  ? 14  ARG A CZ   1 
ATOM   268  C  CZ   B ARG A 1 14  ? 13.72300  -9.72300  -3.08400  0.440 32.96000  ? 14  ARG A CZ   1 
ATOM   269  N  NH1  A ARG A 1 14  ? 11.79200  -9.81100  -4.03900  0.560 32.08000  ? 14  ARG A NH1  1 
ATOM   270  N  NH1  B ARG A 1 14  ? 14.75500  -9.65000  -2.25500  0.440 35.56000  ? 14  ARG A NH1  1 
ATOM   271  N  NH2  A ARG A 1 14  ? 10.44700  -10.72100 -5.65600  0.560 32.14000  ? 14  ARG A NH2  1 
ATOM   272  N  NH2  B ARG A 1 14  ? 12.59500  -9.09300  -2.77400  0.440 37.53000  ? 14  ARG A NH2  1 
ATOM   273  H  H    A ARG A 1 14  ? 13.38000  -15.97100 -5.07600  0.560 23.94000  ? 14  ARG A H    1 
ATOM   274  H  H    B ARG A 1 14  ? 13.50400  -15.90300 -5.06400  0.440 24.25000  ? 14  ARG A H    1 
ATOM   275  H  HA   A ARG A 1 14  ? 15.54600  -14.97900 -4.01100  0.560 23.99000  ? 14  ARG A HA   1 
ATOM   276  H  HA   B ARG A 1 14  ? 15.67800  -15.14900 -3.86700  0.440 25.70000  ? 14  ARG A HA   1 
ATOM   277  H  HB2  A ARG A 1 14  ? 14.73300  -13.64900 -5.55800  0.560 26.11000  ? 14  ARG A HB2  1 
ATOM   278  H  HB2  B ARG A 1 14  ? 14.87100  -13.75700 -5.48900  0.440 29.78000  ? 14  ARG A HB2  1 
ATOM   279  H  HB3  A ARG A 1 14  ? 13.23300  -13.84100 -5.06800  0.560 26.11000  ? 14  ARG A HB3  1 
ATOM   280  H  HB3  B ARG A 1 14  ? 13.54200  -13.49200 -4.65800  0.440 29.78000  ? 14  ARG A HB3  1 
ATOM   281  H  HG2  A ARG A 1 14  ? 13.49700  -12.30300 -3.42200  0.560 41.26000  ? 14  ARG A HG2  1 
ATOM   282  H  HG2  B ARG A 1 14  ? 14.78400  -12.34600 -3.03200  0.440 35.87000  ? 14  ARG A HG2  1 
ATOM   283  H  HG3  A ARG A 1 14  ? 15.06900  -12.25100 -3.64900  0.560 41.26000  ? 14  ARG A HG3  1 
ATOM   284  H  HG3  B ARG A 1 14  ? 16.11600  -12.61700 -3.85500  0.440 35.87000  ? 14  ARG A HG3  1 
ATOM   285  H  HD2  A ARG A 1 14  ? 14.18000  -10.38200 -4.64500  0.560 32.07000  ? 14  ARG A HD2  1 
ATOM   286  H  HD2  B ARG A 1 14  ? 15.73700  -10.58600 -4.55000  0.440 39.59000  ? 14  ARG A HD2  1 
ATOM   287  H  HD3  A ARG A 1 14  ? 14.65600  -11.34900 -5.81300  0.560 32.07000  ? 14  ARG A HD3  1 
ATOM   288  H  HD3  B ARG A 1 14  ? 14.83900  -11.34700 -5.61900  0.440 39.59000  ? 14  ARG A HD3  1 
ATOM   289  H  HE   A ARG A 1 14  ? 12.54700  -11.65100 -6.37600  0.560 38.42000  ? 14  ARG A HE   1 
ATOM   290  H  HE   B ARG A 1 14  ? 13.08100  -10.43500 -4.70800  0.440 38.73000  ? 14  ARG A HE   1 
ATOM   291  H  HH11 A ARG A 1 14  ? 12.56600  -9.71900  -3.67600  0.560 38.49000  ? 14  ARG A HH11 1 
ATOM   292  H  HH11 B ARG A 1 14  ? 15.48700  -10.05900 -2.44400  0.440 42.66000  ? 14  ARG A HH11 1 
ATOM   293  H  HH12 A ARG A 1 14  ? 11.11000  -9.40600  -3.70800  0.560 38.49000  ? 14  ARG A HH12 1 
ATOM   294  H  HH12 B ARG A 1 14  ? 14.69200  -9.19400  -1.52900  0.440 42.66000  ? 14  ARG A HH12 1 
ATOM   295  H  HH21 A ARG A 1 14  ? 10.34500  -11.22200 -6.34800  0.560 38.55000  ? 14  ARG A HH21 1 
ATOM   296  H  HH21 B ARG A 1 14  ? 11.91800  -9.13900  -3.30200  0.440 45.03000  ? 14  ARG A HH21 1 
ATOM   297  H  HH22 A ARG A 1 14  ? 9.77100   -10.31200 -5.31800  0.560 38.55000  ? 14  ARG A HH22 1 
ATOM   298  H  HH22 B ARG A 1 14  ? 12.54200  -8.64000  -2.04500  0.440 45.03000  ? 14  ARG A HH22 1 
ATOM   299  N  N    . HIS A 1 15  ? 13.10000  -15.07900 -2.00000  1.000 21.61000  ? 15  HIS A N    1 
ATOM   300  C  CA   . HIS A 1 15  ? 12.66900  -14.93700 -0.62500  1.000 20.69000  ? 15  HIS A CA   1 
ATOM   301  C  C    . HIS A 1 15  ? 13.04100  -16.13800 0.23600   1.000 24.03000  ? 15  HIS A C    1 
ATOM   302  O  O    . HIS A 1 15  ? 12.59400  -16.20600 1.38200   1.000 29.24000  ? 15  HIS A O    1 
ATOM   303  C  CB   . HIS A 1 15  ? 11.15500  -14.72300 -0.55200  1.000 22.97000  ? 15  HIS A CB   1 
ATOM   304  C  CG   . HIS A 1 15  ? 10.70300  -13.38000 -1.03500  1.000 22.21000  ? 15  HIS A CG   1 
ATOM   305  N  ND1  . HIS A 1 15  ? 10.71100  -12.26700 -0.22400  1.000 33.76000  ? 15  HIS A ND1  1 
ATOM   306  C  CD2  . HIS A 1 15  ? 10.18700  -12.97600 -2.21900  1.000 26.80000  ? 15  HIS A CD2  1 
ATOM   307  C  CE1  . HIS A 1 15  ? 10.23800  -11.23200 -0.89300  1.000 28.22000  ? 15  HIS A CE1  1 
ATOM   308  N  NE2  . HIS A 1 15  ? 9.90800   -11.63400 -2.10400  1.000 28.54000  ? 15  HIS A NE2  1 
ATOM   309  H  H    . HIS A 1 15  ? 12.50700  -15.45300 -2.49800  1.000 25.92000  ? 15  HIS A H    1 
ATOM   310  H  HA   . HIS A 1 15  ? 13.10100  -14.15000 -0.26000  1.000 24.82000  ? 15  HIS A HA   1 
ATOM   311  H  HB2  . HIS A 1 15  ? 10.72000  -15.39500 -1.10000  1.000 27.55000  ? 15  HIS A HB2  1 
ATOM   312  H  HB3  . HIS A 1 15  ? 10.87300  -14.81400 0.37100   1.000 27.55000  ? 15  HIS A HB3  1 
ATOM   313  H  HD1  . HIS A 1 15  ? 10.98300  -12.24900 0.59200   1.000 40.50000  ? 15  HIS A HD1  1 
ATOM   314  H  HD2  . HIS A 1 15  ? 10.04700  -13.50600 -2.97000  1.000 32.14000  ? 15  HIS A HD2  1 
ATOM   315  H  HE1  . HIS A 1 15  ? 10.15300  -10.36500 -0.56600  1.000 33.85000  ? 15  HIS A HE1  1 
ATOM   316  N  N    . GLY A 1 16  ? 13.79400  -17.09700 -0.28600  1.000 21.91000  ? 16  GLY A N    1 
ATOM   317  C  CA   . GLY A 1 16  ? 14.34200  -18.14700 0.55200   1.000 22.90000  ? 16  GLY A CA   1 
ATOM   318  C  C    . GLY A 1 16  ? 13.44100  -19.33600 0.81400   1.000 23.30000  ? 16  GLY A C    1 
ATOM   319  O  O    . GLY A 1 16  ? 13.67100  -20.06200 1.79400   1.000 24.95000  ? 16  GLY A O    1 
ATOM   320  H  H    . GLY A 1 16  ? 13.99900  -17.16000 -1.11900  1.000 26.28000  ? 16  GLY A H    1 
ATOM   321  H  HA2  . GLY A 1 16  ? 15.15000  -18.48200 0.13300   1.000 27.46000  ? 16  GLY A HA2  1 
ATOM   322  H  HA3  . GLY A 1 16  ? 14.57000  -17.76100 1.41300   1.000 27.46000  ? 16  GLY A HA3  1 
ATOM   323  N  N    . LEU A 1 17  ? 12.43400  -19.57500 -0.02700  1.000 21.07000  ? 17  LEU A N    1 
ATOM   324  C  CA   . LEU A 1 17  ? 11.58600  -20.74400 0.17000   1.000 20.84000  ? 17  LEU A CA   1 
ATOM   325  C  C    . LEU A 1 17  ? 12.15800  -22.02200 -0.41600  1.000 23.84000  ? 17  LEU A C    1 
ATOM   326  O  O    . LEU A 1 17  ? 11.71400  -23.11100 -0.03500  1.000 22.36000  ? 17  LEU A O    1 
ATOM   327  C  CB   . LEU A 1 17  ? 10.19600  -20.51400 -0.43400  1.000 24.38000  ? 17  LEU A CB   1 
ATOM   328  C  CG   . LEU A 1 17  ? 9.21400   -19.77300 0.44200   1.000 23.57000  ? 17  LEU A CG   1 
ATOM   329  C  CD1  . LEU A 1 17  ? 7.85400   -19.72700 -0.28200  1.000 22.24000  ? 17  LEU A CD1  1 
ATOM   330  C  CD2  . LEU A 1 17  ? 9.02800   -20.38100 1.82900   1.000 22.74000  ? 17  LEU A CD2  1 
ATOM   331  H  H    . LEU A 1 17  ? 12.22700  -19.08500 -0.70300  1.000 25.27000  ? 17  LEU A H    1 
ATOM   332  H  HA   . LEU A 1 17  ? 11.49200  -20.86900 1.12800   1.000 25.00000  ? 17  LEU A HA   1 
ATOM   333  H  HB2  . LEU A 1 17  ? 10.30200  -19.99900 -1.24900  1.000 29.25000  ? 17  LEU A HB2  1 
ATOM   334  H  HB3  . LEU A 1 17  ? 9.80700   -21.37900 -0.63600  1.000 29.25000  ? 17  LEU A HB3  1 
ATOM   335  H  HG   . LEU A 1 17  ? 9.57100   -18.88400 0.59300   1.000 28.27000  ? 17  LEU A HG   1 
ATOM   336  H  HD11 . LEU A 1 17  ? 7.21300   -19.26300 0.27900   1.000 26.68000  ? 17  LEU A HD11 1 
ATOM   337  H  HD12 . LEU A 1 17  ? 7.96000   -19.25600 -1.12300  1.000 26.68000  ? 17  LEU A HD12 1 
ATOM   338  H  HD13 . LEU A 1 17  ? 7.55300   -20.63400 -0.44700  1.000 26.68000  ? 17  LEU A HD13 1 
ATOM   339  H  HD21 . LEU A 1 17  ? 8.19200   -20.06200 2.20400   1.000 27.27000  ? 17  LEU A HD21 1 
ATOM   340  H  HD22 . LEU A 1 17  ? 9.00800   -21.34700 1.75000   1.000 27.27000  ? 17  LEU A HD22 1 
ATOM   341  H  HD23 . LEU A 1 17  ? 9.76900   -20.11000 2.39400   1.000 27.27000  ? 17  LEU A HD23 1 
ATOM   342  N  N    A ASP A 1 18  ? 13.10000  -21.94200 -1.35400  0.430 21.19000  ? 18  ASP A N    1 
ATOM   343  N  N    B ASP A 1 18  ? 13.15500  -21.93200 -1.29200  0.570 21.19000  ? 18  ASP A N    1 
ATOM   344  C  CA   A ASP A 1 18  ? 13.66600  -23.16500 -1.90500  0.430 22.57000  ? 18  ASP A CA   1 
ATOM   345  C  CA   B ASP A 1 18  ? 13.68300  -23.10700 -1.97600  0.570 22.84000  ? 18  ASP A CA   1 
ATOM   346  C  C    A ASP A 1 18  ? 14.33800  -23.94200 -0.78500  0.430 26.84000  ? 18  ASP A C    1 
ATOM   347  C  C    B ASP A 1 18  ? 14.42200  -23.98500 -0.97400  0.570 27.30000  ? 18  ASP A C    1 
ATOM   348  O  O    A ASP A 1 18  ? 15.26300  -23.44400 -0.12600  0.430 18.90000  ? 18  ASP A O    1 
ATOM   349  O  O    B ASP A 1 18  ? 15.56000  -23.70800 -0.58900  0.570 25.42000  ? 18  ASP A O    1 
ATOM   350  C  CB   A ASP A 1 18  ? 14.66100  -22.86300 -3.02600  0.430 23.24000  ? 18  ASP A CB   1 
ATOM   351  C  CB   B ASP A 1 18  ? 14.58700  -22.69200 -3.13300  0.570 23.02000  ? 18  ASP A CB   1 
ATOM   352  C  CG   A ASP A 1 18  ? 14.96600  -24.08600 -3.90200  0.430 26.28000  ? 18  ASP A CG   1 
ATOM   353  C  CG   B ASP A 1 18  ? 15.66600  -21.69000 -2.71800  0.570 28.78000  ? 18  ASP A CG   1 
ATOM   354  O  OD1  A ASP A 1 18  ? 14.41900  -25.18500 -3.66000  0.430 21.40000  ? 18  ASP A OD1  1 
ATOM   355  O  OD1  B ASP A 1 18  ? 15.33200  -20.66600 -2.07800  0.570 25.71000  ? 18  ASP A OD1  1 
ATOM   356  O  OD2  A ASP A 1 18  ? 15.77600  -23.95000 -4.84600  0.430 30.26000  ? 18  ASP A OD2  1 
ATOM   357  O  OD2  B ASP A 1 18  ? 16.84500  -21.93300 -3.04400  0.570 43.06000  ? 18  ASP A OD2  1 
ATOM   358  H  H    A ASP A 1 18  ? 13.41900  -21.21200 -1.67700  0.430 25.41000  ? 18  ASP A H    1 
ATOM   359  H  H    B ASP A 1 18  ? 13.54500  -21.19600 -1.50800  0.570 25.41000  ? 18  ASP A H    1 
ATOM   360  H  HA   A ASP A 1 18  ? 12.95800  -23.69900 -2.29700  0.430 27.07000  ? 18  ASP A HA   1 
ATOM   361  H  HA   B ASP A 1 18  ? 12.94600  -23.62200 -2.33900  0.570 27.39000  ? 18  ASP A HA   1 
ATOM   362  H  HB2  A ASP A 1 18  ? 14.29200  -22.17100 -3.59700  0.430 27.88000  ? 18  ASP A HB2  1 
ATOM   363  H  HB2  B ASP A 1 18  ? 15.03000  -23.47900 -3.48600  0.570 27.61000  ? 18  ASP A HB2  1 
ATOM   364  H  HB3  A ASP A 1 18  ? 15.49500  -22.56000 -2.63500  0.430 27.88000  ? 18  ASP A HB3  1 
ATOM   365  H  HB3  B ASP A 1 18  ? 14.04600  -22.27900 -3.82400  0.570 27.61000  ? 18  ASP A HB3  1 
ATOM   366  N  N    A ASN A 1 19  ? 13.83600  -25.15100 -0.56100  0.570 21.43000  ? 19  ASN A N    1 
ATOM   367  N  N    B ASN A 1 19  ? 13.76600  -25.06300 -0.55500  0.430 21.22000  ? 19  ASN A N    1 
ATOM   368  C  CA   A ASN A 1 19  ? 14.31500  -26.07900 0.45800   0.570 19.34000  ? 19  ASN A CA   1 
ATOM   369  C  CA   B ASN A 1 19  ? 14.27500  -26.03800 0.40500   0.430 19.57000  ? 19  ASN A CA   1 
ATOM   370  C  C    A ASN A 1 19  ? 14.20800  -25.52300 1.87100   0.570 20.16000  ? 19  ASN A C    1 
ATOM   371  C  C    B ASN A 1 19  ? 14.12800  -25.58800 1.85100   0.430 20.20000  ? 19  ASN A C    1 
ATOM   372  O  O    A ASN A 1 19  ? 14.90200  -25.98100 2.78100   0.570 24.28000  ? 19  ASN A O    1 
ATOM   373  O  O    B ASN A 1 19  ? 14.72600  -26.18100 2.75300   0.430 20.89000  ? 19  ASN A O    1 
ATOM   374  C  CB   A ASN A 1 19  ? 15.70100  -26.63400 0.12900   0.570 23.17000  ? 19  ASN A CB   1 
ATOM   375  C  CB   B ASN A 1 19  ? 15.70800  -26.49800 0.12900   0.430 22.58000  ? 19  ASN A CB   1 
ATOM   376  C  CG   A ASN A 1 19  ? 15.61500  -27.78100 -0.85400  0.570 23.13000  ? 19  ASN A CG   1 
ATOM   377  C  CG   B ASN A 1 19  ? 15.87500  -27.97900 0.36700   0.430 24.67000  ? 19  ASN A CG   1 
ATOM   378  O  OD1  A ASN A 1 19  ? 14.88600  -28.74200 -0.61600  0.570 32.10000  ? 19  ASN A OD1  1 
ATOM   379  O  OD1  B ASN A 1 19  ? 14.89700  -28.73000 0.32400   0.430 26.02000  ? 19  ASN A OD1  1 
ATOM   380  N  ND2  A ASN A 1 19  ? 16.31700  -27.67200 -1.97400  0.570 39.08000  ? 19  ASN A ND2  1 
ATOM   381  N  ND2  B ASN A 1 19  ? 17.10300  -28.41300 0.61600   0.430 39.42000  ? 19  ASN A ND2  1 
ATOM   382  H  H    A ASN A 1 19  ? 13.17900  -25.47600 -1.01300  0.570 25.70000  ? 19  ASN A H    1 
ATOM   383  H  H    B ASN A 1 19  ? 12.97600  -25.26100 -0.83100  0.430 25.45000  ? 19  ASN A H    1 
ATOM   384  H  HA   A ASN A 1 19  ? 13.72900  -26.85200 0.45800   0.570 23.19000  ? 19  ASN A HA   1 
ATOM   385  H  HA   B ASN A 1 19  ? 13.72500  -26.83000 0.29900   0.430 23.47000  ? 19  ASN A HA   1 
ATOM   386  H  HB2  A ASN A 1 19  ? 16.24200  -25.93300 -0.26600  0.570 27.79000  ? 19  ASN A HB2  1 
ATOM   387  H  HB2  B ASN A 1 19  ? 15.93100  -26.31100 -0.79700  0.430 27.08000  ? 19  ASN A HB2  1 
ATOM   388  H  HB3  A ASN A 1 19  ? 16.11900  -26.95800 0.94200   0.570 27.79000  ? 19  ASN A HB3  1 
ATOM   389  H  HB3  B ASN A 1 19  ? 16.31500  -26.02400 0.71800   0.430 27.08000  ? 19  ASN A HB3  1 
ATOM   390  H  HD21 A ASN A 1 19  ? 16.29500  -28.30300 -2.55900  0.570 46.89000  ? 19  ASN A HD21 1 
ATOM   391  H  HD21 B ASN A 1 19  ? 17.24300  -29.25000 0.75800   0.430 47.30000  ? 19  ASN A HD21 1 
ATOM   392  H  HD22 A ASN A 1 19  ? 16.79400  -26.97100 -2.11600  0.570 46.89000  ? 19  ASN A HD22 1 
ATOM   393  H  HD22 B ASN A 1 19  ? 17.75900  -27.85800 0.63700   0.430 47.30000  ? 19  ASN A HD22 1 
ATOM   394  N  N    . TYR A 1 20  ? 13.30000  -24.58800 2.09600   1.000 18.17000  ? 20  TYR A N    1 
ATOM   395  C  CA   . TYR A 1 20  ? 12.99800  -24.16200 3.44500   1.000 16.65000  ? 20  TYR A CA   1 
ATOM   396  C  C    . TYR A 1 20  ? 12.33300  -25.30700 4.20500   1.000 19.44000  ? 20  TYR A C    1 
ATOM   397  O  O    . TYR A 1 20  ? 11.29800  -25.84600 3.77400   1.000 18.06000  ? 20  TYR A O    1 
ATOM   398  C  CB   . TYR A 1 20  ? 12.07500  -22.94900 3.39200   1.000 19.45000  ? 20  TYR A CB   1 
ATOM   399  C  CG   . TYR A 1 20  ? 11.94800  -22.28300 4.73500   1.000 19.43000  ? 20  TYR A CG   1 
ATOM   400  C  CD1  . TYR A 1 20  ? 12.90400  -21.38100 5.16600   1.000 24.38000  ? 20  TYR A CD1  1 
ATOM   401  C  CD2  . TYR A 1 20  ? 10.90900  -22.57200 5.58300   1.000 20.22000  ? 20  TYR A CD2  1 
ATOM   402  C  CE1  . TYR A 1 20  ? 12.82200  -20.79800 6.39400   1.000 24.11000  ? 20  TYR A CE1  1 
ATOM   403  C  CE2  . TYR A 1 20  ? 10.82300  -21.98400 6.82200   1.000 21.80000  ? 20  TYR A CE2  1 
ATOM   404  C  CZ   . TYR A 1 20  ? 11.78200  -21.10600 7.22100   1.000 23.85000  ? 20  TYR A CZ   1 
ATOM   405  O  OH   . TYR A 1 20  ? 11.69600  -20.51500 8.45200   1.000 28.51000  ? 20  TYR A OH   1 
ATOM   406  H  H    . TYR A 1 20  ? 12.84900  -24.18800 1.48300   1.000 21.80000  ? 20  TYR A H    1 
ATOM   407  H  HA   . TYR A 1 20  ? 13.81200  -23.91400 3.91100   1.000 19.97000  ? 20  TYR A HA   1 
ATOM   408  H  HB2  . TYR A 1 20  ? 12.43300  -22.30200 2.76400   1.000 23.33000  ? 20  TYR A HB2  1 
ATOM   409  H  HB3  . TYR A 1 20  ? 11.19200  -23.23300 3.10800   1.000 23.33000  ? 20  TYR A HB3  1 
ATOM   410  H  HD1  . TYR A 1 20  ? 13.61600  -21.16800 4.60600   1.000 29.25000  ? 20  TYR A HD1  1 
ATOM   411  H  HD2  . TYR A 1 20  ? 10.25300  -23.17400 5.31600   1.000 24.26000  ? 20  TYR A HD2  1 
ATOM   412  H  HE1  . TYR A 1 20  ? 13.47300  -20.19200 6.66800   1.000 28.92000  ? 20  TYR A HE1  1 
ATOM   413  H  HE2  . TYR A 1 20  ? 10.11200  -22.18700 7.38600   1.000 26.14000  ? 20  TYR A HE2  1 
ATOM   414  H  HH   . TYR A 1 20  ? 11.18900  -20.96100 8.95100   1.000 34.19000  ? 20  TYR A HH   1 
ATOM   415  N  N    A ARG A 1 21  ? 12.92000  -25.67700 5.34500   0.460 19.34000  ? 21  ARG A N    1 
ATOM   416  N  N    B ARG A 1 21  ? 12.93900  -25.67800 5.33600   0.540 19.30000  ? 21  ARG A N    1 
ATOM   417  C  CA   A ARG A 1 21  ? 12.47500  -26.84900 6.10500   0.460 21.32000  ? 21  ARG A CA   1 
ATOM   418  C  CA   B ARG A 1 21  ? 12.51100  -26.84400 6.11100   0.540 21.24000  ? 21  ARG A CA   1 
ATOM   419  C  C    A ARG A 1 21  ? 12.46000  -28.10400 5.23700   0.460 19.09000  ? 21  ARG A C    1 
ATOM   420  C  C    B ARG A 1 21  ? 12.46700  -28.09700 5.24300   0.540 19.07000  ? 21  ARG A C    1 
ATOM   421  O  O    A ARG A 1 21  ? 11.70800  -29.04800 5.49000   0.460 20.50000  ? 21  ARG A O    1 
ATOM   422  O  O    B ARG A 1 21  ? 11.70300  -29.02900 5.50300   0.540 20.52000  ? 21  ARG A O    1 
ATOM   423  C  CB   A ARG A 1 21  ? 11.11000  -26.60800 6.75500   0.460 20.24000  ? 21  ARG A CB   1 
ATOM   424  C  CB   B ARG A 1 21  ? 11.16800  -26.58400 6.79600   0.540 20.21000  ? 21  ARG A CB   1 
ATOM   425  C  CG   A ARG A 1 21  ? 11.16400  -25.66800 7.94900   0.460 28.13000  ? 21  ARG A CG   1 
ATOM   426  C  CG   B ARG A 1 21  ? 11.17500  -25.33500 7.67200   0.540 29.07000  ? 21  ARG A CG   1 
ATOM   427  C  CD   A ARG A 1 21  ? 11.69600  -26.37300 9.18100   0.460 41.70000  ? 21  ARG A CD   1 
ATOM   428  C  CD   B ARG A 1 21  ? 11.69400  -25.61600 9.06400   0.540 41.45000  ? 21  ARG A CD   1 
ATOM   429  N  NE   A ARG A 1 21  ? 11.45000  -25.60400 10.39500  0.460 42.08000  ? 21  ARG A NE   1 
ATOM   430  N  NE   B ARG A 1 21  ? 11.93000  -24.38400 9.81000   0.540 32.78000  ? 21  ARG A NE   1 
ATOM   431  C  CZ   A ARG A 1 21  ? 11.94700  -25.90800 11.58500  0.460 33.39000  ? 21  ARG A CZ   1 
ATOM   432  C  CZ   B ARG A 1 21  ? 13.12100  -23.83600 10.02500  0.540 36.72000  ? 21  ARG A CZ   1 
ATOM   433  N  NH1  A ARG A 1 21  ? 12.72500  -26.96400 11.76000  0.460 50.37000  ? 21  ARG A NH1  1 
ATOM   434  N  NH1  B ARG A 1 21  ? 14.23300  -24.38100 9.55900   0.540 50.48000  ? 21  ARG A NH1  1 
ATOM   435  N  NH2  A ARG A 1 21  ? 11.65800  -25.13200 12.62600  0.460 40.73000  ? 21  ARG A NH2  1 
ATOM   436  N  NH2  B ARG A 1 21  ? 13.19700  -22.71500 10.73600  0.540 42.35000  ? 21  ARG A NH2  1 
ATOM   437  H  H    A ARG A 1 21  ? 13.58400  -25.26300 5.70300   0.460 23.20000  ? 21  ARG A H    1 
ATOM   438  H  H    B ARG A 1 21  ? 13.60900  -25.26300 5.68000   0.540 23.15000  ? 21  ARG A H    1 
ATOM   439  H  HA   A ARG A 1 21  ? 13.11200  -27.00600 6.82000   0.460 25.57000  ? 21  ARG A HA   1 
ATOM   440  H  HA   B ARG A 1 21  ? 13.16300  -27.01000 6.81000   0.540 25.48000  ? 21  ARG A HA   1 
ATOM   441  H  HB2  A ARG A 1 21  ? 10.51400  -26.21700 6.09600   0.460 24.28000  ? 21  ARG A HB2  1 
ATOM   442  H  HB2  B ARG A 1 21  ? 10.48600  -26.46800 6.11700   0.540 24.24000  ? 21  ARG A HB2  1 
ATOM   443  H  HB3  A ARG A 1 21  ? 10.75400  -27.45700 7.06100   0.460 24.28000  ? 21  ARG A HB3  1 
ATOM   444  H  HB3  B ARG A 1 21  ? 10.95000  -27.34300 7.35900   0.540 24.24000  ? 21  ARG A HB3  1 
ATOM   445  H  HG2  A ARG A 1 21  ? 11.75100  -24.92300 7.74600   0.460 33.74000  ? 21  ARG A HG2  1 
ATOM   446  H  HG2  B ARG A 1 21  ? 11.74700  -24.66500 7.26700   0.540 34.87000  ? 21  ARG A HG2  1 
ATOM   447  H  HG3  A ARG A 1 21  ? 10.27100  -25.34300 8.14400   0.460 33.74000  ? 21  ARG A HG3  1 
ATOM   448  H  HG3  B ARG A 1 21  ? 10.27000  -24.99600 7.75000   0.540 34.87000  ? 21  ARG A HG3  1 
ATOM   449  H  HD2  A ARG A 1 21  ? 11.25700  -27.23300 9.27200   0.460 50.03000  ? 21  ARG A HD2  1 
ATOM   450  H  HD2  B ARG A 1 21  ? 11.04100  -26.14400 9.54900   0.540 49.73000  ? 21  ARG A HD2  1 
ATOM   451  H  HD3  A ARG A 1 21  ? 12.65400  -26.49700 9.08900   0.460 50.03000  ? 21  ARG A HD3  1 
ATOM   452  H  HD3  B ARG A 1 21  ? 12.53200  -26.10000 9.00200   0.540 49.73000  ? 21  ARG A HD3  1 
ATOM   453  H  HE   A ARG A 1 21  ? 10.94900  -24.90800 10.33500  0.460 50.49000  ? 21  ARG A HE   1 
ATOM   454  H  HE   B ARG A 1 21  ? 11.24400  -23.98000 10.13600  0.540 39.32000  ? 21  ARG A HE   1 
ATOM   455  H  HH11 A ARG A 1 21  ? 12.91900  -27.47000 11.09300  0.460 60.43000  ? 21  ARG A HH11 1 
ATOM   456  H  HH11 B ARG A 1 21  ? 14.19700  -25.10900 9.10300   0.540 60.56000  ? 21  ARG A HH11 1 
ATOM   457  H  HH12 A ARG A 1 21  ? 13.03800  -27.14300 12.54100  0.460 60.43000  ? 21  ARG A HH12 1 
ATOM   458  H  HH12 B ARG A 1 21  ? 14.99200  -24.00700 9.71200   0.540 60.56000  ? 21  ARG A HH12 1 
ATOM   459  H  HH21 A ARG A 1 21  ? 11.15400  -24.44300 12.52200  0.460 48.86000  ? 21  ARG A HH21 1 
ATOM   460  H  HH21 B ARG A 1 21  ? 12.48200  -22.35500 11.04900  0.540 50.81000  ? 21  ARG A HH21 1 
ATOM   461  H  HH22 A ARG A 1 21  ? 11.97500  -25.31900 13.40400  0.460 48.86000  ? 21  ARG A HH22 1 
ATOM   462  H  HH22 B ARG A 1 21  ? 13.96200  -22.35100 10.88300  0.540 50.81000  ? 21  ARG A HH22 1 
ATOM   463  N  N    . GLY A 1 22  ? 13.29700  -28.12700 4.20800   1.000 18.07000  ? 22  GLY A N    1 
ATOM   464  C  CA   . GLY A 1 22  ? 13.43000  -29.27900 3.35900   1.000 20.13000  ? 22  GLY A CA   1 
ATOM   465  C  C    . GLY A 1 22  ? 12.41900  -29.40700 2.24500   1.000 18.67000  ? 22  GLY A C    1 
ATOM   466  O  O    . GLY A 1 22  ? 12.37900  -30.44800 1.58800   1.000 20.21000  ? 22  GLY A O    1 
ATOM   467  H  H    . GLY A 1 22  ? 13.80400  -27.47000 3.97800   1.000 21.68000  ? 22  GLY A H    1 
ATOM   468  H  HA2  . GLY A 1 22  ? 14.31000  -29.25700 2.95100   1.000 24.14000  ? 22  GLY A HA2  1 
ATOM   469  H  HA3  . GLY A 1 22  ? 13.35600  -30.07400 3.91000   1.000 24.14000  ? 22  GLY A HA3  1 
ATOM   470  N  N    . TYR A 1 23  ? 11.58900  -28.39500 2.01100   1.000 15.32000  ? 23  TYR A N    1 
ATOM   471  C  CA   . TYR A 1 23  ? 10.60400  -28.44000 0.94200   1.000 14.59000  ? 23  TYR A CA   1 
ATOM   472  C  C    . TYR A 1 23  ? 11.17500  -27.73500 -0.27700  1.000 14.34000  ? 23  TYR A C    1 
ATOM   473  O  O    . TYR A 1 23  ? 11.25300  -26.50700 -0.31500  1.000 16.89000  ? 23  TYR A O    1 
ATOM   474  C  CB   . TYR A 1 23  ? 9.29800   -27.79500 1.39500   1.000 14.90000  ? 23  TYR A CB   1 
ATOM   475  C  CG   . TYR A 1 23  ? 8.60200   -28.61700 2.43600   1.000 13.78000  ? 23  TYR A CG   1 
ATOM   476  C  CD1  . TYR A 1 23  ? 7.73700   -29.64900 2.08400   1.000 16.22000  ? 23  TYR A CD1  1 
ATOM   477  C  CD2  . TYR A 1 23  ? 8.82400   -28.38400 3.77900   1.000 14.53000  ? 23  TYR A CD2  1 
ATOM   478  C  CE1  . TYR A 1 23  ? 7.10000   -30.42600 3.06500   1.000 15.10000  ? 23  TYR A CE1  1 
ATOM   479  C  CE2  . TYR A 1 23  ? 8.19600   -29.14900 4.76600   1.000 13.88000  ? 23  TYR A CE2  1 
ATOM   480  C  CZ   . TYR A 1 23  ? 7.34000   -30.17000 4.39000   1.000 13.58000  ? 23  TYR A CZ   1 
ATOM   481  O  OH   . TYR A 1 23  ? 6.67200   -30.95000 5.32400   1.000 16.18000  ? 23  TYR A OH   1 
ATOM   482  H  H    . TYR A 1 23  ? 11.58000  -27.66400 2.46400   1.000 18.38000  ? 23  TYR A H    1 
ATOM   483  H  HA   . TYR A 1 23  ? 10.42700  -29.36200 0.70100   1.000 17.49000  ? 23  TYR A HA   1 
ATOM   484  H  HB2  . TYR A 1 23  ? 9.48700   -26.92200 1.77400   1.000 17.87000  ? 23  TYR A HB2  1 
ATOM   485  H  HB3  . TYR A 1 23  ? 8.70500   -27.70400 0.63300   1.000 17.87000  ? 23  TYR A HB3  1 
ATOM   486  H  HD1  . TYR A 1 23  ? 7.57900   -29.82600 1.18500   1.000 19.45000  ? 23  TYR A HD1  1 
ATOM   487  H  HD2  . TYR A 1 23  ? 9.40400   -27.70400 4.03200   1.000 17.43000  ? 23  TYR A HD2  1 
ATOM   488  H  HE1  . TYR A 1 23  ? 6.52000   -31.10900 2.81700   1.000 18.10000  ? 23  TYR A HE1  1 
ATOM   489  H  HE2  . TYR A 1 23  ? 8.35100   -28.97300 5.66600   1.000 16.64000  ? 23  TYR A HE2  1 
ATOM   490  H  HH   . TYR A 1 23  ? 6.99600   -30.82200 6.08900   1.000 19.40000  ? 23  TYR A HH   1 
ATOM   491  N  N    . SER A 1 24  ? 11.50400  -28.51800 -1.29600  1.000 14.55000  ? 24  SER A N    1 
ATOM   492  C  CA   . SER A 1 24  ? 12.05800  -27.95400 -2.52300  1.000 16.92000  ? 24  SER A CA   1 
ATOM   493  C  C    . SER A 1 24  ? 11.03700  -27.03300 -3.17900  1.000 17.10000  ? 24  SER A C    1 
ATOM   494  O  O    . SER A 1 24  ? 9.83100   -27.12100 -2.93400  1.000 16.45000  ? 24  SER A O    1 
ATOM   495  C  CB   . SER A 1 24  ? 12.45300  -29.05900 -3.49400  1.000 19.71000  ? 24  SER A CB   1 
ATOM   496  O  OG   . SER A 1 24  ? 11.32500  -29.69900 -4.03700  1.000 23.10000  ? 24  SER A OG   1 
ATOM   497  H  H    . SER A 1 24  ? 11.41900  -29.37400 -1.30400  1.000 17.45000  ? 24  SER A H    1 
ATOM   498  H  HA   . SER A 1 24  ? 12.85400  -27.44200 -2.31400  1.000 20.29000  ? 24  SER A HA   1 
ATOM   499  H  HB2  . SER A 1 24  ? 12.97000  -28.67000 -4.21700  1.000 23.64000  ? 24  SER A HB2  1 
ATOM   500  H  HB3  . SER A 1 24  ? 12.98700  -29.71600 -3.02000  1.000 23.64000  ? 24  SER A HB3  1 
ATOM   501  H  HG   . SER A 1 24  ? 10.88700  -30.07700 -3.42800  1.000 27.71000  ? 24  SER A HG   1 
ATOM   502  N  N    . LEU A 1 25  ? 11.54200  -26.12900 -4.02200  1.000 14.26000  ? 25  LEU A N    1 
ATOM   503  C  CA   . LEU A 1 25  ? 10.73000  -25.05200 -4.57400  1.000 15.69000  ? 25  LEU A CA   1 
ATOM   504  C  C    . LEU A 1 25  ? 9.47300   -25.54600 -5.27900  1.000 16.61000  ? 25  LEU A C    1 
ATOM   505  O  O    . LEU A 1 25  ? 8.42200   -24.88800 -5.20200  1.000 14.63000  ? 25  LEU A O    1 
ATOM   506  C  CB   . LEU A 1 25  ? 11.60200  -24.26800 -5.54000  1.000 17.92000  ? 25  LEU A CB   1 
ATOM   507  C  CG   . LEU A 1 25  ? 11.05800  -22.97400 -6.08100  1.000 17.95000  ? 25  LEU A CG   1 
ATOM   508  C  CD1  . LEU A 1 25  ? 10.68400  -22.00400 -4.96800  1.000 21.55000  ? 25  LEU A CD1  1 
ATOM   509  C  CD2  . LEU A 1 25  ? 12.13700  -22.35800 -6.98000  1.000 18.19000  ? 25  LEU A CD2  1 
ATOM   510  H  H    . LEU A 1 25  ? 12.35900  -26.11900 -4.29100  1.000 17.10000  ? 25  LEU A H    1 
ATOM   511  H  HA   . LEU A 1 25  ? 10.42400  -24.48300 -3.85000  1.000 18.82000  ? 25  LEU A HA   1 
ATOM   512  H  HB2  . LEU A 1 25  ? 12.43000  -24.05500 -5.08400  1.000 21.49000  ? 25  LEU A HB2  1 
ATOM   513  H  HB3  . LEU A 1 25  ? 11.78100  -24.83700 -6.30500  1.000 21.49000  ? 25  LEU A HB3  1 
ATOM   514  H  HG   . LEU A 1 25  ? 10.24500  -23.14100 -6.58300  1.000 21.52000  ? 25  LEU A HG   1 
ATOM   515  H  HD11 . LEU A 1 25  ? 10.49800  -21.13500 -5.35600  1.000 25.84000  ? 25  LEU A HD11 1 
ATOM   516  H  HD12 . LEU A 1 25  ? 9.89600   -22.33800 -4.51000  1.000 25.84000  ? 25  LEU A HD12 1 
ATOM   517  H  HD13 . LEU A 1 25  ? 11.42500  -21.93700 -4.34500  1.000 25.84000  ? 25  LEU A HD13 1 
ATOM   518  H  HD21 . LEU A 1 25  ? 11.79900  -21.53000 -7.35700  1.000 21.81000  ? 25  LEU A HD21 1 
ATOM   519  H  HD22 . LEU A 1 25  ? 12.92800  -22.18000 -6.44800  1.000 21.81000  ? 25  LEU A HD22 1 
ATOM   520  H  HD23 . LEU A 1 25  ? 12.35000  -22.98200 -7.69100  1.000 21.81000  ? 25  LEU A HD23 1 
ATOM   521  N  N    . GLY A 1 26  ? 9.54200   -26.67200 -5.98400  1.000 15.71000  ? 26  GLY A N    1 
ATOM   522  C  CA   . GLY A 1 26  ? 8.37100   -27.18300 -6.67400  1.000 13.41000  ? 26  GLY A CA   1 
ATOM   523  C  C    . GLY A 1 26  ? 7.18600   -27.43400 -5.75900  1.000 15.72000  ? 26  GLY A C    1 
ATOM   524  O  O    . GLY A 1 26  ? 6.03100   -27.30900 -6.18000  1.000 14.80000  ? 26  GLY A O    1 
ATOM   525  H  H    . GLY A 1 26  ? 10.25000  -27.15200 -6.07700  1.000 18.84000  ? 26  GLY A H    1 
ATOM   526  H  HA2  . GLY A 1 26  ? 8.09800   -26.54300 -7.35000  1.000 16.08000  ? 26  GLY A HA2  1 
ATOM   527  H  HA3  . GLY A 1 26  ? 8.60000   -28.02100 -7.10500  1.000 16.08000  ? 26  GLY A HA3  1 
ATOM   528  N  N    . ASN A 1 27  ? 7.44300   -27.78300 -4.49500  1.000 13.18000  ? 27  ASN A N    1 
ATOM   529  C  CA   . ASN A 1 27  ? 6.33000   -27.95200 -3.54900  1.000 12.32000  ? 27  ASN A CA   1 
ATOM   530  C  C    . ASN A 1 27  ? 5.54000   -26.66100 -3.37400  1.000 12.97000  ? 27  ASN A C    1 
ATOM   531  O  O    . ASN A 1 27  ? 4.31000   -26.69000 -3.30600  1.000 14.13000  ? 27  ASN A O    1 
ATOM   532  C  CB   . ASN A 1 27  ? 6.85400   -28.34600 -2.18100  1.000 12.49000  ? 27  ASN A CB   1 
ATOM   533  C  CG   . ASN A 1 27  ? 7.31400   -29.76000 -2.13500  1.000 15.37000  ? 27  ASN A CG   1 
ATOM   534  O  OD1  . ASN A 1 27  ? 6.51200   -30.68400 -2.15000  1.000 14.80000  ? 27  ASN A OD1  1 
ATOM   535  N  ND2  . ASN A 1 27  ? 8.63300   -29.94200 -2.13300  1.000 16.25000  ? 27  ASN A ND2  1 
ATOM   536  H  H    . ASN A 1 27  ? 8.22600   -27.92400 -4.16700  1.000 15.81000  ? 27  ASN A H    1 
ATOM   537  H  HA   . ASN A 1 27  ? 5.75700   -28.64900 -3.90300  1.000 14.77000  ? 27  ASN A HA   1 
ATOM   538  H  HB2  . ASN A 1 27  ? 7.60500   -27.77600 -1.95300  1.000 14.97000  ? 27  ASN A HB2  1 
ATOM   539  H  HB3  . ASN A 1 27  ? 6.14600   -28.23800 -1.52700  1.000 14.97000  ? 27  ASN A HB3  1 
ATOM   540  H  HD21 . ASN A 1 27  ? 8.95700   -30.73900 -2.10700  1.000 19.49000  ? 27  ASN A HD21 1 
ATOM   541  H  HD22 . ASN A 1 27  ? 9.16100   -29.26400 -2.15800  1.000 19.49000  ? 27  ASN A HD22 1 
ATOM   542  N  N    . TRP A 1 28  ? 6.24600   -25.53200 -3.25700  1.000 13.79000  ? 28  TRP A N    1 
ATOM   543  C  CA   . TRP A 1 28  ? 5.60700   -24.24600 -3.02600  1.000 13.57000  ? 28  TRP A CA   1 
ATOM   544  C  C    . TRP A 1 28  ? 4.85000   -23.77800 -4.26100  1.000 15.17000  ? 28  TRP A C    1 
ATOM   545  O  O    . TRP A 1 28  ? 3.78700   -23.17500 -4.13900  1.000 15.18000  ? 28  TRP A O    1 
ATOM   546  C  CB   . TRP A 1 28  ? 6.66800   -23.22200 -2.62200  1.000 13.70000  ? 28  TRP A CB   1 
ATOM   547  C  CG   . TRP A 1 28  ? 7.34700   -23.59400 -1.32500  1.000 13.99000  ? 28  TRP A CG   1 
ATOM   548  C  CD1  . TRP A 1 28  ? 8.56400   -24.18200 -1.18200  1.000 16.07000  ? 28  TRP A CD1  1 
ATOM   549  C  CD2  . TRP A 1 28  ? 6.81200   -23.45400 -0.00900  1.000 14.19000  ? 28  TRP A CD2  1 
ATOM   550  N  NE1  . TRP A 1 28  ? 8.83100   -24.40800 0.14200   1.000 14.86000  ? 28  TRP A NE1  1 
ATOM   551  C  CE2  . TRP A 1 28  ? 7.76900   -23.96300 0.88700   1.000 17.30000  ? 28  TRP A CE2  1 
ATOM   552  C  CE3  . TRP A 1 28  ? 5.61800   -22.94400 0.50400   1.000 16.04000  ? 28  TRP A CE3  1 
ATOM   553  C  CZ2  . TRP A 1 28  ? 7.57400   -23.95200 2.27100   1.000 19.95000  ? 28  TRP A CZ2  1 
ATOM   554  C  CZ3  . TRP A 1 28  ? 5.43700   -22.93400 1.87200   1.000 18.62000  ? 28  TRP A CZ3  1 
ATOM   555  C  CH2  . TRP A 1 28  ? 6.40300   -23.44600 2.73300   1.000 20.67000  ? 28  TRP A CH2  1 
ATOM   556  H  H    . TRP A 1 28  ? 7.10300   -25.48800 -3.30900  1.000 16.54000  ? 28  TRP A H    1 
ATOM   557  H  HA   . TRP A 1 28  ? 4.96800   -24.33000 -2.30100  1.000 16.27000  ? 28  TRP A HA   1 
ATOM   558  H  HB2  . TRP A 1 28  ? 7.34500   -23.17300 -3.31500  1.000 16.43000  ? 28  TRP A HB2  1 
ATOM   559  H  HB3  . TRP A 1 28  ? 6.24800   -22.35600 -2.50700  1.000 16.43000  ? 28  TRP A HB3  1 
ATOM   560  H  HD1  . TRP A 1 28  ? 9.13400   -24.39900 -1.88300  1.000 19.28000  ? 28  TRP A HD1  1 
ATOM   561  H  HE1  . TRP A 1 28  ? 9.54600   -24.77000 0.45400   1.000 17.82000  ? 28  TRP A HE1  1 
ATOM   562  H  HE3  . TRP A 1 28  ? 4.95900   -22.61700 -0.06500  1.000 19.23000  ? 28  TRP A HE3  1 
ATOM   563  H  HZ2  . TRP A 1 28  ? 8.22200   -24.27900 2.85300   1.000 23.93000  ? 28  TRP A HZ2  1 
ATOM   564  H  HZ3  . TRP A 1 28  ? 4.65400   -22.57800 2.22600   1.000 22.34000  ? 28  TRP A HZ3  1 
ATOM   565  H  HH2  . TRP A 1 28  ? 6.24200   -23.44200 3.64900   1.000 24.80000  ? 28  TRP A HH2  1 
ATOM   566  N  N    . VAL A 1 29  ? 5.40500   -24.01600 -5.45000  1.000 13.84000  ? 29  VAL A N    1 
ATOM   567  C  CA   . VAL A 1 29  ? 4.72800   -23.62800 -6.68800  1.000 13.79000  ? 29  VAL A CA   1 
ATOM   568  C  C    . VAL A 1 29  ? 3.48300   -24.47800 -6.89800  1.000 13.22000  ? 29  VAL A C    1 
ATOM   569  O  O    . VAL A 1 29  ? 2.41700   -23.96700 -7.27800  1.000 14.10000  ? 29  VAL A O    1 
ATOM   570  C  CB   . VAL A 1 29  ? 5.71600   -23.73400 -7.86600  1.000 15.22000  ? 29  VAL A CB   1 
ATOM   571  C  CG1  . VAL A 1 29  ? 5.00200   -23.41400 -9.16900  1.000 15.94000  ? 29  VAL A CG1  1 
ATOM   572  C  CG2  . VAL A 1 29  ? 6.88100   -22.81400 -7.64200  1.000 18.61000  ? 29  VAL A CG2  1 
ATOM   573  H  H    . VAL A 1 29  ? 6.16600   -24.39800 -5.56700  1.000 16.60000  ? 29  VAL A H    1 
ATOM   574  H  HA   . VAL A 1 29  ? 4.43800   -22.70500 -6.62200  1.000 16.53000  ? 29  VAL A HA   1 
ATOM   575  H  HB   . VAL A 1 29  ? 6.06000   -24.63900 -7.92800  1.000 18.25000  ? 29  VAL A HB   1 
ATOM   576  H  HG11 . VAL A 1 29  ? 5.64800   -23.42200 -9.89300  1.000 19.12000  ? 29  VAL A HG11 1 
ATOM   577  H  HG12 . VAL A 1 29  ? 4.31900   -24.08400 -9.32800  1.000 19.12000  ? 29  VAL A HG12 1 
ATOM   578  H  HG13 . VAL A 1 29  ? 4.59500   -22.53600 -9.09900  1.000 19.12000  ? 29  VAL A HG13 1 
ATOM   579  H  HG21 . VAL A 1 29  ? 7.44900   -22.82600 -8.42800  1.000 22.33000  ? 29  VAL A HG21 1 
ATOM   580  H  HG22 . VAL A 1 29  ? 6.54900   -21.91500 -7.48800  1.000 22.33000  ? 29  VAL A HG22 1 
ATOM   581  H  HG23 . VAL A 1 29  ? 7.38000   -23.11900 -6.86800  1.000 22.33000  ? 29  VAL A HG23 1 
ATOM   582  N  N    . CYS A 1 30  ? 3.59300   -25.79000 -6.66300  1.000 13.53000  ? 30  CYS A N    1 
ATOM   583  C  CA   . CYS A 1 30  ? 2.44700   -26.67400 -6.75900  1.000 13.81000  ? 30  CYS A CA   1 
ATOM   584  C  C    . CYS A 1 30  ? 1.36000   -26.24300 -5.77800  1.000 14.65000  ? 30  CYS A C    1 
ATOM   585  O  O    . CYS A 1 30  ? 0.17700   -26.17200 -6.14400  1.000 14.17000  ? 30  CYS A O    1 
ATOM   586  C  CB   . CYS A 1 30  ? 2.91800   -28.10200 -6.44900  1.000 13.23000  ? 30  CYS A CB   1 
ATOM   587  S  SG   . CYS A 1 30  ? 1.63900   -29.37700 -6.63600  1.000 15.76000  ? 30  CYS A SG   1 
ATOM   588  H  H    . CYS A 1 30  ? 4.32500   -26.18700 -6.44700  1.000 16.23000  ? 30  CYS A H    1 
ATOM   589  H  HA   . CYS A 1 30  ? 2.07100   -26.65100 -7.65300  1.000 16.57000  ? 30  CYS A HA   1 
ATOM   590  H  HB2  . CYS A 1 30  ? 3.64400   -28.32500 -7.05300  1.000 15.86000  ? 30  CYS A HB2  1 
ATOM   591  H  HB3  . CYS A 1 30  ? 3.22900   -28.13200 -5.53100  1.000 15.86000  ? 30  CYS A HB3  1 
ATOM   592  N  N    . ALA A 1 31  ? 1.73300   -25.92500 -4.53800  1.000 13.38000  ? 31  ALA A N    1 
ATOM   593  C  CA   . ALA A 1 31  ? 0.71700   -25.50300 -3.58400  1.000 14.21000  ? 31  ALA A CA   1 
ATOM   594  C  C    . ALA A 1 31  ? 0.03700   -24.23000 -4.06700  1.000 13.22000  ? 31  ALA A C    1 
ATOM   595  O  O    . ALA A 1 31  ? -1.19400  -24.12200 -4.02900  1.000 15.00000  ? 31  ALA A O    1 
ATOM   596  C  CB   . ALA A 1 31  ? 1.34300   -25.29900 -2.21100  1.000 17.56000  ? 31  ALA A CB   1 
ATOM   597  H  H    . ALA A 1 31  ? 2.53800   -25.94500 -4.23700  1.000 16.04000  ? 31  ALA A H    1 
ATOM   598  H  HA   . ALA A 1 31  ? 0.04500   -26.19800 -3.50000  1.000 17.04000  ? 31  ALA A HA   1 
ATOM   599  H  HB1  . ALA A 1 31  ? 0.64100   -25.10400 -1.57000  1.000 21.06000  ? 31  ALA A HB1  1 
ATOM   600  H  HB2  . ALA A 1 31  ? 1.81100   -26.10900 -1.95300  1.000 21.06000  ? 31  ALA A HB2  1 
ATOM   601  H  HB3  . ALA A 1 31  ? 1.96600   -24.55700 -2.25500  1.000 21.06000  ? 31  ALA A HB3  1 
ATOM   602  N  N    . ALA A 1 32  ? 0.81800   -23.25800 -4.53000  1.000 12.41000  ? 32  ALA A N    1 
ATOM   603  C  CA   . ALA A 1 32  ? 0.22500   -22.00300 -4.97400  1.000 12.45000  ? 32  ALA A CA   1 
ATOM   604  C  C    . ALA A 1 32  ? -0.69900  -22.21600 -6.15600  1.000 13.09000  ? 32  ALA A C    1 
ATOM   605  O  O    . ALA A 1 32  ? -1.75000  -21.56300 -6.25400  1.000 15.11000  ? 32  ALA A O    1 
ATOM   606  C  CB   . ALA A 1 32  ? 1.30200   -20.97100 -5.29900  1.000 16.66000  ? 32  ALA A CB   1 
ATOM   607  H  H    . ALA A 1 32  ? 1.67400   -23.30000 -4.59600  1.000 14.88000  ? 32  ALA A H    1 
ATOM   608  H  HA   . ALA A 1 32  ? -0.30200  -21.64200 -4.24400  1.000 14.92000  ? 32  ALA A HA   1 
ATOM   609  H  HB1  . ALA A 1 32  ? 0.88100   -20.17800 -5.66600  1.000 19.98000  ? 32  ALA A HB1  1 
ATOM   610  H  HB2  . ALA A 1 32  ? 1.77900   -20.74500 -4.48400  1.000 19.98000  ? 32  ALA A HB2  1 
ATOM   611  H  HB3  . ALA A 1 32  ? 1.91600   -21.34900 -5.94700  1.000 19.98000  ? 32  ALA A HB3  1 
ATOM   612  N  N    . LYS A 1 33  ? -0.35400  -23.13700 -7.06200  1.000 13.16000  ? 33  LYS A N    1 
ATOM   613  C  CA   . LYS A 1 33  ? -1.19900  -23.37000 -8.22600  1.000 13.08000  ? 33  LYS A CA   1 
ATOM   614  C  C    . LYS A 1 33  ? -2.58600  -23.80900 -7.80100  1.000 14.42000  ? 33  LYS A C    1 
ATOM   615  O  O    . LYS A 1 33  ? -3.59700  -23.26600 -8.26300  1.000 15.96000  ? 33  LYS A O    1 
ATOM   616  C  CB   . LYS A 1 33  ? -0.57200  -24.44200 -9.11600  1.000 16.81000  ? 33  LYS A CB   1 
ATOM   617  C  CG   . LYS A 1 33  ? -1.42500  -24.85300 -10.29400 1.000 18.54000  ? 33  LYS A CG   1 
ATOM   618  C  CD   . LYS A 1 33  ? -1.47700  -23.75800 -11.32900 1.000 24.28000  ? 33  LYS A CD   1 
ATOM   619  C  CE   . LYS A 1 33  ? -2.26700  -24.19200 -12.54500 1.000 33.02000  ? 33  LYS A CE   1 
ATOM   620  N  NZ   . LYS A 1 33  ? -2.38000  -23.07600 -13.50700 1.000 34.33000  ? 33  LYS A NZ   1 
ATOM   621  H  H    . LYS A 1 33  ? 0.35100   -23.62800 -7.02400  1.000 15.79000  ? 33  LYS A H    1 
ATOM   622  H  HA   . LYS A 1 33  ? -1.27000  -22.54600 -8.73200  1.000 15.69000  ? 33  LYS A HA   1 
ATOM   623  H  HB2  . LYS A 1 33  ? 0.26600   -24.10200 -9.46600  1.000 20.16000  ? 33  LYS A HB2  1 
ATOM   624  H  HB3  . LYS A 1 33  ? -0.41100  -25.23400 -8.58000  1.000 20.16000  ? 33  LYS A HB3  1 
ATOM   625  H  HG2  . LYS A 1 33  ? -1.04800  -25.64700 -10.70500 1.000 22.24000  ? 33  LYS A HG2  1 
ATOM   626  H  HG3  . LYS A 1 33  ? -2.32900  -25.03400 -9.99200  1.000 22.24000  ? 33  LYS A HG3  1 
ATOM   627  H  HD2  . LYS A 1 33  ? -1.90500  -22.97500 -10.94900 1.000 29.12000  ? 33  LYS A HD2  1 
ATOM   628  H  HD3  . LYS A 1 33  ? -0.57500  -23.53800 -11.61100 1.000 29.12000  ? 33  LYS A HD3  1 
ATOM   629  H  HE2  . LYS A 1 33  ? -1.81500  -24.93200 -12.98000 1.000 39.62000  ? 33  LYS A HE2  1 
ATOM   630  H  HE3  . LYS A 1 33  ? -3.15900  -24.46000 -12.27600 1.000 39.62000  ? 33  LYS A HE3  1 
ATOM   631  H  HZ1  . LYS A 1 33  ? -3.07800  -22.56400 -13.29900 1.000 41.18000  ? 33  LYS A HZ1  1 
ATOM   632  H  HZ2  . LYS A 1 33  ? -1.64100  -22.58000 -13.48500 1.000 41.18000  ? 33  LYS A HZ2  1 
ATOM   633  H  HZ3  . LYS A 1 33  ? -2.49000  -23.39400 -14.33100 1.000 41.18000  ? 33  LYS A HZ3  1 
ATOM   634  N  N    . PHE A 1 34  ? -2.65100  -24.78500 -6.90900  1.000 13.81000  ? 34  PHE A N    1 
ATOM   635  C  CA   . PHE A 1 34  ? -3.93400  -25.33800 -6.52300  1.000 15.44000  ? 34  PHE A CA   1 
ATOM   636  C  C    . PHE A 1 34  ? -4.64100  -24.51100 -5.47000  1.000 16.26000  ? 34  PHE A C    1 
ATOM   637  O  O    . PHE A 1 34  ? -5.86700  -24.57900 -5.39500  1.000 19.15000  ? 34  PHE A O    1 
ATOM   638  C  CB   . PHE A 1 34  ? -3.77500  -26.80100 -6.14300  1.000 16.34000  ? 34  PHE A CB   1 
ATOM   639  C  CG   . PHE A 1 34  ? -3.30900  -27.62900 -7.29100  1.000 15.24000  ? 34  PHE A CG   1 
ATOM   640  C  CD1  . PHE A 1 34  ? -4.04600  -27.68100 -8.45300  1.000 16.10000  ? 34  PHE A CD1  1 
ATOM   641  C  CD2  . PHE A 1 34  ? -2.12800  -28.30800 -7.23800  1.000 18.63000  ? 34  PHE A CD2  1 
ATOM   642  C  CE1  . PHE A 1 34  ? -3.59500  -28.38700 -9.54600  1.000 19.50000  ? 34  PHE A CE1  1 
ATOM   643  C  CE2  . PHE A 1 34  ? -1.69300  -29.03900 -8.31700  1.000 23.93000  ? 34  PHE A CE2  1 
ATOM   644  C  CZ   . PHE A 1 34  ? -2.44000  -29.10500 -9.45600  1.000 19.09000  ? 34  PHE A CZ   1 
ATOM   645  H  H    . PHE A 1 34  ? -1.97300  -25.14100 -6.51700  1.000 16.56000  ? 34  PHE A H    1 
ATOM   646  H  HA   . PHE A 1 34  ? -4.53900  -25.33700 -7.28100  1.000 18.52000  ? 34  PHE A HA   1 
ATOM   647  H  HB2  . PHE A 1 34  ? -3.12100  -26.87600 -5.43000  1.000 19.59000  ? 34  PHE A HB2  1 
ATOM   648  H  HB3  . PHE A 1 34  ? -4.63000  -27.14900 -5.84600  1.000 19.59000  ? 34  PHE A HB3  1 
ATOM   649  H  HD1  . PHE A 1 34  ? -4.86000  -27.23300 -8.50100  1.000 19.31000  ? 34  PHE A HD1  1 
ATOM   650  H  HD2  . PHE A 1 34  ? -1.61200  -28.27700 -6.46400  1.000 22.34000  ? 34  PHE A HD2  1 
ATOM   651  H  HE1  . PHE A 1 34  ? -4.07700  -28.37500 -10.34100 1.000 23.39000  ? 34  PHE A HE1  1 
ATOM   652  H  HE2  . PHE A 1 34  ? -0.88300  -29.49300 -8.27000  1.000 28.70000  ? 34  PHE A HE2  1 
ATOM   653  H  HZ   . PHE A 1 34  ? -2.16200  -29.63500 -10.16800 1.000 22.89000  ? 34  PHE A HZ   1 
ATOM   654  N  N    . GLU A 1 35  ? -3.91800  -23.70200 -4.70900  1.000 13.06000  ? 35  GLU A N    1 
ATOM   655  C  CA   . GLU A 1 35  ? -4.56400  -22.84300 -3.72600  1.000 14.01000  ? 35  GLU A CA   1 
ATOM   656  C  C    . GLU A 1 35  ? -5.18500  -21.60900 -4.37200  1.000 15.37000  ? 35  GLU A C    1 
ATOM   657  O  O    . GLU A 1 35  ? -6.29700  -21.21700 -4.00200  1.000 16.31000  ? 35  GLU A O    1 
ATOM   658  C  CB   . GLU A 1 35  ? -3.56800  -22.40400 -2.65000  1.000 15.28000  ? 35  GLU A CB   1 
ATOM   659  C  CG   . GLU A 1 35  ? -3.08500  -23.51400 -1.74200  1.000 15.51000  ? 35  GLU A CG   1 
ATOM   660  C  CD   . GLU A 1 35  ? -4.13000  -23.98400 -0.74300  1.000 19.81000  ? 35  GLU A CD   1 
ATOM   661  O  OE1  . GLU A 1 35  ? -5.27700  -23.52400 -0.81300  1.000 17.81000  ? 35  GLU A OE1  1 
ATOM   662  O  OE2  . GLU A 1 35  ? -3.80800  -24.88400 0.04600   1.000 18.65000  ? 35  GLU A OE2  1 
ATOM   663  H  H    . GLU A 1 35  ? -3.06100  -23.63100 -4.74000  1.000 15.66000  ? 35  GLU A H    1 
ATOM   664  H  HA   . GLU A 1 35  ? -5.26600  -23.35900 -3.30000  1.000 16.80000  ? 35  GLU A HA   1 
ATOM   665  H  HB2  . GLU A 1 35  ? -2.79000  -22.02500 -3.08800  1.000 18.33000  ? 35  GLU A HB2  1 
ATOM   666  H  HB3  . GLU A 1 35  ? -3.99400  -21.73500 -2.09200  1.000 18.33000  ? 35  GLU A HB3  1 
ATOM   667  H  HG2  . GLU A 1 35  ? -2.83200  -24.27600 -2.28700  1.000 18.59000  ? 35  GLU A HG2  1 
ATOM   668  H  HG3  . GLU A 1 35  ? -2.31800  -23.19500 -1.24100  1.000 18.59000  ? 35  GLU A HG3  1 
ATOM   669  N  N    . SER A 1 36  ? -4.47700  -20.96600 -5.32400  1.000 13.61000  ? 36  SER A N    1 
ATOM   670  C  CA   . SER A 1 36  ? -4.89000  -19.65500 -5.82000  1.000 14.05000  ? 36  SER A CA   1 
ATOM   671  C  C    . SER A 1 36  ? -4.78000  -19.48800 -7.32100  1.000 16.90000  ? 36  SER A C    1 
ATOM   672  O  O    . SER A 1 36  ? -5.12000  -18.41100 -7.82500  1.000 16.91000  ? 36  SER A O    1 
ATOM   673  C  CB   . SER A 1 36  ? -4.01100  -18.59400 -5.18100  1.000 15.56000  ? 36  SER A CB   1 
ATOM   674  O  OG   . SER A 1 36  ? -2.67700  -18.67400 -5.67500  1.000 15.98000  ? 36  SER A OG   1 
ATOM   675  H  H    . SER A 1 36  ? -3.76100  -21.27200 -5.68900  1.000 16.32000  ? 36  SER A H    1 
ATOM   676  H  HA   . SER A 1 36  ? -5.81900  -19.51800 -5.57900  1.000 16.85000  ? 36  SER A HA   1 
ATOM   677  H  HB2  . SER A 1 36  ? -4.37200  -17.71800 -5.38800  1.000 18.66000  ? 36  SER A HB2  1 
ATOM   678  H  HB3  . SER A 1 36  ? -4.00000  -18.73000 -4.22000  1.000 18.66000  ? 36  SER A HB3  1 
ATOM   679  H  HG   . SER A 1 36  ? -2.26900  -19.30500 -5.30000  1.000 19.16000  ? 36  SER A HG   1 
ATOM   680  N  N    . ASN A 1 37  ? -4.30000  -20.49800 -8.05400  1.000 14.98000  ? 37  ASN A N    1 
ATOM   681  C  CA   . ASN A 1 37  ? -3.99900  -20.35100 -9.48200  1.000 15.93000  ? 37  ASN A CA   1 
ATOM   682  C  C    . ASN A 1 37  ? -3.06300  -19.18000 -9.70800  1.000 18.20000  ? 37  ASN A C    1 
ATOM   683  O  O    . ASN A 1 37  ? -3.16100  -18.47600 -10.70900 1.000 18.94000  ? 37  ASN A O    1 
ATOM   684  C  CB   . ASN A 1 37  ? -5.23900  -20.21300 -10.36400 1.000 18.60000  ? 37  ASN A CB   1 
ATOM   685  C  CG   . ASN A 1 37  ? -5.01100  -20.74900 -11.76300 1.000 23.37000  ? 37  ASN A CG   1 
ATOM   686  O  OD1  . ASN A 1 37  ? -4.04100  -21.45600 -12.02500 1.000 26.63000  ? 37  ASN A OD1  1 
ATOM   687  N  ND2  . ASN A 1 37  ? -5.90000  -20.37900 -12.68200 1.000 35.88000  ? 37  ASN A ND2  1 
ATOM   688  H  H    . ASN A 1 37  ? -4.13800  -21.28400 -7.74500  1.000 17.96000  ? 37  ASN A H    1 
ATOM   689  H  HA   . ASN A 1 37  ? -3.56500  -21.17200 -9.76100  1.000 19.11000  ? 37  ASN A HA   1 
ATOM   690  H  HB2  . ASN A 1 37  ? -5.97000  -20.71100 -9.96500  1.000 22.30000  ? 37  ASN A HB2  1 
ATOM   691  H  HB3  . ASN A 1 37  ? -5.47600  -19.27500 -10.43400 1.000 22.30000  ? 37  ASN A HB3  1 
ATOM   692  H  HD21 . ASN A 1 37  ? -5.82000  -20.65400 -13.49300 1.000 43.05000  ? 37  ASN A HD21 1 
ATOM   693  H  HD22 . ASN A 1 37  ? -6.55500  -19.86600 -12.46500 1.000 43.05000  ? 37  ASN A HD22 1 
ATOM   694  N  N    . PHE A 1 38  ? -2.14200  -18.94500 -8.77300  1.000 15.58000  ? 38  PHE A N    1 
ATOM   695  C  CA   . PHE A 1 38  ? -1.11800  -17.92700 -8.85100  1.000 15.80000  ? 38  PHE A CA   1 
ATOM   696  C  C    . PHE A 1 38  ? -1.67700  -16.50700 -8.77800  1.000 13.96000  ? 38  PHE A C    1 
ATOM   697  O  O    . PHE A 1 38  ? -0.99600  -15.55600 -9.15800  1.000 16.60000  ? 38  PHE A O    1 
ATOM   698  C  CB   . PHE A 1 38  ? -0.25800  -18.07000 -10.11300 1.000 17.20000  ? 38  PHE A CB   1 
ATOM   699  C  CG   . PHE A 1 38  ? 0.41900   -19.42300 -10.29600 1.000 17.38000  ? 38  PHE A CG   1 
ATOM   700  C  CD1  . PHE A 1 38  ? 0.90500   -20.16900 -9.24800  1.000 17.98000  ? 38  PHE A CD1  1 
ATOM   701  C  CD2  . PHE A 1 38  ? 0.59200   -19.90800 -11.58200 1.000 21.15000  ? 38  PHE A CD2  1 
ATOM   702  C  CE1  . PHE A 1 38  ? 1.56400   -21.39200 -9.49900  1.000 17.76000  ? 38  PHE A CE1  1 
ATOM   703  C  CE2  . PHE A 1 38  ? 1.24700   -21.09900 -11.82900 1.000 21.45000  ? 38  PHE A CE2  1 
ATOM   704  C  CZ   . PHE A 1 38  ? 1.72000   -21.84300 -10.78200 1.000 16.47000  ? 38  PHE A CZ   1 
ATOM   705  H  H    . PHE A 1 38  ? -2.09500  -19.39500 -8.04200  1.000 18.69000  ? 38  PHE A H    1 
ATOM   706  H  HA   . PHE A 1 38  ? -0.54200  -18.05100 -8.08100  1.000 18.95000  ? 38  PHE A HA   1 
ATOM   707  H  HB2  . PHE A 1 38  ? -0.82400  -17.92500 -10.88700 1.000 20.62000  ? 38  PHE A HB2  1 
ATOM   708  H  HB3  . PHE A 1 38  ? 0.44200   -17.39900 -10.08300 1.000 20.62000  ? 38  PHE A HB3  1 
ATOM   709  H  HD1  . PHE A 1 38  ? 0.79800   -19.86800 -8.37400  1.000 21.56000  ? 38  PHE A HD1  1 
ATOM   710  H  HD2  . PHE A 1 38  ? 0.25700   -19.41800 -12.29900 1.000 25.37000  ? 38  PHE A HD2  1 
ATOM   711  H  HE1  . PHE A 1 38  ? 1.89500   -21.89300 -8.78800  1.000 21.30000  ? 38  PHE A HE1  1 
ATOM   712  H  HE2  . PHE A 1 38  ? 1.36600   -21.39400 -12.70200 1.000 25.73000  ? 38  PHE A HE2  1 
ATOM   713  H  HZ   . PHE A 1 38  ? 2.14700   -22.65400 -10.94200 1.000 19.75000  ? 38  PHE A HZ   1 
ATOM   714  N  N    . ASN A 1 39  ? -2.87500  -16.35400 -8.23600  1.000 15.06000  ? 39  ASN A N    1 
ATOM   715  C  CA   . ASN A 1 39  ? -3.53100  -15.04900 -8.11900  1.000 15.11000  ? 39  ASN A CA   1 
ATOM   716  C  C    . ASN A 1 39  ? -3.40600  -14.52700 -6.69300  1.000 14.40000  ? 39  ASN A C    1 
ATOM   717  O  O    . ASN A 1 39  ? -3.96400  -15.12100 -5.75400  1.000 15.36000  ? 39  ASN A O    1 
ATOM   718  C  CB   . ASN A 1 39  ? -4.99200  -15.21600 -8.50700  1.000 15.51000  ? 39  ASN A CB   1 
ATOM   719  C  CG   . ASN A 1 39  ? -5.76400  -13.93200 -8.50900  1.000 15.64000  ? 39  ASN A CG   1 
ATOM   720  O  OD1  . ASN A 1 39  ? -5.22400  -12.86100 -8.28700  1.000 15.24000  ? 39  ASN A OD1  1 
ATOM   721  N  ND2  . ASN A 1 39  ? -7.05700  -14.05500 -8.69200  1.000 21.79000  ? 39  ASN A ND2  1 
ATOM   722  H  H    . ASN A 1 39  ? -3.34300  -17.00200 -7.91900  1.000 18.06000  ? 39  ASN A H    1 
ATOM   723  H  HA   . ASN A 1 39  ? -3.10000  -14.39600 -8.69400  1.000 18.13000  ? 39  ASN A HA   1 
ATOM   724  H  HB2  . ASN A 1 39  ? -5.03800  -15.59100 -9.40000  1.000 18.59000  ? 39  ASN A HB2  1 
ATOM   725  H  HB3  . ASN A 1 39  ? -5.41700  -15.81600 -7.87400  1.000 18.59000  ? 39  ASN A HB3  1 
ATOM   726  H  HD21 . ASN A 1 39  ? -7.55800  -13.35700 -8.70400  1.000 26.14000  ? 39  ASN A HD21 1 
ATOM   727  H  HD22 . ASN A 1 39  ? -7.40300  -14.83500 -8.79900  1.000 26.14000  ? 39  ASN A HD22 1 
ATOM   728  N  N    . THR A 1 40  ? -2.71800  -13.39700 -6.52300  1.000 14.15000  ? 40  THR A N    1 
ATOM   729  C  CA   . THR A 1 40  ? -2.55400  -12.82300 -5.18100  1.000 14.34000  ? 40  THR A CA   1 
ATOM   730  C  C    . THR A 1 40  ? -3.88300  -12.34800 -4.58500  1.000 13.33000  ? 40  THR A C    1 
ATOM   731  O  O    . THR A 1 40  ? -3.97800  -12.23600 -3.36800  1.000 14.97000  ? 40  THR A O    1 
ATOM   732  C  CB   . THR A 1 40  ? -1.56900  -11.66000 -5.14700  1.000 17.91000  ? 40  THR A CB   1 
ATOM   733  O  OG1  . THR A 1 40  ? -2.11500  -10.56300 -5.87400  1.000 17.23000  ? 40  THR A OG1  1 
ATOM   734  C  CG2  . THR A 1 40  ? -0.20200  -12.02300 -5.75100  1.000 17.30000  ? 40  THR A CG2  1 
ATOM   735  H  H    . THR A 1 40  ? -2.34300  -12.94900 -7.15300  1.000 16.96000  ? 40  THR A H    1 
ATOM   736  H  HA   . THR A 1 40  ? -2.17700  -13.52800 -4.63100  1.000 17.19000  ? 40  THR A HA   1 
ATOM   737  H  HB   . THR A 1 40  ? -1.41600  -11.41900 -4.22000  1.000 21.48000  ? 40  THR A HB   1 
ATOM   738  H  HG1  . THR A 1 40  ? -1.65700  -9.87200  -5.73800  1.000 20.67000  ? 40  THR A HG1  1 
ATOM   739  H  HG21 . THR A 1 40  ? 0.46400   -11.37100 -5.48200  1.000 20.75000  ? 40  THR A HG21 1 
ATOM   740  H  HG22 . THR A 1 40  ? 0.07400   -12.90100 -5.44400  1.000 20.75000  ? 40  THR A HG22 1 
ATOM   741  H  HG23 . THR A 1 40  ? -0.25900  -12.03200 -6.72000  1.000 20.75000  ? 40  THR A HG23 1 
ATOM   742  N  N    A GLN A 1 41  ? -4.88000  -12.08500 -5.40300  0.580 14.22000  ? 41  GLN A N    1 
ATOM   743  N  N    B GLN A 1 41  ? -4.89700  -12.07500 -5.39900  0.420 14.38000  ? 41  GLN A N    1 
ATOM   744  C  CA   A GLN A 1 41  ? -6.13400  -11.54400 -4.88500  0.580 14.58000  ? 41  GLN A CA   1 
ATOM   745  C  CA   B GLN A 1 41  ? -6.17500  -11.55500 -4.90100  0.420 14.54000  ? 41  GLN A CA   1 
ATOM   746  C  C    A GLN A 1 41  ? -7.09500  -12.60400 -4.37900  0.580 15.56000  ? 41  GLN A C    1 
ATOM   747  C  C    B GLN A 1 41  ? -7.19300  -12.64600 -4.59000  0.420 16.10000  ? 41  GLN A C    1 
ATOM   748  O  O    A GLN A 1 41  ? -8.11000  -12.23800 -3.78000  0.580 15.99000  ? 41  GLN A O    1 
ATOM   749  O  O    B GLN A 1 41  ? -8.38600  -12.36600 -4.43300  0.420 14.13000  ? 41  GLN A O    1 
ATOM   750  C  CB   A GLN A 1 41  ? -6.82900  -10.70800 -5.95100  0.580 14.58000  ? 41  GLN A CB   1 
ATOM   751  C  CB   B GLN A 1 41  ? -6.78800  -10.59600 -5.91600  0.420 14.51000  ? 41  GLN A CB   1 
ATOM   752  C  CG   A GLN A 1 41  ? -6.08300  -9.43700  -6.24100  0.580 15.55000  ? 41  GLN A CG   1 
ATOM   753  C  CG   B GLN A 1 41  ? -5.92500  -9.40600  -6.24100  0.420 16.24000  ? 41  GLN A CG   1 
ATOM   754  C  CD   A GLN A 1 41  ? -6.93000  -8.41300  -6.94000  0.580 14.75000  ? 41  GLN A CD   1 
ATOM   755  C  CD   B GLN A 1 41  ? -6.70900  -8.31200  -6.91700  0.420 18.13000  ? 41  GLN A CD   1 
ATOM   756  O  OE1  A GLN A 1 41  ? -7.98000  -8.01700  -6.44300  0.580 13.86000  ? 41  GLN A OE1  1 
ATOM   757  O  OE1  B GLN A 1 41  ? -7.28400  -7.45300  -6.25100  0.420 16.32000  ? 41  GLN A OE1  1 
ATOM   758  N  NE2  A GLN A 1 41  ? -6.45800  -7.95100  -8.08900  0.580 16.74000  ? 41  GLN A NE2  1 
ATOM   759  N  NE2  B GLN A 1 41  ? -6.74800  -8.34100  -8.24800  0.420 14.34000  ? 41  GLN A NE2  1 
ATOM   760  H  H    A GLN A 1 41  ? -4.86300  -12.20600 -6.25500  0.580 17.05000  ? 41  GLN A H    1 
ATOM   761  H  H    B GLN A 1 41  ? -4.87300  -12.18300 -6.25200  0.420 17.24000  ? 41  GLN A H    1 
ATOM   762  H  HA   A GLN A 1 41  ? -5.91700  -10.96500 -4.13700  0.580 17.49000  ? 41  GLN A HA   1 
ATOM   763  H  HA   B GLN A 1 41  ? -5.99100  -11.06900 -4.08200  0.420 17.43000  ? 41  GLN A HA   1 
ATOM   764  H  HB2  A GLN A 1 41  ? -6.88500  -11.22100 -6.77300  0.580 17.48000  ? 41  GLN A HB2  1 
ATOM   765  H  HB2  B GLN A 1 41  ? -6.94600  -11.07900 -6.74200  0.420 17.40000  ? 41  GLN A HB2  1 
ATOM   766  H  HB3  A GLN A 1 41  ? -7.71900  -10.47500 -5.64500  0.580 17.48000  ? 41  GLN A HB3  1 
ATOM   767  H  HB3  B GLN A 1 41  ? -7.62600  -10.26300 -5.56000  0.420 17.40000  ? 41  GLN A HB3  1 
ATOM   768  H  HG2  A GLN A 1 41  ? -5.77800  -9.05200  -5.40400  0.580 18.65000  ? 41  GLN A HG2  1 
ATOM   769  H  HG2  B GLN A 1 41  ? -5.55100  -9.04900  -5.42100  0.420 19.48000  ? 41  GLN A HG2  1 
ATOM   770  H  HG3  A GLN A 1 41  ? -5.32400  -9.63800  -6.81000  0.580 18.65000  ? 41  GLN A HG3  1 
ATOM   771  H  HG3  B GLN A 1 41  ? -5.21200  -9.68200  -6.83800  0.420 19.48000  ? 41  GLN A HG3  1 
ATOM   772  H  HE21 A GLN A 1 41  ? -6.90400  -7.36300  -8.53100  0.580 20.07000  ? 41  GLN A HE21 1 
ATOM   773  H  HE21 B GLN A 1 41  ? -7.18300  -7.73700  -8.67900  0.420 17.19000  ? 41  GLN A HE21 1 
ATOM   774  H  HE22 A GLN A 1 41  ? -5.70700  -8.24000  -8.39300  0.580 20.07000  ? 41  GLN A HE22 1 
ATOM   775  H  HE22 B GLN A 1 41  ? -6.33800  -8.96400  -8.67600  0.420 17.19000  ? 41  GLN A HE22 1 
ATOM   776  N  N    . ALA A 1 42  ? -6.77500  -13.88900 -4.54500  1.000 14.01000  ? 42  ALA A N    1 
ATOM   777  C  CA   . ALA A 1 42  ? -7.70300  -14.97200 -4.25400  1.000 13.45000  ? 42  ALA A CA   1 
ATOM   778  C  C    . ALA A 1 42  ? -8.13800  -14.96000 -2.78700  1.000 14.40000  ? 42  ALA A C    1 
ATOM   779  O  O    . ALA A 1 42  ? -7.31900  -14.81600 -1.87600  1.000 14.39000  ? 42  ALA A O    1 
ATOM   780  C  CB   . ALA A 1 42  ? -7.01200  -16.30000 -4.56700  1.000 17.32000  ? 42  ALA A CB   1 
ATOM   781  H  H    . ALA A 1 42  ? -6.01100  -14.16100 -4.83100  1.000 16.80000  ? 42  ALA A H    1 
ATOM   782  H  HA   . ALA A 1 42  ? -8.50000  -14.86800 -4.79700  1.000 16.13000  ? 42  ALA A HA   1 
ATOM   783  H  HB1  . ALA A 1 42  ? -7.65700  -17.01900 -4.48400  1.000 20.77000  ? 42  ALA A HB1  1 
ATOM   784  H  HB2  . ALA A 1 42  ? -6.66500  -16.26900 -5.47300  1.000 20.77000  ? 42  ALA A HB2  1 
ATOM   785  H  HB3  . ALA A 1 42  ? -6.28500  -16.43300 -3.93900  1.000 20.77000  ? 42  ALA A HB3  1 
ATOM   786  N  N    . THR A 1 43  ? -9.44000  -15.09400 -2.56500  1.000 15.00000  ? 43  THR A N    1 
ATOM   787  C  CA   . THR A 1 43  ? -10.02500 -15.26100 -1.23600  1.000 14.32000  ? 43  THR A CA   1 
ATOM   788  C  C    . THR A 1 43  ? -11.04100 -16.38600 -1.31100  1.000 16.59000  ? 43  THR A C    1 
ATOM   789  O  O    . THR A 1 43  ? -11.72900 -16.55400 -2.32500  1.000 19.46000  ? 43  THR A O    1 
ATOM   790  C  CB   . THR A 1 43  ? -10.72300 -14.00200 -0.73300  1.000 17.83000  ? 43  THR A CB   1 
ATOM   791  O  OG1  . THR A 1 43  ? -11.78200 -13.61900 -1.63000  1.000 18.44000  ? 43  THR A OG1  1 
ATOM   792  C  CG2  . THR A 1 43  ? -9.76100  -12.85400 -0.62000  1.000 21.37000  ? 43  THR A CG2  1 
ATOM   793  H  H    . THR A 1 43  ? -10.02900 -15.09100 -3.19100  1.000 17.98000  ? 43  THR A H    1 
ATOM   794  H  HA   . THR A 1 43  ? -9.32300  -15.47600 -0.60200  1.000 17.17000  ? 43  THR A HA   1 
ATOM   795  H  HB   . THR A 1 43  ? -11.09000 -14.19200 0.14400   1.000 21.39000  ? 43  THR A HB   1 
ATOM   796  H  HG1  . THR A 1 43  ? -11.46400 -13.21800 -2.29600  1.000 22.12000  ? 43  THR A HG1  1 
ATOM   797  H  HG21 . THR A 1 43  ? -10.23700 -12.04500 -0.37600  1.000 25.63000  ? 43  THR A HG21 1 
ATOM   798  H  HG22 . THR A 1 43  ? -9.09600  -13.04500 0.06000   1.000 25.63000  ? 43  THR A HG22 1 
ATOM   799  H  HG23 . THR A 1 43  ? -9.31300  -12.71200 -1.46800  1.000 25.63000  ? 43  THR A HG23 1 
ATOM   800  N  N    A ASN A 1 44  ? -11.18100 -17.13200 -0.21300  0.560 14.56000  ? 44  ASN A N    1 
ATOM   801  N  N    B ASN A 1 44  ? -11.14200 -17.16700 -0.23900  0.440 14.78000  ? 44  ASN A N    1 
ATOM   802  C  CA   A ASN A 1 44  ? -12.10600 -18.25900 -0.17700  0.560 15.80000  ? 44  ASN A CA   1 
ATOM   803  C  CA   B ASN A 1 44  ? -12.15000 -18.21100 -0.14900  0.440 15.79000  ? 44  ASN A CA   1 
ATOM   804  C  C    A ASN A 1 44  ? -12.53500 -18.53600 1.25400   0.560 15.20000  ? 44  ASN A C    1 
ATOM   805  C  C    B ASN A 1 44  ? -12.60300 -18.30700 1.29800   0.440 15.13000  ? 44  ASN A C    1 
ATOM   806  O  O    A ASN A 1 44  ? -11.69600 -18.61100 2.15900   0.560 14.03000  ? 44  ASN A O    1 
ATOM   807  O  O    B ASN A 1 44  ? -11.85400 -17.97800 2.22000   0.440 12.92000  ? 44  ASN A O    1 
ATOM   808  C  CB   A ASN A 1 44  ? -11.46900 -19.51400 -0.77300  0.560 16.45000  ? 44  ASN A CB   1 
ATOM   809  C  CB   B ASN A 1 44  ? -11.62600 -19.57600 -0.61900  0.440 15.08000  ? 44  ASN A CB   1 
ATOM   810  C  CG   A ASN A 1 44  ? -11.34200 -19.42400 -2.27400  0.560 14.76000  ? 44  ASN A CG   1 
ATOM   811  C  CG   B ASN A 1 44  ? -12.64600 -20.32900 -1.44400  0.440 31.75000  ? 44  ASN A CG   1 
ATOM   812  O  OD1  A ASN A 1 44  ? -12.34200 -19.38800 -2.98700  0.560 17.80000  ? 44  ASN A OD1  1 
ATOM   813  O  OD1  B ASN A 1 44  ? -13.43200 -21.11600 -0.92000  0.440 30.29000  ? 44  ASN A OD1  1 
ATOM   814  N  ND2  A ASN A 1 44  ? -10.11700 -19.37900 -2.75800  0.560 16.72000  ? 44  ASN A ND2  1 
ATOM   815  N  ND2  B ASN A 1 44  ? -12.65300 -20.07000 -2.74400  0.440 21.83000  ? 44  ASN A ND2  1 
ATOM   816  H  H    A ASN A 1 44  ? -10.75000 -17.00500 0.52100   0.560 17.46000  ? 44  ASN A H    1 
ATOM   817  H  H    B ASN A 1 44  ? -10.63300 -17.11000 0.45200   0.440 17.72000  ? 44  ASN A H    1 
ATOM   818  H  HA   A ASN A 1 44  ? -12.89600 -18.02200 -0.68800  0.560 18.95000  ? 44  ASN A HA   1 
ATOM   819  H  HA   B ASN A 1 44  ? -12.90400 -17.97500 -0.71100  0.440 18.94000  ? 44  ASN A HA   1 
ATOM   820  H  HB2  A ASN A 1 44  ? -10.58000 -19.62800 -0.40000  0.560 19.73000  ? 44  ASN A HB2  1 
ATOM   821  H  HB2  B ASN A 1 44  ? -10.83600 -19.44300 -1.16400  0.440 18.09000  ? 44  ASN A HB2  1 
ATOM   822  H  HB3  A ASN A 1 44  ? -12.01900 -20.28300 -0.56000  0.560 19.73000  ? 44  ASN A HB3  1 
ATOM   823  H  HB3  B ASN A 1 44  ? -11.40700 -20.11600 0.15600   0.440 18.09000  ? 44  ASN A HB3  1 
ATOM   824  H  HD21 A ASN A 1 44  ? -9.44300  -19.40100 -2.22400  0.560 20.05000  ? 44  ASN A HD21 1 
ATOM   825  H  HD21 B ASN A 1 44  ? -12.09800 -19.50100 -3.07200  0.440 26.18000  ? 44  ASN A HD21 1 
ATOM   826  H  HD22 A ASN A 1 44  ? -9.99200  -19.32800 -3.60700  0.560 20.05000  ? 44  ASN A HD22 1 
ATOM   827  H  HD22 B ASN A 1 44  ? -13.21300 -20.47100 -3.25900  0.440 26.18000  ? 44  ASN A HD22 1 
ATOM   828  N  N    A ARG A 1 45  ? -13.83600 -18.71100 1.43700   0.560 15.59000  ? 45  ARG A N    1 
ATOM   829  N  N    B ARG A 1 45  ? -13.82600 -18.77800 1.48500   0.440 16.04000  ? 45  ARG A N    1 
ATOM   830  C  CA   A ARG A 1 45  ? -14.41500 -18.96200 2.74900   0.560 18.89000  ? 45  ARG A CA   1 
ATOM   831  C  CA   B ARG A 1 45  ? -14.43400 -18.89800 2.80400   0.440 18.51000  ? 45  ARG A CA   1 
ATOM   832  C  C    A ARG A 1 45  ? -14.29700 -20.43400 3.14000   0.560 17.12000  ? 45  ARG A C    1 
ATOM   833  C  C    B ARG A 1 45  ? -14.51000 -20.36300 3.20500   0.440 18.61000  ? 45  ARG A C    1 
ATOM   834  O  O    A ARG A 1 45  ? -14.41200 -21.35000 2.31300   0.560 19.89000  ? 45  ARG A O    1 
ATOM   835  O  O    B ARG A 1 45  ? -15.04700 -21.18900 2.46000   0.440 18.71000  ? 45  ARG A O    1 
ATOM   836  C  CB   A ARG A 1 45  ? -15.88700 -18.54500 2.72300   0.560 21.08000  ? 45  ARG A CB   1 
ATOM   837  C  CB   B ARG A 1 45  ? -15.84900 -18.32100 2.78400   0.440 19.48000  ? 45  ARG A CB   1 
ATOM   838  C  CG   A ARG A 1 45  ? -16.57200 -18.61500 4.06900   0.560 25.14000  ? 45  ARG A CG   1 
ATOM   839  C  CG   B ARG A 1 45  ? -16.48400 -18.23600 4.15600   0.440 19.41000  ? 45  ARG A CG   1 
ATOM   840  C  CD   A ARG A 1 45  ? -16.11500 -17.47500 4.93800   0.560 27.54000  ? 45  ARG A CD   1 
ATOM   841  C  CD   B ARG A 1 45  ? -15.97000 -17.05600 4.92800   0.440 32.88000  ? 45  ARG A CD   1 
ATOM   842  N  NE   A ARG A 1 45  ? -16.39700 -16.19000 4.31200   0.560 36.18000  ? 45  ARG A NE   1 
ATOM   843  N  NE   B ARG A 1 45  ? -16.22000 -15.83000 4.18700   0.440 36.88000  ? 45  ARG A NE   1 
ATOM   844  C  CZ   A ARG A 1 45  ? -17.34400 -15.34400 4.70200   0.560 38.62000  ? 45  ARG A CZ   1 
ATOM   845  C  CZ   B ARG A 1 45  ? -17.43000 -15.34900 3.93400   0.440 34.99000  ? 45  ARG A CZ   1 
ATOM   846  N  NH1  A ARG A 1 45  ? -18.05600 -15.55100 5.79700   0.560 44.86000  ? 45  ARG A NH1  1 
ATOM   847  N  NH1  B ARG A 1 45  ? -18.52000 -15.93400 4.40300   0.440 34.46000  ? 45  ARG A NH1  1 
ATOM   848  N  NH2  A ARG A 1 45  ? -17.57300 -14.25500 3.97900   0.560 31.84000  ? 45  ARG A NH2  1 
ATOM   849  N  NH2  B ARG A 1 45  ? -17.54900 -14.26400 3.17900   0.440 31.76000  ? 45  ARG A NH2  1 
ATOM   850  H  H    A ARG A 1 45  ? -14.41800 -18.68800 0.80400   0.560 18.70000  ? 45  ARG A H    1 
ATOM   851  H  H    B ARG A 1 45  ? -14.33900 -19.04300 0.84700   0.440 19.24000  ? 45  ARG A H    1 
ATOM   852  H  HA   A ARG A 1 45  ? -13.93900 -18.45100 3.42200   0.560 22.65000  ? 45  ARG A HA   1 
ATOM   853  H  HA   B ARG A 1 45  ? -13.89100 -18.42300 3.45200   0.440 22.20000  ? 45  ARG A HA   1 
ATOM   854  H  HB2  A ARG A 1 45  ? -15.94500 -17.62900 2.41000   0.560 25.28000  ? 45  ARG A HB2  1 
ATOM   855  H  HB2  B ARG A 1 45  ? -15.81600 -17.42400 2.41500   0.440 23.36000  ? 45  ARG A HB2  1 
ATOM   856  H  HB3  A ARG A 1 45  ? -16.36600 -19.13300 2.11800   0.560 25.28000  ? 45  ARG A HB3  1 
ATOM   857  H  HB3  B ARG A 1 45  ? -16.41000 -18.88600 2.23000   0.440 23.36000  ? 45  ARG A HB3  1 
ATOM   858  H  HG2  A ARG A 1 45  ? -17.53200 -18.55000 3.95000   0.560 30.16000  ? 45  ARG A HG2  1 
ATOM   859  H  HG2  B ARG A 1 45  ? -17.44500 -18.14300 4.06100   0.440 23.28000  ? 45  ARG A HG2  1 
ATOM   860  H  HG3  A ARG A 1 45  ? -16.34700 -19.45100 4.50700   0.560 30.16000  ? 45  ARG A HG3  1 
ATOM   861  H  HG3  B ARG A 1 45  ? -16.27700 -19.04100 4.65600   0.440 23.28000  ? 45  ARG A HG3  1 
ATOM   862  H  HD2  A ARG A 1 45  ? -16.58100 -17.51100 5.78800   0.560 33.04000  ? 45  ARG A HD2  1 
ATOM   863  H  HD2  B ARG A 1 45  ? -16.42500 -17.00100 5.78300   0.440 39.44000  ? 45  ARG A HD2  1 
ATOM   864  H  HD3  A ARG A 1 45  ? -15.15800 -17.54200 5.08100   0.560 33.04000  ? 45  ARG A HD3  1 
ATOM   865  H  HD3  B ARG A 1 45  ? -15.01400 -17.14600 5.06600   0.440 39.44000  ? 45  ARG A HD3  1 
ATOM   866  H  HE   A ARG A 1 45  ? -15.91400 -15.96200 3.63800   0.560 43.40000  ? 45  ARG A HE   1 
ATOM   867  H  HE   B ARG A 1 45  ? -15.54200 -15.39000 3.89500   0.440 44.25000  ? 45  ARG A HE   1 
ATOM   868  H  HH11 A ARG A 1 45  ? -17.91200 -16.24900 6.27800   0.560 53.82000  ? 45  ARG A HH11 1 
ATOM   869  H  HH11 B ARG A 1 45  ? -18.45500 -16.64300 4.88500   0.440 41.34000  ? 45  ARG A HH11 1 
ATOM   870  H  HH12 A ARG A 1 45  ? -18.66300 -14.98800 6.02800   0.560 53.82000  ? 45  ARG A HH12 1 
ATOM   871  H  HH12 B ARG A 1 45  ? -19.29500 -15.60400 4.22700   0.440 41.34000  ? 45  ARG A HH12 1 
ATOM   872  H  HH21 A ARG A 1 45  ? -17.11200 -14.10500 3.26800   0.560 38.20000  ? 45  ARG A HH21 1 
ATOM   873  H  HH21 B ARG A 1 45  ? -16.84700 -13.88200 2.86100   0.440 38.10000  ? 45  ARG A HH21 1 
ATOM   874  H  HH22 A ARG A 1 45  ? -18.18300 -13.69900 4.22000   0.560 38.20000  ? 45  ARG A HH22 1 
ATOM   875  H  HH22 B ARG A 1 45  ? -18.32800 -13.94300 3.00800   0.440 38.10000  ? 45  ARG A HH22 1 
ATOM   876  N  N    . ASN A 1 46  ? -14.05900 -20.66000 4.42300   1.000 18.56000  ? 46  ASN A N    1 
ATOM   877  C  CA   . ASN A 1 46  ? -14.05900 -22.00300 4.98600   1.000 20.69000  ? 46  ASN A CA   1 
ATOM   878  C  C    . ASN A 1 46  ? -15.38600 -22.23200 5.71100   1.000 17.38000  ? 46  ASN A C    1 
ATOM   879  O  O    . ASN A 1 46  ? -16.06200 -21.29000 6.11500   1.000 22.44000  ? 46  ASN A O    1 
ATOM   880  C  CB   . ASN A 1 46  ? -12.92200 -22.13400 6.00900   1.000 20.55000  ? 46  ASN A CB   1 
ATOM   881  C  CG   . ASN A 1 46  ? -11.54400 -21.82100 5.41500   1.000 19.66000  ? 46  ASN A CG   1 
ATOM   882  O  OD1  . ASN A 1 46  ? -10.71800 -21.11000 6.03300   1.000 21.96000  ? 46  ASN A OD1  1 
ATOM   883  N  ND2  . ASN A 1 46  ? -11.28700 -22.34100 4.23800   1.000 20.34000  ? 46  ASN A ND2  1 
ATOM   884  H  H    . ASN A 1 46  ? -13.89200 -20.04200 4.99800   1.000 22.26000  ? 46  ASN A H    1 
ATOM   885  H  HA   . ASN A 1 46  ? -13.94100 -22.66500 4.28600   1.000 24.81000  ? 46  ASN A HA   1 
ATOM   886  H  HB2  . ASN A 1 46  ? -13.08100 -21.51300 6.73700   1.000 24.65000  ? 46  ASN A HB2  1 
ATOM   887  H  HB3  . ASN A 1 46  ? -12.90400 -23.04300 6.34500   1.000 24.65000  ? 46  ASN A HB3  1 
ATOM   888  H  HD21 . ASN A 1 46  ? -10.52700 -22.19700 3.86000   1.000 24.40000  ? 46  ASN A HD21 1 
ATOM   889  H  HD22 . ASN A 1 46  ? -11.87700 -22.82700 3.84400   1.000 24.40000  ? 46  ASN A HD22 1 
ATOM   890  N  N    . THR A 1 47  ? -15.68900 -23.51000 5.95800   1.000 24.08000  ? 47  THR A N    1 
ATOM   891  C  CA   . THR A 1 47  ? -16.97000 -23.85300 6.57100   1.000 26.77000  ? 47  THR A CA   1 
ATOM   892  C  C    . THR A 1 47  ? -17.11800 -23.26900 7.97200   1.000 24.26000  ? 47  THR A C    1 
ATOM   893  O  O    . THR A 1 47  ? -18.24500 -22.98000 8.40700   1.000 27.60000  ? 47  THR A O    1 
ATOM   894  C  CB   . THR A 1 47  ? -17.17100 -25.37600 6.56100   1.000 24.72000  ? 47  THR A CB   1 
ATOM   895  O  OG1  . THR A 1 47  ? -16.16200 -26.02100 7.34100   1.000 34.30000  ? 47  THR A OG1  1 
ATOM   896  C  CG2  . THR A 1 47  ? -17.09000 -25.90300 5.15200   1.000 29.36000  ? 47  THR A CG2  1 
ATOM   897  H  H    . THR A 1 47  ? -15.18100 -24.18100 5.78300   1.000 28.88000  ? 47  THR A H    1 
ATOM   898  H  HA   . THR A 1 47  ? -17.68300 -23.46800 6.03800   1.000 32.12000  ? 47  THR A HA   1 
ATOM   899  H  HB   . THR A 1 47  ? -18.04400 -25.57600 6.93400   1.000 29.66000  ? 47  THR A HB   1 
ATOM   900  H  HG1  . THR A 1 47  ? -15.49200 -26.18900 6.86200   1.000 41.15000  ? 47  THR A HG1  1 
ATOM   901  H  HG21 . THR A 1 47  ? -17.30800 -26.84800 5.13800   1.000 35.21000  ? 47  THR A HG21 1 
ATOM   902  H  HG22 . THR A 1 47  ? -17.71500 -25.42800 4.58300   1.000 35.21000  ? 47  THR A HG22 1 
ATOM   903  H  HG23 . THR A 1 47  ? -16.19300 -25.78300 4.80300   1.000 35.21000  ? 47  THR A HG23 1 
ATOM   904  N  N    A ASP A 1 48  ? -16.00600 -23.07200 8.68700   0.710 21.88000  ? 48  ASP A N    1 
ATOM   905  N  N    B ASP A 1 48  ? -16.01400 -23.06600 8.68900   0.290 22.00000  ? 48  ASP A N    1 
ATOM   906  C  CA   A ASP A 1 48  ? -16.07700 -22.53400 10.04200  0.710 22.39000  ? 48  ASP A CA   1 
ATOM   907  C  CA   B ASP A 1 48  ? -16.09100 -22.53000 10.04400  0.290 22.49000  ? 48  ASP A CA   1 
ATOM   908  C  C    A ASP A 1 48  ? -16.23200 -21.01800 10.09600  0.710 23.15000  ? 48  ASP A C    1 
ATOM   909  C  C    B ASP A 1 48  ? -16.26500 -21.01700 10.09500  0.290 23.18000  ? 48  ASP A C    1 
ATOM   910  O  O    A ASP A 1 48  ? -16.29900 -20.45600 11.19400  0.710 27.48000  ? 48  ASP A O    1 
ATOM   911  O  O    B ASP A 1 48  ? -16.37300 -20.46200 11.19400  0.290 27.38000  ? 48  ASP A O    1 
ATOM   912  C  CB   A ASP A 1 48  ? -14.85800 -22.99200 10.84900  0.710 20.47000  ? 48  ASP A CB   1 
ATOM   913  C  CB   B ASP A 1 48  ? -14.83700 -22.91600 10.82400  0.290 20.64000  ? 48  ASP A CB   1 
ATOM   914  C  CG   A ASP A 1 48  ? -13.56200 -22.35600 10.38000  0.710 24.00000  ? 48  ASP A CG   1 
ATOM   915  C  CG   B ASP A 1 48  ? -13.57800 -22.45500 10.14000  0.290 24.21000  ? 48  ASP A CG   1 
ATOM   916  O  OD1  A ASP A 1 48  ? -13.56700 -21.67300 9.33200   0.710 21.87000  ? 48  ASP A OD1  1 
ATOM   917  O  OD1  B ASP A 1 48  ? -13.14400 -23.15800 9.21100   0.290 21.59000  ? 48  ASP A OD1  1 
ATOM   918  O  OD2  A ASP A 1 48  ? -12.54000 -22.55100 11.07300  0.710 24.82000  ? 48  ASP A OD2  1 
ATOM   919  O  OD2  B ASP A 1 48  ? -13.04300 -21.38800 10.51200  0.290 22.21000  ? 48  ASP A OD2  1 
ATOM   920  H  H    A ASP A 1 48  ? -15.21000 -23.24200 8.41000   0.710 26.24000  ? 48  ASP A H    1 
ATOM   921  H  H    B ASP A 1 48  ? -15.21600 -23.22900 8.41400   0.290 26.38000  ? 48  ASP A H    1 
ATOM   922  H  HA   A ASP A 1 48  ? -16.86400 -22.89700 10.47700  0.710 26.85000  ? 48  ASP A HA   1 
ATOM   923  H  HA   B ASP A 1 48  ? -16.86200 -22.92600 10.48000  0.290 26.98000  ? 48  ASP A HA   1 
ATOM   924  H  HB2  A ASP A 1 48  ? -14.98900 -22.75300 11.78000  0.710 24.55000  ? 48  ASP A HB2  1 
ATOM   925  H  HB2  B ASP A 1 48  ? -14.87100 -22.50800 11.70300  0.290 24.75000  ? 48  ASP A HB2  1 
ATOM   926  H  HB3  A ASP A 1 48  ? -14.76700 -23.95400 10.76300  0.710 24.55000  ? 48  ASP A HB3  1 
ATOM   927  H  HB3  B ASP A 1 48  ? -14.80000 -23.88200 10.90900  0.290 24.75000  ? 48  ASP A HB3  1 
ATOM   928  N  N    . GLY A 1 49  ? -16.28800 -20.32800 8.95500   1.000 23.57000  ? 49  GLY A N    1 
ATOM   929  C  CA   . GLY A 1 49  ? -16.44500 -18.89400 8.93200   1.000 25.40000  ? 49  GLY A CA   1 
ATOM   930  C  C    . GLY A 1 49  ? -15.15800 -18.11800 8.73500   1.000 21.08000  ? 49  GLY A C    1 
ATOM   931  O  O    . GLY A 1 49  ? -15.20600 -16.91200 8.48000   1.000 23.57000  ? 49  GLY A O    1 
ATOM   932  H  H    . GLY A 1 49  ? -16.23600 -20.68300 8.17300   1.000 28.27000  ? 49  GLY A H    1 
ATOM   933  H  HA2  . GLY A 1 49  ? -17.04600 -18.65900 8.20800   1.000 30.47000  ? 49  GLY A HA2  1 
ATOM   934  H  HA3  . GLY A 1 49  ? -16.83600 -18.61100 9.77300   1.000 30.47000  ? 49  GLY A HA3  1 
ATOM   935  N  N    . SER A 1 50  ? -14.01700 -18.77600 8.84000   1.000 19.66000  ? 50  SER A N    1 
ATOM   936  C  CA   . SER A 1 50  ? -12.75600 -18.12600 8.55400   1.000 16.49000  ? 50  SER A CA   1 
ATOM   937  C  C    . SER A 1 50  ? -12.58500 -17.99700 7.03800   1.000 16.99000  ? 50  SER A C    1 
ATOM   938  O  O    . SER A 1 50  ? -13.29900 -18.62400 6.25700   1.000 17.15000  ? 50  SER A O    1 
ATOM   939  C  CB   . SER A 1 50  ? -11.60600 -18.91100 9.18700   1.000 15.54000  ? 50  SER A CB   1 
ATOM   940  O  OG   . SER A 1 50  ? -11.49000 -20.17900 8.60800   1.000 17.29000  ? 50  SER A OG   1 
ATOM   941  H  H    . SER A 1 50  ? -13.94800 -19.60100 9.07500   1.000 23.59000  ? 50  SER A H    1 
ATOM   942  H  HA   . SER A 1 50  ? -12.73600 -17.23500 8.93500   1.000 19.78000  ? 50  SER A HA   1 
ATOM   943  H  HB2  . SER A 1 50  ? -10.77800 -18.42400 9.05000   1.000 18.64000  ? 50  SER A HB2  1 
ATOM   944  H  HB3  . SER A 1 50  ? -11.77800 -19.01200 10.13700  1.000 18.64000  ? 50  SER A HB3  1 
ATOM   945  H  HG   . SER A 1 50  ? -12.24800 -20.53600 8.54400   1.000 20.73000  ? 50  SER A HG   1 
ATOM   946  N  N    . THR A 1 51  ? -11.59700 -17.22000 6.63400   1.000 14.23000  ? 51  THR A N    1 
ATOM   947  C  CA   . THR A 1 51  ? -11.33900 -16.95000 5.22400   1.000 12.74000  ? 51  THR A CA   1 
ATOM   948  C  C    . THR A 1 51  ? -9.86200  -17.19200 4.93700   1.000 14.53000  ? 51  THR A C    1 
ATOM   949  O  O    . THR A 1 51  ? -9.00200  -16.93000 5.77900   1.000 13.34000  ? 51  THR A O    1 
ATOM   950  C  CB   . THR A 1 51  ? -11.75400 -15.51200 4.90800   1.000 13.38000  ? 51  THR A CB   1 
ATOM   951  O  OG1  . THR A 1 51  ? -13.14300 -15.34900 5.23000   1.000 16.11000  ? 51  THR A OG1  1 
ATOM   952  C  CG2  . THR A 1 51  ? -11.51900 -15.17400 3.44200   1.000 16.38000  ? 51  THR A CG2  1 
ATOM   953  H  H    . THR A 1 51  ? -11.04900 -16.82600 7.16700   1.000 17.06000  ? 51  THR A H    1 
ATOM   954  H  HA   . THR A 1 51  ? -11.83200 -17.54500 4.63800   1.000 15.27000  ? 51  THR A HA   1 
ATOM   955  H  HB   . THR A 1 51  ? -11.21900 -14.89600 5.43300   1.000 16.04000  ? 51  THR A HB   1 
ATOM   956  H  HG1  . THR A 1 51  ? -13.23500 -15.22900 6.05600   1.000 19.32000  ? 51  THR A HG1  1 
ATOM   957  H  HG21 . THR A 1 51  ? -11.86000 -14.28700 3.24700   1.000 19.65000  ? 51  THR A HG21 1 
ATOM   958  H  HG22 . THR A 1 51  ? -10.57000 -15.19700 3.24400   1.000 19.65000  ? 51  THR A HG22 1 
ATOM   959  H  HG23 . THR A 1 51  ? -11.97400 -15.81800 2.87600   1.000 19.65000  ? 51  THR A HG23 1 
ATOM   960  N  N    A ASP A 1 52  ? -9.56700  -17.65900 3.72400   0.620 13.24000  ? 52  ASP A N    1 
ATOM   961  N  N    B ASP A 1 52  ? -9.58800  -17.69000 3.72400   0.380 13.39000  ? 52  ASP A N    1 
ATOM   962  C  CA   A ASP A 1 52  ? -8.19900  -17.86600 3.26200   0.620 13.62000  ? 52  ASP A CA   1 
ATOM   963  C  CA   B ASP A 1 52  ? -8.24200  -17.90000 3.19500   0.380 13.80000  ? 52  ASP A CA   1 
ATOM   964  C  C    A ASP A 1 52  ? -7.84600  -16.79800 2.24100   0.620 12.29000  ? 52  ASP A C    1 
ATOM   965  C  C    B ASP A 1 52  ? -7.87800  -16.75000 2.26200   0.380 12.54000  ? 52  ASP A C    1 
ATOM   966  O  O    A ASP A 1 52  ? -8.66100  -16.45900 1.37300   0.620 14.37000  ? 52  ASP A O    1 
ATOM   967  O  O    B ASP A 1 52  ? -8.71000  -16.30400 1.46200   0.380 14.16000  ? 52  ASP A O    1 
ATOM   968  C  CB   A ASP A 1 52  ? -8.06200  -19.23300 2.60600   0.620 13.90000  ? 52  ASP A CB   1 
ATOM   969  C  CB   B ASP A 1 52  ? -8.20100  -19.19400 2.37600   0.380 14.28000  ? 52  ASP A CB   1 
ATOM   970  C  CG   A ASP A 1 52  ? -8.74400  -20.31200 3.39800   0.620 15.31000  ? 52  ASP A CG   1 
ATOM   971  C  CG   B ASP A 1 52  ? -8.16900  -20.44800 3.23900   0.380 16.10000  ? 52  ASP A CG   1 
ATOM   972  O  OD1  A ASP A 1 52  ? -8.40500  -20.43500 4.58500   0.620 15.14000  ? 52  ASP A OD1  1 
ATOM   973  O  OD1  B ASP A 1 52  ? -7.94300  -20.32700 4.45700   0.380 18.12000  ? 52  ASP A OD1  1 
ATOM   974  O  OD2  A ASP A 1 52  ? -9.64800  -20.97200 2.87200   0.620 19.02000  ? 52  ASP A OD2  1 
ATOM   975  O  OD2  B ASP A 1 52  ? -8.36400  -21.55700 2.68700   0.380 17.56000  ? 52  ASP A OD2  1 
ATOM   976  H  H    A ASP A 1 52  ? -10.16000 -17.86900 3.13800   0.620 15.88000  ? 52  ASP A H    1 
ATOM   977  H  H    B ASP A 1 52  ? -10.19800 -17.92400 3.16400   0.380 16.06000  ? 52  ASP A H    1 
ATOM   978  H  HA   A ASP A 1 52  ? -7.58600  -17.80600 4.01100   0.620 16.33000  ? 52  ASP A HA   1 
ATOM   979  H  HA   B ASP A 1 52  ? -7.60700  -17.94600 3.92700   0.380 16.55000  ? 52  ASP A HA   1 
ATOM   980  H  HB2  A ASP A 1 52  ? -8.46300  -19.20500 1.72400   0.620 16.66000  ? 52  ASP A HB2  1 
ATOM   981  H  HB2  B ASP A 1 52  ? -8.99200  -19.23700 1.81600   0.380 17.12000  ? 52  ASP A HB2  1 
ATOM   982  H  HB3  A ASP A 1 52  ? -7.12100  -19.45800 2.53600   0.620 16.66000  ? 52  ASP A HB3  1 
ATOM   983  H  HB3  B ASP A 1 52  ? -7.40300  -19.19100 1.82300   0.380 17.12000  ? 52  ASP A HB3  1 
ATOM   984  N  N    . TYR A 1 53  ? -6.63500  -16.27400 2.35500   1.000 12.63000  ? 53  TYR A N    1 
ATOM   985  C  CA   . TYR A 1 53  ? -6.20100  -15.10700 1.60700   1.000 12.39000  ? 53  TYR A CA   1 
ATOM   986  C  C    . TYR A 1 53  ? -4.89200  -15.30200 0.86300   1.000 13.47000  ? 53  TYR A C    1 
ATOM   987  O  O    . TYR A 1 53  ? -3.89900  -15.77500 1.42800   1.000 13.70000  ? 53  TYR A O    1 
ATOM   988  C  CB   . TYR A 1 53  ? -5.99100  -13.94600 2.57200   1.000 14.78000  ? 53  TYR A CB   1 
ATOM   989  C  CG   . TYR A 1 53  ? -7.23800  -13.48100 3.31100   1.000 13.69000  ? 53  TYR A CG   1 
ATOM   990  C  CD1  . TYR A 1 53  ? -7.64000  -14.07400 4.51100   1.000 15.82000  ? 53  TYR A CD1  1 
ATOM   991  C  CD2  . TYR A 1 53  ? -8.00700  -12.45100 2.79000   1.000 15.11000  ? 53  TYR A CD2  1 
ATOM   992  C  CE1  . TYR A 1 53  ? -8.77500  -13.64700 5.17400   1.000 14.52000  ? 53  TYR A CE1  1 
ATOM   993  C  CE2  . TYR A 1 53  ? -9.13700  -12.01100 3.43400   1.000 15.18000  ? 53  TYR A CE2  1 
ATOM   994  C  CZ   . TYR A 1 53  ? -9.52100  -12.62300 4.61400   1.000 16.68000  ? 53  TYR A CZ   1 
ATOM   995  O  OH   . TYR A 1 53  ? -10.64900 -12.19300 5.25900   1.000 16.24000  ? 53  TYR A OH   1 
ATOM   996  H  H    . TYR A 1 53  ? -6.02600  -16.58600 2.87700   1.000 15.15000  ? 53  TYR A H    1 
ATOM   997  H  HA   . TYR A 1 53  ? -6.87700  -14.93200 0.93400   1.000 14.85000  ? 53  TYR A HA   1 
ATOM   998  H  HB2  . TYR A 1 53  ? -5.34200  -14.21800 3.24000   1.000 17.72000  ? 53  TYR A HB2  1 
ATOM   999  H  HB3  . TYR A 1 53  ? -5.65200  -13.18800 2.07000   1.000 17.72000  ? 53  TYR A HB3  1 
ATOM   1000 H  HD1  . TYR A 1 53  ? -7.13500  -14.76700 4.86900   1.000 18.97000  ? 53  TYR A HD1  1 
ATOM   1001 H  HD2  . TYR A 1 53  ? -7.75200  -12.05000 1.99000   1.000 18.12000  ? 53  TYR A HD2  1 
ATOM   1002 H  HE1  . TYR A 1 53  ? -9.03100  -14.03800 5.97800   1.000 17.41000  ? 53  TYR A HE1  1 
ATOM   1003 H  HE2  . TYR A 1 53  ? -9.63800  -11.31100 3.08200   1.000 18.21000  ? 53  TYR A HE2  1 
ATOM   1004 H  HH   . TYR A 1 53  ? -11.32400 -12.59000 4.95300   1.000 19.48000  ? 53  TYR A HH   1 
ATOM   1005 N  N    . GLY A 1 54  ? -4.88600  -14.85100 -0.38200  1.000 13.29000  ? 54  GLY A N    1 
ATOM   1006 C  CA   . GLY A 1 54  ? -3.67000  -14.65600 -1.12500  1.000 13.45000  ? 54  GLY A CA   1 
ATOM   1007 C  C    . GLY A 1 54  ? -3.18600  -15.90700 -1.81200  1.000 14.50000  ? 54  GLY A C    1 
ATOM   1008 O  O    . GLY A 1 54  ? -3.85100  -16.94500 -1.90400  1.000 13.55000  ? 54  GLY A O    1 
ATOM   1009 H  H    . GLY A 1 54  ? -5.59500  -14.64700 -0.82400  1.000 15.93000  ? 54  GLY A H    1 
ATOM   1010 H  HA2  . GLY A 1 54  ? -3.81600  -13.97700 -1.80200  1.000 16.13000  ? 54  GLY A HA2  1 
ATOM   1011 H  HA3  . GLY A 1 54  ? -2.97300  -14.35400 -0.52100  1.000 16.13000  ? 54  GLY A HA3  1 
ATOM   1012 N  N    . ILE A 1 55  ? -1.95600  -15.76500 -2.30800  1.000 14.75000  ? 55  ILE A N    1 
ATOM   1013 C  CA   . ILE A 1 55  ? -1.37600  -16.76300 -3.18500  1.000 15.75000  ? 55  ILE A CA   1 
ATOM   1014 C  C    . ILE A 1 55  ? -1.22900  -18.11900 -2.50700  1.000 15.54000  ? 55  ILE A C    1 
ATOM   1015 O  O    . ILE A 1 55  ? -1.27200  -19.15000 -3.18000  1.000 16.81000  ? 55  ILE A O    1 
ATOM   1016 C  CB   . ILE A 1 55  ? -0.05500  -16.23000 -3.75700  1.000 24.63000  ? 55  ILE A CB   1 
ATOM   1017 C  CG1  . ILE A 1 55  ? 0.35300   -17.04000 -4.98200  1.000 30.02000  ? 55  ILE A CG1  1 
ATOM   1018 C  CG2  . ILE A 1 55  ? 1.02000   -16.23300 -2.69900  1.000 20.19000  ? 55  ILE A CG2  1 
ATOM   1019 C  CD1  . ILE A 1 55  ? 0.72800   -16.19900 -6.13700  1.000 29.17000  ? 55  ILE A CD1  1 
ATOM   1020 H  H    . ILE A 1 55  ? -1.44100  -15.09600 -2.14800  1.000 17.69000  ? 55  ILE A H    1 
ATOM   1021 H  HA   . ILE A 1 55  ? -1.98500  -16.91500 -3.92400  1.000 18.88000  ? 55  ILE A HA   1 
ATOM   1022 H  HB   . ILE A 1 55  ? -0.18300  -15.31100 -4.04000  1.000 29.54000  ? 55  ILE A HB   1 
ATOM   1023 H  HG12 . ILE A 1 55  ? 1.11800   -17.59200 -4.75400  1.000 36.02000  ? 55  ILE A HG12 1 
ATOM   1024 H  HG13 . ILE A 1 55  ? -0.39200  -17.60100 -5.25100  1.000 36.02000  ? 55  ILE A HG13 1 
ATOM   1025 H  HG21 . ILE A 1 55  ? 1.82200   -15.82500 -3.06300  1.000 24.22000  ? 55  ILE A HG21 1 
ATOM   1026 H  HG22 . ILE A 1 55  ? 0.71000   -15.72600 -1.93300  1.000 24.22000  ? 55  ILE A HG22 1 
ATOM   1027 H  HG23 . ILE A 1 55  ? 1.20400   -17.14900 -2.43800  1.000 24.22000  ? 55  ILE A HG23 1 
ATOM   1028 H  HD11 . ILE A 1 55  ? 0.90000   -16.77000 -6.90200  1.000 35.00000  ? 55  ILE A HD11 1 
ATOM   1029 H  HD12 . ILE A 1 55  ? -0.00200  -15.59200 -6.33600  1.000 35.00000  ? 55  ILE A HD12 1 
ATOM   1030 H  HD13 . ILE A 1 55  ? 1.52600   -15.69400 -5.91400  1.000 35.00000  ? 55  ILE A HD13 1 
ATOM   1031 N  N    . LEU A 1 56  ? -1.02900  -18.15800 -1.18800  1.000 13.56000  ? 56  LEU A N    1 
ATOM   1032 C  CA   . LEU A 1 56  ? -0.95700  -19.41000 -0.44800  1.000 15.19000  ? 56  LEU A CA   1 
ATOM   1033 C  C    . LEU A 1 56  ? -2.14100  -19.63000 0.48900   1.000 16.61000  ? 56  LEU A C    1 
ATOM   1034 O  O    . LEU A 1 56  ? -2.12300  -20.53900 1.31900   1.000 16.27000  ? 56  LEU A O    1 
ATOM   1035 C  CB   . LEU A 1 56  ? 0.36500   -19.49300 0.30700   1.000 16.13000  ? 56  LEU A CB   1 
ATOM   1036 C  CG   . LEU A 1 56  ? 1.57300   -19.78500 -0.59000  1.000 18.37000  ? 56  LEU A CG   1 
ATOM   1037 C  CD1  . LEU A 1 56  ? 2.83600   -19.44900 0.16700   1.000 21.15000  ? 56  LEU A CD1  1 
ATOM   1038 C  CD2  . LEU A 1 56  ? 1.58100   -21.22600 -1.07700  1.000 23.16000  ? 56  LEU A CD2  1 
ATOM   1039 H  H    . LEU A 1 56  ? -0.93200  -17.46000 -0.69600  1.000 16.26000  ? 56  LEU A H    1 
ATOM   1040 H  HA   . LEU A 1 56  ? -0.98300  -20.14000 -1.08600  1.000 18.21000  ? 56  LEU A HA   1 
ATOM   1041 H  HB2  . LEU A 1 56  ? 0.52300   -18.64400 0.75000   1.000 19.34000  ? 56  LEU A HB2  1 
ATOM   1042 H  HB3  . LEU A 1 56  ? 0.30400   -20.20400 0.96400   1.000 19.34000  ? 56  LEU A HB3  1 
ATOM   1043 H  HG   . LEU A 1 56  ? 1.52500   -19.23600 -1.38800  1.000 22.03000  ? 56  LEU A HG   1 
ATOM   1044 H  HD11 . LEU A 1 56  ? 3.58900   -19.87600 -0.27000  1.000 25.37000  ? 56  LEU A HD11 1 
ATOM   1045 H  HD12 . LEU A 1 56  ? 2.95600   -18.48700 0.16900   1.000 25.37000  ? 56  LEU A HD12 1 
ATOM   1046 H  HD13 . LEU A 1 56  ? 2.75400   -19.77400 1.07800   1.000 25.37000  ? 56  LEU A HD13 1 
ATOM   1047 H  HD21 . LEU A 1 56  ? 2.37900   -21.37500 -1.60900  1.000 27.79000  ? 56  LEU A HD21 1 
ATOM   1048 H  HD22 . LEU A 1 56  ? 1.58000   -21.81900 -0.31000  1.000 27.79000  ? 56  LEU A HD22 1 
ATOM   1049 H  HD23 . LEU A 1 56  ? 0.79000   -21.38200 -1.61700  1.000 27.79000  ? 56  LEU A HD23 1 
ATOM   1050 N  N    . GLN A 1 57  ? -3.21100  -18.87300 0.31700   1.000 13.92000  ? 57  GLN A N    1 
ATOM   1051 C  CA   . GLN A 1 57  ? -4.47400  -19.14200 0.98800   1.000 14.01000  ? 57  GLN A CA   1 
ATOM   1052 C  C    . GLN A 1 57  ? -4.30700  -19.31700 2.50100   1.000 13.92000  ? 57  GLN A C    1 
ATOM   1053 O  O    . GLN A 1 57  ? -4.79300  -20.27200 3.10700   1.000 15.98000  ? 57  GLN A O    1 
ATOM   1054 C  CB   . GLN A 1 57  ? -5.16800  -20.31700 0.31500   1.000 14.00000  ? 57  GLN A CB   1 
ATOM   1055 C  CG   . GLN A 1 57  ? -5.72500  -19.98500 -1.05800  1.000 13.34000  ? 57  GLN A CG   1 
ATOM   1056 C  CD   . GLN A 1 57  ? -6.89800  -19.01400 -0.98800  1.000 16.38000  ? 57  GLN A CD   1 
ATOM   1057 O  OE1  . GLN A 1 57  ? -8.03800  -19.43300 -0.73900  1.000 16.64000  ? 57  GLN A OE1  1 
ATOM   1058 N  NE2  . GLN A 1 57  ? -6.62400  -17.73300 -1.17700  1.000 15.61000  ? 57  GLN A NE2  1 
ATOM   1059 H  H    . GLN A 1 57  ? -3.23300  -18.18200 -0.19400  1.000 16.69000  ? 57  GLN A H    1 
ATOM   1060 H  HA   . GLN A 1 57  ? -5.05300  -18.36800 0.90100   1.000 16.80000  ? 57  GLN A HA   1 
ATOM   1061 H  HB2  . GLN A 1 57  ? -4.53000  -21.04000 0.21100   1.000 16.79000  ? 57  GLN A HB2  1 
ATOM   1062 H  HB3  . GLN A 1 57  ? -5.90700  -20.60600 0.87400   1.000 16.79000  ? 57  GLN A HB3  1 
ATOM   1063 H  HG2  . GLN A 1 57  ? -5.02700  -19.57700 -1.59300  1.000 15.99000  ? 57  GLN A HG2  1 
ATOM   1064 H  HG3  . GLN A 1 57  ? -6.03300  -20.80200 -1.48100  1.000 15.99000  ? 57  GLN A HG3  1 
ATOM   1065 H  HE21 . GLN A 1 57  ? -5.81500  -17.48400 -1.33100  1.000 18.72000  ? 57  GLN A HE21 1 
ATOM   1066 H  HE22 . GLN A 1 57  ? -7.25500  -17.15000 -1.14600  1.000 18.72000  ? 57  GLN A HE22 1 
ATOM   1067 N  N    . ILE A 1 58  ? -3.69400  -18.32800 3.10300   1.000 12.72000  ? 58  ILE A N    1 
ATOM   1068 C  CA   . ILE A 1 58  ? -3.42000  -18.32700 4.53000   1.000 13.35000  ? 58  ILE A CA   1 
ATOM   1069 C  C    . ILE A 1 58  ? -4.69200  -17.92900 5.26200   0.820 11.11000  ? 58  ILE A C    1 
ATOM   1070 O  O    . ILE A 1 58  ? -5.35600  -16.95000 4.90400   1.000 14.89000  ? 58  ILE A O    1 
ATOM   1071 C  CB   . ILE A 1 58  ? -2.25000  -17.38500 4.79600   1.000 17.55000  ? 58  ILE A CB   1 
ATOM   1072 C  CG1  . ILE A 1 58  ? -0.99300  -18.03600 4.20400   0.940 16.34000  ? 58  ILE A CG1  1 
ATOM   1073 C  CG2  . ILE A 1 58  ? -2.11900  -17.06300 6.28800   0.850 16.79000  ? 58  ILE A CG2  1 
ATOM   1074 C  CD1  . ILE A 1 58  ? 0.20600   -17.14300 4.24900   0.900 21.53000  ? 58  ILE A CD1  1 
ATOM   1075 H  H    . ILE A 1 58  ? -3.41400  -17.62100 2.70100   1.000 15.25000  ? 58  ILE A H    1 
ATOM   1076 H  HA   . ILE A 1 58  ? -3.17800  -19.20900 4.85300   1.000 16.01000  ? 58  ILE A HA   1 
ATOM   1077 H  HB   . ILE A 1 58  ? -2.39500  -16.52800 4.36600   0.990 21.05000  ? 58  ILE A HB   1 
ATOM   1078 H  HG12 . ILE A 1 58  ? -0.78700  -18.83800 4.70900   1.000 19.59000  ? 58  ILE A HG12 1 
ATOM   1079 H  HG13 . ILE A 1 58  ? -1.16200  -18.26200 3.27600   1.000 19.59000  ? 58  ILE A HG13 1 
ATOM   1080 H  HG21 . ILE A 1 58  ? -1.32900  -16.51700 6.42500   1.000 20.14000  ? 58  ILE A HG21 1 
ATOM   1081 H  HG22 . ILE A 1 58  ? -2.90900  -16.58100 6.57700   0.940 20.14000  ? 58  ILE A HG22 1 
ATOM   1082 H  HG23 . ILE A 1 58  ? -2.03800  -17.89300 6.78400   1.000 20.14000  ? 58  ILE A HG23 1 
ATOM   1083 H  HD11 . ILE A 1 58  ? 0.84700   -17.44200 3.58500   0.980 25.82000  ? 58  ILE A HD11 1 
ATOM   1084 H  HD12 . ILE A 1 58  ? -0.07000  -16.23400 4.05700   1.000 25.82000  ? 58  ILE A HD12 1 
ATOM   1085 H  HD13 . ILE A 1 58  ? 0.60100   -17.18900 5.13400   0.980 25.82000  ? 58  ILE A HD13 1 
ATOM   1086 N  N    A ASN A 1 59  ? -5.07500  -18.71900 6.26200   0.530 14.86000  ? 59  ASN A N    1 
ATOM   1087 N  N    B ASN A 1 59  ? -4.99300  -18.66500 6.33600   0.350 15.03000  ? 59  ASN A N    1 
ATOM   1088 N  N    C ASN A 1 59  ? -5.04400  -18.68900 6.29600   0.120 15.06000  ? 59  ASN A N    1 
ATOM   1089 C  CA   A ASN A 1 59  ? -6.37400  -18.52200 6.90400   0.530 14.69000  ? 59  ASN A CA   1 
ATOM   1090 C  CA   B ASN A 1 59  ? -6.28800  -18.66500 7.01000   0.350 14.78000  ? 59  ASN A CA   1 
ATOM   1091 C  CA   C ASN A 1 59  ? -6.36600  -18.61100 6.91000   0.120 14.86000  ? 59  ASN A CA   1 
ATOM   1092 C  C    A ASN A 1 59  ? -6.35600  -17.62900 8.15200   0.530 14.80000  ? 59  ASN A C    1 
ATOM   1093 C  C    B ASN A 1 59  ? -6.38200  -17.57600 8.08100   0.350 14.90000  ? 59  ASN A C    1 
ATOM   1094 C  C    C ASN A 1 59  ? -6.35800  -17.71600 8.14700   0.120 14.91000  ? 59  ASN A C    1 
ATOM   1095 O  O    A ASN A 1 59  ? -5.44800  -17.68100 8.97400   0.530 17.85000  ? 59  ASN A O    1 
ATOM   1096 O  O    B ASN A 1 59  ? -5.38100  -17.19100 8.70100   0.350 12.47000  ? 59  ASN A O    1 
ATOM   1097 O  O    C ASN A 1 59  ? -5.50700  -17.86700 9.02800   0.120 16.76000  ? 59  ASN A O    1 
ATOM   1098 C  CB   A ASN A 1 59  ? -6.97900  -19.87900 7.25000   0.530 15.52000  ? 59  ASN A CB   1 
ATOM   1099 C  CB   B ASN A 1 59  ? -6.49700  -20.04200 7.65700   0.350 13.64000  ? 59  ASN A CB   1 
ATOM   1100 C  CB   C ASN A 1 59  ? -6.86200  -20.01500 7.26800   0.120 15.57000  ? 59  ASN A CB   1 
ATOM   1101 C  CG   A ASN A 1 59  ? -6.33600  -20.49700 8.46300   0.530 18.74000  ? 59  ASN A CG   1 
ATOM   1102 C  CG   B ASN A 1 59  ? -7.95100  -20.33400 7.97500   0.350 16.36000  ? 59  ASN A CG   1 
ATOM   1103 C  CG   C ASN A 1 59  ? -7.21400  -20.15800 8.73400   0.120 20.28000  ? 59  ASN A CG   1 
ATOM   1104 O  OD1  A ASN A 1 59  ? -6.55200  -20.04300 9.57400   0.530 18.01000  ? 59  ASN A OD1  1 
ATOM   1105 O  OD1  B ASN A 1 59  ? -8.75700  -19.42900 8.12600   0.350 24.61000  ? 59  ASN A OD1  1 
ATOM   1106 O  OD1  C ASN A 1 59  ? -6.33400  -20.21500 9.59000   0.120 18.17000  ? 59  ASN A OD1  1 
ATOM   1107 N  ND2  A ASN A 1 59  ? -5.54500  -21.53000 8.26300   0.530 17.85000  ? 59  ASN A ND2  1 
ATOM   1108 N  ND2  B ASN A 1 59  ? -8.28500  -21.62200 8.08400   0.350 25.27000  ? 59  ASN A ND2  1 
ATOM   1109 N  ND2  C ASN A 1 59  ? -8.50300  -20.22100 9.02900   0.120 15.22000  ? 59  ASN A ND2  1 
ATOM   1110 H  H    A ASN A 1 59  ? -4.60900  -19.36700 6.58200   0.500 17.81000  ? 59  ASN A H    1 
ATOM   1111 H  H    B ASN A 1 59  ? -4.43200  -19.19900 6.71000   0.300 18.02000  ? 59  ASN A H    1 
ATOM   1112 H  H    C ASN A 1 59  ? -4.52600  -19.26800 6.66500   0.060 18.06000  ? 59  ASN A H    1 
ATOM   1113 H  HA   A ASN A 1 59  ? -6.93200  -18.04900 6.26700   0.530 17.62000  ? 59  ASN A HA   1 
ATOM   1114 H  HA   B ASN A 1 59  ? -6.99000  -18.48100 6.36600   0.350 17.72000  ? 59  ASN A HA   1 
ATOM   1115 H  HA   C ASN A 1 59  ? -6.98000  -18.20300 6.28000   0.120 17.82000  ? 59  ASN A HA   1 
ATOM   1116 H  HB2  A ASN A 1 59  ? -7.92500  -19.76700 7.43300   0.530 18.62000  ? 59  ASN A HB2  1 
ATOM   1117 H  HB2  B ASN A 1 59  ? -6.18000  -20.72800 7.04800   0.350 16.36000  ? 59  ASN A HB2  1 
ATOM   1118 H  HB2  C ASN A 1 59  ? -7.65800  -20.21100 6.74800   0.120 18.68000  ? 59  ASN A HB2  1 
ATOM   1119 H  HB3  A ASN A 1 59  ? -6.85500  -20.48200 6.50100   0.530 18.62000  ? 59  ASN A HB3  1 
ATOM   1120 H  HB3  B ASN A 1 59  ? -5.99600  -20.07900 8.48700   0.350 16.36000  ? 59  ASN A HB3  1 
ATOM   1121 H  HB3  C ASN A 1 59  ? -6.16600  -20.65800 7.06200   0.120 18.68000  ? 59  ASN A HB3  1 
ATOM   1122 H  HD21 A ASN A 1 59  ? -5.15900  -21.91200 8.93000   0.530 21.41000  ? 59  ASN A HD21 1 
ATOM   1123 H  HD21 B ASN A 1 59  ? -9.09700  -21.84200 8.26300   0.350 30.32000  ? 59  ASN A HD21 1 
ATOM   1124 H  HD21 C ASN A 1 59  ? -9.09000  -20.18000 8.40200   0.120 18.25000  ? 59  ASN A HD21 1 
ATOM   1125 H  HD22 A ASN A 1 59  ? -5.41400  -21.82300 7.46500   0.530 21.41000  ? 59  ASN A HD22 1 
ATOM   1126 H  HD22 B ASN A 1 59  ? -7.68800  -22.23200 7.97500   0.350 30.32000  ? 59  ASN A HD22 1 
ATOM   1127 H  HD22 C ASN A 1 59  ? -8.75400  -20.30200 9.84800   0.120 18.25000  ? 59  ASN A HD22 1 
ATOM   1128 N  N    B SER A 1 60  ? -7.61300  -17.07300 8.29100   0.700 12.98000  ? 60  SER A N    1 
ATOM   1129 N  N    C SER A 1 60  ? -7.31200  -16.78700 8.20300   0.300 12.71000  ? 60  SER A N    1 
ATOM   1130 C  CA   B SER A 1 60  ? -7.84500  -16.07100 9.31700   0.700 12.91000  ? 60  SER A CA   1 
ATOM   1131 C  CA   C SER A 1 60  ? -7.53900  -15.94400 9.37800   0.300 12.00000  ? 60  SER A CA   1 
ATOM   1132 C  C    B SER A 1 60  ? -8.12900  -16.68100 10.66900  0.700 16.47000  ? 60  SER A C    1 
ATOM   1133 C  C    C SER A 1 60  ? -8.04200  -16.82000 10.53000  0.300 16.76000  ? 60  SER A C    1 
ATOM   1134 O  O    B SER A 1 60  ? -8.03200  -15.94800 11.66900  0.700 14.43000  ? 60  SER A O    1 
ATOM   1135 O  O    C SER A 1 60  ? -8.64800  -16.33000 11.48000  0.300 17.46000  ? 60  SER A O    1 
ATOM   1136 C  CB   B SER A 1 60  ? -9.01400  -15.17600 8.93400   0.700 12.85000  ? 60  SER A CB   1 
ATOM   1137 C  CB   C SER A 1 60  ? -8.57000  -14.85400 9.04700   0.300 12.96000  ? 60  SER A CB   1 
ATOM   1138 O  OG   B SER A 1 60  ? -10.21000 -15.91900 8.81900   0.700 13.18000  ? 60  SER A OG   1 
ATOM   1139 O  OG   C SER A 1 60  ? -9.84600  -15.41800 8.78400   0.300 12.86000  ? 60  SER A OG   1 
ATOM   1140 H  H    B SER A 1 60  ? -8.31500  -17.30200 7.85200   0.350 15.57000  ? 60  SER A H    1 
ATOM   1141 H  H    C SER A 1 60  ? -7.85600  -16.62000 7.55800   0.120 15.24000  ? 60  SER A H    1 
ATOM   1142 H  HA   B SER A 1 60  ? -7.05300  -15.51500 9.38700   0.700 15.48000  ? 60  SER A HA   1 
ATOM   1143 H  HA   C SER A 1 60  ? -6.72000  -15.50200 9.65000   0.300 14.38000  ? 60  SER A HA   1 
ATOM   1144 H  HB2  B SER A 1 60  ? -9.13000  -14.49900 9.61800   0.700 15.40000  ? 60  SER A HB2  1 
ATOM   1145 H  HB2  C SER A 1 60  ? -8.64200  -14.25000 9.80200   0.300 15.54000  ? 60  SER A HB2  1 
ATOM   1146 H  HB3  B SER A 1 60  ? -8.82300  -14.75600 8.08100   0.700 15.40000  ? 60  SER A HB3  1 
ATOM   1147 H  HB3  C SER A 1 60  ? -8.27300  -14.36900 8.26100   0.300 15.54000  ? 60  SER A HB3  1 
ATOM   1148 H  HG   B SER A 1 60  ? -10.34500 -16.35600 9.52400   0.700 15.81000  ? 60  SER A HG   1 
ATOM   1149 H  HG   C SER A 1 60  ? -10.11600 -15.84400 9.45600   0.300 15.42000  ? 60  SER A HG   1 
ATOM   1150 N  N    A ARG A 1 61  ? -8.18800  -17.99800 10.70300  0.610 16.08000  ? 61  ARG A N    1 
ATOM   1151 N  N    B ARG A 1 61  ? -8.46400  -17.98300 10.68700  0.390 17.50000  ? 61  ARG A N    1 
ATOM   1152 C  CA   A ARG A 1 61  ? -8.51500  -18.62800 11.99800  0.610 19.60000  ? 61  ARG A CA   1 
ATOM   1153 C  CA   B ARG A 1 61  ? -8.71900  -18.73400 11.91500  0.390 16.71000  ? 61  ARG A CA   1 
ATOM   1154 C  C    A ARG A 1 61  ? -7.28600  -18.50000 12.88500  0.610 17.96000  ? 61  ARG A C    1 
ATOM   1155 C  C    B ARG A 1 61  ? -7.50600  -18.74700 12.82700  0.390 15.05000  ? 61  ARG A C    1 
ATOM   1156 O  O    A ARG A 1 61  ? -7.36800  -18.19000 14.08000  0.610 17.42000  ? 61  ARG A O    1 
ATOM   1157 O  O    B ARG A 1 61  ? -7.67600  -18.88000 14.04300  0.390 14.16000  ? 61  ARG A O    1 
ATOM   1158 C  CB   A ARG A 1 61  ? -8.91200  -20.09500 11.78600  0.610 19.68000  ? 61  ARG A CB   1 
ATOM   1159 C  CB   B ARG A 1 61  ? -9.12800  -20.17500 11.56000  0.390 19.28000  ? 61  ARG A CB   1 
ATOM   1160 C  CG   A ARG A 1 61  ? -9.14400  -20.92900 13.05900  0.610 22.76000  ? 61  ARG A CG   1 
ATOM   1161 C  CG   B ARG A 1 61  ? -9.32900  -21.12900 12.74800  0.390 18.17000  ? 61  ARG A CG   1 
ATOM   1162 C  CD   A ARG A 1 61  ? -10.30800 -20.44900 13.89000  0.610 24.87000  ? 61  ARG A CD   1 
ATOM   1163 C  CD   B ARG A 1 61  ? -10.41500 -20.67700 13.68900  0.390 22.03000  ? 61  ARG A CD   1 
ATOM   1164 N  NE   A ARG A 1 61  ? -11.56400 -20.47800 13.15900  0.610 27.06000  ? 61  ARG A NE   1 
ATOM   1165 N  NE   B ARG A 1 61  ? -11.65300 -20.36500 12.99200  0.390 30.09000  ? 61  ARG A NE   1 
ATOM   1166 C  CZ   A ARG A 1 61  ? -12.61200 -19.71700 13.44900  0.610 33.94000  ? 61  ARG A CZ   1 
ATOM   1167 C  CZ   B ARG A 1 61  ? -12.73300 -19.86400 13.57600  0.390 34.40000  ? 61  ARG A CZ   1 
ATOM   1168 N  NH1  A ARG A 1 61  ? -12.61200 -18.91100 14.49600  0.610 33.03000  ? 61  ARG A NH1  1 
ATOM   1169 N  NH1  B ARG A 1 61  ? -12.77100 -19.63500 14.87800  0.390 35.80000  ? 61  ARG A NH1  1 
ATOM   1170 N  NH2  A ARG A 1 61  ? -13.68300 -19.76100 12.66500  0.610 29.89000  ? 61  ARG A NH2  1 
ATOM   1171 N  NH2  B ARG A 1 61  ? -13.80000 -19.58700 12.83400  0.390 30.74000  ? 61  ARG A NH2  1 
ATOM   1172 H  H    A ARG A 1 61  ? -8.36100  -18.49800 10.02500  0.610 19.29000  ? 61  ARG A H    1 
ATOM   1173 H  H    B ARG A 1 61  ? -8.55000  -18.46400 9.97900   0.390 20.99000  ? 61  ARG A H    1 
ATOM   1174 H  HA   A ARG A 1 61  ? -9.27200  -18.20500 12.43300  0.610 23.50000  ? 61  ARG A HA   1 
ATOM   1175 H  HA   B ARG A 1 61  ? -9.45300  -18.32300 12.39900  0.390 20.04000  ? 61  ARG A HA   1 
ATOM   1176 H  HB2  A ARG A 1 61  ? -9.73800  -20.11400 11.27800  0.610 23.60000  ? 61  ARG A HB2  1 
ATOM   1177 H  HB2  B ARG A 1 61  ? -9.96800  -20.14100 11.07500  0.390 23.12000  ? 61  ARG A HB2  1 
ATOM   1178 H  HB3  A ARG A 1 61  ? -8.20400  -20.53000 11.28600  0.610 23.60000  ? 61  ARG A HB3  1 
ATOM   1179 H  HB3  B ARG A 1 61  ? -8.43600  -20.55700 10.99900  0.390 23.12000  ? 61  ARG A HB3  1 
ATOM   1180 H  HG2  A ARG A 1 61  ? -9.32100  -21.84800 12.80400  0.610 27.30000  ? 61  ARG A HG2  1 
ATOM   1181 H  HG2  B ARG A 1 61  ? -9.57100  -22.00600 12.41100  0.390 21.79000  ? 61  ARG A HG2  1 
ATOM   1182 H  HG3  A ARG A 1 61  ? -8.34800  -20.88600 13.61200  0.610 27.30000  ? 61  ARG A HG3  1 
ATOM   1183 H  HG3  B ARG A 1 61  ? -8.50100  -21.18400 13.25200  0.390 21.79000  ? 61  ARG A HG3  1 
ATOM   1184 H  HD2  A ARG A 1 61  ? -10.39900 -21.02200 14.66800  0.610 29.83000  ? 61  ARG A HD2  1 
ATOM   1185 H  HD2  B ARG A 1 61  ? -10.59800 -21.38400 14.32700  0.390 26.42000  ? 61  ARG A HD2  1 
ATOM   1186 H  HD3  A ARG A 1 61  ? -10.14300 -19.53500 14.16900  0.610 29.83000  ? 61  ARG A HD3  1 
ATOM   1187 H  HD3  B ARG A 1 61  ? -10.12100 -19.87900 14.15400  0.390 26.42000  ? 61  ARG A HD3  1 
ATOM   1188 H  HE   A ARG A 1 61  ? -11.63200 -21.02300 12.49700  0.610 32.46000  ? 61  ARG A HE   1 
ATOM   1189 H  HE   B ARG A 1 61  ? -11.68700 -20.51400 12.14600  0.390 36.09000  ? 61  ARG A HE   1 
ATOM   1190 H  HH11 A ARG A 1 61  ? -11.92300 -18.87100 15.00800  0.610 39.63000  ? 61  ARG A HH11 1 
ATOM   1191 H  HH11 B ARG A 1 61  ? -13.48200 -19.31000 15.23700  0.390 42.95000  ? 61  ARG A HH11 1 
ATOM   1192 H  HH12 A ARG A 1 61  ? -13.30200 -18.42600 14.66500  0.610 39.63000  ? 61  ARG A HH12 1 
ATOM   1193 H  HH12 B ARG A 1 61  ? -12.08500 -19.81100 15.36600  0.390 42.95000  ? 61  ARG A HH12 1 
ATOM   1194 H  HH21 A ARG A 1 61  ? -13.69200 -20.27900 11.97800  0.610 35.86000  ? 61  ARG A HH21 1 
ATOM   1195 H  HH21 B ARG A 1 61  ? -13.78400 -19.73200 11.98700  0.390 36.87000  ? 61  ARG A HH21 1 
ATOM   1196 H  HH22 A ARG A 1 61  ? -14.36700 -19.27200 12.84300  0.610 35.86000  ? 61  ARG A HH22 1 
ATOM   1197 H  HH22 B ARG A 1 61  ? -14.50600 -19.26200 13.20100  0.390 36.87000  ? 61  ARG A HH22 1 
ATOM   1198 N  N    A TRP A 1 62  ? -6.12500  -18.71500 12.29800  0.740 16.99000  ? 62  TRP A N    1 
ATOM   1199 N  N    B TRP A 1 62  ? -6.29100  -18.57600 12.27400  0.260 18.04000  ? 62  TRP A N    1 
ATOM   1200 C  CA   A TRP A 1 62  ? -4.90100  -18.72400 13.06900  0.740 17.65000  ? 62  TRP A CA   1 
ATOM   1201 C  CA   B TRP A 1 62  ? -5.06100  -18.66300 13.05800  0.260 17.37000  ? 62  TRP A CA   1 
ATOM   1202 C  C    A TRP A 1 62  ? -3.92800  -17.62400 12.73300  0.740 18.01000  ? 62  TRP A C    1 
ATOM   1203 C  C    B TRP A 1 62  ? -4.00000  -17.61900 12.73000  0.260 17.76000  ? 62  TRP A C    1 
ATOM   1204 O  O    A TRP A 1 62  ? -3.17900  -17.19500 13.60800  0.740 21.94000  ? 62  TRP A O    1 
ATOM   1205 O  O    B TRP A 1 62  ? -3.27700  -17.21000 13.64300  0.260 22.23000  ? 62  TRP A O    1 
ATOM   1206 C  CB   A TRP A 1 62  ? -4.16600  -20.06500 12.88200  0.740 20.42000  ? 62  TRP A CB   1 
ATOM   1207 C  CB   B TRP A 1 62  ? -4.41900  -20.05300 12.90900  0.260 19.85000  ? 62  TRP A CB   1 
ATOM   1208 C  CG   A TRP A 1 62  ? -4.93200  -21.20500 13.40800  0.740 20.18000  ? 62  TRP A CG   1 
ATOM   1209 C  CG   B TRP A 1 62  ? -5.20700  -21.15400 13.52100  0.260 22.08000  ? 62  TRP A CG   1 
ATOM   1210 C  CD1  A TRP A 1 62  ? -5.64800  -22.10200 12.68900  0.740 24.61000  ? 62  TRP A CD1  1 
ATOM   1211 C  CD1  B TRP A 1 62  ? -5.93500  -22.09900 12.86900  0.260 26.37000  ? 62  TRP A CD1  1 
ATOM   1212 C  CD2  A TRP A 1 62  ? -5.08300  -21.57300 14.78000  0.740 24.29000  ? 62  TRP A CD2  1 
ATOM   1213 C  CD2  B TRP A 1 62  ? -5.35200  -21.42500 14.91800  0.260 23.62000  ? 62  TRP A CD2  1 
ATOM   1214 N  NE1  A TRP A 1 62  ? -6.24300  -23.01900 13.52700  0.740 30.18000  ? 62  TRP A NE1  1 
ATOM   1215 N  NE1  B TRP A 1 62  ? -6.52900  -22.94700 13.77500  0.260 28.72000  ? 62  TRP A NE1  1 
ATOM   1216 C  CE2  A TRP A 1 62  ? -5.90700  -22.71000 14.81800  0.740 28.43000  ? 62  TRP A CE2  1 
ATOM   1217 C  CE2  B TRP A 1 62  ? -6.18500  -22.55100 15.04100  0.260 30.58000  ? 62  TRP A CE2  1 
ATOM   1218 C  CE3  A TRP A 1 62  ? -4.59300  -21.05100 15.97700  0.740 29.84000  ? 62  TRP A CE3  1 
ATOM   1219 C  CE3  B TRP A 1 62  ? -4.85800  -20.82000 16.07700  0.260 29.62000  ? 62  TRP A CE3  1 
ATOM   1220 C  CZ2  A TRP A 1 62  ? -6.25300  -23.34000 16.01200  0.740 45.58000  ? 62  TRP A CZ2  1 
ATOM   1221 C  CZ2  B TRP A 1 62  ? -6.53500  -23.08900 16.27800  0.260 40.97000  ? 62  TRP A CZ2  1 
ATOM   1222 C  CZ3  A TRP A 1 62  ? -4.93600  -21.67300 17.15900  0.740 39.59000  ? 62  TRP A CZ3  1 
ATOM   1223 C  CZ3  B TRP A 1 62  ? -5.20400  -21.35300 17.30200  0.260 38.37000  ? 62  TRP A CZ3  1 
ATOM   1224 C  CH2  A TRP A 1 62  ? -5.75800  -22.80400 17.16900  0.740 43.53000  ? 62  TRP A CH2  1 
ATOM   1225 C  CH2  B TRP A 1 62  ? -6.03500  -22.47500 17.39400  0.260 42.51000  ? 62  TRP A CH2  1 
ATOM   1226 H  H    A TRP A 1 62  ? -6.02100  -18.85700 11.45600  0.610 20.37000  ? 62  TRP A H    1 
ATOM   1227 H  H    B TRP A 1 62  ? -6.15900  -18.40800 11.44100  0.390 21.64000  ? 62  TRP A H    1 
ATOM   1228 H  HA   A TRP A 1 62  ? -5.14600  -18.62000 14.00200  0.740 21.17000  ? 62  TRP A HA   1 
ATOM   1229 H  HA   B TRP A 1 62  ? -5.30800  -18.53400 13.98700  0.260 20.83000  ? 62  TRP A HA   1 
ATOM   1230 H  HB2  A TRP A 1 62  ? -4.01600  -20.21400 11.93500  0.740 24.49000  ? 62  TRP A HB2  1 
ATOM   1231 H  HB2  B TRP A 1 62  ? -4.32100  -20.25100 11.96500  0.260 23.81000  ? 62  TRP A HB2  1 
ATOM   1232 H  HB3  A TRP A 1 62  ? -3.31800  -20.02900 13.35100  0.740 24.49000  ? 62  TRP A HB3  1 
ATOM   1233 H  HB3  B TRP A 1 62  ? -3.54800  -20.04100 13.33700  0.260 23.81000  ? 62  TRP A HB3  1 
ATOM   1234 H  HD1  A TRP A 1 62  ? -5.72700  -22.09900 11.76200  0.740 29.52000  ? 62  TRP A HD1  1 
ATOM   1235 H  HD1  B TRP A 1 62  ? -6.02000  -22.16200 11.94500  0.260 31.63000  ? 62  TRP A HD1  1 
ATOM   1236 H  HE1  A TRP A 1 62  ? -6.74200  -23.67500 13.28000  0.740 36.21000  ? 62  TRP A HE1  1 
ATOM   1237 H  HE1  B TRP A 1 62  ? -7.03300  -23.61600 13.57900  0.260 34.46000  ? 62  TRP A HE1  1 
ATOM   1238 H  HE3  A TRP A 1 62  ? -4.04600  -20.29800 15.97900  0.740 35.80000  ? 62  TRP A HE3  1 
ATOM   1239 H  HE3  B TRP A 1 62  ? -4.30600  -20.07400 16.02400  0.260 35.53000  ? 62  TRP A HE3  1 
ATOM   1240 H  HZ2  A TRP A 1 62  ? -6.79900  -24.09300 16.02200  0.740 54.69000  ? 62  TRP A HZ2  1 
ATOM   1241 H  HZ2  B TRP A 1 62  ? -7.08600  -23.83500 16.34200  0.260 49.15000  ? 62  TRP A HZ2  1 
ATOM   1242 H  HZ3  A TRP A 1 62  ? -4.61500  -21.33500 17.96300  0.740 47.50000  ? 62  TRP A HZ3  1 
ATOM   1243 H  HZ3  B TRP A 1 62  ? -4.88000  -20.95900 18.08000  0.260 46.03000  ? 62  TRP A HZ3  1 
ATOM   1244 H  HH2  A TRP A 1 62  ? -5.97300  -23.20200 17.98200  0.740 52.22000  ? 62  TRP A HH2  1 
ATOM   1245 H  HH2  B TRP A 1 62  ? -6.25200  -22.81200 18.23300  0.260 51.00000  ? 62  TRP A HH2  1 
ATOM   1246 N  N    . TRP A 1 63  ? -3.85400  -17.16900 11.47700  1.000 15.22000  ? 63  TRP A N    1 
ATOM   1247 C  CA   . TRP A 1 63  ? -2.63600  -16.51500 11.03700  1.000 16.09000  ? 63  TRP A CA   1 
ATOM   1248 C  C    . TRP A 1 63  ? -2.72000  -15.03700 10.74400  1.000 16.54000  ? 63  TRP A C    1 
ATOM   1249 O  O    . TRP A 1 63  ? -1.68600  -14.36100 10.72300  1.000 18.91000  ? 63  TRP A O    1 
ATOM   1250 C  CB   . TRP A 1 63  ? -2.10100  -17.20900 9.77000   1.000 16.86000  ? 63  TRP A CB   1 
ATOM   1251 C  CG   . TRP A 1 63  ? -1.92700  -18.68300 10.00600  1.000 15.92000  ? 63  TRP A CG   1 
ATOM   1252 C  CD1  . TRP A 1 63  ? -2.71300  -19.67700 9.55800   1.000 18.69000  ? 63  TRP A CD1  1 
ATOM   1253 C  CD2  . TRP A 1 63  ? -0.93200  -19.29800 10.84100  1.000 17.01000  ? 63  TRP A CD2  1 
ATOM   1254 N  NE1  . TRP A 1 63  ? -2.27800  -20.88600 10.05000  1.000 20.25000  ? 63  TRP A NE1  1 
ATOM   1255 C  CE2  . TRP A 1 63  ? -1.18500  -20.66900 10.83600  1.000 17.41000  ? 63  TRP A CE2  1 
ATOM   1256 C  CE3  . TRP A 1 63  ? 0.15300   -18.81100 11.56200  1.000 18.58000  ? 63  TRP A CE3  1 
ATOM   1257 C  CZ2  . TRP A 1 63  ? -0.37600  -21.58500 11.52200  1.000 19.49000  ? 63  TRP A CZ2  1 
ATOM   1258 C  CZ3  . TRP A 1 63  ? 0.95100   -19.72500 12.25400  1.000 20.44000  ? 63  TRP A CZ3  1 
ATOM   1259 C  CH2  . TRP A 1 63  ? 0.67700   -21.08300 12.21500  1.000 20.27000  ? 63  TRP A CH2  1 
ATOM   1260 H  H    . TRP A 1 63  ? -4.47800  -17.22800 10.88800  1.000 18.25000  ? 63  TRP A H    1 
ATOM   1261 H  HA   . TRP A 1 63  ? -2.00100  -16.60700 11.76400  1.000 19.30000  ? 63  TRP A HA   1 
ATOM   1262 H  HB2  . TRP A 1 63  ? -2.73000  -17.08500 9.04200   1.000 20.22000  ? 63  TRP A HB2  1 
ATOM   1263 H  HB3  . TRP A 1 63  ? -1.24000  -16.83000 9.53200   1.000 20.22000  ? 63  TRP A HB3  1 
ATOM   1264 H  HD1  . TRP A 1 63  ? -3.44500  -19.56400 8.99600   1.000 22.42000  ? 63  TRP A HD1  1 
ATOM   1265 H  HE1  . TRP A 1 63  ? -2.63600  -21.65100 9.88900   1.000 24.28000  ? 63  TRP A HE1  1 
ATOM   1266 H  HE3  . TRP A 1 63  ? 0.34200   -17.90100 11.58400  1.000 22.28000  ? 63  TRP A HE3  1 
ATOM   1267 H  HZ2  . TRP A 1 63  ? -0.55400  -22.49800 11.50400  1.000 23.38000  ? 63  TRP A HZ2  1 
ATOM   1268 H  HZ3  . TRP A 1 63  ? 1.67800   -19.41800 12.74700  1.000 24.51000  ? 63  TRP A HZ3  1 
ATOM   1269 H  HH2  . TRP A 1 63  ? 1.23200   -21.66800 12.67800  1.000 24.32000  ? 63  TRP A HH2  1 
ATOM   1270 N  N    . CYS A 1 64  ? -3.91300  -14.51100 10.49900  1.000 16.29000  ? 64  CYS A N    1 
ATOM   1271 C  CA   . CYS A 1 64  ? -4.02300  -13.09500 10.17900  1.000 17.58000  ? 64  CYS A CA   1 
ATOM   1272 C  C    . CYS A 1 64  ? -5.32000  -12.55000 10.75100  1.000 14.24000  ? 64  CYS A C    1 
ATOM   1273 O  O    . CYS A 1 64  ? -6.22100  -13.29400 11.08400  1.000 15.88000  ? 64  CYS A O    1 
ATOM   1274 C  CB   . CYS A 1 64  ? -3.91700  -12.84100 8.65000   1.000 16.39000  ? 64  CYS A CB   1 
ATOM   1275 S  SG   . CYS A 1 64  ? -5.16700  -13.59100 7.64200   1.000 15.68000  ? 64  CYS A SG   1 
ATOM   1276 H  H    . CYS A 1 64  ? -4.65600  -14.94400 10.51200  1.000 19.53000  ? 64  CYS A H    1 
ATOM   1277 H  HA   . CYS A 1 64  ? -3.29400  -12.61900 10.60800  1.000 21.09000  ? 64  CYS A HA   1 
ATOM   1278 H  HB2  . CYS A 1 64  ? -3.96400  -11.88400 8.50000   1.000 19.65000  ? 64  CYS A HB2  1 
ATOM   1279 H  HB3  . CYS A 1 64  ? -3.06100  -13.18200 8.34600   1.000 19.65000  ? 64  CYS A HB3  1 
ATOM   1280 N  N    . ASN A 1 65  ? -5.41200  -11.22100 10.79300  1.000 17.20000  ? 65  ASN A N    1 
ATOM   1281 C  CA   . ASN A 1 65  ? -6.60600  -10.57100 11.30800  1.000 17.44000  ? 65  ASN A CA   1 
ATOM   1282 C  C    . ASN A 1 65  ? -7.41800  -9.96100  10.17600  1.000 14.29000  ? 65  ASN A C    1 
ATOM   1283 O  O    . ASN A 1 65  ? -6.91400  -9.13100  9.43200   1.000 16.50000  ? 65  ASN A O    1 
ATOM   1284 C  CB   . ASN A 1 65  ? -6.25500  -9.47800  12.30800  1.000 17.90000  ? 65  ASN A CB   1 
ATOM   1285 C  CG   . ASN A 1 65  ? -7.48500  -8.77700  12.79900  1.000 22.77000  ? 65  ASN A CG   1 
ATOM   1286 O  OD1  . ASN A 1 65  ? -8.40000  -9.41800  13.30900  1.000 27.60000  ? 65  ASN A OD1  1 
ATOM   1287 N  ND2  . ASN A 1 65  ? -7.55100  -7.48000  12.57900  1.000 34.23000  ? 65  ASN A ND2  1 
ATOM   1288 H  H    . ASN A 1 65  ? -4.79700  -10.68100 10.52900  1.000 20.63000  ? 65  ASN A H    1 
ATOM   1289 H  HA   . ASN A 1 65  ? -7.14400  -11.25300 11.74000  1.000 20.91000  ? 65  ASN A HA   1 
ATOM   1290 H  HB2  . ASN A 1 65  ? -5.80300  -9.87200  13.07000  1.000 21.47000  ? 65  ASN A HB2  1 
ATOM   1291 H  HB3  . ASN A 1 65  ? -5.68000  -8.82400  11.88200  1.000 21.47000  ? 65  ASN A HB3  1 
ATOM   1292 H  HD21 . ASN A 1 65  ? -6.90800  -7.07900  12.17200  1.000 41.06000  ? 65  ASN A HD21 1 
ATOM   1293 H  HD22 . ASN A 1 65  ? -8.23800  -7.03300  12.84200  1.000 41.06000  ? 65  ASN A HD22 1 
ATOM   1294 N  N    . ASP A 1 66  ? -8.66500  -10.37700 10.06500  1.000 15.53000  ? 66  ASP A N    1 
ATOM   1295 C  CA   . ASP A 1 66  ? -9.57500  -9.77900  9.10100   1.000 15.85000  ? 66  ASP A CA   1 
ATOM   1296 C  C    . ASP A 1 66  ? -10.75300 -9.09500  9.76000   1.000 17.12000  ? 66  ASP A C    1 
ATOM   1297 O  O    . ASP A 1 66  ? -11.63300 -8.61600  9.03700   1.000 19.85000  ? 66  ASP A O    1 
ATOM   1298 C  CB   . ASP A 1 66  ? -10.03400 -10.76600 8.01400   1.000 15.43000  ? 66  ASP A CB   1 
ATOM   1299 C  CG   . ASP A 1 66  ? -10.85300 -11.92600 8.52600   1.000 15.88000  ? 66  ASP A CG   1 
ATOM   1300 O  OD1  . ASP A 1 66  ? -11.25700 -11.93800 9.71800   1.000 17.05000  ? 66  ASP A OD1  1 
ATOM   1301 O  OD2  . ASP A 1 66  ? -11.20300 -12.82800 7.71900   1.000 14.98000  ? 66  ASP A OD2  1 
ATOM   1302 H  H    . ASP A 1 66  ? -9.01100  -11.00700 10.53700  1.000 18.63000  ? 66  ASP A H    1 
ATOM   1303 H  HA   . ASP A 1 66  ? -9.07400  -9.10000  8.62200   1.000 19.00000  ? 66  ASP A HA   1 
ATOM   1304 H  HB2  . ASP A 1 66  ? -10.57800 -10.28500 7.37100   1.000 18.51000  ? 66  ASP A HB2  1 
ATOM   1305 H  HB3  . ASP A 1 66  ? -9.24900  -11.13200 7.57800   1.000 18.51000  ? 66  ASP A HB3  1 
ATOM   1306 N  N    . GLY A 1 67  ? -10.76500 -9.01900  11.08600  1.000 18.95000  ? 67  GLY A N    1 
ATOM   1307 C  CA   . GLY A 1 67  ? -11.82100 -8.34400  11.82700  1.000 17.78000  ? 67  GLY A CA   1 
ATOM   1308 C  C    . GLY A 1 67  ? -13.15500 -9.03700  11.83500  1.000 24.87000  ? 67  GLY A C    1 
ATOM   1309 O  O    . GLY A 1 67  ? -14.12000 -8.47900  12.36900  1.000 25.94000  ? 67  GLY A O    1 
ATOM   1310 H  H    . GLY A 1 67  ? -10.15800 -9.35900  11.59200  1.000 22.73000  ? 67  GLY A H    1 
ATOM   1311 H  HA2  . GLY A 1 67  ? -11.53700 -8.24700  12.74900  1.000 21.32000  ? 67  GLY A HA2  1 
ATOM   1312 H  HA3  . GLY A 1 67  ? -11.95200 -7.46300  11.44300  1.000 21.32000  ? 67  GLY A HA3  1 
ATOM   1313 N  N    . ARG A 1 68  ? -13.26300 -10.24200 11.29100  1.000 19.35000  ? 68  ARG A N    1 
ATOM   1314 C  CA   . ARG A 1 68  ? -14.56300 -10.89100 11.22700  1.000 18.86000  ? 68  ARG A CA   1 
ATOM   1315 C  C    . ARG A 1 68  ? -14.50900 -12.39500 11.45800  1.000 23.50000  ? 68  ARG A C    1 
ATOM   1316 O  O    . ARG A 1 68  ? -15.39500 -13.11800 10.99800  1.000 27.34000  ? 68  ARG A O    1 
ATOM   1317 C  CB   . ARG A 1 68  ? -15.24400 -10.58400 9.89200   1.000 21.32000  ? 68  ARG A CB   1 
ATOM   1318 C  CG   . ARG A 1 68  ? -14.47200 -11.10200 8.69300   1.000 19.56000  ? 68  ARG A CG   1 
ATOM   1319 C  CD   . ARG A 1 68  ? -15.35700 -11.20600 7.51000   1.000 27.56000  ? 68  ARG A CD   1 
ATOM   1320 N  NE   . ARG A 1 68  ? -14.90300 -12.19800 6.55400   1.000 26.25000  ? 68  ARG A NE   1 
ATOM   1321 C  CZ   . ARG A 1 68  ? -15.39300 -12.28600 5.32600   1.000 25.89000  ? 68  ARG A CZ   1 
ATOM   1322 N  NH1  . ARG A 1 68  ? -16.31000 -11.44100 4.90100   1.000 26.10000  ? 68  ARG A NH1  1 
ATOM   1323 N  NH2  . ARG A 1 68  ? -14.98400 -13.26800 4.51800   1.000 24.07000  ? 68  ARG A NH2  1 
ATOM   1324 H  H    . ARG A 1 68  ? -12.61200 -10.69500 10.95900  1.000 23.21000  ? 68  ARG A H    1 
ATOM   1325 H  HA   . ARG A 1 68  ? -15.11200 -10.53300 11.94300  1.000 22.62000  ? 68  ARG A HA   1 
ATOM   1326 H  HB2  . ARG A 1 68  ? -16.12100 -10.99900 9.88500   1.000 25.57000  ? 68  ARG A HB2  1 
ATOM   1327 H  HB3  . ARG A 1 68  ? -15.33200 -9.62300  9.79800   1.000 25.57000  ? 68  ARG A HB3  1 
ATOM   1328 H  HG2  . ARG A 1 68  ? -13.74800 -10.49100 8.48400   1.000 23.46000  ? 68  ARG A HG2  1 
ATOM   1329 H  HG3  . ARG A 1 68  ? -14.11700 -11.98200 8.89100   1.000 23.46000  ? 68  ARG A HG3  1 
ATOM   1330 H  HD2  . ARG A 1 68  ? -16.24700 -11.45600 7.80300   1.000 33.06000  ? 68  ARG A HD2  1 
ATOM   1331 H  HD3  . ARG A 1 68  ? -15.38500 -10.34700 7.06000   1.000 33.06000  ? 68  ARG A HD3  1 
ATOM   1332 H  HE   . ARG A 1 68  ? -14.29100 -12.75200 6.79400   1.000 31.48000  ? 68  ARG A HE   1 
ATOM   1333 H  HH11 . ARG A 1 68  ? -16.59900 -10.82100 5.42200   1.000 31.31000  ? 68  ARG A HH11 1 
ATOM   1334 H  HH12 . ARG A 1 68  ? -16.62000 -11.51000 4.10200   1.000 31.31000  ? 68  ARG A HH12 1 
ATOM   1335 H  HH21 . ARG A 1 68  ? -14.40400 -13.83900 4.79600   1.000 28.87000  ? 68  ARG A HH21 1 
ATOM   1336 H  HH22 . ARG A 1 68  ? -15.30000 -13.32800 3.72100   1.000 28.87000  ? 68  ARG A HH22 1 
ATOM   1337 N  N    . THR A 1 69  ? -13.47800 -12.89500 12.12400  1.000 19.87000  ? 69  THR A N    1 
ATOM   1338 C  CA   . THR A 1 69  ? -13.35600 -14.31600 12.41800  1.000 18.98000  ? 69  THR A CA   1 
ATOM   1339 C  C    . THR A 1 69  ? -13.35700 -14.50600 13.92800  1.000 20.17000  ? 69  THR A C    1 
ATOM   1340 O  O    . THR A 1 69  ? -12.28800 -14.50900 14.56800  1.000 23.58000  ? 69  THR A O    1 
ATOM   1341 C  CB   . THR A 1 69  ? -12.09900 -14.89800 11.79000  1.000 23.79000  ? 69  THR A CB   1 
ATOM   1342 O  OG1  . THR A 1 69  ? -12.06300 -14.54200 10.40400  1.000 19.51000  ? 69  THR A OG1  1 
ATOM   1343 C  CG2  . THR A 1 69  ? -12.12500 -16.39600 11.90100  1.000 21.22000  ? 69  THR A CG2  1 
ATOM   1344 H  H    . THR A 1 69  ? -12.82300 -12.42200 12.42000  1.000 23.83000  ? 69  THR A H    1 
ATOM   1345 H  HA   . THR A 1 69  ? -14.12500 -14.78400 12.05600  1.000 22.77000  ? 69  THR A HA   1 
ATOM   1346 H  HB   . THR A 1 69  ? -11.31000 -14.55800 12.24100  1.000 28.54000  ? 69  THR A HB   1 
ATOM   1347 H  HG1  . THR A 1 69  ? -12.74100 -14.84500 10.01200  1.000 23.40000  ? 69  THR A HG1  1 
ATOM   1348 H  HG21 . THR A 1 69  ? -11.26400 -16.76200 11.64700  1.000 25.45000  ? 69  THR A HG21 1 
ATOM   1349 H  HG22 . THR A 1 69  ? -12.32100 -16.65700 12.81400  1.000 25.45000  ? 69  THR A HG22 1 
ATOM   1350 H  HG23 . THR A 1 69  ? -12.80700 -16.76000 11.31600  1.000 25.45000  ? 69  THR A HG23 1 
ATOM   1351 N  N    . PRO A 1 70  ? -14.53800 -14.61400 14.54300  1.000 22.52000  ? 70  PRO A N    1 
ATOM   1352 C  CA   . PRO A 1 70  ? -14.60100 -14.66400 16.00900  1.000 23.71000  ? 70  PRO A CA   1 
ATOM   1353 C  C    . PRO A 1 70  ? -13.84100 -15.84700 16.56800  1.000 23.54000  ? 70  PRO A C    1 
ATOM   1354 O  O    . PRO A 1 70  ? -13.93900 -16.97300 16.06800  1.000 31.66000  ? 70  PRO A O    1 
ATOM   1355 C  CB   . PRO A 1 70  ? -16.10400 -14.80600 16.28200  1.000 26.14000  ? 70  PRO A CB   1 
ATOM   1356 C  CG   . PRO A 1 70  ? -16.75500 -14.11100 15.13900  1.000 30.91000  ? 70  PRO A CG   1 
ATOM   1357 C  CD   . PRO A 1 70  ? -15.87400 -14.48400 13.94500  1.000 27.40000  ? 70  PRO A CD   1 
ATOM   1358 H  HA   . PRO A 1 70  ? -14.25500 -13.84200 16.39100  1.000 28.44000  ? 70  PRO A HA   1 
ATOM   1359 H  HB2  . PRO A 1 70  ? -16.35000 -15.74400 16.30700  1.000 31.36000  ? 70  PRO A HB2  1 
ATOM   1360 H  HB3  . PRO A 1 70  ? -16.33000 -14.38000 17.12400  1.000 31.36000  ? 70  PRO A HB3  1 
ATOM   1361 H  HG2  . PRO A 1 70  ? -17.66200 -14.43500 15.02200  1.000 37.07000  ? 70  PRO A HG2  1 
ATOM   1362 H  HG3  . PRO A 1 70  ? -16.76100 -13.15300 15.28700  1.000 37.07000  ? 70  PRO A HG3  1 
ATOM   1363 H  HD2  . PRO A 1 70  ? -16.16000 -15.32300 13.55200  1.000 32.87000  ? 70  PRO A HD2  1 
ATOM   1364 H  HD3  . PRO A 1 70  ? -15.88500 -13.78300 13.27400  1.000 32.87000  ? 70  PRO A HD3  1 
ATOM   1365 N  N    . GLY A 1 71  ? -13.10600 -15.58600 17.64400  1.000 28.50000  ? 71  GLY A N    1 
ATOM   1366 C  CA   . GLY A 1 71  ? -12.40100 -16.63100 18.34400  1.000 31.23000  ? 71  GLY A CA   1 
ATOM   1367 C  C    . GLY A 1 71  ? -11.09800 -17.03600 17.69900  1.000 38.58000  ? 71  GLY A C    1 
ATOM   1368 O  O    . GLY A 1 71  ? -10.53600 -18.07300 18.06700  1.000 53.58000  ? 71  GLY A O    1 
ATOM   1369 H  H    . GLY A 1 71  ? -13.00300 -14.80300 17.98500  1.000 34.19000  ? 71  GLY A H    1 
ATOM   1370 H  HA2  . GLY A 1 71  ? -12.20800 -16.33000 19.24500  1.000 37.47000  ? 71  GLY A HA2  1 
ATOM   1371 H  HA3  . GLY A 1 71  ? -12.96900 -17.41600 18.38900  1.000 37.47000  ? 71  GLY A HA3  1 
ATOM   1372 N  N    . SER A 1 72  ? -10.60200 -16.24800 16.75400  1.000 29.37000  ? 72  SER A N    1 
ATOM   1373 C  CA   . SER A 1 72  ? -9.43000  -16.60300 15.96700  1.000 23.64000  ? 72  SER A CA   1 
ATOM   1374 C  C    . SER A 1 72  ? -8.17600  -15.98000 16.57200  1.000 24.89000  ? 72  SER A C    1 
ATOM   1375 O  O    . SER A 1 72  ? -8.23400  -15.20600 17.52900  1.000 27.57000  ? 72  SER A O    1 
ATOM   1376 C  CB   . SER A 1 72  ? -9.62800  -16.11300 14.52300  1.000 20.11000  ? 72  SER A CB   1 
ATOM   1377 O  OG   . SER A 1 72  ? -9.49000  -14.71300 14.44500  1.000 21.56000  ? 72  SER A OG   1 
ATOM   1378 H  H    . SER A 1 72  ? -10.93500 -15.48400 16.54500  1.000 35.23000  ? 72  SER A H    1 
ATOM   1379 H  HA   . SER A 1 72  ? -9.31000  -17.56500 15.96200  1.000 28.36000  ? 72  SER A HA   1 
ATOM   1380 H  HB2  . SER A 1 72  ? -8.96100  -16.52900 13.95400  1.000 24.12000  ? 72  SER A HB2  1 
ATOM   1381 H  HB3  . SER A 1 72  ? -10.51800 -16.36000 14.22500  1.000 24.12000  ? 72  SER A HB3  1 
ATOM   1382 H  HG   . SER A 1 72  ? -10.22300 -14.36300 14.23300  1.000 25.86000  ? 72  SER A HG   1 
ATOM   1383 N  N    . ARG A 1 73  ? -7.02300  -16.34800 16.01600  1.000 22.03000  ? 73  ARG A N    1 
ATOM   1384 C  CA   . ARG A 1 73  ? -5.74500  -15.76700 16.36500  1.000 19.43000  ? 73  ARG A CA   1 
ATOM   1385 C  C    . ARG A 1 73  ? -5.15600  -15.03100 15.16000  1.000 23.10000  ? 73  ARG A C    1 
ATOM   1386 O  O    . ARG A 1 73  ? -5.71300  -15.05700 14.05800  1.000 22.73000  ? 73  ARG A O    1 
ATOM   1387 C  CB   . ARG A 1 73  ? -4.77500  -16.85300 16.86400  1.000 25.18000  ? 73  ARG A CB   1 
ATOM   1388 C  CG   . ARG A 1 73  ? -5.35900  -17.77200 17.95800  1.000 25.97000  ? 73  ARG A CG   1 
ATOM   1389 C  CD   . ARG A 1 73  ? -5.56200  -17.01200 19.26200  1.000 43.55000  ? 73  ARG A CD   1 
ATOM   1390 N  NE   . ARG A 1 73  ? -4.32200  -16.41700 19.74100  1.000 54.67000  ? 73  ARG A NE   1 
ATOM   1391 C  CZ   . ARG A 1 73  ? -3.47700  -17.00500 20.58000  1.000 75.35000  ? 73  ARG A CZ   1 
ATOM   1392 N  NH1  . ARG A 1 73  ? -3.71400  -18.21100 21.07600  1.000 38.61000  ? 73  ARG A NH1  1 
ATOM   1393 N  NH2  . ARG A 1 73  ? -2.36300  -16.37000 20.92500  1.000 41.49000  ? 73  ARG A NH2  1 
ATOM   1394 H  H    . ARG A 1 73  ? -6.96300  -16.95700 15.41200  1.000 26.42000  ? 73  ARG A H    1 
ATOM   1395 H  HA   . ARG A 1 73  ? -5.88200  -15.12000 17.07600  1.000 23.30000  ? 73  ARG A HA   1 
ATOM   1396 H  HB2  . ARG A 1 73  ? -4.52400  -17.41300 16.11300  1.000 30.20000  ? 73  ARG A HB2  1 
ATOM   1397 H  HB3  . ARG A 1 73  ? -3.98800  -16.42100 17.23300  1.000 30.20000  ? 73  ARG A HB3  1 
ATOM   1398 H  HG2  . ARG A 1 73  ? -6.21800  -18.11600 17.66600  1.000 31.16000  ? 73  ARG A HG2  1 
ATOM   1399 H  HG3  . ARG A 1 73  ? -4.74700  -18.50600 18.12300  1.000 31.16000  ? 73  ARG A HG3  1 
ATOM   1400 H  HD2  . ARG A 1 73  ? -6.20600  -16.30000 19.12000  1.000 52.25000  ? 73  ARG A HD2  1 
ATOM   1401 H  HD3  . ARG A 1 73  ? -5.88900  -17.62300 19.94100  1.000 52.25000  ? 73  ARG A HD3  1 
ATOM   1402 H  HE   . ARG A 1 73  ? -4.12300  -15.62900 19.46100  1.000 65.59000  ? 73  ARG A HE   1 
ATOM   1403 H  HH11 . ARG A 1 73  ? -4.43000  -18.63400 20.85600  1.000 46.32000  ? 73  ARG A HH11 1 
ATOM   1404 H  HH12 . ARG A 1 73  ? -3.15100  -18.57100 21.61800  1.000 46.32000  ? 73  ARG A HH12 1 
ATOM   1405 H  HH21 . ARG A 1 73  ? -2.19700  -15.58900 20.60600  1.000 49.78000  ? 73  ARG A HH21 1 
ATOM   1406 H  HH22 . ARG A 1 73  ? -1.80800  -16.74000 21.46700  1.000 49.78000  ? 73  ARG A HH22 1 
ATOM   1407 N  N    . ASN A 1 74  ? -4.02100  -14.37800 15.38000  1.000 22.05000  ? 74  ASN A N    1 
ATOM   1408 C  CA   . ASN A 1 74  ? -3.32300  -13.56600 14.38300  1.000 19.38000  ? 74  ASN A CA   1 
ATOM   1409 C  C    . ASN A 1 74  ? -1.82600  -13.81000 14.57200  1.000 20.43000  ? 74  ASN A C    1 
ATOM   1410 O  O    . ASN A 1 74  ? -1.04400  -12.92600 14.89900  1.000 22.29000  ? 74  ASN A O    1 
ATOM   1411 C  CB   . ASN A 1 74  ? -3.67600  -12.08600 14.53200  1.000 19.85000  ? 74  ASN A CB   1 
ATOM   1412 C  CG   . ASN A 1 74  ? -2.93600  -11.18800 13.55200  1.000 23.71000  ? 74  ASN A CG   1 
ATOM   1413 O  OD1  . ASN A 1 74  ? -2.34300  -11.64700 12.56500  1.000 22.75000  ? 74  ASN A OD1  1 
ATOM   1414 N  ND2  . ASN A 1 74  ? -2.97700  -9.89500  13.80700  1.000 27.38000  ? 74  ASN A ND2  1 
ATOM   1415 H  H    . ASN A 1 74  ? -3.61300  -14.38900 16.13700  1.000 26.44000  ? 74  ASN A H    1 
ATOM   1416 H  HA   . ASN A 1 74  ? -3.58500  -13.83700 13.49000  1.000 23.24000  ? 74  ASN A HA   1 
ATOM   1417 H  HB2  . ASN A 1 74  ? -4.62700  -11.97400 14.37800  1.000 23.80000  ? 74  ASN A HB2  1 
ATOM   1418 H  HB3  . ASN A 1 74  ? -3.44900  -11.79800 15.42900  1.000 23.80000  ? 74  ASN A HB3  1 
ATOM   1419 H  HD21 . ASN A 1 74  ? -2.57600  -9.34100  13.28600  1.000 32.85000  ? 74  ASN A HD21 1 
ATOM   1420 H  HD22 . ASN A 1 74  ? -3.40500  -9.60600  14.49500  1.000 32.85000  ? 74  ASN A HD22 1 
ATOM   1421 N  N    . LEU A 1 75  ? -1.42400  -15.05700 14.34400  1.000 20.56000  ? 75  LEU A N    1 
ATOM   1422 C  CA   . LEU A 1 75  ? -0.06900  -15.45200 14.72200  1.000 22.26000  ? 75  LEU A CA   1 
ATOM   1423 C  C    . LEU A 1 75  ? 1.00100   -14.84000 13.82500  1.000 23.17000  ? 75  LEU A C    1 
ATOM   1424 O  O    . LEU A 1 75  ? 2.16900   -14.80800 14.21200  1.000 25.13000  ? 75  LEU A O    1 
ATOM   1425 C  CB   . LEU A 1 75  ? 0.01100   -16.97100 14.74100  1.000 22.20000  ? 75  LEU A CB   1 
ATOM   1426 C  CG   . LEU A 1 75  ? -0.70300  -17.60900 15.92500  1.000 26.61000  ? 75  LEU A CG   1 
ATOM   1427 C  CD1  . LEU A 1 75  ? -0.69900  -19.13400 15.83200  1.000 26.46000  ? 75  LEU A CD1  1 
ATOM   1428 C  CD2  . LEU A 1 75  ? -0.09500  -17.14800 17.26900  1.000 40.11000  ? 75  LEU A CD2  1 
ATOM   1429 H  H    . LEU A 1 75  ? -1.90000  -15.67500 13.98300  1.000 24.66000  ? 75  LEU A H    1 
ATOM   1430 H  HA   . LEU A 1 75  ? 0.12800   -15.13400 15.61700  1.000 26.70000  ? 75  LEU A HA   1 
ATOM   1431 H  HB2  . LEU A 1 75  ? -0.39600  -17.31400 13.93000  1.000 26.62000  ? 75  LEU A HB2  1 
ATOM   1432 H  HB3  . LEU A 1 75  ? 0.94400   -17.23300 14.78100  1.000 26.62000  ? 75  LEU A HB3  1 
ATOM   1433 H  HG   . LEU A 1 75  ? -1.62700  -17.31500 15.90000  1.000 31.91000  ? 75  LEU A HG   1 
ATOM   1434 H  HD11 . LEU A 1 75  ? -1.16000  -19.49900 16.60300  1.000 31.74000  ? 75  LEU A HD11 1 
ATOM   1435 H  HD12 . LEU A 1 75  ? -1.15300  -19.40200 15.01800  1.000 31.74000  ? 75  LEU A HD12 1 
ATOM   1436 H  HD13 . LEU A 1 75  ? 0.21900   -19.44700 15.81700  1.000 31.74000  ? 75  LEU A HD13 1 
ATOM   1437 H  HD21 . LEU A 1 75  ? -0.57400  -17.57700 17.99600  1.000 48.12000  ? 75  LEU A HD21 1 
ATOM   1438 H  HD22 . LEU A 1 75  ? 0.84100   -17.40000 17.29600  1.000 48.12000  ? 75  LEU A HD22 1 
ATOM   1439 H  HD23 . LEU A 1 75  ? -0.18000  -16.18400 17.34000  1.000 48.12000  ? 75  LEU A HD23 1 
ATOM   1440 N  N    . CYS A 1 76  ? 0.66200   -14.39400 12.60900  1.000 19.57000  ? 76  CYS A N    1 
ATOM   1441 C  CA   . CYS A 1 76  ? 1.60900   -13.69400 11.76900  1.000 17.68000  ? 76  CYS A CA   1 
ATOM   1442 C  C    . CYS A 1 76  ? 1.59400   -12.19200 11.98800  1.000 18.74000  ? 76  CYS A C    1 
ATOM   1443 O  O    . CYS A 1 76  ? 2.38400   -11.48200 11.37300  1.000 22.52000  ? 76  CYS A O    1 
ATOM   1444 C  CB   . CYS A 1 76  ? 1.39100   -14.02400 10.28300  1.000 20.73000  ? 76  CYS A CB   1 
ATOM   1445 S  SG   . CYS A 1 76  ? 1.91100   -15.74900 9.90100   1.000 19.06000  ? 76  CYS A SG   1 
ATOM   1446 H  H    . CYS A 1 76  ? -0.11600  -14.49000 12.25600  1.000 23.47000  ? 76  CYS A H    1 
ATOM   1447 H  HA   . CYS A 1 76  ? 2.49800   -14.01200 11.98800  1.000 21.21000  ? 76  CYS A HA   1 
ATOM   1448 H  HB2  . CYS A 1 76  ? 0.45000   -13.93300 10.06800  1.000 24.86000  ? 76  CYS A HB2  1 
ATOM   1449 H  HB3  . CYS A 1 76  ? 1.91700   -13.41800 9.73800   1.000 24.86000  ? 76  CYS A HB3  1 
ATOM   1450 N  N    A ASN A 1 77  ? 0.66600   -11.71600 12.81200  0.570 20.93000  ? 77  ASN A N    1 
ATOM   1451 N  N    B ASN A 1 77  ? 0.71400   -11.69300 12.84700  0.430 21.14000  ? 77  ASN A N    1 
ATOM   1452 C  CA   A ASN A 1 77  ? 0.59700   -10.31700 13.21900  0.570 20.55000  ? 77  ASN A CA   1 
ATOM   1453 C  CA   B ASN A 1 77  ? 0.65500   -10.27400 13.19000  0.430 20.67000  ? 77  ASN A CA   1 
ATOM   1454 C  C    A ASN A 1 77  ? 0.47600   -9.38300  12.01600  0.570 20.14000  ? 77  ASN A C    1 
ATOM   1455 C  C    B ASN A 1 77  ? 0.53100   -9.39700  11.94600  0.430 20.35000  ? 77  ASN A C    1 
ATOM   1456 O  O    A ASN A 1 77  ? 1.22200   -8.42000  11.86100  0.570 25.16000  ? 77  ASN A O    1 
ATOM   1457 O  O    B ASN A 1 77  ? 1.33900   -8.50800  11.68200  0.430 25.20000  ? 77  ASN A O    1 
ATOM   1458 C  CB   A ASN A 1 77  ? 1.76700   -9.95200  14.13600  0.570 26.89000  ? 77  ASN A CB   1 
ATOM   1459 C  CB   B ASN A 1 77  ? 1.84800   -9.84900  14.04800  0.430 26.41000  ? 77  ASN A CB   1 
ATOM   1460 C  CG   A ASN A 1 77  ? 1.85700   -10.87100 15.35100  0.570 25.46000  ? 77  ASN A CG   1 
ATOM   1461 C  CG   B ASN A 1 77  ? 1.66100   -8.47000  14.65500  0.430 33.98000  ? 77  ASN A CG   1 
ATOM   1462 O  OD1  A ASN A 1 77  ? 2.79900   -11.65500 15.48200  0.570 44.85000  ? 77  ASN A OD1  1 
ATOM   1463 O  OD1  B ASN A 1 77  ? 0.55000   -8.07800  15.00600  0.430 30.75000  ? 77  ASN A OD1  1 
ATOM   1464 N  ND2  A ASN A 1 77  ? 0.86300   -10.79200 16.23400  0.570 37.21000  ? 77  ASN A ND2  1 
ATOM   1465 N  ND2  B ASN A 1 77  ? 2.75200   -7.72800  14.78000  0.430 32.01000  ? 77  ASN A ND2  1 
ATOM   1466 H  H    A ASN A 1 77  ? 0.04600   -12.19900 13.16100  0.570 25.11000  ? 77  ASN A H    1 
ATOM   1467 H  H    B ASN A 1 77  ? 0.12500   -12.16800 13.25700  0.430 25.35000  ? 77  ASN A H    1 
ATOM   1468 H  HA   A ASN A 1 77  ? -0.21500  -10.18700 13.73300  0.570 24.65000  ? 77  ASN A HA   1 
ATOM   1469 H  HA   B ASN A 1 77  ? -0.14900  -10.14300 13.71600  0.430 24.79000  ? 77  ASN A HA   1 
ATOM   1470 H  HB2  A ASN A 1 77  ? 2.59700   -10.02800 13.63800  0.570 32.26000  ? 77  ASN A HB2  1 
ATOM   1471 H  HB2  B ASN A 1 77  ? 1.96100   -10.48500 14.77200  0.430 31.68000  ? 77  ASN A HB2  1 
ATOM   1472 H  HB3  A ASN A 1 77  ? 1.65200   -9.04300  14.45200  0.570 32.26000  ? 77  ASN A HB3  1 
ATOM   1473 H  HB3  B ASN A 1 77  ? 2.64600   -9.83000  13.49600  0.430 31.68000  ? 77  ASN A HB3  1 
ATOM   1474 H  HD21 A ASN A 1 77  ? 0.21500   -10.24200 16.10300  0.570 44.64000  ? 77  ASN A HD21 1 
ATOM   1475 H  HD21 B ASN A 1 77  ? 3.51300   -8.03600  14.52300  0.430 38.39000  ? 77  ASN A HD21 1 
ATOM   1476 H  HD22 A ASN A 1 77  ? 0.87000   -11.29000 16.93400  0.570 44.64000  ? 77  ASN A HD22 1 
ATOM   1477 H  HD22 B ASN A 1 77  ? 2.69900   -6.93900  15.11800  0.430 38.39000  ? 77  ASN A HD22 1 
ATOM   1478 N  N    . ILE A 1 78  ? -0.51000  -9.67000  11.16400  1.000 20.55000  ? 78  ILE A N    1 
ATOM   1479 C  CA   . ILE A 1 78  ? -0.72800  -8.91800  9.93800   1.000 22.00000  ? 78  ILE A CA   1 
ATOM   1480 C  C    . ILE A 1 78  ? -2.21600  -8.86200  9.63100   1.000 15.66000  ? 78  ILE A C    1 
ATOM   1481 O  O    . ILE A 1 78  ? -2.95200  -9.79300  9.96700   1.000 18.44000  ? 78  ILE A O    1 
ATOM   1482 C  CB   . ILE A 1 78  ? -0.00600  -9.54000  8.73300   1.000 22.65000  ? 78  ILE A CB   1 
ATOM   1483 C  CG1  . ILE A 1 78  ? -0.34000  -11.02600 8.64200   1.000 23.34000  ? 78  ILE A CG1  1 
ATOM   1484 C  CG2  . ILE A 1 78  ? 1.51300   -9.28500  8.79700   1.000 32.11000  ? 78  ILE A CG2  1 
ATOM   1485 C  CD1  . ILE A 1 78  ? -0.00100  -11.61400 7.29300   1.000 32.80000  ? 78  ILE A CD1  1 
ATOM   1486 H  H    . ILE A 1 78  ? -1.07400  -10.30900 11.27900  1.000 24.64000  ? 78  ILE A H    1 
ATOM   1487 H  HA   . ILE A 1 78  ? -0.38600  -8.02400  10.09500  1.000 26.39000  ? 78  ILE A HA   1 
ATOM   1488 H  HB   . ILE A 1 78  ? -0.32200  -9.11200  7.92200   1.000 27.17000  ? 78  ILE A HB   1 
ATOM   1489 H  HG12 . ILE A 1 78  ? 0.16600   -11.50600 9.31600   1.000 28.00000  ? 78  ILE A HG12 1 
ATOM   1490 H  HG13 . ILE A 1 78  ? -1.29000  -11.14700 8.79300   1.000 28.00000  ? 78  ILE A HG13 1 
ATOM   1491 H  HG21 . ILE A 1 78  ? 1.93200   -9.67200  8.01200   1.000 38.52000  ? 78  ILE A HG21 1 
ATOM   1492 H  HG22 . ILE A 1 78  ? 1.67100   -8.32800  8.81900   1.000 38.52000  ? 78  ILE A HG22 1 
ATOM   1493 H  HG23 . ILE A 1 78  ? 1.86900   -9.69800  9.60000   1.000 38.52000  ? 78  ILE A HG23 1 
ATOM   1494 H  HD11 . ILE A 1 78  ? -0.23800  -12.55500 7.29000   1.000 39.35000  ? 78  ILE A HD11 1 
ATOM   1495 H  HD12 . ILE A 1 78  ? -0.50200  -11.14500 6.60900   1.000 39.35000  ? 78  ILE A HD12 1 
ATOM   1496 H  HD13 . ILE A 1 78  ? 0.95100   -11.51300 7.13400   1.000 39.35000  ? 78  ILE A HD13 1 
ATOM   1497 N  N    . PRO A 1 79  ? -2.69800  -7.76800  9.04300   1.000 18.01000  ? 79  PRO A N    1 
ATOM   1498 C  CA   . PRO A 1 79  ? -4.04300  -7.79300  8.46800   1.000 16.67000  ? 79  PRO A CA   1 
ATOM   1499 C  C    . PRO A 1 79  ? -4.07500  -8.74900  7.29400   1.000 16.09000  ? 79  PRO A C    1 
ATOM   1500 O  O    . PRO A 1 79  ? -3.14600  -8.79900  6.48400   1.000 17.23000  ? 79  PRO A O    1 
ATOM   1501 C  CB   . PRO A 1 79  ? -4.26700  -6.34100  8.02000   1.000 18.56000  ? 79  PRO A CB   1 
ATOM   1502 C  CG   . PRO A 1 79  ? -2.91700  -5.78700  7.80100   1.000 26.94000  ? 79  PRO A CG   1 
ATOM   1503 C  CD   . PRO A 1 79  ? -1.96700  -6.53500  8.71600   1.000 22.45000  ? 79  PRO A CD   1 
ATOM   1504 H  HA   . PRO A 1 79  ? -4.71600  -8.03100  9.12500   1.000 19.99000  ? 79  PRO A HA   1 
ATOM   1505 H  HB2  . PRO A 1 79  ? -4.78500  -6.32700  7.20000   1.000 22.27000  ? 79  PRO A HB2  1 
ATOM   1506 H  HB3  . PRO A 1 79  ? -4.73400  -5.85100  8.71600   1.000 22.27000  ? 79  PRO A HB3  1 
ATOM   1507 H  HG2  . PRO A 1 79  ? -2.66400  -5.91400  6.87300   1.000 32.32000  ? 79  PRO A HG2  1 
ATOM   1508 H  HG3  . PRO A 1 79  ? -2.91900  -4.84100  8.01700   1.000 32.32000  ? 79  PRO A HG3  1 
ATOM   1509 H  HD2  . PRO A 1 79  ? -1.13800  -6.73900  8.25700   1.000 26.93000  ? 79  PRO A HD2  1 
ATOM   1510 H  HD3  . PRO A 1 79  ? -1.78500  -6.02100  9.51700   1.000 26.93000  ? 79  PRO A HD3  1 
ATOM   1511 N  N    . CYS A 1 80  ? -5.16600  -9.49700  7.19700   1.000 14.99000  ? 80  CYS A N    1 
ATOM   1512 C  CA   . CYS A 1 80  ? -5.26200  -10.46800 6.11300   1.000 13.62000  ? 80  CYS A CA   1 
ATOM   1513 C  C    . CYS A 1 80  ? -5.15000  -9.79500  4.75600   1.000 16.22000  ? 80  CYS A C    1 
ATOM   1514 O  O    . CYS A 1 80  ? -4.60600  -10.38600 3.82100   1.000 16.62000  ? 80  CYS A O    1 
ATOM   1515 C  CB   . CYS A 1 80  ? -6.54200  -11.28300 6.21300   1.000 15.47000  ? 80  CYS A CB   1 
ATOM   1516 S  SG   . CYS A 1 80  ? -6.69000  -12.23500 7.71500   1.000 15.36000  ? 80  CYS A SG   1 
ATOM   1517 H  H    . CYS A 1 80  ? -5.84200  -9.46500  7.72600   1.000 17.98000  ? 80  CYS A H    1 
ATOM   1518 H  HA   . CYS A 1 80  ? -4.52800  -11.09600 6.20000   1.000 16.33000  ? 80  CYS A HA   1 
ATOM   1519 H  HB2  . CYS A 1 80  ? -7.29800  -10.67700 6.17300   1.000 18.55000  ? 80  CYS A HB2  1 
ATOM   1520 H  HB3  . CYS A 1 80  ? -6.57400  -11.90200 5.46700   1.000 18.55000  ? 80  CYS A HB3  1 
ATOM   1521 N  N    . SER A 1 81  ? -5.64900  -8.56500  4.62300   1.000 18.01000  ? 81  SER A N    1 
ATOM   1522 C  CA   . SER A 1 81  ? -5.61200  -7.88900  3.33600   1.000 16.76000  ? 81  SER A CA   1 
ATOM   1523 C  C    . SER A 1 81  ? -4.19500  -7.67100  2.82300   1.000 17.32000  ? 81  SER A C    1 
ATOM   1524 O  O    . SER A 1 81  ? -4.00500  -7.56700  1.60400   1.000 23.11000  ? 81  SER A O    1 
ATOM   1525 C  CB   . SER A 1 81  ? -6.34400  -6.55100  3.45000   1.000 23.40000  ? 81  SER A CB   1 
ATOM   1526 O  OG   . SER A 1 81  ? -5.65500  -5.68200  4.32900   1.000 27.76000  ? 81  SER A OG   1 
ATOM   1527 H  H    . SER A 1 81  ? -6.00800  -8.10800  5.25700   1.000 21.60000  ? 81  SER A H    1 
ATOM   1528 H  HA   . SER A 1 81  ? -6.07000  -8.43700  2.67900   1.000 20.09000  ? 81  SER A HA   1 
ATOM   1529 H  HB2  . SER A 1 81  ? -6.39300  -6.14000  2.57200   1.000 28.07000  ? 81  SER A HB2  1 
ATOM   1530 H  HB3  . SER A 1 81  ? -7.23800  -6.70700  3.79300   1.000 28.07000  ? 81  SER A HB3  1 
ATOM   1531 H  HG   . SER A 1 81  ? -5.66600  -5.99400  5.10900   1.000 33.31000  ? 81  SER A HG   1 
ATOM   1532 N  N    . ALA A 1 82  ? -3.19600  -7.62800  3.69800   1.000 19.04000  ? 82  ALA A N    1 
ATOM   1533 C  CA   . ALA A 1 82  ? -1.82300  -7.47200  3.22900   1.000 23.73000  ? 82  ALA A CA   1 
ATOM   1534 C  C    . ALA A 1 82  ? -1.39400  -8.65100  2.37900   1.000 28.35000  ? 82  ALA A C    1 
ATOM   1535 O  O    . ALA A 1 82  ? -0.48800  -8.51700  1.54100   1.000 30.53000  ? 82  ALA A O    1 
ATOM   1536 C  CB   . ALA A 1 82  ? -0.85900  -7.33400  4.40800   1.000 25.99000  ? 82  ALA A CB   1 
ATOM   1537 H  H    . ALA A 1 82  ? -3.28300  -7.68700  4.55200   1.000 22.84000  ? 82  ALA A H    1 
ATOM   1538 H  HA   . ALA A 1 82  ? -1.76800  -6.65900  2.70300   1.000 28.46000  ? 82  ALA A HA   1 
ATOM   1539 H  HB1  . ALA A 1 82  ? 0.04600   -7.25200  4.06900   1.000 31.18000  ? 82  ALA A HB1  1 
ATOM   1540 H  HB2  . ALA A 1 82  ? -1.09500  -6.54300  4.91800   1.000 31.18000  ? 82  ALA A HB2  1 
ATOM   1541 H  HB3  . ALA A 1 82  ? -0.93200  -8.12300  4.96900   1.000 31.18000  ? 82  ALA A HB3  1 
ATOM   1542 N  N    . LEU A 1 83  ? -2.03100  -9.79600  2.56600   1.000 18.54000  ? 83  LEU A N    1 
ATOM   1543 C  CA   . LEU A 1 83  ? -1.70500  -11.01700 1.84000   1.000 17.79000  ? 83  LEU A CA   1 
ATOM   1544 C  C    . LEU A 1 83  ? -2.23000  -11.01600 0.41800   1.000 21.32000  ? 83  LEU A C    1 
ATOM   1545 O  O    . LEU A 1 83  ? -1.99600  -11.99800 -0.30300  1.000 22.52000  ? 83  LEU A O    1 
ATOM   1546 C  CB   . LEU A 1 83  ? -2.28400  -12.22100 2.56000   1.000 20.40000  ? 83  LEU A CB   1 
ATOM   1547 C  CG   . LEU A 1 83  ? -1.78600  -12.39300 3.99300   1.000 18.87000  ? 83  LEU A CG   1 
ATOM   1548 C  CD1  . LEU A 1 83  ? -2.55200  -13.46300 4.71100   1.000 23.26000  ? 83  LEU A CD1  1 
ATOM   1549 C  CD2  . LEU A 1 83  ? -0.27200  -12.72400 3.97800   1.000 33.15000  ? 83  LEU A CD2  1 
ATOM   1550 H  H    . LEU A 1 83  ? -2.67700  -9.89700  3.12500   1.000 22.24000  ? 83  LEU A H    1 
ATOM   1551 H  HA   . LEU A 1 83  ? -0.74000  -11.10200 1.81400   1.000 21.34000  ? 83  LEU A HA   1 
ATOM   1552 H  HB2  . LEU A 1 83  ? -3.24900  -12.12800 2.59200   1.000 24.47000  ? 83  LEU A HB2  1 
ATOM   1553 H  HB3  . LEU A 1 83  ? -2.04400  -13.02200 2.06700   1.000 24.47000  ? 83  LEU A HB3  1 
ATOM   1554 H  HG   . LEU A 1 83  ? -1.92500  -11.56500 4.47900   1.000 22.63000  ? 83  LEU A HG   1 
ATOM   1555 H  HD11 . LEU A 1 83  ? -2.09400  -13.67700 5.53900   1.000 27.90000  ? 83  LEU A HD11 1 
ATOM   1556 H  HD12 . LEU A 1 83  ? -3.44600  -13.13800 4.90200   1.000 27.90000  ? 83  LEU A HD12 1 
ATOM   1557 H  HD13 . LEU A 1 83  ? -2.60000  -14.25000 4.14700   1.000 27.90000  ? 83  LEU A HD13 1 
ATOM   1558 H  HD21 . LEU A 1 83  ? 0.00300   -12.98400 4.87100   1.000 39.76000  ? 83  LEU A HD21 1 
ATOM   1559 H  HD22 . LEU A 1 83  ? -0.11500  -13.45400 3.35800   1.000 39.76000  ? 83  LEU A HD22 1 
ATOM   1560 H  HD23 . LEU A 1 83  ? 0.22000   -11.93800 3.69500   1.000 39.76000  ? 83  LEU A HD23 1 
ATOM   1561 N  N    . LEU A 1 84  ? -2.96000  -9.97300  0.00700   1.000 19.72000  ? 84  LEU A N    1 
ATOM   1562 C  CA   . LEU A 1 84  ? -3.48500  -9.86700  -1.34500  1.000 18.06000  ? 84  LEU A CA   1 
ATOM   1563 C  C    . LEU A 1 84  ? -2.63900  -8.97200  -2.23600  1.000 22.64000  ? 84  LEU A C    1 
ATOM   1564 O  O    . LEU A 1 84  ? -2.96000  -8.80900  -3.42100  1.000 26.60000  ? 84  LEU A O    1 
ATOM   1565 C  CB   . LEU A 1 84  ? -4.92400  -9.34300  -1.29700  1.000 18.48000  ? 84  LEU A CB   1 
ATOM   1566 C  CG   . LEU A 1 84  ? -5.83900  -10.13900 -0.35400  1.000 18.00000  ? 84  LEU A CG   1 
ATOM   1567 C  CD1  . LEU A 1 84  ? -7.22000  -9.51800  -0.31900  1.000 27.43000  ? 84  LEU A CD1  1 
ATOM   1568 C  CD2  . LEU A 1 84  ? -5.93100  -11.60100 -0.75100  1.000 20.81000  ? 84  LEU A CD2  1 
ATOM   1569 H  H    . LEU A 1 84  ? -3.16500  -9.30500  0.50800   1.000 23.66000  ? 84  LEU A H    1 
ATOM   1570 H  HA   . LEU A 1 84  ? -3.50000  -10.74800 -1.75000  1.000 21.66000  ? 84  LEU A HA   1 
ATOM   1571 H  HB2  . LEU A 1 84  ? -4.91100  -8.42300  -0.99100  1.000 22.17000  ? 84  LEU A HB2  1 
ATOM   1572 H  HB3  . LEU A 1 84  ? -5.30300  -9.39100  -2.18900  1.000 22.17000  ? 84  LEU A HB3  1 
ATOM   1573 H  HG   . LEU A 1 84  ? -5.45400  -10.10800 0.53600   1.000 21.59000  ? 84  LEU A HG   1 
ATOM   1574 H  HD11 . LEU A 1 84  ? -7.79000  -10.04800 0.26000   1.000 32.90000  ? 84  LEU A HD11 1 
ATOM   1575 H  HD12 . LEU A 1 84  ? -7.15100  -8.61300  0.02400   1.000 32.90000  ? 84  LEU A HD12 1 
ATOM   1576 H  HD13 . LEU A 1 84  ? -7.58400  -9.50400  -1.21800  1.000 32.90000  ? 84  LEU A HD13 1 
ATOM   1577 H  HD21 . LEU A 1 84  ? -6.60000  -12.03600 -0.20000  1.000 24.97000  ? 84  LEU A HD21 1 
ATOM   1578 H  HD22 . LEU A 1 84  ? -6.18300  -11.65900 -1.68600  1.000 24.97000  ? 84  LEU A HD22 1 
ATOM   1579 H  HD23 . LEU A 1 84  ? -5.06600  -12.02000 -0.61600  1.000 24.97000  ? 84  LEU A HD23 1 
ATOM   1580 N  N    A SER A 1 85  ? -1.54500  -8.43500  -1.70700  0.580 23.53000  ? 85  SER A N    1 
ATOM   1581 N  N    B SER A 1 85  ? -1.58300  -8.37000  -1.70100  0.420 23.64000  ? 85  SER A N    1 
ATOM   1582 C  CA   A SER A 1 85  ? -0.71200  -7.48500  -2.42500  0.580 24.38000  ? 85  SER A CA   1 
ATOM   1583 C  CA   B SER A 1 85  ? -0.78200  -7.44200  -2.48400  0.420 24.22000  ? 85  SER A CA   1 
ATOM   1584 C  C    A SER A 1 85  ? 0.08100   -8.18100  -3.53400  0.580 23.82000  ? 85  SER A C    1 
ATOM   1585 C  C    B SER A 1 85  ? -0.07600  -8.17500  -3.62600  0.420 22.92000  ? 85  SER A C    1 
ATOM   1586 O  O    A SER A 1 85  ? 0.36800   -9.38000  -3.47300  0.580 25.28000  ? 85  SER A O    1 
ATOM   1587 O  O    B SER A 1 85  ? -0.05100  -9.40100  -3.70400  0.420 23.87000  ? 85  SER A O    1 
ATOM   1588 C  CB   A SER A 1 85  ? 0.26500   -6.83900  -1.43900  0.580 28.57000  ? 85  SER A CB   1 
ATOM   1589 C  CB   B SER A 1 85  ? 0.25000   -6.75100  -1.59300  0.420 29.40000  ? 85  SER A CB   1 
ATOM   1590 O  OG   A SER A 1 85  ? 1.33100   -6.22400  -2.11500  0.580 22.00000  ? 85  SER A OG   1 
ATOM   1591 O  OG   B SER A 1 85  ? 1.00200   -7.70100  -0.87400  0.420 30.05000  ? 85  SER A OG   1 
ATOM   1592 H  H    A SER A 1 85  ? -1.25900  -8.60900  -0.91500  0.580 28.22000  ? 85  SER A H    1 
ATOM   1593 H  H    B SER A 1 85  ? -1.31100  -8.48200  -0.89300  0.420 28.36000  ? 85  SER A H    1 
ATOM   1594 H  HA   A SER A 1 85  ? -1.26600  -6.80300  -2.83600  0.580 29.24000  ? 85  SER A HA   1 
ATOM   1595 H  HA   B SER A 1 85  ? -1.36300  -6.76600  -2.86800  0.420 29.06000  ? 85  SER A HA   1 
ATOM   1596 H  HB2  A SER A 1 85  ? -0.20700  -6.17000  -0.92000  0.580 34.27000  ? 85  SER A HB2  1 
ATOM   1597 H  HB2  B SER A 1 85  ? 0.84900   -6.22800  -2.14900  0.420 35.27000  ? 85  SER A HB2  1 
ATOM   1598 H  HB3  A SER A 1 85  ? 0.61900   -7.52500  -0.85100  0.580 34.27000  ? 85  SER A HB3  1 
ATOM   1599 H  HB3  B SER A 1 85  ? -0.21000  -6.17100  -0.96600  0.420 35.27000  ? 85  SER A HB3  1 
ATOM   1600 H  HG   A SER A 1 85  ? 1.90100   -5.94800  -1.56300  0.580 26.39000  ? 85  SER A HG   1 
ATOM   1601 H  HG   B SER A 1 85  ? 1.28800   -8.29500  -1.39400  0.420 36.05000  ? 85  SER A HG   1 
ATOM   1602 N  N    . SER A 1 86  ? 0.48600   -7.39200  -4.54000  1.000 23.47000  ? 86  SER A N    1 
ATOM   1603 C  CA   . SER A 1 86  ? 1.33500   -7.93400  -5.59800  1.000 24.15000  ? 86  SER A CA   1 
ATOM   1604 C  C    . SER A 1 86  ? 2.70900   -8.32800  -5.08400  1.000 21.12000  ? 86  SER A C    1 
ATOM   1605 O  O    . SER A 1 86  ? 3.37100   -9.18000  -5.69700  1.000 31.40000  ? 86  SER A O    1 
ATOM   1606 C  CB   . SER A 1 86  ? 1.46800   -6.89800  -6.71500  1.000 31.05000  ? 86  SER A CB   1 
ATOM   1607 O  OG   . SER A 1 86  ? 2.09200   -5.73100  -6.21400  1.000 39.77000  ? 86  SER A OG   1 
ATOM   1608 H  H    . SER A 1 86  ? 0.28400   -6.56100  -4.62700  1.000 28.15000  ? 86  SER A H    1 
ATOM   1609 H  HA   . SER A 1 86  ? 0.92600   -8.73000  -5.97200  1.000 28.97000  ? 86  SER A HA   1 
ATOM   1610 H  HB2  . SER A 1 86  ? 2.00700   -7.26700  -7.43200  1.000 37.25000  ? 86  SER A HB2  1 
ATOM   1611 H  HB3  . SER A 1 86  ? 0.58500   -6.67100  -7.04800  1.000 37.25000  ? 86  SER A HB3  1 
ATOM   1612 H  HG   . SER A 1 86  ? 2.16600   -5.16000  -6.82600  1.000 47.71000  ? 86  SER A HG   1 
ATOM   1613 N  N    . ASP A 1 87  ? 3.13400   -7.75600  -3.97300  1.000 21.87000  ? 87  ASP A N    1 
ATOM   1614 C  CA   . ASP A 1 87  ? 4.35400   -8.13700  -3.27500  1.000 22.90000  ? 87  ASP A CA   1 
ATOM   1615 C  C    . ASP A 1 87  ? 4.03700   -9.30200  -2.34800  1.000 24.35000  ? 87  ASP A C    1 
ATOM   1616 O  O    . ASP A 1 87  ? 3.20700   -9.17200  -1.43700  1.000 24.07000  ? 87  ASP A O    1 
ATOM   1617 C  CB   . ASP A 1 87  ? 4.82700   -6.93500  -2.46300  1.000 30.36000  ? 87  ASP A CB   1 
ATOM   1618 C  CG   . ASP A 1 87  ? 6.10200   -7.21400  -1.68100  1.000 42.70000  ? 87  ASP A CG   1 
ATOM   1619 O  OD1  . ASP A 1 87  ? 6.59500   -8.35600  -1.71600  1.000 57.92000  ? 87  ASP A OD1  1 
ATOM   1620 O  OD2  . ASP A 1 87  ? 6.61700   -6.27300  -1.03900  1.000 60.99000  ? 87  ASP A OD2  1 
ATOM   1621 H  H    . ASP A 1 87  ? 2.71500   -7.11500  -3.58200  1.000 26.23000  ? 87  ASP A H    1 
ATOM   1622 H  HA   . ASP A 1 87  ? 5.04600   -8.41500  -3.89500  1.000 27.47000  ? 87  ASP A HA   1 
ATOM   1623 H  HB2  . ASP A 1 87  ? 5.00200   -6.19500  -3.06600  1.000 36.42000  ? 87  ASP A HB2  1 
ATOM   1624 H  HB3  . ASP A 1 87  ? 4.13500   -6.69000  -1.82900  1.000 36.42000  ? 87  ASP A HB3  1 
ATOM   1625 N  N    . ILE A 1 88  ? 4.68700   -10.44200 -2.58200  1.000 20.91000  ? 88  ILE A N    1 
ATOM   1626 C  CA   . ILE A 1 88  ? 4.37400   -11.65800 -1.83100  1.000 19.15000  ? 88  ILE A CA   1 
ATOM   1627 C  C    . ILE A 1 88  ? 5.16300   -11.80300 -0.54100  1.000 19.50000  ? 88  ILE A C    1 
ATOM   1628 O  O    . ILE A 1 88  ? 5.11200   -12.86400 0.09300   1.000 17.33000  ? 88  ILE A O    1 
ATOM   1629 C  CB   . ILE A 1 88  ? 4.52600   -12.93100 -2.67800  1.000 20.40000  ? 88  ILE A CB   1 
ATOM   1630 C  CG1  . ILE A 1 88  ? 5.98800   -13.16500 -3.07100  1.000 21.92000  ? 88  ILE A CG1  1 
ATOM   1631 C  CG2  . ILE A 1 88  ? 3.62200   -12.86800 -3.89400  1.000 27.40000  ? 88  ILE A CG2  1 
ATOM   1632 C  CD1  . ILE A 1 88  ? 6.21700   -14.57700 -3.66000  1.000 27.96000  ? 88  ILE A CD1  1 
ATOM   1633 H  H    . ILE A 1 88  ? 5.30900   -10.53700 -3.16700  1.000 25.08000  ? 88  ILE A H    1 
ATOM   1634 H  HA   . ILE A 1 88  ? 3.44600   -11.54300 -1.57100  1.000 22.97000  ? 88  ILE A HA   1 
ATOM   1635 H  HB   . ILE A 1 88  ? 4.25200   -13.68900 -2.13900  1.000 24.46000  ? 88  ILE A HB   1 
ATOM   1636 H  HG12 . ILE A 1 88  ? 6.24500   -12.51200 -3.74100  1.000 26.30000  ? 88  ILE A HG12 1 
ATOM   1637 H  HG13 . ILE A 1 88  ? 6.54700   -13.07100 -2.28500  1.000 26.30000  ? 88  ILE A HG13 1 
ATOM   1638 H  HG21 . ILE A 1 88  ? 3.43800   -13.77100 -4.19700  1.000 32.86000  ? 88  ILE A HG21 1 
ATOM   1639 H  HG22 . ILE A 1 88  ? 2.79400   -12.42500 -3.65000  1.000 32.86000  ? 88  ILE A HG22 1 
ATOM   1640 H  HG23 . ILE A 1 88  ? 4.07000   -12.36900 -4.59500  1.000 32.86000  ? 88  ILE A HG23 1 
ATOM   1641 H  HD11 . ILE A 1 88  ? 7.16500   -14.70200 -3.82100  1.000 33.54000  ? 88  ILE A HD11 1 
ATOM   1642 H  HD12 . ILE A 1 88  ? 5.89900   -15.23900 -3.02600  1.000 33.54000  ? 88  ILE A HD12 1 
ATOM   1643 H  HD13 . ILE A 1 88  ? 5.72700   -14.65500 -4.49400  1.000 33.54000  ? 88  ILE A HD13 1 
ATOM   1644 N  N    . THR A 1 89  ? 5.90600   -10.77000 -0.13500  1.000 20.45000  ? 89  THR A N    1 
ATOM   1645 C  CA   . THR A 1 89  ? 6.74800   -10.86600 1.05300   1.000 17.91000  ? 89  THR A CA   1 
ATOM   1646 C  C    . THR A 1 89  ? 5.96500   -11.32300 2.28900   1.000 18.41000  ? 89  THR A C    1 
ATOM   1647 O  O    . THR A 1 89  ? 6.40300   -12.22000 3.03000   1.000 19.61000  ? 89  THR A O    1 
ATOM   1648 C  CB   . THR A 1 89  ? 7.45900   -9.53500  1.31800   1.000 25.13000  ? 89  THR A CB   1 
ATOM   1649 O  OG1  . THR A 1 89  ? 8.23100   -9.17700  0.17200   1.000 26.41000  ? 89  THR A OG1  1 
ATOM   1650 C  CG2  . THR A 1 89  ? 8.38800   -9.67600  2.49800   1.000 28.31000  ? 89  THR A CG2  1 
ATOM   1651 H  H    . THR A 1 89  ? 5.93900   -10.00700 -0.53000  1.000 24.53000  ? 89  THR A H    1 
ATOM   1652 H  HA   . THR A 1 89  ? 7.42600   -11.53700 0.87900   1.000 21.48000  ? 89  THR A HA   1 
ATOM   1653 H  HB   . THR A 1 89  ? 6.80500   -8.84300  1.50600   1.000 30.14000  ? 89  THR A HB   1 
ATOM   1654 H  HG1  . THR A 1 89  ? 9.05100   -9.22000  0.35300   1.000 31.68000  ? 89  THR A HG1  1 
ATOM   1655 H  HG21 . THR A 1 89  ? 9.03100   -8.95000  2.50300   1.000 33.96000  ? 89  THR A HG21 1 
ATOM   1656 H  HG22 . THR A 1 89  ? 7.88100   -9.65400  3.32400   1.000 33.96000  ? 89  THR A HG22 1 
ATOM   1657 H  HG23 . THR A 1 89  ? 8.86600   -10.51900 2.44500   1.000 33.96000  ? 89  THR A HG23 1 
ATOM   1658 N  N    . ALA A 1 90  ? 4.82700   -10.70200 2.56400   1.000 17.34000  ? 90  ALA A N    1 
ATOM   1659 C  CA   . ALA A 1 90  ? 4.10800   -11.07700 3.77000   1.000 19.44000  ? 90  ALA A CA   1 
ATOM   1660 C  C    . ALA A 1 90  ? 3.62600   -12.51700 3.68400   1.000 17.34000  ? 90  ALA A C    1 
ATOM   1661 O  O    . ALA A 1 90  ? 3.67100   -13.24800 4.68200   1.000 18.86000  ? 90  ALA A O    1 
ATOM   1662 C  CB   . ALA A 1 90  ? 2.94400   -10.11700 4.04100   1.000 24.31000  ? 90  ALA A CB   1 
ATOM   1663 H  H    . ALA A 1 90  ? 4.46300   -10.08500 2.08900   1.000 20.80000  ? 90  ALA A H    1 
ATOM   1664 H  HA   . ALA A 1 90  ? 4.71000   -11.00200 4.52600   1.000 23.32000  ? 90  ALA A HA   1 
ATOM   1665 H  HB1  . ALA A 1 90  ? 2.50600   -10.37600 4.86600   1.000 29.16000  ? 90  ALA A HB1  1 
ATOM   1666 H  HB2  . ALA A 1 90  ? 3.29100   -9.21400  4.12000   1.000 29.16000  ? 90  ALA A HB2  1 
ATOM   1667 H  HB3  . ALA A 1 90  ? 2.31600   -10.16600 3.30300   1.000 29.16000  ? 90  ALA A HB3  1 
ATOM   1668 N  N    . SER A 1 91  ? 3.17200   -12.95000 2.50600   1.000 16.48000  ? 91  SER A N    1 
ATOM   1669 C  CA   . SER A 1 91  ? 2.72200   -14.33100 2.37600   1.000 17.18000  ? 91  SER A CA   1 
ATOM   1670 C  C    . SER A 1 91  ? 3.86300   -15.29300 2.62100   1.000 16.73000  ? 91  SER A C    1 
ATOM   1671 O  O    . SER A 1 91  ? 3.68900   -16.32200 3.28300   1.000 18.43000  ? 91  SER A O    1 
ATOM   1672 C  CB   . SER A 1 91  ? 2.14700   -14.57800 0.99500   1.000 17.94000  ? 91  SER A CB   1 
ATOM   1673 O  OG   . SER A 1 91  ? 0.87500   -13.97900 0.90400   1.000 21.22000  ? 91  SER A OG   1 
ATOM   1674 H  H    . SER A 1 91  ? 3.11600   -12.47700 1.78900   1.000 19.76000  ? 91  SER A H    1 
ATOM   1675 H  HA   . SER A 1 91  ? 2.02400   -14.48500 3.03100   1.000 20.61000  ? 91  SER A HA   1 
ATOM   1676 H  HB2  . SER A 1 91  ? 2.73500   -14.19000 0.32800   1.000 21.51000  ? 91  SER A HB2  1 
ATOM   1677 H  HB3  . SER A 1 91  ? 2.06400   -15.53400 0.84800   1.000 21.51000  ? 91  SER A HB3  1 
ATOM   1678 H  HG   . SER A 1 91  ? 0.50700   -14.19500 0.18000   1.000 25.45000  ? 91  SER A HG   1 
ATOM   1679 N  N    . VAL A 1 92  ? 5.03200   -15.00400 2.04900   1.000 17.12000  ? 92  VAL A N    1 
ATOM   1680 C  CA   . VAL A 1 92  ? 6.18300   -15.89300 2.21100   1.000 16.09000  ? 92  VAL A CA   1 
ATOM   1681 C  C    . VAL A 1 92  ? 6.63000   -15.92200 3.66100   1.000 18.60000  ? 92  VAL A C    1 
ATOM   1682 O  O    . VAL A 1 92  ? 6.87700   -16.98800 4.22800   1.000 18.94000  ? 92  VAL A O    1 
ATOM   1683 C  CB   . VAL A 1 92  ? 7.33700   -15.49000 1.27500   1.000 19.72000  ? 92  VAL A CB   1 
ATOM   1684 C  CG1  . VAL A 1 92  ? 8.62300   -16.21800 1.68200   1.000 24.65000  ? 92  VAL A CG1  1 
ATOM   1685 C  CG2  . VAL A 1 92  ? 6.98300   -15.79900 -0.14200  1.000 23.52000  ? 92  VAL A CG2  1 
ATOM   1686 H  H    . VAL A 1 92  ? 5.18500   -14.30800 1.56800   1.000 20.54000  ? 92  VAL A H    1 
ATOM   1687 H  HA   . VAL A 1 92  ? 5.90400   -16.78700 1.95900   1.000 19.29000  ? 92  VAL A HA   1 
ATOM   1688 H  HB   . VAL A 1 92  ? 7.49100   -14.53500 1.34800   1.000 23.65000  ? 92  VAL A HB   1 
ATOM   1689 H  HG11 . VAL A 1 92  ? 9.24600   -16.19900 0.93900   1.000 29.57000  ? 92  VAL A HG11 1 
ATOM   1690 H  HG12 . VAL A 1 92  ? 9.01100   -15.76800 2.45000   1.000 29.57000  ? 92  VAL A HG12 1 
ATOM   1691 H  HG13 . VAL A 1 92  ? 8.40800   -17.13600 1.91100   1.000 29.57000  ? 92  VAL A HG13 1 
ATOM   1692 H  HG21 . VAL A 1 92  ? 7.72200   -15.54100 -0.71500  1.000 28.21000  ? 92  VAL A HG21 1 
ATOM   1693 H  HG22 . VAL A 1 92  ? 6.81600   -16.75100 -0.22500  1.000 28.21000  ? 92  VAL A HG22 1 
ATOM   1694 H  HG23 . VAL A 1 92  ? 6.18700   -15.30100 -0.38400  1.000 28.21000  ? 92  VAL A HG23 1 
ATOM   1695 N  N    . ASN A 1 93  ? 6.73200   -14.75500 4.30200   1.000 17.44000  ? 93  ASN A N    1 
ATOM   1696 C  CA   . ASN A 1 93  ? 7.19700   -14.74000 5.68300   1.000 18.56000  ? 93  ASN A CA   1 
ATOM   1697 C  C    . ASN A 1 93  ? 6.22900   -15.45600 6.61000   1.000 17.34000  ? 93  ASN A C    1 
ATOM   1698 O  O    . ASN A 1 93  ? 6.65000   -16.16900 7.52500   1.000 20.17000  ? 93  ASN A O    1 
ATOM   1699 C  CB   . ASN A 1 93  ? 7.40000   -13.29900 6.15700   1.000 24.81000  ? 93  ASN A CB   1 
ATOM   1700 C  CG   . ASN A 1 93  ? 8.68700   -12.70100 5.64700   1.000 47.02000  ? 93  ASN A CG   1 
ATOM   1701 O  OD1  . ASN A 1 93  ? 9.48000   -13.38500 5.00700   1.000 36.99000  ? 93  ASN A OD1  1 
ATOM   1702 N  ND2  . ASN A 1 93  ? 8.90000   -11.42000 5.92200   1.000 49.43000  ? 93  ASN A ND2  1 
ATOM   1703 H  H    . ASN A 1 93  ? 6.54400   -13.98400 3.96900   1.000 20.92000  ? 93  ASN A H    1 
ATOM   1704 H  HA   . ASN A 1 93  ? 8.05000   -15.20200 5.71800   1.000 22.26000  ? 93  ASN A HA   1 
ATOM   1705 H  HB2  . ASN A 1 93  ? 6.66600   -12.75200 5.83600   1.000 29.76000  ? 93  ASN A HB2  1 
ATOM   1706 H  HB3  . ASN A 1 93  ? 7.42500   -13.28400 7.12700   1.000 29.76000  ? 93  ASN A HB3  1 
ATOM   1707 H  HD21 . ASN A 1 93  ? 8.31800   -10.97400 6.37100   1.000 59.30000  ? 93  ASN A HD21 1 
ATOM   1708 H  HD22 . ASN A 1 93  ? 9.62100   -11.03600 5.65100   1.000 59.30000  ? 93  ASN A HD22 1 
ATOM   1709 N  N    . CYS A 1 94  ? 4.91700   -15.27700 6.40300   1.000 16.33000  ? 94  CYS A N    1 
ATOM   1710 C  CA   . CYS A 1 94  ? 3.93600   -15.99500 7.19900   1.000 15.19000  ? 94  CYS A CA   1 
ATOM   1711 C  C    . CYS A 1 94  ? 4.00400   -17.49200 6.91100   1.000 16.36000  ? 94  CYS A C    1 
ATOM   1712 O  O    . CYS A 1 94  ? 3.92900   -18.30300 7.84100   1.000 16.58000  ? 94  CYS A O    1 
ATOM   1713 C  CB   . CYS A 1 94  ? 2.54500   -15.41500 6.94100   1.000 17.27000  ? 94  CYS A CB   1 
ATOM   1714 S  SG   . CYS A 1 94  ? 1.26200   -16.04800 8.01400   1.000 18.69000  ? 94  CYS A SG   1 
ATOM   1715 H  H    . CYS A 1 94  ? 4.58000   -14.75100 5.81200   1.000 19.58000  ? 94  CYS A H    1 
ATOM   1716 H  HA   . CYS A 1 94  ? 4.11900   -15.87800 8.14400   1.000 18.21000  ? 94  CYS A HA   1 
ATOM   1717 H  HB2  . CYS A 1 94  ? 2.58300   -14.45400 7.06600   1.000 20.71000  ? 94  CYS A HB2  1 
ATOM   1718 H  HB3  . CYS A 1 94  ? 2.29000   -15.62100 6.02800   1.000 20.71000  ? 94  CYS A HB3  1 
ATOM   1719 N  N    . ALA A 1 95  ? 4.17900   -17.86800 5.63400   1.000 15.78000  ? 95  ALA A N    1 
ATOM   1720 C  CA   . ALA A 1 95  ? 4.30300   -19.27600 5.27400   1.000 15.03000  ? 95  ALA A CA   1 
ATOM   1721 C  C    . ALA A 1 95  ? 5.46100   -19.92900 5.99700   1.000 15.80000  ? 95  ALA A C    1 
ATOM   1722 O  O    . ALA A 1 95  ? 5.38200   -21.10500 6.36200   1.000 16.85000  ? 95  ALA A O    1 
ATOM   1723 C  CB   . ALA A 1 95  ? 4.47800   -19.41200 3.76300   1.000 17.97000  ? 95  ALA A CB   1 
ATOM   1724 H  H    . ALA A 1 95  ? 4.22900   -17.32800 4.96700   1.000 18.92000  ? 95  ALA A H    1 
ATOM   1725 H  HA   . ALA A 1 95  ? 3.48800   -19.73600 5.53100   1.000 18.02000  ? 95  ALA A HA   1 
ATOM   1726 H  HB1  . ALA A 1 95  ? 4.67100   -20.33800 3.55000   1.000 21.55000  ? 95  ALA A HB1  1 
ATOM   1727 H  HB2  . ALA A 1 95  ? 3.65900   -19.13500 3.32400   1.000 21.55000  ? 95  ALA A HB2  1 
ATOM   1728 H  HB3  . ALA A 1 95  ? 5.21300   -18.84700 3.47800   1.000 21.55000  ? 95  ALA A HB3  1 
ATOM   1729 N  N    . LYS A 1 96  ? 6.55400   -19.19500 6.18500   1.000 15.57000  ? 96  LYS A N    1 
ATOM   1730 C  CA   . LYS A 1 96  ? 7.69700   -19.74800 6.89400   1.000 15.44000  ? 96  LYS A CA   1 
ATOM   1731 C  C    . LYS A 1 96  ? 7.33600   -20.08300 8.33200   1.000 18.36000  ? 96  LYS A C    1 
ATOM   1732 O  O    . LYS A 1 96  ? 7.78400   -21.10500 8.87500   1.000 20.25000  ? 96  LYS A O    1 
ATOM   1733 C  CB   . LYS A 1 96  ? 8.83100   -18.73200 6.84200   1.000 17.85000  ? 96  LYS A CB   1 
ATOM   1734 C  CG   . LYS A 1 96  ? 9.62800   -18.80300 5.58500   1.000 17.81000  ? 96  LYS A CG   1 
ATOM   1735 C  CD   . LYS A 1 96  ? 10.75800  -17.75900 5.55700   1.000 22.35000  ? 96  LYS A CD   1 
ATOM   1736 C  CE   . LYS A 1 96  ? 11.15800  -17.43500 4.14300   1.000 24.36000  ? 96  LYS A CE   1 
ATOM   1737 N  NZ   . LYS A 1 96  ? 12.48200  -16.72300 4.12400   1.000 27.90000  ? 96  LYS A NZ   1 
ATOM   1738 H  H    . LYS A 1 96  ? 6.65700   -18.38500 5.91500   1.000 18.67000  ? 96  LYS A H    1 
ATOM   1739 H  HA   . LYS A 1 96  ? 7.98900   -20.56900 6.46800   1.000 18.52000  ? 96  LYS A HA   1 
ATOM   1740 H  HB2  . LYS A 1 96  ? 8.45600   -17.83900 6.90800   1.000 21.41000  ? 96  LYS A HB2  1 
ATOM   1741 H  HB3  . LYS A 1 96  ? 9.43200   -18.89400 7.58600   1.000 21.41000  ? 96  LYS A HB3  1 
ATOM   1742 H  HG2  . LYS A 1 96  ? 10.02800  -19.68300 5.51000   1.000 21.36000  ? 96  LYS A HG2  1 
ATOM   1743 H  HG3  . LYS A 1 96  ? 9.04500   -18.63800 4.82800   1.000 21.36000  ? 96  LYS A HG3  1 
ATOM   1744 H  HD2  . LYS A 1 96  ? 10.45400  -16.94200 5.98400   1.000 26.81000  ? 96  LYS A HD2  1 
ATOM   1745 H  HD3  . LYS A 1 96  ? 11.53300  -18.10900 6.02300   1.000 26.81000  ? 96  LYS A HD3  1 
ATOM   1746 H  HE2  . LYS A 1 96  ? 11.24100  -18.25500 3.63200   1.000 29.22000  ? 96  LYS A HE2  1 
ATOM   1747 H  HE3  . LYS A 1 96  ? 10.49100  -16.85900 3.73900   1.000 29.22000  ? 96  LYS A HE3  1 
ATOM   1748 H  HZ1  . LYS A 1 96  ? 12.70000  -16.50900 3.28800   1.000 33.47000  ? 96  LYS A HZ1  1 
ATOM   1749 H  HZ2  . LYS A 1 96  ? 12.43300  -15.97900 4.61000   1.000 33.47000  ? 96  LYS A HZ2  1 
ATOM   1750 H  HZ3  . LYS A 1 96  ? 13.11500  -17.24900 4.46300   1.000 33.47000  ? 96  LYS A HZ3  1 
ATOM   1751 N  N    . LYS A 1 97  ? 6.50800   -19.25100 8.96700   1.000 16.08000  ? 97  LYS A N    1 
ATOM   1752 C  CA   . LYS A 1 97  ? 6.03300   -19.57300 10.30200  1.000 16.89000  ? 97  LYS A CA   1 
ATOM   1753 C  C    . LYS A 1 97  ? 5.10700   -20.78100 10.29300  1.000 18.33000  ? 97  LYS A C    1 
ATOM   1754 O  O    . LYS A 1 97  ? 5.22800   -21.67500 11.14100  1.000 20.98000  ? 97  LYS A O    1 
ATOM   1755 C  CB   . LYS A 1 97  ? 5.32900   -18.36300 10.90200  1.000 19.10000  ? 97  LYS A CB   1 
ATOM   1756 C  CG   . LYS A 1 97  ? 6.22800   -17.12800 10.96700  1.000 31.59000  ? 97  LYS A CG   1 
ATOM   1757 C  CD   . LYS A 1 97  ? 5.72000   -16.06900 11.93900  1.000 49.67000  ? 97  LYS A CD   1 
ATOM   1758 C  CE   . LYS A 1 97  ? 6.75500   -14.95600 12.11100  1.000 78.49000  ? 97  LYS A CE   1 
ATOM   1759 N  NZ   . LYS A 1 97  ? 6.22000   -13.60900 11.77300  1.000 68.40000  ? 97  LYS A NZ   1 
ATOM   1760 H  H    . LYS A 1 97  ? 6.21400   -18.50800 8.64900   1.000 19.28000  ? 97  LYS A H    1 
ATOM   1761 H  HA   . LYS A 1 97  ? 6.79600   -19.79100 10.86000  1.000 20.25000  ? 97  LYS A HA   1 
ATOM   1762 H  HB2  . LYS A 1 97  ? 4.55700   -18.14400 10.35700  1.000 22.90000  ? 97  LYS A HB2  1 
ATOM   1763 H  HB3  . LYS A 1 97  ? 5.04700   -18.57700 11.80500  1.000 22.90000  ? 97  LYS A HB3  1 
ATOM   1764 H  HG2  . LYS A 1 97  ? 7.11300   -17.39800 11.25700  1.000 37.90000  ? 97  LYS A HG2  1 
ATOM   1765 H  HG3  . LYS A 1 97  ? 6.27500   -16.72600 10.08600  1.000 37.90000  ? 97  LYS A HG3  1 
ATOM   1766 H  HD2  . LYS A 1 97  ? 4.90100   -15.67900 11.59500  1.000 59.59000  ? 97  LYS A HD2  1 
ATOM   1767 H  HD3  . LYS A 1 97  ? 5.55600   -16.47400 12.80400  1.000 59.59000  ? 97  LYS A HD3  1 
ATOM   1768 H  HE2  . LYS A 1 97  ? 7.04800   -14.93800 13.03500  1.000 94.18000  ? 97  LYS A HE2  1 
ATOM   1769 H  HE3  . LYS A 1 97  ? 7.50900   -15.13300 11.52700  1.000 94.18000  ? 97  LYS A HE3  1 
ATOM   1770 H  HZ1  . LYS A 1 97  ? 6.84900   -12.99200 11.89900  1.000 82.07000  ? 97  LYS A HZ1  1 
ATOM   1771 H  HZ2  . LYS A 1 97  ? 5.96200   -13.58900 10.92200  1.000 82.07000  ? 97  LYS A HZ2  1 
ATOM   1772 H  HZ3  . LYS A 1 97  ? 5.52200   -13.42000 12.29100  1.000 82.07000  ? 97  LYS A HZ3  1 
ATOM   1773 N  N    . ILE A 1 98  ? 4.18500   -20.83700 9.34100   1.000 16.37000  ? 98  ILE A N    1 
ATOM   1774 C  CA   . ILE A 1 98  ? 3.23300   -21.93600 9.28200   1.000 16.77000  ? 98  ILE A CA   1 
ATOM   1775 C  C    . ILE A 1 98  ? 3.96300   -23.25900 9.12400   1.000 16.72000  ? 98  ILE A C    1 
ATOM   1776 O  O    . ILE A 1 98  ? 3.67300   -24.22900 9.83400   1.000 18.73000  ? 98  ILE A O    1 
ATOM   1777 C  CB   . ILE A 1 98  ? 2.23300   -21.72300 8.13400   1.000 15.89000  ? 98  ILE A CB   1 
ATOM   1778 C  CG1  . ILE A 1 98  ? 1.42600   -20.44400 8.39200   1.000 15.23000  ? 98  ILE A CG1  1 
ATOM   1779 C  CG2  . ILE A 1 98  ? 1.30600   -22.90400 8.03000   1.000 18.13000  ? 98  ILE A CG2  1 
ATOM   1780 C  CD1  . ILE A 1 98  ? 0.63400   -20.01000 7.20700   1.000 20.10000  ? 98  ILE A CD1  1 
ATOM   1781 H  H    . ILE A 1 98  ? 4.08900   -20.25200 8.71800   1.000 19.63000  ? 98  ILE A H    1 
ATOM   1782 H  HA   . ILE A 1 98  ? 2.74100   -21.95500 10.11700  1.000 20.11000  ? 98  ILE A HA   1 
ATOM   1783 H  HB   . ILE A 1 98  ? 2.72100   -21.63400 7.30100   1.000 19.05000  ? 98  ILE A HB   1 
ATOM   1784 H  HG12 . ILE A 1 98  ? 0.80900   -20.60300 9.12400   1.000 18.26000  ? 98  ILE A HG12 1 
ATOM   1785 H  HG13 . ILE A 1 98  ? 2.03700   -19.72700 8.62400   1.000 18.26000  ? 98  ILE A HG13 1 
ATOM   1786 H  HG21 . ILE A 1 98  ? 0.52100   -22.64600 7.52200   1.000 21.74000  ? 98  ILE A HG21 1 
ATOM   1787 H  HG22 . ILE A 1 98  ? 1.76700   -23.62900 7.58000   1.000 21.74000  ? 98  ILE A HG22 1 
ATOM   1788 H  HG23 . ILE A 1 98  ? 1.04500   -23.18100 8.92200   1.000 21.74000  ? 98  ILE A HG23 1 
ATOM   1789 H  HD11 . ILE A 1 98  ? 1.09800   -20.28100 6.40000   1.000 24.11000  ? 98  ILE A HD11 1 
ATOM   1790 H  HD12 . ILE A 1 98  ? -0.24100  -20.42700 7.24200   1.000 24.11000  ? 98  ILE A HD12 1 
ATOM   1791 H  HD13 . ILE A 1 98  ? 0.54000   -19.04400 7.22600   1.000 24.11000  ? 98  ILE A HD13 1 
ATOM   1792 N  N    . VAL A 1 99  ? 4.88200   -23.33200 8.15900   1.000 16.89000  ? 99  VAL A N    1 
ATOM   1793 C  CA   . VAL A 1 99  ? 5.49000   -24.61200 7.82700   1.000 17.35000  ? 99  VAL A CA   1 
ATOM   1794 C  C    . VAL A 1 99  ? 6.39000   -25.06700 8.95500   1.000 18.75000  ? 99  VAL A C    1 
ATOM   1795 O  O    . VAL A 1 99  ? 6.76600   -26.25300 9.01000   1.000 20.23000  ? 99  VAL A O    1 
ATOM   1796 C  CB   . VAL A 1 99  ? 6.21000   -24.49000 6.47200   1.000 16.67000  ? 99  VAL A CB   1 
ATOM   1797 C  CG1  . VAL A 1 99  ? 7.50600   -23.69900 6.57700   1.000 19.71000  ? 99  VAL A CG1  1 
ATOM   1798 C  CG2  . VAL A 1 99  ? 6.47300   -25.87000 5.84600   1.000 19.21000  ? 99  VAL A CG2  1 
ATOM   1799 H  H    . VAL A 1 99  ? 5.16200   -22.66600 7.69300   1.000 20.26000  ? 99  VAL A H    1 
ATOM   1800 H  HA   . VAL A 1 99  ? 4.81900   -25.30400 7.71800   1.000 20.80000  ? 99  VAL A HA   1 
ATOM   1801 H  HB   . VAL A 1 99  ? 5.61800   -23.99800 5.88200   1.000 19.99000  ? 99  VAL A HB   1 
ATOM   1802 H  HG11 . VAL A 1 99  ? 7.87400   -23.57600 5.68800   1.000 23.64000  ? 99  VAL A HG11 1 
ATOM   1803 H  HG12 . VAL A 1 99  ? 7.31700   -22.83700 6.97900   1.000 23.64000  ? 99  VAL A HG12 1 
ATOM   1804 H  HG13 . VAL A 1 99  ? 8.13200   -24.19200 7.13000   1.000 23.64000  ? 99  VAL A HG13 1 
ATOM   1805 H  HG21 . VAL A 1 99  ? 7.03900   -25.76100 5.06700   1.000 23.05000  ? 99  VAL A HG21 1 
ATOM   1806 H  HG22 . VAL A 1 99  ? 6.91500   -26.43400 6.50000   1.000 23.05000  ? 99  VAL A HG22 1 
ATOM   1807 H  HG23 . VAL A 1 99  ? 5.62600   -26.26600 5.58700   1.000 23.05000  ? 99  VAL A HG23 1 
ATOM   1808 N  N    . SER A 1 100 ? 6.77500   -24.15200 9.85600   1.000 19.53000  ? 100 SER A N    1 
ATOM   1809 C  CA   . SER A 1 100 ? 7.59300   -24.46900 11.01000  1.000 18.86000  ? 100 SER A CA   1 
ATOM   1810 C  C    . SER A 1 100 ? 6.77300   -24.86500 12.22800  1.000 23.95000  ? 100 SER A C    1 
ATOM   1811 O  O    . SER A 1 100 ? 7.36500   -25.10800 13.28800  1.000 34.74000  ? 100 SER A O    1 
ATOM   1812 C  CB   . SER A 1 100 ? 8.45600   -23.25300 11.36200  1.000 24.15000  ? 100 SER A CB   1 
ATOM   1813 O  OG   . SER A 1 100 ? 9.35500   -22.94500 10.32600  1.000 26.90000  ? 100 SER A OG   1 
ATOM   1814 H  H    . SER A 1 100 ? 6.56300   -23.31900 9.80900   1.000 23.42000  ? 100 SER A H    1 
ATOM   1815 H  HA   . SER A 1 100 ? 8.17200   -25.21500 10.79100  1.000 22.62000  ? 100 SER A HA   1 
ATOM   1816 H  HB2  . SER A 1 100 ? 7.87700   -22.49000 11.51200  1.000 28.96000  ? 100 SER A HB2  1 
ATOM   1817 H  HB3  . SER A 1 100 ? 8.96100   -23.45000 12.16600  1.000 28.96000  ? 100 SER A HB3  1 
ATOM   1818 H  HG   . SER A 1 100 ? 8.93200   -22.69900 9.64300   1.000 32.27000  ? 100 SER A HG   1 
ATOM   1819 N  N    A ASP A 1 101 ? 5.45100   -24.98400 12.09500  0.590 21.79000  ? 101 ASP A N    1 
ATOM   1820 N  N    B ASP A 1 101 ? 5.45200   -24.95100 12.11900  0.410 22.01000  ? 101 ASP A N    1 
ATOM   1821 C  CA   A ASP A 1 101 ? 4.53000   -25.12400 13.22500  0.590 27.15000  ? 101 ASP A CA   1 
ATOM   1822 C  CA   B ASP A 1 101 ? 4.61300   -25.10000 13.30400  0.410 27.40000  ? 101 ASP A CA   1 
ATOM   1823 C  C    A ASP A 1 101 ? 4.33800   -26.56200 13.67400  0.590 29.65000  ? 101 ASP A C    1 
ATOM   1824 C  C    B ASP A 1 101 ? 4.55300   -26.52900 13.82300  0.410 30.44000  ? 101 ASP A C    1 
ATOM   1825 O  O    A ASP A 1 101 ? 3.49900   -26.81200 14.54600  0.590 27.50000  ? 101 ASP A O    1 
ATOM   1826 O  O    B ASP A 1 101 ? 4.10200   -26.73400 14.95400  0.410 26.26000  ? 101 ASP A O    1 
ATOM   1827 C  CB   A ASP A 1 101 ? 3.15400   -24.51100 12.90400  0.590 33.71000  ? 101 ASP A CB   1 
ATOM   1828 C  CB   B ASP A 1 101 ? 3.19800   -24.58400 13.03000  0.410 32.74000  ? 101 ASP A CB   1 
ATOM   1829 C  CG   A ASP A 1 101 ? 2.22100   -25.46000 12.12500  0.590 37.02000  ? 101 ASP A CG   1 
ATOM   1830 C  CG   B ASP A 1 101 ? 2.45400   -24.21200 14.30000  0.410 41.76000  ? 101 ASP A CG   1 
ATOM   1831 O  OD1  A ASP A 1 101 ? 2.64300   -26.53500 11.64000  0.590 27.08000  ? 101 ASP A OD1  1 
ATOM   1832 O  OD1  B ASP A 1 101 ? 3.09400   -23.68400 15.24000  0.410 41.22000  ? 101 ASP A OD1  1 
ATOM   1833 O  OD2  A ASP A 1 101 ? 1.03100   -25.11400 11.98500  0.590 37.98000  ? 101 ASP A OD2  1 
ATOM   1834 O  OD2  B ASP A 1 101 ? 1.22600   -24.44100 14.35300  0.410 43.78000  ? 101 ASP A OD2  1 
ATOM   1835 H  H    A ASP A 1 101 ? 5.04900   -24.98500 11.33400  0.590 26.14000  ? 101 ASP A H    1 
ATOM   1836 H  H    B ASP A 1 101 ? 5.02000   -24.92600 11.37600  0.410 26.40000  ? 101 ASP A H    1 
ATOM   1837 H  HA   A ASP A 1 101 ? 4.90900   -24.62500 13.96500  0.590 32.57000  ? 101 ASP A HA   1 
ATOM   1838 H  HA   B ASP A 1 101 ? 4.98900   -24.55100 14.00900  0.410 32.87000  ? 101 ASP A HA   1 
ATOM   1839 H  HB2  A ASP A 1 101 ? 2.71300   -24.27900 13.73600  0.590 40.44000  ? 101 ASP A HB2  1 
ATOM   1840 H  HB2  B ASP A 1 101 ? 3.25200   -23.79300 12.47100  0.410 39.27000  ? 101 ASP A HB2  1 
ATOM   1841 H  HB3  A ASP A 1 101 ? 3.28400   -23.71500 12.36500  0.590 40.44000  ? 101 ASP A HB3  1 
ATOM   1842 H  HB3  B ASP A 1 101 ? 2.69100   -25.27600 12.57800  0.410 39.27000  ? 101 ASP A HB3  1 
ATOM   1843 N  N    . GLY A 1 102 ? 5.04700   -27.50500 13.06700  1.000 23.37000  ? 102 GLY A N    1 
ATOM   1844 C  CA   . GLY A 1 102 ? 4.98700   -28.88800 13.49700  1.000 25.58000  ? 102 GLY A CA   1 
ATOM   1845 C  C    . GLY A 1 102 ? 4.57400   -29.84800 12.39900  1.000 21.87000  ? 102 GLY A C    1 
ATOM   1846 O  O    . GLY A 1 102 ? 5.09600   -30.96600 12.32100  1.000 25.43000  ? 102 GLY A O    1 
ATOM   1847 H  H    . GLY A 1 102 ? 5.57100   -27.36500 12.40000  1.000 28.03000  ? 102 GLY A H    1 
ATOM   1848 H  HA2  . GLY A 1 102 ? 5.86200   -29.15700 13.81700  1.000 30.69000  ? 102 GLY A HA2  1 
ATOM   1849 H  HA3  . GLY A 1 102 ? 4.34800   -28.96700 14.22200  1.000 30.69000  ? 102 GLY A HA3  1 
ATOM   1850 N  N    . ASN A 1 103 ? 3.65100   -29.42300 11.53100  1.000 22.07000  ? 103 ASN A N    1 
ATOM   1851 C  CA   . ASN A 1 103 ? 3.04900   -30.30000 10.53600  1.000 20.83000  ? 103 ASN A CA   1 
ATOM   1852 C  C    . ASN A 1 103 ? 3.62200   -30.08400 9.14600   1.000 15.02000  ? 103 ASN A C    1 
ATOM   1853 O  O    . ASN A 1 103 ? 3.14000   -30.70800 8.18700   1.000 17.44000  ? 103 ASN A O    1 
ATOM   1854 C  CB   . ASN A 1 103 ? 1.53400   -30.09600 10.47300  1.000 30.54000  ? 103 ASN A CB   1 
ATOM   1855 C  CG   . ASN A 1 103 ? 0.84300   -30.50500 11.75000  1.000 65.23000  ? 103 ASN A CG   1 
ATOM   1856 O  OD1  . ASN A 1 103 ? 0.14600   -29.71100 12.38300  1.000 66.68000  ? 103 ASN A OD1  1 
ATOM   1857 N  ND2  . ASN A 1 103 ? 1.04200   -31.75200 12.14400  1.000 43.92000  ? 103 ASN A ND2  1 
ATOM   1858 H  H    . ASN A 1 103 ? 3.35500   -28.61600 11.50200  1.000 26.47000  ? 103 ASN A H    1 
ATOM   1859 H  HA   . ASN A 1 103 ? 3.21700   -31.21600 10.80900  1.000 24.99000  ? 103 ASN A HA   1 
ATOM   1860 H  HB2  . ASN A 1 103 ? 1.34700   -29.15700 10.31700  1.000 36.64000  ? 103 ASN A HB2  1 
ATOM   1861 H  HB3  . ASN A 1 103 ? 1.17200   -30.63100 9.74900   1.000 36.64000  ? 103 ASN A HB3  1 
ATOM   1862 H  HD21 . ASN A 1 103 ? 1.54100   -32.27600 11.67900  1.000 52.70000  ? 103 ASN A HD21 1 
ATOM   1863 H  HD22 . ASN A 1 103 ? 0.67200   -32.03900 12.86600  1.000 52.70000  ? 103 ASN A HD22 1 
ATOM   1864 N  N    . GLY A 1 104 ? 4.61500   -29.22500 9.01400   1.000 16.28000  ? 104 GLY A N    1 
ATOM   1865 C  CA   . GLY A 1 104 ? 5.21600   -29.01700 7.70900   1.000 15.25000  ? 104 GLY A CA   1 
ATOM   1866 C  C    . GLY A 1 104 ? 4.18000   -28.50000 6.74000   1.000 15.05000  ? 104 GLY A C    1 
ATOM   1867 O  O    . GLY A 1 104 ? 3.26200   -27.76000 7.11500   1.000 15.61000  ? 104 GLY A O    1 
ATOM   1868 H  H    . GLY A 1 104 ? 4.95500   -28.75800 9.65100   1.000 19.52000  ? 104 GLY A H    1 
ATOM   1869 H  HA2  . GLY A 1 104 ? 5.93600   -28.37100 7.77600   1.000 18.28000  ? 104 GLY A HA2  1 
ATOM   1870 H  HA3  . GLY A 1 104 ? 5.57300   -29.85400 7.37200   1.000 18.28000  ? 104 GLY A HA3  1 
ATOM   1871 N  N    . MET A 1 105 ? 4.28200   -28.93200 5.49900   1.000 13.47000  ? 105 MET A N    1 
ATOM   1872 C  CA   . MET A 1 105 ? 3.41600   -28.38600 4.48000   1.000 13.67000  ? 105 MET A CA   1 
ATOM   1873 C  C    . MET A 1 105 ? 2.06400   -29.08100 4.50600   1.000 13.76000  ? 105 MET A C    1 
ATOM   1874 O  O    . MET A 1 105 ? 1.17300   -28.72400 3.74900   1.000 13.71000  ? 105 MET A O    1 
ATOM   1875 C  CB   . MET A 1 105 ? 4.18200   -28.58600 3.19100   1.000 14.02000  ? 105 MET A CB   1 
ATOM   1876 C  CG   . MET A 1 105 ? 4.90500   -27.32600 2.76000   1.000 15.36000  ? 105 MET A CG   1 
ATOM   1877 S  SD   . MET A 1 105 ? 5.48400   -27.20400 1.07700   1.000 16.45000  ? 105 MET A SD   1 
ATOM   1878 C  CE   . MET A 1 105 ? 4.14500   -26.16300 0.45600   1.000 21.00000  ? 105 MET A CE   1 
ATOM   1879 H  H    . MET A 1 105 ? 4.83600   -29.53100 5.22800   1.000 16.15000  ? 105 MET A H    1 
ATOM   1880 H  HA   . MET A 1 105 ? 3.22300   -27.44000 4.56800   1.000 16.40000  ? 105 MET A HA   1 
ATOM   1881 H  HB2  . MET A 1 105 ? 4.84200   -29.28600 3.31700   1.000 16.82000  ? 105 MET A HB2  1 
ATOM   1882 H  HB3  . MET A 1 105 ? 3.56300   -28.83700 2.48700   1.000 16.82000  ? 105 MET A HB3  1 
ATOM   1883 H  HG2  . MET A 1 105 ? 4.30000   -26.58000 2.89700   1.000 18.42000  ? 105 MET A HG2  1 
ATOM   1884 H  HG3  . MET A 1 105 ? 5.68600   -27.22700 3.32700   1.000 18.42000  ? 105 MET A HG3  1 
ATOM   1885 H  HE1  . MET A 1 105 ? 4.28300   -26.00200 -0.49000  1.000 25.19000  ? 105 MET A HE1  1 
ATOM   1886 H  HE2  . MET A 1 105 ? 3.30000   -26.62000 0.59400   1.000 25.19000  ? 105 MET A HE2  1 
ATOM   1887 H  HE3  . MET A 1 105 ? 4.14800   -25.32200 0.93900   1.000 25.19000  ? 105 MET A HE3  1 
ATOM   1888 N  N    . ASN A 1 106 ? 1.87900   -30.07800 5.38100   1.000 14.99000  ? 106 ASN A N    1 
ATOM   1889 C  CA   . ASN A 1 106 ? 0.55100   -30.65600 5.56300   1.000 14.48000  ? 106 ASN A CA   1 
ATOM   1890 C  C    . ASN A 1 106 ? -0.45100  -29.64100 6.07200   1.000 14.51000  ? 106 ASN A C    1 
ATOM   1891 O  O    . ASN A 1 106 ? -1.66300  -29.89000 5.98200   1.000 17.07000  ? 106 ASN A O    1 
ATOM   1892 C  CB   . ASN A 1 106 ? 0.58800   -31.83300 6.52000   1.000 16.27000  ? 106 ASN A CB   1 
ATOM   1893 C  CG   . ASN A 1 106 ? 1.40700   -33.00400 5.98500   1.000 14.08000  ? 106 ASN A CG   1 
ATOM   1894 O  OD1  . ASN A 1 106 ? 1.05300   -33.64800 5.02300   1.000 16.72000  ? 106 ASN A OD1  1 
ATOM   1895 N  ND2  . ASN A 1 106 ? 2.57800   -33.19400 6.57500   1.000 18.52000  ? 106 ASN A ND2  1 
ATOM   1896 H  H    . ASN A 1 106 ? 2.49600   -30.42700 5.86800   1.000 17.98000  ? 106 ASN A H    1 
ATOM   1897 H  HA   . ASN A 1 106 ? 0.25600   -30.99200 4.70200   1.000 17.36000  ? 106 ASN A HA   1 
ATOM   1898 H  HB2  . ASN A 1 106 ? 0.98400   -31.54800 7.35800   1.000 19.51000  ? 106 ASN A HB2  1 
ATOM   1899 H  HB3  . ASN A 1 106 ? -0.31800  -32.14600 6.67100   1.000 19.51000  ? 106 ASN A HB3  1 
ATOM   1900 H  HD21 . ASN A 1 106 ? 3.08900   -33.83700 6.32100   1.000 22.21000  ? 106 ASN A HD21 1 
ATOM   1901 H  HD22 . ASN A 1 106 ? 2.82800   -32.67400 7.21300   1.000 22.21000  ? 106 ASN A HD22 1 
ATOM   1902 N  N    . ALA A 1 107 ? 0.02500   -28.49400 6.56900   1.000 14.51000  ? 107 ALA A N    1 
ATOM   1903 C  CA   . ALA A 1 107 ? -0.88600  -27.42000 6.94300   1.000 16.91000  ? 107 ALA A CA   1 
ATOM   1904 C  C    . ALA A 1 107 ? -1.72100  -26.95200 5.76700   1.000 16.71000  ? 107 ALA A C    1 
ATOM   1905 O  O    . ALA A 1 107 ? -2.81800  -26.40600 5.96300   1.000 18.72000  ? 107 ALA A O    1 
ATOM   1906 C  CB   . ALA A 1 107 ? -0.08800  -26.23400 7.47000   1.000 19.81000  ? 107 ALA A CB   1 
ATOM   1907 H  H    . ALA A 1 107 ? 0.85800   -28.32000 6.69600   1.000 17.40000  ? 107 ALA A H    1 
ATOM   1908 H  HA   . ALA A 1 107 ? -1.47900  -27.75100 7.63600   1.000 20.28000  ? 107 ALA A HA   1 
ATOM   1909 H  HB1  . ALA A 1 107 ? -0.69800  -25.50700 7.66900   1.000 23.76000  ? 107 ALA A HB1  1 
ATOM   1910 H  HB2  . ALA A 1 107 ? 0.38200   -26.50200 8.27500   1.000 23.76000  ? 107 ALA A HB2  1 
ATOM   1911 H  HB3  . ALA A 1 107 ? 0.54800   -25.95600 6.79200   1.000 23.76000  ? 107 ALA A HB3  1 
ATOM   1912 N  N    . TRP A 1 108 ? -1.20700  -27.08900 4.54400   1.000 14.15000  ? 108 TRP A N    1 
ATOM   1913 C  CA   . TRP A 1 108 ? -1.95800  -26.76600 3.34000   1.000 13.12000  ? 108 TRP A CA   1 
ATOM   1914 C  C    . TRP A 1 108 ? -2.61400  -28.04300 2.84300   1.000 15.76000  ? 108 TRP A C    1 
ATOM   1915 O  O    . TRP A 1 108 ? -1.95400  -28.93800 2.29200   1.000 15.61000  ? 108 TRP A O    1 
ATOM   1916 C  CB   . TRP A 1 108 ? -1.06300  -26.16700 2.26900   1.000 15.90000  ? 108 TRP A CB   1 
ATOM   1917 C  CG   . TRP A 1 108 ? -0.62900  -24.77700 2.55300   1.000 13.64000  ? 108 TRP A CG   1 
ATOM   1918 C  CD1  . TRP A 1 108 ? -1.27600  -23.63600 2.17400   1.000 15.38000  ? 108 TRP A CD1  1 
ATOM   1919 C  CD2  . TRP A 1 108 ? 0.54100   -24.35800 3.25700   1.000 13.13000  ? 108 TRP A CD2  1 
ATOM   1920 N  NE1  . TRP A 1 108 ? -0.58800  -22.54000 2.60800   1.000 15.78000  ? 108 TRP A NE1  1 
ATOM   1921 C  CE2  . TRP A 1 108 ? 0.53800   -22.95200 3.27700   1.000 14.74000  ? 108 TRP A CE2  1 
ATOM   1922 C  CE3  . TRP A 1 108 ? 1.59500   -25.03900 3.87800   1.000 15.45000  ? 108 TRP A CE3  1 
ATOM   1923 C  CZ2  . TRP A 1 108 ? 1.54200   -22.22800 3.88300   1.000 14.85000  ? 108 TRP A CZ2  1 
ATOM   1924 C  CZ3  . TRP A 1 108 ? 2.58600   -24.29300 4.50500   1.000 17.45000  ? 108 TRP A CZ3  1 
ATOM   1925 C  CH2  . TRP A 1 108 ? 2.55700   -22.90800 4.47800   1.000 15.93000  ? 108 TRP A CH2  1 
ATOM   1926 H  H    . TRP A 1 108 ? -0.41100  -27.37300 4.38700   1.000 16.97000  ? 108 TRP A H    1 
ATOM   1927 H  HA   . TRP A 1 108 ? -2.64000  -26.11000 3.55400   1.000 15.73000  ? 108 TRP A HA   1 
ATOM   1928 H  HB2  . TRP A 1 108 ? -0.26700  -26.71400 2.18700   1.000 19.07000  ? 108 TRP A HB2  1 
ATOM   1929 H  HB3  . TRP A 1 108 ? -1.54700  -26.15900 1.42800   1.000 19.07000  ? 108 TRP A HB3  1 
ATOM   1930 H  HD1  . TRP A 1 108 ? -2.07000  -23.61000 1.69000   1.000 18.45000  ? 108 TRP A HD1  1 
ATOM   1931 H  HE1  . TRP A 1 108 ? -0.82300  -21.72200 2.48300   1.000 18.92000  ? 108 TRP A HE1  1 
ATOM   1932 H  HE3  . TRP A 1 108 ? 1.63100   -25.96900 3.87200   1.000 18.53000  ? 108 TRP A HE3  1 
ATOM   1933 H  HZ2  . TRP A 1 108 ? 1.52500   -21.29800 3.88400   1.000 17.80000  ? 108 TRP A HZ2  1 
ATOM   1934 H  HZ3  . TRP A 1 108 ? 3.27700   -24.73000 4.94900   1.000 20.92000  ? 108 TRP A HZ3  1 
ATOM   1935 H  HH2  . TRP A 1 108 ? 3.25000   -22.43200 4.87600   1.000 19.11000  ? 108 TRP A HH2  1 
ATOM   1936 N  N    A VAL A 1 109 ? -3.92600  -28.11900 3.04800   0.460 17.17000  ? 109 VAL A N    1 
ATOM   1937 N  N    B VAL A 1 109 ? -3.92300  -28.17000 3.04100   0.540 17.04000  ? 109 VAL A N    1 
ATOM   1938 C  CA   A VAL A 1 109 ? -4.69900  -29.28600 2.64200   0.460 18.94000  ? 109 VAL A CA   1 
ATOM   1939 C  CA   B VAL A 1 109 ? -4.55500  -29.42500 2.64400   0.540 17.72000  ? 109 VAL A CA   1 
ATOM   1940 C  C    A VAL A 1 109 ? -4.44100  -29.62100 1.18200   0.460 15.88000  ? 109 VAL A C    1 
ATOM   1941 C  C    B VAL A 1 109 ? -4.44700  -29.66000 1.14000   0.540 15.90000  ? 109 VAL A C    1 
ATOM   1942 O  O    A VAL A 1 109 ? -4.25100  -30.78800 0.82000   0.460 18.23000  ? 109 VAL A O    1 
ATOM   1943 O  O    B VAL A 1 109 ? -4.35500  -30.81300 0.70300   0.540 19.52000  ? 109 VAL A O    1 
ATOM   1944 C  CB   A VAL A 1 109 ? -6.19200  -29.03500 2.91200   0.460 18.13000  ? 109 VAL A CB   1 
ATOM   1945 C  CB   B VAL A 1 109 ? -6.00100  -29.51200 3.16500   0.540 23.52000  ? 109 VAL A CB   1 
ATOM   1946 C  CG1  A VAL A 1 109 ? -6.99100  -30.25800 2.55500   0.460 19.05000  ? 109 VAL A CG1  1 
ATOM   1947 C  CG1  B VAL A 1 109 ? -6.01000  -29.39200 4.67900   0.540 27.97000  ? 109 VAL A CG1  1 
ATOM   1948 C  CG2  A VAL A 1 109 ? -6.39900  -28.65000 4.36600   0.460 29.13000  ? 109 VAL A CG2  1 
ATOM   1949 C  CG2  B VAL A 1 109 ? -6.85600  -28.45400 2.50700   0.540 26.32000  ? 109 VAL A CG2  1 
ATOM   1950 H  H    A VAL A 1 109 ? -4.39600  -27.50400 3.42300   0.460 20.60000  ? 109 VAL A H    1 
ATOM   1951 H  H    B VAL A 1 109 ? -4.44100  -27.57600 3.38500   0.540 20.43000  ? 109 VAL A H    1 
ATOM   1952 H  HA   A VAL A 1 109 ? -4.41300  -30.05000 3.16600   0.460 22.71000  ? 109 VAL A HA   1 
ATOM   1953 H  HA   B VAL A 1 109 ? -4.06500  -30.14700 3.06900   0.540 21.25000  ? 109 VAL A HA   1 
ATOM   1954 H  HB   A VAL A 1 109 ? -6.50700  -28.30100 2.36100   0.460 21.74000  ? 109 VAL A HB   1 
ATOM   1955 H  HB   B VAL A 1 109 ? -6.38700  -30.37300 2.93900   0.540 28.21000  ? 109 VAL A HB   1 
ATOM   1956 H  HG11 A VAL A 1 109 ? -7.91400  -30.12200 2.82200   0.460 22.85000  ? 109 VAL A HG11 1 
ATOM   1957 H  HG11 B VAL A 1 109 ? -6.87200  -29.68300 5.01500   0.540 33.55000  ? 109 VAL A HG11 1 
ATOM   1958 H  HG12 A VAL A 1 109 ? -6.94100  -30.40000 1.59600   0.460 22.85000  ? 109 VAL A HG12 1 
ATOM   1959 H  HG12 B VAL A 1 109 ? -5.30600  -29.95100 5.04400   0.540 33.55000  ? 109 VAL A HG12 1 
ATOM   1960 H  HG13 A VAL A 1 109 ? -6.62100  -31.02400 3.02200   0.460 22.85000  ? 109 VAL A HG13 1 
ATOM   1961 H  HG13 B VAL A 1 109 ? -5.85600  -28.46500 4.92300   0.540 33.55000  ? 109 VAL A HG13 1 
ATOM   1962 H  HG21 A VAL A 1 109 ? -7.34400  -28.71300 4.57800   0.460 34.95000  ? 109 VAL A HG21 1 
ATOM   1963 H  HG21 B VAL A 1 109 ? -7.36000  -27.98500 3.19000   0.540 31.57000  ? 109 VAL A HG21 1 
ATOM   1964 H  HG22 A VAL A 1 109 ? -5.89300  -29.25700 4.92800   0.460 34.95000  ? 109 VAL A HG22 1 
ATOM   1965 H  HG22 B VAL A 1 109 ? -6.28100  -27.83300 2.03400   0.540 31.57000  ? 109 VAL A HG22 1 
ATOM   1966 H  HG23 A VAL A 1 109 ? -6.09000  -27.74100 4.49900   0.460 34.95000  ? 109 VAL A HG23 1 
ATOM   1967 H  HG23 B VAL A 1 109 ? -7.46400  -28.88200 1.88400   0.540 31.57000  ? 109 VAL A HG23 1 
ATOM   1968 N  N    . ALA A 1 110 ? -4.44800  -28.60600 0.32600   1.000 17.37000  ? 110 ALA A N    1 
ATOM   1969 C  CA   . ALA A 1 110 ? -4.26900  -28.83600 -1.10300  1.000 15.50000  ? 110 ALA A CA   1 
ATOM   1970 C  C    . ALA A 1 110 ? -2.88200  -29.38900 -1.41600  1.000 17.34000  ? 110 ALA A C    1 
ATOM   1971 O  O    . ALA A 1 110 ? -2.73300  -30.16600 -2.36400  1.000 19.31000  ? 110 ALA A O    1 
ATOM   1972 C  CB   . ALA A 1 110 ? -4.48800  -27.55400 -1.89000  1.000 20.86000  ? 110 ALA A CB   1 
ATOM   1973 H  H    . ALA A 1 110 ? -4.54700  -27.78700 0.56900   1.000 20.83000  ? 110 ALA A H    1 
ATOM   1974 H  HA   . ALA A 1 110 ? -4.93600  -29.48100 -1.38400  1.000 18.59000  ? 110 ALA A HA   1 
ATOM   1975 H  HB1  . ALA A 1 110 ? -4.41600  -27.74900 -2.83800  1.000 25.02000  ? 110 ALA A HB1  1 
ATOM   1976 H  HB2  . ALA A 1 110 ? -5.37100  -27.20700 -1.69000  1.000 25.02000  ? 110 ALA A HB2  1 
ATOM   1977 H  HB3  . ALA A 1 110 ? -3.81200  -26.90700 -1.63400  1.000 25.02000  ? 110 ALA A HB3  1 
ATOM   1978 N  N    . TRP A 1 111 ? -1.85600  -29.00600 -0.65800  1.000 14.42000  ? 111 TRP A N    1 
ATOM   1979 C  CA   . TRP A 1 111 ? -0.54900  -29.62300 -0.86200  1.000 15.09000  ? 111 TRP A CA   1 
ATOM   1980 C  C    . TRP A 1 111 ? -0.60600  -31.11600 -0.54800  1.000 13.98000  ? 111 TRP A C    1 
ATOM   1981 O  O    . TRP A 1 111 ? -0.12400  -31.94000 -1.32500  1.000 14.44000  ? 111 TRP A O    1 
ATOM   1982 C  CB   . TRP A 1 111 ? 0.53800   -28.93500 -0.03100  1.000 13.65000  ? 111 TRP A CB   1 
ATOM   1983 C  CG   . TRP A 1 111 ? 1.86600   -29.59900 -0.19800  1.000 13.20000  ? 111 TRP A CG   1 
ATOM   1984 C  CD1  . TRP A 1 111 ? 2.77900   -29.38800 -1.19600  1.000 15.78000  ? 111 TRP A CD1  1 
ATOM   1985 C  CD2  . TRP A 1 111 ? 2.42600   -30.61300 0.64000   1.000 14.94000  ? 111 TRP A CD2  1 
ATOM   1986 N  NE1  . TRP A 1 111 ? 3.85800   -30.22200 -1.02600  1.000 13.70000  ? 111 TRP A NE1  1 
ATOM   1987 C  CE2  . TRP A 1 111 ? 3.66600   -30.98400 0.08700   1.000 12.99000  ? 111 TRP A CE2  1 
ATOM   1988 C  CE3  . TRP A 1 111 ? 1.99000   -31.25500 1.79700   1.000 15.83000  ? 111 TRP A CE3  1 
ATOM   1989 C  CZ2  . TRP A 1 111 ? 4.48300   -31.93400 0.67900   1.000 17.87000  ? 111 TRP A CZ2  1 
ATOM   1990 C  CZ3  . TRP A 1 111 ? 2.79800   -32.18700 2.39100   1.000 16.55000  ? 111 TRP A CZ3  1 
ATOM   1991 C  CH2  . TRP A 1 111 ? 4.02000   -32.53900 1.82800   1.000 17.98000  ? 111 TRP A CH2  1 
ATOM   1992 H  H    . TRP A 1 111 ? -1.88900  -28.41100 -0.03900  1.000 17.29000  ? 111 TRP A H    1 
ATOM   1993 H  HA   . TRP A 1 111 ? -0.30400  -29.50500 -1.79300  1.000 18.09000  ? 111 TRP A HA   1 
ATOM   1994 H  HB2  . TRP A 1 111 ? 0.62200   -28.01100 -0.31700  1.000 16.36000  ? 111 TRP A HB2  1 
ATOM   1995 H  HB3  . TRP A 1 111 ? 0.29500   -28.97100 0.90700   1.000 16.36000  ? 111 TRP A HB3  1 
ATOM   1996 H  HD1  . TRP A 1 111 ? 2.68300   -28.77200 -1.88600  1.000 18.92000  ? 111 TRP A HD1  1 
ATOM   1997 H  HE1  . TRP A 1 111 ? 4.54500   -30.25800 -1.54100  1.000 16.43000  ? 111 TRP A HE1  1 
ATOM   1998 H  HE3  . TRP A 1 111 ? 1.16000   -31.05200 2.16200   1.000 18.98000  ? 111 TRP A HE3  1 
ATOM   1999 H  HZ2  . TRP A 1 111 ? 5.31000   -32.15400 0.31600   1.000 21.43000  ? 111 TRP A HZ2  1 
ATOM   2000 H  HZ3  . TRP A 1 111 ? 2.52500   -32.59200 3.18300   1.000 19.85000  ? 111 TRP A HZ3  1 
ATOM   2001 H  HH2  . TRP A 1 111 ? 4.53600   -33.19700 2.23500   1.000 21.56000  ? 111 TRP A HH2  1 
ATOM   2002 N  N    A ARG A 1 112 ? -1.17600  -31.48800 0.60400   0.650 13.89000  ? 112 ARG A N    1 
ATOM   2003 N  N    B ARG A 1 112 ? -1.22500  -31.47100 0.57700   0.350 14.10000  ? 112 ARG A N    1 
ATOM   2004 C  CA   A ARG A 1 112 ? -1.25200  -32.89600 0.97600   0.650 16.59000  ? 112 ARG A CA   1 
ATOM   2005 C  CA   B ARG A 1 112 ? -1.26700  -32.85700 1.01300   0.350 16.65000  ? 112 ARG A CA   1 
ATOM   2006 C  C    A ARG A 1 112 ? -1.99800  -33.69100 -0.08600  0.650 14.56000  ? 112 ARG A C    1 
ATOM   2007 C  C    B ARG A 1 112 ? -2.07900  -33.72200 0.06000   0.350 15.03000  ? 112 ARG A C    1 
ATOM   2008 O  O    A ARG A 1 112 ? -1.52200  -34.73400 -0.54300  0.650 14.78000  ? 112 ARG A O    1 
ATOM   2009 O  O    B ARG A 1 112 ? -1.75900  -34.90200 -0.11300  0.350 16.62000  ? 112 ARG A O    1 
ATOM   2010 C  CB   A ARG A 1 112 ? -1.92900  -33.04700 2.34000   0.650 19.05000  ? 112 ARG A CB   1 
ATOM   2011 C  CB   B ARG A 1 112 ? -1.86100  -32.91400 2.41600   0.350 19.46000  ? 112 ARG A CB   1 
ATOM   2012 C  CG   A ARG A 1 112 ? -2.28300  -34.48900 2.70800   0.650 24.97000  ? 112 ARG A CG   1 
ATOM   2013 C  CG   B ARG A 1 112 ? -1.78200  -34.26200 3.08900   0.350 23.72000  ? 112 ARG A CG   1 
ATOM   2014 C  CD   A ARG A 1 112 ? -2.90700  -34.60100 4.09900   0.650 31.59000  ? 112 ARG A CD   1 
ATOM   2015 C  CD   B ARG A 1 112 ? -2.20700  -34.14800 4.54700   0.350 31.48000  ? 112 ARG A CD   1 
ATOM   2016 N  NE   A ARG A 1 112 ? -3.18200  -35.99600 4.41900   0.650 32.51000  ? 112 ARG A NE   1 
ATOM   2017 N  NE   B ARG A 1 112 ? -3.37500  -33.29000 4.71200   0.350 29.07000  ? 112 ARG A NE   1 
ATOM   2018 C  CZ   A ARG A 1 112 ? -4.28800  -36.64700 4.08400   0.650 49.70000  ? 112 ARG A CZ   1 
ATOM   2019 C  CZ   B ARG A 1 112 ? -4.62200  -33.65800 4.45300   0.350 28.37000  ? 112 ARG A CZ   1 
ATOM   2020 N  NH1  A ARG A 1 112 ? -5.29000  -36.04000 3.46100   0.650 32.59000  ? 112 ARG A NH1  1 
ATOM   2021 N  NH1  B ARG A 1 112 ? -4.90700  -34.86100 3.98400   0.350 36.82000  ? 112 ARG A NH1  1 
ATOM   2022 N  NH2  A ARG A 1 112 ? -4.39200  -37.94000 4.37900   0.650 46.35000  ? 112 ARG A NH2  1 
ATOM   2023 N  NH2  B ARG A 1 112 ? -5.61200  -32.79800 4.67700   0.350 33.13000  ? 112 ARG A NH2  1 
ATOM   2024 H  H    A ARG A 1 112 ? -1.52000  -30.94900 1.17900   0.650 16.65000  ? 112 ARG A H    1 
ATOM   2025 H  H    B ARG A 1 112 ? -1.62900  -30.92600 1.10500   0.350 16.91000  ? 112 ARG A H    1 
ATOM   2026 H  HA   A ARG A 1 112 ? -0.35300  -33.25300 1.05100   0.650 19.90000  ? 112 ARG A HA   1 
ATOM   2027 H  HA   B ARG A 1 112 ? -0.36600  -33.21700 1.03700   0.350 19.97000  ? 112 ARG A HA   1 
ATOM   2028 H  HB2  A ARG A 1 112 ? -1.32900  -32.70700 3.02300   0.650 22.84000  ? 112 ARG A HB2  1 
ATOM   2029 H  HB2  B ARG A 1 112 ? -1.38500  -32.28100 2.97700   0.350 23.34000  ? 112 ARG A HB2  1 
ATOM   2030 H  HB3  A ARG A 1 112 ? -2.75200  -32.53300 2.33600   0.650 22.84000  ? 112 ARG A HB3  1 
ATOM   2031 H  HB3  B ARG A 1 112 ? -2.79800  -32.67000 2.36300   0.350 23.34000  ? 112 ARG A HB3  1 
ATOM   2032 H  HG2  A ARG A 1 112 ? -2.92000  -34.83400 2.06300   0.650 29.95000  ? 112 ARG A HG2  1 
ATOM   2033 H  HG2  B ARG A 1 112 ? -2.37400  -34.88600 2.64000   0.350 28.45000  ? 112 ARG A HG2  1 
ATOM   2034 H  HG3  A ARG A 1 112 ? -1.47500  -35.02700 2.69700   0.650 29.95000  ? 112 ARG A HG3  1 
ATOM   2035 H  HG3  B ARG A 1 112 ? -0.86900  -34.59000 3.05600   0.350 28.45000  ? 112 ARG A HG3  1 
ATOM   2036 H  HD2  A ARG A 1 112 ? -2.29400  -34.24500 4.76100   0.650 37.89000  ? 112 ARG A HD2  1 
ATOM   2037 H  HD2  B ARG A 1 112 ? -2.42900  -35.03000 4.88500   0.350 37.76000  ? 112 ARG A HD2  1 
ATOM   2038 H  HD3  A ARG A 1 112 ? -3.74200  -34.10800 4.12100   0.650 37.89000  ? 112 ARG A HD3  1 
ATOM   2039 H  HD3  B ARG A 1 112 ? -1.47800  -33.77000 5.06400   0.350 37.76000  ? 112 ARG A HD3  1 
ATOM   2040 H  HE   A ARG A 1 112 ? -2.58200  -36.42900 4.85800   0.650 39.00000  ? 112 ARG A HE   1 
ATOM   2041 H  HE   B ARG A 1 112 ? -3.24600  -32.48900 4.99700   0.350 34.87000  ? 112 ARG A HE   1 
ATOM   2042 H  HH11 A ARG A 1 112 ? -5.23200  -35.20500 3.26500   0.650 39.10000  ? 112 ARG A HH11 1 
ATOM   2043 H  HH11 B ARG A 1 112 ? -4.27600  -35.42800 3.84100   0.350 44.17000  ? 112 ARG A HH11 1 
ATOM   2044 H  HH12 A ARG A 1 112 ? -5.99800  -36.48200 3.25300   0.650 39.10000  ? 112 ARG A HH12 1 
ATOM   2045 H  HH12 B ARG A 1 112 ? -5.72400  -35.07800 3.82300   0.350 44.17000  ? 112 ARG A HH12 1 
ATOM   2046 H  HH21 A ARG A 1 112 ? -3.74700  -38.34300 4.78100   0.650 55.61000  ? 112 ARG A HH21 1 
ATOM   2047 H  HH21 B ARG A 1 112 ? -5.44000  -32.01400 4.98600   0.350 39.74000  ? 112 ARG A HH21 1 
ATOM   2048 H  HH22 A ARG A 1 112 ? -5.10400  -38.37400 4.16700   0.650 55.61000  ? 112 ARG A HH22 1 
ATOM   2049 H  HH22 B ARG A 1 112 ? -6.42500  -33.02600 4.51200   0.350 39.74000  ? 112 ARG A HH22 1 
ATOM   2050 N  N    . ASN A 1 113 ? -3.13000  -33.16100 -0.54500  1.000 14.12000  ? 113 ASN A N    1 
ATOM   2051 C  CA   . ASN A 1 113 ? -4.00700  -33.91300 -1.44700  1.000 15.27000  ? 113 ASN A CA   1 
ATOM   2052 C  C    . ASN A 1 113 ? -3.63700  -33.85300 -2.92000  1.000 19.36000  ? 113 ASN A C    1 
ATOM   2053 O  O    . ASN A 1 113 ? -4.06900  -34.72600 -3.67600  1.000 19.25000  ? 113 ASN A O    1 
ATOM   2054 C  CB   . ASN A 1 113 ? -5.45500  -33.43100 -1.28200  1.000 14.78000  ? 113 ASN A CB   1 
ATOM   2055 C  CG   . ASN A 1 113 ? -6.03600  -33.83300 0.05200   1.000 17.16000  ? 113 ASN A CG   1 
ATOM   2056 O  OD1  . ASN A 1 113 ? -5.60000  -34.81700 0.65500   1.000 19.72000  ? 113 ASN A OD1  1 
ATOM   2057 N  ND2  . ASN A 1 113 ? -7.04800  -33.10200 0.50800   1.000 18.94000  ? 113 ASN A ND2  1 
ATOM   2058 H  H    . ASN A 1 113 ? -3.41400  -32.37300 -0.35200  1.000 16.93000  ? 113 ASN A H    1 
ATOM   2059 H  HA   . ASN A 1 113 ? -3.94400  -34.84600 -1.19200  1.000 18.31000  ? 113 ASN A HA   1 
ATOM   2060 H  HB2  . ASN A 1 113 ? -5.47800  -32.46300 -1.34300  1.000 17.72000  ? 113 ASN A HB2  1 
ATOM   2061 H  HB3  . ASN A 1 113 ? -6.00300  -33.82100 -1.98100  1.000 17.72000  ? 113 ASN A HB3  1 
ATOM   2062 H  HD21 . ASN A 1 113 ? -7.41100  -33.29400 1.26300   1.000 22.71000  ? 113 ASN A HD21 1 
ATOM   2063 H  HD22 . ASN A 1 113 ? -7.33900  -32.43700 0.04700   1.000 22.71000  ? 113 ASN A HD22 1 
ATOM   2064 N  N    . ARG A 1 114 ? -2.85100  -32.87300 -3.36400  1.000 16.53000  ? 114 ARG A N    1 
ATOM   2065 C  CA   . ARG A 1 114 ? -2.57300  -32.70400 -4.77700  1.000 16.31000  ? 114 ARG A CA   1 
ATOM   2066 C  C    . ARG A 1 114 ? -1.10200  -32.68000 -5.11800  1.000 16.89000  ? 114 ARG A C    1 
ATOM   2067 O  O    . ARG A 1 114 ? -0.76600  -32.92700 -6.28800  1.000 20.42000  ? 114 ARG A O    1 
ATOM   2068 C  CB   . ARG A 1 114 ? -3.23600  -31.43700 -5.28600  1.000 20.84000  ? 114 ARG A CB   1 
ATOM   2069 C  CG   . ARG A 1 114 ? -4.66800  -31.53600 -4.81900  1.000 26.51000  ? 114 ARG A CG   1 
ATOM   2070 C  CD   . ARG A 1 114 ? -5.50700  -30.56300 -5.41400  1.000 29.61000  ? 114 ARG A CD   1 
ATOM   2071 N  NE   . ARG A 1 114 ? -5.69100  -30.74700 -6.84200  1.000 20.00000  ? 114 ARG A NE   1 
ATOM   2072 C  CZ   . ARG A 1 114 ? -6.44100  -29.90700 -7.52900  1.000 20.61000  ? 114 ARG A CZ   1 
ATOM   2073 N  NH1  . ARG A 1 114 ? -7.07200  -28.91900 -6.92300  1.000 19.45000  ? 114 ARG A NH1  1 
ATOM   2074 N  NH2  . ARG A 1 114 ? -6.51400  -30.03500 -8.84400  1.000 23.02000  ? 114 ARG A NH2  1 
ATOM   2075 H  H    . ARG A 1 114 ? -2.46700  -32.29300 -2.85900  1.000 19.83000  ? 114 ARG A H    1 
ATOM   2076 H  HA   . ARG A 1 114 ? -2.95900  -33.44700 -5.26800  1.000 19.56000  ? 114 ARG A HA   1 
ATOM   2077 H  HB2  . ARG A 1 114 ? -2.81600  -30.65000 -4.90600  1.000 24.99000  ? 114 ARG A HB2  1 
ATOM   2078 H  HB3  . ARG A 1 114 ? -3.20400  -31.39500 -6.25500  1.000 24.99000  ? 114 ARG A HB3  1 
ATOM   2079 H  HG2  . ARG A 1 114 ? -5.01600  -32.41200 -5.04800  1.000 31.80000  ? 114 ARG A HG2  1 
ATOM   2080 H  HG3  . ARG A 1 114 ? -4.69700  -31.40900 -3.85800  1.000 31.80000  ? 114 ARG A HG3  1 
ATOM   2081 H  HD2  . ARG A 1 114 ? -6.38000  -30.60400 -4.99600  1.000 35.52000  ? 114 ARG A HD2  1 
ATOM   2082 H  HD3  . ARG A 1 114 ? -5.11400  -29.68600 -5.27800  1.000 35.52000  ? 114 ARG A HD3  1 
ATOM   2083 H  HE   . ARG A 1 114 ? -5.31000  -31.40600 -7.24200  1.000 23.99000  ? 114 ARG A HE   1 
ATOM   2084 H  HH11 . ARG A 1 114 ? -6.99600  -28.81800 -6.07200  1.000 23.33000  ? 114 ARG A HH11 1 
ATOM   2085 H  HH12 . ARG A 1 114 ? -7.55900  -28.37600 -7.37800  1.000 23.33000  ? 114 ARG A HH12 1 
ATOM   2086 H  HH21 . ARG A 1 114 ? -6.07600  -30.66000 -9.24000  1.000 27.61000  ? 114 ARG A HH21 1 
ATOM   2087 H  HH22 . ARG A 1 114 ? -7.00000  -29.49400 -9.30200  1.000 27.61000  ? 114 ARG A HH22 1 
ATOM   2088 N  N    . CYS A 1 115 ? -0.22100  -32.41900 -4.17600  1.000 13.74000  ? 115 CYS A N    1 
ATOM   2089 C  CA   . CYS A 1 115 ? 1.19100   -32.28600 -4.48800  1.000 13.61000  ? 115 CYS A CA   1 
ATOM   2090 C  C    . CYS A 1 115 ? 2.04500   -33.35000 -3.81900  1.000 16.48000  ? 115 CYS A C    1 
ATOM   2091 O  O    . CYS A 1 115 ? 3.00100   -33.86200 -4.42600  1.000 16.97000  ? 115 CYS A O    1 
ATOM   2092 C  CB   . CYS A 1 115 ? 1.69500   -30.90500 -4.04000  1.000 13.91000  ? 115 CYS A CB   1 
ATOM   2093 S  SG   . CYS A 1 115 ? 0.82200   -29.51800 -4.77500  1.000 15.62000  ? 115 CYS A SG   1 
ATOM   2094 H  H    . CYS A 1 115 ? -0.41400  -32.31300 -3.34500  1.000 16.47000  ? 115 CYS A H    1 
ATOM   2095 H  HA   . CYS A 1 115 ? 1.30600   -32.36100 -5.44800  1.000 16.32000  ? 115 CYS A HA   1 
ATOM   2096 H  HB2  . CYS A 1 115 ? 1.59600   -30.83700 -3.07800  1.000 16.68000  ? 115 CYS A HB2  1 
ATOM   2097 H  HB3  . CYS A 1 115 ? 2.63100   -30.82400 -4.28400  1.000 16.68000  ? 115 CYS A HB3  1 
ATOM   2098 N  N    . LYS A 1 116 ? 1.74800   -33.67900 -2.56500  1.000 15.27000  ? 116 LYS A N    1 
ATOM   2099 C  CA   . LYS A 1 116 ? 2.51800   -34.65900 -1.82300  1.000 15.67000  ? 116 LYS A CA   1 
ATOM   2100 C  C    . LYS A 1 116 ? 2.49800   -35.98200 -2.55300  1.000 16.93000  ? 116 LYS A C    1 
ATOM   2101 O  O    . LYS A 1 116 ? 1.44500   -36.43500 -2.99800  1.000 17.62000  ? 116 LYS A O    1 
ATOM   2102 C  CB   . LYS A 1 116 ? 1.85200   -34.83100 -0.46600  1.000 16.62000  ? 116 LYS A CB   1 
ATOM   2103 C  CG   . LYS A 1 116 ? 2.64200   -35.65600 0.55000   1.000 17.33000  ? 116 LYS A CG   1 
ATOM   2104 C  CD   . LYS A 1 116 ? 1.88100   -35.72200 1.87700   1.000 16.96000  ? 116 LYS A CD   1 
ATOM   2105 C  CE   . LYS A 1 116 ? 2.72000   -36.35400 3.01600   1.000 17.03000  ? 116 LYS A CE   1 
ATOM   2106 N  NZ   . LYS A 1 116 ? 1.98300   -36.40200 4.29600   1.000 17.07000  ? 116 LYS A NZ   1 
ATOM   2107 H  H    . LYS A 1 116 ? 1.09600   -33.34100 -2.11800  1.000 18.31000  ? 116 LYS A H    1 
ATOM   2108 H  HA   . LYS A 1 116 ? 3.43900   -34.37300 -1.71700  1.000 18.79000  ? 116 LYS A HA   1 
ATOM   2109 H  HB2  . LYS A 1 116 ? 1.71300   -33.95200 -0.08000  1.000 19.93000  ? 116 LYS A HB2  1 
ATOM   2110 H  HB3  . LYS A 1 116 ? 0.99900   -35.27300 -0.59800  1.000 19.93000  ? 116 LYS A HB3  1 
ATOM   2111 H  HG2  . LYS A 1 116 ? 2.76200   -36.55800 0.21500   1.000 20.79000  ? 116 LYS A HG2  1 
ATOM   2112 H  HG3  . LYS A 1 116 ? 3.50500   -35.24200 0.70700   1.000 20.79000  ? 116 LYS A HG3  1 
ATOM   2113 H  HD2  . LYS A 1 116 ? 1.63700   -34.82300 2.14800   1.000 20.34000  ? 116 LYS A HD2  1 
ATOM   2114 H  HD3  . LYS A 1 116 ? 1.08300   -36.26100 1.75800   1.000 20.34000  ? 116 LYS A HD3  1 
ATOM   2115 H  HE2  . LYS A 1 116 ? 2.95800   -37.26200 2.77000   1.000 20.42000  ? 116 LYS A HE2  1 
ATOM   2116 H  HE3  . LYS A 1 116 ? 3.52300   -35.82600 3.15000   1.000 20.42000  ? 116 LYS A HE3  1 
ATOM   2117 H  HZ1  . LYS A 1 116 ? 2.36800   -36.98500 4.84700   1.000 20.48000  ? 116 LYS A HZ1  1 
ATOM   2118 H  HZ2  . LYS A 1 116 ? 1.98400   -35.59800 4.67800   1.000 20.48000  ? 116 LYS A HZ2  1 
ATOM   2119 H  HZ3  . LYS A 1 116 ? 1.14100   -36.65200 4.15300   1.000 20.48000  ? 116 LYS A HZ3  1 
ATOM   2120 N  N    . GLY A 1 117 ? 3.68300   -36.57000 -2.70900  1.000 17.17000  ? 117 GLY A N    1 
ATOM   2121 C  CA   . GLY A 1 117 ? 3.84200   -37.84000 -3.40200  1.000 22.32000  ? 117 GLY A CA   1 
ATOM   2122 C  C    . GLY A 1 117 ? 3.87200   -37.76100 -4.91200  1.000 25.96000  ? 117 GLY A C    1 
ATOM   2123 O  O    . GLY A 1 117 ? 3.88600   -38.80300 -5.58000  1.000 26.92000  ? 117 GLY A O    1 
ATOM   2124 H  H    . GLY A 1 117 ? 4.42400   -36.24500 -2.41700  1.000 20.60000  ? 117 GLY A H    1 
ATOM   2125 H  HA2  . GLY A 1 117 ? 4.67400   -38.24700 -3.11300  1.000 26.77000  ? 117 GLY A HA2  1 
ATOM   2126 H  HA3  . GLY A 1 117 ? 3.10400   -38.42000 -3.15400  1.000 26.77000  ? 117 GLY A HA3  1 
ATOM   2127 N  N    . THR A 1 118 ? 3.86900   -36.57300 -5.47800  1.000 19.63000  ? 118 THR A N    1 
ATOM   2128 C  CA   . THR A 1 118 ? 3.95800   -36.38400 -6.91400  1.000 19.91000  ? 118 THR A CA   1 
ATOM   2129 C  C    . THR A 1 118 ? 5.31900   -35.80300 -7.25300  1.000 19.79000  ? 118 THR A C    1 
ATOM   2130 O  O    . THR A 1 118 ? 6.09000   -35.40300 -6.38400  1.000 21.47000  ? 118 THR A O    1 
ATOM   2131 C  CB   . THR A 1 118 ? 2.84200   -35.48100 -7.44000  1.000 22.40000  ? 118 THR A CB   1 
ATOM   2132 O  OG1  . THR A 1 118 ? 3.13100   -34.12300 -7.10400  1.000 19.55000  ? 118 THR A OG1  1 
ATOM   2133 C  CG2  . THR A 1 118 ? 1.47900   -35.85800 -6.82600  1.000 23.04000  ? 118 THR A CG2  1 
ATOM   2134 H  H    . THR A 1 118 ? 3.81500   -35.83500 -5.03900  1.000 23.55000  ? 118 THR A H    1 
ATOM   2135 H  HA   . THR A 1 118 ? 3.85700   -37.24200 -7.35500  1.000 23.87000  ? 118 THR A HA   1 
ATOM   2136 H  HB   . THR A 1 118 ? 2.78300   -35.58500 -8.40300  1.000 26.87000  ? 118 THR A HB   1 
ATOM   2137 H  HG1  . THR A 1 118 ? 3.22200   -34.04500 -6.27300  1.000 23.44000  ? 118 THR A HG1  1 
ATOM   2138 H  HG21 . THR A 1 118 ? 0.77100   -35.35200 -7.25400  1.000 27.63000  ? 118 THR A HG21 1 
ATOM   2139 H  HG22 . THR A 1 118 ? 1.30900   -36.80500 -6.95200  1.000 27.63000  ? 118 THR A HG22 1 
ATOM   2140 H  HG23 . THR A 1 118 ? 1.47700   -35.66100 -5.87700  1.000 27.63000  ? 118 THR A HG23 1 
ATOM   2141 N  N    . ASP A 1 119 ? 5.59000   -35.71900 -8.55000  1.000 23.91000  ? 119 ASP A N    1 
ATOM   2142 C  CA   . ASP A 1 119 ? 6.85300   -35.18500 -9.04900  1.000 23.43000  ? 119 ASP A CA   1 
ATOM   2143 C  C    . ASP A 1 119 ? 6.75200   -33.66100 -9.08000  1.000 22.40000  ? 119 ASP A C    1 
ATOM   2144 O  O    . ASP A 1 119 ? 6.49100   -33.03700 -10.11200 1.000 27.20000  ? 119 ASP A O    1 
ATOM   2145 C  CB   . ASP A 1 119 ? 7.14700   -35.75000 -10.43000 1.000 24.36000  ? 119 ASP A CB   1 
ATOM   2146 C  CG   . ASP A 1 119 ? 8.42300   -35.19500 -11.02900 1.000 40.67000  ? 119 ASP A CG   1 
ATOM   2147 O  OD1  . ASP A 1 119 ? 9.27100   -34.70700 -10.25600 1.000 42.86000  ? 119 ASP A OD1  1 
ATOM   2148 O  OD2  . ASP A 1 119 ? 8.58900   -35.27000 -12.26700 1.000 45.35000  ? 119 ASP A OD2  1 
ATOM   2149 H  H    . ASP A 1 119 ? 5.05000   -35.97000 -9.17200  1.000 28.68000  ? 119 ASP A H    1 
ATOM   2150 H  HA   . ASP A 1 119 ? 7.57200   -35.43300 -8.44800  1.000 28.10000  ? 119 ASP A HA   1 
ATOM   2151 H  HB2  . ASP A 1 119 ? 7.24000   -36.71300 -10.36500 1.000 29.22000  ? 119 ASP A HB2  1 
ATOM   2152 H  HB3  . ASP A 1 119 ? 6.41400   -35.52700 -11.02600 1.000 29.22000  ? 119 ASP A HB3  1 
ATOM   2153 N  N    . VAL A 1 120 ? 6.97900   -33.04900 -7.90900  1.000 21.34000  ? 120 VAL A N    1 
ATOM   2154 C  CA   . VAL A 1 120 ? 6.79200   -31.59600 -7.79500  1.000 18.88000  ? 120 VAL A CA   1 
ATOM   2155 C  C    . VAL A 1 120 ? 7.84100   -30.80300 -8.56200  1.000 19.68000  ? 120 VAL A C    1 
ATOM   2156 O  O    . VAL A 1 120 ? 7.58900   -29.64700 -8.90900  1.000 20.89000  ? 120 VAL A O    1 
ATOM   2157 C  CB   . VAL A 1 120 ? 6.70500   -31.12900 -6.32700  1.000 18.64000  ? 120 VAL A CB   1 
ATOM   2158 C  CG1  . VAL A 1 120 ? 5.45700   -31.69100 -5.64000  1.000 23.24000  ? 120 VAL A CG1  1 
ATOM   2159 C  CG2  . VAL A 1 120 ? 7.95600   -31.49300 -5.58200  1.000 24.10000  ? 120 VAL A CG2  1 
ATOM   2160 H  H    . VAL A 1 120 ? 7.23400   -33.44000 -7.18600  1.000 25.60000  ? 120 VAL A H    1 
ATOM   2161 H  HA   . VAL A 1 120 ? 5.93200   -31.40400 -8.20000  1.000 22.64000  ? 120 VAL A HA   1 
ATOM   2162 H  HB   . VAL A 1 120 ? 6.62400   -30.16200 -6.31400  1.000 22.36000  ? 120 VAL A HB   1 
ATOM   2163 H  HG11 . VAL A 1 120 ? 5.42500   -31.36500 -4.72700  1.000 27.87000  ? 120 VAL A HG11 1 
ATOM   2164 H  HG12 . VAL A 1 120 ? 4.66900   -31.39700 -6.12300  1.000 27.87000  ? 120 VAL A HG12 1 
ATOM   2165 H  HG13 . VAL A 1 120 ? 5.50400   -32.66000 -5.64300  1.000 27.87000  ? 120 VAL A HG13 1 
ATOM   2166 H  HG21 . VAL A 1 120 ? 7.87300   -31.19900 -4.66200  1.000 28.91000  ? 120 VAL A HG21 1 
ATOM   2167 H  HG22 . VAL A 1 120 ? 8.07300   -32.45600 -5.61200  1.000 28.91000  ? 120 VAL A HG22 1 
ATOM   2168 H  HG23 . VAL A 1 120 ? 8.71300   -31.05500 -6.00300  1.000 28.91000  ? 120 VAL A HG23 1 
ATOM   2169 N  N    . GLN A 1 121 ? 9.01900   -31.38700 -8.82800  1.000 20.57000  ? 121 GLN A N    1 
ATOM   2170 C  CA   . GLN A 1 121 ? 10.01500  -30.72500 -9.66200  1.000 21.61000  ? 121 GLN A CA   1 
ATOM   2171 C  C    . GLN A 1 121 ? 9.45000   -30.31500 -11.00900 1.000 20.21000  ? 121 GLN A C    1 
ATOM   2172 O  O    . GLN A 1 121 ? 9.95100   -29.37100 -11.62000 1.000 22.92000  ? 121 GLN A O    1 
ATOM   2173 C  CB   . GLN A 1 121 ? 11.21500  -31.66000 -9.89800  1.000 25.48000  ? 121 GLN A CB   1 
ATOM   2174 C  CG   . GLN A 1 121 ? 12.33000  -31.06400 -10.76900 1.000 54.48000  ? 121 GLN A CG   1 
ATOM   2175 C  CD   . GLN A 1 121 ? 13.23800  -30.06700 -10.04700 1.000 108.57000 ? 121 GLN A CD   1 
ATOM   2176 O  OE1  . GLN A 1 121 ? 14.02300  -29.37000 -10.69100 1.000 134.94000 ? 121 GLN A OE1  1 
ATOM   2177 N  NE2  . GLN A 1 121 ? 13.13700  -29.99300 -8.72000  1.000 113.40000 ? 121 GLN A NE2  1 
ATOM   2178 H  H    . GLN A 1 121 ? 9.25900   -32.16100 -8.53800  1.000 24.68000  ? 121 GLN A H    1 
ATOM   2179 H  HA   . GLN A 1 121 ? 10.31400  -29.93000 -9.19200  1.000 25.92000  ? 121 GLN A HA   1 
ATOM   2180 H  HB2  . GLN A 1 121 ? 11.60500  -31.88400 -9.03800  1.000 30.56000  ? 121 GLN A HB2  1 
ATOM   2181 H  HB3  . GLN A 1 121 ? 10.89800  -32.46300 -10.33800 1.000 30.56000  ? 121 GLN A HB3  1 
ATOM   2182 H  HG2  . GLN A 1 121 ? 12.88900  -31.78800 -11.09300 1.000 65.36000  ? 121 GLN A HG2  1 
ATOM   2183 H  HG3  . GLN A 1 121 ? 11.92200  -30.60000 -11.51700 1.000 65.36000  ? 121 GLN A HG3  1 
ATOM   2184 H  HE21 . GLN A 1 121 ? 12.57600  -30.49400 -8.30300  1.000 136.07000 ? 121 GLN A HE21 1 
ATOM   2185 H  HE22 . GLN A 1 121 ? 13.63200  -29.44300 -8.28100  1.000 136.07000 ? 121 GLN A HE22 1 
ATOM   2186 N  N    . ALA A 1 122 ? 8.44400   -31.03000 -11.51600 1.000 20.99000  ? 122 ALA A N    1 
ATOM   2187 C  CA   . ALA A 1 122 ? 7.83800   -30.64200 -12.78600 1.000 19.41000  ? 122 ALA A CA   1 
ATOM   2188 C  C    . ALA A 1 122 ? 7.36500   -29.19600 -12.78200 1.000 22.27000  ? 122 ALA A C    1 
ATOM   2189 O  O    . ALA A 1 122 ? 7.31400   -28.54400 -13.83000 1.000 24.32000  ? 122 ALA A O    1 
ATOM   2190 C  CB   . ALA A 1 122 ? 6.65500   -31.55100 -13.10900 1.000 29.31000  ? 122 ALA A CB   1 
ATOM   2191 H  H    . ALA A 1 122 ? 8.10200   -31.72900 -11.15100 1.000 25.18000  ? 122 ALA A H    1 
ATOM   2192 H  HA   . ALA A 1 122 ? 8.51100   -30.74400 -13.47800 1.000 23.28000  ? 122 ALA A HA   1 
ATOM   2193 H  HB1  . ALA A 1 122 ? 6.30100   -31.31200 -13.98000 1.000 35.17000  ? 122 ALA A HB1  1 
ATOM   2194 H  HB2  . ALA A 1 122 ? 6.95700   -32.47200 -13.11600 1.000 35.17000  ? 122 ALA A HB2  1 
ATOM   2195 H  HB3  . ALA A 1 122 ? 5.97200   -31.43200 -12.43000 1.000 35.17000  ? 122 ALA A HB3  1 
ATOM   2196 N  N    . TRP A 1 123 ? 6.96900   -28.69100 -11.61900 1.000 20.08000  ? 123 TRP A N    1 
ATOM   2197 C  CA   . TRP A 1 123 ? 6.40700   -27.35600 -11.55600 1.000 20.65000  ? 123 TRP A CA   1 
ATOM   2198 C  C    . TRP A 1 123 ? 7.43700   -26.26700 -11.78900 1.000 21.38000  ? 123 TRP A C    1 
ATOM   2199 O  O    . TRP A 1 123 ? 7.04800   -25.12800 -12.04200 1.000 21.51000  ? 123 TRP A O    1 
ATOM   2200 C  CB   . TRP A 1 123 ? 5.71700   -27.17100 -10.19400 1.000 19.85000  ? 123 TRP A CB   1 
ATOM   2201 C  CG   . TRP A 1 123 ? 4.44800   -27.92100 -10.16200 1.000 21.07000  ? 123 TRP A CG   1 
ATOM   2202 C  CD1  . TRP A 1 123 ? 4.22300   -29.14200 -9.59500  1.000 22.98000  ? 123 TRP A CD1  1 
ATOM   2203 C  CD2  . TRP A 1 123 ? 3.22800   -27.53900 -10.79100 1.000 19.69000  ? 123 TRP A CD2  1 
ATOM   2204 N  NE1  . TRP A 1 123 ? 2.93800   -29.53600 -9.81500  1.000 23.17000  ? 123 TRP A NE1  1 
ATOM   2205 C  CE2  . TRP A 1 123 ? 2.30100   -28.57700 -10.55800 1.000 19.95000  ? 123 TRP A CE2  1 
ATOM   2206 C  CE3  . TRP A 1 123 ? 2.82700   -26.43100 -11.53500 1.000 22.25000  ? 123 TRP A CE3  1 
ATOM   2207 C  CZ2  . TRP A 1 123 ? 0.99500   -28.52700 -11.03100 1.000 26.03000  ? 123 TRP A CZ2  1 
ATOM   2208 C  CZ3  . TRP A 1 123 ? 1.52500   -26.39500 -12.02300 1.000 26.27000  ? 123 TRP A CZ3  1 
ATOM   2209 C  CH2  . TRP A 1 123 ? 0.63500   -27.44400 -11.77900 1.000 25.29000  ? 123 TRP A CH2  1 
ATOM   2210 H  H    . TRP A 1 123 ? 7.01600   -29.09800 -10.86400 1.000 24.08000  ? 123 TRP A H    1 
ATOM   2211 H  HA   . TRP A 1 123 ? 5.73600   -27.25400 -12.24900 1.000 24.77000  ? 123 TRP A HA   1 
ATOM   2212 H  HB2  . TRP A 1 123 ? 6.29400   -27.50400 -9.48800  1.000 23.81000  ? 123 TRP A HB2  1 
ATOM   2213 H  HB3  . TRP A 1 123 ? 5.52700   -26.23000 -10.05000 1.000 23.81000  ? 123 TRP A HB3  1 
ATOM   2214 H  HD1  . TRP A 1 123 ? 4.85600   -29.63400 -9.12400  1.000 27.56000  ? 123 TRP A HD1  1 
ATOM   2215 H  HE1  . TRP A 1 123 ? 2.58400   -30.26700 -9.53500  1.000 27.79000  ? 123 TRP A HE1  1 
ATOM   2216 H  HE3  . TRP A 1 123 ? 3.41700   -25.73100 -11.70200 1.000 26.69000  ? 123 TRP A HE3  1 
ATOM   2217 H  HZ2  . TRP A 1 123 ? 0.38900   -29.20800 -10.84500 1.000 31.22000  ? 123 TRP A HZ2  1 
ATOM   2218 H  HZ3  . TRP A 1 123 ? 1.24300   -25.66100 -12.52000 1.000 31.52000  ? 123 TRP A HZ3  1 
ATOM   2219 H  HH2  . TRP A 1 123 ? -0.22400  -27.40300 -12.13400 1.000 30.34000  ? 123 TRP A HH2  1 
ATOM   2220 N  N    . ILE A 1 124 ? 8.72800   -26.57900 -11.72400 1.000 20.31000  ? 124 ILE A N    1 
ATOM   2221 C  CA   . ILE A 1 124 ? 9.74800   -25.58600 -12.01900 1.000 18.73000  ? 124 ILE A CA   1 
ATOM   2222 C  C    . ILE A 1 124 ? 10.55700  -25.95300 -13.25000 1.000 18.16000  ? 124 ILE A C    1 
ATOM   2223 O  O    . ILE A 1 124 ? 11.55200  -25.29200 -13.54400 1.000 21.82000  ? 124 ILE A O    1 
ATOM   2224 C  CB   . ILE A 1 124 ? 10.64600  -25.28200 -10.80600 1.000 21.19000  ? 124 ILE A CB   1 
ATOM   2225 C  CG1  . ILE A 1 124 ? 11.36400  -26.53700 -10.33900 1.000 23.83000  ? 124 ILE A CG1  1 
ATOM   2226 C  CG2  . ILE A 1 124 ? 9.79100   -24.75400 -9.64700  1.000 25.26000  ? 124 ILE A CG2  1 
ATOM   2227 C  CD1  . ILE A 1 124 ? 12.54700  -26.20700 -9.42800  1.000 30.17000  ? 124 ILE A CD1  1 
ATOM   2228 H  H    . ILE A 1 124 ? 9.03200   -27.35500 -11.51200 1.000 24.36000  ? 124 ILE A H    1 
ATOM   2229 H  HA   . ILE A 1 124 ? 9.29400   -24.75300 -12.22300 1.000 22.47000  ? 124 ILE A HA   1 
ATOM   2230 H  HB   . ILE A 1 124 ? 11.29900  -24.61800 -11.07800 1.000 25.41000  ? 124 ILE A HB   1 
ATOM   2231 H  HG12 . ILE A 1 124 ? 10.74300  -27.09400 -9.84300  1.000 28.59000  ? 124 ILE A HG12 1 
ATOM   2232 H  HG13 . ILE A 1 124 ? 11.69800  -27.02000 -11.11100 1.000 28.59000  ? 124 ILE A HG13 1 
ATOM   2233 H  HG21 . ILE A 1 124 ? 10.36700  -24.56400 -8.89000  1.000 30.30000  ? 124 ILE A HG21 1 
ATOM   2234 H  HG22 . ILE A 1 124 ? 9.34000   -23.94400 -9.93100  1.000 30.30000  ? 124 ILE A HG22 1 
ATOM   2235 H  HG23 . ILE A 1 124 ? 9.13700   -25.42900 -9.40400  1.000 30.30000  ? 124 ILE A HG23 1 
ATOM   2236 H  HD11 . ILE A 1 124 ? 13.04400  -27.02100 -9.24900  1.000 36.19000  ? 124 ILE A HD11 1 
ATOM   2237 H  HD12 . ILE A 1 124 ? 13.11800  -25.56200 -9.87400  1.000 36.19000  ? 124 ILE A HD12 1 
ATOM   2238 H  HD13 . ILE A 1 124 ? 12.21200  -25.83400 -8.59800  1.000 36.19000  ? 124 ILE A HD13 1 
ATOM   2239 N  N    A ARG A 1 125 ? 10.11700  -26.96700 -13.99000 0.390 21.39000  ? 125 ARG A N    1 
ATOM   2240 N  N    B ARG A 1 125 ? 10.11900  -26.95600 -14.00000 0.610 21.16000  ? 125 ARG A N    1 
ATOM   2241 C  CA   A ARG A 1 125 ? 10.75900  -27.33700 -15.24400 0.390 23.65000  ? 125 ARG A CA   1 
ATOM   2242 C  CA   B ARG A 1 125 ? 10.84100  -27.36900 -15.19900 0.610 23.38000  ? 125 ARG A CA   1 
ATOM   2243 C  C    A ARG A 1 125 ? 10.80700  -26.13400 -16.17100 0.390 21.49000  ? 125 ARG A C    1 
ATOM   2244 C  C    B ARG A 1 125 ? 10.79100  -26.26100 -16.24000 0.610 21.28000  ? 125 ARG A C    1 
ATOM   2245 O  O    A ARG A 1 125 ? 9.83000   -25.39100 -16.30600 0.390 24.12000  ? 125 ARG A O    1 
ATOM   2246 O  O    B ARG A 1 125 ? 9.72100   -25.73600 -16.55500 0.610 25.68000  ? 125 ARG A O    1 
ATOM   2247 C  CB   A ARG A 1 125 ? 9.95400   -28.46100 -15.89900 0.390 27.82000  ? 125 ARG A CB   1 
ATOM   2248 C  CB   B ARG A 1 125 ? 10.21400  -28.64200 -15.76400 0.610 26.99000  ? 125 ARG A CB   1 
ATOM   2249 C  CG   A ARG A 1 125 ? 10.76700  -29.36800 -16.81900 0.390 39.18000  ? 125 ARG A CG   1 
ATOM   2250 C  CG   B ARG A 1 125 ? 10.94100  -29.20300 -16.99100 0.610 36.99000  ? 125 ARG A CG   1 
ATOM   2251 C  CD   A ARG A 1 125 ? 9.91900   -29.98600 -17.92900 0.390 33.06000  ? 125 ARG A CD   1 
ATOM   2252 C  CD   B ARG A 1 125 ? 11.30700  -30.67000 -16.78400 0.610 46.56000  ? 125 ARG A CD   1 
ATOM   2253 N  NE   A ARG A 1 125 ? 8.50100   -30.05900 -17.59400 0.390 46.71000  ? 125 ARG A NE   1 
ATOM   2254 N  NE   B ARG A 1 125 ? 12.18000  -31.19400 -17.83000 0.610 66.20000  ? 125 ARG A NE   1 
ATOM   2255 C  CZ   A ARG A 1 125 ? 7.94200   -31.03200 -16.88700 0.390 47.46000  ? 125 ARG A CZ   1 
ATOM   2256 C  CZ   B ARG A 1 125 ? 11.77100  -31.58400 -19.03000 0.610 56.63000  ? 125 ARG A CZ   1 
ATOM   2257 N  NH1  A ARG A 1 125 ? 8.65400   -32.04500 -16.41800 0.390 51.26000  ? 125 ARG A NH1  1 
ATOM   2258 N  NH1  B ARG A 1 125 ? 10.49900  -31.51000 -19.38700 0.610 55.68000  ? 125 ARG A NH1  1 
ATOM   2259 N  NH2  A ARG A 1 125 ? 6.63400   -30.99100 -16.64800 0.390 46.12000  ? 125 ARG A NH2  1 
ATOM   2260 N  NH2  B ARG A 1 125 ? 12.66000  -32.06700 -19.89300 0.610 61.45000  ? 125 ARG A NH2  1 
ATOM   2261 H  H    A ARG A 1 125 ? 9.44300   -27.46000 -13.78500 0.390 25.65000  ? 125 ARG A H    1 
ATOM   2262 H  H    B ARG A 1 125 ? 9.40800   -27.41300 -13.83800 0.610 25.38000  ? 125 ARG A H    1 
ATOM   2263 H  HA   A ARG A 1 125 ? 11.66500  -27.64300 -15.08200 0.390 28.37000  ? 125 ARG A HA   1 
ATOM   2264 H  HA   B ARG A 1 125 ? 11.76900  -27.54700 -14.98000 0.610 28.05000  ? 125 ARG A HA   1 
ATOM   2265 H  HB2  A ARG A 1 125 ? 9.57500   -29.01700 -15.20000 0.390 33.37000  ? 125 ARG A HB2  1 
ATOM   2266 H  HB2  B ARG A 1 125 ? 10.22500  -29.32600 -15.07600 0.610 32.37000  ? 125 ARG A HB2  1 
ATOM   2267 H  HB3  A ARG A 1 125 ? 9.24500   -28.06500 -16.42900 0.390 33.37000  ? 125 ARG A HB3  1 
ATOM   2268 H  HB3  B ARG A 1 125 ? 9.30000   -28.45000 -16.02500 0.610 32.37000  ? 125 ARG A HB3  1 
ATOM   2269 H  HG2  A ARG A 1 125 ? 11.47300  -28.84800 -17.23400 0.390 47.00000  ? 125 ARG A HG2  1 
ATOM   2270 H  HG2  B ARG A 1 125 ? 10.36400  -29.13600 -17.76700 0.610 44.38000  ? 125 ARG A HG2  1 
ATOM   2271 H  HG3  A ARG A 1 125 ? 11.15000  -30.08900 -16.29600 0.390 47.00000  ? 125 ARG A HG3  1 
ATOM   2272 H  HG3  B ARG A 1 125 ? 11.75700  -28.70000 -17.14100 0.610 44.38000  ? 125 ARG A HG3  1 
ATOM   2273 H  HD2  A ARG A 1 125 ? 10.00800  -29.44700 -18.73100 0.390 39.66000  ? 125 ARG A HD2  1 
ATOM   2274 H  HD2  B ARG A 1 125 ? 11.76900  -30.76300 -15.93500 0.610 55.86000  ? 125 ARG A HD2  1 
ATOM   2275 H  HD3  A ARG A 1 125 ? 10.23200  -30.88800 -18.09900 0.390 39.66000  ? 125 ARG A HD3  1 
ATOM   2276 H  HD3  B ARG A 1 125 ? 10.49500  -31.20000 -16.77900 0.610 55.86000  ? 125 ARG A HD3  1 
ATOM   2277 H  HE   A ARG A 1 125 ? 7.99100   -29.42700 -17.87600 0.390 56.04000  ? 125 ARG A HE   1 
ATOM   2278 H  HE   B ARG A 1 125 ? 13.02000  -31.25500 -17.65500 0.610 79.42000  ? 125 ARG A HE   1 
ATOM   2279 H  HH11 A ARG A 1 125 ? 9.49900   -32.08300 -16.57000 0.390 61.50000  ? 125 ARG A HH11 1 
ATOM   2280 H  HH11 B ARG A 1 125 ? 9.91500   -31.20300 -18.83600 0.610 66.81000  ? 125 ARG A HH11 1 
ATOM   2281 H  HH12 A ARG A 1 125 ? 8.27100   -32.66500 -15.96200 0.390 61.50000  ? 125 ARG A HH12 1 
ATOM   2282 H  HH12 B ARG A 1 125 ? 10.25600  -31.76800 -20.17100 0.610 66.81000  ? 125 ARG A HH12 1 
ATOM   2283 H  HH21 A ARG A 1 125 ? 6.16200   -30.33800 -16.95000 0.390 55.33000  ? 125 ARG A HH21 1 
ATOM   2284 H  HH21 B ARG A 1 125 ? 13.48900  -32.12400 -19.67000 0.610 73.73000  ? 125 ARG A HH21 1 
ATOM   2285 H  HH22 A ARG A 1 125 ? 6.26100   -31.61600 -16.19000 0.390 55.33000  ? 125 ARG A HH22 1 
ATOM   2286 H  HH22 B ARG A 1 125 ? 12.40700  -32.32300 -20.67400 0.610 73.73000  ? 125 ARG A HH22 1 
ATOM   2287 N  N    . GLY A 1 126 ? 11.96100  -25.91400 -16.79300 1.000 24.77000  ? 126 GLY A N    1 
ATOM   2288 C  CA   . GLY A 1 126 ? 12.07100  -24.87700 -17.79300 1.000 23.03000  ? 126 GLY A CA   1 
ATOM   2289 C  C    . GLY A 1 126 ? 12.36500  -23.50100 -17.25900 1.000 26.84000  ? 126 GLY A C    1 
ATOM   2290 O  O    . GLY A 1 126 ? 12.64300  -22.59300 -18.05100 1.000 33.04000  ? 126 GLY A O    1 
ATOM   2291 H  H    . GLY A 1 126 ? 12.71400  -26.27900 -16.59300 1.000 29.72000  ? 126 GLY A H    1 
ATOM   2292 H  HA2  . GLY A 1 126 ? 12.78400  -25.11400 -18.40700 1.000 27.63000  ? 126 GLY A HA2  1 
ATOM   2293 H  HA3  . GLY A 1 126 ? 11.23500  -24.83100 -18.28300 1.000 27.63000  ? 126 GLY A HA3  1 
ATOM   2294 N  N    . CYS A 1 127 ? 12.31600  -23.30800 -15.94800 1.000 18.91000  ? 127 CYS A N    1 
ATOM   2295 C  CA   . CYS A 1 127 ? 12.43400  -21.99700 -15.35600 1.000 21.41000  ? 127 CYS A CA   1 
ATOM   2296 C  C    . CYS A 1 127 ? 13.89400  -21.65500 -15.14600 1.000 23.24000  ? 127 CYS A C    1 
ATOM   2297 O  O    . CYS A 1 127 ? 14.69200  -22.48600 -14.67900 1.000 23.49000  ? 127 CYS A O    1 
ATOM   2298 C  CB   . CYS A 1 127 ? 11.73800  -21.93900 -14.00000 1.000 21.92000  ? 127 CYS A CB   1 
ATOM   2299 S  SG   . CYS A 1 127 ? 9.94400   -22.23700 -14.02900 1.000 23.31000  ? 127 CYS A SG   1 
ATOM   2300 H  H    . CYS A 1 127 ? 12.21200  -23.93800 -15.37300 1.000 22.67000  ? 127 CYS A H    1 
ATOM   2301 H  HA   . CYS A 1 127 ? 12.02300  -21.35100 -15.95200 1.000 25.68000  ? 127 CYS A HA   1 
ATOM   2302 H  HB2  . CYS A 1 127 ? 12.13300  -22.61300 -13.42500 1.000 26.29000  ? 127 CYS A HB2  1 
ATOM   2303 H  HB3  . CYS A 1 127 ? 11.87800  -21.05700 -13.62200 1.000 26.29000  ? 127 CYS A HB3  1 
ATOM   2304 N  N    A ARG A 1 128 ? 14.23000  -20.40900 -15.46700 0.370 23.99000  ? 128 ARG A N    1 
ATOM   2305 N  N    B ARG A 1 128 ? 14.24800  -20.42300 -15.48100 0.630 23.86000  ? 128 ARG A N    1 
ATOM   2306 C  CA   A ARG A 1 128 ? 15.55200  -19.85500 -15.22400 0.370 22.56000  ? 128 ARG A CA   1 
ATOM   2307 C  CA   B ARG A 1 128 ? 15.58600  -19.92500 -15.22500 0.630 22.36000  ? 128 ARG A CA   1 
ATOM   2308 C  C    A ARG A 1 128 ? 15.59500  -19.36700 -13.78200 0.370 31.60000  ? 128 ARG A C    1 
ATOM   2309 C  C    B ARG A 1 128 ? 15.61700  -19.37900 -13.80500 0.630 31.74000  ? 128 ARG A C    1 
ATOM   2310 O  O    A ARG A 1 128 ? 15.00400  -18.33200 -13.45700 0.370 33.05000  ? 128 ARG A O    1 
ATOM   2311 O  O    B ARG A 1 128 ? 15.04500  -18.32000 -13.52600 0.630 33.08000  ? 128 ARG A O    1 
ATOM   2312 C  CB   A ARG A 1 128 ? 15.77100  -18.68800 -16.18300 0.370 29.18000  ? 128 ARG A CB   1 
ATOM   2313 C  CB   B ARG A 1 128 ? 15.96100  -18.85700 -16.24500 0.630 27.77000  ? 128 ARG A CB   1 
ATOM   2314 C  CG   A ARG A 1 128 ? 17.03200  -18.75900 -17.01300 0.370 28.79000  ? 128 ARG A CG   1 
ATOM   2315 C  CG   B ARG A 1 128 ? 17.44100  -18.76400 -16.47700 0.630 30.34000  ? 128 ARG A CG   1 
ATOM   2316 C  CD   A ARG A 1 128 ? 17.07600  -17.62100 -18.03500 0.370 23.90000  ? 128 ARG A CD   1 
ATOM   2317 C  CD   B ARG A 1 128 ? 17.79200  -17.63100 -17.41800 0.630 26.81000  ? 128 ARG A CD   1 
ATOM   2318 N  NE   A ARG A 1 128 ? 16.40800  -17.94800 -19.29400 0.370 32.28000  ? 128 ARG A NE   1 
ATOM   2319 N  NE   B ARG A 1 128 ? 19.23500  -17.46600 -17.49300 0.630 32.13000  ? 128 ARG A NE   1 
ATOM   2320 C  CZ   A ARG A 1 128 ? 15.39300  -17.27500 -19.82900 0.370 32.81000  ? 128 ARG A CZ   1 
ATOM   2321 C  CZ   B ARG A 1 128 ? 20.02900  -18.15900 -18.29900 0.630 29.32000  ? 128 ARG A CZ   1 
ATOM   2322 N  NH1  A ARG A 1 128 ? 14.85400  -16.22600 -19.22800 0.370 34.79000  ? 128 ARG A NH1  1 
ATOM   2323 N  NH1  B ARG A 1 128 ? 19.54700  -19.06600 -19.13400 0.630 35.42000  ? 128 ARG A NH1  1 
ATOM   2324 N  NH2  A ARG A 1 128 ? 14.90200  -17.66700 -21.00200 0.370 35.85000  ? 128 ARG A NH2  1 
ATOM   2325 N  NH2  B ARG A 1 128 ? 21.33900  -17.93900 -18.26100 0.630 48.45000  ? 128 ARG A NH2  1 
ATOM   2326 H  H    A ARG A 1 128 ? 13.69100  -19.85000 -15.83700 0.370 28.77000  ? 128 ARG A H    1 
ATOM   2327 H  H    B ARG A 1 128 ? 13.72500  -19.85500 -15.85900 0.630 28.63000  ? 128 ARG A H    1 
ATOM   2328 H  HA   A ARG A 1 128 ? 16.24100  -20.52400 -15.35600 0.370 27.06000  ? 128 ARG A HA   1 
ATOM   2329 H  HA   B ARG A 1 128 ? 16.23100  -20.64500 -15.29600 0.630 26.82000  ? 128 ARG A HA   1 
ATOM   2330 H  HB2  A ARG A 1 128 ? 15.02200  -18.65400 -16.79900 0.370 35.00000  ? 128 ARG A HB2  1 
ATOM   2331 H  HB2  B ARG A 1 128 ? 15.53700  -19.06700 -17.09100 0.630 33.31000  ? 128 ARG A HB2  1 
ATOM   2332 H  HB3  A ARG A 1 128 ? 15.81200  -17.87000 -15.66400 0.370 35.00000  ? 128 ARG A HB3  1 
ATOM   2333 H  HB3  B ARG A 1 128 ? 15.65300  -17.99400 -15.92500 0.630 33.31000  ? 128 ARG A HB3  1 
ATOM   2334 H  HG2  A ARG A 1 128 ? 17.80600  -18.68100 -16.43300 0.370 34.53000  ? 128 ARG A HG2  1 
ATOM   2335 H  HG2  B ARG A 1 128 ? 17.88900  -18.60600 -15.63100 0.630 36.39000  ? 128 ARG A HG2  1 
ATOM   2336 H  HG3  A ARG A 1 128 ? 17.05900  -19.60300 -17.49000 0.370 34.53000  ? 128 ARG A HG3  1 
ATOM   2337 H  HG3  B ARG A 1 128 ? 17.75600  -19.59400 -16.86900 0.630 36.39000  ? 128 ARG A HG3  1 
ATOM   2338 H  HD2  A ARG A 1 128 ? 16.63600  -16.84200 -17.65900 0.370 28.67000  ? 128 ARG A HD2  1 
ATOM   2339 H  HD2  B ARG A 1 128 ? 17.45600  -17.82900 -18.30600 0.630 32.16000  ? 128 ARG A HD2  1 
ATOM   2340 H  HD3  A ARG A 1 128 ? 18.00300  -17.41400 -18.23500 0.370 28.67000  ? 128 ARG A HD3  1 
ATOM   2341 H  HD3  B ARG A 1 128 ? 17.40200  -16.80500 -17.09200 0.630 32.16000  ? 128 ARG A HD3  1 
ATOM   2342 H  HE   A ARG A 1 128 ? 16.69500  -18.63500 -19.72400 0.370 38.72000  ? 128 ARG A HE   1 
ATOM   2343 H  HE   B ARG A 1 128 ? 19.59900  -16.87900 -16.98100 0.630 38.54000  ? 128 ARG A HE   1 
ATOM   2344 H  HH11 A ARG A 1 128 ? 15.16000  -15.96200 -18.46900 0.370 41.73000  ? 128 ARG A HH11 1 
ATOM   2345 H  HH11 B ARG A 1 128 ? 18.70100  -19.21800 -19.16200 0.630 42.49000  ? 128 ARG A HH11 1 
ATOM   2346 H  HH12 A ARG A 1 128 ? 14.19800  -15.80900 -19.59700 0.370 41.73000  ? 128 ARG A HH12 1 
ATOM   2347 H  HH12 B ARG A 1 128 ? 20.08000  -19.50400 -19.64700 0.630 42.49000  ? 128 ARG A HH12 1 
ATOM   2348 H  HH21 A ARG A 1 128 ? 15.24100  -18.34800 -21.40400 0.370 43.01000  ? 128 ARG A HH21 1 
ATOM   2349 H  HH21 B ARG A 1 128 ? 21.66200  -17.35400 -17.72000 0.630 58.12000  ? 128 ARG A HH21 1 
ATOM   2350 H  HH22 A ARG A 1 128 ? 14.24600  -17.24000 -21.35800 0.370 43.01000  ? 128 ARG A HH22 1 
ATOM   2351 H  HH22 B ARG A 1 128 ? 21.86400  -18.38200 -18.77900 0.630 58.12000  ? 128 ARG A HH22 1 
ATOM   2352 N  N    . LEU A 1 129 ? 16.28100  -20.10700 -12.91300 1.000 25.86000  ? 129 LEU A N    1 
ATOM   2353 C  CA   . LEU A 1 129 ? 16.33700  -19.75300 -11.50200 1.000 27.66000  ? 129 LEU A CA   1 
ATOM   2354 C  C    . LEU A 1 129 ? 17.72400  -19.60300 -10.93600 1.000 43.84000  ? 129 LEU A C    1 
ATOM   2355 O  O    . LEU A 1 129 ? 17.83000  -19.29700 -9.75000  1.000 35.97000  ? 129 LEU A O    1 
ATOM   2356 C  CB   . LEU A 1 129 ? 15.61300  -20.79900 -10.64700 1.000 27.96000  ? 129 LEU A CB   1 
ATOM   2357 C  CG   . LEU A 1 129 ? 14.17700  -21.11100 -11.03200 1.000 32.02000  ? 129 LEU A CG   1 
ATOM   2358 C  CD1  . LEU A 1 129 ? 13.86300  -22.54300 -10.66000 1.000 37.59000  ? 129 LEU A CD1  1 
ATOM   2359 C  CD2  . LEU A 1 129 ? 13.24300  -20.14000 -10.33400 1.000 45.56000  ? 129 LEU A CD2  1 
ATOM   2360 O  OXT  . LEU A 1 129 ? 18.72300  -19.80300 -11.61300 1.000 37.99000  ? 129 LEU A OXT  1 
ATOM   2361 H  H    . LEU A 1 129 ? 16.71500  -20.82400 -13.10500 1.000 31.03000  ? 129 LEU A H    1 
ATOM   2362 H  HA   . LEU A 1 129 ? 15.90500  -18.88600 -11.44600 1.000 33.18000  ? 129 LEU A HA   1 
ATOM   2363 H  HB2  . LEU A 1 129 ? 16.11000  -21.63000 -10.70200 1.000 33.54000  ? 129 LEU A HB2  1 
ATOM   2364 H  HB3  . LEU A 1 129 ? 15.60000  -20.48100 -9.73000  1.000 33.54000  ? 129 LEU A HB3  1 
ATOM   2365 H  HG   . LEU A 1 129 ? 14.04600  -21.01300 -11.98800 1.000 38.41000  ? 129 LEU A HG   1 
ATOM   2366 H  HD11 . LEU A 1 129 ? 12.94500  -22.74000 -10.90700 1.000 45.10000  ? 129 LEU A HD11 1 
ATOM   2367 H  HD12 . LEU A 1 129 ? 14.46700  -23.13300 -11.13600 1.000 45.10000  ? 129 LEU A HD12 1 
ATOM   2368 H  HD13 . LEU A 1 129 ? 13.97800  -22.65400 -9.70300  1.000 45.10000  ? 129 LEU A HD13 1 
ATOM   2369 H  HD21 . LEU A 1 129 ? 12.32900  -20.34600 -10.58400 1.000 54.66000  ? 129 LEU A HD21 1 
ATOM   2370 H  HD22 . LEU A 1 129 ? 13.35200  -20.23200 -9.37500  1.000 54.66000  ? 129 LEU A HD22 1 
ATOM   2371 H  HD23 . LEU A 1 129 ? 13.46500  -19.23600 -10.60700 1.000 54.66000  ? 129 LEU A HD23 1 
HETATM 2372 C  C1   . EDO B 2 .   ? 7.90500   -28.89500 10.83400  1.000 30.13000  ? 201 EDO A C1   1 
HETATM 2373 O  O1   . EDO B 2 .   ? 6.75800   -28.02900 10.87100  1.000 21.20000  ? 201 EDO A O1   1 
HETATM 2374 C  C2   . EDO B 2 .   ? 9.18800   -28.16500 11.24600  1.000 33.70000  ? 201 EDO A C2   1 
HETATM 2375 O  O2   . EDO B 2 .   ? 8.99300   -27.49500 12.49600  1.000 58.99000  ? 201 EDO A O2   1 
HETATM 2376 H  H11  . EDO B 2 .   ? 7.74000   -29.74000 11.50600  1.000 36.15000  ? 201 EDO A H11  1 
HETATM 2377 H  H12  . EDO B 2 .   ? 8.02500   -29.29000 9.82300   1.000 36.15000  ? 201 EDO A H12  1 
HETATM 2378 H  HO1  . EDO B 2 .   ? 6.36900   -27.97000 9.98800   1.000 25.43000  ? 201 EDO A HO1  1 
HETATM 2379 H  H21  . EDO B 2 .   ? 10.00700  -28.88300 11.33700  1.000 40.43000  ? 201 EDO A H21  1 
HETATM 2380 H  H22  . EDO B 2 .   ? 9.46200   -27.43900 10.47800  1.000 40.43000  ? 201 EDO A H22  1 
HETATM 2381 H  HO2  . EDO B 2 .   ? 9.79100   -27.00100 12.72500  1.000 70.78000  ? 201 EDO A HO2  1 
HETATM 2382 C  C1   . EDO C 2 .   ? -2.94900  -21.63600 6.00800   1.000 32.88000  ? 202 EDO A C1   1 
HETATM 2383 O  O1   . EDO C 2 .   ? -4.31600  -21.49100 5.60600   1.000 26.94000  ? 202 EDO A O1   1 
HETATM 2384 C  C2   . EDO C 2 .   ? -2.59300  -23.10800 5.95900   1.000 28.27000  ? 202 EDO A C2   1 
HETATM 2385 O  O2   . EDO C 2 .   ? -3.30900  -23.81900 6.97400   1.000 31.47000  ? 202 EDO A O2   1 
HETATM 2386 H  H11  . EDO C 2 .   ? -2.29800  -21.06800 5.34000   1.000 39.44000  ? 202 EDO A H11  1 
HETATM 2387 H  H12  . EDO C 2 .   ? -2.81100  -21.24800 7.01900   1.000 39.44000  ? 202 EDO A H12  1 
HETATM 2388 H  HO1  . EDO C 2 .   ? -4.50400  -22.09900 4.87800   1.000 32.32000  ? 202 EDO A HO1  1 
HETATM 2389 H  H21  . EDO C 2 .   ? -2.84500  -23.51600 4.97700   1.000 33.91000  ? 202 EDO A H21  1 
HETATM 2390 H  H22  . EDO C 2 .   ? -1.51900  -23.23300 6.10900   1.000 33.91000  ? 202 EDO A H22  1 
HETATM 2391 H  HO2  . EDO C 2 .   ? -3.03800  -24.74800 6.96900   1.000 37.75000  ? 202 EDO A HO2  1 
HETATM 2392 C  C1   . EDO D 2 .   ? -14.97600 -14.83500 0.58000   0.370 21.13000  ? 203 EDO A C1   1 
HETATM 2393 O  O1   . EDO D 2 .   ? -13.63400 -14.50100 0.92300   0.370 22.11000  ? 203 EDO A O1   1 
HETATM 2394 C  C2   . EDO D 2 .   ? -15.24000 -14.29500 -0.81100  0.370 23.40000  ? 203 EDO A C2   1 
HETATM 2395 O  O2   . EDO D 2 .   ? -14.36700 -14.94000 -1.74600  0.370 21.20000  ? 203 EDO A O2   1 
HETATM 2396 H  H11  . EDO D 2 .   ? -15.11500 -15.91800 0.60000   0.370 25.34000  ? 203 EDO A H11  1 
HETATM 2397 H  H12  . EDO D 2 .   ? -15.67200 -14.39300 1.29600   0.370 25.34000  ? 203 EDO A H12  1 
HETATM 2398 H  HO1  . EDO D 2 .   ? -13.45900 -14.76900 1.83600   0.370 26.52000  ? 203 EDO A HO1  1 
HETATM 2399 H  H21  . EDO D 2 .   ? -16.28000 -14.47700 -1.08900  0.370 28.07000  ? 203 EDO A H21  1 
HETATM 2400 H  H22  . EDO D 2 .   ? -15.07200 -13.21600 -0.82900  0.370 28.07000  ? 203 EDO A H22  1 
HETATM 2401 H  HO2  . EDO D 2 .   ? -14.47500 -14.53800 -2.61900  0.370 25.43000  ? 203 EDO A HO2  1 
HETATM 2402 C  C1   . EDO E 2 .   ? 15.88600  -16.60100 -8.93700  0.350 29.25000  ? 204 EDO A C1   1 
HETATM 2403 O  O1   . EDO E 2 .   ? 16.06200  -15.73000 -7.81400  0.350 35.12000  ? 204 EDO A O1   1 
HETATM 2404 C  C2   . EDO E 2 .   ? 16.31400  -15.90100 -10.22000 0.350 31.10000  ? 204 EDO A C2   1 
HETATM 2405 O  O2   . EDO E 2 .   ? 15.32600  -14.93800 -10.60500 0.350 35.31000  ? 204 EDO A O2   1 
HETATM 2406 H  H11  . EDO E 2 .   ? 16.48000  -17.50600 -8.79700  0.350 35.09000  ? 204 EDO A H11  1 
HETATM 2407 H  H12  . EDO E 2 .   ? 14.83700  -16.89600 -9.01300  0.350 35.09000  ? 204 EDO A H12  1 
HETATM 2408 H  HO1  . EDO E 2 .   ? 15.83900  -16.20300 -7.00100  0.350 42.13000  ? 204 EDO A HO1  1 
HETATM 2409 H  H21  . EDO E 2 .   ? 17.27400  -15.40300 -10.06500 0.350 37.31000  ? 204 EDO A H21  1 
HETATM 2410 H  H22  . EDO E 2 .   ? 16.44200  -16.63700 -11.01600 0.350 37.31000  ? 204 EDO A H22  1 
HETATM 2411 H  HO2  . EDO E 2 .   ? 15.59200  -14.51700 -11.43400 0.350 42.36000  ? 204 EDO A HO2  1 
HETATM 2412 C  C1   . EDO F 2 .   ? 6.55900   -35.22400 -3.03200  1.000 37.96000  ? 205 EDO A C1   1 
HETATM 2413 O  O1   . EDO F 2 .   ? 6.21800   -35.88600 -1.80400  1.000 33.19000  ? 205 EDO A O1   1 
HETATM 2414 C  C2   . EDO F 2 .   ? 7.33700   -33.93300 -2.78400  1.000 30.26000  ? 205 EDO A C2   1 
HETATM 2415 O  O2   . EDO F 2 .   ? 7.02800   -33.31900 -1.51700  1.000 27.54000  ? 205 EDO A O2   1 
HETATM 2416 H  H11  . EDO F 2 .   ? 7.16100   -35.89500 -3.64800  1.000 45.54000  ? 205 EDO A H11  1 
HETATM 2417 H  H12  . EDO F 2 .   ? 5.64400   -34.99300 -3.58300  1.000 45.54000  ? 205 EDO A H12  1 
HETATM 2418 H  HO1  . EDO F 2 .   ? 6.07300   -36.82700 -1.97500  1.000 39.81000  ? 205 EDO A HO1  1 
HETATM 2419 H  H21  . EDO F 2 .   ? 8.40600   -34.15100 -2.81900  1.000 36.29000  ? 205 EDO A H21  1 
HETATM 2420 H  H22  . EDO F 2 .   ? 7.11200   -33.22500 -3.58400  1.000 36.29000  ? 205 EDO A H22  1 
HETATM 2421 H  HO2  . EDO F 2 .   ? 7.57300   -32.53000 -1.40000  1.000 33.04000  ? 205 EDO A HO2  1 
HETATM 2422 C  C1   . EDO G 2 .   ? 2.83200   -6.35400  2.17300   1.000 48.82000  ? 206 EDO A C1   1 
HETATM 2423 O  O1   . EDO G 2 .   ? 1.56300   -6.81300  1.69900   1.000 54.21000  ? 206 EDO A O1   1 
HETATM 2424 C  C2   . EDO G 2 .   ? 3.94900   -6.98700  1.35500   1.000 50.13000  ? 206 EDO A C2   1 
HETATM 2425 O  O2   . EDO G 2 .   ? 3.68900   -8.38000  1.14600   1.000 30.18000  ? 206 EDO A O2   1 
HETATM 2426 H  H11  . EDO G 2 .   ? 2.88600   -5.26600  2.09100   1.000 58.58000  ? 206 EDO A H11  1 
HETATM 2427 H  H12  . EDO G 2 .   ? 2.95000   -6.61800  3.22600   1.000 58.58000  ? 206 EDO A H12  1 
HETATM 2428 H  HO1  . EDO G 2 .   ? 0.85700   -6.32900  2.14900   1.000 65.05000  ? 206 EDO A HO1  1 
HETATM 2429 H  H21  . EDO G 2 .   ? 4.03000   -6.48100  0.39100   1.000 60.14000  ? 206 EDO A H21  1 
HETATM 2430 H  H22  . EDO G 2 .   ? 4.90000   -6.86600  1.87800   1.000 60.14000  ? 206 EDO A H22  1 
HETATM 2431 H  HO2  . EDO G 2 .   ? 4.42800   -8.77700  0.66500   1.000 36.20000  ? 206 EDO A HO2  1 
HETATM 2432 C  C1   . EDO H 2 .   ? 6.53700   -19.05100 -17.11400 1.000 43.84000  ? 207 EDO A C1   1 
HETATM 2433 O  O1   . EDO H 2 .   ? 5.48800   -19.93700 -17.52600 1.000 72.91000  ? 207 EDO A O1   1 
HETATM 2434 C  C2   . EDO H 2 .   ? 5.92700   -17.85100 -16.39600 1.000 35.95000  ? 207 EDO A C2   1 
HETATM 2435 O  O2   . EDO H 2 .   ? 6.83300   -16.82300 -16.01400 1.000 26.48000  ? 207 EDO A O2   1 
HETATM 2436 H  H11  . EDO H 2 .   ? 7.22500   -19.57400 -16.44700 1.000 52.60000  ? 207 EDO A H11  1 
HETATM 2437 H  H12  . EDO H 2 .   ? 7.10400   -18.71500 -17.98500 1.000 52.60000  ? 207 EDO A H12  1 
HETATM 2438 H  HO1  . EDO H 2 .   ? 5.85600   -20.81500 -17.69700 1.000 87.48000  ? 207 EDO A HO1  1 
HETATM 2439 H  H21  . EDO H 2 .   ? 5.17100   -17.41200 -17.05000 1.000 43.13000  ? 207 EDO A H21  1 
HETATM 2440 H  H22  . EDO H 2 .   ? 5.42400   -18.21300 -15.49700 1.000 43.13000  ? 207 EDO A H22  1 
HETATM 2441 H  HO2  . EDO H 2 .   ? 6.47700   -16.34700 -15.25200 1.000 31.76000  ? 207 EDO A HO2  1 
HETATM 2442 CL CL   . CL  I 3 .   ? 8.55200   -31.50000 7.66900   1.000 20.79000  ? 208 CL  A CL   1 
HETATM 2443 CL CL   . CL  J 3 .   ? 11.25800  -31.78200 -1.64300  1.000 25.09000  ? 209 CL  A CL   1 
HETATM 2444 CL CL   . CL  K 3 .   ? 7.73300   -10.19900 -4.22600  1.000 46.91000  ? 210 CL  A CL   1 
HETATM 2445 CL CL   . CL  L 3 .   ? 0.89500   -23.14400 -14.89200 1.000 46.32000  ? 211 CL  A CL   1 
HETATM 2446 NA NA   . NA  M 4 .   ? -7.61200  -14.13100 12.91200  1.000 20.04000  ? 212 NA  A NA   1 
HETATM 2447 NA NA   . NA  N 4 .   ? 11.35600  -28.91700 -6.73400  1.000 26.42000  ? 213 NA  A NA   1 
HETATM 2448 O  O    . HOH O 5 .   ? 2.64500   -11.40200 -13.94500 1.000 45.24000  ? 301 HOH A O    1 
HETATM 2449 O  O    . HOH O 5 .   ? -0.44100  -12.29200 17.38200  1.000 44.92000  ? 302 HOH A O    1 
HETATM 2450 O  O    . HOH O 5 .   ? 14.58500  -31.10300 0.03200   1.000 28.05000  ? 303 HOH A O    1 
HETATM 2451 O  O    . HOH O 5 .   ? -1.83000  -33.50500 -8.46800  1.000 29.89000  ? 304 HOH A O    1 
HETATM 2452 O  O    . HOH O 5 .   ? -1.02500  -23.56800 15.14800  1.000 51.83000  ? 305 HOH A O    1 
HETATM 2453 O  O    . HOH O 5 .   ? -0.59600  -13.24000 -2.03500  1.000 25.26000  ? 306 HOH A O    1 
HETATM 2454 O  O    . HOH O 5 .   ? -11.97600 -24.71700 12.34000  1.000 37.08000  ? 307 HOH A O    1 
HETATM 2455 O  O    . HOH O 5 .   ? -7.78200  -23.97200 -1.24000  1.000 25.73000  ? 308 HOH A O    1 
HETATM 2456 O  O    . HOH O 5 .   ? -2.98600  -7.72800  -5.78900  1.000 36.41000  ? 309 HOH A O    1 
HETATM 2457 O  O    . HOH O 5 .   ? -10.94300 -12.74700 -4.07900  1.000 19.67000  ? 310 HOH A O    1 
HETATM 2458 O  O    . HOH O 5 .   ? -8.32700  -22.62900 -3.14100  1.000 33.43000  ? 311 HOH A O    1 
HETATM 2459 O  O    . HOH O 5 .   ? -13.47400 -14.57600 7.72100   1.000 20.56000  ? 312 HOH A O    1 
HETATM 2460 O  O    . HOH O 5 .   ? -3.69600  -23.50600 9.57400   1.000 32.68000  ? 313 HOH A O    1 
HETATM 2461 O  O    . HOH O 5 .   ? -13.33400 -21.55700 -4.84100  1.000 50.56000  ? 314 HOH A O    1 
HETATM 2462 O  O    . HOH O 5 .   ? 16.31400  -29.50600 -3.91200  1.000 53.36000  ? 315 HOH A O    1 
HETATM 2463 O  O    A HOH O 5 .   ? -12.27300 -13.21400 18.55200  0.580 29.01000  ? 316 HOH A O    1 
HETATM 2464 O  O    B HOH O 5 .   ? -12.36300 -11.68600 17.95200  0.420 34.59000  ? 316 HOH A O    1 
HETATM 2465 O  O    . HOH O 5 .   ? 14.47700  -17.26600 5.83700   1.000 47.24000  ? 317 HOH A O    1 
HETATM 2466 O  O    . HOH O 5 .   ? -7.21600  -23.91400 1.00800   1.000 36.46000  ? 318 HOH A O    1 
HETATM 2467 O  O    . HOH O 5 .   ? 6.395     -34.942   0.709     1.000 25.05000  ? 319 HOH A O    1 
HETATM 2468 O  O    . HOH O 5 .   ? -1.21600  -35.99600 -3.17100  1.000 24.22000  ? 320 HOH A O    1 
HETATM 2469 O  O    . HOH O 5 .   ? -0.22100  -17.84100 -14.66800 1.000 33.96000  ? 321 HOH A O    1 
HETATM 2470 O  O    . HOH O 5 .   ? 10.79500  -31.60900 5.32900   1.000 23.32000  ? 322 HOH A O    1 
HETATM 2471 O  O    . HOH O 5 .   ? -8.55100  -22.20800 0.03200   1.000 31.01000  ? 323 HOH A O    1 
HETATM 2472 O  O    . HOH O 5 .   ? 6.86700   -9.58300  6.17700   1.000 43.56000  ? 324 HOH A O    1 
HETATM 2473 O  O    . HOH O 5 .   ? -4.95300  -10.32300 -9.48800  1.000 18.40000  ? 325 HOH A O    1 
HETATM 2474 O  O    . HOH O 5 .   ? 10.70100  -7.94900  0.35300   1.000 46.35000  ? 326 HOH A O    1 
HETATM 2475 O  O    . HOH O 5 .   ? 13.785    -25.708   14.309    1.000 30.35000  ? 327 HOH A O    1 
HETATM 2476 O  O    . HOH O 5 .   ? -2.33200  -6.69000  -8.19100  1.000 37.93000  ? 328 HOH A O    1 
HETATM 2477 O  O    . HOH O 5 .   ? -10.39300 -23.47400 9.47300   1.000 48.35000  ? 329 HOH A O    1 
HETATM 2478 O  O    . HOH O 5 .   ? 2.98700   -32.31100 -9.21100  1.000 34.08000  ? 330 HOH A O    1 
HETATM 2479 O  O    . HOH O 5 .   ? -7.15500  -25.69200 -3.18400  1.000 29.54000  ? 331 HOH A O    1 
HETATM 2480 O  O    . HOH O 5 .   ? 4.82400   -12.71900 9.52100   1.000 45.58000  ? 332 HOH A O    1 
HETATM 2481 O  O    A HOH O 5 .   ? 15.34100  -19.93000 -1.76400  0.430 17.72000  ? 333 HOH A O    1 
HETATM 2482 O  O    B HOH O 5 .   ? 14.49500  -26.03200 -4.28700  0.570 18.38000  ? 333 HOH A O    1 
HETATM 2483 O  O    . HOH O 5 .   ? -5.51600  -25.73000 2.09600   1.000 21.12000  ? 334 HOH A O    1 
HETATM 2484 O  O    B HOH O 5 .   ? 2.67100   -26.84900 9.88400   0.410 21.25000  ? 335 HOH A O    1 
HETATM 2485 O  O    . HOH O 5 .   ? 21.06800  -19.89600 -21.38000 1.000 47.29000  ? 336 HOH A O    1 
HETATM 2486 O  O    . HOH O 5 .   ? 4.63700   -22.48100 -18.46800 1.000 51.38000  ? 337 HOH A O    1 
HETATM 2487 O  O    . HOH O 5 .   ? -1.10900  -16.09500 0.87400   1.000 17.41000  ? 338 HOH A O    1 
HETATM 2488 O  O    . HOH O 5 .   ? 5.66700   -11.37600 13.48200  1.000 53.57000  ? 339 HOH A O    1 
HETATM 2489 O  O    . HOH O 5 .   ? -7.807    -23.543   -7.248    1.000 41.55000  ? 340 HOH A O    1 
HETATM 2490 O  O    . HOH O 5 .   ? -7.73000  -17.14500 -8.22000  1.000 25.43000  ? 341 HOH A O    1 
HETATM 2491 O  O    . HOH O 5 .   ? -2.40000  -18.97800 -13.49300 1.000 33.40000  ? 342 HOH A O    1 
HETATM 2492 O  O    . HOH O 5 .   ? -16.50300 -7.01000  11.39800  1.000 41.18000  ? 343 HOH A O    1 
HETATM 2493 O  O    . HOH O 5 .   ? -0.34000  -38.11000 3.59600   1.000 33.98000  ? 344 HOH A O    1 
HETATM 2494 O  O    . HOH O 5 .   ? -18.802   -15.832   0.986     1.000 26.62000  ? 345 HOH A O    1 
HETATM 2495 O  O    . HOH O 5 .   ? 1.67000   -11.16300 0.36000   1.000 21.35000  ? 346 HOH A O    1 
HETATM 2496 O  O    . HOH O 5 .   ? -7.44500  -12.08000 14.29900  1.000 25.18000  ? 347 HOH A O    1 
HETATM 2497 O  O    . HOH O 5 .   ? -8.96900  -20.33300 16.86300  1.000 48.91000  ? 348 HOH A O    1 
HETATM 2498 O  O    . HOH O 5 .   ? 15.48600  -24.55200 6.46800   1.000 35.39000  ? 349 HOH A O    1 
HETATM 2499 O  O    . HOH O 5 .   ? -4.62300  -8.84700  16.10500  1.000 41.63000  ? 350 HOH A O    1 
HETATM 2500 O  O    A HOH O 5 .   ? 12.26600  -18.29400 -16.37000 0.760 33.02000  ? 351 HOH A O    1 
HETATM 2501 O  O    B HOH O 5 .   ? 12.21300  -18.27500 -13.62300 0.240 18.05000  ? 351 HOH A O    1 
HETATM 2502 O  O    . HOH O 5 .   ? -1.86600  -9.62600  -13.24400 1.000 32.30000  ? 352 HOH A O    1 
HETATM 2503 O  O    B HOH O 5 .   ? -17.17400 -14.78700 7.57600   0.590 32.53000  ? 353 HOH A O    1 
HETATM 2504 O  O    . HOH O 5 .   ? -9.45600  -12.48200 12.10400  1.000 23.27000  ? 354 HOH A O    1 
HETATM 2505 O  O    . HOH O 5 .   ? -1.25600  -27.59900 10.70800  1.000 45.92000  ? 355 HOH A O    1 
HETATM 2506 O  O    . HOH O 5 .   ? 12.08400  -35.26500 -11.36100 1.000 63.17000  ? 356 HOH A O    1 
HETATM 2507 O  O    . HOH O 5 .   ? 9.587     -25.879   15.306    1.000 64.00000  ? 357 HOH A O    1 
HETATM 2508 O  O    . HOH O 5 .   ? -2.94400  -13.90400 18.24800  1.000 28.32000  ? 358 HOH A O    1 
HETATM 2509 O  O    . HOH O 5 .   ? 0.130     -31.961   15.100    1.000 65.75000  ? 359 HOH A O    1 
HETATM 2510 O  O    . HOH O 5 .   ? 13.66100  -18.14300 8.84200   1.000 45.53000  ? 360 HOH A O    1 
HETATM 2511 O  O    . HOH O 5 .   ? -18.505   -9.577    6.089     1.000 19.59000  ? 361 HOH A O    1 
HETATM 2512 O  O    . HOH O 5 .   ? 3.83400   -37.30300 -10.58500 1.000 38.01000  ? 362 HOH A O    1 
HETATM 2513 O  O    . HOH O 5 .   ? 5.82900   -21.63200 14.22500  1.000 50.53000  ? 363 HOH A O    1 
HETATM 2514 O  O    . HOH O 5 .   ? 2.84600   -22.87400 -16.89800 1.000 53.65000  ? 364 HOH A O    1 
HETATM 2515 O  O    . HOH O 5 .   ? -11.42400 -11.45300 14.06200  1.000 20.60000  ? 365 HOH A O    1 
HETATM 2516 O  O    A HOH O 5 .   ? -2.10800  -7.05100  12.67800  0.660 31.50000  ? 366 HOH A O    1 
HETATM 2517 O  O    B HOH O 5 .   ? -3.21300  -6.69000  12.30500  0.340 31.90000  ? 366 HOH A O    1 
HETATM 2518 O  O    . HOH O 5 .   ? -9.602    -5.056    12.341    1.000 30.91000  ? 367 HOH A O    1 
HETATM 2519 O  O    . HOH O 5 .   ? 12.16500  -12.38700 2.61300   1.000 51.24000  ? 368 HOH A O    1 
HETATM 2520 O  O    . HOH O 5 .   ? 1.99500   -19.78900 -16.13700 1.000 49.08000  ? 369 HOH A O    1 
HETATM 2521 O  O    . HOH O 5 .   ? 0.66200   -34.03700 9.90300   1.000 50.98000  ? 370 HOH A O    1 
HETATM 2522 O  O    . HOH O 5 .   ? 15.397    -27.365   9.997     1.000 59.61000  ? 371 HOH A O    1 
HETATM 2523 O  O    . HOH O 5 .   ? -1.82300  -9.60600  17.59700  1.000 56.57000  ? 372 HOH A O    1 
HETATM 2524 O  O    . HOH O 5 .   ? 0.02200   -4.08600  -4.30500  1.000 45.39000  ? 373 HOH A O    1 
HETATM 2525 O  O    . HOH O 5 .   ? 0.35300   -14.58300 20.46700  1.000 58.32000  ? 374 HOH A O    1 
HETATM 2526 O  O    . HOH O 5 .   ? -6.004    -20.594   21.076    1.000 35.50000  ? 375 HOH A O    1 
HETATM 2527 O  O    . HOH O 5 .   ? -4.36600  -7.87500  -10.82100 1.000 48.85000  ? 376 HOH A O    1 
HETATM 2528 O  O    . HOH O 5 .   ? -4.70200  -4.70200  0.00000   0.50  47.83000  ? 377 HOH A O    1 
HETATM 2529 O  O    . HOH O 5 .   ? 9.10800   -23.41600 -19.63300 1.000 52.49000  ? 378 HOH A O    1 
HETATM 2530 O  O    . HOH O 5 .   ? -5.973    -24.801   -10.178   1.000 42.35000  ? 379 HOH A O    1 
HETATM 2531 O  O    . HOH O 5 .   ? -8.87000  -25.40900 13.22900  1.000 43.00000  ? 380 HOH A O    1 
HETATM 2532 O  O    . HOH O 5 .   ? -18.207   -18.649   13.492    1.000 51.40000  ? 381 HOH A O    1 
HETATM 2533 O  O    . HOH O 5 .   ? 14.96100  -25.98800 -13.55200 1.000 55.53000  ? 382 HOH A O    1 
HETATM 2534 O  O    . HOH O 5 .   ? -7.79600  -25.83200 0.37400   1.000 42.05000  ? 383 HOH A O    1 
HETATM 2535 O  O    . HOH O 5 .   ? 15.160    -29.222   7.141     1.000 38.07000  ? 384 HOH A O    1 
HETATM 2536 O  O    . HOH O 5 .   ? 4.73000   -7.37500  10.79700  1.000 58.44000  ? 385 HOH A O    1 
HETATM 2537 O  O    . HOH O 5 .   ? -0.514    -29.203   15.977    1.000 63.11000  ? 386 HOH A O    1 
HETATM 2538 O  O    . HOH O 5 .   ? -5.71300  -24.14800 -14.72000 1.000 67.92000  ? 387 HOH A O    1 
HETATM 2539 O  O    . HOH O 5 .   ? -13.80500 -11.12800 15.77700  1.000 45.62000  ? 388 HOH A O    1 
HETATM 2540 O  O    . HOH O 5 .   ? -10.54600 -5.83000  14.44700  1.000 59.54000  ? 389 HOH A O    1 
HETATM 2541 O  O    . HOH O 5 .   ? 11.55700  -32.30600 -13.81100 1.000 65.61000  ? 390 HOH A O    1 
HETATM 2542 O  O    . HOH O 5 .   ? -9.10400  -19.00800 -10.83400 1.000 47.88000  ? 391 HOH A O    1 
HETATM 2543 O  O    . HOH O 5 .   ? -13.467   -6.515    15.735    1.000 52.27000  ? 392 HOH A O    1 
HETATM 2544 O  O    . HOH O 5 .   ? 3.38900   -29.01500 -15.21400 1.000 52.38000  ? 393 HOH A O    1 
HETATM 2545 O  O    . HOH O 5 .   ? 9.72500   -16.64400 10.18100  1.000 61.96000  ? 394 HOH A O    1 
HETATM 2546 O  O    . HOH O 5 .   ? 7.88700   -39.19400 -6.94600  1.000 57.81000  ? 395 HOH A O    1 
HETATM 2547 O  O    . HOH O 5 .   ? -0.06700  -38.85800 0.38200   1.000 56.40000  ? 396 HOH A O    1 
# 
