data_8Z52
# 
_entry.id   8Z52 
# 
_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   8Z52         pdb_00008z52 10.2210/pdb8z52/pdb 
WWPDB D_1300045294 ?            ?                   
# 
_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       2025-04-23 
_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                        8Z52 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
4 ncmaiti@iicb.res.in      Nakul  Maiti Chandra 'principal investigator/group leader' 0000-0002-8498-6502 
5 saumen_datta@iicb.res.in Saumen Datta ?       'principal investigator/group leader' 0000-0002-3638-9383 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Roy, A.'         1 ? 
'Khanppnavar, B.' 2 ? 
'Dolui, S.'       3 ? 
'Datta, S.'       4 ? 
'Maiti, N.C.'     5 ? 
# 
_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                     'Hen Egg-White Lysozyme (HEWL) complexed with Theophylline' 
_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 'Roy, A.'         1 ? 
primary 'Khanppnavar, B.' 2 ? 
primary 'Dolui, S.'       3 ? 
primary 'Datta, S.'       4 ? 
primary 'Maiti, N.C.'     5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'Lysozyme C' 14331.160 1   3.2.1.17 ? ? ? 
2 non-polymer syn THEOPHYLLINE 180.164   1   ?        ? ? ? 
3 water       nat water        18.015    215 ?        ? ? ? 
# 
_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 THEOPHYLLINE TEP 
3 water        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LYS n 
1 2   VAL n 
1 3   PHE n 
1 4   GLY n 
1 5   ARG n 
1 6   CYS n 
1 7   GLU n 
1 8   LEU n 
1 9   ALA n 
1 10  ALA n 
1 11  ALA n 
1 12  MET n 
1 13  LYS n 
1 14  ARG n 
1 15  HIS n 
1 16  GLY n 
1 17  LEU n 
1 18  ASP n 
1 19  ASN n 
1 20  TYR n 
1 21  ARG n 
1 22  GLY n 
1 23  TYR n 
1 24  SER n 
1 25  LEU n 
1 26  GLY n 
1 27  ASN n 
1 28  TRP n 
1 29  VAL n 
1 30  CYS n 
1 31  ALA n 
1 32  ALA n 
1 33  LYS n 
1 34  PHE n 
1 35  GLU n 
1 36  SER n 
1 37  ASN n 
1 38  PHE n 
1 39  ASN n 
1 40  THR n 
1 41  GLN n 
1 42  ALA n 
1 43  THR n 
1 44  ASN n 
1 45  ARG n 
1 46  ASN n 
1 47  THR n 
1 48  ASP n 
1 49  GLY n 
1 50  SER n 
1 51  THR n 
1 52  ASP n 
1 53  TYR n 
1 54  GLY n 
1 55  ILE n 
1 56  LEU n 
1 57  GLN n 
1 58  ILE n 
1 59  ASN n 
1 60  SER n 
1 61  ARG n 
1 62  TRP n 
1 63  TRP n 
1 64  CYS n 
1 65  ASN n 
1 66  ASP n 
1 67  GLY n 
1 68  ARG n 
1 69  THR n 
1 70  PRO n 
1 71  GLY n 
1 72  SER n 
1 73  ARG n 
1 74  ASN n 
1 75  LEU n 
1 76  CYS n 
1 77  ASN n 
1 78  ILE n 
1 79  PRO n 
1 80  CYS n 
1 81  SER n 
1 82  ALA n 
1 83  LEU n 
1 84  LEU n 
1 85  SER n 
1 86  SER n 
1 87  ASP n 
1 88  ILE n 
1 89  THR n 
1 90  ALA n 
1 91  SER n 
1 92  VAL n 
1 93  ASN n 
1 94  CYS n 
1 95  ALA n 
1 96  LYS n 
1 97  LYS n 
1 98  ILE n 
1 99  VAL n 
1 100 SER n 
1 101 ASP n 
1 102 GLY n 
1 103 ASN n 
1 104 GLY n 
1 105 MET n 
1 106 ASN n 
1 107 ALA n 
1 108 TRP n 
1 109 VAL n 
1 110 ALA n 
1 111 TRP n 
1 112 ARG n 
1 113 ASN n 
1 114 ARG n 
1 115 CYS n 
1 116 LYS n 
1 117 GLY n 
1 118 THR n 
1 119 ASP n 
1 120 VAL n 
1 121 GLN n 
1 122 ALA n 
1 123 TRP n 
1 124 ILE n 
1 125 ARG n 
1 126 GLY n 
1 127 CYS n 
1 128 ARG n 
1 129 LEU n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           129 
_entity_src_nat.common_name                chicken 
_entity_src_nat.pdbx_organism_scientific   'Gallus gallus' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9031 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
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 
TEP non-polymer         . THEOPHYLLINE    ? 'C7 H8 N4 O2'    180.164 
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        TEP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TEP 
_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 TEP 1   201 1   TEP TEP A . 
C 3 HOH 1   301 7   HOH HOH A . 
C 3 HOH 2   302 93  HOH HOH A . 
C 3 HOH 3   303 109 HOH HOH A . 
C 3 HOH 4   304 161 HOH HOH A . 
C 3 HOH 5   305 171 HOH HOH A . 
C 3 HOH 6   306 70  HOH HOH A . 
C 3 HOH 7   307 46  HOH HOH A . 
C 3 HOH 8   308 80  HOH HOH A . 
C 3 HOH 9   309 156 HOH HOH A . 
C 3 HOH 10  310 62  HOH HOH A . 
C 3 HOH 11  311 90  HOH HOH A . 
C 3 HOH 12  312 189 HOH HOH A . 
C 3 HOH 13  313 73  HOH HOH A . 
C 3 HOH 14  314 50  HOH HOH A . 
C 3 HOH 15  315 165 HOH HOH A . 
C 3 HOH 16  316 112 HOH HOH A . 
C 3 HOH 17  317 36  HOH HOH A . 
C 3 HOH 18  318 101 HOH HOH A . 
C 3 HOH 19  319 152 HOH HOH A . 
C 3 HOH 20  320 38  HOH HOH A . 
C 3 HOH 21  321 96  HOH HOH A . 
C 3 HOH 22  322 162 HOH HOH A . 
C 3 HOH 23  323 201 HOH HOH A . 
C 3 HOH 24  324 4   HOH HOH A . 
C 3 HOH 25  325 82  HOH HOH A . 
C 3 HOH 26  326 60  HOH HOH A . 
C 3 HOH 27  327 5   HOH HOH A . 
C 3 HOH 28  328 48  HOH HOH A . 
C 3 HOH 29  329 22  HOH HOH A . 
C 3 HOH 30  330 28  HOH HOH A . 
C 3 HOH 31  331 17  HOH HOH A . 
C 3 HOH 32  332 64  HOH HOH A . 
C 3 HOH 33  333 74  HOH HOH A . 
C 3 HOH 34  334 94  HOH HOH A . 
C 3 HOH 35  335 39  HOH HOH A . 
C 3 HOH 36  336 71  HOH HOH A . 
C 3 HOH 37  337 40  HOH HOH A . 
C 3 HOH 38  338 159 HOH HOH A . 
C 3 HOH 39  339 193 HOH HOH A . 
C 3 HOH 40  340 33  HOH HOH A . 
C 3 HOH 41  341 130 HOH HOH A . 
C 3 HOH 42  342 67  HOH HOH A . 
C 3 HOH 43  343 102 HOH HOH A . 
C 3 HOH 44  344 116 HOH HOH A . 
C 3 HOH 45  345 23  HOH HOH A . 
C 3 HOH 46  346 87  HOH HOH A . 
C 3 HOH 47  347 160 HOH HOH A . 
C 3 HOH 48  348 15  HOH HOH A . 
C 3 HOH 49  349 175 HOH HOH A . 
C 3 HOH 50  350 59  HOH HOH A . 
C 3 HOH 51  351 218 HOH HOH A . 
C 3 HOH 52  352 29  HOH HOH A . 
C 3 HOH 53  353 43  HOH HOH A . 
C 3 HOH 54  354 77  HOH HOH A . 
C 3 HOH 55  355 12  HOH HOH A . 
C 3 HOH 56  356 108 HOH HOH A . 
C 3 HOH 57  357 61  HOH HOH A . 
C 3 HOH 58  358 104 HOH HOH A . 
C 3 HOH 59  359 19  HOH HOH A . 
C 3 HOH 60  360 174 HOH HOH A . 
C 3 HOH 61  361 56  HOH HOH A . 
C 3 HOH 62  362 41  HOH HOH A . 
C 3 HOH 63  363 103 HOH HOH A . 
C 3 HOH 64  364 31  HOH HOH A . 
C 3 HOH 65  365 20  HOH HOH A . 
C 3 HOH 66  366 47  HOH HOH A . 
C 3 HOH 67  367 139 HOH HOH A . 
C 3 HOH 68  368 97  HOH HOH A . 
C 3 HOH 69  369 66  HOH HOH A . 
C 3 HOH 70  370 10  HOH HOH A . 
C 3 HOH 71  371 134 HOH HOH A . 
C 3 HOH 72  372 81  HOH HOH A . 
C 3 HOH 73  373 140 HOH HOH A . 
C 3 HOH 74  374 198 HOH HOH A . 
C 3 HOH 75  375 91  HOH HOH A . 
C 3 HOH 76  376 68  HOH HOH A . 
C 3 HOH 77  377 25  HOH HOH A . 
C 3 HOH 78  378 24  HOH HOH A . 
C 3 HOH 79  379 128 HOH HOH A . 
C 3 HOH 80  380 16  HOH HOH A . 
C 3 HOH 81  381 125 HOH HOH A . 
C 3 HOH 82  382 54  HOH HOH A . 
C 3 HOH 83  383 127 HOH HOH A . 
C 3 HOH 84  384 79  HOH HOH A . 
C 3 HOH 85  385 53  HOH HOH A . 
C 3 HOH 86  386 142 HOH HOH A . 
C 3 HOH 87  387 11  HOH HOH A . 
C 3 HOH 88  388 32  HOH HOH A . 
C 3 HOH 89  389 75  HOH HOH A . 
C 3 HOH 90  390 164 HOH HOH A . 
C 3 HOH 91  391 154 HOH HOH A . 
C 3 HOH 92  392 52  HOH HOH A . 
C 3 HOH 93  393 30  HOH HOH A . 
C 3 HOH 94  394 88  HOH HOH A . 
C 3 HOH 95  395 95  HOH HOH A . 
C 3 HOH 96  396 188 HOH HOH A . 
C 3 HOH 97  397 197 HOH HOH A . 
C 3 HOH 98  398 194 HOH HOH A . 
C 3 HOH 99  399 13  HOH HOH A . 
C 3 HOH 100 400 21  HOH HOH A . 
C 3 HOH 101 401 207 HOH HOH A . 
C 3 HOH 102 402 57  HOH HOH A . 
C 3 HOH 103 403 183 HOH HOH A . 
C 3 HOH 104 404 118 HOH HOH A . 
C 3 HOH 105 405 26  HOH HOH A . 
C 3 HOH 106 406 86  HOH HOH A . 
C 3 HOH 107 407 45  HOH HOH A . 
C 3 HOH 108 408 214 HOH HOH A . 
C 3 HOH 109 409 106 HOH HOH A . 
C 3 HOH 110 410 27  HOH HOH A . 
C 3 HOH 111 411 172 HOH HOH A . 
C 3 HOH 112 412 35  HOH HOH A . 
C 3 HOH 113 413 92  HOH HOH A . 
C 3 HOH 114 414 55  HOH HOH A . 
C 3 HOH 115 415 219 HOH HOH A . 
C 3 HOH 116 416 42  HOH HOH A . 
C 3 HOH 117 417 131 HOH HOH A . 
C 3 HOH 118 418 190 HOH HOH A . 
C 3 HOH 119 419 34  HOH HOH A . 
C 3 HOH 120 420 3   HOH HOH A . 
C 3 HOH 121 421 200 HOH HOH A . 
C 3 HOH 122 422 58  HOH HOH A . 
C 3 HOH 123 423 8   HOH HOH A . 
C 3 HOH 124 424 136 HOH HOH A . 
C 3 HOH 125 425 14  HOH HOH A . 
C 3 HOH 126 426 107 HOH HOH A . 
C 3 HOH 127 427 138 HOH HOH A . 
C 3 HOH 128 428 65  HOH HOH A . 
C 3 HOH 129 429 220 HOH HOH A . 
C 3 HOH 130 430 9   HOH HOH A . 
C 3 HOH 131 431 196 HOH HOH A . 
C 3 HOH 132 432 205 HOH HOH A . 
C 3 HOH 133 433 2   HOH HOH A . 
C 3 HOH 134 434 187 HOH HOH A . 
C 3 HOH 135 435 170 HOH HOH A . 
C 3 HOH 136 436 6   HOH HOH A . 
C 3 HOH 137 437 78  HOH HOH A . 
C 3 HOH 138 438 206 HOH HOH A . 
C 3 HOH 139 439 117 HOH HOH A . 
C 3 HOH 140 440 37  HOH HOH A . 
C 3 HOH 141 441 44  HOH HOH A . 
C 3 HOH 142 442 181 HOH HOH A . 
C 3 HOH 143 443 186 HOH HOH A . 
C 3 HOH 144 444 121 HOH HOH A . 
C 3 HOH 145 445 115 HOH HOH A . 
C 3 HOH 146 446 63  HOH HOH A . 
C 3 HOH 147 447 99  HOH HOH A . 
C 3 HOH 148 448 151 HOH HOH A . 
C 3 HOH 149 449 178 HOH HOH A . 
C 3 HOH 150 450 166 HOH HOH A . 
C 3 HOH 151 451 122 HOH HOH A . 
C 3 HOH 152 452 137 HOH HOH A . 
C 3 HOH 153 453 213 HOH HOH A . 
C 3 HOH 154 454 144 HOH HOH A . 
C 3 HOH 155 455 133 HOH HOH A . 
C 3 HOH 156 456 209 HOH HOH A . 
C 3 HOH 157 457 113 HOH HOH A . 
C 3 HOH 158 458 89  HOH HOH A . 
C 3 HOH 159 459 216 HOH HOH A . 
C 3 HOH 160 460 132 HOH HOH A . 
C 3 HOH 161 461 150 HOH HOH A . 
C 3 HOH 162 462 83  HOH HOH A . 
C 3 HOH 163 463 169 HOH HOH A . 
C 3 HOH 164 464 185 HOH HOH A . 
C 3 HOH 165 465 211 HOH HOH A . 
C 3 HOH 166 466 167 HOH HOH A . 
C 3 HOH 167 467 123 HOH HOH A . 
C 3 HOH 168 468 135 HOH HOH A . 
C 3 HOH 169 469 195 HOH HOH A . 
C 3 HOH 170 470 143 HOH HOH A . 
C 3 HOH 171 471 76  HOH HOH A . 
C 3 HOH 172 472 49  HOH HOH A . 
C 3 HOH 173 473 147 HOH HOH A . 
C 3 HOH 174 474 204 HOH HOH A . 
C 3 HOH 175 475 180 HOH HOH A . 
C 3 HOH 176 476 119 HOH HOH A . 
C 3 HOH 177 477 100 HOH HOH A . 
C 3 HOH 178 478 179 HOH HOH A . 
C 3 HOH 179 479 141 HOH HOH A . 
C 3 HOH 180 480 215 HOH HOH A . 
C 3 HOH 181 481 177 HOH HOH A . 
C 3 HOH 182 482 208 HOH HOH A . 
C 3 HOH 183 483 114 HOH HOH A . 
C 3 HOH 184 484 126 HOH HOH A . 
C 3 HOH 185 485 176 HOH HOH A . 
C 3 HOH 186 486 145 HOH HOH A . 
C 3 HOH 187 487 149 HOH HOH A . 
C 3 HOH 188 488 69  HOH HOH A . 
C 3 HOH 189 489 210 HOH HOH A . 
C 3 HOH 190 490 199 HOH HOH A . 
C 3 HOH 191 491 163 HOH HOH A . 
C 3 HOH 192 492 191 HOH HOH A . 
C 3 HOH 193 493 182 HOH HOH A . 
C 3 HOH 194 494 202 HOH HOH A . 
C 3 HOH 195 495 203 HOH HOH A . 
C 3 HOH 196 496 120 HOH HOH A . 
C 3 HOH 197 497 155 HOH HOH A . 
C 3 HOH 198 498 110 HOH HOH A . 
C 3 HOH 199 499 192 HOH HOH A . 
C 3 HOH 200 500 168 HOH HOH A . 
C 3 HOH 201 501 153 HOH HOH A . 
C 3 HOH 202 502 124 HOH HOH A . 
C 3 HOH 203 503 129 HOH HOH A . 
C 3 HOH 204 504 146 HOH HOH A . 
C 3 HOH 205 505 72  HOH HOH A . 
C 3 HOH 206 506 111 HOH HOH A . 
C 3 HOH 207 507 98  HOH HOH A . 
C 3 HOH 208 508 173 HOH HOH A . 
C 3 HOH 209 509 184 HOH HOH A . 
C 3 HOH 210 510 212 HOH HOH A . 
C 3 HOH 211 511 148 HOH HOH A . 
C 3 HOH 212 512 84  HOH HOH A . 
C 3 HOH 213 513 158 HOH HOH A . 
C 3 HOH 214 514 85  HOH HOH A . 
C 3 HOH 215 515 51  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         ? ? ? 1.15.2_3472 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER         ? ? ? .           4 
# 
_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                     8Z52 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.378 
_cell.length_a_esd                 ? 
_cell.length_b                     78.378 
_cell.length_b_esd                 ? 
_cell.length_c                     36.904 
_cell.length_c_esd                 ? 
_cell.volume                       226705.364 
_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                         8Z52 
_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                   8Z52 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.98 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.80 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '0.1M Na-acetate pH 4.5, 6.5% (w/v) NaCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'Bruker PHOTON III' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-04-14 
_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   1.5 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'BRUKER X8 PROTEUM' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          11.23 
_reflns.entry_id                                       8Z52 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.48 
_reflns.d_resolution_low                               22.159 
_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                                     19519 
_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                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.101 
_reflns.pdbx_Rpim_I_all                                0.04 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.093 
_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                                    1.48 
_reflns_shell.d_res_low                                     1.54 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3246 
_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                               4.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.929 
_reflns_shell.pdbx_Rpim_I_all                               0.44 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.183 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          91.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.811 
_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                               16.92 
_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                                 8Z52 
_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                            1.48 
_refine.ls_d_res_low                             21.74 
_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                     19519 
_refine.ls_number_reflns_R_free                  1952 
_refine.ls_number_reflns_R_work                  17567 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.88 
_refine.ls_percent_reflns_R_free                 10.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1815 
_refine.ls_R_factor_R_free                       0.2088 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1785 
_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                          1.34 
_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             1.1100 
_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                 19.5285 
_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                            0.1416 
_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                       1.48 
_refine_hist.d_res_low                        21.74 
_refine_hist.number_atoms_solvent             215 
_refine_hist.number_atoms_total               1229 
_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         13 
_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' ? 0.0035  ? 1084 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6902  ? 1476 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0785  ? 151  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0043  ? 195  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 23.0014 ? 401  ? 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' 1.48 1.52  . . 134 1210 98.75  . . . . 0.3201 . . . . . . . . . . . 0.3246 
'X-RAY DIFFRACTION' 1.52 1.56  . . 138 1232 100.00 . . . . 0.2629 . . . . . . . . . . . 0.2949 
'X-RAY DIFFRACTION' 1.56 1.61  . . 138 1241 100.00 . . . . 0.2328 . . . . . . . . . . . 0.2800 
'X-RAY DIFFRACTION' 1.61 1.66  . . 137 1228 100.00 . . . . 0.2105 . . . . . . . . . . . 0.2604 
'X-RAY DIFFRACTION' 1.66 1.72  . . 135 1220 100.00 . . . . 0.1979 . . . . . . . . . . . 0.2429 
'X-RAY DIFFRACTION' 1.72 1.79  . . 138 1246 100.00 . . . . 0.1932 . . . . . . . . . . . 0.2675 
'X-RAY DIFFRACTION' 1.79 1.87  . . 138 1236 100.00 . . . . 0.1940 . . . . . . . . . . . 0.2222 
'X-RAY DIFFRACTION' 1.87 1.97  . . 139 1257 100.00 . . . . 0.1735 . . . . . . . . . . . 0.2059 
'X-RAY DIFFRACTION' 1.97 2.09  . . 138 1240 100.00 . . . . 0.1700 . . . . . . . . . . . 0.1904 
'X-RAY DIFFRACTION' 2.09 2.25  . . 139 1252 100.00 . . . . 0.1580 . . . . . . . . . . . 0.2222 
'X-RAY DIFFRACTION' 2.25 2.48  . . 141 1267 100.00 . . . . 0.1628 . . . . . . . . . . . 0.1828 
'X-RAY DIFFRACTION' 2.48 2.84  . . 142 1283 100.00 . . . . 0.1632 . . . . . . . . . . . 0.1802 
'X-RAY DIFFRACTION' 2.84 3.57  . . 143 1289 100.00 . . . . 0.1571 . . . . . . . . . . . 0.1650 
'X-RAY DIFFRACTION' 3.57 21.74 . . 152 1366 99.61  . . . . 0.1625 . . . . . . . . . . . 0.2007 
# 
_struct.entry_id                     8Z52 
_struct.title                        'Hen Egg-White Lysozyme (HEWL) complexed with Theophylline' 
_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        8Z52 
_struct_keywords.text            'Lysozyme, Emetine, dimerization, drug-carrier, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_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              8Z52 
_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_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 ? ? ? ? ? ? ? 2.035 ? ? 
disulf2 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 115 SG ? ? A CYS 30 A CYS 115 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 80  SG ? ? A CYS 64 A CYS 80  1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf4 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 94  SG ? ? A CYS 76 A CYS 94  1_555 ? ? ? ? ? ? ? 2.025 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 6  ? CYS A 127 ? CYS A 6  ? 1_555 CYS A 127 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 30 ? CYS A 115 ? CYS A 30 ? 1_555 CYS A 115 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 64 ? CYS A 80  ? CYS A 64 ? 1_555 CYS A 80  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 76 ? CYS A 94  ? CYS A 76 ? 1_555 CYS A 94  ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 43 ? ARG A 45 ? THR A 43 ARG A 45 
AA1 2 THR A 51 ? TYR A 53 ? THR A 51 TYR A 53 
AA1 3 ILE A 58 ? ASN A 59 ? ILE A 58 ASN A 59 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASN A 44 ? N ASN A 44 O ASP A 52 ? O ASP A 52 
AA1 2 3 N TYR A 53 ? N TYR A 53 O ILE A 58 ? O ILE A 58 
# 
_pdbx_entry_details.entry_id                   8Z52 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 344 ? C HOH . 
2 1 A HOH 364 ? C HOH . 
3 1 A HOH 510 ? C HOH . 
# 
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  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
TEP C1   C N N 304 
TEP N1   N Y N 305 
TEP C2   C Y N 306 
TEP O2   O N N 307 
TEP N3   N Y N 308 
TEP C3   C N N 309 
TEP C4   C Y N 310 
TEP C5   C Y N 311 
TEP C6   C Y N 312 
TEP O6   O N N 313 
TEP N7   N Y N 314 
TEP C8   C Y N 315 
TEP N9   N Y N 316 
TEP H11  H N N 317 
TEP H12  H N N 318 
TEP H13  H N N 319 
TEP H31  H N N 320 
TEP H32  H N N 321 
TEP H33  H N N 322 
TEP HN7  H N N 323 
TEP H8   H N N 324 
THR N    N N N 325 
THR CA   C N S 326 
THR C    C N N 327 
THR O    O N N 328 
THR CB   C N R 329 
THR OG1  O N N 330 
THR CG2  C N N 331 
THR OXT  O N N 332 
THR H    H N N 333 
THR H2   H N N 334 
THR HA   H N N 335 
THR HB   H N N 336 
THR HG1  H N N 337 
THR HG21 H N N 338 
THR HG22 H N N 339 
THR HG23 H N N 340 
THR HXT  H N N 341 
TRP N    N N N 342 
TRP CA   C N S 343 
TRP C    C N N 344 
TRP O    O N N 345 
TRP CB   C N N 346 
TRP CG   C Y N 347 
TRP CD1  C Y N 348 
TRP CD2  C Y N 349 
TRP NE1  N Y N 350 
TRP CE2  C Y N 351 
TRP CE3  C Y N 352 
TRP CZ2  C Y N 353 
TRP CZ3  C Y N 354 
TRP CH2  C Y N 355 
TRP OXT  O N N 356 
TRP H    H N N 357 
TRP H2   H N N 358 
TRP HA   H N N 359 
TRP HB2  H N N 360 
TRP HB3  H N N 361 
TRP HD1  H N N 362 
TRP HE1  H N N 363 
TRP HE3  H N N 364 
TRP HZ2  H N N 365 
TRP HZ3  H N N 366 
TRP HH2  H N N 367 
TRP HXT  H N N 368 
TYR N    N N N 369 
TYR CA   C N S 370 
TYR C    C N N 371 
TYR O    O N N 372 
TYR CB   C N N 373 
TYR CG   C Y N 374 
TYR CD1  C Y N 375 
TYR CD2  C Y N 376 
TYR CE1  C Y N 377 
TYR CE2  C Y N 378 
TYR CZ   C Y N 379 
TYR OH   O N N 380 
TYR OXT  O N N 381 
TYR H    H N N 382 
TYR H2   H N N 383 
TYR HA   H N N 384 
TYR HB2  H N N 385 
TYR HB3  H N N 386 
TYR HD1  H N N 387 
TYR HD2  H N N 388 
TYR HE1  H N N 389 
TYR HE2  H N N 390 
TYR HH   H N N 391 
TYR HXT  H N N 392 
VAL N    N N N 393 
VAL CA   C N S 394 
VAL C    C N N 395 
VAL O    O N N 396 
VAL CB   C N N 397 
VAL CG1  C N N 398 
VAL CG2  C N N 399 
VAL OXT  O N N 400 
VAL H    H N N 401 
VAL H2   H N N 402 
VAL HA   H N N 403 
VAL HB   H N N 404 
VAL HG11 H N N 405 
VAL HG12 H N N 406 
VAL HG13 H N N 407 
VAL HG21 H N N 408 
VAL HG22 H N N 409 
VAL HG23 H N N 410 
VAL HXT  H N N 411 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
TEP C1  N1   sing N N 290 
TEP C1  H11  sing N N 291 
TEP C1  H12  sing N N 292 
TEP C1  H13  sing N N 293 
TEP N1  C2   sing Y N 294 
TEP N1  C6   sing Y N 295 
TEP C2  O2   doub N N 296 
TEP C2  N3   sing Y N 297 
TEP N3  C3   sing N N 298 
TEP N3  C4   sing Y N 299 
TEP C3  H31  sing N N 300 
TEP C3  H32  sing N N 301 
TEP C3  H33  sing N N 302 
TEP C4  C5   doub Y N 303 
TEP C4  N9   sing Y N 304 
TEP C5  C6   sing Y N 305 
TEP C5  N7   sing Y N 306 
TEP C6  O6   doub N N 307 
TEP N7  C8   sing Y N 308 
TEP N7  HN7  sing N N 309 
TEP C8  N9   doub Y N 310 
TEP C8  H8   sing N N 311 
THR N   CA   sing N N 312 
THR N   H    sing N N 313 
THR N   H2   sing N N 314 
THR CA  C    sing N N 315 
THR CA  CB   sing N N 316 
THR CA  HA   sing N N 317 
THR C   O    doub N N 318 
THR C   OXT  sing N N 319 
THR CB  OG1  sing N N 320 
THR CB  CG2  sing N N 321 
THR CB  HB   sing N N 322 
THR OG1 HG1  sing N N 323 
THR CG2 HG21 sing N N 324 
THR CG2 HG22 sing N N 325 
THR CG2 HG23 sing N N 326 
THR OXT HXT  sing N N 327 
TRP N   CA   sing N N 328 
TRP N   H    sing N N 329 
TRP N   H2   sing N N 330 
TRP CA  C    sing N N 331 
TRP CA  CB   sing N N 332 
TRP CA  HA   sing N N 333 
TRP C   O    doub N N 334 
TRP C   OXT  sing N N 335 
TRP CB  CG   sing N N 336 
TRP CB  HB2  sing N N 337 
TRP CB  HB3  sing N N 338 
TRP CG  CD1  doub Y N 339 
TRP CG  CD2  sing Y N 340 
TRP CD1 NE1  sing Y N 341 
TRP CD1 HD1  sing N N 342 
TRP CD2 CE2  doub Y N 343 
TRP CD2 CE3  sing Y N 344 
TRP NE1 CE2  sing Y N 345 
TRP NE1 HE1  sing N N 346 
TRP CE2 CZ2  sing Y N 347 
TRP CE3 CZ3  doub Y N 348 
TRP CE3 HE3  sing N N 349 
TRP CZ2 CH2  doub Y N 350 
TRP CZ2 HZ2  sing N N 351 
TRP CZ3 CH2  sing Y N 352 
TRP CZ3 HZ3  sing N N 353 
TRP CH2 HH2  sing N N 354 
TRP OXT HXT  sing N N 355 
TYR N   CA   sing N N 356 
TYR N   H    sing N N 357 
TYR N   H2   sing N N 358 
TYR CA  C    sing N N 359 
TYR CA  CB   sing N N 360 
TYR CA  HA   sing N N 361 
TYR C   O    doub N N 362 
TYR C   OXT  sing N N 363 
TYR CB  CG   sing N N 364 
TYR CB  HB2  sing N N 365 
TYR CB  HB3  sing N N 366 
TYR CG  CD1  doub Y N 367 
TYR CG  CD2  sing Y N 368 
TYR CD1 CE1  sing Y N 369 
TYR CD1 HD1  sing N N 370 
TYR CD2 CE2  doub Y N 371 
TYR CD2 HD2  sing N N 372 
TYR CE1 CZ   doub Y N 373 
TYR CE1 HE1  sing N N 374 
TYR CE2 CZ   sing Y N 375 
TYR CE2 HE2  sing N N 376 
TYR CZ  OH   sing N N 377 
TYR OH  HH   sing N N 378 
TYR OXT HXT  sing N N 379 
VAL N   CA   sing N N 380 
VAL N   H    sing N N 381 
VAL N   H2   sing N N 382 
VAL CA  C    sing N N 383 
VAL CA  CB   sing N N 384 
VAL CA  HA   sing N N 385 
VAL C   O    doub N N 386 
VAL C   OXT  sing N N 387 
VAL CB  CG1  sing N N 388 
VAL CB  CG2  sing N N 389 
VAL CB  HB   sing N N 390 
VAL CG1 HG11 sing N N 391 
VAL CG1 HG12 sing N N 392 
VAL CG1 HG13 sing N N 393 
VAL CG2 HG21 sing N N 394 
VAL CG2 HG22 sing N N 395 
VAL CG2 HG23 sing N N 396 
VAL OXT HXT  sing N N 397 
# 
_pdbx_audit_support.funding_organization   'Department of Biotechnology (DBT, India)' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           GAP299 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1BVX 
_pdbx_initial_refinement_model.details          ? 
# 
_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                    8Z52 
_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]   0.012759 
_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]   0.012759 
_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]   0.027097 
_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.
;
? 
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.
;
? 
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   . LYS A 1 1   ? 2.94699   10.02349 9.82823  1.000 11.42772 ? 1   LYS A N   1 
ATOM   2    C CA  . LYS A 1 1   ? 1.99678   10.42747 8.79640  1.000 10.67504 ? 1   LYS A CA  1 
ATOM   3    C C   . LYS A 1 1   ? 2.05986   11.93144 8.57524  1.000 11.74260 ? 1   LYS A C   1 
ATOM   4    O O   . LYS A 1 1   ? 2.05214   12.70354 9.53716  1.000 11.47974 ? 1   LYS A O   1 
ATOM   5    C CB  . LYS A 1 1   ? 0.57985   10.02963 9.20677  1.000 13.36555 ? 1   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 1   ? -0.49433  10.51062 8.24697  1.000 14.35764 ? 1   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 1   ? -1.85729  9.99077  8.64833  1.000 13.59138 ? 1   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 1   ? -2.95342  10.64077 7.81352  1.000 16.24064 ? 1   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 1   ? -4.26044  9.94990  8.00188  1.000 28.11873 ? 1   LYS A NZ  1 
ATOM   10   N N   . VAL A 1 2   ? 2.13260   12.35231 7.31618  1.000 12.66591 ? 2   VAL A N   1 
ATOM   11   C CA  . VAL A 1 2   ? 2.05764   13.76428 6.96006  1.000 11.87469 ? 2   VAL A CA  1 
ATOM   12   C C   . VAL A 1 2   ? 0.64554   14.03735 6.46435  1.000 12.85067 ? 2   VAL A C   1 
ATOM   13   O O   . VAL A 1 2   ? 0.26426   13.60627 5.36948  1.000 13.52260 ? 2   VAL A O   1 
ATOM   14   C CB  . VAL A 1 2   ? 3.11543   14.15809 5.92078  1.000 11.87387 ? 2   VAL A CB  1 
ATOM   15   C CG1 . VAL A 1 2   ? 2.95346   15.61707 5.54667  1.000 12.57679 ? 2   VAL A CG1 1 
ATOM   16   C CG2 . VAL A 1 2   ? 4.51054   13.91703 6.48348  1.000 11.03251 ? 2   VAL A CG2 1 
ATOM   17   N N   . PHE A 1 3   ? -0.13521  14.74249 7.27746  1.000 12.15520 ? 3   PHE A N   1 
ATOM   18   C CA  . PHE A 1 3   ? -1.50926  15.06757 6.93374  1.000 11.86413 ? 3   PHE A CA  1 
ATOM   19   C C   . PHE A 1 3   ? -1.55441  16.17747 5.89564  1.000 12.75109 ? 3   PHE A C   1 
ATOM   20   O O   . PHE A 1 3   ? -0.70035  17.06740 5.86036  1.000 11.37346 ? 3   PHE A O   1 
ATOM   21   C CB  . PHE A 1 3   ? -2.25394  15.58375 8.16886  1.000 10.70124 ? 3   PHE A CB  1 
ATOM   22   C CG  . PHE A 1 3   ? -2.84783  14.50589 9.02211  1.000 13.41929 ? 3   PHE A CG  1 
ATOM   23   C CD1 . PHE A 1 3   ? -4.19189  14.17498 8.90845  1.000 11.05682 ? 3   PHE A CD1 1 
ATOM   24   C CD2 . PHE A 1 3   ? -2.07067  13.83592 9.95799  1.000 11.49585 ? 3   PHE A CD2 1 
ATOM   25   C CE1 . PHE A 1 3   ? -4.74478  13.18911 9.69967  1.000 11.55743 ? 3   PHE A CE1 1 
ATOM   26   C CE2 . PHE A 1 3   ? -2.62057  12.84604 10.74922 1.000 12.32990 ? 3   PHE A CE2 1 
ATOM   27   C CZ  . PHE A 1 3   ? -3.96163  12.52514 10.62556 1.000 14.98251 ? 3   PHE A CZ  1 
ATOM   28   N N   . GLY A 1 4   ? -2.58161  16.12147 5.04588  1.000 15.71050 ? 4   GLY A N   1 
ATOM   29   C CA  . GLY A 1 4   ? -2.96869  17.28942 4.29586  1.000 14.06392 ? 4   GLY A CA  1 
ATOM   30   C C   . GLY A 1 4   ? -3.71641  18.28657 5.16293  1.000 10.65067 ? 4   GLY A C   1 
ATOM   31   O O   . GLY A 1 4   ? -4.21719  17.95972 6.23507  1.000 12.80735 ? 4   GLY A O   1 
ATOM   32   N N   . ARG A 1 5   ? -3.78242  19.52453 4.67582  1.000 15.27856 ? 5   ARG A N   1 
ATOM   33   C CA  . ARG A 1 5   ? -4.38415  20.61265 5.44185  1.000 14.86943 ? 5   ARG A CA  1 
ATOM   34   C C   . ARG A 1 5   ? -5.82909  20.29981 5.82221  1.000 12.58698 ? 5   ARG A C   1 
ATOM   35   O O   . ARG A 1 5   ? -6.19782  20.31496 7.00529  1.000 12.33464 ? 5   ARG A O   1 
ATOM   36   C CB  . ARG A 1 5   ? -4.29724  21.90156 4.62570  1.000 15.08491 ? 5   ARG A CB  1 
ATOM   37   C CG  . ARG A 1 5   ? -4.87698  23.10568 5.30471  1.000 13.55780 ? 5   ARG A CG  1 
ATOM   38   C CD  . ARG A 1 5   ? -4.61407  24.37058 4.49152  1.000 16.37909 ? 5   ARG A CD  1 
ATOM   39   N NE  . ARG A 1 5   ? -5.14838  24.30448 3.13265  1.000 20.96536 ? 5   ARG A NE  1 
ATOM   40   C CZ  . ARG A 1 5   ? -6.42244  24.52556 2.81892  1.000 19.96445 ? 5   ARG A CZ  1 
ATOM   41   N NH1 . ARG A 1 5   ? -7.30120  24.82172 3.76709  1.000 14.99658 ? 5   ARG A NH1 1 
ATOM   42   N NH2 . ARG A 1 5   ? -6.81873  24.44746 1.55702  1.000 19.53831 ? 5   ARG A NH2 1 
ATOM   43   N N   . CYS A 1 6   ? -6.67434  20.02578 4.82443  1.000 13.99159 ? 6   CYS A N   1 
ATOM   44   C CA  . CYS A 1 6   ? -8.07430  19.72192 5.11078  1.000 16.36867 ? 6   CYS A CA  1 
ATOM   45   C C   . CYS A 1 6   ? -8.23526  18.36800 5.78295  1.000 12.32043 ? 6   CYS A C   1 
ATOM   46   O O   . CYS A 1 6   ? -9.15809  18.18016 6.58418  1.000 13.09842 ? 6   CYS A O   1 
ATOM   47   C CB  . CYS A 1 6   ? -8.89359  19.75186 3.82496  1.000 13.81355 ? 6   CYS A CB  1 
ATOM   48   S SG  . CYS A 1 6   ? -8.99462  21.38280 3.12482  1.000 16.27289 ? 6   CYS A SG  1 
ATOM   49   N N   . GLU A 1 7   ? -7.36441  17.41290 5.45485  1.000 12.55322 ? 7   GLU A N   1 
ATOM   50   C CA  . GLU A 1 7   ? -7.41537  16.11397 6.11099  1.000 10.88572 ? 7   GLU A CA  1 
ATOM   51   C C   . GLU A 1 7   ? -7.21101  16.25610 7.61193  1.000 11.87977 ? 7   GLU A C   1 
ATOM   52   O O   . GLU A 1 7   ? -7.91388  15.62124 8.40715  1.000 12.77084 ? 7   GLU A O   1 
ATOM   53   C CB  . GLU A 1 7   ? -6.35158  15.19582 5.51184  1.000 14.83548 ? 7   GLU A CB  1 
ATOM   54   C CG  . GLU A 1 7   ? -6.37056  13.79488 6.08698  1.000 15.07482 ? 7   GLU A CG  1 
ATOM   55   C CD  . GLU A 1 7   ? -5.18273  12.95474 5.64979  1.000 19.76739 ? 7   GLU A CD  1 
ATOM   56   O OE1 . GLU A 1 7   ? -4.18480  13.52361 5.14651  1.000 16.30133 ? 7   GLU A OE1 1 
ATOM   57   O OE2 . GLU A 1 7   ? -5.25179  11.71976 5.81493  1.000 17.84919 ? 7   GLU A OE2 1 
ATOM   58   N N   . LEU A 1 8   ? -6.25685  17.09306 8.02063  1.000 12.82747 ? 8   LEU A N   1 
ATOM   59   C CA  . LEU A 1 8   ? -6.01351  17.28319 9.44455  1.000 9.01622  ? 8   LEU A CA  1 
ATOM   60   C C   . LEU A 1 8   ? -7.14930  18.05634 10.09873 1.000 11.17203 ? 8   LEU A C   1 
ATOM   61   O O   . LEU A 1 8   ? -7.55107  17.74049 11.22286 1.000 10.07805 ? 8   LEU A O   1 
ATOM   62   C CB  . LEU A 1 8   ? -4.68540  18.00210 9.65918  1.000 12.75031 ? 8   LEU A CB  1 
ATOM   63   C CG  . LEU A 1 8   ? -4.32605  18.20722 11.12907 1.000 10.80479 ? 8   LEU A CG  1 
ATOM   64   C CD1 . LEU A 1 8   ? -4.14900  16.86327 11.83317 1.000 10.37277 ? 8   LEU A CD1 1 
ATOM   65   C CD2 . LEU A 1 8   ? -3.08295  19.05913 11.24370 1.000 11.37714 ? 8   LEU A CD2 1 
ATOM   66   N N   . ALA A 1 9   ? -7.67037  19.07632 9.41575  1.000 13.31334 ? 9   ALA A N   1 
ATOM   67   C CA  . ALA A 1 9   ? -8.82919  19.79346 9.93695  1.000 14.60912 ? 9   ALA A CA  1 
ATOM   68   C C   . ALA A 1 9   ? -9.96420  18.82659 10.24730 1.000 11.77701 ? 9   ALA A C   1 
ATOM   69   O O   . ALA A 1 9   ? -10.56395 18.87574 11.32543 1.000 13.29424 ? 9   ALA A O   1 
ATOM   70   C CB  . ALA A 1 9   ? -9.27534  20.85940 8.93494  1.000 12.95512 ? 9   ALA A CB  1 
ATOM   71   N N   . ALA A 1 10  ? -10.24349 17.90652 9.31946  1.000 13.53585 ? 10  ALA A N   1 
ATOM   72   C CA  . ALA A 1 10  ? -11.33252 16.95462 9.51880  1.000 11.33598 ? 10  ALA A CA  1 
ATOM   73   C C   . ALA A 1 10  ? -11.05333 16.02172 10.69183 1.000 13.93042 ? 10  ALA A C   1 
ATOM   74   O O   . ALA A 1 10  ? -11.95717 15.71887 11.48307 1.000 13.96324 ? 10  ALA A O   1 
ATOM   75   C CB  . ALA A 1 10  ? -11.56388 16.15752 8.23693  1.000 14.54330 ? 10  ALA A CB  1 
ATOM   76   N N   . ALA A 1 11  ? -9.80934  15.55463 10.82259 1.000 13.35254 ? 11  ALA A N   1 
ATOM   77   C CA  . ALA A 1 11  ? -9.46515  14.68071 11.93860 1.000 9.79290  ? 11  ALA A CA  1 
ATOM   78   C C   . ALA A 1 11  ? -9.56879  15.41786 13.26555 1.000 12.98546 ? 11  ALA A C   1 
ATOM   79   O O   . ALA A 1 11  ? -10.02761 14.85199 14.26471 1.000 13.65837 ? 11  ALA A O   1 
ATOM   80   C CB  . ALA A 1 11  ? -8.05924  14.11258 11.74834 1.000 15.87459 ? 11  ALA A CB  1 
ATOM   81   N N   . MET A 1 12  ? -9.15068  16.68182 13.29733 1.000 14.52157 ? 12  MET A N   1 
ATOM   82   C CA  . MET A 1 12  ? -9.24533  17.45296 14.53127 1.000 11.47585 ? 12  MET A CA  1 
ATOM   83   C C   . MET A 1 12  ? -10.69722 17.68811 14.92258 1.000 12.96043 ? 12  MET A C   1 
ATOM   84   O O   . MET A 1 12  ? -11.04796 17.59726 16.10567 1.000 14.07680 ? 12  MET A O   1 
ATOM   85   C CB  . MET A 1 12  ? -8.50426  18.77688 14.37397 1.000 12.30918 ? 12  MET A CB  1 
ATOM   86   C CG  . MET A 1 12  ? -6.99228  18.62775 14.33264 1.000 9.77948  ? 12  MET A CG  1 
ATOM   87   S SD  . MET A 1 12  ? -6.19523  20.20566 14.01130 1.000 10.68663 ? 12  MET A SD  1 
ATOM   88   C CE  . MET A 1 12  ? -4.63006  19.95661 14.84097 1.000 11.70539 ? 12  MET A CE  1 
ATOM   89   N N   . LYS A 1 13  ? -11.55142 17.99008 13.93975 1.000 13.68509 ? 13  LYS A N   1 
ATOM   90   C CA  . LYS A 1 13  ? -12.97335 18.15523 14.22006 1.000 15.61026 ? 13  LYS A CA  1 
ATOM   91   C C   . LYS A 1 13  ? -13.58635 16.84732 14.69433 1.000 18.50522 ? 13  LYS A C   1 
ATOM   92   O O   . LYS A 1 13  ? -14.35112 16.82448 15.66851 1.000 18.79097 ? 13  LYS A O   1 
ATOM   93   C CB  . LYS A 1 13  ? -13.69659 18.64816 12.96817 1.000 14.64030 ? 13  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 13  ? -15.20154 18.75630 13.14851 1.000 17.80788 ? 13  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 13  ? -15.85776 19.44524 11.96959 1.000 20.99171 ? 13  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 13  ? -17.36671 19.51638 12.15793 1.000 29.21288 ? 13  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 13  ? -18.04491 20.21632 11.03201 1.000 28.05615 ? 13  LYS A NZ  1 
ATOM   98   N N   . ARG A 1 14  ? -13.25159 15.74823 14.01536 1.000 15.97579 ? 14  ARG A N   1 
ATOM   99   C CA  . ARG A 1 14  ? -13.70160 14.42331 14.42260 1.000 20.58275 ? 14  ARG A CA  1 
ATOM   100  C C   . ARG A 1 14  ? -13.40929 14.15343 15.89256 1.000 20.24354 ? 14  ARG A C   1 
ATOM   101  O O   . ARG A 1 14  ? -14.20719 13.50056 16.57580 1.000 22.73236 ? 14  ARG A O   1 
ATOM   102  C CB  . ARG A 1 14  ? -13.01989 13.38116 13.52754 1.000 23.74093 ? 14  ARG A CB  1 
ATOM   103  C CG  . ARG A 1 14  ? -13.10490 11.94522 14.00571 1.000 26.74493 ? 14  ARG A CG  1 
ATOM   104  C CD  . ARG A 1 14  ? -14.21613 11.21023 13.28103 1.000 28.39327 ? 14  ARG A CD  1 
ATOM   105  N NE  . ARG A 1 14  ? -15.51500 11.78437 13.61027 1.000 30.20134 ? 14  ARG A NE  1 
ATOM   106  C CZ  . ARG A 1 14  ? -16.34184 11.27853 14.51851 1.000 42.74690 ? 14  ARG A CZ  1 
ATOM   107  N NH1 . ARG A 1 14  ? -16.00478 10.17657 15.17755 1.000 26.49128 ? 14  ARG A NH1 1 
ATOM   108  N NH2 . ARG A 1 14  ? -17.50473 11.87365 14.76272 1.000 36.08129 ? 14  ARG A NH2 1 
ATOM   109  N N   . HIS A 1 15  ? -12.29113 14.66739 16.40525 1.000 16.74989 ? 15  HIS A N   1 
ATOM   110  C CA  . HIS A 1 15  ? -11.88183 14.43349 17.78418 1.000 16.85724 ? 15  HIS A CA  1 
ATOM   111  C C   . HIS A 1 15  ? -12.26153 15.57162 18.72715 1.000 15.46590 ? 15  HIS A C   1 
ATOM   112  O O   . HIS A 1 15  ? -11.75526 15.62469 19.85303 1.000 20.47728 ? 15  HIS A O   1 
ATOM   113  C CB  . HIS A 1 15  ? -10.37984 14.13738 17.84987 1.000 16.17365 ? 15  HIS A CB  1 
ATOM   114  C CG  . HIS A 1 15  ? -9.99909  12.82729 17.23191 1.000 13.26370 ? 15  HIS A CG  1 
ATOM   115  N ND1 . HIS A 1 15  ? -9.78641  12.67713 15.87887 1.000 16.31156 ? 15  HIS A ND1 1 
ATOM   116  C CD2 . HIS A 1 15  ? -9.81107  11.60433 17.78199 1.000 21.25382 ? 15  HIS A CD2 1 
ATOM   117  C CE1 . HIS A 1 15  ? -9.47157  11.41808 15.62093 1.000 23.45522 ? 15  HIS A CE1 1 
ATOM   118  N NE2 . HIS A 1 15  ? -9.48237  10.74720 16.75800 1.000 19.75800 ? 15  HIS A NE2 1 
ATOM   119  N N   . GLY A 1 16  ? -13.14055 16.47765 18.30026 1.000 17.77690 ? 16  GLY A N   1 
ATOM   120  C CA  . GLY A 1 16  ? -13.69426 17.46878 19.20529 1.000 18.02723 ? 16  GLY A CA  1 
ATOM   121  C C   . GLY A 1 16  ? -12.82410 18.67374 19.47197 1.000 14.59462 ? 16  GLY A C   1 
ATOM   122  O O   . GLY A 1 16  ? -13.02382 19.35486 20.48295 1.000 17.50474 ? 16  GLY A O   1 
ATOM   123  N N   . LEU A 1 17  ? -11.86228 18.96757 18.59872 1.000 13.84356 ? 17  LEU A N   1 
ATOM   124  C CA  . LEU A 1 17  ? -11.00314 20.12453 18.80941 1.000 13.18530 ? 17  LEU A CA  1 
ATOM   125  C C   . LEU A 1 17  ? -11.61115 21.41552 18.28742 1.000 17.50171 ? 17  LEU A C   1 
ATOM   126  O O   . LEU A 1 17  ? -11.21796 22.49554 18.73922 1.000 13.87265 ? 17  LEU A O   1 
ATOM   127  C CB  . LEU A 1 17  ? -9.65431  19.90735 18.12312 1.000 15.02446 ? 17  LEU A CB  1 
ATOM   128  C CG  . LEU A 1 17  ? -8.44115  19.50833 18.95389 1.000 22.22505 ? 17  LEU A CG  1 
ATOM   129  C CD1 . LEU A 1 17  ? -7.18931  19.80815 18.14857 1.000 11.58041 ? 17  LEU A CD1 1 
ATOM   130  C CD2 . LEU A 1 17  ? -8.40579  20.20546 20.32081 1.000 11.17177 ? 17  LEU A CD2 1 
ATOM   131  N N   . ASP A 1 18  ? -12.55037 21.34151 17.34664 1.000 18.98424 ? 18  ASP A N   1 
ATOM   132  C CA  . ASP A 1 18  ? -13.09941 22.55749 16.76265 1.000 19.51787 ? 18  ASP A CA  1 
ATOM   133  C C   . ASP A 1 18  ? -13.86810 23.34666 17.82174 1.000 18.22291 ? 18  ASP A C   1 
ATOM   134  O O   . ASP A 1 18  ? -14.82301 22.83980 18.42001 1.000 16.55492 ? 18  ASP A O   1 
ATOM   135  C CB  . ASP A 1 18  ? -13.97071 22.23544 15.54988 1.000 24.37980 ? 18  ASP A CB  1 
ATOM   136  C CG  . ASP A 1 18  ? -14.99174 21.15655 15.82422 1.000 25.43107 ? 18  ASP A CG  1 
ATOM   137  O OD1 . ASP A 1 18  ? -16.11985 21.28359 15.30346 1.000 35.08546 ? 18  ASP A OD1 1 
ATOM   138  O OD2 . ASP A 1 18  ? -14.67465 20.18460 16.54524 1.000 20.96322 ? 18  ASP A OD2 1 
ATOM   139  N N   B ASN A 1 19  ? -13.43995 24.58565 18.05452 0.473 15.50126 ? 19  ASN A N   1 
ATOM   140  N N   C ASN A 1 19  ? -13.43495 24.58565 18.05052 0.527 15.48636 ? 19  ASN A N   1 
ATOM   141  C CA  B ASN A 1 19  ? -13.97764 25.47779 19.07756 0.473 16.11617 ? 19  ASN A CA  1 
ATOM   142  C CA  C ASN A 1 19  ? -13.97064 25.47479 19.08156 0.527 16.10057 ? 19  ASN A CA  1 
ATOM   143  C C   B ASN A 1 19  ? -13.69935 25.00691 20.50054 0.473 15.46017 ? 19  ASN A C   1 
ATOM   144  C C   C ASN A 1 19  ? -13.73836 24.96492 20.49955 0.527 15.47225 ? 19  ASN A C   1 
ATOM   145  O O   B ASN A 1 19  ? -14.30310 25.53306 21.44263 0.473 15.70207 ? 19  ASN A O   1 
ATOM   146  O O   C ASN A 1 19  ? -14.40211 25.41406 21.43866 0.527 15.81150 ? 19  ASN A O   1 
ATOM   147  C CB  B ASN A 1 19  ? -15.46566 25.80189 18.87786 0.473 20.49431 ? 19  ASN A CB  1 
ATOM   148  C CB  C ASN A 1 19  ? -15.43966 25.85589 18.84985 0.527 20.47651 ? 19  ASN A CB  1 
ATOM   149  C CG  B ASN A 1 19  ? -15.75593 26.39078 17.50987 0.473 23.01611 ? 19  ASN A CG  1 
ATOM   150  C CG  C ASN A 1 19  ? -15.72446 27.30095 19.21077 0.527 22.59680 ? 19  ASN A CG  1 
ATOM   151  O OD1 B ASN A 1 19  ? -15.16893 27.40070 17.11764 0.473 26.66019 ? 19  ASN A OD1 1 
ATOM   152  O OD1 C ASN A 1 19  ? -14.86543 28.17286 19.05849 0.527 20.70517 ? 19  ASN A OD1 1 
ATOM   153  N ND2 B ASN A 1 19  ? -16.66314 25.75978 16.77414 0.473 23.09632 ? 19  ASN A ND2 1 
ATOM   154  N ND2 C ASN A 1 19  ? -16.93033 27.56310 19.70002 0.527 23.77079 ? 19  ASN A ND2 1 
ATOM   155  N N   . TYR A 1 20  ? -12.80239 24.03986 20.68843 1.000 12.33393 ? 20  TYR A N   1 
ATOM   156  C CA  . TYR A 1 20  ? -12.45912 23.59697 22.03340 1.000 11.20609 ? 20  TYR A CA  1 
ATOM   157  C C   . TYR A 1 20  ? -11.78685 24.74399 22.78013 1.000 12.43003 ? 20  TYR A C   1 
ATOM   158  O O   . TYR A 1 20  ? -10.83092 25.34786 22.28385 1.000 14.94469 ? 20  TYR A O   1 
ATOM   159  C CB  . TYR A 1 20  ? -11.54922 22.36689 22.00631 1.000 13.26668 ? 20  TYR A CB  1 
ATOM   160  C CG  . TYR A 1 20  ? -11.38996 21.75001 23.38134 1.000 14.08136 ? 20  TYR A CG  1 
ATOM   161  C CD1 . TYR A 1 20  ? -12.24994 20.75113 23.82363 1.000 14.17926 ? 20  TYR A CD1 1 
ATOM   162  C CD2 . TYR A 1 20  ? -10.39672 22.18602 24.25207 1.000 12.72005 ? 20  TYR A CD2 1 
ATOM   163  C CE1 . TYR A 1 20  ? -12.11969 20.20124 25.08966 1.000 15.54904 ? 20  TYR A CE1 1 
ATOM   164  C CE2 . TYR A 1 20  ? -10.25948 21.64013 25.51809 1.000 12.91390 ? 20  TYR A CE2 1 
ATOM   165  C CZ  . TYR A 1 20  ? -11.12247 20.65125 25.93039 1.000 13.62219 ? 20  TYR A CZ  1 
ATOM   166  O OH  . TYR A 1 20  ? -10.98022 20.10736 27.18541 1.000 17.01576 ? 20  TYR A OH  1 
ATOM   167  N N   A ARG A 1 21  ? -12.30356 25.03915 23.97322 0.385 11.63268 ? 21  ARG A N   1 
ATOM   168  N N   B ARG A 1 21  ? -12.29456 25.04215 23.97722 0.615 11.67026 ? 21  ARG A N   1 
ATOM   169  C CA  A ARG A 1 21  ? -11.87228 26.19419 24.76300 0.385 12.80151 ? 21  ARG A CA  1 
ATOM   170  C CA  B ARG A 1 21  ? -11.85328 26.19919 24.75800 0.615 12.63755 ? 21  ARG A CA  1 
ATOM   171  C C   A ARG A 1 21  ? -11.97336 27.49512 23.97190 0.385 11.50744 ? 21  ARG A C   1 
ATOM   172  C C   B ARG A 1 21  ? -11.95836 27.49512 23.95889 0.615 11.34753 ? 21  ARG A C   1 
ATOM   173  O O   A ARG A 1 21  ? -11.25022 28.45709 24.23964 0.385 11.77400 ? 21  ARG A O   1 
ATOM   174  O O   B ARG A 1 21  ? -11.22323 28.45408 24.20863 0.615 11.80274 ? 21  ARG A O   1 
ATOM   175  C CB  A ARG A 1 21  ? -10.47616 26.00614 25.36670 0.385 13.41473 ? 21  ARG A CB  1 
ATOM   176  C CB  B ARG A 1 21  ? -10.45316 26.01113 25.34870 0.615 13.33712 ? 21  ARG A CB  1 
ATOM   177  C CG  A ARG A 1 21  ? -10.46892 25.25127 26.68778 0.385 19.34302 ? 21  ARG A CG  1 
ATOM   178  C CG  B ARG A 1 21  ? -10.39597 25.04325 26.52078 0.615 19.59308 ? 21  ARG A CG  1 
ATOM   179  C CD  A ARG A 1 21  ? -10.40457 26.19838 27.88067 0.385 19.54772 ? 21  ARG A CD  1 
ATOM   180  C CD  B ARG A 1 21  ? -10.65561 25.74840 27.84377 0.615 19.53026 ? 21  ARG A CD  1 
ATOM   181  N NE  A ARG A 1 21  ? -11.55448 27.10048 27.94284 0.385 21.35674 ? 21  ARG A NE  1 
ATOM   182  N NE  B ARG A 1 21  ? -11.06645 24.81454 28.88796 0.615 24.25334 ? 21  ARG A NE  1 
ATOM   183  C CZ  A ARG A 1 21  ? -12.77342 26.73962 28.33216 0.385 28.58471 ? 21  ARG A CZ  1 
ATOM   184  C CZ  B ARG A 1 21  ? -10.98613 25.06766 30.19091 0.615 17.85810 ? 21  ARG A CZ  1 
ATOM   185  N NH1 A ARG A 1 21  ? -13.01644 25.48868 28.69834 0.385 31.70175 ? 21  ARG A NH1 1 
ATOM   186  N NH1 B ARG A 1 21  ? -11.38301 24.15478 31.07110 0.615 18.69418 ? 21  ARG A NH1 1 
ATOM   187  N NH2 A ARG A 1 21  ? -13.75534 27.63370 28.35329 0.385 23.67490 ? 21  ARG A NH2 1 
ATOM   188  N NH2 B ARG A 1 21  ? -10.50894 26.22866 30.61469 0.615 24.24570 ? 21  ARG A NH2 1 
ATOM   189  N N   . GLY A 1 22  ? -12.87458 27.53209 22.99310 1.000 10.89468 ? 22  GLY A N   1 
ATOM   190  C CA  . GLY A 1 22  ? -13.10366 28.72504 22.20903 1.000 10.41010 ? 22  GLY A CA  1 
ATOM   191  C C   . GLY A 1 22  ? -12.18391 28.92784 21.02880 1.000 11.46923 ? 22  GLY A C   1 
ATOM   192  O O   . GLY A 1 22  ? -12.25498 29.98078 20.38471 1.000 11.88509 ? 22  GLY A O   1 
ATOM   193  N N   . TYR A 1 23  ? -11.32506 27.95974 20.71770 1.000 9.73667  ? 23  TYR A N   1 
ATOM   194  C CA  . TYR A 1 23  ? -10.34130 28.09556 19.65046 1.000 9.49319  ? 23  TYR A CA  1 
ATOM   195  C C   . TYR A 1 23  ? -10.86864 27.40947 18.39965 1.000 8.81561  ? 23  TYR A C   1 
ATOM   196  O O   . TYR A 1 23  ? -11.02874 26.18448 18.37581 1.000 10.35077 ? 23  TYR A O   1 
ATOM   197  C CB  . TYR A 1 23  ? -9.00424  27.50649 20.08922 1.000 10.42892 ? 23  TYR A CB  1 
ATOM   198  C CG  . TYR A 1 23  ? -8.31694  28.38953 21.08997 1.000 7.11161  ? 23  TYR A CG  1 
ATOM   199  C CD1 . TYR A 1 23  ? -7.56595  29.47743 20.67169 1.000 8.00393  ? 23  TYR A CD1 1 
ATOM   200  C CD2 . TYR A 1 23  ? -8.43965  28.15268 22.45402 1.000 9.62913  ? 23  TYR A CD2 1 
ATOM   201  C CE1 . TYR A 1 23  ? -6.94668  30.30247 21.57547 1.000 10.32882 ? 23  TYR A CE1 1 
ATOM   202  C CE2 . TYR A 1 23  ? -7.82437  28.98372 23.37680 1.000 8.24009  ? 23  TYR A CE2 1 
ATOM   203  C CZ  . TYR A 1 23  ? -7.07639  30.05162 22.92652 1.000 11.32379 ? 23  TYR A CZ  1 
ATOM   204  O OH  . TYR A 1 23  ? -6.45412  30.88466 23.82430 1.000 10.70689 ? 23  TYR A OH  1 
ATOM   205  N N   . SER A 1 24  ? -11.12681 28.20039 17.36063 1.000 9.81458  ? 24  SER A N   1 
ATOM   206  C CA  . SER A 1 24  ? -11.67414 27.65331 16.13081 1.000 11.92404 ? 24  SER A CA  1 
ATOM   207  C C   . SER A 1 24  ? -10.69236 26.67517 15.49169 1.000 14.84750 ? 24  SER A C   1 
ATOM   208  O O   . SER A 1 24  ? -9.48830  26.66510 15.78041 1.000 14.29300 ? 24  SER A O   1 
ATOM   209  C CB  . SER A 1 24  ? -11.97027 28.77624 15.14277 1.000 12.95788 ? 24  SER A CB  1 
ATOM   210  O OG  . SER A 1 24  ? -10.76632 29.39410 14.73343 1.000 14.65058 ? 24  SER A OG  1 
ATOM   211  N N   . LEU A 1 25  ? -11.23464 25.85012 14.59389 1.000 13.24899 ? 25  LEU A N   1 
ATOM   212  C CA  . LEU A 1 25  ? -10.44687 24.80899 13.94682 1.000 11.88709 ? 25  LEU A CA  1 
ATOM   213  C C   . LEU A 1 25  ? -9.23699  25.38682 13.21948 1.000 12.45461 ? 25  LEU A C   1 
ATOM   214  O O   . LEU A 1 25  ? -8.16804  24.76573 13.19030 1.000 12.38206 ? 25  LEU A O   1 
ATOM   215  C CB  . LEU A 1 25  ? -11.34015 24.04997 12.97310 1.000 14.97169 ? 25  LEU A CB  1 
ATOM   216  C CG  . LEU A 1 25  ? -10.84139 22.73987 12.38211 1.000 15.91345 ? 25  LEU A CG  1 
ATOM   217  C CD1 . LEU A 1 25  ? -10.39322 21.78494 13.48610 1.000 17.07467 ? 25  LEU A CD1 1 
ATOM   218  C CD2 . LEU A 1 25  ? -11.95963 22.12988 11.55343 1.000 18.20363 ? 25  LEU A CD2 1 
ATOM   219  N N   . GLY A 1 26  ? -9.38403  26.57278 12.62540 1.000 10.69733 ? 26  GLY A N   1 
ATOM   220  C CA  . GLY A 1 26  ? -8.26014  27.18362 11.93608 1.000 10.98624 ? 26  GLY A CA  1 
ATOM   221  C C   . GLY A 1 26  ? -7.08390  27.47061 12.84978 1.000 8.08584  ? 26  GLY A C   1 
ATOM   222  O O   . GLY A 1 26  ? -5.92701  27.39348 12.42152 1.000 9.80923  ? 26  GLY A O   1 
ATOM   223  N N   . ASN A 1 27  ? -7.35659  27.81376 14.11381 1.000 8.01749  ? 27  ASN A N   1 
ATOM   224  C CA  . ASN A 1 27  ? -6.27735  28.01877 15.07654 1.000 8.44491  ? 27  ASN A CA  1 
ATOM   225  C C   . ASN A 1 27  ? -5.48040  26.74272 15.28949 1.000 9.32817  ? 27  ASN A C   1 
ATOM   226  O O   . ASN A 1 27  ? -4.24439  26.77563 15.35520 1.000 9.55430  ? 27  ASN A O   1 
ATOM   227  C CB  . ASN A 1 27  ? -6.84800  28.49395 16.41162 1.000 9.59150  ? 27  ASN A CB  1 
ATOM   228  C CG  . ASN A 1 27  ? -7.15188  29.97497 16.41555 1.000 8.19017  ? 27  ASN A CG  1 
ATOM   229  O OD1 . ASN A 1 27  ? -6.24380  30.80591 16.49426 1.000 8.97426  ? 27  ASN A OD1 1 
ATOM   230  N ND2 . ASN A 1 27  ? -8.43488  30.31807 16.29981 1.000 11.23441 ? 27  ASN A ND2 1 
ATOM   231  N N   . TRP A 1 28  ? -6.17547  25.61179 15.40176 1.000 8.75857  ? 28  TRP A N   1 
ATOM   232  C CA  . TRP A 1 28  ? -5.51452  24.33076 15.62774 1.000 8.81485  ? 28  TRP A CA  1 
ATOM   233  C C   . TRP A 1 28  ? -4.72284  23.88157 14.40360 1.000 6.93704  ? 28  TRP A C   1 
ATOM   234  O O   . TRP A 1 28  ? -3.62485  23.33250 14.54040 1.000 8.22571  ? 28  TRP A O   1 
ATOM   235  C CB  . TRP A 1 28  ? -6.55752  23.28589 16.02108 1.000 8.86527  ? 28  TRP A CB  1 
ATOM   236  C CG  . TRP A 1 28  ? -7.18419  23.58207 17.34819 1.000 7.85855  ? 28  TRP A CG  1 
ATOM   237  C CD1 . TRP A 1 28  ? -8.43410  24.09219 17.57843 1.000 10.20163 ? 28  TRP A CD1 1 
ATOM   238  C CD2 . TRP A 1 28  ? -6.57991  23.40515 18.63607 1.000 8.94344  ? 28  TRP A CD2 1 
ATOM   239  N NE1 . TRP A 1 28  ? -8.64277  24.23735 18.93146 1.000 9.36938  ? 28  TRP A NE1 1 
ATOM   240  C CE2 . TRP A 1 28  ? -7.52066  23.82132 19.60125 1.000 7.94585  ? 28  TRP A CE2 1 
ATOM   241  C CE3 . TRP A 1 28  ? -5.33385  22.92909 19.06583 1.000 11.62926 ? 28  TRP A CE3 1 
ATOM   242  C CZ2 . TRP A 1 28  ? -7.25735  23.76844 20.97119 1.000 9.50723  ? 28  TRP A CZ2 1 
ATOM   243  C CZ3 . TRP A 1 28  ? -5.07254  22.88220 20.42578 1.000 12.15673 ? 28  TRP A CZ3 1 
ATOM   244  C CH2 . TRP A 1 28  ? -6.02930  23.30038 21.36196 1.000 10.46107 ? 28  TRP A CH2 1 
ATOM   245  N N   . VAL A 1 29  ? -5.27810  24.08050 13.20071 1.000 6.68679  ? 29  VAL A N   1 
ATOM   246  C CA  . VAL A 1 29  ? -4.56441  23.71032 11.97558 1.000 5.84683  ? 29  VAL A CA  1 
ATOM   247  C C   . VAL A 1 29  ? -3.33238  24.58920 11.78721 1.000 10.36649 ? 29  VAL A C   1 
ATOM   248  O O   . VAL A 1 29  ? -2.25150  24.10608 11.42701 1.000 8.81978  ? 29  VAL A O   1 
ATOM   249  C CB  . VAL A 1 29  ? -5.51168  23.76528 10.75979 1.000 8.47924  ? 29  VAL A CB  1 
ATOM   250  C CG1 . VAL A 1 29  ? -4.75200  23.49408 9.46464  1.000 9.03470  ? 29  VAL A CG1 1 
ATOM   251  C CG2 . VAL A 1 29  ? -6.64872  22.75839 10.93115 1.000 11.74492 ? 29  VAL A CG2 1 
ATOM   252  N N   . CYS A 1 30  ? -3.48222  25.89424 12.02111 1.000 9.16100  ? 30  CYS A N   1 
ATOM   253  C CA  . CYS A 1 30  ? -2.34716  26.80914 11.94976 1.000 9.80237  ? 30  CYS A CA  1 
ATOM   254  C C   . CYS A 1 30  ? -1.24797  26.41515 12.93255 1.000 8.49728  ? 30  CYS A C   1 
ATOM   255  O O   . CYS A 1 30  ? -0.06405  26.37801 12.57628 1.000 9.34429  ? 30  CYS A O   1 
ATOM   256  C CB  . CYS A 1 30  ? -2.82598  28.23720 12.22073 1.000 6.75660  ? 30  CYS A CB  1 
ATOM   257  S SG  . CYS A 1 30  ? -1.54992  29.49508 12.04231 1.000 8.60616  ? 30  CYS A SG  1 
ATOM   258  N N   . ALA A 1 31  ? -1.62571  26.09630 14.17067 1.000 8.75349  ? 31  ALA A N   1 
ATOM   259  C CA  . ALA A 1 31  ? -0.62552  25.67832 15.14548 1.000 7.71878  ? 31  ALA A CA  1 
ATOM   260  C C   . ALA A 1 31  ? 0.08927   24.42021 14.68044 1.000 9.27420  ? 31  ALA A C   1 
ATOM   261  O O   . ALA A 1 31  ? 1.31928   24.33112 14.75517 1.000 10.04954 ? 31  ALA A O   1 
ATOM   262  C CB  . ALA A 1 31  ? -1.27823  25.46051 16.51065 1.000 9.75982  ? 31  ALA A CB  1 
ATOM   263  N N   . ALA A 1 32  ? -0.66393  23.44722 14.17171 1.000 7.60855  ? 32  ALA A N   1 
ATOM   264  C CA  . ALA A 1 32  ? -0.04013  22.21013 13.71869 1.000 7.26563  ? 32  ALA A CA  1 
ATOM   265  C C   . ALA A 1 32  ? 0.87662   22.46193 12.52946 1.000 6.98937  ? 32  ALA A C   1 
ATOM   266  O O   . ALA A 1 32  ? 1.94254   21.83883 12.41528 1.000 7.99030  ? 32  ALA A O   1 
ATOM   267  C CB  . ALA A 1 32  ? -1.10329  21.17018 13.37804 1.000 7.35752  ? 32  ALA A CB  1 
ATOM   268  N N   . LYS A 1 33  ? 0.48949   23.38088 11.64046 1.000 8.02298  ? 33  LYS A N   1 
ATOM   269  C CA  . LYS A 1 33  ? 1.32825   23.69369 10.48923 1.000 9.70743  ? 33  LYS A CA  1 
ATOM   270  C C   . LYS A 1 33  ? 2.71039   24.16462 10.92587 1.000 6.92084  ? 33  LYS A C   1 
ATOM   271  O O   . LYS A 1 33  ? 3.73224   23.66849 10.43669 1.000 9.87304  ? 33  LYS A O   1 
ATOM   272  C CB  . LYS A 1 33  ? 0.65714   24.75466 9.61328  1.000 8.65431  ? 33  LYS A CB  1 
ATOM   273  C CG  . LYS A 1 33  ? 1.58794   25.32548 8.56401  1.000 12.29566 ? 33  LYS A CG  1 
ATOM   274  C CD  . LYS A 1 33  ? 1.82760   24.31735 7.44406  1.000 12.04315 ? 33  LYS A CD  1 
ATOM   275  C CE  . LYS A 1 33  ? 2.79741   24.87117 6.41378  1.000 20.70278 ? 33  LYS A CE  1 
ATOM   276  N NZ  . LYS A 1 33  ? 3.04008   23.90404 5.30882  1.000 20.67980 ? 33  LYS A NZ  1 
ATOM   277  N N   . PHE A 1 34  ? 2.76568   25.11371 11.85076 1.000 9.86373  ? 34  PHE A N   1 
ATOM   278  C CA  . PHE A 1 34  ? 4.05481   25.67464 12.22641 1.000 9.53811  ? 34  PHE A CA  1 
ATOM   279  C C   . PHE A 1 34  ? 4.76799   24.88169 13.31033 1.000 10.90992 ? 34  PHE A C   1 
ATOM   280  O O   . PHE A 1 34  ? 5.99403   25.00161 13.44004 1.000 11.42816 ? 34  PHE A O   1 
ATOM   281  C CB  . PHE A 1 34  ? 3.90001   27.15769 12.57630 1.000 8.92416  ? 34  PHE A CB  1 
ATOM   282  C CG  . PHE A 1 34  ? 3.43481   27.98461 11.41632 1.000 9.53640  ? 34  PHE A CG  1 
ATOM   283  C CD1 . PHE A 1 34  ? 2.29190   28.75972 11.51151 1.000 13.55735 ? 34  PHE A CD1 1 
ATOM   284  C CD2 . PHE A 1 34  ? 4.11853   27.94444 10.20917 1.000 10.09680 ? 34  PHE A CD2 1 
ATOM   285  C CE1 . PHE A 1 34  ? 1.85571   29.50964 10.43753 1.000 13.53345 ? 34  PHE A CE1 1 
ATOM   286  C CE2 . PHE A 1 34  ? 3.69035   28.68736 9.13320  1.000 11.46634 ? 34  PHE A CE2 1 
ATOM   287  C CZ  . PHE A 1 34  ? 2.55244   29.47147 9.24738  1.000 9.90840  ? 34  PHE A CZ  1 
ATOM   288  N N   . GLU A 1 35  ? 4.04810   24.05783 14.06958 1.000 8.50831  ? 35  GLU A N   1 
ATOM   289  C CA  . GLU A 1 35  ? 4.73224   23.18787 15.01651 1.000 10.81055 ? 35  GLU A CA  1 
ATOM   290  C C   . GLU A 1 35  ? 5.37699   21.99375 14.32548 1.000 10.10225 ? 35  GLU A C   1 
ATOM   291  O O   . GLU A 1 35  ? 6.52903   21.65668 14.62625 1.000 9.09316  ? 35  GLU A O   1 
ATOM   292  C CB  . GLU A 1 35  ? 3.76645   22.69505 16.09778 1.000 9.30147  ? 35  GLU A CB  1 
ATOM   293  C CG  . GLU A 1 35  ? 3.25675   23.76419 17.04079 1.000 7.95206  ? 35  GLU A CG  1 
ATOM   294  C CD  . GLU A 1 35  ? 4.32501   24.33719 17.95048 1.000 10.83673 ? 35  GLU A CD  1 
ATOM   295  O OE1 . GLU A 1 35  ? 5.47996   23.86310 17.92227 1.000 11.76892 ? 35  GLU A OE1 1 
ATOM   296  O OE2 . GLU A 1 35  ? 3.99726   25.28429 18.69146 1.000 10.85425 ? 35  GLU A OE2 1 
ATOM   297  N N   . SER A 1 36  ? 4.66172   21.33271 13.40171 1.000 7.53243  ? 36  SER A N   1 
ATOM   298  C CA  . SER A 1 36  ? 5.13250   20.06062 12.86173 1.000 8.09070  ? 36  SER A CA  1 
ATOM   299  C C   . SER A 1 36  ? 5.10014   19.96847 11.34474 1.000 7.65137  ? 36  SER A C   1 
ATOM   300  O O   . SER A 1 36  ? 5.51594   18.93538 10.80475 1.000 9.42778  ? 36  SER A O   1 
ATOM   301  C CB  . SER A 1 36  ? 4.25252   18.91474 13.36804 1.000 9.21597  ? 36  SER A CB  1 
ATOM   302  O OG  . SER A 1 36  ? 2.91044   19.13181 12.95533 1.000 8.30992  ? 36  SER A OG  1 
ATOM   303  N N   . ASN A 1 37  ? 4.59106   20.98244 10.64176 1.000 9.87178  ? 37  ASN A N   1 
ATOM   304  C CA  . ASN A 1 37  ? 4.33273   20.87032 9.20183  1.000 11.26800 ? 37  ASN A CA  1 
ATOM   305  C C   . ASN A 1 37  ? 3.40356   19.69936 8.88916  1.000 7.35247  ? 37  ASN A C   1 
ATOM   306  O O   . ASN A 1 37  ? 3.53527   19.04325 7.84719  1.000 10.18033 ? 37  ASN A O   1 
ATOM   307  C CB  . ASN A 1 37  ? 5.61553   20.80713 8.36254  1.000 11.22713 ? 37  ASN A CB  1 
ATOM   308  C CG  . ASN A 1 37  ? 5.41025   21.32001 6.95054  1.000 14.44386 ? 37  ASN A CG  1 
ATOM   309  O OD1 . ASN A 1 37  ? 4.40723   21.96006 6.65670  1.000 14.94866 ? 37  ASN A OD1 1 
ATOM   310  N ND2 . ASN A 1 37  ? 6.35402   21.02884 6.06735  1.000 17.25398 ? 37  ASN A ND2 1 
ATOM   311  N N   . PHE A 1 38  ? 2.47475   19.42953 9.80940  1.000 7.70527  ? 38  PHE A N   1 
ATOM   312  C CA  . PHE A 1 38  ? 1.45264   18.38960 9.70673  1.000 8.70823  ? 38  PHE A CA  1 
ATOM   313  C C   . PHE A 1 38  ? 2.02555   16.97957 9.80974  1.000 8.12274  ? 38  PHE A C   1 
ATOM   314  O O   . PHE A 1 38  ? 1.34339   16.00859 9.44900  1.000 9.87974  ? 38  PHE A O   1 
ATOM   315  C CB  . PHE A 1 38  ? 0.60236   18.51355 8.43392  1.000 8.18070  ? 38  PHE A CB  1 
ATOM   316  C CG  . PHE A 1 38  ? -0.09557  19.84359 8.27294  1.000 10.86895 ? 38  PHE A CG  1 
ATOM   317  C CD1 . PHE A 1 38  ? -0.59126  20.53474 9.36599  1.000 10.16203 ? 38  PHE A CD1 1 
ATOM   318  C CD2 . PHE A 1 38  ? -0.27481  20.38348 7.01193  1.000 10.85149 ? 38  PHE A CD2 1 
ATOM   319  C CE1 . PHE A 1 38  ? -1.25020  21.74977 9.19702  1.000 7.71413  ? 38  PHE A CE1 1 
ATOM   320  C CE2 . PHE A 1 38  ? -0.92876  21.59351 6.83596  1.000 10.70250 ? 38  PHE A CE2 1 
ATOM   321  C CZ  . PHE A 1 38  ? -1.41745  22.28066 7.92900  1.000 9.21991  ? 38  PHE A CZ  1 
ATOM   322  N N   . ASN A 1 39  ? 3.26065   16.83152 10.28748 1.000 7.08481  ? 39  ASN A N   1 
ATOM   323  C CA  . ASN A 1 39  ? 3.93256   15.53847 10.36545 1.000 7.45135  ? 39  ASN A CA  1 
ATOM   324  C C   . ASN A 1 39  ? 3.76884   14.97762 11.77455 1.000 8.11057  ? 39  ASN A C   1 
ATOM   325  O O   . ASN A 1 39  ? 4.31510   15.53067 12.73437 1.000 9.61998  ? 39  ASN A O   1 
ATOM   326  C CB  . ASN A 1 39  ? 5.41150   15.72432 10.03709 1.000 9.63629  ? 39  ASN A CB  1 
ATOM   327  C CG  . ASN A 1 39  ? 6.14436   14.41324 9.89106  1.000 8.43024  ? 39  ASN A CG  1 
ATOM   328  O OD1 . ASN A 1 39  ? 5.64736   13.36232 10.28228 1.000 8.90989  ? 39  ASN A OD1 1 
ATOM   329  N ND2 . ASN A 1 39  ? 7.33923   14.46809 9.31178  1.000 13.11442 ? 39  ASN A ND2 1 
ATOM   330  N N   . THR A 1 40  ? 3.04277   13.86169 11.89982 1.000 8.64483  ? 40  THR A N   1 
ATOM   331  C CA  . THR A 1 40  ? 2.85503   13.26184 13.21893 1.000 9.45658  ? 40  THR A CA  1 
ATOM   332  C C   . THR A 1 40  ? 4.16113   12.79480 13.84367 1.000 9.17041  ? 40  THR A C   1 
ATOM   333  O O   . THR A 1 40  ? 4.23740   12.68591 15.06967 1.000 9.91954  ? 40  THR A O   1 
ATOM   334  C CB  . THR A 1 40  ? 1.85793   12.09392 13.19927 1.000 10.02704 ? 40  THR A CB  1 
ATOM   335  O OG1 . THR A 1 40  ? 2.44569   10.96181 12.54925 1.000 11.92320 ? 40  THR A OG1 1 
ATOM   336  C CG2 . THR A 1 40  ? 0.56980   12.46995 12.50153 1.000 11.16684 ? 40  THR A CG2 1 
ATOM   337  N N   . GLN A 1 41  ? 5.18293   12.50963 13.04647 1.000 9.37074  ? 41  GLN A N   1 
ATOM   338  C CA  . GLN A 1 41  ? 6.41601   11.96559 13.59724 1.000 7.76422  ? 41  GLN A CA  1 
ATOM   339  C C   . GLN A 1 41  ? 7.42918   13.03854 13.97390 1.000 11.02579 ? 41  GLN A C   1 
ATOM   340  O O   . GLN A 1 41  ? 8.55424   12.70149 14.35968 1.000 12.07945 ? 41  GLN A O   1 
ATOM   341  C CB  . GLN A 1 41  ? 7.03170   10.96144 12.62320 1.000 9.11853  ? 41  GLN A CB  1 
ATOM   342  C CG  . GLN A 1 41  ? 6.13254   9.77849  12.33952 1.000 9.89081  ? 41  GLN A CG  1 
ATOM   343  C CD  . GLN A 1 41  ? 6.87830   8.64736  11.67747 1.000 9.77807  ? 41  GLN A CD  1 
ATOM   344  O OE1 . GLN A 1 41  ? 7.56239   7.87637  12.34639 1.000 11.35702 ? 41  GLN A OE1 1 
ATOM   345  N NE2 . GLN A 1 41  ? 6.75799   8.54124  10.35950 1.000 11.51845 ? 41  GLN A NE2 1 
ATOM   346  N N   . ALA A 1 42  ? 7.05027   14.31357 13.89986 1.000 9.28242  ? 42  ALA A N   1 
ATOM   347  C CA  . ALA A 1 42  ? 7.97743   15.39552 14.20754 1.000 10.61163 ? 42  ALA A CA  1 
ATOM   348  C C   . ALA A 1 42  ? 8.43275   15.32463 15.66244 1.000 10.39484 ? 42  ALA A C   1 
ATOM   349  O O   . ALA A 1 42  ? 7.62595   15.12979 16.57265 1.000 8.80721  ? 42  ALA A O   1 
ATOM   350  C CB  . ALA A 1 42  ? 7.29748   16.73855 13.94756 1.000 10.73674 ? 42  ALA A CB  1 
ATOM   351  N N   . THR A 1 43  ? 9.73781   15.47755 15.87813 1.000 10.60155 ? 43  THR A N   1 
ATOM   352  C CA  . THR A 1 43  ? 10.30213  15.61963 17.21299 1.000 11.04198 ? 43  THR A CA  1 
ATOM   353  C C   . THR A 1 43  ? 11.32221  16.74455 17.16764 1.000 14.60614 ? 43  THR A C   1 
ATOM   354  O O   . THR A 1 43  ? 11.94200  16.99139 16.13048 1.000 15.44627 ? 43  THR A O   1 
ATOM   355  C CB  . THR A 1 43  ? 11.02414  14.34662 17.68295 1.000 8.73648  ? 43  THR A CB  1 
ATOM   356  O OG1 . THR A 1 43  ? 12.10491  14.04944 16.78473 1.000 12.08153 ? 43  THR A OG1 1 
ATOM   357  C CG2 . THR A 1 43  ? 10.07105  13.15671 17.74429 1.000 9.46472  ? 43  THR A CG2 1 
ATOM   358  N N   A ASN A 1 44  ? 11.47053  17.44565 18.29054 0.455 11.17130 ? 44  ASN A N   1 
ATOM   359  N N   B ASN A 1 44  ? 11.51853  17.40664 18.30753 0.545 11.16319 ? 44  ASN A N   1 
ATOM   360  C CA  A ASN A 1 44  ? 12.49564  18.47457 18.39920 0.455 11.85575 ? 44  ASN A CA  1 
ATOM   361  C CA  B ASN A 1 44  ? 12.48963  18.49557 18.38520 0.545 11.86900 ? 44  ASN A CA  1 
ATOM   362  C C   A ASN A 1 44  ? 13.00097  18.51568 19.83008 0.455 10.73057 ? 44  ASN A C   1 
ATOM   363  C C   B ASN A 1 44  ? 13.00097  18.61267 19.81307 0.545 10.63630 ? 44  ASN A C   1 
ATOM   364  O O   A ASN A 1 44  ? 12.20318  18.55883 20.77026 0.455 10.52845 ? 44  ASN A O   1 
ATOM   365  O O   B ASN A 1 44  ? 12.20820  18.80083 20.74123 0.545 10.09725 ? 44  ASN A O   1 
ATOM   366  C CB  A ASN A 1 44  ? 11.96566  19.85658 18.00118 0.455 15.21599 ? 44  ASN A CB  1 
ATOM   367  C CB  B ASN A 1 44  ? 11.85664  19.81058 17.92521 0.545 15.22815 ? 44  ASN A CB  1 
ATOM   368  C CG  A ASN A 1 44  ? 13.08370  20.87547 17.82483 0.455 17.23728 ? 44  ASN A CG  1 
ATOM   369  C CG  B ASN A 1 44  ? 11.69930  19.88244 16.41424 0.545 14.35910 ? 44  ASN A CG  1 
ATOM   370  O OD1 A ASN A 1 44  ? 13.83747  20.82431 16.85266 0.455 26.27182 ? 44  ASN A OD1 1 
ATOM   371  O OD1 B ASN A 1 44  ? 12.68713  19.90829 15.67401 0.545 18.07044 ? 44  ASN A OD1 1 
ATOM   372  N ND2 A ASN A 1 44  ? 13.19999  21.79855 18.76871 0.455 24.81162 ? 44  ASN A ND2 1 
ATOM   373  N ND2 B ASN A 1 44  ? 10.45319  19.89150 15.94853 0.545 17.68172 ? 44  ASN A ND2 1 
ATOM   374  N N   . ARG A 1 45  ? 14.32100  18.50958 19.98478 1.000 12.02369 ? 45  ARG A N   1 
ATOM   375  C CA  . ARG A 1 45  ? 14.93431  18.60166 21.30263 1.000 11.78458 ? 45  ARG A CA  1 
ATOM   376  C C   . ARG A 1 45  ? 15.05052  20.06070 21.71346 1.000 15.39732 ? 45  ARG A C   1 
ATOM   377  O O   . ARG A 1 45  ? 15.50841  20.90058 20.93227 1.000 14.78518 ? 45  ARG A O   1 
ATOM   378  C CB  . ARG A 1 45  ? 16.33126  17.98355 21.28537 1.000 14.84637 ? 45  ARG A CB  1 
ATOM   379  C CG  . ARG A 1 45  ? 16.86455  17.65965 22.68128 1.000 16.25063 ? 45  ARG A CG  1 
ATOM   380  C CD  . ARG A 1 45  ? 16.25955  16.35874 23.15255 1.000 14.51064 ? 45  ARG A CD  1 
ATOM   381  N NE  . ARG A 1 45  ? 16.55784  16.02286 24.54252 1.000 29.84750 ? 45  ARG A NE  1 
ATOM   382  C CZ  . ARG A 1 45  ? 17.44385  15.10282 24.91441 1.000 31.68611 ? 45  ARG A CZ  1 
ATOM   383  N NH1 . ARG A 1 45  ? 18.13659  14.43667 23.99931 1.000 31.68706 ? 45  ARG A NH1 1 
ATOM   384  N NH2 . ARG A 1 45  ? 17.63913  14.84793 26.20239 1.000 16.04373 ? 45  ARG A NH2 1 
ATOM   385  N N   . ASN A 1 46  ? 14.64983  20.35485 22.94152 1.000 12.62600 ? 46  ASN A N   1 
ATOM   386  C CA  . ASN A 1 46  ? 14.76506  21.69590 23.49136 1.000 14.05248 ? 46  ASN A CA  1 
ATOM   387  C C   . ASN A 1 46  ? 16.09624  21.86486 24.21504 1.000 17.55054 ? 46  ASN A C   1 
ATOM   388  O O   . ASN A 1 46  ? 16.78324  20.89584 24.54098 1.000 18.92582 ? 46  ASN A O   1 
ATOM   389  C CB  . ASN A 1 46  ? 13.60630  21.96909 24.45160 1.000 14.83522 ? 46  ASN A CB  1 
ATOM   390  C CG  . ASN A 1 46  ? 12.25314  21.76413 23.79693 1.000 17.69541 ? 46  ASN A CG  1 
ATOM   391  O OD1 . ASN A 1 46  ? 11.36721  21.11326 24.35120 1.000 27.14163 ? 46  ASN A OD1 1 
ATOM   392  N ND2 . ASN A 1 46  ? 12.08991  22.32103 22.60291 1.000 20.72409 ? 46  ASN A ND2 1 
ATOM   393  N N   . THR A 1 47  ? 16.44840  23.12886 24.46883 1.000 21.82640 ? 47  THR A N   1 
ATOM   394  C CA  . THR A 1 47  ? 17.71458  23.44482 25.12451 1.000 25.14776 ? 47  THR A CA  1 
ATOM   395  C C   . THR A 1 47  ? 17.81883  22.76395 26.48556 1.000 23.79710 ? 47  THR A C   1 
ATOM   396  O O   . THR A 1 47  ? 18.89689  22.29990 26.87736 1.000 22.77614 ? 47  THR A O   1 
ATOM   397  C CB  . THR A 1 47  ? 17.82874  24.95783 25.29633 1.000 18.75002 ? 47  THR A CB  1 
ATOM   398  O OG1 . THR A 1 47  ? 16.59990  25.47098 25.83056 1.000 31.21815 ? 47  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 47  ? 18.08949  25.61567 23.96221 1.000 19.32596 ? 47  THR A CG2 1 
ATOM   400  N N   . ASP A 1 48  ? 16.70799  22.69411 27.20982 1.000 18.95034 ? 48  ASP A N   1 
ATOM   401  C CA  . ASP A 1 48  ? 16.66727  22.19425 28.57688 1.000 18.39805 ? 48  ASP A CA  1 
ATOM   402  C C   . ASP A 1 48  ? 16.65916  20.67426 28.66603 1.000 21.64203 ? 48  ASP A C   1 
ATOM   403  O O   . ASP A 1 48  ? 16.51837  20.13838 29.77011 1.000 20.72820 ? 48  ASP A O   1 
ATOM   404  C CB  . ASP A 1 48  ? 15.46548  22.78842 29.32109 1.000 18.49234 ? 48  ASP A CB  1 
ATOM   405  C CG  . ASP A 1 48  ? 14.12833  22.21748 28.85445 1.000 25.08423 ? 48  ASP A CG  1 
ATOM   406  O OD1 . ASP A 1 48  ? 14.07604  21.53038 27.81253 1.000 20.38329 ? 48  ASP A OD1 1 
ATOM   407  O OD2 . ASP A 1 48  ? 13.11551  22.47163 29.53566 1.000 30.37494 ? 48  ASP A OD2 1 
ATOM   408  N N   . GLY A 1 49  ? 16.80185  19.97414 27.54207 1.000 20.74630 ? 49  GLY A N   1 
ATOM   409  C CA  . GLY A 1 49  ? 16.80573  18.52913 27.53821 1.000 18.91984 ? 49  GLY A CA  1 
ATOM   410  C C   . GLY A 1 49  ? 15.45363  17.88422 27.32058 1.000 16.22077 ? 49  GLY A C   1 
ATOM   411  O O   . GLY A 1 49  ? 15.40147  16.67820 27.05372 1.000 16.22546 ? 49  GLY A O   1 
ATOM   412  N N   . SER A 1 50  ? 14.36272  18.63632 27.43876 1.000 11.89435 ? 50  SER A N   1 
ATOM   413  C CA  . SER A 1 50  ? 13.05760  18.09340 27.10611 1.000 11.40319 ? 50  SER A CA  1 
ATOM   414  C C   . SER A 1 50  ? 12.93524  17.96126 25.59115 1.000 11.94244 ? 50  SER A C   1 
ATOM   415  O O   . SER A 1 50  ? 13.78110  18.44011 24.82991 1.000 10.45289 ? 50  SER A O   1 
ATOM   416  C CB  . SER A 1 50  ? 11.94479  18.99154 27.64728 1.000 13.67946 ? 50  SER A CB  1 
ATOM   417  O OG  . SER A 1 50  ? 11.90573  20.22447 26.94916 1.000 15.34039 ? 50  SER A OG  1 
ATOM   418  N N   . THR A 1 51  ? 11.86608  17.29430 25.15446 1.000 9.17715  ? 51  THR A N   1 
ATOM   419  C CA  . THR A 1 51  ? 11.61774  17.06718 23.73454 1.000 6.14251  ? 51  THR A CA  1 
ATOM   420  C C   . THR A 1 51  ? 10.14869  17.31327 23.42985 1.000 7.21420  ? 51  THR A C   1 
ATOM   421  O O   . THR A 1 51  ? 9.27685   16.97742 24.23609 1.000 8.36004  ? 51  THR A O   1 
ATOM   422  C CB  . THR A 1 51  ? 12.00054  15.63311 23.35160 1.000 6.65236  ? 51  THR A CB  1 
ATOM   423  O OG1 . THR A 1 51  ? 13.38259  15.42603 23.65030 1.000 7.25806  ? 51  THR A OG1 1 
ATOM   424  C CG2 . THR A 1 51  ? 11.78117  15.37398 21.85767 1.000 10.20486 ? 51  THR A CG2 1 
ATOM   425  N N   . ASP A 1 52  ? 9.87847   17.89917 22.26086 1.000 7.48192  ? 52  ASP A N   1 
ATOM   426  C CA  . ASP A 1 52  ? 8.51938   18.10823 21.77115 1.000 7.05193  ? 52  ASP A CA  1 
ATOM   427  C C   . ASP A 1 52  ? 8.17606   17.01416 20.76933 1.000 7.56962  ? 52  ASP A C   1 
ATOM   428  O O   . ASP A 1 52  ? 9.00784   16.65401 19.93018 1.000 9.24238  ? 52  ASP A O   1 
ATOM   429  C CB  . ASP A 1 52  ? 8.40432   19.45817 21.06104 1.000 11.26560 ? 52  ASP A CB  1 
ATOM   430  C CG  . ASP A 1 52  ? 8.75362   20.62823 21.95484 1.000 16.96284 ? 52  ASP A CG  1 
ATOM   431  O OD1 . ASP A 1 52  ? 8.64390   20.49936 23.18888 1.000 14.29664 ? 52  ASP A OD1 1 
ATOM   432  O OD2 . ASP A 1 52  ? 9.12759   21.69015 21.41365 1.000 23.86710 ? 52  ASP A OD2 1 
ATOM   433  N N   . TYR A 1 53  ? 6.94003   16.51227 20.83567 1.000 6.07754  ? 53  TYR A N   1 
ATOM   434  C CA  . TYR A 1 53  ? 6.53076   15.33623 20.07688 1.000 6.61680  ? 53  TYR A CA  1 
ATOM   435  C C   . TYR A 1 53  ? 5.23961   15.58425 19.31315 1.000 9.06195  ? 53  TYR A C   1 
ATOM   436  O O   . TYR A 1 53  ? 4.25778   16.05639 19.89133 1.000 8.33700  ? 53  TYR A O   1 
ATOM   437  C CB  . TYR A 1 53  ? 6.29588   14.15634 21.02205 1.000 7.43687  ? 53  TYR A CB  1 
ATOM   438  C CG  . TYR A 1 53  ? 7.53001   13.67931 21.73981 1.000 11.06542 ? 53  TYR A CG  1 
ATOM   439  C CD1 . TYR A 1 53  ? 8.30181   12.64820 21.21574 1.000 8.18986  ? 53  TYR A CD1 1 
ATOM   440  C CD2 . TYR A 1 53  ? 7.92933   14.25840 22.93967 1.000 8.78482  ? 53  TYR A CD2 1 
ATOM   441  C CE1 . TYR A 1 53  ? 9.43692   12.20417 21.86753 1.000 7.27470  ? 53  TYR A CE1 1 
ATOM   442  C CE2 . TYR A 1 53  ? 9.05445   13.81837 23.60245 1.000 7.06046  ? 53  TYR A CE2 1 
ATOM   443  C CZ  . TYR A 1 53  ? 9.80524   12.79726 23.05638 1.000 6.68397  ? 53  TYR A CZ  1 
ATOM   444  O OH  . TYR A 1 53  ? 10.93535  12.36623 23.70717 1.000 9.32086  ? 53  TYR A OH  1 
ATOM   445  N N   . GLY A 1 54  ? 5.23429   15.23513 18.02418 1.000 9.57079  ? 54  GLY A N   1 
ATOM   446  C CA  . GLY A 1 54  ? 3.98711   15.07415 17.29149 1.000 7.84564  ? 54  GLY A CA  1 
ATOM   447  C C   . GLY A 1 54  ? 3.50105   16.32312 16.58547 1.000 8.71385  ? 54  GLY A C   1 
ATOM   448  O O   . GLY A 1 54  ? 4.17911   17.35306 16.50521 1.000 9.05670  ? 54  GLY A O   1 
ATOM   449  N N   . ILE A 1 55  ? 2.26392   16.21117 16.07277 1.000 8.99274  ? 55  ILE A N   1 
ATOM   450  C CA  . ILE A 1 55  ? 1.66581   17.25714 15.23680 1.000 11.11557 ? 55  ILE A CA  1 
ATOM   451  C C   . ILE A 1 55  ? 1.57709   18.58022 15.96969 1.000 9.75609  ? 55  ILE A C   1 
ATOM   452  O O   . ILE A 1 55  ? 1.64303   19.64415 15.34757 1.000 10.36264 ? 55  ILE A O   1 
ATOM   453  C CB  . ILE A 1 55  ? 0.27666   16.85920 14.69216 1.000 13.79456 ? 55  ILE A CB  1 
ATOM   454  C CG1 . ILE A 1 55  ? -0.65912  16.44139 15.82741 1.000 14.54846 ? 55  ILE A CG1 1 
ATOM   455  C CG2 . ILE A 1 55  ? 0.39132   15.81308 13.61023 1.000 18.87366 ? 55  ILE A CG2 1 
ATOM   456  C CD1 . ILE A 1 55  ? -2.12117  16.69647 15.51972 1.000 21.80113 ? 55  ILE A CD1 1 
ATOM   457  N N   . LEU A 1 56  ? 1.38539   18.54437 17.28573 1.000 10.29163 ? 56  LEU A N   1 
ATOM   458  C CA  . LEU A 1 56  ? 1.29867   19.75445 18.08963 1.000 9.76985  ? 56  LEU A CA  1 
ATOM   459  C C   . LEU A 1 56  ? 2.50089   19.93845 19.01034 1.000 12.02894 ? 56  LEU A C   1 
ATOM   460  O O   . LEU A 1 56  ? 2.46317   20.79154 19.90626 1.000 10.03907 ? 56  LEU A O   1 
ATOM   461  C CB  . LEU A 1 56  ? -0.02915  19.80964 18.85593 1.000 9.51324  ? 56  LEU A CB  1 
ATOM   462  C CG  . LEU A 1 56  ? -1.22933  20.14465 17.95917 1.000 10.68364 ? 56  LEU A CG  1 
ATOM   463  C CD1 . LEU A 1 56  ? -2.54019  19.83682 18.68050 1.000 16.73610 ? 56  LEU A CD1 1 
ATOM   464  C CD2 . LEU A 1 56  ? -1.17931  21.60660 17.52302 1.000 11.49259 ? 56  LEU A CD2 1 
ATOM   465  N N   . GLN A 1 57  ? 3.57078   19.17034 18.79817 1.000 9.65098  ? 57  GLN A N   1 
ATOM   466  C CA  . GLN A 1 57  ? 4.85595   19.39630 19.46186 1.000 8.57304  ? 57  GLN A CA  1 
ATOM   467  C C   . GLN A 1 57  ? 4.70431   19.52046 20.97888 1.000 11.33777 ? 57  GLN A C   1 
ATOM   468  O O   . GLN A 1 57  ? 5.18153   20.46849 21.61067 1.000 10.98602 ? 57  GLN A O   1 
ATOM   469  C CB  . GLN A 1 57  ? 5.59391   20.58518 18.84857 1.000 7.60566  ? 57  GLN A CB  1 
ATOM   470  C CG  . GLN A 1 57  ? 6.12257   20.27500 17.45748 1.000 8.04690  ? 57  GLN A CG  1 
ATOM   471  C CD  . GLN A 1 57  ? 7.28449   19.30091 17.48931 1.000 10.14522 ? 57  GLN A CD  1 
ATOM   472  O OE1 . GLN A 1 57  ? 8.42957   19.69783 17.69701 1.000 11.30129 ? 57  GLN A OE1 1 
ATOM   473  N NE2 . GLN A 1 57  ? 6.99734   18.01891 17.28150 1.000 8.83134  ? 57  GLN A NE2 1 
ATOM   474  N N   . ILE A 1 58  ? 4.03136   18.52658 21.55613 1.000 8.68060  ? 58  ILE A N   1 
ATOM   475  C CA  . ILE A 1 58  ? 3.76769   18.49774 22.98919 1.000 9.05555  ? 58  ILE A CA  1 
ATOM   476  C C   . ILE A 1 58  ? 5.03683   18.11871 23.74094 1.000 9.73755  ? 58  ILE A C   1 
ATOM   477  O O   . ILE A 1 58  ? 5.76766   17.19861 23.34787 1.000 10.11867 ? 58  ILE A O   1 
ATOM   478  C CB  . ILE A 1 58  ? 2.60667   17.52986 23.26456 1.000 9.17928  ? 58  ILE A CB  1 
ATOM   479  C CG1 . ILE A 1 58  ? 1.29861   18.15692 22.76779 1.000 11.92889 ? 58  ILE A CG1 1 
ATOM   480  C CG2 . ILE A 1 58  ? 2.52498   17.17502 24.72761 1.000 12.26025 ? 58  ILE A CG2 1 
ATOM   481  C CD1 . ILE A 1 58  ? 0.14252   17.20401 22.70415 1.000 12.30868 ? 58  ILE A CD1 1 
ATOM   482  N N   . ASN A 1 59  ? 5.31113   18.84180 24.82481 1.000 10.85838 ? 59  ASN A N   1 
ATOM   483  C CA  . ASN A 1 59  ? 6.61128   18.80776 25.47951 1.000 10.75769 ? 59  ASN A CA  1 
ATOM   484  C C   . ASN A 1 59  ? 6.64246   17.79987 26.62161 1.000 10.20709 ? 59  ASN A C   1 
ATOM   485  O O   . ASN A 1 59  ? 5.68463   17.67302 27.39284 1.000 13.92061 ? 59  ASN A O   1 
ATOM   486  C CB  . ASN A 1 59  ? 6.96452   20.18578 26.03230 1.000 15.63584 ? 59  ASN A CB  1 
ATOM   487  C CG  . ASN A 1 59  ? 8.41662   20.29170 26.41095 1.000 21.63777 ? 59  ASN A CG  1 
ATOM   488  O OD1 . ASN A 1 59  ? 8.78685   19.99779 27.53590 1.000 32.81546 ? 59  ASN A OD1 1 
ATOM   489  N ND2 . ASN A 1 59  ? 9.24644   20.74154 25.48072 1.000 34.44554 ? 59  ASN A ND2 1 
ATOM   490  N N   . SER A 1 60  ? 7.78243   17.11779 26.74441 1.000 8.83107  ? 60  SER A N   1 
ATOM   491  C CA  . SER A 1 60  ? 7.99959   16.10987 27.77147 1.000 8.95319  ? 60  SER A CA  1 
ATOM   492  C C   . SER A 1 60  ? 8.20795   16.68700 29.16836 1.000 11.84481 ? 60  SER A C   1 
ATOM   493  O O   . SER A 1 60  ? 8.14211   15.92210 30.13245 1.000 14.17266 ? 60  SER A O   1 
ATOM   494  C CB  . SER A 1 60  ? 9.17842   15.21774 27.35728 1.000 7.70929  ? 60  SER A CB  1 
ATOM   495  O OG  . SER A 1 60  ? 10.40448  15.93764 27.37893 1.000 10.09952 ? 60  SER A OG  1 
ATOM   496  N N   . ARG A 1 61  ? 8.44509   17.99399 29.31718 1.000 13.27020 ? 61  ARG A N   1 
ATOM   497  C CA  . ARG A 1 61  ? 8.70944   18.48911 30.67107 1.000 14.14524 ? 61  ARG A CA  1 
ATOM   498  C C   . ARG A 1 61  ? 7.45564   18.45729 31.53136 1.000 19.00936 ? 61  ARG A C   1 
ATOM   499  O O   . ARG A 1 61  ? 7.55291   18.32941 32.75635 1.000 17.54877 ? 61  ARG A O   1 
ATOM   500  C CB  . ARG A 1 61  ? 9.39356   19.86505 30.67877 1.000 27.09505 ? 61  ARG A CB  1 
ATOM   501  C CG  . ARG A 1 61  ? 8.55455   21.04808 30.23685 1.000 38.90216 ? 61  ARG A CG  1 
ATOM   502  C CD  . ARG A 1 61  ? 9.38365   22.33301 30.21453 1.000 49.38483 ? 61  ARG A CD  1 
ATOM   503  N NE  . ARG A 1 61  ? 10.29539  22.37582 29.07031 1.000 38.92876 ? 61  ARG A NE  1 
ATOM   504  C CZ  . ARG A 1 61  ? 10.42929  23.41372 28.25018 1.000 43.61003 ? 61  ARG A CZ  1 
ATOM   505  N NH1 . ARG A 1 61  ? 9.70542   24.50980 28.43524 1.000 54.87431 ? 61  ARG A NH1 1 
ATOM   506  N NH2 . ARG A 1 61  ? 11.28705  23.35555 27.23799 1.000 38.95112 ? 61  ARG A NH2 1 
ATOM   507  N N   . TRP A 1 62  ? 6.27650   18.51633 30.91362 0.961 12.33392 ? 62  TRP A N   1 
ATOM   508  C CA  . TRP A 1 62  ? 5.03267   18.50950 31.67290 0.961 13.18121 ? 62  TRP A CA  1 
ATOM   509  C C   . TRP A 1 62  ? 4.06349   17.41054 31.26324 0.961 11.11275 ? 62  TRP A C   1 
ATOM   510  O O   . TRP A 1 62  ? 3.31364   16.90469 32.09946 0.961 11.27306 ? 62  TRP A O   1 
ATOM   511  C CB  . TRP A 1 62  ? 4.31275   19.85455 31.54593 0.961 15.63453 ? 62  TRP A CB  1 
ATOM   512  C CG  . TRP A 1 62  ? 5.05699   20.98055 32.16065 0.961 17.83861 ? 62  TRP A CG  1 
ATOM   513  C CD1 . TRP A 1 62  ? 5.62892   22.03444 31.51342 0.961 23.78534 ? 62  TRP A CD1 1 
ATOM   514  C CD2 . TRP A 1 62  ? 5.32332   21.16767 33.55257 0.961 25.97805 ? 62  TRP A CD2 1 
ATOM   515  N NE1 . TRP A 1 62  ? 6.23420   22.87048 32.41919 0.961 30.43880 ? 62  TRP A NE1 1 
ATOM   516  C CE2 . TRP A 1 62  ? 6.06045   22.35862 33.67829 0.961 27.00714 ? 62  TRP A CE2 1 
ATOM   517  C CE3 . TRP A 1 62  ? 5.00952   20.44181 34.70572 0.961 23.00642 ? 62  TRP A CE3 1 
ATOM   518  C CZ2 . TRP A 1 62  ? 6.49277   22.84171 34.91114 0.961 37.68933 ? 62  TRP A CZ2 1 
ATOM   519  C CZ3 . TRP A 1 62  ? 5.43484   20.92390 35.92857 0.961 34.52867 ? 62  TRP A CZ3 1 
ATOM   520  C CH2 . TRP A 1 62  ? 6.16596   22.11385 36.02229 0.961 38.23135 ? 62  TRP A CH2 1 
ATOM   521  N N   . TRP A 1 63  ? 4.04217   17.03842 29.98528 1.000 9.23680  ? 63  TRP A N   1 
ATOM   522  C CA  . TRP A 1 63  ? 2.83599   16.42546 29.44461 1.000 8.33823  ? 63  TRP A CA  1 
ATOM   523  C C   . TRP A 1 63  ? 2.93180   14.94542 29.12174 1.000 8.94030  ? 63  TRP A C   1 
ATOM   524  O O   . TRP A 1 63  ? 1.91376   14.25651 29.17504 1.000 11.71597 ? 63  TRP A O   1 
ATOM   525  C CB  . TRP A 1 63  ? 2.35977   17.19338 28.20665 1.000 9.51863  ? 63  TRP A CB  1 
ATOM   526  C CG  . TRP A 1 63  ? 2.16996   18.64542 28.51655 1.000 7.32487  ? 63  TRP A CG  1 
ATOM   527  C CD1 . TRP A 1 63  ? 2.94695   19.68732 28.10526 1.000 13.00119 ? 63  TRP A CD1 1 
ATOM   528  C CD2 . TRP A 1 63  ? 1.14420   19.20959 29.33972 1.000 11.26113 ? 63  TRP A CD2 1 
ATOM   529  N NE1 . TRP A 1 63  ? 2.46017   20.87041 28.61226 1.000 14.38110 ? 63  TRP A NE1 1 
ATOM   530  C CE2 . TRP A 1 63  ? 1.35432   20.60157 29.37354 1.000 11.58293 ? 63  TRP A CE2 1 
ATOM   531  C CE3 . TRP A 1 63  ? 0.05931   18.67275 30.04003 1.000 12.76480 ? 63  TRP A CE3 1 
ATOM   532  C CZ2 . TRP A 1 63  ? 0.52255   21.46371 30.08564 1.000 13.74127 ? 63  TRP A CZ2 1 
ATOM   533  C CZ3 . TRP A 1 63  ? -0.76246  19.52788 30.74513 1.000 14.11995 ? 63  TRP A CZ3 1 
ATOM   534  C CH2 . TRP A 1 63  ? -0.52834  20.90887 30.76094 1.000 13.05594 ? 63  TRP A CH2 1 
ATOM   535  N N   . CYS A 1 64  ? 4.10768   14.43729 28.77552 1.000 9.91059  ? 64  CYS A N   1 
ATOM   536  C CA  . CYS A 1 64  ? 4.24149   13.03025 28.43863 1.000 9.59034  ? 64  CYS A CA  1 
ATOM   537  C C   . CYS A 1 64  ? 5.54258   12.51320 29.02439 1.000 8.67978  ? 64  CYS A C   1 
ATOM   538  O O   . CYS A 1 64  ? 6.43373   13.28616 29.38810 1.000 11.13580 ? 64  CYS A O   1 
ATOM   539  C CB  . CYS A 1 64  ? 4.17512   12.79210 26.92567 1.000 9.67190  ? 64  CYS A CB  1 
ATOM   540  S SG  . CYS A 1 64  ? 5.46998   13.62590 25.98329 1.000 9.14656  ? 64  CYS A SG  1 
ATOM   541  N N   . ASN A 1 65  ? 5.64650   11.19220 29.12549 1.000 9.57901  ? 65  ASN A N   1 
ATOM   542  C CA  . ASN A 1 65  ? 6.85057   10.57116 29.65228 1.000 9.86397  ? 65  ASN A CA  1 
ATOM   543  C C   . ASN A 1 65  ? 7.69526   10.02897 28.51114 1.000 8.45029  ? 65  ASN A C   1 
ATOM   544  O O   . ASN A 1 65  ? 7.22701   9.18993  27.73233 1.000 8.56317  ? 65  ASN A O   1 
ATOM   545  C CB  . ASN A 1 65  ? 6.54969   9.43528  30.62046 1.000 10.46380 ? 65  ASN A CB  1 
ATOM   546  C CG  . ASN A 1 65  ? 7.81774   8.72922  31.04924 1.000 10.99011 ? 65  ASN A CG  1 
ATOM   547  O OD1 . ASN A 1 65  ? 8.72691   9.36320  31.58997 1.000 13.64178 ? 65  ASN A OD1 1 
ATOM   548  N ND2 . ASN A 1 65  ? 7.92256   7.44018  30.74835 1.000 15.63297 ? 65  ASN A ND2 1 
ATOM   549  N N   . ASP A 1 66  ? 8.94128   10.48886 28.43181 1.000 8.70093  ? 66  ASP A N   1 
ATOM   550  C CA  . ASP A 1 66  ? 9.91302   9.90169  27.52465 1.000 9.70742  ? 66  ASP A CA  1 
ATOM   551  C C   . ASP A 1 66  ? 11.10414  9.27667  28.23944 1.000 12.04314 ? 66  ASP A C   1 
ATOM   552  O O   . ASP A 1 66  ? 12.03395  8.80953  27.57027 1.000 12.54051 ? 66  ASP A O   1 
ATOM   553  C CB  . ASP A 1 66  ? 10.35386  10.89755 26.43445 1.000 8.74236  ? 66  ASP A CB  1 
ATOM   554  C CG  . ASP A 1 66  ? 11.15108  12.08654 26.97415 1.000 8.71772  ? 66  ASP A CG  1 
ATOM   555  O OD1 . ASP A 1 66  ? 11.53235  12.11463 28.17206 1.000 8.70456  ? 66  ASP A OD1 1 
ATOM   556  O OD2 . ASP A 1 66  ? 11.40797  13.00444 26.16600 1.000 8.53092  ? 66  ASP A OD2 1 
ATOM   557  N N   . GLY A 1 67  ? 11.09844  9.25180  29.57144 1.000 11.45321 ? 67  GLY A N   1 
ATOM   558  C CA  . GLY A 1 67  ? 12.14156  8.61179  30.34327 1.000 12.89278 ? 67  GLY A CA  1 
ATOM   559  C C   . GLY A 1 67  ? 13.46563  9.33269  30.36089 1.000 12.97598 ? 67  GLY A C   1 
ATOM   560  O O   . GLY A 1 67  ? 14.41872  8.82267  30.96072 1.000 15.36838 ? 67  GLY A O   1 
ATOM   561  N N   . ARG A 1 68  ? 13.56758  10.49862 29.72175 1.000 9.57897  ? 68  ARG A N   1 
ATOM   562  C CA  . ARG A 1 68  ? 14.85261  11.17650 29.62139 1.000 10.09898 ? 68  ARG A CA  1 
ATOM   563  C C   . ARG A 1 68  ? 14.72878  12.67654 29.85827 1.000 12.82353 ? 68  ARG A C   1 
ATOM   564  O O   . ARG A 1 68  ? 15.55874  13.45142 29.37300 1.000 14.58360 ? 68  ARG A O   1 
ATOM   565  C CB  . ARG A 1 68  ? 15.52528  10.90331 28.27426 1.000 10.78758 ? 68  ARG A CB  1 
ATOM   566  C CG  . ARG A 1 68  ? 14.76705  11.44025 27.07038 1.000 11.96633 ? 68  ARG A CG  1 
ATOM   567  C CD  . ARG A 1 68  ? 15.67877  11.46806 25.86117 1.000 13.37616 ? 68  ARG A CD  1 
ATOM   568  N NE  . ARG A 1 68  ? 15.30763  12.46999 24.86916 1.000 21.65846 ? 68  ARG A NE  1 
ATOM   569  C CZ  . ARG A 1 68  ? 15.74534  12.45283 23.61306 1.000 19.15642 ? 68  ARG A CZ  1 
ATOM   570  N NH1 . ARG A 1 68  ? 15.37422  13.38877 22.74705 1.000 14.80215 ? 68  ARG A NH1 1 
ATOM   571  N NH2 . ARG A 1 68  ? 16.56317  11.48772 23.22297 1.000 19.97642 ? 68  ARG A NH2 1 
ATOM   572  N N   . THR A 1 69  ? 13.70899  13.10669 30.60046 1.000 11.46212 ? 69  THR A N   1 
ATOM   573  C CA  . THR A 1 69  ? 13.52918  14.51474 30.94736 1.000 12.05456 ? 69  THR A CA  1 
ATOM   574  C C   . THR A 1 69  ? 13.51154  14.62489 32.46635 1.000 10.96711 ? 69  THR A C   1 
ATOM   575  O O   . THR A 1 69  ? 12.44068  14.57404 33.09160 1.000 12.30892 ? 69  THR A O   1 
ATOM   576  C CB  . THR A 1 69  ? 12.24909  15.07478 30.32960 1.000 12.09767 ? 69  THR A CB  1 
ATOM   577  O OG1 . THR A 1 69  ? 12.18274  14.68765 28.94965 1.000 11.38223 ? 69  THR A OG1 1 
ATOM   578  C CG2 . THR A 1 69  ? 12.24123  16.59379 30.41845 1.000 13.74352 ? 69  THR A CG2 1 
ATOM   579  N N   . PRO A 1 70  ? 14.67570  14.77986 33.09507 1.000 12.58028 ? 70  PRO A N   1 
ATOM   580  C CA  . PRO A 1 70  ? 14.73403  14.78900 34.56306 1.000 13.49918 ? 70  PRO A CA  1 
ATOM   581  C C   . PRO A 1 70  ? 13.82026  15.83014 35.18916 1.000 19.44329 ? 70  PRO A C   1 
ATOM   582  O O   . PRO A 1 70  ? 13.73725  16.97410 34.73507 1.000 21.00496 ? 70  PRO A O   1 
ATOM   583  C CB  . PRO A 1 70  ? 16.20612  15.10391 34.84569 1.000 19.60445 ? 70  PRO A CB  1 
ATOM   584  C CG  . PRO A 1 70  ? 16.92681  14.50274 33.68458 1.000 17.18526 ? 70  PRO A CG  1 
ATOM   585  C CD  . PRO A 1 70  ? 16.01855  14.71469 32.49177 1.000 17.76593 ? 70  PRO A CD  1 
ATOM   586  N N   . GLY A 1 71  ? 13.13647  15.41430 36.25436 1.000 16.63018 ? 71  GLY A N   1 
ATOM   587  C CA  . GLY A 1 71  ? 12.26171  16.28845 37.00447 1.000 19.49667 ? 71  GLY A CA  1 
ATOM   588  C C   . GLY A 1 71  ? 10.94759  16.59249 36.33974 1.000 19.51384 ? 71  GLY A C   1 
ATOM   589  O O   . GLY A 1 71  ? 10.17677  17.40061 36.86984 1.000 23.30893 ? 71  GLY A O   1 
ATOM   590  N N   . SER A 1 72  ? 10.66227  15.97540 35.19887 1.000 17.10019 ? 72  SER A N   1 
ATOM   591  C CA  . SER A 1 72  ? 9.47213   16.29442 34.44011 1.000 18.82039 ? 72  SER A CA  1 
ATOM   592  C C   . SER A 1 72  ? 8.26120   15.56358 35.00946 1.000 22.02227 ? 72  SER A C   1 
ATOM   593  O O   . SER A 1 72  ? 8.37031   14.65165 35.83553 1.000 21.44892 ? 72  SER A O   1 
ATOM   594  C CB  . SER A 1 72  ? 9.66676   15.91626 32.97510 1.000 18.96854 ? 72  SER A CB  1 
ATOM   595  O OG  . SER A 1 72  ? 9.68561   14.50824 32.81424 1.000 19.13899 ? 72  SER A OG  1 
ATOM   596  N N   . ARG A 1 73  ? 7.08913   15.98362 34.55069 1.000 16.01929 ? 73  ARG A N   1 
ATOM   597  C CA  . ARG A 1 73  ? 5.82914   15.32276 34.84004 1.000 16.21467 ? 73  ARG A CA  1 
ATOM   598  C C   . ARG A 1 73  ? 5.28980   14.68367 33.56623 1.000 15.51147 ? 73  ARG A C   1 
ATOM   599  O O   . ARG A 1 73  ? 5.85056   14.83652 32.47608 1.000 17.25060 ? 73  ARG A O   1 
ATOM   600  C CB  . ARG A 1 73  ? 4.81635   16.32390 35.40917 1.000 17.16088 ? 73  ARG A CB  1 
ATOM   601  C CG  . ARG A 1 73  ? 5.34869   17.12097 36.59297 1.000 16.97369 ? 73  ARG A CG  1 
ATOM   602  C CD  . ARG A 1 73  ? 5.31091   16.29110 37.86706 1.000 20.58762 ? 73  ARG A CD  1 
ATOM   603  N NE  . ARG A 1 73  ? 3.94995   15.88524 38.20341 1.000 25.56896 ? 73  ARG A NE  1 
ATOM   604  C CZ  . ARG A 1 73  ? 3.09817   16.63838 38.89153 1.000 26.91420 ? 73  ARG A CZ  1 
ATOM   605  N NH1 . ARG A 1 73  ? 1.87720   16.19451 39.15086 1.000 32.78491 ? 73  ARG A NH1 1 
ATOM   606  N NH2 . ARG A 1 73  ? 3.47137   17.83440 39.32633 1.000 27.35981 ? 73  ARG A NH2 1 
ATOM   607  N N   . ASN A 1 74  ? 4.17577   13.95778 33.72255 1.000 15.49579 ? 74  ASN A N   1 
ATOM   608  C CA  . ASN A 1 74  ? 3.52346   13.22272 32.63978 1.000 12.35883 ? 74  ASN A CA  1 
ATOM   609  C C   . ASN A 1 74  ? 2.01552   13.44086 32.80510 1.000 11.72656 ? 74  ASN A C   1 
ATOM   610  O O   . ASN A 1 74  ? 1.24051   12.52695 33.06737 1.000 13.07052 ? 74  ASN A O   1 
ATOM   611  C CB  . ASN A 1 74  ? 3.89635   11.73570 32.67884 1.000 13.10968 ? 74  ASN A CB  1 
ATOM   612  C CG  . ASN A 1 74  ? 3.17604   10.90965 31.61709 1.000 12.65335 ? 74  ASN A CG  1 
ATOM   613  O OD1 . ASN A 1 74  ? 2.57887   11.44561 30.68617 1.000 13.01907 ? 74  ASN A OD1 1 
ATOM   614  N ND2 . ASN A 1 74  ? 3.23497   9.58666  31.76121 1.000 14.93364 ? 74  ASN A ND2 1 
ATOM   615  N N   . LEU A 1 75  ? 1.58558   14.69388 32.63807 1.000 11.85343 ? 75  LEU A N   1 
ATOM   616  C CA  . LEU A 1 75  ? 0.22270   15.06303 33.01135 1.000 15.97710 ? 75  LEU A CA  1 
ATOM   617  C C   . LEU A 1 75  ? -0.83256  14.49102 32.07565 1.000 15.44761 ? 75  LEU A C   1 
ATOM   618  O O   . LEU A 1 75  ? -1.99748  14.37516 32.47392 1.000 16.81095 ? 75  LEU A O   1 
ATOM   619  C CB  . LEU A 1 75  ? 0.08984   16.57805 33.10623 1.000 14.58607 ? 75  LEU A CB  1 
ATOM   620  C CG  . LEU A 1 75  ? 0.93715   17.17909 34.22197 1.000 16.81894 ? 75  LEU A CG  1 
ATOM   621  C CD1 . LEU A 1 75  ? 0.99623   18.68007 34.06581 1.000 19.06329 ? 75  LEU A CD1 1 
ATOM   622  C CD2 . LEU A 1 75  ? 0.39843   16.77527 35.59314 1.000 21.24932 ? 75  LEU A CD2 1 
ATOM   623  N N   . CYS A 1 76  ? -0.46887  14.13187 30.84860 1.000 12.62671 ? 76  CYS A N   1 
ATOM   624  C CA  . CYS A 1 76  ? -1.41613  13.47086 29.96388 1.000 14.04559 ? 76  CYS A CA  1 
ATOM   625  C C   . CYS A 1 76  ? -1.41221  11.95988 30.13903 1.000 12.21424 ? 76  CYS A C   1 
ATOM   626  O O   . CYS A 1 76  ? -2.18042  11.26587 29.46228 1.000 15.58481 ? 76  CYS A O   1 
ATOM   627  C CB  . CYS A 1 76  ? -1.14043  13.85169 28.50378 1.000 12.34002 ? 76  CYS A CB  1 
ATOM   628  S SG  . CYS A 1 76  ? -1.43036  15.60768 28.19667 1.000 11.80848 ? 76  CYS A SG  1 
ATOM   629  N N   . ASN A 1 77  ? -0.56005  11.44090 31.03189 1.000 13.29626 ? 77  ASN A N   1 
ATOM   630  C CA  . ASN A 1 77  ? -0.51009  10.01192 31.35702 1.000 13.99214 ? 77  ASN A CA  1 
ATOM   631  C C   . ASN A 1 77  ? -0.29844  9.15178  30.11206 1.000 13.73816 ? 77  ASN A C   1 
ATOM   632  O O   . ASN A 1 77  ? -1.00458  8.16682  29.88132 1.000 17.40258 ? 77  ASN A O   1 
ATOM   633  C CB  . ASN A 1 77  ? -1.74094  9.57310  32.15535 1.000 18.27977 ? 77  ASN A CB  1 
ATOM   634  C CG  . ASN A 1 77  ? -1.97059  10.43624 33.38131 1.000 26.31340 ? 77  ASN A CG  1 
ATOM   635  O OD1 . ASN A 1 77  ? -1.16138  10.44227 34.30813 1.000 34.03610 ? 77  ASN A OD1 1 
ATOM   636  N ND2 . ASN A 1 77  ? -3.07653  11.17634 33.39049 1.000 30.67401 ? 77  ASN A ND2 1 
ATOM   637  N N   . ILE A 1 78  ? 0.69340   9.52962  29.31079 1.000 12.39597 ? 78  ILE A N   1 
ATOM   638  C CA  . ILE A 1 78  ? 0.98706   8.82447  28.05980 1.000 11.63780 ? 78  ILE A CA  1 
ATOM   639  C C   . ILE A 1 78  ? 2.48901   8.81433  27.83245 1.000 10.98327 ? 78  ILE A C   1 
ATOM   640  O O   . ILE A 1 78  ? 3.20617   9.74431  28.20920 1.000 10.64324 ? 78  ILE A O   1 
ATOM   641  C CB  . ILE A 1 78  ? 0.30584   9.49941  26.84588 1.000 11.39548 ? 78  ILE A CB  1 
ATOM   642  C CG1 . ILE A 1 78  ? 0.52297   11.01239 26.89268 1.000 12.43285 ? 78  ILE A CG1 1 
ATOM   643  C CG2 . ILE A 1 78  ? -1.16621  9.13852  26.77426 1.000 16.79939 ? 78  ILE A CG2 1 
ATOM   644  C CD1 . ILE A 1 78  ? 0.32072   11.70028 25.55566 1.000 16.29949 ? 78  ILE A CD1 1 
ATOM   645  N N   . PRO A 1 79  ? 2.97777   7.76222  27.18245 1.000 12.51946 ? 79  PRO A N   1 
ATOM   646  C CA  . PRO A 1 79  ? 4.34466   7.82906  26.65113 1.000 10.68455 ? 79  PRO A CA  1 
ATOM   647  C C   . PRO A 1 79  ? 4.38048   8.83994  25.52102 1.000 8.96314  ? 79  PRO A C   1 
ATOM   648  O O   . PRO A 1 79  ? 3.44131   8.94294  24.72822 1.000 10.45962 ? 79  PRO A O   1 
ATOM   649  C CB  . PRO A 1 79  ? 4.60642   6.40999  26.12621 1.000 13.39956 ? 79  PRO A CB  1 
ATOM   650  C CG  . PRO A 1 79  ? 3.32839   5.65011  26.27958 1.000 21.49085 ? 79  PRO A CG  1 
ATOM   651  C CD  . PRO A 1 79  ? 2.24557   6.57624  26.71273 1.000 14.60692 ? 79  PRO A CD  1 
ATOM   652  N N   . CYS A 1 80  ? 5.47053   9.60785  25.46569 1.000 9.17125  ? 80  CYS A N   1 
ATOM   653  C CA  . CYS A 1 80  ? 5.59237   10.60573 24.41256 1.000 7.46803  ? 80  CYS A CA  1 
ATOM   654  C C   . CYS A 1 80  ? 5.48900   9.96961  23.03165 1.000 10.05167 ? 80  CYS A C   1 
ATOM   655  O O   . CYS A 1 80  ? 5.00284   10.60455 22.08870 1.000 9.97702  ? 80  CYS A O   1 
ATOM   656  C CB  . CYS A 1 80  ? 6.91547   11.35564 24.56519 1.000 7.38341  ? 80  CYS A CB  1 
ATOM   657  S SG  . CYS A 1 80  ? 7.05389   12.34978 26.07506 1.000 8.47486  ? 80  CYS A SG  1 
ATOM   658  N N   . SER A 1 81  ? 5.91787   8.71156  22.90168 1.000 8.68299  ? 81  SER A N   1 
ATOM   659  C CA  . SER A 1 81  ? 5.81352   8.00544  21.62677 1.000 8.67913  ? 81  SER A CA  1 
ATOM   660  C C   . SER A 1 81  ? 4.37640   7.93350  21.11211 1.000 11.24428 ? 81  SER A C   1 
ATOM   661  O O   . SER A 1 81  ? 4.15712   7.94940  19.89616 1.000 13.02358 ? 81  SER A O   1 
ATOM   662  C CB  . SER A 1 81  ? 6.44944   6.62040  21.76277 1.000 12.16988 ? 81  SER A CB  1 
ATOM   663  O OG  . SER A 1 81  ? 5.65256   5.78055  22.58103 1.000 14.04930 ? 81  SER A OG  1 
ATOM   664  N N   . ALA A 1 82  ? 3.38760   7.87367  22.00934 1.000 11.68902 ? 82  ALA A N   1 
ATOM   665  C CA  . ALA A 1 82  ? 1.99250   7.85974  21.57366 1.000 11.49582 ? 82  ALA A CA  1 
ATOM   666  C C   . ALA A 1 82  ? 1.61343   9.12770  20.82162 1.000 15.34184 ? 82  ALA A C   1 
ATOM   667  O O   . ALA A 1 82  ? 0.63625   9.12370  20.06285 1.000 15.38887 ? 82  ALA A O   1 
ATOM   668  C CB  . ALA A 1 82  ? 1.06376   7.66994  22.77489 1.000 15.37974 ? 82  ALA A CB  1 
ATOM   669  N N   . LEU A 1 83  ? 2.35856   10.21066 21.02234 1.000 9.22244  ? 83  LEU A N   1 
ATOM   670  C CA  . LEU A 1 83  ? 2.12050   11.46161 20.31827 1.000 12.30607 ? 83  LEU A CA  1 
ATOM   671  C C   . LEU A 1 83  ? 2.65118   11.45142 18.89215 1.000 11.59632 ? 83  LEU A C   1 
ATOM   672  O O   . LEU A 1 83  ? 2.49110   12.45037 18.18109 1.000 11.79088 ? 83  LEU A O   1 
ATOM   673  C CB  . LEU A 1 83  ? 2.74178   12.61564 21.10202 1.000 12.11899 ? 83  LEU A CB  1 
ATOM   674  C CG  . LEU A 1 83  ? 2.15211   12.83082 22.49713 1.000 13.78069 ? 83  LEU A CG  1 
ATOM   675  C CD1 . LEU A 1 83  ? 2.94837   13.87184 23.26884 1.000 11.65731 ? 83  LEU A CD1 1 
ATOM   676  C CD2 . LEU A 1 83  ? 0.69612   13.24693 22.37642 1.000 15.60564 ? 83  LEU A CD2 1 
ATOM   677  N N   . LEU A 1 84  ? 3.27999   10.36333 18.45212 1.000 11.59678 ? 84  LEU A N   1 
ATOM   678  C CA  . LEU A 1 84  ? 3.82867   10.27415 17.10600 1.000 8.84722  ? 84  LEU A CA  1 
ATOM   679  C C   . LEU A 1 84  ? 3.00139   9.38113  16.19428 1.000 9.84335  ? 84  LEU A C   1 
ATOM   680  O O   . LEU A 1 84  ? 3.38511   9.17598  15.03721 1.000 11.88366 ? 84  LEU A O   1 
ATOM   681  C CB  . LEU A 1 84  ? 5.27364   9.75704  17.14872 1.000 11.95121 ? 84  LEU A CB  1 
ATOM   682  C CG  . LEU A 1 84  ? 6.27490   10.54404 17.99141 1.000 11.23387 ? 84  LEU A CG  1 
ATOM   683  C CD1 . LEU A 1 84  ? 7.66481   9.96591  17.80415 1.000 14.79126 ? 84  LEU A CD1 1 
ATOM   684  C CD2 . LEU A 1 84  ? 6.26493   12.02200 17.62227 1.000 9.84267  ? 84  LEU A CD2 1 
ATOM   685  N N   A SER A 1 85  ? 1.88646   8.85527  16.68459 0.502 13.84843 ? 85  SER A N   1 
ATOM   686  N N   B SER A 1 85  ? 1.88146   8.85426  16.67459 0.498 13.86308 ? 85  SER A N   1 
ATOM   687  C CA  A SER A 1 85  ? 1.08421   7.90826  15.93086 0.502 12.09418 ? 85  SER A CA  1 
ATOM   688  C CA  B SER A 1 85  ? 1.10020   7.90225  15.90086 0.498 12.14706 ? 85  SER A CA  1 
ATOM   689  C C   A SER A 1 85  ? 0.38500   8.59119  14.75896 0.502 13.87580 ? 85  SER A C   1 
ATOM   690  C C   B SER A 1 85  ? 0.40499   8.58119  14.72195 0.498 13.82925 ? 85  SER A C   1 
ATOM   691  O O   A SER A 1 85  ? 0.15410   9.80321  14.74989 0.502 13.35568 ? 85  SER A O   1 
ATOM   692  O O   B SER A 1 85  ? 0.19508   9.79620  14.69788 0.498 13.20810 ? 85  SER A O   1 
ATOM   693  C CB  A SER A 1 85  ? 0.04137   7.26943  16.84717 0.502 13.64591 ? 85  SER A CB  1 
ATOM   694  C CB  B SER A 1 85  ? 0.05235   7.23442  16.79217 0.498 13.71753 ? 85  SER A CB  1 
ATOM   695  O OG  A SER A 1 85  ? -0.91386  6.54143  16.10046 0.502 10.34135 ? 85  SER A OG  1 
ATOM   696  O OG  B SER A 1 85  ? -0.56738  8.18056  17.64422 0.498 17.35232 ? 85  SER A OG  1 
ATOM   697  N N   A SER A 1 86  ? 0.04870   7.78212  13.74911 0.502 13.44758 ? 86  SER A N   1 
ATOM   698  N N   B SER A 1 86  ? 0.04769   7.76412  13.72512 0.498 13.45145 ? 86  SER A N   1 
ATOM   699  C CA  A SER A 1 86  ? -0.75051  8.28708  12.63925 0.502 13.58075 ? 86  SER A CA  1 
ATOM   700  C CA  B SER A 1 86  ? -0.76152  8.26507  12.62025 0.498 13.58950 ? 86  SER A CA  1 
ATOM   701  C C   A SER A 1 86  ? -2.15238  8.66824  13.09353 0.502 16.33871 ? 86  SER A C   1 
ATOM   702  C C   B SER A 1 86  ? -2.15438  8.66323  13.08953 0.498 16.35124 ? 86  SER A C   1 
ATOM   703  O O   A SER A 1 86  ? -2.78544  9.54323  12.49059 0.502 15.01334 ? 86  SER A O   1 
ATOM   704  O O   B SER A 1 86  ? -2.78244  9.54823  12.49359 0.498 14.99641 ? 86  SER A O   1 
ATOM   705  C CB  A SER A 1 86  ? -0.80785  7.24697  11.52136 0.502 16.18369 ? 86  SER A CB  1 
ATOM   706  C CB  B SER A 1 86  ? -0.84786  7.21597  11.51138 0.498 16.19118 ? 86  SER A CB  1 
ATOM   707  O OG  A SER A 1 86  ? 0.43499   7.17580  10.84409 0.502 20.33147 ? 86  SER A OG  1 
ATOM   708  O OG  B SER A 1 86  ? -1.27784  5.96606  12.02060 0.498 14.44088 ? 86  SER A OG  1 
ATOM   709  N N   . ASP A 1 87  ? -2.64719  8.03038  14.14871 1.000 12.22978 ? 87  ASP A N   1 
ATOM   710  C CA  . ASP A 1 87  ? -3.92502  8.37954  14.75096 1.000 13.90442 ? 87  ASP A CA  1 
ATOM   711  C C   . ASP A 1 87  ? -3.66670  9.49262  15.75879 1.000 13.18118 ? 87  ASP A C   1 
ATOM   712  O O   . ASP A 1 87  ? -2.83351  9.33765  16.65762 1.000 12.28431 ? 87  ASP A O   1 
ATOM   713  C CB  . ASP A 1 87  ? -4.49496  7.14966  15.45622 1.000 19.41120 ? 87  ASP A CB  1 
ATOM   714  C CG  . ASP A 1 87  ? -5.88581  7.37683  16.01051 1.000 27.40139 ? 87  ASP A CG  1 
ATOM   715  O OD1 . ASP A 1 87  ? -6.09357  8.37492  16.72846 1.000 17.43293 ? 87  ASP A OD1 1 
ATOM   716  O OD2 . ASP A 1 87  ? -6.77595  6.54787  15.73180 1.000 28.80871 ? 87  ASP A OD2 1 
ATOM   717  N N   . ILE A 1 88  ? -4.37764  10.60867 15.61484 1.000 13.51453 ? 88  ILE A N   1 
ATOM   718  C CA  . ILE A 1 88  ? -4.05137  11.80572 16.38765 1.000 11.08680 ? 88  ILE A CA  1 
ATOM   719  C C   . ILE A 1 88  ? -4.77606  11.86291 17.72481 1.000 13.24655 ? 88  ILE A C   1 
ATOM   720  O O   . ILE A 1 88  ? -4.70482  12.88397 18.41569 1.000 11.66944 ? 88  ILE A O   1 
ATOM   721  C CB  . ILE A 1 88  ? -4.30245  13.09466 15.57958 1.000 10.09975 ? 88  ILE A CB  1 
ATOM   722  C CG1 . ILE A 1 88  ? -5.80249  13.29975 15.31890 1.000 11.35263 ? 88  ILE A CG1 1 
ATOM   723  C CG2 . ILE A 1 88  ? -3.51575  13.06846 14.27440 1.000 15.85650 ? 88  ILE A CG2 1 
ATOM   724  C CD1 . ILE A 1 88  ? -6.13649  14.69073 14.81184 1.000 10.78086 ? 88  ILE A CD1 1 
ATOM   725  N N   . THR A 1 89  ? -5.45606  10.77400 18.11107 1.000 12.61419 ? 89  THR A N   1 
ATOM   726  C CA  . THR A 1 89  ? -6.27678  10.79119 19.32426 1.000 11.60796 ? 89  THR A CA  1 
ATOM   727  C C   . THR A 1 89  ? -5.47146  11.22225 20.54803 1.000 14.89721 ? 89  THR A C   1 
ATOM   728  O O   . THR A 1 89  ? -5.89122  12.11036 21.29704 1.000 12.38543 ? 89  THR A O   1 
ATOM   729  C CB  . THR A 1 89  ? -6.90684  9.41727  19.56454 1.000 14.08823 ? 89  THR A CB  1 
ATOM   730  O OG1 . THR A 1 89  ? -7.81010  9.10923  18.49878 1.000 16.51611 ? 89  THR A OG1 1 
ATOM   731  C CG2 . THR A 1 89  ? -7.67053  9.40146  20.88572 1.000 19.31279 ? 89  THR A CG2 1 
ATOM   732  N N   . ALA A 1 90  ? -4.30946  10.60018 20.76983 1.000 11.54931 ? 90  ALA A N   1 
ATOM   733  C CA  . ALA A 1 90  ? -3.52017  10.93723 21.95162 1.000 12.31046 ? 90  ALA A CA  1 
ATOM   734  C C   . ALA A 1 90  ? -3.08705  12.39619 21.92837 1.000 12.29148 ? 90  ALA A C   1 
ATOM   735  O O   . ALA A 1 90  ? -3.14476  13.08530 22.95432 1.000 11.82959 ? 90  ALA A O   1 
ATOM   736  C CB  . ALA A 1 90  ? -2.30822  10.01214 22.06543 1.000 13.62224 ? 90  ALA A CB  1 
ATOM   737  N N   . SER A 1 91  ? -2.66228  12.89104 20.76322 1.000 9.78727  ? 91  SER A N   1 
ATOM   738  C CA  . SER A 1 91  ? -2.23619  14.28300 20.66999 1.000 9.82497  ? 91  SER A CA  1 
ATOM   739  C C   . SER A 1 91  ? -3.39705  15.23212 20.93516 1.000 10.02156 ? 91  SER A C   1 
ATOM   740  O O   . SER A 1 91  ? -3.23481  16.25017 21.62002 1.000 10.18916 ? 91  SER A O   1 
ATOM   741  C CB  . SER A 1 91  ? -1.62548  14.54881 19.29182 1.000 13.08234 ? 91  SER A CB  1 
ATOM   742  O OG  . SER A 1 91  ? -0.25852  14.16170 19.25555 1.000 10.06849 ? 91  SER A OG  1 
ATOM   743  N N   . VAL A 1 92  ? -4.57820  14.91616 20.40346 1.000 11.41952 ? 92  VAL A N   1 
ATOM   744  C CA  . VAL A 1 92  ? -5.74108  15.77128 20.62364 1.000 10.46674 ? 92  VAL A CA  1 
ATOM   745  C C   . VAL A 1 92  ? -6.13774  15.76746 22.09473 1.000 13.56660 ? 92  VAL A C   1 
ATOM   746  O O   . VAL A 1 92  ? -6.37652  16.82554 22.69368 1.000 11.82294 ? 92  VAL A O   1 
ATOM   747  C CB  . VAL A 1 92  ? -6.90532  15.34228 19.71295 1.000 11.06504 ? 92  VAL A CB  1 
ATOM   748  C CG1 . VAL A 1 92  ? -8.18817  16.03243 20.14117 1.000 13.13955 ? 92  VAL A CG1 1 
ATOM   749  C CG2 . VAL A 1 92  ? -6.58162  15.67011 18.26584 1.000 13.34857 ? 92  VAL A CG2 1 
ATOM   750  N N   . ASN A 1 93  ? -6.21870  14.58052 22.70187 1.000 10.62403 ? 93  ASN A N   1 
ATOM   751  C CA  . ASN A 1 93  ? -6.62538  14.50470 24.10297 1.000 11.09840 ? 93  ASN A CA  1 
ATOM   752  C C   . ASN A 1 93  ? -5.65812  15.25871 25.00267 1.000 12.77797 ? 93  ASN A C   1 
ATOM   753  O O   . ASN A 1 93  ? -6.07184  15.92984 25.95670 1.000 13.02633 ? 93  ASN A O   1 
ATOM   754  C CB  . ASN A 1 93  ? -6.73440  13.04675 24.54514 1.000 17.73869 ? 93  ASN A CB  1 
ATOM   755  C CG  . ASN A 1 93  ? -7.94059  12.34979 23.95049 1.000 21.96223 ? 93  ASN A CG  1 
ATOM   756  O OD1 . ASN A 1 93  ? -8.79868  12.98580 23.33662 1.000 26.11400 ? 93  ASN A OD1 1 
ATOM   757  N ND2 . ASN A 1 93  ? -8.01066  11.03481 24.12563 1.000 24.98366 ? 93  ASN A ND2 1 
ATOM   758  N N   . CYS A 1 94  ? -4.36119  15.14957 24.71839 1.000 10.11431 ? 94  CYS A N   1 
ATOM   759  C CA  . CYS A 1 94  ? -3.37595  15.86057 25.52109 1.000 10.13435 ? 94  CYS A CA  1 
ATOM   760  C C   . CYS A 1 94  ? -3.43289  17.36255 25.25995 1.000 11.26153 ? 94  CYS A C   1 
ATOM   761  O O   . CYS A 1 94  ? -3.33861  18.16664 26.19685 1.000 10.56634 ? 94  CYS A O   1 
ATOM   762  C CB  . CYS A 1 94  ? -1.97806  15.30443 25.23983 1.000 11.33508 ? 94  CYS A CB  1 
ATOM   763  S SG  . CYS A 1 94  ? -0.69976  15.92844 26.33547 1.000 11.04827 ? 94  CYS A SG  1 
ATOM   764  N N   . ALA A 1 95  ? -3.60014  17.75944 23.99295 1.000 10.86091 ? 95  ALA A N   1 
ATOM   765  C CA  . ALA A 1 95  ? -3.73810  19.17742 23.67384 1.000 8.80896  ? 95  ALA A CA  1 
ATOM   766  C C   . ALA A 1 95  ? -4.94089  19.80159 24.36906 1.000 9.78341  ? 95  ALA A C   1 
ATOM   767  O O   . ALA A 1 95  ? -4.89571  20.97662 24.74493 1.000 11.21708 ? 95  ALA A O   1 
ATOM   768  C CB  . ALA A 1 95  ? -3.83543  19.37828 22.16085 1.000 10.08063 ? 95  ALA A CB  1 
ATOM   769  N N   . LYS A 1 96  ? -6.02591  19.04269 24.54538 1.000 8.55703  ? 96  LYS A N   1 
ATOM   770  C CA  . LYS A 1 96  ? -7.16470  19.56586 25.29659 1.000 8.36104  ? 96  LYS A CA  1 
ATOM   771  C C   . LYS A 1 96  ? -6.77034  19.90297 26.72946 1.000 9.03930  ? 96  LYS A C   1 
ATOM   772  O O   . LYS A 1 96  ? -7.20814  20.92106 27.27846 1.000 13.19845 ? 96  LYS A O   1 
ATOM   773  C CB  . LYS A 1 96  ? -8.31479  18.55895 25.27095 1.000 12.24546 ? 96  LYS A CB  1 
ATOM   774  C CG  . LYS A 1 96  ? -9.05009  18.51588 23.94612 1.000 13.72248 ? 96  LYS A CG  1 
ATOM   775  C CD  . LYS A 1 96  ? -10.06819 17.39696 23.92147 1.000 14.64345 ? 96  LYS A CD  1 
ATOM   776  C CE  . LYS A 1 96  ? -10.82449 17.38089 22.60164 1.000 16.47837 ? 96  LYS A CE  1 
ATOM   777  N NZ  . LYS A 1 96  ? -11.78260 16.24296 22.52798 1.000 21.78137 ? 96  LYS A NZ  1 
ATOM   778  N N   . LYS A 1 97  ? -5.94627  19.05997 27.35436 1.000 9.42410  ? 97  LYS A N   1 
ATOM   779  C CA  . LYS A 1 97  ? -5.48194  19.36606 28.70522 1.000 9.46397  ? 97  LYS A CA  1 
ATOM   780  C C   . LYS A 1 97  ? -4.58284  20.59499 28.70690 1.000 12.32297 ? 97  LYS A C   1 
ATOM   781  O O   . LYS A 1 97  ? -4.69556  21.45709 29.58784 1.000 11.79352 ? 97  LYS A O   1 
ATOM   782  C CB  . LYS A 1 97  ? -4.74390  18.15606 29.28218 1.000 13.19393 ? 97  LYS A CB  1 
ATOM   783  C CG  . LYS A 1 97  ? -4.71356  18.10621 30.80117 1.000 27.86354 ? 97  LYS A CG  1 
ATOM   784  C CD  . LYS A 1 97  ? -4.13155  16.78821 31.29917 1.000 27.70733 ? 97  LYS A CD  1 
ATOM   785  C CE  . LYS A 1 97  ? -5.21360  15.72832 31.46153 1.000 44.26017 ? 97  LYS A CE  1 
ATOM   786  N NZ  . LYS A 1 97  ? -4.66475  14.35226 31.30454 1.000 49.44031 ? 97  LYS A NZ  1 
ATOM   787  N N   . ILE A 1 98  ? -3.69405  20.69982 27.71568 1.000 8.81736  ? 98  ILE A N   1 
ATOM   788  C CA  . ILE A 1 98  ? -2.75297  21.81774 27.66235 1.000 8.63480  ? 98  ILE A CA  1 
ATOM   789  C C   . ILE A 1 98  ? -3.49590  23.13678 27.50539 1.000 10.88992 ? 98  ILE A C   1 
ATOM   790  O O   . ILE A 1 98  ? -3.24066  24.10583 28.22824 1.000 10.45846 ? 98  ILE A O   1 
ATOM   791  C CB  . ILE A 1 98  ? -1.73525  21.60754 26.52814 1.000 10.53368 ? 98  ILE A CB  1 
ATOM   792  C CG1 . ILE A 1 98  ? -0.90930  20.34750 26.78108 1.000 10.13043 ? 98  ILE A CG1 1 
ATOM   793  C CG2 . ILE A 1 98  ? -0.84319  22.83245 26.37782 1.000 12.81336 ? 98  ILE A CG2 1 
ATOM   794  C CD1 . ILE A 1 98  ? -0.03760  19.95031 25.60692 1.000 11.21945 ? 98  ILE A CD1 1 
ATOM   795  N N   . VAL A 1 99  ? -4.40812  23.20276 26.53360 1.000 9.65091  ? 99  VAL A N   1 
ATOM   796  C CA  . VAL A 1 99  ? -5.12908  24.43979 26.26464 1.000 11.26869 ? 99  VAL A CA  1 
ATOM   797  C C   . VAL A 1 99  ? -6.06479  24.83298 27.39781 1.000 12.87378 ? 99  VAL A C   1 
ATOM   798  O O   . VAL A 1 99  ? -6.51469  25.98502 27.44680 1.000 12.68736 ? 99  VAL A O   1 
ATOM   799  C CB  . VAL A 1 99  ? -5.83440  24.33271 24.89581 1.000 10.05691 ? 99  VAL A CB  1 
ATOM   800  C CG1 . VAL A 1 99  ? -7.06545  23.43682 24.99818 1.000 9.73255  ? 99  VAL A CG1 1 
ATOM   801  C CG2 . VAL A 1 99  ? -6.18642  25.70969 24.34675 1.000 10.88476 ? 99  VAL A CG2 1 
ATOM   802  N N   . SER A 1 100 ? -6.36066  23.90910 28.31197 1.000 13.64034 ? 100 SER A N   1 
ATOM   803  C CA  . SER A 1 100 ? -7.17236  24.18628 29.49113 1.000 12.81668 ? 100 SER A CA  1 
ATOM   804  C C   . SER A 1 100 ? -6.34705  24.61633 30.69790 1.000 13.94711 ? 100 SER A C   1 
ATOM   805  O O   . SER A 1 100 ? -6.92079  24.87849 31.75900 1.000 18.71635 ? 100 SER A O   1 
ATOM   806  C CB  . SER A 1 100 ? -8.00338  22.95238 29.86644 1.000 12.72497 ? 100 SER A CB  1 
ATOM   807  O OG  . SER A 1 100 ? -8.82766  22.52135 28.79767 1.000 14.24548 ? 100 SER A OG  1 
ATOM   808  N N   . ASP A 1 101 ? -5.02408  24.70021 30.56559 1.000 14.29678 ? 101 ASP A N   1 
ATOM   809  C CA  . ASP A 1 101 ? -4.14780  24.87626 31.71937 1.000 13.89468 ? 101 ASP A CA  1 
ATOM   810  C C   . ASP A 1 101 ? -4.11456  26.30631 32.24322 1.000 19.79298 ? 101 ASP A C   1 
ATOM   811  O O   . ASP A 1 101 ? -3.56630  26.53337 33.32607 1.000 21.18873 ? 101 ASP A O   1 
ATOM   812  C CB  . ASP A 1 101 ? -2.72891  24.39511 31.38409 1.000 18.14140 ? 101 ASP A CB  1 
ATOM   813  C CG  . ASP A 1 101 ? -1.88265  24.14116 32.62292 1.000 27.16419 ? 101 ASP A CG  1 
ATOM   814  O OD1 . ASP A 1 101 ? -0.77359  24.70808 32.71061 1.000 33.19293 ? 101 ASP A OD1 1 
ATOM   815  O OD2 . ASP A 1 101 ? -2.32751  23.37529 33.50510 1.000 30.74421 ? 101 ASP A OD2 1 
ATOM   816  N N   . GLY A 1 102 ? -4.67965  27.26928 31.51725 1.000 16.02838 ? 102 GLY A N   1 
ATOM   817  C CA  . GLY A 1 102 ? -4.72443  28.63533 32.00513 1.000 17.26668 ? 102 GLY A CA  1 
ATOM   818  C C   . GLY A 1 102 ? -4.36058  29.69220 30.97794 1.000 15.15951 ? 102 GLY A C   1 
ATOM   819  O O   . GLY A 1 102 ? -4.91348  30.79525 30.99795 1.000 16.45880 ? 102 GLY A O   1 
ATOM   820  N N   . ASN A 1 103 ? -3.43381  29.37803 30.07576 1.000 12.88599 ? 103 ASN A N   1 
ATOM   821  C CA  . ASN A 1 103 ? -2.95295  30.35190 29.10355 1.000 10.96541 ? 103 ASN A CA  1 
ATOM   822  C C   . ASN A 1 103 ? -3.48629  30.09680 27.70170 1.000 11.13868 ? 103 ASN A C   1 
ATOM   823  O O   . ASN A 1 103 ? -3.02246  30.73067 26.74653 1.000 10.24161 ? 103 ASN A O   1 
ATOM   824  C CB  . ASN A 1 103 ? -1.42494  30.40577 29.11119 1.000 16.08924 ? 103 ASN A CB  1 
ATOM   825  C CG  . ASN A 1 103 ? -0.87760  30.87786 30.44002 1.000 21.22158 ? 103 ASN A CG  1 
ATOM   826  O OD1 . ASN A 1 103 ? -0.08751  30.18386 31.08291 1.000 31.32369 ? 103 ASN A OD1 1 
ATOM   827  N ND2 . ASN A 1 103 ? -1.31141  32.05294 30.87000 1.000 22.28319 ? 103 ASN A ND2 1 
ATOM   828  N N   . GLY A 1 104 ? -4.45940  29.20287 27.56201 1.000 9.15961  ? 104 GLY A N   1 
ATOM   829  C CA  . GLY A 1 104 ? -5.04472  28.94578 26.26017 1.000 8.43270  ? 104 GLY A CA  1 
ATOM   830  C C   . GLY A 1 104 ? -3.99698  28.44560 25.28798 1.000 9.14647  ? 104 GLY A C   1 
ATOM   831  O O   . GLY A 1 104 ? -3.08996  27.68556 25.64085 1.000 10.38519 ? 104 GLY A O   1 
ATOM   832  N N   . MET A 1 105 ? -4.09923  28.89349 24.04296 1.000 7.93372  ? 105 MET A N   1 
ATOM   833  C CA  . MET A 1 105 ? -3.16750  28.40231 23.04079 1.000 8.09572  ? 105 MET A CA  1 
ATOM   834  C C   . MET A 1 105 ? -1.80343  29.07921 23.10641 1.000 9.72113  ? 105 MET A C   1 
ATOM   835  O O   . MET A 1 105 ? -0.89663  28.67606 22.37125 1.000 8.69079  ? 105 MET A O   1 
ATOM   836  C CB  . MET A 1 105 ? -3.78181  28.48822 21.64192 1.000 7.87544  ? 105 MET A CB  1 
ATOM   837  C CG  . MET A 1 105 ? -4.79796  27.38528 21.37727 1.000 10.39153 ? 105 MET A CG  1 
ATOM   838  S SD  . MET A 1 105 ? -5.26737  27.20714 19.64839 1.000 8.90146  ? 105 MET A SD  1 
ATOM   839  C CE  . MET A 1 105 ? -3.81459  26.37696 18.99314 1.000 9.24094  ? 105 MET A CE  1 
ATOM   840  N N   . ASN A 1 106 ? -1.62414  30.07128 23.98627 1.000 8.47743  ? 106 ASN A N   1 
ATOM   841  C CA  . ASN A 1 106 ? -0.30605  30.67019 24.16891 1.000 8.16157  ? 106 ASN A CA  1 
ATOM   842  C C   . ASN A 1 106 ? 0.72497   29.65215 24.64078 1.000 9.02393  ? 106 ASN A C   1 
ATOM   843  O O   . ASN A 1 106 ? 1.92597   29.91705 24.53848 1.000 12.36498 ? 106 ASN A O   1 
ATOM   844  C CB  . ASN A 1 106 ? -0.37173  31.84129 25.15081 1.000 10.24447 ? 106 ASN A CB  1 
ATOM   845  C CG  . ASN A 1 106 ? -1.20576  32.99031 24.62789 1.000 11.16279 ? 106 ASN A CG  1 
ATOM   846  O OD1 . ASN A 1 106 ? -0.84593  33.63518 23.64074 1.000 13.24075 ? 106 ASN A OD1 1 
ATOM   847  N ND2 . ASN A 1 106 ? -2.33059  33.25247 25.28512 1.000 12.28007 ? 106 ASN A ND2 1 
ATOM   848  N N   . ALA A 1 107 ? 0.28100   28.49924 25.15899 1.000 9.72911  ? 107 ALA A N   1 
ATOM   849  C CA  . ALA A 1 107 ? 1.21399   27.43120 25.50889 1.000 9.83674  ? 107 ALA A CA  1 
ATOM   850  C C   . ALA A 1 107 ? 2.02868   26.98401 24.30375 1.000 12.37500 ? 107 ALA A C   1 
ATOM   851  O O   . ALA A 1 107 ? 3.15367   26.49994 24.46054 1.000 15.73393 ? 107 ALA A O   1 
ATOM   852  C CB  . ALA A 1 107 ? 0.45803   26.24432 26.10618 1.000 13.81482 ? 107 ALA A CB  1 
ATOM   853  N N   . TRP A 1 108 ? 1.47841   27.11894 23.10086 1.000 9.04383  ? 108 TRP A N   1 
ATOM   854  C CA  . TRP A 1 108 ? 2.22011   26.85076 21.87172 1.000 9.12600  ? 108 TRP A CA  1 
ATOM   855  C C   . TRP A 1 108 ? 2.82811   28.16866 21.41544 1.000 11.18472 ? 108 TRP A C   1 
ATOM   856  O O   . TRP A 1 108 ? 2.13606   29.02266 20.85752 1.000 11.56469 ? 108 TRP A O   1 
ATOM   857  C CB  . TRP A 1 108 ? 1.29782   26.27072 20.80598 1.000 11.71273 ? 108 TRP A CB  1 
ATOM   858  C CG  . TRP A 1 108 ? 0.86377   24.86479 21.08822 1.000 11.16765 ? 108 TRP A CG  1 
ATOM   859  C CD1 . TRP A 1 108 ? 1.52960   23.71770 20.75419 1.000 10.38106 ? 108 TRP A CD1 1 
ATOM   860  C CD2 . TRP A 1 108 ? -0.32511  24.45195 21.77454 1.000 10.16890 ? 108 TRP A CD2 1 
ATOM   861  N NE1 . TRP A 1 108 ? 0.82561   22.61880 21.18446 1.000 9.43608  ? 108 TRP A NE1 1 
ATOM   862  C CE2 . TRP A 1 108 ? -0.31321  23.04096 21.81867 1.000 10.33262 ? 108 TRP A CE2 1 
ATOM   863  C CE3 . TRP A 1 108 ? -1.39692  25.13810 22.36171 1.000 9.11569  ? 108 TRP A CE3 1 
ATOM   864  C CZ2 . TRP A 1 108 ? -1.33614  22.30310 22.41198 1.000 9.77643  ? 108 TRP A CZ2 1 
ATOM   865  C CZ3 . TRP A 1 108 ? -2.41384  24.40224 22.95602 1.000 8.97067  ? 108 TRP A CZ3 1 
ATOM   866  C CH2 . TRP A 1 108 ? -2.37095  22.99824 22.98115 1.000 8.82847  ? 108 TRP A CH2 1 
ATOM   867  N N   . VAL A 1 109 ? 4.13018   28.34158 21.65413 1.000 13.01861 ? 109 VAL A N   1 
ATOM   868  C CA  . VAL A 1 109 ? 4.77521   29.60749 21.31486 1.000 12.94892 ? 109 VAL A CA  1 
ATOM   869  C C   . VAL A 1 109 ? 4.66489   29.89835 19.82185 1.000 11.66394 ? 109 VAL A C   1 
ATOM   870  O O   . VAL A 1 109 ? 4.47789   31.05233 19.42278 1.000 13.72316 ? 109 VAL A O   1 
ATOM   871  C CB  . VAL A 1 109 ? 6.22733   29.64843 21.83052 1.000 16.35920 ? 109 VAL A CB  1 
ATOM   872  C CG1 . VAL A 1 109 ? 6.91633   30.93433 21.38923 1.000 22.64871 ? 109 VAL A CG1 1 
ATOM   873  C CG2 . VAL A 1 109 ? 6.24767   29.52758 23.35153 1.000 22.97268 ? 109 VAL A CG2 1 
ATOM   874  N N   . ALA A 1 110 ? 4.73261   28.86326 18.98094 1.000 14.17829 ? 110 ALA A N   1 
ATOM   875  C CA  . ALA A 1 110 ? 4.56030   29.08413 17.54796 1.000 12.74908 ? 110 ALA A CA  1 
ATOM   876  C C   . ALA A 1 110 ? 3.15026   29.55121 17.21023 1.000 12.11219 ? 110 ALA A C   1 
ATOM   877  O O   . ALA A 1 110 ? 2.97011   30.32514 16.26420 1.000 11.31589 ? 110 ALA A O   1 
ATOM   878  C CB  . ALA A 1 110 ? 4.91902   27.82603 16.75700 1.000 14.27758 ? 110 ALA A CB  1 
ATOM   879  N N   . TRP A 1 111 ? 2.13740   29.10337 17.95951 1.000 9.11316  ? 111 TRP A N   1 
ATOM   880  C CA  . TRP A 1 111 ? 0.80040   29.65646 17.75076 1.000 9.18050  ? 111 TRP A CA  1 
ATOM   881  C C   . TRP A 1 111 ? 0.77160   31.13950 18.09562 1.000 9.70000  ? 111 TRP A C   1 
ATOM   882  O O   . TRP A 1 111 ? 0.25349   31.95846 17.32866 1.000 9.44066  ? 111 TRP A O   1 
ATOM   883  C CB  . TRP A 1 111 ? -0.25748  28.89463 18.55708 1.000 11.07489 ? 111 TRP A CB  1 
ATOM   884  C CG  . TRP A 1 111 ? -1.62746  29.53472 18.42833 1.000 8.04832  ? 111 TRP A CG  1 
ATOM   885  C CD1 . TRP A 1 111 ? -2.55270  29.29170 17.45056 1.000 9.42551  ? 111 TRP A CD1 1 
ATOM   886  C CD2 . TRP A 1 111 ? -2.20118  30.54186 19.27836 1.000 7.96858  ? 111 TRP A CD2 1 
ATOM   887  N NE1 . TRP A 1 111 ? -3.66559  30.07381 17.64774 1.000 8.83735  ? 111 TRP A NE1 1 
ATOM   888  C CE2 . TRP A 1 111 ? -3.47428  30.85291 18.75662 1.000 7.68718  ? 111 TRP A CE2 1 
ATOM   889  C CE3 . TRP A 1 111 ? -1.76486  31.20794 20.43219 1.000 9.27315  ? 111 TRP A CE3 1 
ATOM   890  C CZ2 . TRP A 1 111 ? -4.31906  31.79004 19.35072 1.000 10.19099 ? 111 TRP A CZ2 1 
ATOM   891  C CZ3 . TRP A 1 111 ? -2.60365  32.13806 21.02029 1.000 10.57909 ? 111 TRP A CZ3 1 
ATOM   892  C CH2 . TRP A 1 111 ? -3.86676  32.42311 20.47655 1.000 10.05058 ? 111 TRP A CH2 1 
ATOM   893  N N   . ARG A 1 112 ? 1.32189   31.50557 19.25546 1.000 9.52676  ? 112 ARG A N   1 
ATOM   894  C CA  . ARG A 1 112 ? 1.32609   32.91161 19.64231 1.000 9.56791  ? 112 ARG A CA  1 
ATOM   895  C C   . ARG A 1 112 ? 2.07393   33.75844 18.62306 1.000 11.91914 ? 112 ARG A C   1 
ATOM   896  O O   . ARG A 1 112 ? 1.62394   34.84944 18.26205 1.000 11.68212 ? 112 ARG A O   1 
ATOM   897  C CB  . ARG A 1 112 ? 1.93943   33.08569 21.03316 1.000 10.96142 ? 112 ARG A CB  1 
ATOM   898  C CG  . ARG A 1 112 ? 2.04364   34.54273 21.46899 1.000 13.99792 ? 112 ARG A CG  1 
ATOM   899  C CD  . ARG A 1 112 ? 2.49399   34.66984 22.92087 1.000 22.01476 ? 112 ARG A CD  1 
ATOM   900  N NE  . ARG A 1 112 ? 3.77498   34.00576 23.14165 1.000 26.64314 ? 112 ARG A NE  1 
ATOM   901  C CZ  . ARG A 1 112 ? 4.95596   34.54063 22.84532 1.000 31.08971 ? 112 ARG A CZ  1 
ATOM   902  N NH1 . ARG A 1 112 ? 5.02694   35.75657 22.32018 1.000 29.02694 ? 112 ARG A NH1 1 
ATOM   903  N NH2 . ARG A 1 112 ? 6.06796   33.85956 23.07514 1.000 27.52299 ? 112 ARG A NH2 1 
ATOM   904  N N   . ASN A 1 113 ? 3.20878   33.26230 18.12985 1.000 10.87990 ? 113 ASN A N   1 
ATOM   905  C CA  . ASN A 1 113 ? 4.04965   34.08015 17.26958 1.000 11.51472 ? 113 ASN A CA  1 
ATOM   906  C C   . ASN A 1 113 ? 3.61031   34.06504 15.81568 1.000 10.23457 ? 113 ASN A C   1 
ATOM   907  O O   . ASN A 1 113 ? 3.90922   35.01594 15.08851 1.000 11.39452 ? 113 ASN A O   1 
ATOM   908  C CB  . ASN A 1 113 ? 5.51064   33.64704 17.38528 1.000 11.61658 ? 113 ASN A CB  1 
ATOM   909  C CG  . ASN A 1 113 ? 6.13297   34.06312 18.70310 1.000 11.85460 ? 113 ASN A CG  1 
ATOM   910  O OD1 . ASN A 1 113 ? 5.72119   35.05322 19.31110 1.000 14.12835 ? 113 ASN A OD1 1 
ATOM   911  N ND2 . ASN A 1 113 ? 7.12901   33.30709 19.15295 1.000 13.52598 ? 113 ASN A ND2 1 
ATOM   912  N N   . ARG A 1 114 ? 2.90413   33.03005 15.36694 1.000 9.75921  ? 114 ARG A N   1 
ATOM   913  C CA  . ARG A 1 114 ? 2.58779   32.91794 13.94703 1.000 9.09351  ? 114 ARG A CA  1 
ATOM   914  C C   . ARG A 1 114 ? 1.11570   32.74602 13.61338 1.000 12.24533 ? 114 ARG A C   1 
ATOM   915  O O   . ARG A 1 114 ? 0.75445   32.90093 12.44345 1.000 16.57005 ? 114 ARG A O   1 
ATOM   916  C CB  . ARG A 1 114 ? 3.40155   31.78780 13.29995 1.000 9.67080  ? 114 ARG A CB  1 
ATOM   917  C CG  . ARG A 1 114 ? 4.87364   31.87872 13.64461 1.000 11.81543 ? 114 ARG A CG  1 
ATOM   918  C CD  . ARG A 1 114 ? 5.63443   30.68361 13.14855 1.000 9.50209  ? 114 ARG A CD  1 
ATOM   919  N NE  . ARG A 1 114 ? 5.82310   30.72345 11.70350 1.000 7.86107  ? 114 ARG A NE  1 
ATOM   920  C CZ  . ARG A 1 114 ? 6.62488   29.89632 11.04340 1.000 10.67639 ? 114 ARG A CZ  1 
ATOM   921  N NH1 . ARG A 1 114 ? 6.74459   29.99718 9.72837  1.000 10.28089 ? 114 ARG A NH1 1 
ATOM   922  N NH2 . ARG A 1 114 ? 7.30196   28.96633 11.70734 1.000 9.23624  ? 114 ARG A NH2 1 
ATOM   923  N N   . CYS A 1 115 ? 0.26090   32.44519 14.57360 1.000 10.17936 ? 115 CYS A N   1 
ATOM   924  C CA  . CYS A 1 115 ? -1.15618  32.26227 14.28895 1.000 10.21953 ? 115 CYS A CA  1 
ATOM   925  C C   . CYS A 1 115 ? -2.04794  33.26942 14.98305 1.000 11.39682 ? 115 CYS A C   1 
ATOM   926  O O   . CYS A 1 115 ? -3.01404  33.75143 14.37922 1.000 9.91316  ? 115 CYS A O   1 
ATOM   927  C CB  . CYS A 1 115 ? -1.58520  30.86735 14.71518 1.000 8.89432  ? 115 CYS A CB  1 
ATOM   928  S SG  . CYS A 1 115 ? -0.65550  29.58619 13.85810 1.000 8.49992  ? 115 CYS A SG  1 
ATOM   929  N N   . LYS A 1 116 ? -1.76563  33.54452 16.25096 1.000 9.52369  ? 116 LYS A N   1 
ATOM   930  C CA  . LYS A 1 116 ? -2.58037  34.43467 17.05806 1.000 10.30860 ? 116 LYS A CA  1 
ATOM   931  C C   . LYS A 1 116 ? -2.81343  35.74261 16.32898 1.000 11.08600 ? 116 LYS A C   1 
ATOM   932  O O   . LYS A 1 116 ? -1.86949  36.38549 15.86070 1.000 11.85388 ? 116 LYS A O   1 
ATOM   933  C CB  . LYS A 1 116 ? -1.84205  34.70274 18.36786 1.000 9.38250  ? 116 LYS A CB  1 
ATOM   934  C CG  . LYS A 1 116 ? -2.60975  35.52890 19.38395 1.000 11.05350 ? 116 LYS A CG  1 
ATOM   935  C CD  . LYS A 1 116 ? -1.80545  35.63396 20.66576 1.000 11.06423 ? 116 LYS A CD  1 
ATOM   936  C CE  . LYS A 1 116 ? -2.59714  36.28514 21.78488 1.000 12.29805 ? 116 LYS A CE  1 
ATOM   937  N NZ  . LYS A 1 116 ? -1.78985  36.29620 23.03669 1.000 13.08262 ? 116 LYS A NZ  1 
ATOM   938  N N   . GLY A 1 117 ? -4.09043  36.10870 16.20123 1.000 11.66978 ? 117 GLY A N   1 
ATOM   939  C CA  . GLY A 1 117 ? -4.48147  37.35767 15.59620 1.000 12.07214 ? 117 GLY A CA  1 
ATOM   940  C C   . GLY A 1 117 ? -4.54682  37.35253 14.09021 1.000 17.25945 ? 117 GLY A C   1 
ATOM   941  O O   . GLY A 1 117 ? -5.07287  38.31051 13.51324 1.000 17.78072 ? 117 GLY A O   1 
ATOM   942  N N   . THR A 1 118 ? -4.03705  36.31142 13.43020 1.000 14.26036 ? 118 THR A N   1 
ATOM   943  C CA  . THR A 1 118 ? -4.01839  36.25828 11.97820 1.000 13.33058 ? 118 THR A CA  1 
ATOM   944  C C   . THR A 1 118 ? -5.33355  35.69133 11.45256 1.000 13.54647 ? 118 THR A C   1 
ATOM   945  O O   . THR A 1 118 ? -6.20142  35.24948 12.20580 1.000 12.64351 ? 118 THR A O   1 
ATOM   946  C CB  . THR A 1 118 ? -2.84457  35.41413 11.47902 1.000 12.73974 ? 118 THR A CB  1 
ATOM   947  O OG1 . THR A 1 118 ? -3.11563  34.02918 11.72922 1.000 11.49269 ? 118 THR A OG1 1 
ATOM   948  C CG2 . THR A 1 118 ? -1.54438  35.82109 12.16068 1.000 12.34318 ? 118 THR A CG2 1 
ATOM   949  N N   . ASP A 1 119 ? -5.47686  35.68821 10.12859 1.000 15.07603 ? 119 ASP A N   1 
ATOM   950  C CA  . ASP A 1 119 ? -6.66005  35.13024 9.47892  1.000 13.01164 ? 119 ASP A CA  1 
ATOM   951  C C   . ASP A 1 119 ? -6.53317  33.61023 9.48304  1.000 15.13057 ? 119 ASP A C   1 
ATOM   952  O O   . ASP A 1 119 ? -6.21346  32.97310 8.47703  1.000 17.36606 ? 119 ASP A O   1 
ATOM   953  C CB  . ASP A 1 119 ? -6.79133  35.68111 8.06389  1.000 16.93203 ? 119 ASP A CB  1 
ATOM   954  C CG  . ASP A 1 119 ? -8.00654  35.14514 7.34423  1.000 31.95916 ? 119 ASP A CG  1 
ATOM   955  O OD1 . ASP A 1 119 ? -8.88643  34.55228 8.00749  1.000 25.00822 ? 119 ASP A OD1 1 
ATOM   956  O OD2 . ASP A 1 119 ? -8.08181  35.31602 6.11123  1.000 29.53729 ? 119 ASP A OD2 1 
ATOM   957  N N   . VAL A 1 120 ? -6.79695  33.01937 10.65116 1.000 14.65118 ? 120 VAL A N   1 
ATOM   958  C CA  . VAL A 1 120 ? -6.63604  31.57737 10.79927 1.000 11.72554 ? 120 VAL A CA  1 
ATOM   959  C C   . VAL A 1 120 ? -7.68828  30.79738 10.02259 1.000 12.05388 ? 120 VAL A C   1 
ATOM   960  O O   . VAL A 1 120 ? -7.47844  29.61533 9.72766  1.000 11.90605 ? 120 VAL A O   1 
ATOM   961  C CB  . VAL A 1 120 ? -6.60273  31.15652 12.28230 1.000 12.52423 ? 120 VAL A CB  1 
ATOM   962  C CG1 . VAL A 1 120 ? -5.35253  31.71048 12.96996 1.000 12.64650 ? 120 VAL A CG1 1 
ATOM   963  C CG2 . VAL A 1 120 ? -7.86753  31.60469 12.99055 1.000 16.52360 ? 120 VAL A CG2 1 
ATOM   964  N N   . GLN A 1 121 ? -8.82130  31.42144 9.68678  1.000 15.39254 ? 121 GLN A N   1 
ATOM   965  C CA  . GLN A 1 121 ? -9.84054  30.72144 8.90909  1.000 14.36421 ? 121 GLN A CA  1 
ATOM   966  C C   . GLN A 1 121 ? -9.30089  30.27226 7.55801  1.000 14.57294 ? 121 GLN A C   1 
ATOM   967  O O   . GLN A 1 121 ? -9.77309  29.27225 7.00222  1.000 15.51090 ? 121 GLN A O   1 
ATOM   968  C CB  . GLN A 1 121 ? -11.07551 31.60953 8.73328  1.000 19.30928 ? 121 GLN A CB  1 
ATOM   969  C CG  . GLN A 1 121 ? -12.31368 30.85858 8.25564  1.000 26.50435 ? 121 GLN A CG  1 
ATOM   970  C CD  . GLN A 1 121 ? -12.38703 30.75343 6.74367  1.000 28.94523 ? 121 GLN A CD  1 
ATOM   971  O OE1 . GLN A 1 121 ? -11.81613 31.57632 6.02745  1.000 33.33525 ? 121 GLN A OE1 1 
ATOM   972  N NE2 . GLN A 1 121 ? -13.08523 29.73644 6.25193  1.000 30.85366 ? 121 GLN A NE2 1 
ATOM   973  N N   . ALA A 1 122 ? -8.30295  30.98413 7.02571  1.000 11.36428 ? 122 ALA A N   1 
ATOM   974  C CA  . ALA A 1 122 ? -7.67827  30.57495 5.77261  1.000 12.05492 ? 122 ALA A CA  1 
ATOM   975  C C   . ALA A 1 122 ? -7.18537  29.13692 5.83264  1.000 12.44576 ? 122 ALA A C   1 
ATOM   976  O O   . ALA A 1 122 ? -7.14966  28.44581 4.80870  1.000 14.29404 ? 122 ALA A O   1 
ATOM   977  C CB  . ALA A 1 122 ? -6.52227  31.51783 5.43525  1.000 15.97039 ? 122 ALA A CB  1 
ATOM   978  N N   . TRP A 1 123 ? -6.81914  28.65901 7.02260  1.000 11.91512 ? 123 TRP A N   1 
ATOM   979  C CA  . TRP A 1 123 ? -6.28422  27.30898 7.14161  1.000 11.89592 ? 123 TRP A CA  1 
ATOM   980  C C   . TRP A 1 123 ? -7.32637  26.22804 6.89596  1.000 14.52698 ? 123 TRP A C   1 
ATOM   981  O O   . TRP A 1 123 ? -6.95953  25.09298 6.57999  1.000 13.94152 ? 123 TRP A O   1 
ATOM   982  C CB  . TRP A 1 123 ? -5.60093  27.13506 8.49748  1.000 12.35503 ? 123 TRP A CB  1 
ATOM   983  C CG  . TRP A 1 123 ? -4.33585  27.90896 8.53811  1.000 10.83643 ? 123 TRP A CG  1 
ATOM   984  C CD1 . TRP A 1 123 ? -4.12462  29.10600 9.14794  1.000 14.03344 ? 123 TRP A CD1 1 
ATOM   985  C CD2 . TRP A 1 123 ? -3.10303  27.55979 7.89686  1.000 12.84921 ? 123 TRP A CD2 1 
ATOM   986  N NE1 . TRP A 1 123 ? -2.83363  29.52088 8.94060  1.000 13.24053 ? 123 TRP A NE1 1 
ATOM   987  C CE2 . TRP A 1 123 ? -2.18388  28.58875 8.17655  1.000 14.55968 ? 123 TRP A CE2 1 
ATOM   988  C CE3 . TRP A 1 123 ? -2.68929  26.47468 7.11887  1.000 12.42891 ? 123 TRP A CE3 1 
ATOM   989  C CZ2 . TRP A 1 123 ? -0.87399  28.56659 7.70625  1.000 16.91774 ? 123 TRP A CZ2 1 
ATOM   990  C CZ3 . TRP A 1 123 ? -1.38840  26.45253 6.65058  1.000 16.19525 ? 123 TRP A CZ3 1 
ATOM   991  C CH2 . TRP A 1 123 ? -0.49725  27.49449 6.94627  1.000 16.90821 ? 123 TRP A CH2 1 
ATOM   992  N N   . ILE A 1 124 ? -8.61131  26.54416 7.03822  1.000 15.03071 ? 124 ILE A N   1 
ATOM   993  C CA  A ILE A 1 124 ? -9.67545  25.58922 6.76656  0.999 13.96541 ? 124 ILE A CA  1 
ATOM   994  C CA  B ILE A 1 124 ? -9.68945  25.60022 6.76856  0.001 14.45553 ? 124 ILE A CA  1 
ATOM   995  C C   . ILE A 1 124 ? -10.50369 25.99016 5.54771  1.000 16.55567 ? 124 ILE A C   1 
ATOM   996  O O   . ILE A 1 124 ? -11.50082 25.32521 5.24600  1.000 16.02943 ? 124 ILE A O   1 
ATOM   997  C CB  A ILE A 1 124 ? -10.55419 25.32441 7.99979  0.999 16.40565 ? 124 ILE A CB  1 
ATOM   998  C CB  B ILE A 1 124 ? -10.59318 25.38241 7.99679  0.001 16.17372 ? 124 ILE A CB  1 
ATOM   999  C CG1 A ILE A 1 124 ? -11.29399 26.59551 8.41883  0.999 17.02037 ? 124 ILE A CG1 1 
ATOM   1000 C CG1 B ILE A 1 124 ? -11.05094 26.72451 8.57176  0.001 16.95480 ? 124 ILE A CG1 1 
ATOM   1001 C CG2 A ILE A 1 124 ? -9.70597  24.78346 9.14865  0.999 15.88324 ? 124 ILE A CG2 1 
ATOM   1002 C CG2 B ILE A 1 124 ? -9.86901  24.56546 9.05371  0.001 15.83878 ? 124 ILE A CG2 1 
ATOM   1003 C CD1 A ILE A 1 124 ? -12.42478 26.34570 9.40511  0.999 23.01805 ? 124 ILE A CD1 1 
ATOM   1004 C CD1 B ILE A 1 124 ? -12.51097 27.03160 8.32107  0.001 18.39540 ? 124 ILE A CD1 1 
ATOM   1005 N N   . ARG A 1 125 ? -10.10477 27.04606 4.84551  0.808 13.38589 ? 125 ARG A N   1 
ATOM   1006 C CA  . ARG A 1 125 ? -10.84899 27.51900 3.68464  0.808 18.11994 ? 125 ARG A CA  1 
ATOM   1007 C C   . ARG A 1 125 ? -10.87833 26.44590 2.60775  0.808 15.65305 ? 125 ARG A C   1 
ATOM   1008 O O   . ARG A 1 125 ? -9.85945  25.81879 2.30658  0.808 14.32661 ? 125 ARG A O   1 
ATOM   1009 C CB  . ARG A 1 125 ? -10.19002 28.78790 3.14336  0.808 18.55164 ? 125 ARG A CB  1 
ATOM   1010 C CG  . ARG A 1 125 ? -11.09115 29.64588 2.26248  0.808 23.78061 ? 125 ARG A CG  1 
ATOM   1011 C CD  . ARG A 1 125 ? -10.54006 31.06382 2.14021  0.808 22.72111 ? 125 ARG A CD  1 
ATOM   1012 N NE  . ARG A 1 125 ? -10.47871 31.74495 3.43413  0.808 22.19687 ? 125 ARG A NE  1 
ATOM   1013 C CZ  . ARG A 1 125 ? -9.69456  32.78691 3.69585  0.808 27.11666 ? 125 ARG A CZ  1 
ATOM   1014 N NH1 . ARG A 1 125 ? -8.89574  33.27275 2.75462  0.808 30.69966 ? 125 ARG A NH1 1 
ATOM   1015 N NH2 . ARG A 1 125 ? -9.70224  33.34403 4.90179  0.808 25.19552 ? 125 ARG A NH2 1 
ATOM   1016 N N   . GLY A 1 126 ? -12.06148 26.22594 2.03704  1.000 21.59348 ? 126 GLY A N   1 
ATOM   1017 C CA  . GLY A 1 126 ? -12.23879 25.21985 1.01818  1.000 21.71369 ? 126 GLY A CA  1 
ATOM   1018 C C   . GLY A 1 126 ? -12.40779 23.80391 1.52136  1.000 22.31030 ? 126 GLY A C   1 
ATOM   1019 O O   . GLY A 1 126 ? -12.75405 22.92186 0.72553  1.000 22.25873 ? 126 GLY A O   1 
ATOM   1020 N N   . CYS A 1 127 ? -12.18652 23.54402 2.80534  1.000 16.81037 ? 127 CYS A N   1 
ATOM   1021 C CA  . CYS A 1 127 ? -12.27351 22.18208 3.31550  1.000 16.25833 ? 127 CYS A CA  1 
ATOM   1022 C C   . CYS A 1 127 ? -13.72450 21.76722 3.50387  1.000 17.24430 ? 127 CYS A C   1 
ATOM   1023 O O   . CYS A 1 127 ? -14.54332 22.52534 4.03198  1.000 20.35678 ? 127 CYS A O   1 
ATOM   1024 C CB  . CYS A 1 127 ? -11.54022 22.05416 4.64834  1.000 13.40432 ? 127 CYS A CB  1 
ATOM   1025 S SG  . CYS A 1 127 ? -9.79919  22.51601 4.61090  1.000 15.90466 ? 127 CYS A SG  1 
ATOM   1026 N N   . ARG A 1 128 ? -14.03270 20.54720 3.06806  1.000 22.10798 ? 128 ARG A N   1 
ATOM   1027 C CA  . ARG A 1 128 ? -15.33370 19.93233 3.30742  1.000 22.52108 ? 128 ARG A CA  1 
ATOM   1028 C C   . ARG A 1 128 ? -15.32841 19.43547 4.74547  1.000 27.27937 ? 128 ARG A C   1 
ATOM   1029 O O   . ARG A 1 128 ? -14.73242 18.40146 5.05743  1.000 34.47479 ? 128 ARG A O   1 
ATOM   1030 C CB  . ARG A 1 128 ? -15.55702 18.78825 2.32558  1.000 21.25389 ? 128 ARG A CB  1 
ATOM   1031 C CG  . ARG A 1 128 ? -16.96806 18.22736 2.31396  1.000 22.71996 ? 128 ARG A CG  1 
ATOM   1032 C CD  . ARG A 1 128 ? -17.15741 17.25826 1.16010  1.000 22.01514 ? 128 ARG A CD  1 
ATOM   1033 N NE  . ARG A 1 128 ? -18.55648 16.87736 0.97546  1.000 23.85319 ? 128 ARG A NE  1 
ATOM   1034 C CZ  . ARG A 1 128 ? -19.40761 17.50635 0.17059  1.000 21.87293 ? 128 ARG A CZ  1 
ATOM   1035 N NH1 . ARG A 1 128 ? -19.01169 18.56425 -0.52960 1.000 26.80029 ? 128 ARG A NH1 1 
ATOM   1036 N NH2 . ARG A 1 128 ? -20.66067 17.07844 0.06792  1.000 27.36585 ? 128 ARG A NH2 1 
ATOM   1037 N N   . LEU A 1 129 ? -15.97515 20.18461 5.63254  1.000 23.56761 ? 129 LEU A N   1 
ATOM   1038 C CA  . LEU A 1 129 ? -15.94385 19.87775 7.05356  1.000 24.64244 ? 129 LEU A CA  1 
ATOM   1039 C C   . LEU A 1 129 ? -17.35272 19.79392 7.61790  1.000 38.68656 ? 129 LEU A C   1 
ATOM   1040 O O   . LEU A 1 129 ? -18.31382 20.28794 7.02207  1.000 42.76417 ? 129 LEU A O   1 
ATOM   1041 C CB  . LEU A 1 129 ? -15.15259 20.94477 7.81128  1.000 21.86291 ? 129 LEU A CB  1 
ATOM   1042 C CG  . LEU A 1 129 ? -13.65865 21.02461 7.51293  1.000 23.98947 ? 129 LEU A CG  1 
ATOM   1043 C CD1 . LEU A 1 129 ? -13.07842 22.33062 8.03366  1.000 26.55621 ? 129 LEU A CD1 1 
ATOM   1044 C CD2 . LEU A 1 129 ? -12.93961 19.83262 8.12088  1.000 22.77953 ? 129 LEU A CD2 1 
ATOM   1045 O OXT . LEU A 1 129 ? -17.54752 19.23205 8.69400  1.000 30.35164 ? 129 LEU A OXT 1 
HETATM 1046 C C1  . TEP B 2 .   ? 4.26700   24.92100 37.45400 0.897 46.71943 ? 201 TEP A C1  1 
HETATM 1047 N N1  . TEP B 2 .   ? 3.59900   24.31800 36.31400 0.730 60.97075 ? 201 TEP A N1  1 
HETATM 1048 C C2  . TEP B 2 .   ? 2.68300   23.34200 36.51200 0.691 60.06508 ? 201 TEP A C2  1 
HETATM 1049 O O2  . TEP B 2 .   ? 2.42500   22.98000 37.61000 0.759 54.16217 ? 201 TEP A O2  1 
HETATM 1050 N N3  . TEP B 2 .   ? 2.06000   22.77800 35.45700 0.754 48.17990 ? 201 TEP A N3  1 
HETATM 1051 C C3  . TEP B 2 .   ? 1.07600   21.73900 35.68200 0.869 30.98248 ? 201 TEP A C3  1 
HETATM 1052 C C4  . TEP B 2 .   ? 2.34300   23.18200 34.20700 1.000 32.71020 ? 201 TEP A C4  1 
HETATM 1053 C C5  . TEP B 2 .   ? 3.24600   24.14400 34.00700 1.000 43.99080 ? 201 TEP A C5  1 
HETATM 1054 C C6  . TEP B 2 .   ? 3.88100   24.72200 35.08600 0.730 53.74640 ? 201 TEP A C6  1 
HETATM 1055 O O6  . TEP B 2 .   ? 4.68700   25.57500 34.91400 0.857 51.84931 ? 201 TEP A O6  1 
HETATM 1056 N N7  . TEP B 2 .   ? 3.34000   24.35400 32.68700 1.000 36.13472 ? 201 TEP A N7  1 
HETATM 1057 C C8  . TEP B 2 .   ? 2.49400   23.51900 32.07500 1.000 44.21043 ? 201 TEP A C8  1 
HETATM 1058 N N9  . TEP B 2 .   ? 1.87700   22.79400 33.01100 1.000 42.49202 ? 201 TEP A N9  1 
HETATM 1059 O O   . HOH C 3 .   ? 7.86300   14.01100 31.20900 1.000 8.80005  ? 301 HOH A O   1 
HETATM 1060 O O   . HOH C 3 .   ? 14.64900  24.56300 26.46700 1.000 24.57621 ? 302 HOH A O   1 
HETATM 1061 O O   . HOH C 3 .   ? 11.53300  22.59500 20.07800 1.000 26.28361 ? 303 HOH A O   1 
HETATM 1062 O O   . HOH C 3 .   ? -14.20900 29.86500 17.66300 1.000 33.50151 ? 304 HOH A O   1 
HETATM 1063 O O   . HOH C 3 .   ? -14.90900 25.33600 30.05600 1.000 38.71701 ? 305 HOH A O   1 
HETATM 1064 O O   . HOH C 3 .   ? -14.68600 16.27100 6.02200  1.000 22.88997 ? 306 HOH A O   1 
HETATM 1065 O O   . HOH C 3 .   ? 2.86000   7.36700  10.69200 1.000 17.74656 ? 307 HOH A O   1 
HETATM 1066 O O   . HOH C 3 .   ? -10.82500 14.07900 24.19000 1.000 36.93226 ? 308 HOH A O   1 
HETATM 1067 O O   . HOH C 3 .   ? -18.43400 20.51100 15.60400 1.000 34.99577 ? 309 HOH A O   1 
HETATM 1068 O O   . HOH C 3 .   ? -7.92300  15.37700 27.53300 1.000 23.99469 ? 310 HOH A O   1 
HETATM 1069 O O   . HOH C 3 .   ? 3.81200   31.83000 24.36900 1.000 32.46886 ? 311 HOH A O   1 
HETATM 1070 O O   . HOH C 3 .   ? -17.04700 8.92800  17.08800 1.000 37.97313 ? 312 HOH A O   1 
HETATM 1071 O O   . HOH C 3 .   ? -4.75200  9.13100  10.98500 1.000 25.18458 ? 313 HOH A O   1 
HETATM 1072 O O   . HOH C 3 .   ? 5.89700   26.55500 19.78300 1.000 18.23087 ? 314 HOH A O   1 
HETATM 1073 O O   . HOH C 3 .   ? -16.53800 13.44200 17.63800 1.000 36.89877 ? 315 HOH A O   1 
HETATM 1074 O O   . HOH C 3 .   ? 8.49900   19.24400 37.47000 1.000 32.17012 ? 316 HOH A O   1 
HETATM 1075 O O   . HOH C 3 .   ? 18.27600  9.98800  24.41400 1.000 22.00979 ? 317 HOH A O   1 
HETATM 1076 O O   . HOH C 3 .   ? -0.67500  5.62600  29.55400 1.000 35.51035 ? 318 HOH A O   1 
HETATM 1077 O O   . HOH C 3 .   ? 14.61100  7.34100  33.11100 1.000 24.21212 ? 319 HOH A O   1 
HETATM 1078 O O   . HOH C 3 .   ? -14.32700 31.59600 20.40900 1.000 15.39848 ? 320 HOH A O   1 
HETATM 1079 O O   . HOH C 3 .   ? -3.81900  33.21600 7.42200  1.000 25.02171 ? 321 HOH A O   1 
HETATM 1080 O O   . HOH C 3 .   ? 1.21000   13.28500 2.93700  1.000 40.43097 ? 322 HOH A O   1 
HETATM 1081 O O   . HOH C 3 .   ? -7.52700  26.61600 33.64700 1.000 35.80023 ? 323 HOH A O   1 
HETATM 1082 O O   . HOH C 3 .   ? 13.68200  14.64500 26.15300 1.000 10.59604 ? 324 HOH A O   1 
HETATM 1083 O O   . HOH C 3 .   ? -9.97900  7.60500  18.62000 1.000 27.27936 ? 325 HOH A O   1 
HETATM 1084 O O   . HOH C 3 .   ? -5.05500  21.43400 32.21400 1.000 23.73189 ? 326 HOH A O   1 
HETATM 1085 O O   . HOH C 3 .   ? 11.31800  13.17500 14.40700 1.000 10.66744 ? 327 HOH A O   1 
HETATM 1086 O O   . HOH C 3 .   ? 7.14900   3.82100  23.57800 1.000 17.18791 ? 328 HOH A O   1 
HETATM 1087 O O   . HOH C 3 .   ? 0.85800   13.76200 16.53700 1.000 14.38439 ? 329 HOH A O   1 
HETATM 1088 O O   . HOH C 3 .   ? 1.71500   33.41000 10.00200 1.000 14.57551 ? 330 HOH A O   1 
HETATM 1089 O O   . HOH C 3 .   ? 0.71200   18.42200 4.03400  1.000 16.06488 ? 331 HOH A O   1 
HETATM 1090 O O   . HOH C 3 .   ? 7.59700   24.11500 19.54300 1.000 23.54501 ? 332 HOH A O   1 
HETATM 1091 O O   . HOH C 3 .   ? -14.42500 15.16800 10.60000 1.000 27.66991 ? 333 HOH A O   1 
HETATM 1092 O O   . HOH C 3 .   ? -16.63500 22.48300 10.80900 1.000 35.29010 ? 334 HOH A O   1 
HETATM 1093 O O   . HOH C 3 .   ? -2.57400  32.39500 9.67700  1.000 15.87241 ? 335 HOH A O   1 
HETATM 1094 O O   . HOH C 3 .   ? 1.46500   37.46700 18.82700 1.000 24.22713 ? 336 HOH A O   1 
HETATM 1095 O O   . HOH C 3 .   ? 3.40000   4.64100  21.66500 1.000 20.79244 ? 337 HOH A O   1 
HETATM 1096 O O   . HOH C 3 .   ? 15.26100  18.65800 33.29000 1.000 36.76161 ? 338 HOH A O   1 
HETATM 1097 O O   . HOH C 3 .   ? -3.25100  14.56900 34.85000 1.000 37.55441 ? 339 HOH A O   1 
HETATM 1098 O O   . HOH C 3 .   ? 7.60700   25.92100 15.39200 1.000 13.57932 ? 340 HOH A O   1 
HETATM 1099 O O   . HOH C 3 .   ? 4.64500   37.52600 19.29800 1.000 25.85040 ? 341 HOH A O   1 
HETATM 1100 O O   . HOH C 3 .   ? -1.82300  12.07500 4.59600  1.000 23.52349 ? 342 HOH A O   1 
HETATM 1101 O O   . HOH C 3 .   ? 8.89600   14.09100 38.42700 1.000 29.76966 ? 343 HOH A O   1 
HETATM 1102 O O   . HOH C 3 .   ? 14.23400  14.23400 18.45200 0.50  20.96340 ? 344 HOH A O   1 
HETATM 1103 O O   . HOH C 3 .   ? -0.61100  11.99200 16.16200 1.000 12.44715 ? 345 HOH A O   1 
HETATM 1104 O O   . HOH C 3 .   ? 12.05100  24.41200 31.11400 1.000 36.06190 ? 346 HOH A O   1 
HETATM 1105 O O   . HOH C 3 .   ? -9.23600  12.66600 20.66900 1.000 27.39261 ? 347 HOH A O   1 
HETATM 1106 O O   . HOH C 3 .   ? -6.39600  27.94700 29.33400 1.000 14.66058 ? 348 HOH A O   1 
HETATM 1107 O O   . HOH C 3 .   ? 0.87000   8.65400  34.66300 1.000 35.23390 ? 349 HOH A O   1 
HETATM 1108 O O   . HOH C 3 .   ? -1.11800  38.83300 14.91100 1.000 22.37714 ? 350 HOH A O   1 
HETATM 1109 O O   . HOH C 3 .   ? -12.60800 17.97900 27.73400 1.000 30.69042 ? 351 HOH A O   1 
HETATM 1110 O O   . HOH C 3 .   ? 9.14900   22.23800 18.41700 1.000 15.83002 ? 352 HOH A O   1 
HETATM 1111 O O   . HOH C 3 .   ? 8.14600   18.19300 10.61500 1.000 22.41010 ? 353 HOH A O   1 
HETATM 1112 O O   . HOH C 3 .   ? -16.86100 25.94700 22.52400 1.000 24.25097 ? 354 HOH A O   1 
HETATM 1113 O O   . HOH C 3 .   ? 5.55400   10.91500 9.05200  1.000 10.73098 ? 355 HOH A O   1 
HETATM 1114 O O   . HOH C 3 .   ? -4.21400  10.16500 3.80300  1.000 37.10005 ? 356 HOH A O   1 
HETATM 1115 O O   . HOH C 3 .   ? 4.08000   6.03100  17.93000 1.000 21.48751 ? 357 HOH A O   1 
HETATM 1116 O O   . HOH C 3 .   ? -6.80700  28.93400 2.12300  1.000 29.26321 ? 358 HOH A O   1 
HETATM 1117 O O   . HOH C 3 .   ? -10.64300 31.10800 23.75500 1.000 13.33996 ? 359 HOH A O   1 
HETATM 1118 O O   . HOH C 3 .   ? -18.98000 11.84000 17.11200 1.000 24.96180 ? 360 HOH A O   1 
HETATM 1119 O O   . HOH C 3 .   ? -8.98700  13.07400 8.16200  1.000 20.55384 ? 361 HOH A O   1 
HETATM 1120 O O   . HOH C 3 .   ? -6.10600  33.56600 16.76500 1.000 14.13917 ? 362 HOH A O   1 
HETATM 1121 O O   . HOH C 3 .   ? -9.14500  28.54300 29.89600 1.000 30.73828 ? 363 HOH A O   1 
HETATM 1122 O O   . HOH C 3 .   ? 12.73700  12.73700 36.90400 0.50  16.09506 ? 364 HOH A O   1 
HETATM 1123 O O   . HOH C 3 .   ? -2.56900  26.80700 28.33800 1.000 13.87898 ? 365 HOH A O   1 
HETATM 1124 O O   . HOH C 3 .   ? -3.09200  11.83500 25.44600 1.000 20.04951 ? 366 HOH A O   1 
HETATM 1125 O O   . HOH C 3 .   ? -4.00900  6.16700  11.49500 1.000 35.08087 ? 367 HOH A O   1 
HETATM 1126 O O   . HOH C 3 .   ? -7.788    38.074   5.811    1.000 36.91609 ? 368 HOH A O   1 
HETATM 1127 O O   . HOH C 3 .   ? 10.41200  8.74400  33.72800 1.000 28.01899 ? 369 HOH A O   1 
HETATM 1128 O O   . HOH C 3 .   ? 1.55600   16.50500 19.30500 1.000 8.76428  ? 370 HOH A O   1 
HETATM 1129 O O   . HOH C 3 .   ? -15.55000 19.33300 21.70400 1.000 30.45396 ? 371 HOH A O   1 
HETATM 1130 O O   . HOH C 3 .   ? -13.78100 16.95800 24.37200 1.000 26.52326 ? 372 HOH A O   1 
HETATM 1131 O O   . HOH C 3 .   ? -15.55800 22.17600 21.05300 1.000 30.59080 ? 373 HOH A O   1 
HETATM 1132 O O   . HOH C 3 .   ? 2.79000   20.18900 37.94300 1.000 39.31018 ? 374 HOH A O   1 
HETATM 1133 O O   . HOH C 3 .   ? -14.30900 25.07800 5.20400  1.000 29.46171 ? 375 HOH A O   1 
HETATM 1134 O O   . HOH C 3 .   ? -3.56500  7.66700  6.48500  1.000 29.23288 ? 376 HOH A O   1 
HETATM 1135 O O   . HOH C 3 .   ? -7.23100  35.12300 14.83800 1.000 18.89749 ? 377 HOH A O   1 
HETATM 1136 O O   . HOH C 3 .   ? 0.89100   35.95900 15.40700 1.000 16.31310 ? 378 HOH A O   1 
HETATM 1137 O O   . HOH C 3 .   ? -9.23300  7.92000  16.05100 1.000 32.30511 ? 379 HOH A O   1 
HETATM 1138 O O   . HOH C 3 .   ? -11.38600 31.00800 17.65700 1.000 14.14373 ? 380 HOH A O   1 
HETATM 1139 O O   . HOH C 3 .   ? 17.49000  15.53200 29.47500 1.000 27.49283 ? 381 HOH A O   1 
HETATM 1140 O O   . HOH C 3 .   ? 5.88400   24.49100 8.76700  1.000 21.77793 ? 382 HOH A O   1 
HETATM 1141 O O   . HOH C 3 .   ? 5.42000   23.30900 21.42800 1.000 29.53822 ? 383 HOH A O   1 
HETATM 1142 O O   . HOH C 3 .   ? -15.95200 23.33500 13.32100 1.000 35.42252 ? 384 HOH A O   1 
HETATM 1143 O O   . HOH C 3 .   ? -1.23600  6.96600  20.18500 1.000 17.45302 ? 385 HOH A O   1 
HETATM 1144 O O   . HOH C 3 .   ? 8.89400   23.70000 23.44200 1.000 31.99215 ? 386 HOH A O   1 
HETATM 1145 O O   . HOH C 3 .   ? 9.65600   12.61500 30.28100 1.000 9.79611  ? 387 HOH A O   1 
HETATM 1146 O O   . HOH C 3 .   ? 2.96100   19.69300 5.11200  1.000 17.42068 ? 388 HOH A O   1 
HETATM 1147 O O   . HOH C 3 .   ? 5.87100   17.61700 6.96900  1.000 18.59643 ? 389 HOH A O   1 
HETATM 1148 O O   . HOH C 3 .   ? -10.18300 9.29400  23.40200 1.000 37.75005 ? 390 HOH A O   1 
HETATM 1149 O O   . HOH C 3 .   ? -7.19000  39.71900 14.86200 1.000 34.63736 ? 391 HOH A O   1 
HETATM 1150 O O   . HOH C 3 .   ? -4.09800  12.62900 27.79900 1.000 19.71711 ? 392 HOH A O   1 
HETATM 1151 O O   . HOH C 3 .   ? -14.11900 25.74300 14.31600 1.000 17.58612 ? 393 HOH A O   1 
HETATM 1152 O O   . HOH C 3 .   ? -17.66700 22.38000 4.77500  1.000 28.92998 ? 394 HOH A O   1 
HETATM 1153 O O   . HOH C 3 .   ? 18.85700  20.13200 31.49900 1.000 27.53316 ? 395 HOH A O   1 
HETATM 1154 O O   . HOH C 3 .   ? 5.83400   26.18600 22.60800 1.000 19.94883 ? 396 HOH A O   1 
HETATM 1155 O O   . HOH C 3 .   ? 7.41200   11.99000 35.15300 1.000 35.55752 ? 397 HOH A O   1 
HETATM 1156 O O   . HOH C 3 .   ? -18.54500 25.17400 20.12300 1.000 34.18733 ? 398 HOH A O   1 
HETATM 1157 O O   . HOH C 3 .   ? 4.56000   32.70600 9.97400  1.000 11.43175 ? 399 HOH A O   1 
HETATM 1158 O O   . HOH C 3 .   ? -3.49800  8.20200  19.26300 1.000 15.23301 ? 400 HOH A O   1 
HETATM 1159 O O   . HOH C 3 .   ? 16.02900  18.34100 17.62300 1.000 22.86224 ? 401 HOH A O   1 
HETATM 1160 O O   . HOH C 3 .   ? 2.95900   13.43000 36.34800 1.000 20.40506 ? 402 HOH A O   1 
HETATM 1161 O O   . HOH C 3 .   ? -19.444   19.682   -3.218   1.000 37.86144 ? 403 HOH A O   1 
HETATM 1162 O O   . HOH C 3 .   ? -14.06200 24.43200 32.28400 1.000 26.60339 ? 404 HOH A O   1 
HETATM 1163 O O   . HOH C 3 .   ? -3.64500  37.25900 8.41700  1.000 17.54268 ? 405 HOH A O   1 
HETATM 1164 O O   . HOH C 3 .   ? 1.39900   5.11800  13.73900 1.000 20.47916 ? 406 HOH A O   1 
HETATM 1165 O O   . HOH C 3 .   ? -5.91500  20.06900 1.95000  1.000 21.38408 ? 407 HOH A O   1 
HETATM 1166 O O   . HOH C 3 .   ? -8.32800  31.44200 26.06800 1.000 9.50686  ? 408 HOH A O   1 
HETATM 1167 O O   . HOH C 3 .   ? -7.14000  10.70300 8.02000  1.000 27.62490 ? 409 HOH A O   1 
HETATM 1168 O O   . HOH C 3 .   ? 7.71900   12.01100 32.51100 1.000 14.77479 ? 410 HOH A O   1 
HETATM 1169 O O   . HOH C 3 .   ? -3.86900  8.80000  29.34600 1.000 32.31235 ? 411 HOH A O   1 
HETATM 1170 O O   . HOH C 3 .   ? -9.20200  33.16700 15.86300 1.000 16.74223 ? 412 HOH A O   1 
HETATM 1171 O O   . HOH C 3 .   ? -13.60100 14.03800 21.66900 1.000 31.39364 ? 413 HOH A O   1 
HETATM 1172 O O   . HOH C 3 .   ? 0.13400   38.31700 21.95700 1.000 18.14817 ? 414 HOH A O   1 
HETATM 1173 O O   . HOH C 3 .   ? 3.69700   23.56900 28.21500 1.000 30.56767 ? 415 HOH A O   1 
HETATM 1174 O O   . HOH C 3 .   ? 2.08600   10.36400 5.07400  1.000 19.13170 ? 416 HOH A O   1 
HETATM 1175 O O   . HOH C 3 .   ? 4.98600   27.64900 26.53700 1.000 29.80758 ? 417 HOH A O   1 
HETATM 1176 O O   . HOH C 3 .   ? 8.58500   20.17200 34.89000 1.000 26.09719 ? 418 HOH A O   1 
HETATM 1177 O O   . HOH C 3 .   ? -14.58400 23.56200 25.26200 1.000 18.83693 ? 419 HOH A O   1 
HETATM 1178 O O   . HOH C 3 .   ? -11.15100 29.04200 11.77000 1.000 6.07984  ? 420 HOH A O   1 
HETATM 1179 O O   . HOH C 3 .   ? -0.313    36.332   25.671   1.000 23.64966 ? 421 HOH A O   1 
HETATM 1180 O O   . HOH C 3 .   ? -9.77100  33.99400 10.96900 1.000 22.72269 ? 422 HOH A O   1 
HETATM 1181 O O   . HOH C 3 .   ? -1.29800  11.02400 18.70100 1.000 11.62408 ? 423 HOH A O   1 
HETATM 1182 O O   . HOH C 3 .   ? -9.01800  18.94800 29.20900 1.000 31.54450 ? 424 HOH A O   1 
HETATM 1183 O O   . HOH C 3 .   ? -6.03900  17.48600 2.69700  1.000 15.97305 ? 425 HOH A O   1 
HETATM 1184 O O   . HOH C 3 .   ? -5.20600  24.15600 -1.04500 1.000 34.92519 ? 426 HOH A O   1 
HETATM 1185 O O   . HOH C 3 .   ? 3.399     21.450   40.115   1.000 37.82081 ? 427 HOH A O   1 
HETATM 1186 O O   . HOH C 3 .   ? 2.83900   6.79800  30.47800 1.000 19.96749 ? 428 HOH A O   1 
HETATM 1187 O O   . HOH C 3 .   ? 3.86100   21.54900 25.26600 1.000 26.47119 ? 429 HOH A O   1 
HETATM 1188 O O   . HOH C 3 .   ? 10.44300  5.63100  30.78800 1.000 9.70897  ? 430 HOH A O   1 
HETATM 1189 O O   . HOH C 3 .   ? -17.04200 30.60400 20.31500 1.000 31.18970 ? 431 HOH A O   1 
HETATM 1190 O O   . HOH C 3 .   ? -10.401   29.984   27.773   1.000 34.95522 ? 432 HOH A O   1 
HETATM 1191 O O   . HOH C 3 .   ? 11.67500  11.54500 32.36300 1.000 4.95006  ? 433 HOH A O   1 
HETATM 1192 O O   . HOH C 3 .   ? -7.61700  8.16300  13.20400 1.000 42.40153 ? 434 HOH A O   1 
HETATM 1193 O O   . HOH C 3 .   ? -5.12800  10.84400 31.06800 1.000 38.01945 ? 435 HOH A O   1 
HETATM 1194 O O   . HOH C 3 .   ? 5.47000   5.85900  29.63500 1.000 11.20217 ? 436 HOH A O   1 
HETATM 1195 O O   . HOH C 3 .   ? -0.27900  27.35600 29.71900 1.000 22.42619 ? 437 HOH A O   1 
HETATM 1196 O O   . HOH C 3 .   ? -13.413   29.258   31.052   1.000 39.55692 ? 438 HOH A O   1 
HETATM 1197 O O   . HOH C 3 .   ? -13.77000 22.53400 27.82600 1.000 28.17620 ? 439 HOH A O   1 
HETATM 1198 O O   . HOH C 3 .   ? 5.26100   8.71400  34.05100 1.000 19.26356 ? 440 HOH A O   1 
HETATM 1199 O O   . HOH C 3 .   ? 6.08000   21.97800 3.04000  1.000 27.78995 ? 441 HOH A O   1 
HETATM 1200 O O   . HOH C 3 .   ? 12.826    23.601   15.641   1.000 31.45914 ? 442 HOH A O   1 
HETATM 1201 O O   . HOH C 3 .   ? 4.02600   8.08500  7.52600  1.000 35.01562 ? 443 HOH A O   1 
HETATM 1202 O O   . HOH C 3 .   ? 10.612    12.406   35.284   1.000 26.81021 ? 444 HOH A O   1 
HETATM 1203 O O   . HOH C 3 .   ? -21.886   18.962   -2.259   1.000 23.49390 ? 445 HOH A O   1 
HETATM 1204 O O   . HOH C 3 .   ? 8.14500   17.29000 7.94100  1.000 22.33318 ? 446 HOH A O   1 
HETATM 1205 O O   . HOH C 3 .   ? -12.39500 31.28400 12.65900 1.000 31.23097 ? 447 HOH A O   1 
HETATM 1206 O O   . HOH C 3 .   ? 13.35500  20.01200 31.64000 1.000 34.62597 ? 448 HOH A O   1 
HETATM 1207 O O   . HOH C 3 .   ? -6.57700  10.48600 13.17700 1.000 11.65514 ? 449 HOH A O   1 
HETATM 1208 O O   . HOH C 3 .   ? 18.81600  13.13100 29.80300 1.000 38.37168 ? 450 HOH A O   1 
HETATM 1209 O O   . HOH C 3 .   ? 14.82500  16.05400 17.45500 1.000 22.91216 ? 451 HOH A O   1 
HETATM 1210 O O   . HOH C 3 .   ? -1.13400  20.48100 2.91200  1.000 35.66366 ? 452 HOH A O   1 
HETATM 1211 O O   . HOH C 3 .   ? 2.05600   27.23400 36.82400 1.000 38.51456 ? 453 HOH A O   1 
HETATM 1212 O O   . HOH C 3 .   ? -2.883    40.872   14.055   1.000 30.17657 ? 454 HOH A O   1 
HETATM 1213 O O   . HOH C 3 .   ? 1.65100   28.21600 28.89200 1.000 32.57744 ? 455 HOH A O   1 
HETATM 1214 O O   . HOH C 3 .   ? -22.91200 19.52300 0.93900  1.000 37.37622 ? 456 HOH A O   1 
HETATM 1215 O O   . HOH C 3 .   ? -3.508    38.855   18.246   1.000 16.74064 ? 457 HOH A O   1 
HETATM 1216 O O   . HOH C 3 .   ? 2.56800   38.03000 21.38200 1.000 31.54810 ? 458 HOH A O   1 
HETATM 1217 O O   . HOH C 3 .   ? -12.77800 8.87100  15.03800 1.000 29.52511 ? 459 HOH A O   1 
HETATM 1218 O O   . HOH C 3 .   ? 20.62600  16.76600 23.27500 1.000 36.41247 ? 460 HOH A O   1 
HETATM 1219 O O   . HOH C 3 .   ? 14.294    11.479   34.148   1.000 22.33805 ? 461 HOH A O   1 
HETATM 1220 O O   . HOH C 3 .   ? -11.21300 12.42900 9.97200  1.000 24.63319 ? 462 HOH A O   1 
HETATM 1221 O O   . HOH C 3 .   ? 8.07600   26.26200 18.18500 1.000 25.19474 ? 463 HOH A O   1 
HETATM 1222 O O   . HOH C 3 .   ? 19.38600  21.53600 22.21200 1.000 40.33487 ? 464 HOH A O   1 
HETATM 1223 O O   . HOH C 3 .   ? 1.94800   25.17400 29.50200 1.000 33.53813 ? 465 HOH A O   1 
HETATM 1224 O O   . HOH C 3 .   ? -8.29600  38.02000 11.37400 1.000 34.31657 ? 466 HOH A O   1 
HETATM 1225 O O   . HOH C 3 .   ? -3.68800  3.71200  13.39000 1.000 34.28900 ? 467 HOH A O   1 
HETATM 1226 O O   . HOH C 3 .   ? 5.49300   5.87400  32.85800 1.000 28.19622 ? 468 HOH A O   1 
HETATM 1227 O O   . HOH C 3 .   ? -11.675   32.820   15.390   1.000 32.30098 ? 469 HOH A O   1 
HETATM 1228 O O   . HOH C 3 .   ? 6.28600   25.11100 6.43900  1.000 32.02708 ? 470 HOH A O   1 
HETATM 1229 O O   . HOH C 3 .   ? -0.10500  31.89900 8.35800  1.000 18.15893 ? 471 HOH A O   1 
HETATM 1230 O O   . HOH C 3 .   ? -4.81100  9.53100  25.09800 1.000 22.35145 ? 472 HOH A O   1 
HETATM 1231 O O   . HOH C 3 .   ? 3.22000   5.46800  9.11500  1.000 34.68950 ? 473 HOH A O   1 
HETATM 1232 O O   . HOH C 3 .   ? 2.985     32.869   26.585   1.000 49.71203 ? 474 HOH A O   1 
HETATM 1233 O O   . HOH C 3 .   ? -16.895   16.989   -3.142   1.000 40.32299 ? 475 HOH A O   1 
HETATM 1234 O O   . HOH C 3 .   ? 6.598     17.341   41.280   1.000 27.49821 ? 476 HOH A O   1 
HETATM 1235 O O   . HOH C 3 .   ? 6.75500   19.59800 39.23000 1.000 34.39323 ? 477 HOH A O   1 
HETATM 1236 O O   . HOH C 3 .   ? 0.612     33.469   28.004   1.000 35.52496 ? 478 HOH A O   1 
HETATM 1237 O O   . HOH C 3 .   ? -6.82500  12.86700 28.63800 1.000 36.50510 ? 479 HOH A O   1 
HETATM 1238 O O   . HOH C 3 .   ? -0.40000  23.60200 3.86700  1.000 22.59698 ? 480 HOH A O   1 
HETATM 1239 O O   . HOH C 3 .   ? 1.767     34.737   26.247   1.000 37.83072 ? 481 HOH A O   1 
HETATM 1240 O O   . HOH C 3 .   ? -15.199   29.428   25.320   1.000 26.16898 ? 482 HOH A O   1 
HETATM 1241 O O   . HOH C 3 .   ? -8.46800  37.57900 15.07600 1.000 25.27334 ? 483 HOH A O   1 
HETATM 1242 O O   . HOH C 3 .   ? -2.10300  15.43400 1.32100  1.000 31.22658 ? 484 HOH A O   1 
HETATM 1243 O O   . HOH C 3 .   ? -16.38800 15.37400 20.00200 1.000 36.72460 ? 485 HOH A O   1 
HETATM 1244 O O   . HOH C 3 .   ? 8.26200   24.13300 4.85800  1.000 31.68591 ? 486 HOH A O   1 
HETATM 1245 O O   . HOH C 3 .   ? -0.80900  4.58500  19.40500 1.000 38.78631 ? 487 HOH A O   1 
HETATM 1246 O O   . HOH C 3 .   ? 2.32000   4.47600  16.38700 1.000 23.82472 ? 488 HOH A O   1 
HETATM 1247 O O   . HOH C 3 .   ? 4.832     35.819   26.376   1.000 38.91810 ? 489 HOH A O   1 
HETATM 1248 O O   . HOH C 3 .   ? -19.42000 23.68300 9.83200  1.000 37.24446 ? 490 HOH A O   1 
HETATM 1249 O O   . HOH C 3 .   ? -2.995    30.226   5.074    1.000 31.18112 ? 491 HOH A O   1 
HETATM 1250 O O   . HOH C 3 .   ? -9.62000  11.06200 12.24100 1.000 33.30503 ? 492 HOH A O   1 
HETATM 1251 O O   . HOH C 3 .   ? 2.15000   3.64600  11.81300 1.000 42.38026 ? 493 HOH A O   1 
HETATM 1252 O O   . HOH C 3 .   ? 6.82600   24.10400 25.58800 1.000 36.44647 ? 494 HOH A O   1 
HETATM 1253 O O   . HOH C 3 .   ? 9.400     10.729   36.274   1.000 38.86159 ? 495 HOH A O   1 
HETATM 1254 O O   . HOH C 3 .   ? -8.75800  29.26700 32.71900 1.000 31.79745 ? 496 HOH A O   1 
HETATM 1255 O O   . HOH C 3 .   ? -0.60900  9.70300  4.44100  1.000 37.78223 ? 497 HOH A O   1 
HETATM 1256 O O   . HOH C 3 .   ? -5.29300  6.17000  20.12600 1.000 30.86866 ? 498 HOH A O   1 
HETATM 1257 O O   . HOH C 3 .   ? 5.66500   11.64400 36.86300 1.000 35.46474 ? 499 HOH A O   1 
HETATM 1258 O O   . HOH C 3 .   ? -8.35300  38.57600 9.19300  1.000 39.98041 ? 500 HOH A O   1 
HETATM 1259 O O   . HOH C 3 .   ? 11.91700  6.24800  33.14800 1.000 26.69943 ? 501 HOH A O   1 
HETATM 1260 O O   . HOH C 3 .   ? -2.08900  35.52700 7.40300  1.000 28.40173 ? 502 HOH A O   1 
HETATM 1261 O O   . HOH C 3 .   ? -1.15000  4.62500  27.23400 1.000 40.35628 ? 503 HOH A O   1 
HETATM 1262 O O   . HOH C 3 .   ? 0.41400   40.15700 16.56700 1.000 34.53716 ? 504 HOH A O   1 
HETATM 1263 O O   . HOH C 3 .   ? -0.814    38.945   19.369   1.000 20.78969 ? 505 HOH A O   1 
HETATM 1264 O O   . HOH C 3 .   ? 3.32600   11.55200 2.77100  1.000 31.13767 ? 506 HOH A O   1 
HETATM 1265 O O   . HOH C 3 .   ? -2.54000  39.16500 9.76900  1.000 35.48320 ? 507 HOH A O   1 
HETATM 1266 O O   . HOH C 3 .   ? 3.77900   9.83700  36.29300 1.000 43.79985 ? 508 HOH A O   1 
HETATM 1267 O O   . HOH C 3 .   ? -7.80300  19.05400 31.95300 1.000 38.22053 ? 509 HOH A O   1 
HETATM 1268 O O   . HOH C 3 .   ? 19.07500  19.07500 18.45200 0.50  35.78966 ? 510 HOH A O   1 
HETATM 1269 O O   . HOH C 3 .   ? -7.54900  20.14300 -0.23000 1.000 39.60187 ? 511 HOH A O   1 
HETATM 1270 O O   . HOH C 3 .   ? 1.54800   3.60300  23.61800 1.000 30.53819 ? 512 HOH A O   1 
HETATM 1271 O O   . HOH C 3 .   ? -3.23800  17.55800 0.34900  1.000 35.99753 ? 513 HOH A O   1 
HETATM 1272 O O   . HOH C 3 .   ? -0.47300  5.20800  25.04000 1.000 32.34358 ? 514 HOH A O   1 
HETATM 1273 O O   . HOH C 3 .   ? -2.21700  6.05100  22.74300 1.000 26.73087 ? 515 HOH A O   1 
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