data_9EEG
# 
_entry.id   9EEG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9EEG         pdb_00009eeg 10.2210/pdb9eeg/pdb 
WWPDB D_1000290309 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-02-05 
2 'Structure model' 1 1 2025-02-12 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EEG 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        '9EEE contains the same protein complexed with a diastereomer' 
_pdbx_database_related.db_id          9EEE 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              kovalevskyay@ornl.gov 
_pdbx_contact_author.name_first         Andrey 
_pdbx_contact_author.name_last          Kovalevsky 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4459-9142 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kovalevsky, A.' 1 ? 
'Gerlits, O.'    2 ? 
'Ghosh, A.'      3 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem.Lett. 
_citation.journal_id_ASTM           BMCLE8 
_citation.journal_id_CSD            1127 
_citation.journal_id_ISSN           1464-3405 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            120 
_citation.language                  ? 
_citation.page_first                130109 
_citation.page_last                 130109 
_citation.title                     
;Potent HIV&#8208;1 protease inhibitors containing oxabicyclo octanol-derived P2-ligands: Design, synthesis, and X&#8208;ray structural studies of inhibitor-HIV-1 protease complexes.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmcl.2025.130109 
_citation.pdbx_database_id_PubMed   39848476 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ghosh, A.K.'    1  ? 
primary 'Yadav, M.'      2  ? 
primary 'Sharma, A.'     3  ? 
primary 'Johnson, M.'    4  ? 
primary 'Ghosh, A.K.'    5  ? 
primary 'Prasad, R.'     6  ? 
primary 'Amano, M.'      7  ? 
primary 'Gerlits, O.'    8  ? 
primary 'Kovalevsky, A.' 9  ? 
primary 'Mitsuya, H.'    10 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Protease 10740.677 2   3.4.23.16 ? ? ? 
2 non-polymer syn 
;(3S,3aS,4R,7R,8aS)-3-methylhexahydro-1H,3H-3a,7-epoxycyclohepta[c]furan-4-yl {(2S,3R)-3-hydroxy-4-[(4-methoxybenzene-1-sulfonyl)(2-methylpropyl)amino]-1-phenylbutan-2-yl}carbamate
;
616.765   1   ?         ? ? ? 
3 non-polymer syn 'CHLORIDE ION' 35.453    1   ?         ? ? ? 
4 water       nat water 18.015    110 ?         ? ? ? 
# 
_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       
;PQITLWKRPLVTIKIGGQLKEALLDTGADDTVIEEMSLPGRWKPKMIGGIGGFIKVRQYDQIIIEIAGHKAIGTVLVGPT
PVNIIGRNLLTQIGATLNF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PQITLWKRPLVTIKIGGQLKEALLDTGADDTVIEEMSLPGRWKPKMIGGIGGFIKVRQYDQIIIEIAGHKAIGTVLVGPT
PVNIIGRNLLTQIGATLNF
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(3S,3aS,4R,7R,8aS)-3-methylhexahydro-1H,3H-3a,7-epoxycyclohepta[c]furan-4-yl {(2S,3R)-3-hydroxy-4-[(4-methoxybenzene-1-sulfonyl)(2-methylpropyl)amino]-1-phenylbutan-2-yl}carbamate
;
A1BHV 
3 'CHLORIDE ION' CL    
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  PRO n 
1 2  GLN n 
1 3  ILE n 
1 4  THR n 
1 5  LEU n 
1 6  TRP n 
1 7  LYS n 
1 8  ARG n 
1 9  PRO n 
1 10 LEU n 
1 11 VAL n 
1 12 THR n 
1 13 ILE n 
1 14 LYS n 
1 15 ILE n 
1 16 GLY n 
1 17 GLY n 
1 18 GLN n 
1 19 LEU n 
1 20 LYS n 
1 21 GLU n 
1 22 ALA n 
1 23 LEU n 
1 24 LEU n 
1 25 ASP n 
1 26 THR n 
1 27 GLY n 
1 28 ALA n 
1 29 ASP n 
1 30 ASP n 
1 31 THR n 
1 32 VAL n 
1 33 ILE n 
1 34 GLU n 
1 35 GLU n 
1 36 MET n 
1 37 SER n 
1 38 LEU n 
1 39 PRO n 
1 40 GLY n 
1 41 ARG n 
1 42 TRP n 
1 43 LYS n 
1 44 PRO n 
1 45 LYS n 
1 46 MET n 
1 47 ILE n 
1 48 GLY n 
1 49 GLY n 
1 50 ILE n 
1 51 GLY n 
1 52 GLY n 
1 53 PHE n 
1 54 ILE n 
1 55 LYS n 
1 56 VAL n 
1 57 ARG n 
1 58 GLN n 
1 59 TYR n 
1 60 ASP n 
1 61 GLN n 
1 62 ILE n 
1 63 ILE n 
1 64 ILE n 
1 65 GLU n 
1 66 ILE n 
1 67 ALA n 
1 68 GLY n 
1 69 HIS n 
1 70 LYS n 
1 71 ALA n 
1 72 ILE n 
1 73 GLY n 
1 74 THR n 
1 75 VAL n 
1 76 LEU n 
1 77 VAL n 
1 78 GLY n 
1 79 PRO n 
1 80 THR n 
1 81 PRO n 
1 82 VAL n 
1 83 ASN n 
1 84 ILE n 
1 85 ILE n 
1 86 GLY n 
1 87 ARG n 
1 88 ASN n 
1 89 LEU n 
1 90 LEU n 
1 91 THR n 
1 92 GLN n 
1 93 ILE n 
1 94 GLY n 
1 95 ALA n 
1 96 THR n 
1 97 LEU n 
1 98 ASN n 
1 99 PHE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   99 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 pol 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Human immunodeficiency virus 1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11676 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BHV non-polymer         . 
;(3S,3aS,4R,7R,8aS)-3-methylhexahydro-1H,3H-3a,7-epoxycyclohepta[c]furan-4-yl {(2S,3R)-3-hydroxy-4-[(4-methoxybenzene-1-sulfonyl)(2-methylpropyl)amino]-1-phenylbutan-2-yl}carbamate
;
? 'C32 H44 N2 O8 S' 616.765 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CL    non-polymer         . 'CHLORIDE ION' ? 'Cl -1'           35.453  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
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 
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  PRO 1  1   1   PRO PRO A . n 
A 1 2  GLN 2  2   2   GLN GLN A . n 
A 1 3  ILE 3  3   3   ILE ILE A . n 
A 1 4  THR 4  4   4   THR THR A . n 
A 1 5  LEU 5  5   5   LEU LEU A . n 
A 1 6  TRP 6  6   6   TRP TRP A . n 
A 1 7  LYS 7  7   7   LYS LYS A . n 
A 1 8  ARG 8  8   8   ARG ARG A . n 
A 1 9  PRO 9  9   9   PRO PRO A . n 
A 1 10 LEU 10 10  10  LEU LEU A . n 
A 1 11 VAL 11 11  11  VAL VAL A . n 
A 1 12 THR 12 12  12  THR THR A . n 
A 1 13 ILE 13 13  13  ILE ILE A . n 
A 1 14 LYS 14 14  14  LYS LYS A . n 
A 1 15 ILE 15 15  15  ILE ILE A . n 
A 1 16 GLY 16 16  16  GLY GLY A . n 
A 1 17 GLY 17 17  17  GLY GLY A . n 
A 1 18 GLN 18 18  18  GLN GLN A . n 
A 1 19 LEU 19 19  19  LEU LEU A . n 
A 1 20 LYS 20 20  20  LYS LYS A . n 
A 1 21 GLU 21 21  21  GLU GLU A . n 
A 1 22 ALA 22 22  22  ALA ALA A . n 
A 1 23 LEU 23 23  23  LEU LEU A . n 
A 1 24 LEU 24 24  24  LEU LEU A . n 
A 1 25 ASP 25 25  25  ASP ASP A . n 
A 1 26 THR 26 26  26  THR THR A . n 
A 1 27 GLY 27 27  27  GLY GLY A . n 
A 1 28 ALA 28 28  28  ALA ALA A . n 
A 1 29 ASP 29 29  29  ASP ASP A . n 
A 1 30 ASP 30 30  30  ASP ASP A . n 
A 1 31 THR 31 31  31  THR THR A . n 
A 1 32 VAL 32 32  32  VAL VAL A . n 
A 1 33 ILE 33 33  33  ILE ILE A . n 
A 1 34 GLU 34 34  34  GLU GLU A . n 
A 1 35 GLU 35 35  35  GLU GLU A . n 
A 1 36 MET 36 36  36  MET MET A . n 
A 1 37 SER 37 37  37  SER SER A . n 
A 1 38 LEU 38 38  38  LEU LEU A . n 
A 1 39 PRO 39 39  39  PRO PRO A . n 
A 1 40 GLY 40 40  40  GLY GLY A . n 
A 1 41 ARG 41 41  41  ARG ARG A . n 
A 1 42 TRP 42 42  42  TRP TRP A . n 
A 1 43 LYS 43 43  43  LYS LYS A . n 
A 1 44 PRO 44 44  44  PRO PRO A . n 
A 1 45 LYS 45 45  45  LYS LYS A . n 
A 1 46 MET 46 46  46  MET MET A . n 
A 1 47 ILE 47 47  47  ILE ILE A . n 
A 1 48 GLY 48 48  48  GLY GLY A . n 
A 1 49 GLY 49 49  49  GLY GLY A . n 
A 1 50 ILE 50 50  50  ILE ILE A . n 
A 1 51 GLY 51 51  51  GLY GLY A . n 
A 1 52 GLY 52 52  52  GLY GLY A . n 
A 1 53 PHE 53 53  53  PHE PHE A . n 
A 1 54 ILE 54 54  54  ILE ILE A . n 
A 1 55 LYS 55 55  55  LYS LYS A . n 
A 1 56 VAL 56 56  56  VAL VAL A . n 
A 1 57 ARG 57 57  57  ARG ARG A . n 
A 1 58 GLN 58 58  58  GLN GLN A . n 
A 1 59 TYR 59 59  59  TYR TYR A . n 
A 1 60 ASP 60 60  60  ASP ASP A . n 
A 1 61 GLN 61 61  61  GLN GLN A . n 
A 1 62 ILE 62 62  62  ILE ILE A . n 
A 1 63 ILE 63 63  63  ILE ILE A . n 
A 1 64 ILE 64 64  64  ILE ILE A . n 
A 1 65 GLU 65 65  65  GLU GLU A . n 
A 1 66 ILE 66 66  66  ILE ILE A . n 
A 1 67 ALA 67 67  67  ALA ALA A . n 
A 1 68 GLY 68 68  68  GLY GLY A . n 
A 1 69 HIS 69 69  69  HIS HIS A . n 
A 1 70 LYS 70 70  70  LYS LYS A . n 
A 1 71 ALA 71 71  71  ALA ALA A . n 
A 1 72 ILE 72 72  72  ILE ILE A . n 
A 1 73 GLY 73 73  73  GLY GLY A . n 
A 1 74 THR 74 74  74  THR THR A . n 
A 1 75 VAL 75 75  75  VAL VAL A . n 
A 1 76 LEU 76 76  76  LEU LEU A . n 
A 1 77 VAL 77 77  77  VAL VAL A . n 
A 1 78 GLY 78 78  78  GLY GLY A . n 
A 1 79 PRO 79 79  79  PRO PRO A . n 
A 1 80 THR 80 80  80  THR THR A . n 
A 1 81 PRO 81 81  81  PRO PRO A . n 
A 1 82 VAL 82 82  82  VAL VAL A . n 
A 1 83 ASN 83 83  83  ASN ASN A . n 
A 1 84 ILE 84 84  84  ILE ILE A . n 
A 1 85 ILE 85 85  85  ILE ILE A . n 
A 1 86 GLY 86 86  86  GLY GLY A . n 
A 1 87 ARG 87 87  87  ARG ARG A . n 
A 1 88 ASN 88 88  88  ASN ASN A . n 
A 1 89 LEU 89 89  89  LEU LEU A . n 
A 1 90 LEU 90 90  90  LEU LEU A . n 
A 1 91 THR 91 91  91  THR THR A . n 
A 1 92 GLN 92 92  92  GLN GLN A . n 
A 1 93 ILE 93 93  93  ILE ILE A . n 
A 1 94 GLY 94 94  94  GLY GLY A . n 
A 1 95 ALA 95 95  95  ALA ALA A . n 
A 1 96 THR 96 96  96  THR THR A . n 
A 1 97 LEU 97 97  97  LEU LEU A . n 
A 1 98 ASN 98 98  98  ASN ASN A . n 
A 1 99 PHE 99 99  99  PHE PHE A . n 
B 1 1  PRO 1  101 101 PRO PRO B . n 
B 1 2  GLN 2  102 102 GLN GLN B . n 
B 1 3  ILE 3  103 103 ILE ILE B . n 
B 1 4  THR 4  104 104 THR THR B . n 
B 1 5  LEU 5  105 105 LEU LEU B . n 
B 1 6  TRP 6  106 106 TRP TRP B . n 
B 1 7  LYS 7  107 107 LYS LYS B . n 
B 1 8  ARG 8  108 108 ARG ARG B . n 
B 1 9  PRO 9  109 109 PRO PRO B . n 
B 1 10 LEU 10 110 110 LEU LEU B . n 
B 1 11 VAL 11 111 111 VAL VAL B . n 
B 1 12 THR 12 112 112 THR THR B . n 
B 1 13 ILE 13 113 113 ILE ILE B . n 
B 1 14 LYS 14 114 114 LYS LYS B . n 
B 1 15 ILE 15 115 115 ILE ILE B . n 
B 1 16 GLY 16 116 116 GLY GLY B . n 
B 1 17 GLY 17 117 117 GLY GLY B . n 
B 1 18 GLN 18 118 118 GLN GLN B . n 
B 1 19 LEU 19 119 119 LEU LEU B . n 
B 1 20 LYS 20 120 120 LYS LYS B . n 
B 1 21 GLU 21 121 121 GLU GLU B . n 
B 1 22 ALA 22 122 122 ALA ALA B . n 
B 1 23 LEU 23 123 123 LEU LEU B . n 
B 1 24 LEU 24 124 124 LEU LEU B . n 
B 1 25 ASP 25 125 125 ASP ASP B . n 
B 1 26 THR 26 126 126 THR THR B . n 
B 1 27 GLY 27 127 127 GLY GLY B . n 
B 1 28 ALA 28 128 128 ALA ALA B . n 
B 1 29 ASP 29 129 129 ASP ASP B . n 
B 1 30 ASP 30 130 130 ASP ASP B . n 
B 1 31 THR 31 131 131 THR THR B . n 
B 1 32 VAL 32 132 132 VAL VAL B . n 
B 1 33 ILE 33 133 133 ILE ILE B . n 
B 1 34 GLU 34 134 134 GLU GLU B . n 
B 1 35 GLU 35 135 135 GLU GLU B . n 
B 1 36 MET 36 136 136 MET MET B . n 
B 1 37 SER 37 137 137 SER SER B . n 
B 1 38 LEU 38 138 138 LEU LEU B . n 
B 1 39 PRO 39 139 139 PRO PRO B . n 
B 1 40 GLY 40 140 140 GLY GLY B . n 
B 1 41 ARG 41 141 141 ARG ARG B . n 
B 1 42 TRP 42 142 142 TRP TRP B . n 
B 1 43 LYS 43 143 143 LYS LYS B . n 
B 1 44 PRO 44 144 144 PRO PRO B . n 
B 1 45 LYS 45 145 145 LYS LYS B . n 
B 1 46 MET 46 146 146 MET MET B . n 
B 1 47 ILE 47 147 147 ILE ILE B . n 
B 1 48 GLY 48 148 148 GLY GLY B . n 
B 1 49 GLY 49 149 149 GLY GLY B . n 
B 1 50 ILE 50 150 150 ILE ILE B . n 
B 1 51 GLY 51 151 151 GLY GLY B . n 
B 1 52 GLY 52 152 152 GLY GLY B . n 
B 1 53 PHE 53 153 153 PHE PHE B . n 
B 1 54 ILE 54 154 154 ILE ILE B . n 
B 1 55 LYS 55 155 155 LYS LYS B . n 
B 1 56 VAL 56 156 156 VAL VAL B . n 
B 1 57 ARG 57 157 157 ARG ARG B . n 
B 1 58 GLN 58 158 158 GLN GLN B . n 
B 1 59 TYR 59 159 159 TYR TYR B . n 
B 1 60 ASP 60 160 160 ASP ASP B . n 
B 1 61 GLN 61 161 161 GLN GLN B . n 
B 1 62 ILE 62 162 162 ILE ILE B . n 
B 1 63 ILE 63 163 163 ILE ILE B . n 
B 1 64 ILE 64 164 164 ILE ILE B . n 
B 1 65 GLU 65 165 165 GLU GLU B . n 
B 1 66 ILE 66 166 166 ILE ILE B . n 
B 1 67 ALA 67 167 167 ALA ALA B . n 
B 1 68 GLY 68 168 168 GLY GLY B . n 
B 1 69 HIS 69 169 169 HIS HIS B . n 
B 1 70 LYS 70 170 170 LYS LYS B . n 
B 1 71 ALA 71 171 171 ALA ALA B . n 
B 1 72 ILE 72 172 172 ILE ILE B . n 
B 1 73 GLY 73 173 173 GLY GLY B . n 
B 1 74 THR 74 174 174 THR THR B . n 
B 1 75 VAL 75 175 175 VAL VAL B . n 
B 1 76 LEU 76 176 176 LEU LEU B . n 
B 1 77 VAL 77 177 177 VAL VAL B . n 
B 1 78 GLY 78 178 178 GLY GLY B . n 
B 1 79 PRO 79 179 179 PRO PRO B . n 
B 1 80 THR 80 180 180 THR THR B . n 
B 1 81 PRO 81 181 181 PRO PRO B . n 
B 1 82 VAL 82 182 182 VAL VAL B . n 
B 1 83 ASN 83 183 183 ASN ASN B . n 
B 1 84 ILE 84 184 184 ILE ILE B . n 
B 1 85 ILE 85 185 185 ILE ILE B . n 
B 1 86 GLY 86 186 186 GLY GLY B . n 
B 1 87 ARG 87 187 187 ARG ARG B . n 
B 1 88 ASN 88 188 188 ASN ASN B . n 
B 1 89 LEU 89 189 189 LEU LEU B . n 
B 1 90 LEU 90 190 190 LEU LEU B . n 
B 1 91 THR 91 191 191 THR THR B . n 
B 1 92 GLN 92 192 192 GLN GLN B . n 
B 1 93 ILE 93 193 193 ILE ILE B . n 
B 1 94 GLY 94 194 194 GLY GLY B . n 
B 1 95 ALA 95 195 195 ALA ALA B . n 
B 1 96 THR 96 196 196 THR THR B . n 
B 1 97 LEU 97 197 197 LEU LEU B . n 
B 1 98 ASN 98 198 198 ASN ASN B . n 
B 1 99 PHE 99 199 199 PHE PHE B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BHV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BHV 
_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 
C 2 A1BHV 1  401 401 A1BHV G11 B . 
D 3 CL    1  402 1   CL    CL  B . 
E 4 HOH   1  101 73  HOH   HOH A . 
E 4 HOH   2  102 79  HOH   HOH A . 
E 4 HOH   3  103 20  HOH   HOH A . 
E 4 HOH   4  104 78  HOH   HOH A . 
E 4 HOH   5  105 83  HOH   HOH A . 
E 4 HOH   6  106 14  HOH   HOH A . 
E 4 HOH   7  107 45  HOH   HOH A . 
E 4 HOH   8  108 8   HOH   HOH A . 
E 4 HOH   9  109 110 HOH   HOH A . 
E 4 HOH   10 110 71  HOH   HOH A . 
E 4 HOH   11 111 38  HOH   HOH A . 
E 4 HOH   12 112 2   HOH   HOH A . 
E 4 HOH   13 113 32  HOH   HOH A . 
E 4 HOH   14 114 6   HOH   HOH A . 
E 4 HOH   15 115 5   HOH   HOH A . 
E 4 HOH   16 116 93  HOH   HOH A . 
E 4 HOH   17 117 85  HOH   HOH A . 
E 4 HOH   18 118 51  HOH   HOH A . 
E 4 HOH   19 119 16  HOH   HOH A . 
E 4 HOH   20 120 46  HOH   HOH A . 
E 4 HOH   21 121 9   HOH   HOH A . 
E 4 HOH   22 122 28  HOH   HOH A . 
E 4 HOH   23 123 76  HOH   HOH A . 
E 4 HOH   24 124 17  HOH   HOH A . 
E 4 HOH   25 125 77  HOH   HOH A . 
E 4 HOH   26 126 40  HOH   HOH A . 
E 4 HOH   27 127 99  HOH   HOH A . 
E 4 HOH   28 128 30  HOH   HOH A . 
E 4 HOH   29 129 92  HOH   HOH A . 
E 4 HOH   30 130 62  HOH   HOH A . 
E 4 HOH   31 131 60  HOH   HOH A . 
E 4 HOH   32 132 61  HOH   HOH A . 
E 4 HOH   33 133 48  HOH   HOH A . 
E 4 HOH   34 134 39  HOH   HOH A . 
E 4 HOH   35 135 18  HOH   HOH A . 
E 4 HOH   36 136 90  HOH   HOH A . 
E 4 HOH   37 137 75  HOH   HOH A . 
E 4 HOH   38 138 15  HOH   HOH A . 
E 4 HOH   39 139 33  HOH   HOH A . 
E 4 HOH   40 140 12  HOH   HOH A . 
E 4 HOH   41 141 10  HOH   HOH A . 
E 4 HOH   42 142 74  HOH   HOH A . 
E 4 HOH   43 143 1   HOH   HOH A . 
E 4 HOH   44 144 87  HOH   HOH A . 
E 4 HOH   45 145 59  HOH   HOH A . 
E 4 HOH   46 146 91  HOH   HOH A . 
E 4 HOH   47 147 104 HOH   HOH A . 
E 4 HOH   48 148 63  HOH   HOH A . 
E 4 HOH   49 149 50  HOH   HOH A . 
E 4 HOH   50 150 81  HOH   HOH A . 
E 4 HOH   51 151 57  HOH   HOH A . 
E 4 HOH   52 152 106 HOH   HOH A . 
E 4 HOH   53 153 97  HOH   HOH A . 
E 4 HOH   54 154 69  HOH   HOH A . 
E 4 HOH   55 155 101 HOH   HOH A . 
E 4 HOH   56 156 96  HOH   HOH A . 
F 4 HOH   1  501 65  HOH   HOH B . 
F 4 HOH   2  502 37  HOH   HOH B . 
F 4 HOH   3  503 35  HOH   HOH B . 
F 4 HOH   4  504 67  HOH   HOH B . 
F 4 HOH   5  505 7   HOH   HOH B . 
F 4 HOH   6  506 34  HOH   HOH B . 
F 4 HOH   7  507 36  HOH   HOH B . 
F 4 HOH   8  508 4   HOH   HOH B . 
F 4 HOH   9  509 19  HOH   HOH B . 
F 4 HOH   10 510 22  HOH   HOH B . 
F 4 HOH   11 511 3   HOH   HOH B . 
F 4 HOH   12 512 26  HOH   HOH B . 
F 4 HOH   13 513 102 HOH   HOH B . 
F 4 HOH   14 514 13  HOH   HOH B . 
F 4 HOH   15 515 31  HOH   HOH B . 
F 4 HOH   16 516 25  HOH   HOH B . 
F 4 HOH   17 517 42  HOH   HOH B . 
F 4 HOH   18 518 68  HOH   HOH B . 
F 4 HOH   19 519 29  HOH   HOH B . 
F 4 HOH   20 520 94  HOH   HOH B . 
F 4 HOH   21 521 24  HOH   HOH B . 
F 4 HOH   22 522 58  HOH   HOH B . 
F 4 HOH   23 523 52  HOH   HOH B . 
F 4 HOH   24 524 11  HOH   HOH B . 
F 4 HOH   25 525 23  HOH   HOH B . 
F 4 HOH   26 526 84  HOH   HOH B . 
F 4 HOH   27 527 53  HOH   HOH B . 
F 4 HOH   28 528 44  HOH   HOH B . 
F 4 HOH   29 529 21  HOH   HOH B . 
F 4 HOH   30 530 49  HOH   HOH B . 
F 4 HOH   31 531 43  HOH   HOH B . 
F 4 HOH   32 532 54  HOH   HOH B . 
F 4 HOH   33 533 27  HOH   HOH B . 
F 4 HOH   34 534 56  HOH   HOH B . 
F 4 HOH   35 535 64  HOH   HOH B . 
F 4 HOH   36 536 105 HOH   HOH B . 
F 4 HOH   37 537 55  HOH   HOH B . 
F 4 HOH   38 538 86  HOH   HOH B . 
F 4 HOH   39 539 89  HOH   HOH B . 
F 4 HOH   40 540 111 HOH   HOH B . 
F 4 HOH   41 541 108 HOH   HOH B . 
F 4 HOH   42 542 109 HOH   HOH B . 
F 4 HOH   43 543 82  HOH   HOH B . 
F 4 HOH   44 544 41  HOH   HOH B . 
F 4 HOH   45 545 88  HOH   HOH B . 
F 4 HOH   46 546 70  HOH   HOH B . 
F 4 HOH   47 547 100 HOH   HOH B . 
F 4 HOH   48 548 72  HOH   HOH B . 
F 4 HOH   49 549 66  HOH   HOH B . 
F 4 HOH   50 550 103 HOH   HOH B . 
F 4 HOH   51 551 98  HOH   HOH B . 
F 4 HOH   52 552 95  HOH   HOH B . 
F 4 HOH   53 553 80  HOH   HOH B . 
F 4 HOH   54 554 107 HOH   HOH B . 
# 
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      ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EEG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.034 
_cell.length_a_esd                 ? 
_cell.length_b                     87.576 
_cell.length_b_esd                 ? 
_cell.length_c                     46.315 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9EEG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 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                   9EEG 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.60 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.0 
_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    '0.1 M MES, 0.7-1.0 M sodium chloride, pH 6.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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                         'DECTRIS EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-09-06 
_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   1.56 
_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                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.56 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EEG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               87.58 
_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                                     27513 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.70 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.956 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.067 
_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                                    1.70 
_reflns_shell.d_res_low                                     1.76 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.35 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2733 
_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                               6.7 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.649 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.721 
_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                               ? 
_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                                 9EEG 
_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                            1.70 
_refine.ls_d_res_low                             26.25 
_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                     27441 
_refine.ls_number_reflns_R_free                  1322 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.53 
_refine.ls_percent_reflns_R_free                 4.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1779 
_refine.ls_R_factor_R_free                       0.2062 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1765 
_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       ML 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 22.85 
_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                            0.21 
_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.pdbx_number_atoms_protein        1512 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             110 
_refine_hist.number_atoms_total               1666 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        26.25 
# 
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' ? 0.010  ? 1664 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.120  ? 2274 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.681 ? 235  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.086  ? 271  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 282  ? f_plane_restr      ? ? 
# 
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' 1.70 1.77  . . 153 2837 99.00  . . . . 0.2959 . . . . . . . . . . . 0.3596 
'X-RAY DIFFRACTION' 1.77 1.85  . . 131 2851 100.00 . . . . 0.2568 . . . . . . . . . . . 0.2756 
'X-RAY DIFFRACTION' 1.85 1.95  . . 158 2858 100.00 . . . . 0.2214 . . . . . . . . . . . 0.2779 
'X-RAY DIFFRACTION' 1.95 2.07  . . 147 2859 100.00 . . . . 0.1864 . . . . . . . . . . . 0.2125 
'X-RAY DIFFRACTION' 2.07 2.23  . . 140 2890 100.00 . . . . 0.1800 . . . . . . . . . . . 0.2121 
'X-RAY DIFFRACTION' 2.23 2.45  . . 162 2872 100.00 . . . . 0.1849 . . . . . . . . . . . 0.2780 
'X-RAY DIFFRACTION' 2.45 2.81  . . 157 2910 100.00 . . . . 0.1876 . . . . . . . . . . . 0.2059 
'X-RAY DIFFRACTION' 2.81 3.53  . . 127 2981 100.00 . . . . 0.1697 . . . . . . . . . . . 0.2165 
'X-RAY DIFFRACTION' 3.53 26.25 . . 147 3061 99.00  . . . . 0.1500 . . . . . . . . . . . 0.1537 
# 
_struct.entry_id                     9EEG 
_struct.title                        'Room-temperature X-ray structure of HIV-1 protease in complex with GRL-11124A inhibitor' 
_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        9EEG 
_struct_keywords.text            'HIV-1 protease, homodimer, inhibitor complex, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/INHIBITOR 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q5RZ08_9HIV1 
_struct_ref.pdbx_db_accession          Q5RZ08 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPT
PVNIIGRNLLTQIGCTLNF
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EEG A 1 ? 99 ? Q5RZ08 1 ? 99 ? 1   99  
2 1 9EEG B 1 ? 99 ? Q5RZ08 1 ? 99 ? 101 199 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EEG LYS A 7  ? UNP Q5RZ08 GLN 7  'engineered mutation' 7   1  
1 9EEG ILE A 33 ? UNP Q5RZ08 LEU 33 'engineered mutation' 33  2  
1 9EEG ILE A 63 ? UNP Q5RZ08 LEU 63 'engineered mutation' 63  3  
1 9EEG ALA A 67 ? UNP Q5RZ08 CYS 67 'engineered mutation' 67  4  
1 9EEG ALA A 95 ? UNP Q5RZ08 CYS 95 'engineered mutation' 95  5  
2 9EEG LYS B 7  ? UNP Q5RZ08 GLN 7  'engineered mutation' 107 6  
2 9EEG ILE B 33 ? UNP Q5RZ08 LEU 33 'engineered mutation' 133 7  
2 9EEG ILE B 63 ? UNP Q5RZ08 LEU 63 'engineered mutation' 163 8  
2 9EEG ALA B 67 ? UNP Q5RZ08 CYS 67 'engineered mutation' 167 9  
2 9EEG ALA B 95 ? UNP Q5RZ08 CYS 95 'engineered mutation' 195 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4200 ? 
1 MORE         -30  ? 
1 'SSA (A^2)'  9580 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 86 ? THR A 91 ? GLY A 86  THR A 91  1 ? 6 
HELX_P HELX_P2 AA2 GLY B 86 ? THR B 91 ? GLY B 186 THR B 191 1 ? 6 
HELX_P HELX_P3 AA3 GLN B 92 ? GLY B 94 ? GLN B 192 GLY B 194 5 ? 3 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
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 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? parallel      
AA3 6 7 ? anti-parallel 
AA3 7 8 ? 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 GLN A 2  ? ILE A 3  ? GLN A 2   ILE A 3   
AA1 2 THR B 96 ? ASN B 98 ? THR B 196 ASN B 198 
AA1 3 THR A 96 ? ASN A 98 ? THR A 96  ASN A 98  
AA1 4 GLN B 2  ? ILE B 3  ? GLN B 102 ILE B 103 
AA2 1 LYS A 43 ? GLY A 49 ? LYS A 43  GLY A 49  
AA2 2 GLY A 52 ? ILE A 66 ? GLY A 52  ILE A 66  
AA2 3 HIS A 69 ? VAL A 77 ? HIS A 69  VAL A 77  
AA2 4 VAL A 32 ? ILE A 33 ? VAL A 32  ILE A 33  
AA2 5 ILE A 84 ? ILE A 85 ? ILE A 84  ILE A 85  
AA2 6 GLN A 18 ? LEU A 24 ? GLN A 18  LEU A 24  
AA2 7 LEU A 10 ? ILE A 15 ? LEU A 10  ILE A 15  
AA2 8 GLY A 52 ? ILE A 66 ? GLY A 52  ILE A 66  
AA3 1 LYS B 43 ? GLY B 49 ? LYS B 143 GLY B 149 
AA3 2 GLY B 52 ? ILE B 66 ? GLY B 152 ILE B 166 
AA3 3 HIS B 69 ? VAL B 77 ? HIS B 169 VAL B 177 
AA3 4 THR B 31 ? ILE B 33 ? THR B 131 ILE B 133 
AA3 5 ILE B 84 ? ILE B 85 ? ILE B 184 ILE B 185 
AA3 6 GLN B 18 ? LEU B 24 ? GLN B 118 LEU B 124 
AA3 7 LEU B 10 ? ILE B 15 ? LEU B 110 ILE B 115 
AA3 8 GLY B 52 ? ILE B 66 ? GLY B 152 ILE B 166 
# 
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 ILE A 3  ? N ILE A 3   O LEU B 97 ? O LEU B 197 
AA1 2 3 O THR B 96 ? O THR B 196 N ASN A 98 ? N ASN A 98  
AA1 3 4 N LEU A 97 ? N LEU A 97  O ILE B 3  ? O ILE B 103 
AA2 1 2 N LYS A 43 ? N LYS A 43  O GLN A 58 ? O GLN A 58  
AA2 2 3 N ILE A 66 ? N ILE A 66  O HIS A 69 ? O HIS A 69  
AA2 3 4 O LEU A 76 ? O LEU A 76  N ILE A 33 ? N ILE A 33  
AA2 4 5 N VAL A 32 ? N VAL A 32  O ILE A 84 ? O ILE A 84  
AA2 5 6 O ILE A 85 ? O ILE A 85  N LEU A 23 ? N LEU A 23  
AA2 6 7 O LYS A 20 ? O LYS A 20  N ILE A 13 ? N ILE A 13  
AA2 7 8 N LYS A 14 ? N LYS A 14  O GLU A 65 ? O GLU A 65  
AA3 1 2 N LYS B 43 ? N LYS B 143 O GLN B 58 ? O GLN B 158 
AA3 2 3 N ILE B 66 ? N ILE B 166 O HIS B 69 ? O HIS B 169 
AA3 3 4 O LEU B 76 ? O LEU B 176 N ILE B 33 ? N ILE B 133 
AA3 4 5 N VAL B 32 ? N VAL B 132 O ILE B 84 ? O ILE B 184 
AA3 5 6 O ILE B 85 ? O ILE B 185 N LEU B 23 ? N LEU B 123 
AA3 6 7 O LYS B 20 ? O LYS B 120 N ILE B 13 ? N ILE B 113 
AA3 7 8 N LYS B 14 ? N LYS B 114 O GLU B 65 ? O GLU B 165 
# 
_pdbx_entry_details.entry_id                   9EEG 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
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 
A1BHV C2   C  N N 1   
A1BHV C4   C  N S 2   
A1BHV C5   C  N R 3   
A1BHV C9   C  N N 4   
A1BHV C12  C  N N 5   
A1BHV C13  C  N N 6   
A1BHV C14  C  N N 7   
A1BHV O16  O  N N 8   
A1BHV C18  C  Y N 9   
A1BHV C21  C  Y N 10  
A1BHV C22  C  Y N 11  
A1BHV C23  C  Y N 12  
A1BHV C25  C  Y N 13  
A1BHV C26  C  Y N 14  
A1BHV C15  C  N N 15  
A1BHV C19  C  Y N 16  
A1BHV C20  C  Y N 17  
A1BHV C27  C  Y N 18  
A1BHV C28  C  Y N 19  
A1BHV C29  C  Y N 20  
A1BHV C30  C  Y N 21  
A1BHV C31  C  N N 22  
A1BHV C32  C  N R 23  
A1BHV C33  C  N N 24  
A1BHV C34  C  N N 25  
A1BHV C35  C  N R 26  
A1BHV C36  C  N N 27  
A1BHV C37  C  N S 28  
A1BHV C38  C  N S 29  
A1BHV C39  C  N N 30  
A1BHV C41  C  N S 31  
A1BHV C43  C  N N 32  
A1BHV C6   C  N N 33  
A1BHV N3   N  N N 34  
A1BHV N7   N  N N 35  
A1BHV O1   O  N N 36  
A1BHV O10  O  N N 37  
A1BHV O17  O  N N 38  
A1BHV O24  O  N N 39  
A1BHV O40  O  N N 40  
A1BHV O42  O  N N 41  
A1BHV O8   O  N N 42  
A1BHV S11  S  N N 43  
A1BHV H1   H  N N 44  
A1BHV H2   H  N N 45  
A1BHV H3   H  N N 46  
A1BHV H4   H  N N 47  
A1BHV H5   H  N N 48  
A1BHV H6   H  N N 49  
A1BHV H7   H  N N 50  
A1BHV H8   H  N N 51  
A1BHV H9   H  N N 52  
A1BHV H10  H  N N 53  
A1BHV H11  H  N N 54  
A1BHV H12  H  N N 55  
A1BHV H13  H  N N 56  
A1BHV H14  H  N N 57  
A1BHV H15  H  N N 58  
A1BHV H16  H  N N 59  
A1BHV H17  H  N N 60  
A1BHV H18  H  N N 61  
A1BHV H19  H  N N 62  
A1BHV H20  H  N N 63  
A1BHV H21  H  N N 64  
A1BHV H22  H  N N 65  
A1BHV H23  H  N N 66  
A1BHV H24  H  N N 67  
A1BHV H25  H  N N 68  
A1BHV H26  H  N N 69  
A1BHV H27  H  N N 70  
A1BHV H28  H  N N 71  
A1BHV H29  H  N N 72  
A1BHV H30  H  N N 73  
A1BHV H31  H  N N 74  
A1BHV H32  H  N N 75  
A1BHV H33  H  N N 76  
A1BHV H34  H  N N 77  
A1BHV H35  H  N N 78  
A1BHV H36  H  N N 79  
A1BHV H37  H  N N 80  
A1BHV H38  H  N N 81  
A1BHV H39  H  N N 82  
A1BHV H40  H  N N 83  
A1BHV H41  H  N N 84  
A1BHV H42  H  N N 85  
A1BHV H43  H  N N 86  
A1BHV H44  H  N N 87  
ALA   N    N  N N 88  
ALA   CA   C  N S 89  
ALA   C    C  N N 90  
ALA   O    O  N N 91  
ALA   CB   C  N N 92  
ALA   OXT  O  N N 93  
ALA   H    H  N N 94  
ALA   H2   H  N N 95  
ALA   HA   H  N N 96  
ALA   HB1  H  N N 97  
ALA   HB2  H  N N 98  
ALA   HB3  H  N N 99  
ALA   HXT  H  N N 100 
ARG   N    N  N N 101 
ARG   CA   C  N S 102 
ARG   C    C  N N 103 
ARG   O    O  N N 104 
ARG   CB   C  N N 105 
ARG   CG   C  N N 106 
ARG   CD   C  N N 107 
ARG   NE   N  N N 108 
ARG   CZ   C  N N 109 
ARG   NH1  N  N N 110 
ARG   NH2  N  N N 111 
ARG   OXT  O  N N 112 
ARG   H    H  N N 113 
ARG   H2   H  N N 114 
ARG   HA   H  N N 115 
ARG   HB2  H  N N 116 
ARG   HB3  H  N N 117 
ARG   HG2  H  N N 118 
ARG   HG3  H  N N 119 
ARG   HD2  H  N N 120 
ARG   HD3  H  N N 121 
ARG   HE   H  N N 122 
ARG   HH11 H  N N 123 
ARG   HH12 H  N N 124 
ARG   HH21 H  N N 125 
ARG   HH22 H  N N 126 
ARG   HXT  H  N N 127 
ASN   N    N  N N 128 
ASN   CA   C  N S 129 
ASN   C    C  N N 130 
ASN   O    O  N N 131 
ASN   CB   C  N N 132 
ASN   CG   C  N N 133 
ASN   OD1  O  N N 134 
ASN   ND2  N  N N 135 
ASN   OXT  O  N N 136 
ASN   H    H  N N 137 
ASN   H2   H  N N 138 
ASN   HA   H  N N 139 
ASN   HB2  H  N N 140 
ASN   HB3  H  N N 141 
ASN   HD21 H  N N 142 
ASN   HD22 H  N N 143 
ASN   HXT  H  N N 144 
ASP   N    N  N N 145 
ASP   CA   C  N S 146 
ASP   C    C  N N 147 
ASP   O    O  N N 148 
ASP   CB   C  N N 149 
ASP   CG   C  N N 150 
ASP   OD1  O  N N 151 
ASP   OD2  O  N N 152 
ASP   OXT  O  N N 153 
ASP   H    H  N N 154 
ASP   H2   H  N N 155 
ASP   HA   H  N N 156 
ASP   HB2  H  N N 157 
ASP   HB3  H  N N 158 
ASP   HD2  H  N N 159 
ASP   HXT  H  N N 160 
CL    CL   CL N N 161 
CYS   N    N  N N 162 
CYS   CA   C  N R 163 
CYS   C    C  N N 164 
CYS   O    O  N N 165 
CYS   CB   C  N N 166 
CYS   SG   S  N N 167 
CYS   OXT  O  N N 168 
CYS   H    H  N N 169 
CYS   H2   H  N N 170 
CYS   HA   H  N N 171 
CYS   HB2  H  N N 172 
CYS   HB3  H  N N 173 
CYS   HG   H  N N 174 
CYS   HXT  H  N N 175 
GLN   N    N  N N 176 
GLN   CA   C  N S 177 
GLN   C    C  N N 178 
GLN   O    O  N N 179 
GLN   CB   C  N N 180 
GLN   CG   C  N N 181 
GLN   CD   C  N N 182 
GLN   OE1  O  N N 183 
GLN   NE2  N  N N 184 
GLN   OXT  O  N N 185 
GLN   H    H  N N 186 
GLN   H2   H  N N 187 
GLN   HA   H  N N 188 
GLN   HB2  H  N N 189 
GLN   HB3  H  N N 190 
GLN   HG2  H  N N 191 
GLN   HG3  H  N N 192 
GLN   HE21 H  N N 193 
GLN   HE22 H  N N 194 
GLN   HXT  H  N N 195 
GLU   N    N  N N 196 
GLU   CA   C  N S 197 
GLU   C    C  N N 198 
GLU   O    O  N N 199 
GLU   CB   C  N N 200 
GLU   CG   C  N N 201 
GLU   CD   C  N N 202 
GLU   OE1  O  N N 203 
GLU   OE2  O  N N 204 
GLU   OXT  O  N N 205 
GLU   H    H  N N 206 
GLU   H2   H  N N 207 
GLU   HA   H  N N 208 
GLU   HB2  H  N N 209 
GLU   HB3  H  N N 210 
GLU   HG2  H  N N 211 
GLU   HG3  H  N N 212 
GLU   HE2  H  N N 213 
GLU   HXT  H  N N 214 
GLY   N    N  N N 215 
GLY   CA   C  N N 216 
GLY   C    C  N N 217 
GLY   O    O  N N 218 
GLY   OXT  O  N N 219 
GLY   H    H  N N 220 
GLY   H2   H  N N 221 
GLY   HA2  H  N N 222 
GLY   HA3  H  N N 223 
GLY   HXT  H  N N 224 
HIS   N    N  N N 225 
HIS   CA   C  N S 226 
HIS   C    C  N N 227 
HIS   O    O  N N 228 
HIS   CB   C  N N 229 
HIS   CG   C  Y N 230 
HIS   ND1  N  Y N 231 
HIS   CD2  C  Y N 232 
HIS   CE1  C  Y N 233 
HIS   NE2  N  Y N 234 
HIS   OXT  O  N N 235 
HIS   H    H  N N 236 
HIS   H2   H  N N 237 
HIS   HA   H  N N 238 
HIS   HB2  H  N N 239 
HIS   HB3  H  N N 240 
HIS   HD1  H  N N 241 
HIS   HD2  H  N N 242 
HIS   HE1  H  N N 243 
HIS   HE2  H  N N 244 
HIS   HXT  H  N N 245 
HOH   O    O  N N 246 
HOH   H1   H  N N 247 
HOH   H2   H  N N 248 
ILE   N    N  N N 249 
ILE   CA   C  N S 250 
ILE   C    C  N N 251 
ILE   O    O  N N 252 
ILE   CB   C  N S 253 
ILE   CG1  C  N N 254 
ILE   CG2  C  N N 255 
ILE   CD1  C  N N 256 
ILE   OXT  O  N N 257 
ILE   H    H  N N 258 
ILE   H2   H  N N 259 
ILE   HA   H  N N 260 
ILE   HB   H  N N 261 
ILE   HG12 H  N N 262 
ILE   HG13 H  N N 263 
ILE   HG21 H  N N 264 
ILE   HG22 H  N N 265 
ILE   HG23 H  N N 266 
ILE   HD11 H  N N 267 
ILE   HD12 H  N N 268 
ILE   HD13 H  N N 269 
ILE   HXT  H  N N 270 
LEU   N    N  N N 271 
LEU   CA   C  N S 272 
LEU   C    C  N N 273 
LEU   O    O  N N 274 
LEU   CB   C  N N 275 
LEU   CG   C  N N 276 
LEU   CD1  C  N N 277 
LEU   CD2  C  N N 278 
LEU   OXT  O  N N 279 
LEU   H    H  N N 280 
LEU   H2   H  N N 281 
LEU   HA   H  N N 282 
LEU   HB2  H  N N 283 
LEU   HB3  H  N N 284 
LEU   HG   H  N N 285 
LEU   HD11 H  N N 286 
LEU   HD12 H  N N 287 
LEU   HD13 H  N N 288 
LEU   HD21 H  N N 289 
LEU   HD22 H  N N 290 
LEU   HD23 H  N N 291 
LEU   HXT  H  N N 292 
LYS   N    N  N N 293 
LYS   CA   C  N S 294 
LYS   C    C  N N 295 
LYS   O    O  N N 296 
LYS   CB   C  N N 297 
LYS   CG   C  N N 298 
LYS   CD   C  N N 299 
LYS   CE   C  N N 300 
LYS   NZ   N  N N 301 
LYS   OXT  O  N N 302 
LYS   H    H  N N 303 
LYS   H2   H  N N 304 
LYS   HA   H  N N 305 
LYS   HB2  H  N N 306 
LYS   HB3  H  N N 307 
LYS   HG2  H  N N 308 
LYS   HG3  H  N N 309 
LYS   HD2  H  N N 310 
LYS   HD3  H  N N 311 
LYS   HE2  H  N N 312 
LYS   HE3  H  N N 313 
LYS   HZ1  H  N N 314 
LYS   HZ2  H  N N 315 
LYS   HZ3  H  N N 316 
LYS   HXT  H  N N 317 
MET   N    N  N N 318 
MET   CA   C  N S 319 
MET   C    C  N N 320 
MET   O    O  N N 321 
MET   CB   C  N N 322 
MET   CG   C  N N 323 
MET   SD   S  N N 324 
MET   CE   C  N N 325 
MET   OXT  O  N N 326 
MET   H    H  N N 327 
MET   H2   H  N N 328 
MET   HA   H  N N 329 
MET   HB2  H  N N 330 
MET   HB3  H  N N 331 
MET   HG2  H  N N 332 
MET   HG3  H  N N 333 
MET   HE1  H  N N 334 
MET   HE2  H  N N 335 
MET   HE3  H  N N 336 
MET   HXT  H  N N 337 
PHE   N    N  N N 338 
PHE   CA   C  N S 339 
PHE   C    C  N N 340 
PHE   O    O  N N 341 
PHE   CB   C  N N 342 
PHE   CG   C  Y N 343 
PHE   CD1  C  Y N 344 
PHE   CD2  C  Y N 345 
PHE   CE1  C  Y N 346 
PHE   CE2  C  Y N 347 
PHE   CZ   C  Y N 348 
PHE   OXT  O  N N 349 
PHE   H    H  N N 350 
PHE   H2   H  N N 351 
PHE   HA   H  N N 352 
PHE   HB2  H  N N 353 
PHE   HB3  H  N N 354 
PHE   HD1  H  N N 355 
PHE   HD2  H  N N 356 
PHE   HE1  H  N N 357 
PHE   HE2  H  N N 358 
PHE   HZ   H  N N 359 
PHE   HXT  H  N N 360 
PRO   N    N  N N 361 
PRO   CA   C  N S 362 
PRO   C    C  N N 363 
PRO   O    O  N N 364 
PRO   CB   C  N N 365 
PRO   CG   C  N N 366 
PRO   CD   C  N N 367 
PRO   OXT  O  N N 368 
PRO   H    H  N N 369 
PRO   HA   H  N N 370 
PRO   HB2  H  N N 371 
PRO   HB3  H  N N 372 
PRO   HG2  H  N N 373 
PRO   HG3  H  N N 374 
PRO   HD2  H  N N 375 
PRO   HD3  H  N N 376 
PRO   HXT  H  N N 377 
SER   N    N  N N 378 
SER   CA   C  N S 379 
SER   C    C  N N 380 
SER   O    O  N N 381 
SER   CB   C  N N 382 
SER   OG   O  N N 383 
SER   OXT  O  N N 384 
SER   H    H  N N 385 
SER   H2   H  N N 386 
SER   HA   H  N N 387 
SER   HB2  H  N N 388 
SER   HB3  H  N N 389 
SER   HG   H  N N 390 
SER   HXT  H  N N 391 
THR   N    N  N N 392 
THR   CA   C  N S 393 
THR   C    C  N N 394 
THR   O    O  N N 395 
THR   CB   C  N R 396 
THR   OG1  O  N N 397 
THR   CG2  C  N N 398 
THR   OXT  O  N N 399 
THR   H    H  N N 400 
THR   H2   H  N N 401 
THR   HA   H  N N 402 
THR   HB   H  N N 403 
THR   HG1  H  N N 404 
THR   HG21 H  N N 405 
THR   HG22 H  N N 406 
THR   HG23 H  N N 407 
THR   HXT  H  N N 408 
TRP   N    N  N N 409 
TRP   CA   C  N S 410 
TRP   C    C  N N 411 
TRP   O    O  N N 412 
TRP   CB   C  N N 413 
TRP   CG   C  Y N 414 
TRP   CD1  C  Y N 415 
TRP   CD2  C  Y N 416 
TRP   NE1  N  Y N 417 
TRP   CE2  C  Y N 418 
TRP   CE3  C  Y N 419 
TRP   CZ2  C  Y N 420 
TRP   CZ3  C  Y N 421 
TRP   CH2  C  Y N 422 
TRP   OXT  O  N N 423 
TRP   H    H  N N 424 
TRP   H2   H  N N 425 
TRP   HA   H  N N 426 
TRP   HB2  H  N N 427 
TRP   HB3  H  N N 428 
TRP   HD1  H  N N 429 
TRP   HE1  H  N N 430 
TRP   HE3  H  N N 431 
TRP   HZ2  H  N N 432 
TRP   HZ3  H  N N 433 
TRP   HH2  H  N N 434 
TRP   HXT  H  N N 435 
TYR   N    N  N N 436 
TYR   CA   C  N S 437 
TYR   C    C  N N 438 
TYR   O    O  N N 439 
TYR   CB   C  N N 440 
TYR   CG   C  Y N 441 
TYR   CD1  C  Y N 442 
TYR   CD2  C  Y N 443 
TYR   CE1  C  Y N 444 
TYR   CE2  C  Y N 445 
TYR   CZ   C  Y N 446 
TYR   OH   O  N N 447 
TYR   OXT  O  N N 448 
TYR   H    H  N N 449 
TYR   H2   H  N N 450 
TYR   HA   H  N N 451 
TYR   HB2  H  N N 452 
TYR   HB3  H  N N 453 
TYR   HD1  H  N N 454 
TYR   HD2  H  N N 455 
TYR   HE1  H  N N 456 
TYR   HE2  H  N N 457 
TYR   HH   H  N N 458 
TYR   HXT  H  N N 459 
VAL   N    N  N N 460 
VAL   CA   C  N S 461 
VAL   C    C  N N 462 
VAL   O    O  N N 463 
VAL   CB   C  N N 464 
VAL   CG1  C  N N 465 
VAL   CG2  C  N N 466 
VAL   OXT  O  N N 467 
VAL   H    H  N N 468 
VAL   H2   H  N N 469 
VAL   HA   H  N N 470 
VAL   HB   H  N N 471 
VAL   HG11 H  N N 472 
VAL   HG12 H  N N 473 
VAL   HG13 H  N N 474 
VAL   HG21 H  N N 475 
VAL   HG22 H  N N 476 
VAL   HG23 H  N N 477 
VAL   HXT  H  N N 478 
# 
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 
A1BHV C39 O40  sing N N 1   
A1BHV C39 C37  sing N N 2   
A1BHV C15 C13  sing N N 3   
A1BHV O40 C41  sing N N 4   
A1BHV C13 C14  sing N N 5   
A1BHV C13 C12  sing N N 6   
A1BHV C37 C36  sing N N 7   
A1BHV C37 C38  sing N N 8   
A1BHV C41 C43  sing N N 9   
A1BHV C41 C38  sing N N 10  
A1BHV C36 C35  sing N N 11  
A1BHV C38 O42  sing N N 12  
A1BHV C38 C32  sing N N 13  
A1BHV C12 N7   sing N N 14  
A1BHV O10 C5   sing N N 15  
A1BHV O42 C35  sing N N 16  
A1BHV C5  C6   sing N N 17  
A1BHV C5  C4   sing N N 18  
A1BHV C35 C34  sing N N 19  
A1BHV O1  C2   sing N N 20  
A1BHV O1  C32  sing N N 21  
A1BHV N3  C2   sing N N 22  
A1BHV N3  C4   sing N N 23  
A1BHV C2  O8   doub N N 24  
A1BHV N7  C6   sing N N 25  
A1BHV N7  S11  sing N N 26  
A1BHV C32 C33  sing N N 27  
A1BHV C4  C9   sing N N 28  
A1BHV C33 C34  sing N N 29  
A1BHV O16 S11  doub N N 30  
A1BHV C23 C22  doub Y N 31  
A1BHV C23 C18  sing Y N 32  
A1BHV S11 C18  sing N N 33  
A1BHV S11 O17  doub N N 34  
A1BHV C22 C21  sing Y N 35  
A1BHV C9  C25  sing N N 36  
A1BHV C18 C19  doub Y N 37  
A1BHV C31 O24  sing N N 38  
A1BHV C21 O24  sing N N 39  
A1BHV C21 C20  doub Y N 40  
A1BHV C19 C20  sing Y N 41  
A1BHV C25 C26  doub Y N 42  
A1BHV C25 C30  sing Y N 43  
A1BHV C26 C27  sing Y N 44  
A1BHV C30 C29  doub Y N 45  
A1BHV C27 C28  doub Y N 46  
A1BHV C29 C28  sing Y N 47  
A1BHV C4  H1   sing N N 48  
A1BHV C5  H2   sing N N 49  
A1BHV C9  H3   sing N N 50  
A1BHV C9  H4   sing N N 51  
A1BHV C12 H5   sing N N 52  
A1BHV C12 H6   sing N N 53  
A1BHV C13 H7   sing N N 54  
A1BHV C14 H8   sing N N 55  
A1BHV C14 H9   sing N N 56  
A1BHV C14 H10  sing N N 57  
A1BHV C22 H11  sing N N 58  
A1BHV C23 H12  sing N N 59  
A1BHV C26 H13  sing N N 60  
A1BHV C15 H14  sing N N 61  
A1BHV C15 H15  sing N N 62  
A1BHV C15 H16  sing N N 63  
A1BHV C19 H17  sing N N 64  
A1BHV C20 H18  sing N N 65  
A1BHV C27 H19  sing N N 66  
A1BHV C28 H20  sing N N 67  
A1BHV C29 H21  sing N N 68  
A1BHV C30 H22  sing N N 69  
A1BHV C31 H23  sing N N 70  
A1BHV C31 H24  sing N N 71  
A1BHV C31 H25  sing N N 72  
A1BHV C32 H26  sing N N 73  
A1BHV C33 H27  sing N N 74  
A1BHV C33 H28  sing N N 75  
A1BHV C34 H29  sing N N 76  
A1BHV C34 H30  sing N N 77  
A1BHV C35 H31  sing N N 78  
A1BHV C36 H32  sing N N 79  
A1BHV C36 H33  sing N N 80  
A1BHV C37 H34  sing N N 81  
A1BHV C39 H35  sing N N 82  
A1BHV C39 H36  sing N N 83  
A1BHV C41 H37  sing N N 84  
A1BHV C43 H38  sing N N 85  
A1BHV C43 H39  sing N N 86  
A1BHV C43 H40  sing N N 87  
A1BHV C6  H41  sing N N 88  
A1BHV C6  H42  sing N N 89  
A1BHV N3  H43  sing N N 90  
A1BHV O10 H44  sing N N 91  
ALA   N   CA   sing N N 92  
ALA   N   H    sing N N 93  
ALA   N   H2   sing N N 94  
ALA   CA  C    sing N N 95  
ALA   CA  CB   sing N N 96  
ALA   CA  HA   sing N N 97  
ALA   C   O    doub N N 98  
ALA   C   OXT  sing N N 99  
ALA   CB  HB1  sing N N 100 
ALA   CB  HB2  sing N N 101 
ALA   CB  HB3  sing N N 102 
ALA   OXT HXT  sing N N 103 
ARG   N   CA   sing N N 104 
ARG   N   H    sing N N 105 
ARG   N   H2   sing N N 106 
ARG   CA  C    sing N N 107 
ARG   CA  CB   sing N N 108 
ARG   CA  HA   sing N N 109 
ARG   C   O    doub N N 110 
ARG   C   OXT  sing N N 111 
ARG   CB  CG   sing N N 112 
ARG   CB  HB2  sing N N 113 
ARG   CB  HB3  sing N N 114 
ARG   CG  CD   sing N N 115 
ARG   CG  HG2  sing N N 116 
ARG   CG  HG3  sing N N 117 
ARG   CD  NE   sing N N 118 
ARG   CD  HD2  sing N N 119 
ARG   CD  HD3  sing N N 120 
ARG   NE  CZ   sing N N 121 
ARG   NE  HE   sing N N 122 
ARG   CZ  NH1  sing N N 123 
ARG   CZ  NH2  doub N N 124 
ARG   NH1 HH11 sing N N 125 
ARG   NH1 HH12 sing N N 126 
ARG   NH2 HH21 sing N N 127 
ARG   NH2 HH22 sing N N 128 
ARG   OXT HXT  sing N N 129 
ASN   N   CA   sing N N 130 
ASN   N   H    sing N N 131 
ASN   N   H2   sing N N 132 
ASN   CA  C    sing N N 133 
ASN   CA  CB   sing N N 134 
ASN   CA  HA   sing N N 135 
ASN   C   O    doub N N 136 
ASN   C   OXT  sing N N 137 
ASN   CB  CG   sing N N 138 
ASN   CB  HB2  sing N N 139 
ASN   CB  HB3  sing N N 140 
ASN   CG  OD1  doub N N 141 
ASN   CG  ND2  sing N N 142 
ASN   ND2 HD21 sing N N 143 
ASN   ND2 HD22 sing N N 144 
ASN   OXT HXT  sing N N 145 
ASP   N   CA   sing N N 146 
ASP   N   H    sing N N 147 
ASP   N   H2   sing N N 148 
ASP   CA  C    sing N N 149 
ASP   CA  CB   sing N N 150 
ASP   CA  HA   sing N N 151 
ASP   C   O    doub N N 152 
ASP   C   OXT  sing N N 153 
ASP   CB  CG   sing N N 154 
ASP   CB  HB2  sing N N 155 
ASP   CB  HB3  sing N N 156 
ASP   CG  OD1  doub N N 157 
ASP   CG  OD2  sing N N 158 
ASP   OD2 HD2  sing N N 159 
ASP   OXT HXT  sing N N 160 
CYS   N   CA   sing N N 161 
CYS   N   H    sing N N 162 
CYS   N   H2   sing N N 163 
CYS   CA  C    sing N N 164 
CYS   CA  CB   sing N N 165 
CYS   CA  HA   sing N N 166 
CYS   C   O    doub N N 167 
CYS   C   OXT  sing N N 168 
CYS   CB  SG   sing N N 169 
CYS   CB  HB2  sing N N 170 
CYS   CB  HB3  sing N N 171 
CYS   SG  HG   sing N N 172 
CYS   OXT HXT  sing N N 173 
GLN   N   CA   sing N N 174 
GLN   N   H    sing N N 175 
GLN   N   H2   sing N N 176 
GLN   CA  C    sing N N 177 
GLN   CA  CB   sing N N 178 
GLN   CA  HA   sing N N 179 
GLN   C   O    doub N N 180 
GLN   C   OXT  sing N N 181 
GLN   CB  CG   sing N N 182 
GLN   CB  HB2  sing N N 183 
GLN   CB  HB3  sing N N 184 
GLN   CG  CD   sing N N 185 
GLN   CG  HG2  sing N N 186 
GLN   CG  HG3  sing N N 187 
GLN   CD  OE1  doub N N 188 
GLN   CD  NE2  sing N N 189 
GLN   NE2 HE21 sing N N 190 
GLN   NE2 HE22 sing N N 191 
GLN   OXT HXT  sing N N 192 
GLU   N   CA   sing N N 193 
GLU   N   H    sing N N 194 
GLU   N   H2   sing N N 195 
GLU   CA  C    sing N N 196 
GLU   CA  CB   sing N N 197 
GLU   CA  HA   sing N N 198 
GLU   C   O    doub N N 199 
GLU   C   OXT  sing N N 200 
GLU   CB  CG   sing N N 201 
GLU   CB  HB2  sing N N 202 
GLU   CB  HB3  sing N N 203 
GLU   CG  CD   sing N N 204 
GLU   CG  HG2  sing N N 205 
GLU   CG  HG3  sing N N 206 
GLU   CD  OE1  doub N N 207 
GLU   CD  OE2  sing N N 208 
GLU   OE2 HE2  sing N N 209 
GLU   OXT HXT  sing N N 210 
GLY   N   CA   sing N N 211 
GLY   N   H    sing N N 212 
GLY   N   H2   sing N N 213 
GLY   CA  C    sing N N 214 
GLY   CA  HA2  sing N N 215 
GLY   CA  HA3  sing N N 216 
GLY   C   O    doub N N 217 
GLY   C   OXT  sing N N 218 
GLY   OXT HXT  sing N N 219 
HIS   N   CA   sing N N 220 
HIS   N   H    sing N N 221 
HIS   N   H2   sing N N 222 
HIS   CA  C    sing N N 223 
HIS   CA  CB   sing N N 224 
HIS   CA  HA   sing N N 225 
HIS   C   O    doub N N 226 
HIS   C   OXT  sing N N 227 
HIS   CB  CG   sing N N 228 
HIS   CB  HB2  sing N N 229 
HIS   CB  HB3  sing N N 230 
HIS   CG  ND1  sing Y N 231 
HIS   CG  CD2  doub Y N 232 
HIS   ND1 CE1  doub Y N 233 
HIS   ND1 HD1  sing N N 234 
HIS   CD2 NE2  sing Y N 235 
HIS   CD2 HD2  sing N N 236 
HIS   CE1 NE2  sing Y N 237 
HIS   CE1 HE1  sing N N 238 
HIS   NE2 HE2  sing N N 239 
HIS   OXT HXT  sing N N 240 
HOH   O   H1   sing N N 241 
HOH   O   H2   sing N N 242 
ILE   N   CA   sing N N 243 
ILE   N   H    sing N N 244 
ILE   N   H2   sing N N 245 
ILE   CA  C    sing N N 246 
ILE   CA  CB   sing N N 247 
ILE   CA  HA   sing N N 248 
ILE   C   O    doub N N 249 
ILE   C   OXT  sing N N 250 
ILE   CB  CG1  sing N N 251 
ILE   CB  CG2  sing N N 252 
ILE   CB  HB   sing N N 253 
ILE   CG1 CD1  sing N N 254 
ILE   CG1 HG12 sing N N 255 
ILE   CG1 HG13 sing N N 256 
ILE   CG2 HG21 sing N N 257 
ILE   CG2 HG22 sing N N 258 
ILE   CG2 HG23 sing N N 259 
ILE   CD1 HD11 sing N N 260 
ILE   CD1 HD12 sing N N 261 
ILE   CD1 HD13 sing N N 262 
ILE   OXT HXT  sing N N 263 
LEU   N   CA   sing N N 264 
LEU   N   H    sing N N 265 
LEU   N   H2   sing N N 266 
LEU   CA  C    sing N N 267 
LEU   CA  CB   sing N N 268 
LEU   CA  HA   sing N N 269 
LEU   C   O    doub N N 270 
LEU   C   OXT  sing N N 271 
LEU   CB  CG   sing N N 272 
LEU   CB  HB2  sing N N 273 
LEU   CB  HB3  sing N N 274 
LEU   CG  CD1  sing N N 275 
LEU   CG  CD2  sing N N 276 
LEU   CG  HG   sing N N 277 
LEU   CD1 HD11 sing N N 278 
LEU   CD1 HD12 sing N N 279 
LEU   CD1 HD13 sing N N 280 
LEU   CD2 HD21 sing N N 281 
LEU   CD2 HD22 sing N N 282 
LEU   CD2 HD23 sing N N 283 
LEU   OXT HXT  sing N N 284 
LYS   N   CA   sing N N 285 
LYS   N   H    sing N N 286 
LYS   N   H2   sing N N 287 
LYS   CA  C    sing N N 288 
LYS   CA  CB   sing N N 289 
LYS   CA  HA   sing N N 290 
LYS   C   O    doub N N 291 
LYS   C   OXT  sing N N 292 
LYS   CB  CG   sing N N 293 
LYS   CB  HB2  sing N N 294 
LYS   CB  HB3  sing N N 295 
LYS   CG  CD   sing N N 296 
LYS   CG  HG2  sing N N 297 
LYS   CG  HG3  sing N N 298 
LYS   CD  CE   sing N N 299 
LYS   CD  HD2  sing N N 300 
LYS   CD  HD3  sing N N 301 
LYS   CE  NZ   sing N N 302 
LYS   CE  HE2  sing N N 303 
LYS   CE  HE3  sing N N 304 
LYS   NZ  HZ1  sing N N 305 
LYS   NZ  HZ2  sing N N 306 
LYS   NZ  HZ3  sing N N 307 
LYS   OXT HXT  sing N N 308 
MET   N   CA   sing N N 309 
MET   N   H    sing N N 310 
MET   N   H2   sing N N 311 
MET   CA  C    sing N N 312 
MET   CA  CB   sing N N 313 
MET   CA  HA   sing N N 314 
MET   C   O    doub N N 315 
MET   C   OXT  sing N N 316 
MET   CB  CG   sing N N 317 
MET   CB  HB2  sing N N 318 
MET   CB  HB3  sing N N 319 
MET   CG  SD   sing N N 320 
MET   CG  HG2  sing N N 321 
MET   CG  HG3  sing N N 322 
MET   SD  CE   sing N N 323 
MET   CE  HE1  sing N N 324 
MET   CE  HE2  sing N N 325 
MET   CE  HE3  sing N N 326 
MET   OXT HXT  sing N N 327 
PHE   N   CA   sing N N 328 
PHE   N   H    sing N N 329 
PHE   N   H2   sing N N 330 
PHE   CA  C    sing N N 331 
PHE   CA  CB   sing N N 332 
PHE   CA  HA   sing N N 333 
PHE   C   O    doub N N 334 
PHE   C   OXT  sing N N 335 
PHE   CB  CG   sing N N 336 
PHE   CB  HB2  sing N N 337 
PHE   CB  HB3  sing N N 338 
PHE   CG  CD1  doub Y N 339 
PHE   CG  CD2  sing Y N 340 
PHE   CD1 CE1  sing Y N 341 
PHE   CD1 HD1  sing N N 342 
PHE   CD2 CE2  doub Y N 343 
PHE   CD2 HD2  sing N N 344 
PHE   CE1 CZ   doub Y N 345 
PHE   CE1 HE1  sing N N 346 
PHE   CE2 CZ   sing Y N 347 
PHE   CE2 HE2  sing N N 348 
PHE   CZ  HZ   sing N N 349 
PHE   OXT HXT  sing N N 350 
PRO   N   CA   sing N N 351 
PRO   N   CD   sing N N 352 
PRO   N   H    sing N N 353 
PRO   CA  C    sing N N 354 
PRO   CA  CB   sing N N 355 
PRO   CA  HA   sing N N 356 
PRO   C   O    doub N N 357 
PRO   C   OXT  sing N N 358 
PRO   CB  CG   sing N N 359 
PRO   CB  HB2  sing N N 360 
PRO   CB  HB3  sing N N 361 
PRO   CG  CD   sing N N 362 
PRO   CG  HG2  sing N N 363 
PRO   CG  HG3  sing N N 364 
PRO   CD  HD2  sing N N 365 
PRO   CD  HD3  sing N N 366 
PRO   OXT HXT  sing N N 367 
SER   N   CA   sing N N 368 
SER   N   H    sing N N 369 
SER   N   H2   sing N N 370 
SER   CA  C    sing N N 371 
SER   CA  CB   sing N N 372 
SER   CA  HA   sing N N 373 
SER   C   O    doub N N 374 
SER   C   OXT  sing N N 375 
SER   CB  OG   sing N N 376 
SER   CB  HB2  sing N N 377 
SER   CB  HB3  sing N N 378 
SER   OG  HG   sing N N 379 
SER   OXT HXT  sing N N 380 
THR   N   CA   sing N N 381 
THR   N   H    sing N N 382 
THR   N   H2   sing N N 383 
THR   CA  C    sing N N 384 
THR   CA  CB   sing N N 385 
THR   CA  HA   sing N N 386 
THR   C   O    doub N N 387 
THR   C   OXT  sing N N 388 
THR   CB  OG1  sing N N 389 
THR   CB  CG2  sing N N 390 
THR   CB  HB   sing N N 391 
THR   OG1 HG1  sing N N 392 
THR   CG2 HG21 sing N N 393 
THR   CG2 HG22 sing N N 394 
THR   CG2 HG23 sing N N 395 
THR   OXT HXT  sing N N 396 
TRP   N   CA   sing N N 397 
TRP   N   H    sing N N 398 
TRP   N   H2   sing N N 399 
TRP   CA  C    sing N N 400 
TRP   CA  CB   sing N N 401 
TRP   CA  HA   sing N N 402 
TRP   C   O    doub N N 403 
TRP   C   OXT  sing N N 404 
TRP   CB  CG   sing N N 405 
TRP   CB  HB2  sing N N 406 
TRP   CB  HB3  sing N N 407 
TRP   CG  CD1  doub Y N 408 
TRP   CG  CD2  sing Y N 409 
TRP   CD1 NE1  sing Y N 410 
TRP   CD1 HD1  sing N N 411 
TRP   CD2 CE2  doub Y N 412 
TRP   CD2 CE3  sing Y N 413 
TRP   NE1 CE2  sing Y N 414 
TRP   NE1 HE1  sing N N 415 
TRP   CE2 CZ2  sing Y N 416 
TRP   CE3 CZ3  doub Y N 417 
TRP   CE3 HE3  sing N N 418 
TRP   CZ2 CH2  doub Y N 419 
TRP   CZ2 HZ2  sing N N 420 
TRP   CZ3 CH2  sing Y N 421 
TRP   CZ3 HZ3  sing N N 422 
TRP   CH2 HH2  sing N N 423 
TRP   OXT HXT  sing N N 424 
TYR   N   CA   sing N N 425 
TYR   N   H    sing N N 426 
TYR   N   H2   sing N N 427 
TYR   CA  C    sing N N 428 
TYR   CA  CB   sing N N 429 
TYR   CA  HA   sing N N 430 
TYR   C   O    doub N N 431 
TYR   C   OXT  sing N N 432 
TYR   CB  CG   sing N N 433 
TYR   CB  HB2  sing N N 434 
TYR   CB  HB3  sing N N 435 
TYR   CG  CD1  doub Y N 436 
TYR   CG  CD2  sing Y N 437 
TYR   CD1 CE1  sing Y N 438 
TYR   CD1 HD1  sing N N 439 
TYR   CD2 CE2  doub Y N 440 
TYR   CD2 HD2  sing N N 441 
TYR   CE1 CZ   doub Y N 442 
TYR   CE1 HE1  sing N N 443 
TYR   CE2 CZ   sing Y N 444 
TYR   CE2 HE2  sing N N 445 
TYR   CZ  OH   sing N N 446 
TYR   OH  HH   sing N N 447 
TYR   OXT HXT  sing N N 448 
VAL   N   CA   sing N N 449 
VAL   N   H    sing N N 450 
VAL   N   H2   sing N N 451 
VAL   CA  C    sing N N 452 
VAL   CA  CB   sing N N 453 
VAL   CA  HA   sing N N 454 
VAL   C   O    doub N N 455 
VAL   C   OXT  sing N N 456 
VAL   CB  CG1  sing N N 457 
VAL   CB  CG2  sing N N 458 
VAL   CB  HB   sing N N 459 
VAL   CG1 HG11 sing N N 460 
VAL   CG1 HG12 sing N N 461 
VAL   CG1 HG13 sing N N 462 
VAL   CG2 HG21 sing N N 463 
VAL   CG2 HG22 sing N N 464 
VAL   CG2 HG23 sing N N 465 
VAL   OXT HXT  sing N N 466 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           AI150466 
_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   4JEC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EEG 
_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]   0.016657 
_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]   0.011419 
_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]   0.021591 
_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 
C  
CL 
N  
O  
S  
# 
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   . PRO   A 1 1  ? 7.536  6.734  -10.867 1.00 46.88  ? 1   PRO   A N   1 
ATOM   2    C  CA  . PRO   A 1 1  ? 8.202  5.562  -10.300 1.00 44.43  ? 1   PRO   A CA  1 
ATOM   3    C  C   . PRO   A 1 1  ? 7.978  5.438  -8.798  1.00 43.31  ? 1   PRO   A C   1 
ATOM   4    O  O   . PRO   A 1 1  ? 7.293  6.253  -8.185  1.00 40.34  ? 1   PRO   A O   1 
ATOM   5    C  CB  . PRO   A 1 1  ? 9.681  5.832  -10.595 1.00 51.18  ? 1   PRO   A CB  1 
ATOM   6    C  CG  . PRO   A 1 1  ? 9.784  7.304  -10.553 1.00 44.66  ? 1   PRO   A CG  1 
ATOM   7    C  CD  . PRO   A 1 1  ? 8.501  7.802  -11.183 1.00 46.52  ? 1   PRO   A CD  1 
ATOM   8    N  N   . GLN   A 1 2  ? 8.554  4.394  -8.217  1.00 34.74  ? 2   GLN   A N   1 
ATOM   9    C  CA  . GLN   A 1 2  ? 8.620  4.206  -6.776  1.00 32.43  ? 2   GLN   A CA  1 
ATOM   10   C  C   . GLN   A 1 2  ? 10.090 4.261  -6.381  1.00 45.42  ? 2   GLN   A C   1 
ATOM   11   O  O   . GLN   A 1 2  ? 10.910 3.502  -6.907  1.00 45.25  ? 2   GLN   A O   1 
ATOM   12   C  CB  . GLN   A 1 2  ? 7.998  2.875  -6.353  1.00 42.16  ? 2   GLN   A CB  1 
ATOM   13   C  CG  . GLN   A 1 2  ? 8.520  2.391  -5.020  1.00 45.90  ? 2   GLN   A CG  1 
ATOM   14   C  CD  . GLN   A 1 2  ? 7.964  1.040  -4.636  1.00 73.00  ? 2   GLN   A CD  1 
ATOM   15   O  OE1 . GLN   A 1 2  ? 6.750  0.844  -4.621  1.00 77.96  ? 2   GLN   A OE1 1 
ATOM   16   N  NE2 . GLN   A 1 2  ? 8.853  0.088  -4.348  1.00 70.27  ? 2   GLN   A NE2 1 
ATOM   17   N  N   . ILE   A 1 3  ? 10.427 5.172  -5.484  1.00 28.83  ? 3   ILE   A N   1 
ATOM   18   C  CA  . ILE   A 1 3  ? 11.817 5.494  -5.187  1.00 33.40  ? 3   ILE   A CA  1 
ATOM   19   C  C   . ILE   A 1 3  ? 12.075 5.045  -3.758  1.00 30.85  ? 3   ILE   A C   1 
ATOM   20   O  O   . ILE   A 1 3  ? 11.416 5.525  -2.827  1.00 25.85  ? 3   ILE   A O   1 
ATOM   21   C  CB  . ILE   A 1 3  ? 12.097 6.996  -5.384  1.00 31.03  ? 3   ILE   A CB  1 
ATOM   22   C  CG1 . ILE   A 1 3  ? 12.005 7.361  -6.867  1.00 37.60  ? 3   ILE   A CG1 1 
ATOM   23   C  CG2 . ILE   A 1 3  ? 13.449 7.403  -4.842  1.00 32.61  ? 3   ILE   A CG2 1 
ATOM   24   C  CD1 . ILE   A 1 3  ? 11.890 8.804  -7.096  1.00 33.69  ? 3   ILE   A CD1 1 
ATOM   25   N  N   . THR   A 1 4  ? 12.983 4.077  -3.589  1.00 29.66  ? 4   THR   A N   1 
ATOM   26   C  CA  . THR   A 1 4  ? 13.429 3.712  -2.253  1.00 27.17  ? 4   THR   A CA  1 
ATOM   27   C  C   . THR   A 1 4  ? 14.512 4.692  -1.782  1.00 24.72  ? 4   THR   A C   1 
ATOM   28   O  O   . THR   A 1 4  ? 15.031 5.513  -2.542  1.00 28.29  ? 4   THR   A O   1 
ATOM   29   C  CB  . THR   A 1 4  ? 13.950 2.266  -2.222  1.00 31.64  ? 4   THR   A CB  1 
ATOM   30   O  OG1 . THR   A 1 4  ? 15.055 2.167  -3.120  1.00 27.59  ? 4   THR   A OG1 1 
ATOM   31   C  CG2 . THR   A 1 4  ? 12.856 1.293  -2.650  1.00 32.17  ? 4   THR   A CG2 1 
ATOM   32   N  N   . LEU   A 1 5  ? 14.850 4.619  -0.494  1.00 21.04  ? 5   LEU   A N   1 
ATOM   33   C  CA  . LEU   A 1 5  ? 15.651 5.684  0.109   1.00 21.01  ? 5   LEU   A CA  1 
ATOM   34   C  C   . LEU   A 1 5  ? 17.009 5.183  0.609   1.00 23.80  ? 5   LEU   A C   1 
ATOM   35   O  O   . LEU   A 1 5  ? 17.648 5.821  1.455   1.00 21.33  ? 5   LEU   A O   1 
ATOM   36   C  CB  . LEU   A 1 5  ? 14.828 6.331  1.226   1.00 19.34  ? 5   LEU   A CB  1 
ATOM   37   C  CG  . LEU   A 1 5  ? 13.521 6.958  0.690   1.00 21.39  ? 5   LEU   A CG  1 
ATOM   38   C  CD1 . LEU   A 1 5  ? 12.625 7.356  1.844   1.00 25.64  ? 5   LEU   A CD1 1 
ATOM   39   C  CD2 . LEU   A 1 5  ? 13.828 8.219  -0.156  1.00 23.98  ? 5   LEU   A CD2 1 
ATOM   40   N  N   . TRP   A 1 6  ? 17.503 4.067  0.057   1.00 22.11  ? 6   TRP   A N   1 
ATOM   41   C  CA  . TRP   A 1 6  ? 18.833 3.600  0.412   1.00 25.50  ? 6   TRP   A CA  1 
ATOM   42   C  C   . TRP   A 1 6  ? 19.913 4.549  -0.095  1.00 24.84  ? 6   TRP   A C   1 
ATOM   43   O  O   . TRP   A 1 6  ? 20.990 4.611  0.494   1.00 28.06  ? 6   TRP   A O   1 
ATOM   44   C  CB  . TRP   A 1 6  ? 19.045 2.182  -0.134  1.00 22.68  ? 6   TRP   A CB  1 
ATOM   45   C  CG  . TRP   A 1 6  ? 17.975 1.250  0.356   1.00 21.21  ? 6   TRP   A CG  1 
ATOM   46   C  CD1 . TRP   A 1 6  ? 16.848 0.874  -0.327  1.00 25.25  ? 6   TRP   A CD1 1 
ATOM   47   C  CD2 . TRP   A 1 6  ? 17.907 0.594  1.637   1.00 23.43  ? 6   TRP   A CD2 1 
ATOM   48   N  NE1 . TRP   A 1 6  ? 16.090 0.016  0.441   1.00 26.72  ? 6   TRP   A NE1 1 
ATOM   49   C  CE2 . TRP   A 1 6  ? 16.717 -0.179 1.647   1.00 24.76  ? 6   TRP   A CE2 1 
ATOM   50   C  CE3 . TRP   A 1 6  ? 18.759 0.548  2.755   1.00 22.97  ? 6   TRP   A CE3 1 
ATOM   51   C  CZ2 . TRP   A 1 6  ? 16.332 -0.965 2.751   1.00 26.35  ? 6   TRP   A CZ2 1 
ATOM   52   C  CZ3 . TRP   A 1 6  ? 18.366 -0.228 3.862   1.00 20.14  ? 6   TRP   A CZ3 1 
ATOM   53   C  CH2 . TRP   A 1 6  ? 17.173 -0.972 3.846   1.00 26.12  ? 6   TRP   A CH2 1 
ATOM   54   N  N   . LYS   A 1 7  ? 19.646 5.282  -1.173  1.00 23.84  ? 7   LYS   A N   1 
ATOM   55   C  CA  . LYS   A 1 7  ? 20.508 6.359  -1.654  1.00 24.08  ? 7   LYS   A CA  1 
ATOM   56   C  C   . LYS   A 1 7  ? 19.704 7.658  -1.672  1.00 24.81  ? 7   LYS   A C   1 
ATOM   57   O  O   . LYS   A 1 7  ? 18.475 7.628  -1.578  1.00 21.09  ? 7   LYS   A O   1 
ATOM   58   C  CB  . LYS   A 1 7  ? 21.043 6.098  -3.073  1.00 31.43  ? 7   LYS   A CB  1 
ATOM   59   C  CG  . LYS   A 1 7  ? 21.305 4.659  -3.465  1.00 38.04  ? 7   LYS   A CG  1 
ATOM   60   C  CD  . LYS   A 1 7  ? 21.668 4.623  -4.953  1.00 64.38  ? 7   LYS   A CD  1 
ATOM   61   C  CE  . LYS   A 1 7  ? 20.595 5.318  -5.809  1.00 64.12  ? 7   LYS   A CE  1 
ATOM   62   N  NZ  . LYS   A 1 7  ? 20.883 5.298  -7.278  1.00 68.86  ? 7   LYS   A NZ  1 
ATOM   63   N  N   . ARG   A 1 8  ? 20.413 8.784  -1.786  1.00 22.55  ? 8   ARG   A N   1 
ATOM   64   C  CA  . ARG   A 1 8  ? 19.733 10.089 -1.867  1.00 19.33  ? 8   ARG   A CA  1 
ATOM   65   C  C   . ARG   A 1 8  ? 18.782 10.077 -3.055  1.00 22.05  ? 8   ARG   A C   1 
ATOM   66   O  O   . ARG   A 1 8  ? 19.170 9.618  -4.153  1.00 22.21  ? 8   ARG   A O   1 
ATOM   67   C  CB  . ARG   A 1 8  ? 20.745 11.222 -2.050  1.00 25.53  ? 8   ARG   A CB  1 
ATOM   68   C  CG  . ARG   A 1 8  ? 21.303 11.756 -0.760  1.00 26.86  ? 8   ARG   A CG  1 
ATOM   69   C  CD  . ARG   A 1 8  ? 22.400 12.759 -1.048  1.00 33.69  ? 8   ARG   A CD  1 
ATOM   70   N  NE  . ARG   A 1 8  ? 22.903 13.336 0.187   1.00 36.46  ? 8   ARG   A NE  1 
ATOM   71   C  CZ  . ARG   A 1 8  ? 23.164 14.626 0.354   1.00 61.59  ? 8   ARG   A CZ  1 
ATOM   72   N  NH1 . ARG   A 1 8  ? 23.024 15.497 -0.637  1.00 47.80  ? 8   ARG   A NH1 1 
ATOM   73   N  NH2 . ARG   A 1 8  ? 23.582 15.053 1.542   1.00 49.53  ? 8   ARG   A NH2 1 
ATOM   74   N  N   . PRO   A 1 9  ? 17.526 10.562 -2.893  1.00 20.21  ? 9   PRO   A N   1 
ATOM   75   C  CA  . PRO   A 1 9  ? 16.560 10.563 -4.008  1.00 19.57  ? 9   PRO   A CA  1 
ATOM   76   C  C   . PRO   A 1 9  ? 16.830 11.749 -4.931  1.00 26.58  ? 9   PRO   A C   1 
ATOM   77   O  O   . PRO   A 1 9  ? 16.146 12.778 -4.892  1.00 22.76  ? 9   PRO   A O   1 
ATOM   78   C  CB  . PRO   A 1 9  ? 15.206 10.661 -3.291  1.00 22.25  ? 9   PRO   A CB  1 
ATOM   79   C  CG  . PRO   A 1 9  ? 15.491 11.359 -1.989  1.00 23.18  ? 9   PRO   A CG  1 
ATOM   80   C  CD  . PRO   A 1 9  ? 16.923 11.010 -1.611  1.00 22.42  ? 9   PRO   A CD  1 
ATOM   81   N  N   . LEU   A 1 10 ? 17.863 11.605 -5.772  1.00 20.39  ? 10  LEU   A N   1 
ATOM   82   C  CA  . LEU   A 1 10 ? 18.268 12.645 -6.713  1.00 20.72  ? 10  LEU   A CA  1 
ATOM   83   C  C   . LEU   A 1 10 ? 17.571 12.431 -8.044  1.00 24.38  ? 10  LEU   A C   1 
ATOM   84   O  O   . LEU   A 1 10 ? 17.418 11.292 -8.505  1.00 28.02  ? 10  LEU   A O   1 
ATOM   85   C  CB  . LEU   A 1 10 ? 19.788 12.653 -6.908  1.00 22.67  ? 10  LEU   A CB  1 
ATOM   86   C  CG  . LEU   A 1 10 ? 20.628 13.059 -5.675  1.00 32.45  ? 10  LEU   A CG  1 
ATOM   87   C  CD1 . LEU   A 1 10 ? 22.107 12.747 -5.876  1.00 42.21  ? 10  LEU   A CD1 1 
ATOM   88   C  CD2 . LEU   A 1 10 ? 20.413 14.532 -5.309  1.00 29.53  ? 10  LEU   A CD2 1 
ATOM   89   N  N   . VAL   A 1 11 ? 17.102 13.522 -8.648  1.00 20.75  ? 11  VAL   A N   1 
ATOM   90   C  CA  . VAL   A 1 11 ? 16.484 13.457 -9.969  1.00 22.52  ? 11  VAL   A CA  1 
ATOM   91   C  C   . VAL   A 1 11 ? 17.066 14.557 -10.846 1.00 27.06  ? 11  VAL   A C   1 
ATOM   92   O  O   . VAL   A 1 11 ? 17.683 15.509 -10.373 1.00 23.87  ? 11  VAL   A O   1 
ATOM   93   C  CB  . VAL   A 1 11 ? 14.933 13.562 -9.940  1.00 22.88  ? 11  VAL   A CB  1 
ATOM   94   C  CG1 . VAL   A 1 11 ? 14.268 12.332 -9.225  1.00 28.28  ? 11  VAL   A CG1 1 
ATOM   95   C  CG2 . VAL   A 1 11 ? 14.470 14.898 -9.349  1.00 24.58  ? 11  VAL   A CG2 1 
ATOM   96   N  N   . THR   A 1 12 ? 16.826 14.432 -12.149 1.00 22.47  ? 12  THR   A N   1 
ATOM   97   C  CA  . THR   A 1 12 ? 17.175 15.499 -13.075 1.00 20.54  ? 12  THR   A CA  1 
ATOM   98   C  C   . THR   A 1 12 ? 16.016 16.476 -13.194 1.00 22.69  ? 12  THR   A C   1 
ATOM   99   O  O   . THR   A 1 12 ? 14.867 16.060 -13.348 1.00 27.31  ? 12  THR   A O   1 
ATOM   100  C  CB  . THR   A 1 12 ? 17.500 14.928 -14.455 1.00 29.64  ? 12  THR   A CB  1 
ATOM   101  O  OG1 . THR   A 1 12 ? 18.649 14.094 -14.334 1.00 29.70  ? 12  THR   A OG1 1 
ATOM   102  C  CG2 . THR   A 1 12 ? 17.778 16.056 -15.439 1.00 30.68  ? 12  THR   A CG2 1 
ATOM   103  N  N   . ILE   A 1 13 ? 16.327 17.766 -13.123 1.00 20.39  ? 13  ILE   A N   1 
ATOM   104  C  CA  . ILE   A 1 13 ? 15.344 18.800 -13.388 1.00 20.54  ? 13  ILE   A CA  1 
ATOM   105  C  C   . ILE   A 1 13 ? 15.832 19.598 -14.577 1.00 22.86  ? 13  ILE   A C   1 
ATOM   106  O  O   . ILE   A 1 13 ? 17.023 19.635 -14.878 1.00 23.29  ? 13  ILE   A O   1 
ATOM   107  C  CB  . ILE   A 1 13 ? 15.108 19.706 -12.171 1.00 22.85  ? 13  ILE   A CB  1 
ATOM   108  C  CG1 . ILE   A 1 13 ? 16.376 20.468 -11.782 1.00 25.25  ? 13  ILE   A CG1 1 
ATOM   109  C  CG2 . ILE   A 1 13 ? 14.575 18.878 -11.034 1.00 26.22  ? 13  ILE   A CG2 1 
ATOM   110  C  CD1 . ILE   A 1 13 ? 16.097 21.584 -10.742 1.00 24.79  ? 13  ILE   A CD1 1 
ATOM   111  N  N   . LYS   A 1 14 ? 14.903 20.260 -15.242 1.00 21.01  ? 14  LYS   A N   1 
ATOM   112  C  CA  . LYS   A 1 14 ? 15.267 21.159 -16.320 1.00 22.76  ? 14  LYS   A CA  1 
ATOM   113  C  C   . LYS   A 1 14 ? 14.635 22.505 -16.010 1.00 24.44  ? 14  LYS   A C   1 
ATOM   114  O  O   . LYS   A 1 14 ? 13.414 22.604 -15.843 1.00 23.07  ? 14  LYS   A O   1 
ATOM   115  C  CB  . LYS   A 1 14 ? 14.802 20.593 -17.669 1.00 28.04  ? 14  LYS   A CB  1 
ATOM   116  C  CG  . LYS   A 1 14 ? 15.233 21.448 -18.856 1.00 36.81  ? 14  LYS   A CG  1 
ATOM   117  C  CD  . LYS   A 1 14 ? 15.616 20.567 -20.059 1.00 46.67  ? 14  LYS   A CD  1 
ATOM   118  C  CE  . LYS   A 1 14 ? 14.485 20.504 -21.057 1.00 52.85  ? 14  LYS   A CE  1 
ATOM   119  N  NZ  . LYS   A 1 14 ? 14.915 20.025 -22.412 1.00 43.58  ? 14  LYS   A NZ  1 
ATOM   120  N  N   . ILE   A 1 15 ? 15.457 23.531 -15.875 1.00 24.78  ? 15  ILE   A N   1 
ATOM   121  C  CA  . ILE   A 1 15 ? 14.944 24.846 -15.522 1.00 27.83  ? 15  ILE   A CA  1 
ATOM   122  C  C   . ILE   A 1 15 ? 15.768 25.889 -16.271 1.00 38.28  ? 15  ILE   A C   1 
ATOM   123  O  O   . ILE   A 1 15 ? 16.997 25.780 -16.360 1.00 30.86  ? 15  ILE   A O   1 
ATOM   124  C  CB  . ILE   A 1 15 ? 14.946 25.059 -13.990 1.00 29.16  ? 15  ILE   A CB  1 
ATOM   125  C  CG1 . ILE   A 1 15 ? 14.431 26.462 -13.638 1.00 46.01  ? 15  ILE   A CG1 1 
ATOM   126  C  CG2 . ILE   A 1 15 ? 16.340 24.820 -13.397 1.00 31.58  ? 15  ILE   A CG2 1 
ATOM   127  C  CD1 . ILE   A 1 15 ? 14.298 26.699 -12.160 1.00 35.05  ? 15  ILE   A CD1 1 
ATOM   128  N  N   . GLY   A 1 16 ? 15.085 26.856 -16.873 1.00 38.80  ? 16  GLY   A N   1 
ATOM   129  C  CA  . GLY   A 1 16 ? 15.786 27.856 -17.675 1.00 39.71  ? 16  GLY   A CA  1 
ATOM   130  C  C   . GLY   A 1 16 ? 16.713 27.269 -18.716 1.00 41.11  ? 16  GLY   A C   1 
ATOM   131  O  O   . GLY   A 1 16 ? 17.833 27.767 -18.897 1.00 50.81  ? 16  GLY   A O   1 
ATOM   132  N  N   . GLY   A 1 17 ? 16.286 26.195 -19.387 1.00 42.86  ? 17  GLY   A N   1 
ATOM   133  C  CA  . GLY   A 1 17 ? 17.059 25.552 -20.439 1.00 44.96  ? 17  GLY   A CA  1 
ATOM   134  C  C   . GLY   A 1 17 ? 18.196 24.645 -19.995 1.00 50.12  ? 17  GLY   A C   1 
ATOM   135  O  O   . GLY   A 1 17 ? 18.805 23.986 -20.849 1.00 53.83  ? 17  GLY   A O   1 
ATOM   136  N  N   . GLN   A 1 18 ? 18.481 24.567 -18.698 1.00 37.76  ? 18  GLN   A N   1 
ATOM   137  C  CA  . GLN   A 1 18 ? 19.642 23.859 -18.174 1.00 35.44  ? 18  GLN   A CA  1 
ATOM   138  C  C   . GLN   A 1 18 ? 19.204 22.591 -17.457 1.00 34.18  ? 18  GLN   A C   1 
ATOM   139  O  O   . GLN   A 1 18 ? 18.169 22.591 -16.793 1.00 28.07  ? 18  GLN   A O   1 
ATOM   140  C  CB  . GLN   A 1 18 ? 20.384 24.739 -17.175 1.00 36.74  ? 18  GLN   A CB  1 
ATOM   141  C  CG  . GLN   A 1 18 ? 20.838 26.079 -17.711 1.00 51.82  ? 18  GLN   A CG  1 
ATOM   142  C  CD  . GLN   A 1 18 ? 21.682 26.829 -16.699 1.00 76.03  ? 18  GLN   A CD  1 
ATOM   143  O  OE1 . GLN   A 1 18 ? 21.309 27.905 -16.233 1.00 76.13  ? 18  GLN   A OE1 1 
ATOM   144  N  NE2 . GLN   A 1 18 ? 22.834 26.261 -16.357 1.00 77.50  ? 18  GLN   A NE2 1 
ATOM   145  N  N   . LEU   A 1 19 ? 19.995 21.508 -17.579 1.00 28.86  ? 19  LEU   A N   1 
ATOM   146  C  CA  . LEU   A 1 19 ? 19.786 20.330 -16.743 1.00 25.85  ? 19  LEU   A CA  1 
ATOM   147  C  C   . LEU   A 1 19 ? 20.562 20.484 -15.449 1.00 32.72  ? 19  LEU   A C   1 
ATOM   148  O  O   . LEU   A 1 19 ? 21.717 20.912 -15.451 1.00 31.56  ? 19  LEU   A O   1 
ATOM   149  C  CB  . LEU   A 1 19 ? 20.196 19.025 -17.436 1.00 32.50  ? 19  LEU   A CB  1 
ATOM   150  C  CG  . LEU   A 1 19 ? 19.482 18.572 -18.692 1.00 34.94  ? 19  LEU   A CG  1 
ATOM   151  C  CD1 . LEU   A 1 19 ? 20.037 17.236 -19.149 1.00 34.81  ? 19  LEU   A CD1 1 
ATOM   152  C  CD2 . LEU   A 1 19 ? 18.011 18.394 -18.382 1.00 39.51  ? 19  LEU   A CD2 1 
ATOM   153  N  N   . LYS   A 1 20 ? 19.904 20.156 -14.339 1.00 22.53  ? 20  LYS   A N   1 
ATOM   154  C  CA  . LYS   A 1 20 ? 20.526 20.199 -13.036 1.00 21.16  ? 20  LYS   A CA  1 
ATOM   155  C  C   . LYS   A 1 20 ? 20.069 18.947 -12.301 1.00 22.12  ? 20  LYS   A C   1 
ATOM   156  O  O   . LYS   A 1 20 ? 19.086 18.304 -12.684 1.00 26.99  ? 20  LYS   A O   1 
ATOM   157  C  CB  . LYS   A 1 20 ? 20.088 21.462 -12.254 1.00 22.31  ? 20  LYS   A CB  1 
ATOM   158  C  CG  . LYS   A 1 20 ? 20.813 22.741 -12.686 1.00 31.78  ? 20  LYS   A CG  1 
ATOM   159  C  CD  . LYS   A 1 20 ? 20.021 23.978 -12.301 1.00 45.48  ? 20  LYS   A CD  1 
ATOM   160  C  CE  . LYS   A 1 20 ? 20.709 25.278 -12.742 1.00 52.51  ? 20  LYS   A CE  1 
ATOM   161  N  NZ  . LYS   A 1 20 ? 22.151 25.304 -12.392 1.00 49.64  ? 20  LYS   A NZ  1 
ATOM   162  N  N   . GLU   A 1 21 ? 20.775 18.606 -11.236 1.00 22.76  ? 21  GLU   A N   1 
ATOM   163  C  CA  . GLU   A 1 21 ? 20.342 17.525 -10.361 1.00 19.61  ? 21  GLU   A CA  1 
ATOM   164  C  C   . GLU   A 1 21 ? 19.735 18.125 -9.092  1.00 21.91  ? 21  GLU   A C   1 
ATOM   165  O  O   . GLU   A 1 21 ? 20.196 19.171 -8.614  1.00 22.13  ? 21  GLU   A O   1 
ATOM   166  C  CB  . GLU   A 1 21 ? 21.547 16.658 -10.031 1.00 28.43  ? 21  GLU   A CB  1 
ATOM   167  C  CG  . GLU   A 1 21 ? 21.302 15.487 -9.199  1.00 40.02  ? 21  GLU   A CG  1 
ATOM   168  C  CD  . GLU   A 1 21 ? 22.558 14.626 -9.155  1.00 82.42  ? 21  GLU   A CD  1 
ATOM   169  O  OE1 . GLU   A 1 21 ? 23.540 15.009 -8.469  1.00 62.44  ? 21  GLU   A OE1 1 
ATOM   170  O  OE2 . GLU   A 1 21 ? 22.569 13.586 -9.851  1.00 53.85  ? 21  GLU   A OE2 1 
ATOM   171  N  N   . ALA   A 1 22 ? 18.702 17.471 -8.552  1.00 20.83  ? 22  ALA   A N   1 
ATOM   172  C  CA  . ALA   A 1 22 ? 18.046 18.030 -7.378  1.00 16.06  ? 22  ALA   A CA  1 
ATOM   173  C  C   . ALA   A 1 22 ? 17.556 16.902 -6.475  1.00 21.75  ? 22  ALA   A C   1 
ATOM   174  O  O   . ALA   A 1 22 ? 17.276 15.789 -6.923  1.00 23.02  ? 22  ALA   A O   1 
ATOM   175  C  CB  . ALA   A 1 22 ? 16.886 18.968 -7.768  1.00 18.13  ? 22  ALA   A CB  1 
ATOM   176  N  N   . LEU   A 1 23 ? 17.414 17.232 -5.198  1.00 17.15  ? 23  LEU   A N   1 
ATOM   177  C  CA  . LEU   A 1 23 ? 17.006 16.287 -4.165  1.00 17.43  ? 23  LEU   A CA  1 
ATOM   178  C  C   . LEU   A 1 23 ? 15.513 16.402 -3.914  1.00 23.95  ? 23  LEU   A C   1 
ATOM   179  O  O   . LEU   A 1 23 ? 15.004 17.509 -3.663  1.00 20.68  ? 23  LEU   A O   1 
ATOM   180  C  CB  . LEU   A 1 23 ? 17.777 16.622 -2.884  1.00 18.77  ? 23  LEU   A CB  1 
ATOM   181  C  CG  . LEU   A 1 23 ? 17.723 15.753 -1.635  1.00 27.37  ? 23  LEU   A CG  1 
ATOM   182  C  CD1 . LEU   A 1 23 ? 18.235 14.343 -1.893  1.00 29.33  ? 23  LEU   A CD1 1 
ATOM   183  C  CD2 . LEU   A 1 23 ? 18.515 16.478 -0.513  1.00 25.50  ? 23  LEU   A CD2 1 
ATOM   184  N  N   . LEU   A 1 24 ? 14.799 15.273 -3.966  1.00 18.72  ? 24  LEU   A N   1 
ATOM   185  C  CA  . LEU   A 1 24 ? 13.387 15.283 -3.628  1.00 16.98  ? 24  LEU   A CA  1 
ATOM   186  C  C   . LEU   A 1 24 ? 13.279 15.298 -2.102  1.00 23.52  ? 24  LEU   A C   1 
ATOM   187  O  O   . LEU   A 1 24 ? 13.731 14.351 -1.428  1.00 21.67  ? 24  LEU   A O   1 
ATOM   188  C  CB  . LEU   A 1 24 ? 12.677 14.063 -4.210  1.00 19.12  ? 24  LEU   A CB  1 
ATOM   189  C  CG  . LEU   A 1 24 ? 12.727 13.894 -5.733  1.00 23.17  ? 24  LEU   A CG  1 
ATOM   190  C  CD1 . LEU   A 1 24 ? 12.053 12.547 -6.056  1.00 29.70  ? 24  LEU   A CD1 1 
ATOM   191  C  CD2 . LEU   A 1 24 ? 12.069 15.086 -6.462  1.00 25.95  ? 24  LEU   A CD2 1 
ATOM   192  N  N   . ASP   A 1 25 ? 12.705 16.377 -1.546  1.00 17.59  ? 25  ASP   A N   1 
ATOM   193  C  CA  . ASP   A 1 25 ? 12.904 16.680 -0.127  1.00 18.71  ? 25  ASP   A CA  1 
ATOM   194  C  C   . ASP   A 1 25 ? 11.545 16.920 0.539   1.00 20.66  ? 25  ASP   A C   1 
ATOM   195  O  O   . ASP   A 1 25 ? 11.058 18.055 0.551   1.00 18.95  ? 25  ASP   A O   1 
ATOM   196  C  CB  . ASP   A 1 25 ? 13.879 17.888 -0.000  1.00 19.00  ? 25  ASP   A CB  1 
ATOM   197  C  CG  . ASP   A 1 25 ? 14.259 18.206 1.451   1.00 17.93  ? 25  ASP   A CG  1 
ATOM   198  O  OD1 . ASP   A 1 25 ? 13.743 17.596 2.404   1.00 21.21  ? 25  ASP   A OD1 1 
ATOM   199  O  OD2 . ASP   A 1 25 ? 15.177 19.001 1.603   1.00 23.07  ? 25  ASP   A OD2 1 
ATOM   200  N  N   . THR   A 1 26 ? 10.972 15.861 1.155   1.00 17.90  ? 26  THR   A N   1 
ATOM   201  C  CA  . THR   A 1 26 ? 9.672  16.023 1.809   1.00 18.18  ? 26  THR   A CA  1 
ATOM   202  C  C   . THR   A 1 26 ? 9.759  16.894 3.052   1.00 17.44  ? 26  THR   A C   1 
ATOM   203  O  O   . THR   A 1 26 ? 8.723  17.397 3.511   1.00 20.02  ? 26  THR   A O   1 
ATOM   204  C  CB  . THR   A 1 26 ? 9.063  14.675 2.210   1.00 17.94  ? 26  THR   A CB  1 
ATOM   205  O  OG1 . THR   A 1 26 ? 9.986  14.011 3.052   1.00 18.73  ? 26  THR   A OG1 1 
ATOM   206  C  CG2 . THR   A 1 26 ? 8.817  13.781 0.945   1.00 19.48  ? 26  THR   A CG2 1 
ATOM   207  N  N   . GLY   A 1 27 ? 10.956 17.103 3.597   1.00 16.17  ? 27  GLY   A N   1 
ATOM   208  C  CA  . GLY   A 1 27 ? 11.138 17.975 4.755   1.00 15.29  ? 27  GLY   A CA  1 
ATOM   209  C  C   . GLY   A 1 27 ? 11.273 19.450 4.431   1.00 21.39  ? 27  GLY   A C   1 
ATOM   210  O  O   . GLY   A 1 27 ? 11.445 20.264 5.354   1.00 21.41  ? 27  GLY   A O   1 
ATOM   211  N  N   . ALA   A 1 28 ? 11.241 19.815 3.154   1.00 17.23  ? 28  ALA   A N   1 
ATOM   212  C  CA  . ALA   A 1 28 ? 11.333 21.222 2.730   1.00 17.28  ? 28  ALA   A CA  1 
ATOM   213  C  C   . ALA   A 1 28 ? 9.966  21.728 2.263   1.00 18.42  ? 28  ALA   A C   1 
ATOM   214  O  O   . ALA   A 1 28 ? 9.341  21.121 1.387   1.00 18.54  ? 28  ALA   A O   1 
ATOM   215  C  CB  . ALA   A 1 28 ? 12.382 21.359 1.611   1.00 19.03  ? 28  ALA   A CB  1 
ATOM   216  N  N   . ASP   A 1 29 ? 9.474  22.829 2.861   1.00 18.30  ? 29  ASP   A N   1 
ATOM   217  C  CA  . ASP   A 1 29 ? 8.186  23.377 2.411   1.00 20.75  ? 29  ASP   A CA  1 
ATOM   218  C  C   . ASP   A 1 29 ? 8.262  23.900 0.983   1.00 19.80  ? 29  ASP   A C   1 
ATOM   219  O  O   . ASP   A 1 29 ? 7.297  23.763 0.206   1.00 21.04  ? 29  ASP   A O   1 
ATOM   220  C  CB  . ASP   A 1 29 ? 7.750  24.546 3.305   1.00 20.47  ? 29  ASP   A CB  1 
ATOM   221  C  CG  . ASP   A 1 29 ? 7.607  24.162 4.779   1.00 32.05  ? 29  ASP   A CG  1 
ATOM   222  O  OD1 . ASP   A 1 29 ? 7.206  23.045 5.110   1.00 24.26  ? 29  ASP   A OD1 1 
ATOM   223  O  OD2 . ASP   A 1 29 ? 7.871  25.023 5.622   1.00 43.06  ? 29  ASP   A OD2 1 
ATOM   224  N  N   . ASP   A 1 30 ? 9.381  24.536 0.642   1.00 18.83  ? 30  ASP   A N   1 
ATOM   225  C  CA  . ASP   A 1 30 ? 9.567  25.271 -0.601  1.00 18.34  ? 30  ASP   A CA  1 
ATOM   226  C  C   . ASP   A 1 30 ? 10.726 24.652 -1.384  1.00 17.21  ? 30  ASP   A C   1 
ATOM   227  O  O   . ASP   A 1 30 ? 11.505 23.843 -0.871  1.00 21.21  ? 30  ASP   A O   1 
ATOM   228  C  CB  . ASP   A 1 30 ? 9.877  26.744 -0.316  1.00 21.85  ? 30  ASP   A CB  1 
ATOM   229  C  CG  . ASP   A 1 30 ? 8.772  27.430 0.491   1.00 26.16  ? 30  ASP   A CG  1 
ATOM   230  O  OD1 . ASP   A 1 30 ? 7.593  27.191 0.199   1.00 30.38  ? 30  ASP   A OD1 1 
ATOM   231  O  OD2 . ASP   A 1 30 ? 9.121  28.138 1.447   1.00 37.98  ? 30  ASP   A OD2 1 
ATOM   232  N  N   . THR   A 1 31 ? 10.897 25.124 -2.614  1.00 17.93  ? 31  THR   A N   1 
ATOM   233  C  CA  . THR   A 1 31 ? 11.916 24.637 -3.541  1.00 15.54  ? 31  THR   A CA  1 
ATOM   234  C  C   . THR   A 1 31 ? 13.021 25.677 -3.609  1.00 18.57  ? 31  THR   A C   1 
ATOM   235  O  O   . THR   A 1 31 ? 12.735 26.863 -3.808  1.00 20.76  ? 31  THR   A O   1 
ATOM   236  C  CB  . THR   A 1 31 ? 11.280 24.427 -4.915  1.00 18.57  ? 31  THR   A CB  1 
ATOM   237  O  OG1 . THR   A 1 31 ? 10.380 23.323 -4.822  1.00 18.41  ? 31  THR   A OG1 1 
ATOM   238  C  CG2 . THR   A 1 31 ? 12.291 24.179 -6.022  1.00 17.26  ? 31  THR   A CG2 1 
ATOM   239  N  N   . VAL   A 1 32 ? 14.276 25.234 -3.467  1.00 18.42  ? 32  VAL   A N   1 
ATOM   240  C  CA  . VAL   A 1 32 ? 15.414 26.150 -3.394  1.00 18.47  ? 32  VAL   A CA  1 
ATOM   241  C  C   . VAL   A 1 32 ? 16.480 25.653 -4.354  1.00 20.98  ? 32  VAL   A C   1 
ATOM   242  O  O   . VAL   A 1 32 ? 16.929 24.510 -4.249  1.00 19.01  ? 32  VAL   A O   1 
ATOM   243  C  CB  . VAL   A 1 32 ? 16.005 26.249 -1.970  1.00 23.28  ? 32  VAL   A CB  1 
ATOM   244  C  CG1 . VAL   A 1 32 ? 17.073 27.372 -1.941  1.00 26.27  ? 32  VAL   A CG1 1 
ATOM   245  C  CG2 . VAL   A 1 32 ? 14.928 26.522 -0.943  1.00 24.77  ? 32  VAL   A CG2 1 
ATOM   246  N  N   . ILE   A 1 33 ? 16.950 26.539 -5.223  1.00 18.65  ? 33  ILE   A N   1 
ATOM   247  C  CA  . ILE   A 1 33 ? 17.877 26.187 -6.295  1.00 18.01  ? 33  ILE   A CA  1 
ATOM   248  C  C   . ILE   A 1 33 ? 19.072 27.117 -6.163  1.00 24.15  ? 33  ILE   A C   1 
ATOM   249  O  O   . ILE   A 1 33 ? 18.936 28.267 -5.720  1.00 21.54  ? 33  ILE   A O   1 
ATOM   250  C  CB  . ILE   A 1 33 ? 17.216 26.368 -7.685  1.00 24.49  ? 33  ILE   A CB  1 
ATOM   251  C  CG1 . ILE   A 1 33 ? 16.006 25.440 -7.873  1.00 29.78  ? 33  ILE   A CG1 1 
ATOM   252  C  CG2 . ILE   A 1 33 ? 18.219 26.245 -8.849  1.00 38.20  ? 33  ILE   A CG2 1 
ATOM   253  C  CD1 . ILE   A 1 33 ? 16.346 24.058 -7.817  1.00 34.01  ? 33  ILE   A CD1 1 
ATOM   254  N  N   . GLU   A 1 34 ? 20.244 26.610 -6.553  1.00 22.99  ? 34  GLU   A N   1 
ATOM   255  C  CA  . GLU   A 1 34 ? 21.466 27.411 -6.514  1.00 27.20  ? 34  GLU   A CA  1 
ATOM   256  C  C   . GLU   A 1 34 ? 21.372 28.633 -7.432  1.00 28.96  ? 34  GLU   A C   1 
ATOM   257  O  O   . GLU   A 1 34 ? 20.558 28.702 -8.364  1.00 27.55  ? 34  GLU   A O   1 
ATOM   258  C  CB  . GLU   A 1 34 ? 22.646 26.541 -6.939  1.00 25.89  ? 34  GLU   A CB  1 
ATOM   259  C  CG  . GLU   A 1 34 ? 22.540 26.140 -8.401  1.00 31.08  ? 34  GLU   A CG  1 
ATOM   260  C  CD  . GLU   A 1 34 ? 23.380 24.906 -8.720  1.00 64.64  ? 34  GLU   A CD  1 
ATOM   261  O  OE1 . GLU   A 1 34 ? 24.422 24.703 -8.057  1.00 66.31  ? 34  GLU   A OE1 1 
ATOM   262  O  OE2 . GLU   A 1 34 ? 22.989 24.135 -9.625  1.00 46.90  ? 34  GLU   A OE2 1 
ATOM   263  N  N   . GLU   A 1 35 ? 22.258 29.601 -7.174  1.00 29.47  ? 35  GLU   A N   1 
ATOM   264  C  CA  . GLU   A 1 35 ? 22.295 30.854 -7.927  1.00 32.27  ? 35  GLU   A CA  1 
ATOM   265  C  C   . GLU   A 1 35 ? 22.227 30.606 -9.427  1.00 29.11  ? 35  GLU   A C   1 
ATOM   266  O  O   . GLU   A 1 35 ? 22.993 29.802 -9.976  1.00 37.41  ? 35  GLU   A O   1 
ATOM   267  C  CB  . GLU   A 1 35 ? 23.581 31.613 -7.585  1.00 37.14  ? 35  GLU   A CB  1 
ATOM   268  C  CG  . GLU   A 1 35 ? 23.594 32.249 -6.211  1.00 60.26  ? 35  GLU   A CG  1 
ATOM   269  C  CD  . GLU   A 1 35 ? 22.766 33.509 -6.148  1.00 85.49  ? 35  GLU   A CD  1 
ATOM   270  O  OE1 . GLU   A 1 35 ? 22.434 34.056 -7.229  1.00 65.38  ? 35  GLU   A OE1 1 
ATOM   271  O  OE2 . GLU   A 1 35 ? 22.479 33.961 -5.012  1.00 73.24  ? 35  GLU   A OE2 1 
ATOM   272  N  N   . MET   A 1 36 ? 21.270 31.251 -10.074 1.00 32.29  ? 36  MET   A N   1 
ATOM   273  C  CA  . MET   A 1 36 ? 21.175 31.305 -11.525 1.00 36.82  ? 36  MET   A CA  1 
ATOM   274  C  C   . MET   A 1 36 ? 20.275 32.481 -11.854 1.00 40.44  ? 36  MET   A C   1 
ATOM   275  O  O   . MET   A 1 36 ? 19.594 33.024 -10.984 1.00 35.08  ? 36  MET   A O   1 
ATOM   276  C  CB  . MET   A 1 36 ? 20.611 30.021 -12.137 1.00 38.80  ? 36  MET   A CB  1 
ATOM   277  C  CG  . MET   A 1 36 ? 19.242 29.652 -11.605 1.00 33.67  ? 36  MET   A CG  1 
ATOM   278  S  SD  . MET   A 1 36 ? 18.513 28.175 -12.373 1.00 40.70  ? 36  MET   A SD  1 
ATOM   279  C  CE  . MET   A 1 36 ? 18.745 28.513 -14.121 1.00 42.45  ? 36  MET   A CE  1 
ATOM   280  N  N   . SER   A 1 37 ? 20.265 32.862 -13.123 1.00 41.20  ? 37  SER   A N   1 
ATOM   281  C  CA  . SER   A 1 37 ? 19.413 33.954 -13.560 1.00 43.51  ? 37  SER   A CA  1 
ATOM   282  C  C   . SER   A 1 37 ? 18.091 33.378 -14.040 1.00 44.63  ? 37  SER   A C   1 
ATOM   283  O  O   . SER   A 1 37 ? 18.067 32.438 -14.843 1.00 46.53  ? 37  SER   A O   1 
ATOM   284  C  CB  . SER   A 1 37 ? 20.083 34.772 -14.663 1.00 52.22  ? 37  SER   A CB  1 
ATOM   285  O  OG  . SER   A 1 37 ? 20.027 34.071 -15.887 1.00 79.82  ? 37  SER   A OG  1 
ATOM   286  N  N   . LEU   A 1 38 ? 17.002 33.916 -13.516 1.00 34.18  ? 38  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 38 ? 15.662 33.546 -13.924 1.00 33.81  ? 38  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 38 ? 14.945 34.802 -14.380 1.00 40.84  ? 38  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 38 ? 15.328 35.917 -13.996 1.00 34.05  ? 38  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 38 ? 14.882 32.890 -12.779 1.00 29.01  ? 38  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 38 ? 15.402 31.507 -12.385 1.00 29.80  ? 38  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 38 ? 14.697 31.065 -11.095 1.00 33.31  ? 38  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 38 ? 15.154 30.520 -13.524 1.00 33.86  ? 38  LEU   A CD2 1 
ATOM   294  N  N   . PRO   A 1 39 ? 13.895 34.661 -15.187 1.00 37.32  ? 39  PRO   A N   1 
ATOM   295  C  CA  . PRO   A 1 39 ? 13.178 35.839 -15.686 1.00 49.20  ? 39  PRO   A CA  1 
ATOM   296  C  C   . PRO   A 1 39 ? 12.239 36.461 -14.659 1.00 42.17  ? 39  PRO   A C   1 
ATOM   297  O  O   . PRO   A 1 39 ? 11.757 35.807 -13.733 1.00 35.52  ? 39  PRO   A O   1 
ATOM   298  C  CB  . PRO   A 1 39 ? 12.397 35.279 -16.885 1.00 43.22  ? 39  PRO   A CB  1 
ATOM   299  C  CG  . PRO   A 1 39 ? 12.133 33.855 -16.520 1.00 44.07  ? 39  PRO   A CG  1 
ATOM   300  C  CD  . PRO   A 1 39 ? 13.400 33.413 -15.806 1.00 34.80  ? 39  PRO   A CD  1 
ATOM   301  N  N   . GLY   A 1 40 ? 11.988 37.759 -14.828 1.00 31.74  ? 40  GLY   A N   1 
ATOM   302  C  CA  . GLY   A 1 40 ? 10.960 38.439 -14.061 1.00 34.15  ? 40  GLY   A CA  1 
ATOM   303  C  C   . GLY   A 1 40 ? 11.502 39.143 -12.828 1.00 24.52  ? 40  GLY   A C   1 
ATOM   304  O  O   . GLY   A 1 40 ? 12.711 39.209 -12.577 1.00 30.15  ? 40  GLY   A O   1 
ATOM   305  N  N   . ARG   A 1 41 ? 10.564 39.666 -12.045 1.00 24.14  ? 41  ARG   A N   1 
ATOM   306  C  CA  . ARG   A 1 41 ? 10.898 40.348 -10.799 1.00 23.81  ? 41  ARG   A CA  1 
ATOM   307  C  C   . ARG   A 1 41 ? 10.939 39.320 -9.680  1.00 28.71  ? 41  ARG   A C   1 
ATOM   308  O  O   . ARG   A 1 41 ? 10.328 38.255 -9.768  1.00 30.77  ? 41  ARG   A O   1 
ATOM   309  C  CB  . ARG   A 1 41 ? 9.870  41.430 -10.482 1.00 24.40  ? 41  ARG   A CB  1 
ATOM   310  C  CG  . ARG   A 1 41 ? 9.889  42.553 -11.502 1.00 27.81  ? 41  ARG   A CG  1 
ATOM   311  C  CD  . ARG   A 1 41 ? 8.995  43.703 -11.128 1.00 25.79  ? 41  ARG   A CD  1 
ATOM   312  N  NE  . ARG   A 1 41 ? 9.185  44.182 -9.761  1.00 30.40  ? 41  ARG   A NE  1 
ATOM   313  C  CZ  . ARG   A 1 41 ? 10.007 45.176 -9.431  1.00 29.67  ? 41  ARG   A CZ  1 
ATOM   314  N  NH1 . ARG   A 1 41 ? 10.818 45.727 -10.321 1.00 22.08  ? 41  ARG   A NH1 1 
ATOM   315  N  NH2 . ARG   A 1 41 ? 10.033 45.606 -8.174  1.00 25.31  ? 41  ARG   A NH2 1 
ATOM   316  N  N   . TRP   A 1 42 ? 11.693 39.624 -8.645  1.00 21.38  ? 42  TRP   A N   1 
ATOM   317  C  CA  . TRP   A 1 42 ? 11.781 38.743 -7.501  1.00 21.49  ? 42  TRP   A CA  1 
ATOM   318  C  C   . TRP   A 1 42 ? 11.426 39.527 -6.255  1.00 26.70  ? 42  TRP   A C   1 
ATOM   319  O  O   . TRP   A 1 42 ? 11.399 40.766 -6.250  1.00 23.08  ? 42  TRP   A O   1 
ATOM   320  C  CB  . TRP   A 1 42 ? 13.168 38.101 -7.393  1.00 25.50  ? 42  TRP   A CB  1 
ATOM   321  C  CG  . TRP   A 1 42 ? 14.345 39.075 -7.254  1.00 24.45  ? 42  TRP   A CG  1 
ATOM   322  C  CD1 . TRP   A 1 42 ? 15.062 39.670 -8.278  1.00 25.05  ? 42  TRP   A CD1 1 
ATOM   323  C  CD2 . TRP   A 1 42 ? 14.928 39.529 -6.034  1.00 21.75  ? 42  TRP   A CD2 1 
ATOM   324  N  NE1 . TRP   A 1 42 ? 16.043 40.471 -7.753  1.00 24.27  ? 42  TRP   A NE1 1 
ATOM   325  C  CE2 . TRP   A 1 42 ? 15.984 40.406 -6.379  1.00 23.90  ? 42  TRP   A CE2 1 
ATOM   326  C  CE3 . TRP   A 1 42 ? 14.661 39.279 -4.671  1.00 21.72  ? 42  TRP   A CE3 1 
ATOM   327  C  CZ2 . TRP   A 1 42 ? 16.801 41.007 -5.409  1.00 24.06  ? 42  TRP   A CZ2 1 
ATOM   328  C  CZ3 . TRP   A 1 42 ? 15.452 39.889 -3.708  1.00 27.19  ? 42  TRP   A CZ3 1 
ATOM   329  C  CH2 . TRP   A 1 42 ? 16.507 40.755 -4.084  1.00 26.39  ? 42  TRP   A CH2 1 
ATOM   330  N  N   . LYS   A 1 43 ? 11.110 38.727 -5.259  1.00 21.15  ? 43  LYS   A N   1 
ATOM   331  C  CA  . LYS   A 1 43 ? 10.740 39.246 -4.008  1.00 25.30  ? 43  LYS   A CA  1 
ATOM   332  C  C   . LYS   A 1 43 ? 11.669 38.629 -2.905  1.00 26.78  ? 43  LYS   A C   1 
ATOM   333  O  O   . LYS   A 1 43 ? 12.215 37.572 -3.107  1.00 24.07  ? 43  LYS   A O   1 
ATOM   334  C  CB  . LYS   A 1 43 ? 9.291  38.882 -3.688  1.00 30.31  ? 43  LYS   A CB  1 
ATOM   335  C  CG  . LYS   A 1 43 ? 8.265  39.811 -4.296  1.00 47.71  ? 43  LYS   A CG  1 
ATOM   336  C  CD  . LYS   A 1 43 ? 6.866  39.412 -3.873  1.00 69.99  ? 43  LYS   A CD  1 
ATOM   337  C  CE  . LYS   A 1 43 ? 6.567  37.976 -4.248  1.00 65.33  ? 43  LYS   A CE  1 
ATOM   338  N  NZ  . LYS   A 1 43 ? 5.528  37.921 -5.310  1.00 74.14  ? 43  LYS   A NZ  1 
ATOM   339  N  N   . PRO   A 1 44 ? 11.836 39.296 -1.742  1.00 22.37  ? 44  PRO   A N   1 
ATOM   340  C  CA  . PRO   A 1 44 ? 12.742 38.763 -0.728  1.00 24.09  ? 44  PRO   A CA  1 
ATOM   341  C  C   . PRO   A 1 44 ? 12.043 37.747 0.163   1.00 27.32  ? 44  PRO   A C   1 
ATOM   342  O  O   . PRO   A 1 44 ? 10.837 37.822 0.414   1.00 30.40  ? 44  PRO   A O   1 
ATOM   343  C  CB  . PRO   A 1 44 ? 13.146 40.019 0.061   1.00 31.35  ? 44  PRO   A CB  1 
ATOM   344  C  CG  . PRO   A 1 44 ? 11.908 40.890 -0.011  1.00 31.83  ? 44  PRO   A CG  1 
ATOM   345  C  CD  . PRO   A 1 44 ? 11.271 40.620 -1.358  1.00 30.76  ? 44  PRO   A CD  1 
ATOM   346  N  N   . LYS   A 1 45 ? 12.820 36.770 0.630   1.00 27.53  ? 45  LYS   A N   1 
ATOM   347  C  CA  . LYS   A 1 45 ? 12.288 35.779 1.558   1.00 24.14  ? 45  LYS   A CA  1 
ATOM   348  C  C   . LYS   A 1 45 ? 13.423 35.312 2.454   1.00 32.91  ? 45  LYS   A C   1 
ATOM   349  O  O   . LYS   A 1 45 ? 14.563 35.185 2.003   1.00 31.55  ? 45  LYS   A O   1 
ATOM   350  C  CB  . LYS   A 1 45 ? 11.673 34.581 0.820   1.00 31.14  ? 45  LYS   A CB  1 
ATOM   351  C  CG  . LYS   A 1 45 ? 10.883 33.667 1.729   1.00 33.54  ? 45  LYS   A CG  1 
ATOM   352  C  CD  . LYS   A 1 45 ? 9.900  32.862 0.938   1.00 41.38  ? 45  LYS   A CD  1 
ATOM   353  C  CE  . LYS   A 1 45 ? 9.382  31.680 1.719   1.00 47.03  ? 45  LYS   A CE  1 
ATOM   354  N  NZ  . LYS   A 1 45 ? 8.012  31.963 2.218   1.00 52.39  ? 45  LYS   A NZ  1 
ATOM   355  N  N   . MET   A 1 46 ? 13.105 35.065 3.719   1.00 29.69  ? 46  MET   A N   1 
ATOM   356  C  CA  . MET   A 1 46 ? 14.046 34.461 4.657   1.00 31.70  ? 46  MET   A CA  1 
ATOM   357  C  C   . MET   A 1 46 ? 13.663 33.002 4.826   1.00 32.94  ? 46  MET   A C   1 
ATOM   358  O  O   . MET   A 1 46 ? 12.478 32.684 4.969   1.00 33.39  ? 46  MET   A O   1 
ATOM   359  C  CB  . MET   A 1 46 ? 14.013 35.154 6.018   1.00 41.63  ? 46  MET   A CB  1 
ATOM   360  C  CG  . MET   A 1 46 ? 14.514 36.563 6.014   1.00 54.38  ? 46  MET   A CG  1 
ATOM   361  S  SD  . MET   A 1 46 ? 16.292 36.481 6.243   1.00 78.16  ? 46  MET   A SD  1 
ATOM   362  C  CE  . MET   A 1 46 ? 16.331 36.011 7.966   1.00 57.41  ? 46  MET   A CE  1 
ATOM   363  N  N   . ILE   A 1 47 ? 14.646 32.114 4.748   1.00 32.65  ? 47  ILE   A N   1 
ATOM   364  C  CA  . ILE   A 1 47 ? 14.377 30.705 4.977   1.00 29.11  ? 47  ILE   A CA  1 
ATOM   365  C  C   . ILE   A 1 47 ? 15.325 30.209 6.050   1.00 42.47  ? 47  ILE   A C   1 
ATOM   366  O  O   . ILE   A 1 47 ? 16.479 30.649 6.135   1.00 32.22  ? 47  ILE   A O   1 
ATOM   367  C  CB  . ILE   A 1 47 ? 14.469 29.869 3.689   1.00 28.85  ? 47  ILE   A CB  1 
ATOM   368  C  CG1 . ILE   A 1 47 ? 15.844 29.977 3.043   1.00 30.12  ? 47  ILE   A CG1 1 
ATOM   369  C  CG2 . ILE   A 1 47 ? 13.309 30.255 2.728   1.00 28.95  ? 47  ILE   A CG2 1 
ATOM   370  C  CD1 . ILE   A 1 47 ? 16.060 28.964 1.936   1.00 38.31  ? 47  ILE   A CD1 1 
ATOM   371  N  N   . GLY   A 1 48 ? 14.807 29.335 6.899   1.00 44.77  ? 48  GLY   A N   1 
ATOM   372  C  CA  . GLY   A 1 48 ? 15.542 28.870 8.045   1.00 61.55  ? 48  GLY   A CA  1 
ATOM   373  C  C   . GLY   A 1 48 ? 15.652 27.377 7.973   1.00 45.87  ? 48  GLY   A C   1 
ATOM   374  O  O   . GLY   A 1 48 ? 14.668 26.680 7.734   1.00 43.03  ? 48  GLY   A O   1 
ATOM   375  N  N   . GLY   A 1 49 ? 16.856 26.877 8.115   1.00 33.67  ? 49  GLY   A N   1 
ATOM   376  C  CA  . GLY   A 1 49 ? 17.005 25.450 8.158   1.00 34.62  ? 49  GLY   A CA  1 
ATOM   377  C  C   . GLY   A 1 49 ? 17.729 25.082 9.427   1.00 49.73  ? 49  GLY   A C   1 
ATOM   378  O  O   . GLY   A 1 49 ? 17.581 25.717 10.480  1.00 40.91  ? 49  GLY   A O   1 
ATOM   379  N  N   A ILE   A 1 50 ? 18.577 24.067 9.327   0.53 36.13  ? 50  ILE   A N   1 
ATOM   380  N  N   B ILE   A 1 50 ? 18.501 24.018 9.343   0.47 36.19  ? 50  ILE   A N   1 
ATOM   381  C  CA  A ILE   A 1 50 ? 19.180 23.543 10.537  0.53 32.82  ? 50  ILE   A CA  1 
ATOM   382  C  CA  B ILE   A 1 50 ? 19.426 23.695 10.409  0.47 32.69  ? 50  ILE   A CA  1 
ATOM   383  C  C   A ILE   A 1 50 ? 20.255 24.479 11.064  0.53 33.56  ? 50  ILE   A C   1 
ATOM   384  C  C   B ILE   A 1 50 ? 20.592 24.662 10.287  0.47 35.01  ? 50  ILE   A C   1 
ATOM   385  O  O   A ILE   A 1 50 ? 20.480 24.540 12.274  0.53 39.06  ? 50  ILE   A O   1 
ATOM   386  O  O   B ILE   A 1 50 ? 21.067 24.942 9.179   0.47 30.98  ? 50  ILE   A O   1 
ATOM   387  C  CB  A ILE   A 1 50 ? 19.709 22.121 10.270  0.53 38.54  ? 50  ILE   A CB  1 
ATOM   388  C  CB  B ILE   A 1 50 ? 19.860 22.223 10.313  0.47 38.32  ? 50  ILE   A CB  1 
ATOM   389  C  CG1 A ILE   A 1 50 ? 19.501 21.258 11.509  0.53 40.27  ? 50  ILE   A CG1 1 
ATOM   390  C  CG1 B ILE   A 1 50 ? 19.710 21.548 11.671  0.47 39.94  ? 50  ILE   A CG1 1 
ATOM   391  C  CG2 A ILE   A 1 50 ? 21.156 22.147 9.809   0.53 40.42  ? 50  ILE   A CG2 1 
ATOM   392  C  CG2 B ILE   A 1 50 ? 21.287 22.075 9.807   0.47 40.64  ? 50  ILE   A CG2 1 
ATOM   393  C  CD1 A ILE   A 1 50 ? 19.018 19.865 11.199  0.53 42.13  ? 50  ILE   A CD1 1 
ATOM   394  C  CD1 B ILE   A 1 50 ? 19.248 20.118 11.570  0.47 42.02  ? 50  ILE   A CD1 1 
ATOM   395  N  N   A GLY   A 1 51 ? 20.911 25.243 10.188  0.53 26.59  ? 51  GLY   A N   1 
ATOM   396  N  N   B GLY   A 1 51 ? 20.995 25.244 11.407  0.47 30.15  ? 51  GLY   A N   1 
ATOM   397  C  CA  A GLY   A 1 51 ? 22.077 26.000 10.599  0.53 27.32  ? 51  GLY   A CA  1 
ATOM   398  C  CA  B GLY   A 1 51 ? 22.145 26.107 11.401  0.47 33.36  ? 51  GLY   A CA  1 
ATOM   399  C  C   A GLY   A 1 51 ? 21.873 27.502 10.696  0.53 39.78  ? 51  GLY   A C   1 
ATOM   400  C  C   B GLY   A 1 51 ? 21.860 27.572 11.158  0.47 39.69  ? 51  GLY   A C   1 
ATOM   401  O  O   A GLY   A 1 51 ? 22.847 28.255 10.676  0.53 41.90  ? 51  GLY   A O   1 
ATOM   402  O  O   B GLY   A 1 51 ? 22.787 28.380 11.259  0.47 44.65  ? 51  GLY   A O   1 
ATOM   403  N  N   . GLY   A 1 52 ? 20.625 27.947 10.825  1.00 35.33  ? 52  GLY   A N   1 
ATOM   404  C  CA  . GLY   A 1 52 ? 20.316 29.369 10.791  1.00 49.44  ? 52  GLY   A CA  1 
ATOM   405  C  C   . GLY   A 1 52 ? 19.471 29.786 9.591   1.00 50.24  ? 52  GLY   A C   1 
ATOM   406  O  O   . GLY   A 1 52 ? 18.805 28.959 8.967   1.00 43.61  ? 52  GLY   A O   1 
ATOM   407  N  N   . PHE   A 1 53 ? 19.499 31.090 9.285   1.00 45.17  ? 53  PHE   A N   1 
ATOM   408  C  CA  . PHE   A 1 53 ? 18.659 31.710 8.263   1.00 41.41  ? 53  PHE   A CA  1 
ATOM   409  C  C   . PHE   A 1 53 ? 19.535 32.288 7.156   1.00 52.94  ? 53  PHE   A C   1 
ATOM   410  O  O   . PHE   A 1 53 ? 20.653 32.740 7.408   1.00 44.99  ? 53  PHE   A O   1 
ATOM   411  C  CB  . PHE   A 1 53 ? 17.801 32.825 8.885   1.00 47.75  ? 53  PHE   A CB  1 
ATOM   412  C  CG  . PHE   A 1 53 ? 16.561 32.324 9.581   1.00 55.43  ? 53  PHE   A CG  1 
ATOM   413  C  CD1 . PHE   A 1 53 ? 15.393 32.085 8.877   1.00 68.86  ? 53  PHE   A CD1 1 
ATOM   414  C  CD2 . PHE   A 1 53 ? 16.584 32.052 10.944  1.00 62.25  ? 53  PHE   A CD2 1 
ATOM   415  C  CE1 . PHE   A 1 53 ? 14.254 31.615 9.527   1.00 66.68  ? 53  PHE   A CE1 1 
ATOM   416  C  CE2 . PHE   A 1 53 ? 15.462 31.577 11.596  1.00 57.10  ? 53  PHE   A CE2 1 
ATOM   417  C  CZ  . PHE   A 1 53 ? 14.293 31.355 10.887  1.00 68.00  ? 53  PHE   A CZ  1 
ATOM   418  N  N   . ILE   A 1 54 ? 19.031 32.251 5.915   1.00 33.43  ? 54  ILE   A N   1 
ATOM   419  C  CA  . ILE   A 1 54 ? 19.669 32.897 4.775   1.00 28.49  ? 54  ILE   A CA  1 
ATOM   420  C  C   . ILE   A 1 54 ? 18.577 33.652 4.022   1.00 29.03  ? 54  ILE   A C   1 
ATOM   421  O  O   . ILE   A 1 54 ? 17.393 33.325 4.117   1.00 31.27  ? 54  ILE   A O   1 
ATOM   422  C  CB  . ILE   A 1 54 ? 20.388 31.919 3.821   1.00 38.78  ? 54  ILE   A CB  1 
ATOM   423  C  CG1 . ILE   A 1 54 ? 19.376 31.023 3.093   1.00 39.53  ? 54  ILE   A CG1 1 
ATOM   424  C  CG2 . ILE   A 1 54 ? 21.401 31.057 4.581   1.00 47.23  ? 54  ILE   A CG2 1 
ATOM   425  C  CD1 . ILE   A 1 54 ? 19.981 30.206 1.953   1.00 41.28  ? 54  ILE   A CD1 1 
ATOM   426  N  N   . LYS   A 1 55 ? 18.992 34.684 3.286   1.00 34.35  ? 55  LYS   A N   1 
ATOM   427  C  CA  . LYS   A 1 55 ? 18.088 35.432 2.415   1.00 28.90  ? 55  LYS   A CA  1 
ATOM   428  C  C   . LYS   A 1 55 ? 18.180 34.862 1.011   1.00 26.28  ? 55  LYS   A C   1 
ATOM   429  O  O   . LYS   A 1 55 ? 19.271 34.577 0.506   1.00 33.44  ? 55  LYS   A O   1 
ATOM   430  C  CB  . LYS   A 1 55 ? 18.434 36.925 2.389   1.00 38.43  ? 55  LYS   A CB  1 
ATOM   431  C  CG  . LYS   A 1 55 ? 19.861 37.194 1.947   1.00 77.98  ? 55  LYS   A CG  1 
ATOM   432  C  CD  . LYS   A 1 55 ? 20.552 38.264 2.777   1.00 98.18  ? 55  LYS   A CD  1 
ATOM   433  C  CE  . LYS   A 1 55 ? 21.997 38.458 2.316   1.00 99.01  ? 55  LYS   A CE  1 
ATOM   434  N  NZ  . LYS   A 1 55 ? 22.540 39.802 2.676   1.00 94.85  ? 55  LYS   A NZ  1 
ATOM   435  N  N   . VAL   A 1 56 ? 17.028 34.675 0.382   1.00 24.82  ? 56  VAL   A N   1 
ATOM   436  C  CA  . VAL   A 1 56 ? 16.958 34.131 -0.965  1.00 25.03  ? 56  VAL   A CA  1 
ATOM   437  C  C   . VAL   A 1 56 ? 16.058 35.050 -1.781  1.00 24.13  ? 56  VAL   A C   1 
ATOM   438  O  O   . VAL   A 1 56 ? 15.368 35.933 -1.248  1.00 26.31  ? 56  VAL   A O   1 
ATOM   439  C  CB  . VAL   A 1 56 ? 16.423 32.675 -0.972  1.00 28.23  ? 56  VAL   A CB  1 
ATOM   440  C  CG1 . VAL   A 1 56 ? 17.395 31.745 -0.207  1.00 31.31  ? 56  VAL   A CG1 1 
ATOM   441  C  CG2 . VAL   A 1 56 ? 15.077 32.655 -0.270  1.00 26.72  ? 56  VAL   A CG2 1 
ATOM   442  N  N   . ARG   A 1 57 ? 16.093 34.849 -3.087  1.00 21.39  ? 57  ARG   A N   1 
ATOM   443  C  CA  . ARG   A 1 57 ? 15.224 35.543 -4.014  1.00 20.47  ? 57  ARG   A CA  1 
ATOM   444  C  C   . ARG   A 1 57 ? 14.066 34.657 -4.427  1.00 26.92  ? 57  ARG   A C   1 
ATOM   445  O  O   . ARG   A 1 57 ? 14.284 33.528 -4.869  1.00 23.44  ? 57  ARG   A O   1 
ATOM   446  C  CB  . ARG   A 1 57 ? 16.015 35.991 -5.242  1.00 22.46  ? 57  ARG   A CB  1 
ATOM   447  C  CG  . ARG   A 1 57 ? 17.346 36.673 -4.869  1.00 25.73  ? 57  ARG   A CG  1 
ATOM   448  C  CD  . ARG   A 1 57 ? 17.877 37.527 -6.005  1.00 29.94  ? 57  ARG   A CD  1 
ATOM   449  N  NE  . ARG   A 1 57 ? 17.969 36.805 -7.274  1.00 40.81  ? 57  ARG   A NE  1 
ATOM   450  C  CZ  . ARG   A 1 57 ? 18.954 35.976 -7.613  1.00 57.96  ? 57  ARG   A CZ  1 
ATOM   451  N  NH1 . ARG   A 1 57 ? 19.933 35.678 -6.773  1.00 46.59  ? 57  ARG   A NH1 1 
ATOM   452  N  NH2 . ARG   A 1 57 ? 18.956 35.429 -8.827  1.00 44.65  ? 57  ARG   A NH2 1 
ATOM   453  N  N   . GLN   A 1 58 ? 12.842 35.168 -4.294  1.00 21.75  ? 58  GLN   A N   1 
ATOM   454  C  CA  . GLN   A 1 58 ? 11.654 34.398 -4.659  1.00 17.97  ? 58  GLN   A CA  1 
ATOM   455  C  C   . GLN   A 1 58 ? 11.177 34.767 -6.058  1.00 25.13  ? 58  GLN   A C   1 
ATOM   456  O  O   . GLN   A 1 58 ? 10.850 35.935 -6.320  1.00 22.80  ? 58  GLN   A O   1 
ATOM   457  C  CB  . GLN   A 1 58 ? 10.538 34.643 -3.648  1.00 20.29  ? 58  GLN   A CB  1 
ATOM   458  C  CG  . GLN   A 1 58 ? 9.229  33.994 -4.109  1.00 24.69  ? 58  GLN   A CG  1 
ATOM   459  C  CD  . GLN   A 1 58 ? 8.109  34.103 -3.080  1.00 31.98  ? 58  GLN   A CD  1 
ATOM   460  O  OE1 . GLN   A 1 58 ? 8.351  34.122 -1.884  1.00 31.99  ? 58  GLN   A OE1 1 
ATOM   461  N  NE2 . GLN   A 1 58 ? 6.875  34.156 -3.557  1.00 33.70  ? 58  GLN   A NE2 1 
ATOM   462  N  N   . TYR   A 1 59 ? 11.113 33.776 -6.954  1.00 19.47  ? 59  TYR   A N   1 
ATOM   463  C  CA  . TYR   A 1 59 ? 10.556 33.971 -8.289  1.00 19.15  ? 59  TYR   A CA  1 
ATOM   464  C  C   . TYR   A 1 59 ? 9.266  33.177 -8.394  1.00 28.56  ? 59  TYR   A C   1 
ATOM   465  O  O   . TYR   A 1 59 ? 9.223  32.016 -7.982  1.00 27.19  ? 59  TYR   A O   1 
ATOM   466  C  CB  . TYR   A 1 59 ? 11.530 33.500 -9.386  1.00 20.66  ? 59  TYR   A CB  1 
ATOM   467  C  CG  . TYR   A 1 59 ? 12.779 34.320 -9.514  1.00 21.91  ? 59  TYR   A CG  1 
ATOM   468  C  CD1 . TYR   A 1 59 ? 13.887 34.081 -8.710  1.00 22.31  ? 59  TYR   A CD1 1 
ATOM   469  C  CD2 . TYR   A 1 59 ? 12.844 35.387 -10.437 1.00 25.50  ? 59  TYR   A CD2 1 
ATOM   470  C  CE1 . TYR   A 1 59 ? 15.043 34.849 -8.829  1.00 26.80  ? 59  TYR   A CE1 1 
ATOM   471  C  CE2 . TYR   A 1 59 ? 14.007 36.158 -10.544 1.00 26.09  ? 59  TYR   A CE2 1 
ATOM   472  C  CZ  . TYR   A 1 59 ? 15.095 35.873 -9.751  1.00 32.91  ? 59  TYR   A CZ  1 
ATOM   473  O  OH  . TYR   A 1 59 ? 16.247 36.624 -9.865  1.00 30.02  ? 59  TYR   A OH  1 
ATOM   474  N  N   . ASP   A 1 60 ? 8.227  33.773 -8.972  1.00 23.49  ? 60  ASP   A N   1 
ATOM   475  C  CA  . ASP   A 1 60 ? 6.953  33.068 -9.079  1.00 24.95  ? 60  ASP   A CA  1 
ATOM   476  C  C   . ASP   A 1 60 ? 6.694  32.577 -10.503 1.00 23.65  ? 60  ASP   A C   1 
ATOM   477  O  O   . ASP   A 1 60 ? 7.233  33.094 -11.484 1.00 25.45  ? 60  ASP   A O   1 
ATOM   478  C  CB  . ASP   A 1 60 ? 5.809  33.960 -8.604  1.00 30.50  ? 60  ASP   A CB  1 
ATOM   479  C  CG  . ASP   A 1 60 ? 5.933  34.322 -7.116  1.00 35.39  ? 60  ASP   A CG  1 
ATOM   480  O  OD1 . ASP   A 1 60 ? 6.289  33.423 -6.297  1.00 33.50  ? 60  ASP   A OD1 1 
ATOM   481  O  OD2 . ASP   A 1 60 ? 5.665  35.484 -6.760  1.00 47.48  ? 60  ASP   A OD2 1 
ATOM   482  N  N   . GLN   A 1 61 ? 5.851  31.553 -10.588 1.00 21.34  ? 61  GLN   A N   1 
ATOM   483  C  CA  . GLN   A 1 61 ? 5.335  31.029 -11.853 1.00 24.54  ? 61  GLN   A CA  1 
ATOM   484  C  C   . GLN   A 1 61 ? 6.464  30.659 -12.836 1.00 29.58  ? 61  GLN   A C   1 
ATOM   485  O  O   . GLN   A 1 61 ? 6.445  31.004 -14.022 1.00 29.97  ? 61  GLN   A O   1 
ATOM   486  C  CB  . GLN   A 1 61 ? 4.335  32.037 -12.436 1.00 31.68  ? 61  GLN   A CB  1 
ATOM   487  C  CG  . GLN   A 1 61 ? 3.135  31.375 -13.124 1.00 41.80  ? 61  GLN   A CG  1 
ATOM   488  C  CD  . GLN   A 1 61 ? 2.013  32.366 -13.396 1.00 58.34  ? 61  GLN   A CD  1 
ATOM   489  O  OE1 . GLN   A 1 61 ? 1.701  33.207 -12.549 1.00 57.05  ? 61  GLN   A OE1 1 
ATOM   490  N  NE2 . GLN   A 1 61 ? 1.406  32.277 -14.576 1.00 38.77  ? 61  GLN   A NE2 1 
ATOM   491  N  N   . ILE   A 1 62 ? 7.449  29.909 -12.319 1.00 24.21  ? 62  ILE   A N   1 
ATOM   492  C  CA  . ILE   A 1 62 ? 8.602  29.420 -13.074 1.00 21.41  ? 62  ILE   A CA  1 
ATOM   493  C  C   . ILE   A 1 62 ? 8.268  28.019 -13.595 1.00 23.76  ? 62  ILE   A C   1 
ATOM   494  O  O   . ILE   A 1 62 ? 7.798  27.156 -12.832 1.00 22.31  ? 62  ILE   A O   1 
ATOM   495  C  CB  . ILE   A 1 62 ? 9.863  29.388 -12.178 1.00 18.92  ? 62  ILE   A CB  1 
ATOM   496  C  CG1 . ILE   A 1 62 ? 10.232 30.819 -11.694 1.00 22.02  ? 62  ILE   A CG1 1 
ATOM   497  C  CG2 . ILE   A 1 62 ? 11.038 28.671 -12.863 1.00 25.18  ? 62  ILE   A CG2 1 
ATOM   498  C  CD1 . ILE   A 1 62 ? 10.480 31.794 -12.853 1.00 29.07  ? 62  ILE   A CD1 1 
ATOM   499  N  N   . ILE   A 1 63 ? 8.534  27.777 -14.874 1.00 23.22  ? 63  ILE   A N   1 
ATOM   500  C  CA  . ILE   A 1 63 ? 8.348  26.441 -15.444 1.00 22.95  ? 63  ILE   A CA  1 
ATOM   501  C  C   . ILE   A 1 63 ? 9.567  25.589 -15.106 1.00 28.99  ? 63  ILE   A C   1 
ATOM   502  O  O   . ILE   A 1 63 ? 10.718 26.009 -15.286 1.00 28.41  ? 63  ILE   A O   1 
ATOM   503  C  CB  . ILE   A 1 63 ? 8.128  26.513 -16.965 1.00 24.52  ? 63  ILE   A CB  1 
ATOM   504  C  CG1 . ILE   A 1 63 ? 6.887  27.359 -17.284 1.00 38.04  ? 63  ILE   A CG1 1 
ATOM   505  C  CG2 . ILE   A 1 63 ? 7.955  25.092 -17.532 1.00 27.87  ? 63  ILE   A CG2 1 
ATOM   506  C  CD1 . ILE   A 1 63 ? 6.836  27.871 -18.711 1.00 38.70  ? 63  ILE   A CD1 1 
ATOM   507  N  N   . ILE   A 1 64 ? 9.315  24.383 -14.619 1.00 24.39  ? 64  ILE   A N   1 
ATOM   508  C  CA  . ILE   A 1 64 ? 10.369 23.462 -14.236 1.00 23.67  ? 64  ILE   A CA  1 
ATOM   509  C  C   . ILE   A 1 64 ? 9.890  22.047 -14.516 1.00 24.82  ? 64  ILE   A C   1 
ATOM   510  O  O   . ILE   A 1 64 ? 8.775  21.674 -14.154 1.00 29.63  ? 64  ILE   A O   1 
ATOM   511  C  CB  . ILE   A 1 64 ? 10.762 23.676 -12.757 1.00 32.94  ? 64  ILE   A CB  1 
ATOM   512  C  CG1 . ILE   A 1 64 ? 11.807 22.666 -12.304 1.00 31.91  ? 64  ILE   A CG1 1 
ATOM   513  C  CG2 . ILE   A 1 64 ? 9.548  23.725 -11.865 1.00 37.27  ? 64  ILE   A CG2 1 
ATOM   514  C  CD1 . ILE   A 1 64 ? 12.287 22.934 -10.881 1.00 40.50  ? 64  ILE   A CD1 1 
ATOM   515  N  N   A GLU   A 1 65 ? 10.721 21.272 -15.202 0.46 25.10  ? 65  GLU   A N   1 
ATOM   516  N  N   B GLU   A 1 65 ? 10.742 21.249 -15.151 0.54 25.02  ? 65  GLU   A N   1 
ATOM   517  C  CA  A GLU   A 1 65 ? 10.431 19.866 -15.433 0.46 21.90  ? 65  GLU   A CA  1 
ATOM   518  C  CA  B GLU   A 1 65 ? 10.422 19.860 -15.449 0.54 21.81  ? 65  GLU   A CA  1 
ATOM   519  C  C   A GLU   A 1 65 ? 11.187 19.052 -14.397 0.46 25.84  ? 65  GLU   A C   1 
ATOM   520  C  C   B GLU   A 1 65 ? 11.202 18.976 -14.487 0.54 25.74  ? 65  GLU   A C   1 
ATOM   521  O  O   A GLU   A 1 65 ? 12.376 19.289 -14.169 0.46 27.87  ? 65  GLU   A O   1 
ATOM   522  O  O   B GLU   A 1 65 ? 12.424 19.095 -14.395 0.54 28.10  ? 65  GLU   A O   1 
ATOM   523  C  CB  A GLU   A 1 65 ? 10.827 19.434 -16.846 0.46 28.71  ? 65  GLU   A CB  1 
ATOM   524  C  CB  B GLU   A 1 65 ? 10.768 19.537 -16.905 0.54 28.75  ? 65  GLU   A CB  1 
ATOM   525  C  CG  A GLU   A 1 65 ? 10.666 17.942 -17.048 0.46 24.67  ? 65  GLU   A CG  1 
ATOM   526  C  CG  B GLU   A 1 65 ? 10.268 20.608 -17.855 0.54 34.06  ? 65  GLU   A CG  1 
ATOM   527  C  CD  A GLU   A 1 65 ? 11.197 17.467 -18.384 0.46 38.01  ? 65  GLU   A CD  1 
ATOM   528  C  CD  B GLU   A 1 65 ? 10.502 20.284 -19.318 0.54 46.12  ? 65  GLU   A CD  1 
ATOM   529  O  OE1 A GLU   A 1 65 ? 10.804 18.042 -19.414 0.46 41.48  ? 65  GLU   A OE1 1 
ATOM   530  O  OE1 B GLU   A 1 65 ? 10.610 19.091 -19.650 0.54 43.60  ? 65  GLU   A OE1 1 
ATOM   531  O  OE2 A GLU   A 1 65 ? 11.990 16.512 -18.407 0.46 39.53  ? 65  GLU   A OE2 1 
ATOM   532  O  OE2 B GLU   A 1 65 ? 10.585 21.233 -20.129 0.54 50.71  ? 65  GLU   A OE2 1 
ATOM   533  N  N   . ILE   A 1 66 ? 10.491 18.125 -13.748 1.00 22.91  ? 66  ILE   A N   1 
ATOM   534  C  CA  . ILE   A 1 66 ? 11.069 17.333 -12.667 1.00 23.47  ? 66  ILE   A CA  1 
ATOM   535  C  C   . ILE   A 1 66 ? 10.938 15.877 -13.068 1.00 30.35  ? 66  ILE   A C   1 
ATOM   536  O  O   . ILE   A 1 66 ? 9.820  15.353 -13.138 1.00 28.65  ? 66  ILE   A O   1 
ATOM   537  C  CB  . ILE   A 1 66 ? 10.376 17.590 -11.322 1.00 26.70  ? 66  ILE   A CB  1 
ATOM   538  C  CG1 . ILE   A 1 66 ? 10.522 19.058 -10.921 1.00 25.43  ? 66  ILE   A CG1 1 
ATOM   539  C  CG2 . ILE   A 1 66 ? 10.925 16.662 -10.220 1.00 25.74  ? 66  ILE   A CG2 1 
ATOM   540  C  CD1 . ILE   A 1 66 ? 9.426  19.514 -9.991  1.00 30.34  ? 66  ILE   A CD1 1 
ATOM   541  N  N   . ALA   A 1 67 ? 12.066 15.228 -13.315 1.00 28.94  ? 67  ALA   A N   1 
ATOM   542  C  CA  . ALA   A 1 67 ? 12.075 13.848 -13.809 1.00 35.25  ? 67  ALA   A CA  1 
ATOM   543  C  C   . ALA   A 1 67 ? 11.007 13.645 -14.887 1.00 32.58  ? 67  ALA   A C   1 
ATOM   544  O  O   . ALA   A 1 67 ? 10.230 12.688 -14.864 1.00 36.40  ? 67  ALA   A O   1 
ATOM   545  C  CB  . ALA   A 1 67 ? 11.897 12.870 -12.649 1.00 34.43  ? 67  ALA   A CB  1 
ATOM   546  N  N   . GLY   A 1 68 ? 10.933 14.598 -15.816 1.00 33.17  ? 68  GLY   A N   1 
ATOM   547  C  CA  . GLY   A 1 68 ? 10.007 14.494 -16.936 1.00 39.71  ? 68  GLY   A CA  1 
ATOM   548  C  C   . GLY   A 1 68 ? 8.588  14.980 -16.700 1.00 40.25  ? 68  GLY   A C   1 
ATOM   549  O  O   . GLY   A 1 68 ? 7.774  14.902 -17.628 1.00 38.11  ? 68  GLY   A O   1 
ATOM   550  N  N   . HIS   A 1 69 ? 8.262  15.466 -15.499 1.00 30.40  ? 69  HIS   A N   1 
ATOM   551  C  CA  . HIS   A 1 69 ? 6.937  15.966 -15.155 1.00 30.37  ? 69  HIS   A CA  1 
ATOM   552  C  C   . HIS   A 1 69 ? 6.996  17.483 -15.095 1.00 35.35  ? 69  HIS   A C   1 
ATOM   553  O  O   . HIS   A 1 69 ? 7.869  18.040 -14.423 1.00 32.48  ? 69  HIS   A O   1 
ATOM   554  C  CB  . HIS   A 1 69 ? 6.482  15.429 -13.798 1.00 28.69  ? 69  HIS   A CB  1 
ATOM   555  C  CG  . HIS   A 1 69 ? 6.308  13.950 -13.767 1.00 38.63  ? 69  HIS   A CG  1 
ATOM   556  N  ND1 . HIS   A 1 69 ? 7.361  13.072 -13.908 1.00 49.20  ? 69  HIS   A ND1 1 
ATOM   557  C  CD2 . HIS   A 1 69 ? 5.200  13.192 -13.604 1.00 41.37  ? 69  HIS   A CD2 1 
ATOM   558  C  CE1 . HIS   A 1 69 ? 6.907  11.832 -13.846 1.00 41.97  ? 69  HIS   A CE1 1 
ATOM   559  N  NE2 . HIS   A 1 69 ? 5.601  11.877 -13.656 1.00 46.50  ? 69  HIS   A NE2 1 
ATOM   560  N  N   . LYS   A 1 70 ? 6.071  18.147 -15.777 1.00 29.19  ? 70  LYS   A N   1 
ATOM   561  C  CA  . LYS   A 1 70 ? 6.076  19.603 -15.799 1.00 36.45  ? 70  LYS   A CA  1 
ATOM   562  C  C   . LYS   A 1 70 ? 5.366  20.171 -14.572 1.00 30.82  ? 70  LYS   A C   1 
ATOM   563  O  O   . LYS   A 1 70 ? 4.330  19.661 -14.125 1.00 36.30  ? 70  LYS   A O   1 
ATOM   564  C  CB  . LYS   A 1 70 ? 5.422  20.107 -17.080 1.00 41.37  ? 70  LYS   A CB  1 
ATOM   565  C  CG  . LYS   A 1 70 ? 6.089  21.323 -17.674 1.00 53.91  ? 70  LYS   A CG  1 
ATOM   566  C  CD  . LYS   A 1 70 ? 5.749  21.432 -19.149 1.00 72.72  ? 70  LYS   A CD  1 
ATOM   567  C  CE  . LYS   A 1 70 ? 6.944  21.062 -20.006 1.00 72.13  ? 70  LYS   A CE  1 
ATOM   568  N  NZ  . LYS   A 1 70 ? 6.845  21.663 -21.371 1.00 88.94  ? 70  LYS   A NZ  1 
ATOM   569  N  N   . ALA   A 1 71 ? 5.972  21.197 -13.986 1.00 23.40  ? 71  ALA   A N   1 
ATOM   570  C  CA  . ALA   A 1 71 ? 5.419  21.904 -12.849 1.00 21.85  ? 71  ALA   A CA  1 
ATOM   571  C  C   . ALA   A 1 71 ? 5.603  23.381 -13.148 1.00 23.19  ? 71  ALA   A C   1 
ATOM   572  O  O   . ALA   A 1 71 ? 6.487  23.752 -13.920 1.00 26.18  ? 71  ALA   A O   1 
ATOM   573  C  CB  . ALA   A 1 71 ? 6.116  21.546 -11.532 1.00 27.48  ? 71  ALA   A CB  1 
ATOM   574  N  N   . ILE   A 1 72 ? 4.741  24.214 -12.574 1.00 21.83  ? 72  ILE   A N   1 
ATOM   575  C  CA  . ILE   A 1 72 ? 4.874  25.664 -12.717 1.00 20.24  ? 72  ILE   A CA  1 
ATOM   576  C  C   . ILE   A 1 72 ? 4.605  26.248 -11.341 1.00 18.85  ? 72  ILE   A C   1 
ATOM   577  O  O   . ILE   A 1 72 ? 3.492  26.109 -10.820 1.00 22.43  ? 72  ILE   A O   1 
ATOM   578  C  CB  . ILE   A 1 72 ? 3.894  26.274 -13.746 1.00 19.74  ? 72  ILE   A CB  1 
ATOM   579  C  CG1 . ILE   A 1 72 ? 3.968  25.520 -15.081 1.00 22.59  ? 72  ILE   A CG1 1 
ATOM   580  C  CG2 . ILE   A 1 72 ? 4.235  27.752 -13.909 1.00 23.68  ? 72  ILE   A CG2 1 
ATOM   581  C  CD1 . ILE   A 1 72 ? 2.909  25.964 -16.094 1.00 24.26  ? 72  ILE   A CD1 1 
ATOM   582  N  N   . GLY   A 1 73 ? 5.601  26.886 -10.743 1.00 19.83  ? 73  GLY   A N   1 
ATOM   583  C  CA  . GLY   A 1 73 ? 5.386  27.390 -9.403  1.00 21.00  ? 73  GLY   A CA  1 
ATOM   584  C  C   . GLY   A 1 73 ? 6.526  28.232 -8.897  1.00 23.92  ? 73  GLY   A C   1 
ATOM   585  O  O   . GLY   A 1 73 ? 7.364  28.694 -9.667  1.00 23.27  ? 73  GLY   A O   1 
ATOM   586  N  N   . THR   A 1 74 ? 6.552  28.420 -7.578  1.00 19.91  ? 74  THR   A N   1 
ATOM   587  C  CA  . THR   A 1 74 ? 7.509  29.335 -6.950  1.00 20.51  ? 74  THR   A CA  1 
ATOM   588  C  C   . THR   A 1 74 ? 8.842  28.639 -6.703  1.00 22.92  ? 74  THR   A C   1 
ATOM   589  O  O   . THR   A 1 74 ? 8.882  27.527 -6.169  1.00 22.16  ? 74  THR   A O   1 
ATOM   590  C  CB  . THR   A 1 74 ? 6.948  29.853 -5.629  1.00 26.37  ? 74  THR   A CB  1 
ATOM   591  O  OG1 . THR   A 1 74 ? 5.747  30.597 -5.884  1.00 30.49  ? 74  THR   A OG1 1 
ATOM   592  C  CG2 . THR   A 1 74 ? 7.962  30.785 -4.942  1.00 25.93  ? 74  THR   A CG2 1 
ATOM   593  N  N   . VAL   A 1 75 ? 9.935  29.309 -7.055  1.00 17.41  ? 75  VAL   A N   1 
ATOM   594  C  CA  . VAL   A 1 75 ? 11.279 28.780 -6.860  1.00 17.92  ? 75  VAL   A CA  1 
ATOM   595  C  C   . VAL   A 1 75 ? 12.068 29.838 -6.086  1.00 23.35  ? 75  VAL   A C   1 
ATOM   596  O  O   . VAL   A 1 75 ? 11.986 31.027 -6.411  1.00 24.88  ? 75  VAL   A O   1 
ATOM   597  C  CB  . VAL   A 1 75 ? 11.942 28.471 -8.218  1.00 23.99  ? 75  VAL   A CB  1 
ATOM   598  C  CG1 . VAL   A 1 75 ? 13.388 28.139 -8.053  1.00 27.37  ? 75  VAL   A CG1 1 
ATOM   599  C  CG2 . VAL   A 1 75 ? 11.225 27.300 -8.917  1.00 25.33  ? 75  VAL   A CG2 1 
ATOM   600  N  N   . LEU   A 1 76 ? 12.785 29.424 -5.054  1.00 16.94  ? 76  LEU   A N   1 
ATOM   601  C  CA  . LEU   A 1 76 ? 13.680 30.301 -4.300  1.00 18.17  ? 76  LEU   A CA  1 
ATOM   602  C  C   . LEU   A 1 76 ? 15.105 30.087 -4.766  1.00 25.98  ? 76  LEU   A C   1 
ATOM   603  O  O   . LEU   A 1 76 ? 15.527 28.961 -5.023  1.00 22.81  ? 76  LEU   A O   1 
ATOM   604  C  CB  . LEU   A 1 76 ? 13.586 30.010 -2.793  1.00 18.85  ? 76  LEU   A CB  1 
ATOM   605  C  CG  . LEU   A 1 76 ? 12.167 29.983 -2.236  1.00 22.48  ? 76  LEU   A CG  1 
ATOM   606  C  CD1 . LEU   A 1 76 ? 12.214 29.655 -0.755  1.00 22.18  ? 76  LEU   A CD1 1 
ATOM   607  C  CD2 . LEU   A 1 76 ? 11.377 31.334 -2.509  1.00 22.49  ? 76  LEU   A CD2 1 
ATOM   608  N  N   . VAL   A 1 77 ? 15.858 31.171 -4.899  1.00 18.72  ? 77  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 77 ? 17.200 31.085 -5.460  1.00 20.52  ? 77  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 77 ? 18.169 31.667 -4.440  1.00 23.72  ? 77  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 77 ? 17.995 32.810 -3.996  1.00 24.63  ? 77  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 77 ? 17.314 31.830 -6.810  1.00 25.65  ? 77  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 77 ? 18.763 31.800 -7.289  1.00 30.00  ? 77  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 77 ? 16.391 31.192 -7.856  1.00 27.69  ? 77  VAL   A CG2 1 
ATOM   615  N  N   . GLY   A 1 78 ? 19.219 30.913 -4.118  1.00 23.31  ? 78  GLY   A N   1 
ATOM   616  C  CA  . GLY   A 1 78 ? 20.191 31.367 -3.147  1.00 25.89  ? 78  GLY   A CA  1 
ATOM   617  C  C   . GLY   A 1 78 ? 21.307 30.362 -2.964  1.00 33.71  ? 78  GLY   A C   1 
ATOM   618  O  O   . GLY   A 1 78 ? 21.350 29.319 -3.629  1.00 30.23  ? 78  GLY   A O   1 
ATOM   619  N  N   . PRO   A 1 79 ? 22.209 30.641 -2.002  1.00 32.74  ? 79  PRO   A N   1 
ATOM   620  C  CA  . PRO   A 1 79 ? 23.376 29.774 -1.785  1.00 43.71  ? 79  PRO   A CA  1 
ATOM   621  C  C   . PRO   A 1 79 ? 23.021 28.530 -0.983  1.00 40.94  ? 79  PRO   A C   1 
ATOM   622  O  O   . PRO   A 1 79 ? 23.171 28.460 0.240   1.00 41.30  ? 79  PRO   A O   1 
ATOM   623  C  CB  . PRO   A 1 79 ? 24.355 30.685 -1.025  1.00 39.09  ? 79  PRO   A CB  1 
ATOM   624  C  CG  . PRO   A 1 79 ? 23.514 31.763 -0.436  1.00 40.82  ? 79  PRO   A CG  1 
ATOM   625  C  CD  . PRO   A 1 79 ? 22.142 31.739 -1.020  1.00 39.11  ? 79  PRO   A CD  1 
ATOM   626  N  N   . THR   A 1 80 ? 22.554 27.547 -1.673  1.00 37.65  ? 80  THR   A N   1 
ATOM   627  C  CA  . THR   A 1 80 ? 22.251 26.295 -1.041  1.00 28.04  ? 80  THR   A CA  1 
ATOM   628  C  C   . THR   A 1 80 ? 23.267 25.245 -1.472  1.00 25.08  ? 80  THR   A C   1 
ATOM   629  O  O   . THR   A 1 80 ? 23.757 25.269 -2.608  1.00 34.83  ? 80  THR   A O   1 
ATOM   630  C  CB  . THR   A 1 80 ? 20.831 25.869 -1.431  1.00 25.21  ? 80  THR   A CB  1 
ATOM   631  O  OG1 . THR   A 1 80 ? 20.581 24.544 -0.941  1.00 29.53  ? 80  THR   A OG1 1 
ATOM   632  C  CG2 . THR   A 1 80 ? 20.671 25.917 -2.964  1.00 27.24  ? 80  THR   A CG2 1 
ATOM   633  N  N   . PRO   A 1 81 ? 23.640 24.325 -0.579  1.00 30.91  ? 81  PRO   A N   1 
ATOM   634  C  CA  . PRO   A 1 81 ? 24.610 23.288 -0.958  1.00 36.92  ? 81  PRO   A CA  1 
ATOM   635  C  C   . PRO   A 1 81 ? 24.072 22.301 -1.976  1.00 37.75  ? 81  PRO   A C   1 
ATOM   636  O  O   . PRO   A 1 81 ? 24.852 21.709 -2.728  1.00 33.07  ? 81  PRO   A O   1 
ATOM   637  C  CB  . PRO   A 1 81 ? 24.927 22.592 0.369   1.00 32.59  ? 81  PRO   A CB  1 
ATOM   638  C  CG  . PRO   A 1 81 ? 23.826 22.960 1.277   1.00 37.28  ? 81  PRO   A CG  1 
ATOM   639  C  CD  . PRO   A 1 81 ? 23.249 24.252 0.838   1.00 35.00  ? 81  PRO   A CD  1 
ATOM   640  N  N   A VAL   A 1 82 ? 22.765 22.099 -2.030  0.55 28.85  ? 82  VAL   A N   1 
ATOM   641  N  N   B VAL   A 1 82 ? 22.757 22.118 -2.039  0.45 28.86  ? 82  VAL   A N   1 
ATOM   642  C  CA  A VAL   A 1 82 ? 22.164 21.201 -3.005  0.55 26.09  ? 82  VAL   A CA  1 
ATOM   643  C  CA  B VAL   A 1 82 ? 22.125 21.147 -2.931  0.45 26.30  ? 82  VAL   A CA  1 
ATOM   644  C  C   A VAL   A 1 82 ? 20.848 21.812 -3.455  0.55 22.16  ? 82  VAL   A C   1 
ATOM   645  C  C   B VAL   A 1 82 ? 20.813 21.752 -3.419  0.45 22.17  ? 82  VAL   A C   1 
ATOM   646  O  O   A VAL   A 1 82 ? 20.208 22.574 -2.718  0.55 23.80  ? 82  VAL   A O   1 
ATOM   647  O  O   B VAL   A 1 82 ? 20.136 22.460 -2.661  0.45 23.87  ? 82  VAL   A O   1 
ATOM   648  C  CB  A VAL   A 1 82 ? 21.932 19.773 -2.446  0.55 30.88  ? 82  VAL   A CB  1 
ATOM   649  C  CB  B VAL   A 1 82 ? 21.864 19.796 -2.215  0.45 30.43  ? 82  VAL   A CB  1 
ATOM   650  C  CG1 A VAL   A 1 82 ? 23.255 19.056 -2.216  0.55 44.51  ? 82  VAL   A CG1 1 
ATOM   651  C  CG1 B VAL   A 1 82 ? 21.188 18.814 -3.146  0.45 20.08  ? 82  VAL   A CG1 1 
ATOM   652  C  CG2 A VAL   A 1 82 ? 21.131 19.850 -1.166  0.55 27.07  ? 82  VAL   A CG2 1 
ATOM   653  C  CG2 B VAL   A 1 82 ? 23.149 19.200 -1.663  0.45 41.99  ? 82  VAL   A CG2 1 
ATOM   654  N  N   . ASN   A 1 83 ? 20.462 21.497 -4.688  1.00 20.54  ? 83  ASN   A N   1 
ATOM   655  C  CA  . ASN   A 1 83 ? 19.167 21.939 -5.199  1.00 19.07  ? 83  ASN   A CA  1 
ATOM   656  C  C   . ASN   A 1 83 ? 18.103 21.061 -4.551  1.00 20.56  ? 83  ASN   A C   1 
ATOM   657  O  O   . ASN   A 1 83 ? 18.256 19.833 -4.522  1.00 19.36  ? 83  ASN   A O   1 
ATOM   658  C  CB  . ASN   A 1 83 ? 19.094 21.780 -6.720  1.00 18.49  ? 83  ASN   A CB  1 
ATOM   659  C  CG  . ASN   A 1 83 ? 20.087 22.674 -7.429  1.00 21.48  ? 83  ASN   A CG  1 
ATOM   660  O  OD1 . ASN   A 1 83 ? 20.281 23.809 -7.022  1.00 26.21  ? 83  ASN   A OD1 1 
ATOM   661  N  ND2 . ASN   A 1 83 ? 20.804 22.125 -8.412  1.00 22.67  ? 83  ASN   A ND2 1 
ATOM   662  N  N   . ILE   A 1 84 ? 17.040 21.689 -4.038  1.00 16.44  ? 84  ILE   A N   1 
ATOM   663  C  CA  . ILE   A 1 84 ? 16.012 21.018 -3.233  1.00 17.92  ? 84  ILE   A CA  1 
ATOM   664  C  C   . ILE   A 1 84 ? 14.658 21.192 -3.899  1.00 20.10  ? 84  ILE   A C   1 
ATOM   665  O  O   . ILE   A 1 84 ? 14.211 22.325 -4.067  1.00 19.69  ? 84  ILE   A O   1 
ATOM   666  C  CB  . ILE   A 1 84 ? 15.935 21.655 -1.832  1.00 27.12  ? 84  ILE   A CB  1 
ATOM   667  C  CG1 . ILE   A 1 84 ? 17.235 21.439 -1.110  1.00 30.68  ? 84  ILE   A CG1 1 
ATOM   668  C  CG2 . ILE   A 1 84 ? 14.770 21.054 -1.064  1.00 29.28  ? 84  ILE   A CG2 1 
ATOM   669  C  CD1 . ILE   A 1 84 ? 17.424 20.048 -0.806  1.00 29.62  ? 84  ILE   A CD1 1 
ATOM   670  N  N   . ILE   A 1 85 ? 13.962 20.081 -4.183  1.00 16.89  ? 85  ILE   A N   1 
ATOM   671  C  CA  . ILE   A 1 85 ? 12.568 20.142 -4.620  1.00 15.09  ? 85  ILE   A CA  1 
ATOM   672  C  C   . ILE   A 1 85 ? 11.690 19.924 -3.394  1.00 17.27  ? 85  ILE   A C   1 
ATOM   673  O  O   . ILE   A 1 85 ? 11.668 18.826 -2.822  1.00 20.34  ? 85  ILE   A O   1 
ATOM   674  C  CB  . ILE   A 1 85 ? 12.263 19.067 -5.662  1.00 18.56  ? 85  ILE   A CB  1 
ATOM   675  C  CG1 . ILE   A 1 85 ? 13.204 19.218 -6.853  1.00 20.78  ? 85  ILE   A CG1 1 
ATOM   676  C  CG2 . ILE   A 1 85 ? 10.820 19.255 -6.116  1.00 17.59  ? 85  ILE   A CG2 1 
ATOM   677  C  CD1 . ILE   A 1 85 ? 13.263 20.598 -7.501  1.00 24.21  ? 85  ILE   A CD1 1 
ATOM   678  N  N   . GLY   A 1 86 ? 10.936 20.947 -2.996  1.00 18.56  ? 86  GLY   A N   1 
ATOM   679  C  CA  . GLY   A 1 86 ? 10.126 20.877 -1.797  1.00 19.35  ? 86  GLY   A CA  1 
ATOM   680  C  C   . GLY   A 1 86 ? 8.653  20.555 -2.071  1.00 15.27  ? 86  GLY   A C   1 
ATOM   681  O  O   . GLY   A 1 86 ? 8.214  20.304 -3.191  1.00 17.83  ? 86  GLY   A O   1 
ATOM   682  N  N   . ARG   A 1 87 ? 7.867  20.579 -0.985  1.00 18.64  ? 87  ARG   A N   1 
ATOM   683  C  CA  . ARG   A 1 87 ? 6.491  20.096 -1.083  1.00 18.49  ? 87  ARG   A CA  1 
ATOM   684  C  C   . ARG   A 1 87 ? 5.642  20.926 -2.047  1.00 19.30  ? 87  ARG   A C   1 
ATOM   685  O  O   . ARG   A 1 87 ? 4.696  20.392 -2.649  1.00 20.76  ? 87  ARG   A O   1 
ATOM   686  C  CB  . ARG   A 1 87 ? 5.841  20.110 0.308   1.00 19.90  ? 87  ARG   A CB  1 
ATOM   687  C  CG  . ARG   A 1 87 ? 6.407  19.043 1.239   1.00 19.07  ? 87  ARG   A CG  1 
ATOM   688  C  CD  . ARG   A 1 87 ? 5.530  18.937 2.525   1.00 21.17  ? 87  ARG   A CD  1 
ATOM   689  N  NE  . ARG   A 1 87 ? 5.546  20.188 3.283   1.00 21.47  ? 87  ARG   A NE  1 
ATOM   690  C  CZ  . ARG   A 1 87 ? 4.560  21.085 3.284   1.00 23.44  ? 87  ARG   A CZ  1 
ATOM   691  N  NH1 . ARG   A 1 87 ? 3.439  20.893 2.602   1.00 26.05  ? 87  ARG   A NH1 1 
ATOM   692  N  NH2 . ARG   A 1 87 ? 4.714  22.214 3.969   1.00 24.47  ? 87  ARG   A NH2 1 
ATOM   693  N  N   . ASN   A 1 88 ? 5.963  22.215 -2.234  1.00 19.72  ? 88  ASN   A N   1 
ATOM   694  C  CA  . ASN   A 1 88 ? 5.160  23.016 -3.161  1.00 20.47  ? 88  ASN   A CA  1 
ATOM   695  C  C   . ASN   A 1 88 ? 5.162  22.423 -4.562  1.00 23.04  ? 88  ASN   A C   1 
ATOM   696  O  O   . ASN   A 1 88 ? 4.135  22.460 -5.258  1.00 24.93  ? 88  ASN   A O   1 
ATOM   697  C  CB  . ASN   A 1 88 ? 5.638  24.477 -3.177  1.00 19.80  ? 88  ASN   A CB  1 
ATOM   698  C  CG  . ASN   A 1 88 ? 6.965  24.663 -3.891  1.00 21.45  ? 88  ASN   A CG  1 
ATOM   699  O  OD1 . ASN   A 1 88 ? 7.970  24.010 -3.554  1.00 19.57  ? 88  ASN   A OD1 1 
ATOM   700  N  ND2 . ASN   A 1 88 ? 6.992  25.593 -4.845  1.00 22.02  ? 88  ASN   A ND2 1 
ATOM   701  N  N   . LEU   A 1 89 ? 6.296  21.862 -5.008  1.00 19.60  ? 89  LEU   A N   1 
ATOM   702  C  CA  . LEU   A 1 89 ? 6.293  21.211 -6.307  1.00 18.10  ? 89  LEU   A CA  1 
ATOM   703  C  C   . LEU   A 1 89 ? 6.076  19.707 -6.232  1.00 21.69  ? 89  LEU   A C   1 
ATOM   704  O  O   . LEU   A 1 89 ? 5.580  19.120 -7.208  1.00 21.82  ? 89  LEU   A O   1 
ATOM   705  C  CB  . LEU   A 1 89 ? 7.602  21.515 -7.069  1.00 19.06  ? 89  LEU   A CB  1 
ATOM   706  C  CG  . LEU   A 1 89 ? 7.836  23.016 -7.308  1.00 23.52  ? 89  LEU   A CG  1 
ATOM   707  C  CD1 . LEU   A 1 89 ? 9.120  23.243 -8.168  1.00 25.85  ? 89  LEU   A CD1 1 
ATOM   708  C  CD2 . LEU   A 1 89 ? 6.601  23.722 -7.921  1.00 22.70  ? 89  LEU   A CD2 1 
ATOM   709  N  N   . LEU   A 1 90 ? 6.409  19.058 -5.110  1.00 18.56  ? 90  LEU   A N   1 
ATOM   710  C  CA  . LEU   A 1 90 ? 6.111  17.619 -5.022  1.00 18.44  ? 90  LEU   A CA  1 
ATOM   711  C  C   . LEU   A 1 90 ? 4.603  17.372 -5.149  1.00 23.98  ? 90  LEU   A C   1 
ATOM   712  O  O   . LEU   A 1 90 ? 4.176  16.396 -5.775  1.00 24.16  ? 90  LEU   A O   1 
ATOM   713  C  CB  . LEU   A 1 90 ? 6.667  17.051 -3.702  1.00 19.92  ? 90  LEU   A CB  1 
ATOM   714  C  CG  . LEU   A 1 90 ? 8.198  17.035 -3.567  1.00 20.11  ? 90  LEU   A CG  1 
ATOM   715  C  CD1 . LEU   A 1 90 ? 8.588  16.644 -2.132  1.00 20.48  ? 90  LEU   A CD1 1 
ATOM   716  C  CD2 . LEU   A 1 90 ? 8.832  16.078 -4.613  1.00 25.67  ? 90  LEU   A CD2 1 
ATOM   717  N  N   . THR   A 1 91 ? 3.774  18.267 -4.588  1.00 19.85  ? 91  THR   A N   1 
ATOM   718  C  CA  . THR   A 1 91 ? 2.329  18.070 -4.727  1.00 23.41  ? 91  THR   A CA  1 
ATOM   719  C  C   . THR   A 1 91 ? 1.880  18.228 -6.176  1.00 25.81  ? 91  THR   A C   1 
ATOM   720  O  O   . THR   A 1 91 ? 0.947  17.539 -6.609  1.00 25.63  ? 91  THR   A O   1 
ATOM   721  C  CB  . THR   A 1 91 ? 1.547  19.040 -3.832  1.00 23.17  ? 91  THR   A CB  1 
ATOM   722  O  OG1 . THR   A 1 91 ? 1.908  20.390 -4.139  1.00 26.96  ? 91  THR   A OG1 1 
ATOM   723  C  CG2 . THR   A 1 91 ? 1.863  18.772 -2.362  1.00 23.37  ? 91  THR   A CG2 1 
ATOM   724  N  N   . GLN   A 1 92 ? 2.545  19.095 -6.956  1.00 21.36  ? 92  GLN   A N   1 
ATOM   725  C  CA  . GLN   A 1 92 ? 2.134  19.275 -8.352  1.00 23.74  ? 92  GLN   A CA  1 
ATOM   726  C  C   . GLN   A 1 92 ? 2.420  18.042 -9.189  1.00 27.05  ? 92  GLN   A C   1 
ATOM   727  O  O   . GLN   A 1 92 ? 1.702  17.769 -10.154 1.00 29.71  ? 92  GLN   A O   1 
ATOM   728  C  CB  . GLN   A 1 92 ? 2.841  20.472 -9.000  1.00 23.14  ? 92  GLN   A CB  1 
ATOM   729  C  CG  . GLN   A 1 92 ? 2.386  21.831 -8.444  1.00 25.29  ? 92  GLN   A CG  1 
ATOM   730  C  CD  . GLN   A 1 92 ? 2.835  22.970 -9.346  1.00 22.35  ? 92  GLN   A CD  1 
ATOM   731  O  OE1 . GLN   A 1 92 ? 3.161  22.758 -10.528 1.00 22.79  ? 92  GLN   A OE1 1 
ATOM   732  N  NE2 . GLN   A 1 92 ? 2.805  24.180 -8.819  1.00 24.18  ? 92  GLN   A NE2 1 
ATOM   733  N  N   . ILE   A 1 93 ? 3.464  17.283 -8.864  1.00 24.54  ? 93  ILE   A N   1 
ATOM   734  C  CA  . ILE   A 1 93 ? 3.716  16.067 -9.626  1.00 25.48  ? 93  ILE   A CA  1 
ATOM   735  C  C   . ILE   A 1 93 ? 3.064  14.853 -8.972  1.00 26.88  ? 93  ILE   A C   1 
ATOM   736  O  O   . ILE   A 1 93 ? 3.284  13.724 -9.418  1.00 32.81  ? 93  ILE   A O   1 
ATOM   737  C  CB  . ILE   A 1 93 ? 5.219  15.830 -9.865  1.00 26.58  ? 93  ILE   A CB  1 
ATOM   738  C  CG1 . ILE   A 1 93 ? 5.937  15.567 -8.549  1.00 29.14  ? 93  ILE   A CG1 1 
ATOM   739  C  CG2 . ILE   A 1 93 ? 5.825  17.048 -10.576 1.00 28.30  ? 93  ILE   A CG2 1 
ATOM   740  C  CD1 . ILE   A 1 93 ? 7.413  15.145 -8.728  1.00 29.95  ? 93  ILE   A CD1 1 
ATOM   741  N  N   . GLY   A 1 94 ? 2.253  15.055 -7.937  1.00 26.21  ? 94  GLY   A N   1 
ATOM   742  C  CA  . GLY   A 1 94 ? 1.500  13.952 -7.365  1.00 28.73  ? 94  GLY   A CA  1 
ATOM   743  C  C   . GLY   A 1 94 ? 2.285  12.995 -6.488  1.00 34.85  ? 94  GLY   A C   1 
ATOM   744  O  O   . GLY   A 1 94 ? 1.911  11.823 -6.369  1.00 30.62  ? 94  GLY   A O   1 
ATOM   745  N  N   . ALA   A 1 95 ? 3.358  13.457 -5.853  1.00 22.95  ? 95  ALA   A N   1 
ATOM   746  C  CA  . ALA   A 1 95 ? 4.188  12.573 -5.038  1.00 23.26  ? 95  ALA   A CA  1 
ATOM   747  C  C   . ALA   A 1 95 ? 3.554  12.307 -3.691  1.00 25.24  ? 95  ALA   A C   1 
ATOM   748  O  O   . ALA   A 1 95 ? 3.000  13.215 -3.056  1.00 28.23  ? 95  ALA   A O   1 
ATOM   749  C  CB  . ALA   A 1 95 ? 5.578  13.182 -4.830  1.00 25.13  ? 95  ALA   A CB  1 
ATOM   750  N  N   . THR   A 1 96 ? 3.671  11.055 -3.230  1.00 24.08  ? 96  THR   A N   1 
ATOM   751  C  CA  . THR   A 1 96 ? 3.264  10.685 -1.884  1.00 24.62  ? 96  THR   A CA  1 
ATOM   752  C  C   . THR   A 1 96 ? 4.375  9.876  -1.229  1.00 24.03  ? 96  THR   A C   1 
ATOM   753  O  O   . THR   A 1 96 ? 5.245  9.312  -1.901  1.00 26.21  ? 96  THR   A O   1 
ATOM   754  C  CB  . THR   A 1 96 ? 1.960  9.855  -1.879  1.00 29.51  ? 96  THR   A CB  1 
ATOM   755  O  OG1 . THR   A 1 96 ? 2.169  8.676  -2.652  1.00 29.08  ? 96  THR   A OG1 1 
ATOM   756  C  CG2 . THR   A 1 96 ? 0.812  10.667 -2.506  1.00 28.35  ? 96  THR   A CG2 1 
ATOM   757  N  N   A LEU   A 1 97 ? 4.339  9.832  0.102   0.50 23.86  ? 97  LEU   A N   1 
ATOM   758  N  N   B LEU   A 1 97 ? 4.311  9.817  0.094   0.50 23.87  ? 97  LEU   A N   1 
ATOM   759  C  CA  A LEU   A 1 97 ? 5.213  8.978  0.900   0.50 26.64  ? 97  LEU   A CA  1 
ATOM   760  C  CA  B LEU   A 1 97 ? 5.184  8.983  0.906   0.50 26.70  ? 97  LEU   A CA  1 
ATOM   761  C  C   A LEU   A 1 97 ? 4.395  7.775  1.353   0.50 27.04  ? 97  LEU   A C   1 
ATOM   762  C  C   B LEU   A 1 97 ? 4.367  7.767  1.319   0.50 27.06  ? 97  LEU   A C   1 
ATOM   763  O  O   A LEU   A 1 97 ? 3.289  7.946  1.877   0.50 31.32  ? 97  LEU   A O   1 
ATOM   764  O  O   B LEU   A 1 97 ? 3.218  7.916  1.746   0.50 31.32  ? 97  LEU   A O   1 
ATOM   765  C  CB  A LEU   A 1 97 ? 5.737  9.747  2.117   0.50 27.30  ? 97  LEU   A CB  1 
ATOM   766  C  CB  B LEU   A 1 97 ? 5.642  9.789  2.123   0.50 27.37  ? 97  LEU   A CB  1 
ATOM   767  C  CG  A LEU   A 1 97 ? 7.007  9.342  2.849   0.50 34.45  ? 97  LEU   A CG  1 
ATOM   768  C  CG  B LEU   A 1 97 ? 7.081  10.248 2.273   0.50 26.67  ? 97  LEU   A CG  1 
ATOM   769  C  CD1 A LEU   A 1 97 ? 8.181  9.254  1.870   0.50 30.22  ? 97  LEU   A CD1 1 
ATOM   770  C  CD1 B LEU   A 1 97 ? 7.183  10.984 3.606   0.50 33.08  ? 97  LEU   A CD1 1 
ATOM   771  C  CD2 A LEU   A 1 97 ? 7.270  10.340 3.968   0.50 36.36  ? 97  LEU   A CD2 1 
ATOM   772  C  CD2 B LEU   A 1 97 ? 8.058  9.074  2.220   0.50 31.69  ? 97  LEU   A CD2 1 
ATOM   773  N  N   . ASN   A 1 98 ? 4.930  6.570  1.157   1.00 22.97  ? 98  ASN   A N   1 
ATOM   774  C  CA  . ASN   A 1 98 ? 4.207  5.329  1.441   1.00 23.07  ? 98  ASN   A CA  1 
ATOM   775  C  C   . ASN   A 1 98 ? 5.045  4.393  2.302   1.00 27.05  ? 98  ASN   A C   1 
ATOM   776  O  O   . ASN   A 1 98 ? 6.242  4.220  2.064   1.00 29.92  ? 98  ASN   A O   1 
ATOM   777  C  CB  . ASN   A 1 98 ? 3.855  4.612  0.140   1.00 25.42  ? 98  ASN   A CB  1 
ATOM   778  C  CG  . ASN   A 1 98 ? 2.927  5.439  -0.722  1.00 37.86  ? 98  ASN   A CG  1 
ATOM   779  O  OD1 . ASN   A 1 98 ? 1.718  5.237  -0.718  1.00 49.55  ? 98  ASN   A OD1 1 
ATOM   780  N  ND2 . ASN   A 1 98 ? 3.486  6.408  -1.422  1.00 36.15  ? 98  ASN   A ND2 1 
ATOM   781  N  N   . PHE   A 1 99 ? 4.407  3.777  3.281   1.00 28.38  ? 99  PHE   A N   1 
ATOM   782  C  CA  . PHE   A 1 99 ? 5.052  2.675  3.999   1.00 29.06  ? 99  PHE   A CA  1 
ATOM   783  C  C   . PHE   A 1 99 ? 4.001  1.775  4.626   1.00 50.83  ? 99  PHE   A C   1 
ATOM   784  O  O   . PHE   A 1 99 ? 4.309  0.720  5.166   1.00 41.26  ? 99  PHE   A O   1 
ATOM   785  C  CB  . PHE   A 1 99 ? 6.012  3.197  5.070   1.00 31.67  ? 99  PHE   A CB  1 
ATOM   786  C  CG  . PHE   A 1 99 ? 5.370  4.101  6.074   1.00 33.47  ? 99  PHE   A CG  1 
ATOM   787  C  CD1 . PHE   A 1 99 ? 5.264  5.448  5.825   1.00 34.14  ? 99  PHE   A CD1 1 
ATOM   788  C  CD2 . PHE   A 1 99 ? 4.886  3.606  7.273   1.00 41.68  ? 99  PHE   A CD2 1 
ATOM   789  C  CE1 . PHE   A 1 99 ? 4.675  6.294  6.749   1.00 37.45  ? 99  PHE   A CE1 1 
ATOM   790  C  CE2 . PHE   A 1 99 ? 4.295  4.453  8.208   1.00 42.70  ? 99  PHE   A CE2 1 
ATOM   791  C  CZ  . PHE   A 1 99 ? 4.190  5.778  7.953   1.00 40.36  ? 99  PHE   A CZ  1 
ATOM   792  O  OXT . PHE   A 1 99 ? 2.821  2.103  4.605   1.00 39.18  ? 99  PHE   A OXT 1 
ATOM   793  N  N   . PRO   B 1 1  ? 0.460  3.277  5.487   1.00 44.17  ? 101 PRO   B N   1 
ATOM   794  C  CA  . PRO   B 1 1  ? -0.291 4.457  5.062   1.00 42.63  ? 101 PRO   B CA  1 
ATOM   795  C  C   . PRO   B 1 1  ? 0.302  5.126  3.837   1.00 41.90  ? 101 PRO   B C   1 
ATOM   796  O  O   . PRO   B 1 1  ? 1.456  4.925  3.484   1.00 37.92  ? 101 PRO   B O   1 
ATOM   797  C  CB  . PRO   B 1 1  ? -0.210 5.404  6.267   1.00 43.30  ? 101 PRO   B CB  1 
ATOM   798  C  CG  . PRO   B 1 1  ? 0.755  4.806  7.201   1.00 43.85  ? 101 PRO   B CG  1 
ATOM   799  C  CD  . PRO   B 1 1  ? 0.915  3.368  6.883   1.00 44.51  ? 101 PRO   B CD  1 
ATOM   800  N  N   . GLN   B 1 2  ? -0.527 5.917  3.178   1.00 39.29  ? 102 GLN   B N   1 
ATOM   801  C  CA  . GLN   B 1 2  ? -0.103 6.777  2.093   1.00 34.30  ? 102 GLN   B CA  1 
ATOM   802  C  C   . GLN   B 1 2  ? -0.222 8.207  2.596   1.00 45.13  ? 102 GLN   B C   1 
ATOM   803  O  O   . GLN   B 1 2  ? -1.286 8.601  3.087   1.00 40.85  ? 102 GLN   B O   1 
ATOM   804  C  CB  . GLN   B 1 2  ? -0.985 6.576  0.871   1.00 41.25  ? 102 GLN   B CB  1 
ATOM   805  C  CG  . GLN   B 1 2  ? -0.834 7.683  -0.120  1.00 42.69  ? 102 GLN   B CG  1 
ATOM   806  C  CD  . GLN   B 1 2  ? -1.292 7.274  -1.486  1.00 59.01  ? 102 GLN   B CD  1 
ATOM   807  O  OE1 . GLN   B 1 2  ? -2.374 7.667  -1.920  1.00 60.51  ? 102 GLN   B OE1 1 
ATOM   808  N  NE2 . GLN   B 1 2  ? -0.497 6.445  -2.162  1.00 58.38  ? 102 GLN   B NE2 1 
ATOM   809  N  N   . ILE   B 1 3  ? 0.858  8.978  2.502   1.00 31.22  ? 103 ILE   B N   1 
ATOM   810  C  CA  . ILE   B 1 3  ? 0.886  10.312 3.092   1.00 32.50  ? 103 ILE   B CA  1 
ATOM   811  C  C   . ILE   B 1 3  ? 1.016  11.322 1.964   1.00 33.29  ? 103 ILE   B C   1 
ATOM   812  O  O   . ILE   B 1 3  ? 1.982  11.281 1.191   1.00 29.40  ? 103 ILE   B O   1 
ATOM   813  C  CB  . ILE   B 1 3  ? 2.017  10.454 4.121   1.00 39.62  ? 103 ILE   B CB  1 
ATOM   814  C  CG1 . ILE   B 1 3  ? 1.647  9.685  5.392   1.00 45.86  ? 103 ILE   B CG1 1 
ATOM   815  C  CG2 . ILE   B 1 3  ? 2.233  11.919 4.492   1.00 38.21  ? 103 ILE   B CG2 1 
ATOM   816  C  CD1 . ILE   B 1 3  ? 2.822  9.229  6.171   1.00 48.17  ? 103 ILE   B CD1 1 
ATOM   817  N  N   . THR   B 1 4  ? 0.006  12.181 1.825   1.00 30.93  ? 104 THR   B N   1 
ATOM   818  C  CA  . THR   B 1 4  ? 0.094  13.255 0.852   1.00 29.76  ? 104 THR   B CA  1 
ATOM   819  C  C   . THR   B 1 4  ? 0.912  14.389 1.447   1.00 27.04  ? 104 THR   B C   1 
ATOM   820  O  O   . THR   B 1 4  ? 1.162  14.452 2.659   1.00 28.08  ? 104 THR   B O   1 
ATOM   821  C  CB  . THR   B 1 4  ? -1.295 13.757 0.431   1.00 37.85  ? 104 THR   B CB  1 
ATOM   822  O  OG1 . THR   B 1 4  ? -1.999 14.235 1.585   1.00 37.04  ? 104 THR   B OG1 1 
ATOM   823  C  CG2 . THR   B 1 4  ? -2.100 12.645 -0.245  1.00 38.15  ? 104 THR   B CG2 1 
ATOM   824  N  N   . LEU   B 1 5  ? 1.336  15.302 0.582   1.00 24.49  ? 105 LEU   B N   1 
ATOM   825  C  CA  . LEU   B 1 5  ? 2.305  16.303 1.003   1.00 24.58  ? 105 LEU   B CA  1 
ATOM   826  C  C   . LEU   B 1 5  ? 1.716  17.706 0.987   1.00 28.34  ? 105 LEU   B C   1 
ATOM   827  O  O   . LEU   B 1 5  ? 2.464  18.689 0.926   1.00 24.69  ? 105 LEU   B O   1 
ATOM   828  C  CB  . LEU   B 1 5  ? 3.549  16.206 0.102   1.00 23.27  ? 105 LEU   B CB  1 
ATOM   829  C  CG  . LEU   B 1 5  ? 4.259  14.854 0.277   1.00 25.63  ? 105 LEU   B CG  1 
ATOM   830  C  CD1 . LEU   B 1 5  ? 5.337  14.706 -0.793  1.00 25.29  ? 105 LEU   B CD1 1 
ATOM   831  C  CD2 . LEU   B 1 5  ? 4.849  14.772 1.690   1.00 31.46  ? 105 LEU   B CD2 1 
ATOM   832  N  N   . TRP   B 1 6  ? 0.382  17.825 1.060   1.00 25.75  ? 106 TRP   B N   1 
ATOM   833  C  CA  . TRP   B 1 6  ? -0.224 19.151 1.221   1.00 27.07  ? 106 TRP   B CA  1 
ATOM   834  C  C   . TRP   B 1 6  ? 0.264  19.851 2.483   1.00 27.52  ? 106 TRP   B C   1 
ATOM   835  O  O   . TRP   B 1 6  ? 0.399  21.082 2.510   1.00 27.99  ? 106 TRP   B O   1 
ATOM   836  C  CB  . TRP   B 1 6  ? -1.750 19.044 1.263   1.00 28.61  ? 106 TRP   B CB  1 
ATOM   837  C  CG  . TRP   B 1 6  ? -2.376 18.432 0.068   1.00 28.61  ? 106 TRP   B CG  1 
ATOM   838  C  CD1 . TRP   B 1 6  ? -3.040 17.235 0.005   1.00 32.36  ? 106 TRP   B CD1 1 
ATOM   839  C  CD2 . TRP   B 1 6  ? -2.443 19.004 -1.249  1.00 25.71  ? 106 TRP   B CD2 1 
ATOM   840  N  NE1 . TRP   B 1 6  ? -3.515 17.033 -1.269  1.00 36.65  ? 106 TRP   B NE1 1 
ATOM   841  C  CE2 . TRP   B 1 6  ? -3.160 18.101 -2.057  1.00 33.33  ? 106 TRP   B CE2 1 
ATOM   842  C  CE3 . TRP   B 1 6  ? -1.977 20.196 -1.813  1.00 32.33  ? 106 TRP   B CE3 1 
ATOM   843  C  CZ2 . TRP   B 1 6  ? -3.415 18.351 -3.415  1.00 42.82  ? 106 TRP   B CZ2 1 
ATOM   844  C  CZ3 . TRP   B 1 6  ? -2.230 20.449 -3.161  1.00 31.58  ? 106 TRP   B CZ3 1 
ATOM   845  C  CH2 . TRP   B 1 6  ? -2.945 19.530 -3.944  1.00 33.06  ? 106 TRP   B CH2 1 
ATOM   846  N  N   . LYS   B 1 7  ? 0.497  19.087 3.550   1.00 26.84  ? 107 LYS   B N   1 
ATOM   847  C  CA  . LYS   B 1 7  ? 1.009  19.588 4.811   1.00 24.37  ? 107 LYS   B CA  1 
ATOM   848  C  C   . LYS   B 1 7  ? 2.305  18.848 5.143   1.00 22.61  ? 107 LYS   B C   1 
ATOM   849  O  O   . LYS   B 1 7  ? 2.623  17.831 4.522   1.00 24.60  ? 107 LYS   B O   1 
ATOM   850  C  CB  . LYS   B 1 7  ? -0.042 19.389 5.920   1.00 31.73  ? 107 LYS   B CB  1 
ATOM   851  C  CG  . LYS   B 1 7  ? -1.224 20.354 5.753   1.00 44.70  ? 107 LYS   B CG  1 
ATOM   852  C  CD  . LYS   B 1 7  ? -2.068 20.539 7.013   1.00 87.92  ? 107 LYS   B CD  1 
ATOM   853  C  CE  . LYS   B 1 7  ? -3.365 21.295 6.695   1.00 88.01  ? 107 LYS   B CE  1 
ATOM   854  N  NZ  . LYS   B 1 7  ? -4.083 21.775 7.921   1.00 76.83  ? 107 LYS   B NZ  1 
ATOM   855  N  N   . ARG   B 1 8  ? 3.058  19.387 6.108   1.00 25.45  ? 108 ARG   B N   1 
ATOM   856  C  CA  . ARG   B 1 8  ? 4.284  18.729 6.552   1.00 24.68  ? 108 ARG   B CA  1 
ATOM   857  C  C   . ARG   B 1 8  ? 3.973  17.304 7.002   1.00 27.20  ? 108 ARG   B C   1 
ATOM   858  O  O   . ARG   B 1 8  ? 3.013  17.085 7.756   1.00 26.85  ? 108 ARG   B O   1 
ATOM   859  C  CB  . ARG   B 1 8  ? 4.891  19.477 7.724   1.00 21.05  ? 108 ARG   B CB  1 
ATOM   860  C  CG  . ARG   B 1 8  ? 5.557  20.793 7.300   1.00 24.65  ? 108 ARG   B CG  1 
ATOM   861  C  CD  . ARG   B 1 8  ? 6.240  21.481 8.474   1.00 29.30  ? 108 ARG   B CD  1 
ATOM   862  N  NE  . ARG   B 1 8  ? 7.004  22.646 8.035   1.00 34.89  ? 108 ARG   B NE  1 
ATOM   863  C  CZ  . ARG   B 1 8  ? 7.986  23.207 8.732   1.00 61.19  ? 108 ARG   B CZ  1 
ATOM   864  N  NH1 . ARG   B 1 8  ? 8.341  22.749 9.926   1.00 49.17  ? 108 ARG   B NH1 1 
ATOM   865  N  NH2 . ARG   B 1 8  ? 8.617  24.265 8.227   1.00 43.42  ? 108 ARG   B NH2 1 
ATOM   866  N  N   . PRO   B 1 9  ? 4.774  16.327 6.610   1.00 23.04  ? 109 PRO   B N   1 
ATOM   867  C  CA  . PRO   B 1 9  ? 4.508  14.924 6.975   1.00 21.54  ? 109 PRO   B CA  1 
ATOM   868  C  C   . PRO   B 1 9  ? 5.039  14.622 8.372   1.00 25.60  ? 109 PRO   B C   1 
ATOM   869  O  O   . PRO   B 1 9  ? 6.100  14.042 8.575   1.00 23.98  ? 109 PRO   B O   1 
ATOM   870  C  CB  . PRO   B 1 9  ? 5.265  14.142 5.896   1.00 23.52  ? 109 PRO   B CB  1 
ATOM   871  C  CG  . PRO   B 1 9  ? 6.405  15.050 5.525   1.00 23.22  ? 109 PRO   B CG  1 
ATOM   872  C  CD  . PRO   B 1 9  ? 5.876  16.465 5.630   1.00 24.97  ? 109 PRO   B CD  1 
ATOM   873  N  N   . LEU   B 1 10 ? 4.263  15.022 9.385   1.00 26.63  ? 110 LEU   B N   1 
ATOM   874  C  CA  . LEU   B 1 10 ? 4.642  14.844 10.779  1.00 24.74  ? 110 LEU   B CA  1 
ATOM   875  C  C   . LEU   B 1 10 ? 4.008  13.568 11.315  1.00 27.28  ? 110 LEU   B C   1 
ATOM   876  O  O   . LEU   B 1 10 ? 2.856  13.251 10.991  1.00 31.09  ? 110 LEU   B O   1 
ATOM   877  C  CB  . LEU   B 1 10 ? 4.188  16.029 11.629  1.00 27.07  ? 110 LEU   B CB  1 
ATOM   878  C  CG  . LEU   B 1 10 ? 4.890  17.352 11.299  1.00 38.28  ? 110 LEU   B CG  1 
ATOM   879  C  CD1 . LEU   B 1 10 ? 4.037  18.550 11.717  1.00 44.90  ? 110 LEU   B CD1 1 
ATOM   880  C  CD2 . LEU   B 1 10 ? 6.278  17.423 11.864  1.00 38.94  ? 110 LEU   B CD2 1 
ATOM   881  N  N   . VAL   B 1 11 ? 4.758  12.825 12.119  1.00 26.44  ? 111 VAL   B N   1 
ATOM   882  C  CA  . VAL   B 1 11 ? 4.246  11.610 12.744  1.00 25.65  ? 111 VAL   B CA  1 
ATOM   883  C  C   . VAL   B 1 11 ? 4.721  11.565 14.191  1.00 30.12  ? 111 VAL   B C   1 
ATOM   884  O  O   . VAL   B 1 11 ? 5.598  12.324 14.615  1.00 26.25  ? 111 VAL   B O   1 
ATOM   885  C  CB  . VAL   B 1 11 ? 4.682  10.322 12.012  1.00 31.78  ? 111 VAL   B CB  1 
ATOM   886  C  CG1 . VAL   B 1 11 ? 4.081  10.241 10.590  1.00 35.39  ? 111 VAL   B CG1 1 
ATOM   887  C  CG2 . VAL   B 1 11 ? 6.207  10.161 12.042  1.00 27.87  ? 111 VAL   B CG2 1 
ATOM   888  N  N   . THR   B 1 12 ? 4.116  10.659 14.963  1.00 33.70  ? 112 THR   B N   1 
ATOM   889  C  CA  . THR   B 1 12 ? 4.502  10.493 16.358  1.00 34.49  ? 112 THR   B CA  1 
ATOM   890  C  C   . THR   B 1 12 ? 5.572  9.420  16.441  1.00 28.66  ? 112 THR   B C   1 
ATOM   891  O  O   . THR   B 1 12 ? 5.456  8.367  15.803  1.00 33.80  ? 112 THR   B O   1 
ATOM   892  C  CB  . THR   B 1 12 ? 3.298  10.120 17.231  1.00 40.29  ? 112 THR   B CB  1 
ATOM   893  O  OG1 . THR   B 1 12 ? 2.586  9.039  16.624  1.00 66.41  ? 112 THR   B OG1 1 
ATOM   894  C  CG2 . THR   B 1 12 ? 2.378  11.307 17.347  1.00 32.40  ? 112 THR   B CG2 1 
ATOM   895  N  N   . ILE   B 1 13 ? 6.628  9.712  17.190  1.00 24.91  ? 113 ILE   B N   1 
ATOM   896  C  CA  . ILE   B 1 13 ? 7.705  8.764  17.410  1.00 25.76  ? 113 ILE   B CA  1 
ATOM   897  C  C   . ILE   B 1 13 ? 7.855  8.551  18.911  1.00 27.71  ? 113 ILE   B C   1 
ATOM   898  O  O   . ILE   B 1 13 ? 7.516  9.414  19.728  1.00 32.95  ? 113 ILE   B O   1 
ATOM   899  C  CB  . ILE   B 1 13 ? 9.055  9.219  16.795  1.00 35.68  ? 113 ILE   B CB  1 
ATOM   900  C  CG1 . ILE   B 1 13 ? 9.587  10.466 17.510  1.00 28.66  ? 113 ILE   B CG1 1 
ATOM   901  C  CG2 . ILE   B 1 13 ? 8.887  9.473  15.315  1.00 30.43  ? 113 ILE   B CG2 1 
ATOM   902  C  CD1 . ILE   B 1 13 ? 11.061 10.808 17.238  1.00 32.35  ? 113 ILE   B CD1 1 
ATOM   903  N  N   . LYS   B 1 14 ? 8.378  7.388  19.265  1.00 27.87  ? 114 LYS   B N   1 
ATOM   904  C  CA  . LYS   B 1 14 ? 8.760  7.104  20.639  1.00 31.21  ? 114 LYS   B CA  1 
ATOM   905  C  C   . LYS   B 1 14 ? 10.257 6.858  20.681  1.00 24.47  ? 114 LYS   B C   1 
ATOM   906  O  O   . LYS   B 1 14 ? 10.771 5.976  19.977  1.00 31.82  ? 114 LYS   B O   1 
ATOM   907  C  CB  . LYS   B 1 14 ? 7.980  5.905  21.186  1.00 31.03  ? 114 LYS   B CB  1 
ATOM   908  C  CG  . LYS   B 1 14 ? 8.318  5.623  22.653  1.00 49.87  ? 114 LYS   B CG  1 
ATOM   909  C  CD  . LYS   B 1 14 ? 7.917  4.218  23.103  1.00 78.58  ? 114 LYS   B CD  1 
ATOM   910  C  CE  . LYS   B 1 14 ? 7.909  4.117  24.636  1.00 87.05  ? 114 LYS   B CE  1 
ATOM   911  N  NZ  . LYS   B 1 14 ? 6.852  3.206  25.179  1.00 87.07  ? 114 LYS   B NZ  1 
ATOM   912  N  N   . ILE   B 1 15 ? 10.960 7.629  21.505  1.00 26.81  ? 115 ILE   B N   1 
ATOM   913  C  CA  . ILE   B 1 15 ? 12.403 7.497  21.635  1.00 28.03  ? 115 ILE   B CA  1 
ATOM   914  C  C   . ILE   B 1 15 ? 12.783 7.749  23.085  1.00 39.87  ? 115 ILE   B C   1 
ATOM   915  O  O   . ILE   B 1 15 ? 12.298 8.706  23.697  1.00 34.37  ? 115 ILE   B O   1 
ATOM   916  C  CB  . ILE   B 1 15 ? 13.159 8.465  20.701  1.00 30.04  ? 115 ILE   B CB  1 
ATOM   917  C  CG1 . ILE   B 1 15 ? 14.662 8.348  20.950  1.00 31.55  ? 115 ILE   B CG1 1 
ATOM   918  C  CG2 . ILE   B 1 15 ? 12.676 9.881  20.900  1.00 31.60  ? 115 ILE   B CG2 1 
ATOM   919  C  CD1 . ILE   B 1 15 ? 15.500 9.106  19.919  1.00 39.49  ? 115 ILE   B CD1 1 
ATOM   920  N  N   . GLY   B 1 16 ? 13.638 6.888  23.638  1.00 35.97  ? 116 GLY   B N   1 
ATOM   921  C  CA  . GLY   B 1 16 ? 14.105 7.097  25.004  1.00 42.36  ? 116 GLY   B CA  1 
ATOM   922  C  C   . GLY   B 1 16 ? 12.990 7.212  26.024  1.00 40.49  ? 116 GLY   B C   1 
ATOM   923  O  O   . GLY   B 1 16 ? 13.116 7.968  26.991  1.00 42.70  ? 116 GLY   B O   1 
ATOM   924  N  N   . GLY   B 1 17 ? 11.884 6.503  25.810  1.00 40.44  ? 117 GLY   B N   1 
ATOM   925  C  CA  . GLY   B 1 17 ? 10.738 6.565  26.687  1.00 44.80  ? 117 GLY   B CA  1 
ATOM   926  C  C   . GLY   B 1 17 ? 9.868  7.795  26.558  1.00 51.37  ? 117 GLY   B C   1 
ATOM   927  O  O   . GLY   B 1 17 ? 8.946  7.957  27.358  1.00 45.82  ? 117 GLY   B O   1 
ATOM   928  N  N   . GLN   B 1 18 ? 10.115 8.672  25.587  1.00 43.14  ? 118 GLN   B N   1 
ATOM   929  C  CA  . GLN   B 1 18 ? 9.335  9.896  25.443  1.00 35.29  ? 118 GLN   B CA  1 
ATOM   930  C  C   . GLN   B 1 18 ? 8.612  9.901  24.107  1.00 38.12  ? 118 GLN   B C   1 
ATOM   931  O  O   . GLN   B 1 18 ? 9.077  9.316  23.131  1.00 35.32  ? 118 GLN   B O   1 
ATOM   932  C  CB  . GLN   B 1 18 ? 10.226 11.143 25.556  1.00 37.06  ? 118 GLN   B CB  1 
ATOM   933  C  CG  . GLN   B 1 18 ? 11.264 11.060 26.660  1.00 41.34  ? 118 GLN   B CG  1 
ATOM   934  C  CD  . GLN   B 1 18 ? 11.990 12.375 26.882  1.00 46.71  ? 118 GLN   B CD  1 
ATOM   935  O  OE1 . GLN   B 1 18 ? 11.686 13.384 26.243  1.00 44.70  ? 118 GLN   B OE1 1 
ATOM   936  N  NE2 . GLN   B 1 18 ? 12.978 12.359 27.766  1.00 57.29  ? 118 GLN   B NE2 1 
ATOM   937  N  N   . LEU   B 1 19 ? 7.471  10.569 24.062  1.00 38.01  ? 119 LEU   B N   1 
ATOM   938  C  CA  . LEU   B 1 19 ? 6.726  10.737 22.821  1.00 37.81  ? 119 LEU   B CA  1 
ATOM   939  C  C   . LEU   B 1 19 ? 7.058  12.095 22.221  1.00 38.53  ? 119 LEU   B C   1 
ATOM   940  O  O   . LEU   B 1 19 ? 7.067  13.103 22.931  1.00 39.95  ? 119 LEU   B O   1 
ATOM   941  C  CB  . LEU   B 1 19 ? 5.223  10.612 23.063  1.00 45.03  ? 119 LEU   B CB  1 
ATOM   942  C  CG  . LEU   B 1 19 ? 4.609  9.363  22.441  1.00 50.20  ? 119 LEU   B CG  1 
ATOM   943  C  CD1 . LEU   B 1 19 ? 5.114  8.130  23.146  1.00 50.91  ? 119 LEU   B CD1 1 
ATOM   944  C  CD2 . LEU   B 1 19 ? 3.085  9.421  22.472  1.00 59.69  ? 119 LEU   B CD2 1 
ATOM   945  N  N   . LYS   B 1 20 ? 7.368  12.117 20.924  1.00 35.81  ? 120 LYS   B N   1 
ATOM   946  C  CA  . LYS   B 1 20 ? 7.709  13.357 20.234  1.00 29.98  ? 120 LYS   B CA  1 
ATOM   947  C  C   . LYS   B 1 20 ? 7.084  13.334 18.845  1.00 35.97  ? 120 LYS   B C   1 
ATOM   948  O  O   . LYS   B 1 20 ? 6.742  12.269 18.316  1.00 32.01  ? 120 LYS   B O   1 
ATOM   949  C  CB  . LYS   B 1 20 ? 9.228  13.566 20.112  1.00 35.50  ? 120 LYS   B CB  1 
ATOM   950  C  CG  . LYS   B 1 20 ? 10.013 13.437 21.414  1.00 39.13  ? 120 LYS   B CG  1 
ATOM   951  C  CD  . LYS   B 1 20 ? 11.295 14.241 21.343  1.00 48.21  ? 120 LYS   B CD  1 
ATOM   952  C  CE  . LYS   B 1 20 ? 12.011 14.291 22.691  1.00 45.82  ? 120 LYS   B CE  1 
ATOM   953  N  NZ  . LYS   B 1 20 ? 12.099 15.688 23.212  1.00 48.45  ? 120 LYS   B NZ  1 
ATOM   954  N  N   . GLU   B 1 21 ? 6.908  14.534 18.280  1.00 31.82  ? 121 GLU   B N   1 
ATOM   955  C  CA  . GLU   B 1 21 ? 6.477  14.702 16.894  1.00 26.31  ? 121 GLU   B CA  1 
ATOM   956  C  C   . GLU   B 1 21 ? 7.716  14.844 16.028  1.00 27.43  ? 121 GLU   B C   1 
ATOM   957  O  O   . GLU   B 1 21 ? 8.665  15.516 16.429  1.00 27.62  ? 121 GLU   B O   1 
ATOM   958  C  CB  . GLU   B 1 21 ? 5.617  15.949 16.726  1.00 34.39  ? 121 GLU   B CB  1 
ATOM   959  C  CG  . GLU   B 1 21 ? 4.303  15.920 17.457  1.00 62.27  ? 121 GLU   B CG  1 
ATOM   960  C  CD  . GLU   B 1 21 ? 3.161  16.377 16.583  1.00 87.96  ? 121 GLU   B CD  1 
ATOM   961  O  OE1 . GLU   B 1 21 ? 2.090  15.733 16.616  1.00 100.87 ? 121 GLU   B OE1 1 
ATOM   962  O  OE2 . GLU   B 1 21 ? 3.339  17.392 15.871  1.00 85.48  ? 121 GLU   B OE2 1 
ATOM   963  N  N   . ALA   B 1 22 ? 7.704  14.225 14.838  1.00 26.19  ? 122 ALA   B N   1 
ATOM   964  C  CA  . ALA   B 1 22 ? 8.873  14.344 13.970  1.00 23.26  ? 122 ALA   B CA  1 
ATOM   965  C  C   . ALA   B 1 22 ? 8.458  14.360 12.506  1.00 23.19  ? 122 ALA   B C   1 
ATOM   966  O  O   . ALA   B 1 22 ? 7.394  13.866 12.124  1.00 27.03  ? 122 ALA   B O   1 
ATOM   967  C  CB  . ALA   B 1 22 ? 9.877  13.205 14.184  1.00 21.99  ? 122 ALA   B CB  1 
ATOM   968  N  N   . LEU   B 1 23 ? 9.348  14.912 11.684  1.00 22.20  ? 123 LEU   B N   1 
ATOM   969  C  CA  . LEU   B 1 23 ? 9.105  15.105 10.266  1.00 19.97  ? 123 LEU   B CA  1 
ATOM   970  C  C   . LEU   B 1 23 ? 9.722  13.953 9.483   1.00 21.43  ? 123 LEU   B C   1 
ATOM   971  O  O   . LEU   B 1 23 ? 10.895 13.613 9.703   1.00 25.65  ? 123 LEU   B O   1 
ATOM   972  C  CB  . LEU   B 1 23 ? 9.723  16.453 9.871   1.00 22.98  ? 123 LEU   B CB  1 
ATOM   973  C  CG  . LEU   B 1 23 ? 9.561  17.076 8.510   1.00 32.84  ? 123 LEU   B CG  1 
ATOM   974  C  CD1 . LEU   B 1 23 ? 8.121  17.428 8.351   1.00 34.59  ? 123 LEU   B CD1 1 
ATOM   975  C  CD2 . LEU   B 1 23 ? 10.421 18.359 8.515   1.00 28.78  ? 123 LEU   B CD2 1 
ATOM   976  N  N   . LEU   B 1 24 ? 8.938  13.325 8.599   1.00 19.59  ? 124 LEU   B N   1 
ATOM   977  C  CA  . LEU   B 1 24 ? 9.475  12.268 7.736   1.00 19.71  ? 124 LEU   B CA  1 
ATOM   978  C  C   . LEU   B 1 24 ? 10.176 12.935 6.563   1.00 23.18  ? 124 LEU   B C   1 
ATOM   979  O  O   . LEU   B 1 24 ? 9.530  13.565 5.722   1.00 24.42  ? 124 LEU   B O   1 
ATOM   980  C  CB  . LEU   B 1 24 ? 8.395  11.325 7.212   1.00 22.20  ? 124 LEU   B CB  1 
ATOM   981  C  CG  . LEU   B 1 24 ? 7.534  10.607 8.244   1.00 26.72  ? 124 LEU   B CG  1 
ATOM   982  C  CD1 . LEU   B 1 24 ? 6.506  9.696  7.554   1.00 32.55  ? 124 LEU   B CD1 1 
ATOM   983  C  CD2 . LEU   B 1 24 ? 8.482  9.783  9.131   1.00 24.52  ? 124 LEU   B CD2 1 
ATOM   984  N  N   . ASP   B 1 25 ? 11.498 12.843 6.516   1.00 16.83  ? 125 ASP   B N   1 
ATOM   985  C  CA  . ASP   B 1 25 ? 12.255 13.791 5.689   1.00 16.08  ? 125 ASP   B CA  1 
ATOM   986  C  C   . ASP   B 1 25 ? 13.166 13.041 4.717   1.00 20.11  ? 125 ASP   B C   1 
ATOM   987  O  O   . ASP   B 1 25 ? 14.274 12.653 5.095   1.00 19.15  ? 125 ASP   B O   1 
ATOM   988  C  CB  . ASP   B 1 25 ? 13.089 14.684 6.594   1.00 18.34  ? 125 ASP   B CB  1 
ATOM   989  C  CG  . ASP   B 1 25 ? 13.763 15.820 5.863   1.00 24.39  ? 125 ASP   B CG  1 
ATOM   990  O  OD1 . ASP   B 1 25 ? 13.834 15.824 4.620   1.00 22.36  ? 125 ASP   B OD1 1 
ATOM   991  O  OD2 . ASP   B 1 25 ? 14.271 16.689 6.574   1.00 20.98  ? 125 ASP   B OD2 1 
ATOM   992  N  N   . THR   B 1 26 ? 12.745 12.932 3.452   1.00 16.91  ? 126 THR   B N   1 
ATOM   993  C  CA  . THR   B 1 26 ? 13.585 12.244 2.468   1.00 16.85  ? 126 THR   B CA  1 
ATOM   994  C  C   . THR   B 1 26 ? 14.846 13.025 2.116   1.00 20.80  ? 126 THR   B C   1 
ATOM   995  O  O   . THR   B 1 26 ? 15.756 12.441 1.524   1.00 18.17  ? 126 THR   B O   1 
ATOM   996  C  CB  . THR   B 1 26 ? 12.810 11.989 1.178   1.00 15.65  ? 126 THR   B CB  1 
ATOM   997  O  OG1 . THR   B 1 26 ? 12.348 13.258 0.654   1.00 18.91  ? 126 THR   B OG1 1 
ATOM   998  C  CG2 . THR   B 1 26 ? 11.631 11.070 1.455   1.00 20.50  ? 126 THR   B CG2 1 
ATOM   999  N  N   . GLY   B 1 27 ? 14.921 14.314 2.454   1.00 15.17  ? 127 GLY   B N   1 
ATOM   1000 C  CA  . GLY   B 1 27 ? 16.118 15.106 2.163   1.00 18.36  ? 127 GLY   B CA  1 
ATOM   1001 C  C   . GLY   B 1 27 ? 17.199 15.015 3.227   1.00 20.43  ? 127 GLY   B C   1 
ATOM   1002 O  O   . GLY   B 1 27 ? 18.274 15.564 3.044   1.00 21.63  ? 127 GLY   B O   1 
ATOM   1003 N  N   . ALA   B 1 28 ? 16.963 14.281 4.313   1.00 16.58  ? 128 ALA   B N   1 
ATOM   1004 C  CA  . ALA   B 1 28 ? 17.889 14.187 5.431   1.00 17.25  ? 128 ALA   B CA  1 
ATOM   1005 C  C   . ALA   B 1 28 ? 18.585 12.832 5.383   1.00 19.92  ? 128 ALA   B C   1 
ATOM   1006 O  O   . ALA   B 1 28 ? 17.906 11.800 5.423   1.00 20.73  ? 128 ALA   B O   1 
ATOM   1007 C  CB  . ALA   B 1 28 ? 17.124 14.332 6.754   1.00 20.27  ? 128 ALA   B CB  1 
ATOM   1008 N  N   . ASP   B 1 29 ? 19.927 12.829 5.314   1.00 18.28  ? 129 ASP   B N   1 
ATOM   1009 C  CA  . ASP   B 1 29 ? 20.629 11.529 5.280   1.00 18.35  ? 129 ASP   B CA  1 
ATOM   1010 C  C   . ASP   B 1 29 ? 20.456 10.795 6.607   1.00 24.05  ? 129 ASP   B C   1 
ATOM   1011 O  O   . ASP   B 1 29 ? 20.311 9.564  6.649   1.00 22.32  ? 129 ASP   B O   1 
ATOM   1012 C  CB  . ASP   B 1 29 ? 22.131 11.716 5.030   1.00 24.10  ? 129 ASP   B CB  1 
ATOM   1013 C  CG  . ASP   B 1 29 ? 22.471 12.344 3.680   1.00 32.79  ? 129 ASP   B CG  1 
ATOM   1014 O  OD1 . ASP   B 1 29 ? 21.728 12.153 2.692   1.00 24.07  ? 129 ASP   B OD1 1 
ATOM   1015 O  OD2 . ASP   B 1 29 ? 23.544 12.995 3.620   1.00 33.44  ? 129 ASP   B OD2 1 
ATOM   1016 N  N   . ASP   B 1 30 ? 20.498 11.545 7.693   1.00 19.78  ? 130 ASP   B N   1 
ATOM   1017 C  CA  . ASP   B 1 30 ? 20.527 11.038 9.057   1.00 20.60  ? 130 ASP   B CA  1 
ATOM   1018 C  C   . ASP   B 1 30 ? 19.347 11.609 9.833   1.00 21.75  ? 130 ASP   B C   1 
ATOM   1019 O  O   . ASP   B 1 30 ? 18.710 12.573 9.435   1.00 21.58  ? 130 ASP   B O   1 
ATOM   1020 C  CB  . ASP   B 1 30 ? 21.836 11.441 9.731   1.00 24.10  ? 130 ASP   B CB  1 
ATOM   1021 C  CG  . ASP   B 1 30 ? 23.017 10.670 9.182   1.00 32.76  ? 130 ASP   B CG  1 
ATOM   1022 O  OD1 . ASP   B 1 30 ? 22.897 9.425  9.111   1.00 48.36  ? 130 ASP   B OD1 1 
ATOM   1023 O  OD2 . ASP   B 1 30 ? 24.031 11.309 8.849   1.00 49.13  ? 130 ASP   B OD2 1 
ATOM   1024 N  N   . THR   B 1 31 ? 19.074 10.987 10.969  1.00 18.49  ? 131 THR   B N   1 
ATOM   1025 C  CA  . THR   B 1 31 ? 18.003 11.366 11.861  1.00 17.57  ? 131 THR   B CA  1 
ATOM   1026 C  C   . THR   B 1 31 ? 18.550 12.318 12.924  1.00 18.64  ? 131 THR   B C   1 
ATOM   1027 O  O   . THR   B 1 31 ? 19.637 12.087 13.466  1.00 21.97  ? 131 THR   B O   1 
ATOM   1028 C  CB  . THR   B 1 31 ? 17.456 10.083 12.489  1.00 19.89  ? 131 THR   B CB  1 
ATOM   1029 O  OG1 . THR   B 1 31 ? 16.780 9.358  11.450  1.00 23.28  ? 131 THR   B OG1 1 
ATOM   1030 C  CG2 . THR   B 1 31 ? 16.480 10.399 13.622  1.00 17.93  ? 131 THR   B CG2 1 
ATOM   1031 N  N   . VAL   B 1 32 ? 17.821 13.399 13.185  1.00 21.09  ? 132 VAL   B N   1 
ATOM   1032 C  CA  . VAL   B 1 32 ? 18.299 14.476 14.046  1.00 18.78  ? 132 VAL   B CA  1 
ATOM   1033 C  C   . VAL   B 1 32 ? 17.167 14.817 15.002  1.00 23.51  ? 132 VAL   B C   1 
ATOM   1034 O  O   . VAL   B 1 32 ? 16.090 15.228 14.560  1.00 20.93  ? 132 VAL   B O   1 
ATOM   1035 C  CB  . VAL   B 1 32 ? 18.713 15.745 13.271  1.00 21.25  ? 132 VAL   B CB  1 
ATOM   1036 C  CG1 . VAL   B 1 32 ? 19.403 16.700 14.245  1.00 22.47  ? 132 VAL   B CG1 1 
ATOM   1037 C  CG2 . VAL   B 1 32 ? 19.599 15.416 12.070  1.00 25.22  ? 132 VAL   B CG2 1 
ATOM   1038 N  N   . ILE   B 1 33 ? 17.434 14.706 16.304  1.00 19.93  ? 133 ILE   B N   1 
ATOM   1039 C  CA  . ILE   B 1 33 ? 16.433 14.886 17.349  1.00 21.60  ? 133 ILE   B CA  1 
ATOM   1040 C  C   . ILE   B 1 33 ? 16.862 16.033 18.264  1.00 22.76  ? 133 ILE   B C   1 
ATOM   1041 O  O   . ILE   B 1 33 ? 18.058 16.221 18.524  1.00 21.93  ? 133 ILE   B O   1 
ATOM   1042 C  CB  . ILE   B 1 33 ? 16.271 13.575 18.147  1.00 24.01  ? 133 ILE   B CB  1 
ATOM   1043 C  CG1 . ILE   B 1 33 ? 15.856 12.421 17.209  1.00 27.61  ? 133 ILE   B CG1 1 
ATOM   1044 C  CG2 . ILE   B 1 33 ? 15.296 13.761 19.322  1.00 28.38  ? 133 ILE   B CG2 1 
ATOM   1045 C  CD1 . ILE   B 1 33 ? 14.473 12.596 16.606  1.00 31.43  ? 133 ILE   B CD1 1 
ATOM   1046 N  N   . GLU   B 1 34 ? 15.880 16.801 18.740  1.00 22.93  ? 134 GLU   B N   1 
ATOM   1047 C  CA  . GLU   B 1 34 ? 16.175 17.912 19.634  1.00 23.14  ? 134 GLU   B CA  1 
ATOM   1048 C  C   . GLU   B 1 34 ? 16.837 17.414 20.932  1.00 28.91  ? 134 GLU   B C   1 
ATOM   1049 O  O   . GLU   B 1 34 ? 16.761 16.240 21.301  1.00 25.01  ? 134 GLU   B O   1 
ATOM   1050 C  CB  . GLU   B 1 34 ? 14.890 18.684 19.912  1.00 29.05  ? 134 GLU   B CB  1 
ATOM   1051 C  CG  . GLU   B 1 34 ? 13.938 17.940 20.809  1.00 35.35  ? 134 GLU   B CG  1 
ATOM   1052 C  CD  . GLU   B 1 34 ? 12.510 18.427 20.646  1.00 62.17  ? 134 GLU   B CD  1 
ATOM   1053 O  OE1 . GLU   B 1 34 ? 12.324 19.587 20.209  1.00 65.00  ? 134 GLU   B OE1 1 
ATOM   1054 O  OE2 . GLU   B 1 34 ? 11.576 17.636 20.920  1.00 44.37  ? 134 GLU   B OE2 1 
ATOM   1055 N  N   . GLU   B 1 35 ? 17.490 18.347 21.629  1.00 27.74  ? 135 GLU   B N   1 
ATOM   1056 C  CA  . GLU   B 1 35 ? 18.268 18.037 22.828  1.00 27.49  ? 135 GLU   B CA  1 
ATOM   1057 C  C   . GLU   B 1 35 ? 17.472 17.191 23.813  1.00 29.93  ? 135 GLU   B C   1 
ATOM   1058 O  O   . GLU   B 1 35 ? 16.368 17.571 24.219  1.00 30.71  ? 135 GLU   B O   1 
ATOM   1059 C  CB  . GLU   B 1 35 ? 18.680 19.350 23.495  1.00 36.93  ? 135 GLU   B CB  1 
ATOM   1060 C  CG  . GLU   B 1 35 ? 20.051 19.349 24.085  1.00 53.08  ? 135 GLU   B CG  1 
ATOM   1061 C  CD  . GLU   B 1 35 ? 21.090 19.546 23.027  1.00 55.10  ? 135 GLU   B CD  1 
ATOM   1062 O  OE1 . GLU   B 1 35 ? 21.132 20.651 22.443  1.00 63.88  ? 135 GLU   B OE1 1 
ATOM   1063 O  OE2 . GLU   B 1 35 ? 21.870 18.603 22.792  1.00 65.05  ? 135 GLU   B OE2 1 
ATOM   1064 N  N   . MET   B 1 36 ? 18.023 16.026 24.151  1.00 29.25  ? 136 MET   B N   1 
ATOM   1065 C  CA  . MET   B 1 36 ? 17.465 15.145 25.173  1.00 31.28  ? 136 MET   B CA  1 
ATOM   1066 C  C   . MET   B 1 36 ? 18.582 14.256 25.693  1.00 34.01  ? 136 MET   B C   1 
ATOM   1067 O  O   . MET   B 1 36 ? 19.654 14.155 25.098  1.00 32.04  ? 136 MET   B O   1 
ATOM   1068 C  CB  . MET   B 1 36 ? 16.350 14.246 24.663  1.00 31.15  ? 136 MET   B CB  1 
ATOM   1069 C  CG  . MET   B 1 36 ? 16.802 13.344 23.538  1.00 28.69  ? 136 MET   B CG  1 
ATOM   1070 S  SD  . MET   B 1 36 ? 15.450 12.321 22.913  1.00 34.89  ? 136 MET   B SD  1 
ATOM   1071 C  CE  . MET   B 1 36 ? 14.997 11.345 24.373  1.00 33.94  ? 136 MET   B CE  1 
ATOM   1072 N  N   . SER   B 1 37 ? 18.300 13.567 26.791  1.00 30.34  ? 137 SER   B N   1 
ATOM   1073 C  CA  . SER   B 1 37 ? 19.268 12.652 27.359  1.00 35.77  ? 137 SER   B CA  1 
ATOM   1074 C  C   . SER   B 1 37 ? 19.009 11.262 26.795  1.00 39.06  ? 137 SER   B C   1 
ATOM   1075 O  O   . SER   B 1 37 ? 17.862 10.812 26.748  1.00 34.66  ? 137 SER   B O   1 
ATOM   1076 C  CB  . SER   B 1 37 ? 19.171 12.647 28.884  1.00 43.61  ? 137 SER   B CB  1 
ATOM   1077 O  OG  . SER   B 1 37 ? 19.641 11.415 29.370  1.00 58.28  ? 137 SER   B OG  1 
ATOM   1078 N  N   . LEU   B 1 38 ? 20.065 10.619 26.309  1.00 37.14  ? 138 LEU   B N   1 
ATOM   1079 C  CA  . LEU   B 1 38 ? 20.015 9.243  25.849  1.00 38.47  ? 138 LEU   B CA  1 
ATOM   1080 C  C   . LEU   B 1 38 ? 21.145 8.476  26.514  1.00 35.29  ? 138 LEU   B C   1 
ATOM   1081 O  O   . LEU   B 1 38 ? 22.157 9.064  26.906  1.00 39.22  ? 138 LEU   B O   1 
ATOM   1082 C  CB  . LEU   B 1 38 ? 20.154 9.135  24.316  1.00 33.32  ? 138 LEU   B CB  1 
ATOM   1083 C  CG  . LEU   B 1 38 ? 18.908 9.495  23.505  1.00 32.60  ? 138 LEU   B CG  1 
ATOM   1084 C  CD1 . LEU   B 1 38 ? 19.242 9.615  22.009  1.00 37.24  ? 138 LEU   B CD1 1 
ATOM   1085 C  CD2 . LEU   B 1 38 ? 17.754 8.524  23.742  1.00 39.52  ? 138 LEU   B CD2 1 
ATOM   1086 N  N   . PRO   B 1 39 ? 21.004 7.163  26.654  1.00 51.80  ? 139 PRO   B N   1 
ATOM   1087 C  CA  . PRO   B 1 39 ? 22.078 6.387  27.259  1.00 46.14  ? 139 PRO   B CA  1 
ATOM   1088 C  C   . PRO   B 1 39 ? 23.128 5.969  26.244  1.00 42.71  ? 139 PRO   B C   1 
ATOM   1089 O  O   . PRO   B 1 39 ? 22.856 5.767  25.058  1.00 52.37  ? 139 PRO   B O   1 
ATOM   1090 C  CB  . PRO   B 1 39 ? 21.319 5.174  27.805  1.00 42.93  ? 139 PRO   B CB  1 
ATOM   1091 C  CG  . PRO   B 1 39 ? 20.339 4.879  26.694  1.00 51.74  ? 139 PRO   B CG  1 
ATOM   1092 C  CD  . PRO   B 1 39 ? 19.988 6.261  26.072  1.00 45.68  ? 139 PRO   B CD  1 
ATOM   1093 N  N   . GLY   B 1 40 ? 24.349 5.853  26.736  1.00 44.67  ? 140 GLY   B N   1 
ATOM   1094 C  CA  . GLY   B 1 40 ? 25.437 5.292  25.970  1.00 45.39  ? 140 GLY   B CA  1 
ATOM   1095 C  C   . GLY   B 1 40 ? 26.529 6.310  25.715  1.00 43.39  ? 140 GLY   B C   1 
ATOM   1096 O  O   . GLY   B 1 40 ? 26.460 7.469  26.132  1.00 51.44  ? 140 GLY   B O   1 
ATOM   1097 N  N   . ARG   B 1 41 ? 27.574 5.830  25.050  1.00 45.01  ? 141 ARG   B N   1 
ATOM   1098 C  CA  . ARG   B 1 41 ? 28.613 6.705  24.555  1.00 51.62  ? 141 ARG   B CA  1 
ATOM   1099 C  C   . ARG   B 1 41 ? 28.092 7.440  23.329  1.00 41.71  ? 141 ARG   B C   1 
ATOM   1100 O  O   . ARG   B 1 41 ? 27.177 6.984  22.638  1.00 36.96  ? 141 ARG   B O   1 
ATOM   1101 C  CB  . ARG   B 1 41 ? 29.877 5.924  24.170  1.00 62.69  ? 141 ARG   B CB  1 
ATOM   1102 C  CG  . ARG   B 1 41 ? 30.202 4.700  25.006  1.00 93.20  ? 141 ARG   B CG  1 
ATOM   1103 C  CD  . ARG   B 1 41 ? 31.711 4.498  25.129  1.00 105.35 ? 141 ARG   B CD  1 
ATOM   1104 N  NE  . ARG   B 1 41 ? 32.057 3.516  26.151  1.00 137.39 ? 141 ARG   B NE  1 
ATOM   1105 C  CZ  . ARG   B 1 41 ? 33.249 3.410  26.723  1.00 141.63 ? 141 ARG   B CZ  1 
ATOM   1106 N  NH1 . ARG   B 1 41 ? 34.240 4.230  26.412  1.00 132.76 ? 141 ARG   B NH1 1 
ATOM   1107 N  NH2 . ARG   B 1 41 ? 33.454 2.453  27.624  1.00 135.80 ? 141 ARG   B NH2 1 
ATOM   1108 N  N   . TRP   B 1 42 ? 28.694 8.589  23.063  1.00 39.24  ? 142 TRP   B N   1 
ATOM   1109 C  CA  . TRP   B 1 42 ? 28.394 9.352  21.866  1.00 37.23  ? 142 TRP   B CA  1 
ATOM   1110 C  C   . TRP   B 1 42 ? 29.692 9.954  21.361  1.00 39.43  ? 142 TRP   B C   1 
ATOM   1111 O  O   . TRP   B 1 42 ? 30.681 10.042 22.091  1.00 34.38  ? 142 TRP   B O   1 
ATOM   1112 C  CB  . TRP   B 1 42 ? 27.340 10.425 22.155  1.00 33.26  ? 142 TRP   B CB  1 
ATOM   1113 C  CG  . TRP   B 1 42 ? 27.727 11.326 23.284  1.00 35.70  ? 142 TRP   B CG  1 
ATOM   1114 C  CD1 . TRP   B 1 42 ? 27.450 11.140 24.605  1.00 44.23  ? 142 TRP   B CD1 1 
ATOM   1115 C  CD2 . TRP   B 1 42 ? 28.481 12.543 23.197  1.00 41.33  ? 142 TRP   B CD2 1 
ATOM   1116 N  NE1 . TRP   B 1 42 ? 27.967 12.174 25.348  1.00 42.53  ? 142 TRP   B NE1 1 
ATOM   1117 C  CE2 . TRP   B 1 42 ? 28.609 13.047 24.509  1.00 50.43  ? 142 TRP   B CE2 1 
ATOM   1118 C  CE3 . TRP   B 1 42 ? 29.049 13.262 22.135  1.00 43.30  ? 142 TRP   B CE3 1 
ATOM   1119 C  CZ2 . TRP   B 1 42 ? 29.286 14.232 24.793  1.00 51.00  ? 142 TRP   B CZ2 1 
ATOM   1120 C  CZ3 . TRP   B 1 42 ? 29.715 14.448 22.416  1.00 43.16  ? 142 TRP   B CZ3 1 
ATOM   1121 C  CH2 . TRP   B 1 42 ? 29.833 14.917 23.737  1.00 44.59  ? 142 TRP   B CH2 1 
ATOM   1122 N  N   . LYS   B 1 43 ? 29.702 10.324 20.087  1.00 31.08  ? 143 LYS   B N   1 
ATOM   1123 C  CA  . LYS   B 1 43 ? 30.848 11.056 19.570  1.00 31.70  ? 143 LYS   B CA  1 
ATOM   1124 C  C   . LYS   B 1 43 ? 30.350 12.342 18.934  1.00 31.34  ? 143 LYS   B C   1 
ATOM   1125 O  O   . LYS   B 1 43 ? 29.203 12.408 18.492  1.00 27.49  ? 143 LYS   B O   1 
ATOM   1126 C  CB  . LYS   B 1 43 ? 31.648 10.238 18.547  1.00 33.30  ? 143 LYS   B CB  1 
ATOM   1127 C  CG  . LYS   B 1 43 ? 30.882 9.189  17.813  1.00 52.48  ? 143 LYS   B CG  1 
ATOM   1128 C  CD  . LYS   B 1 43 ? 31.837 8.315  17.000  1.00 65.42  ? 143 LYS   B CD  1 
ATOM   1129 C  CE  . LYS   B 1 43 ? 31.120 7.116  16.389  1.00 75.92  ? 143 LYS   B CE  1 
ATOM   1130 N  NZ  . LYS   B 1 43 ? 31.740 6.688  15.105  1.00 79.97  ? 143 LYS   B NZ  1 
ATOM   1131 N  N   . PRO   B 1 44 ? 31.155 13.393 18.933  1.00 26.28  ? 144 PRO   B N   1 
ATOM   1132 C  CA  . PRO   B 1 44 ? 30.690 14.648 18.348  1.00 22.87  ? 144 PRO   B CA  1 
ATOM   1133 C  C   . PRO   B 1 44 ? 30.759 14.597 16.834  1.00 24.50  ? 144 PRO   B C   1 
ATOM   1134 O  O   . PRO   B 1 44 ? 31.561 13.879 16.243  1.00 25.90  ? 144 PRO   B O   1 
ATOM   1135 C  CB  . PRO   B 1 44 ? 31.660 15.685 18.920  1.00 31.26  ? 144 PRO   B CB  1 
ATOM   1136 C  CG  . PRO   B 1 44 ? 32.923 14.917 19.085  1.00 28.43  ? 144 PRO   B CG  1 
ATOM   1137 C  CD  . PRO   B 1 44 ? 32.503 13.533 19.517  1.00 32.50  ? 144 PRO   B CD  1 
ATOM   1138 N  N   . LYS   B 1 45 ? 29.893 15.385 16.214  1.00 24.91  ? 145 LYS   B N   1 
ATOM   1139 C  CA  . LYS   B 1 45 ? 29.787 15.434 14.764  1.00 24.09  ? 145 LYS   B CA  1 
ATOM   1140 C  C   . LYS   B 1 45 ? 29.282 16.818 14.399  1.00 25.51  ? 145 LYS   B C   1 
ATOM   1141 O  O   . LYS   B 1 45 ? 28.542 17.433 15.168  1.00 26.33  ? 145 LYS   B O   1 
ATOM   1142 C  CB  . LYS   B 1 45 ? 28.822 14.365 14.217  1.00 29.34  ? 145 LYS   B CB  1 
ATOM   1143 C  CG  . LYS   B 1 45 ? 28.840 14.236 12.703  1.00 31.68  ? 145 LYS   B CG  1 
ATOM   1144 C  CD  . LYS   B 1 45 ? 27.876 13.125 12.232  1.00 30.79  ? 145 LYS   B CD  1 
ATOM   1145 C  CE  . LYS   B 1 45 ? 28.249 12.637 10.834  1.00 38.97  ? 145 LYS   B CE  1 
ATOM   1146 N  NZ  . LYS   B 1 45 ? 28.212 11.151 10.806  1.00 61.30  ? 145 LYS   B NZ  1 
ATOM   1147 N  N   . MET   B 1 46 ? 29.707 17.313 13.233  1.00 22.87  ? 146 MET   B N   1 
ATOM   1148 C  CA  . MET   B 1 46 ? 29.158 18.533 12.651  1.00 21.62  ? 146 MET   B CA  1 
ATOM   1149 C  C   . MET   B 1 46 ? 28.307 18.184 11.440  1.00 24.49  ? 146 MET   B C   1 
ATOM   1150 O  O   . MET   B 1 46 ? 28.755 17.423 10.569  1.00 27.90  ? 146 MET   B O   1 
ATOM   1151 C  CB  . MET   B 1 46 ? 30.269 19.505 12.227  1.00 27.29  ? 146 MET   B CB  1 
ATOM   1152 C  CG  . MET   B 1 46 ? 31.188 19.926 13.327  1.00 30.49  ? 146 MET   B CG  1 
ATOM   1153 S  SD  . MET   B 1 46 ? 30.252 21.169 14.232  1.00 43.26  ? 146 MET   B SD  1 
ATOM   1154 C  CE  . MET   B 1 46 ? 30.324 22.518 13.054  1.00 48.83  ? 146 MET   B CE  1 
ATOM   1155 N  N   . ILE   B 1 47 ? 27.087 18.738 11.381  1.00 21.41  ? 147 ILE   B N   1 
ATOM   1156 C  CA  . ILE   B 1 47 ? 26.226 18.517 10.222  1.00 20.71  ? 147 ILE   B CA  1 
ATOM   1157 C  C   . ILE   B 1 47 ? 25.791 19.864 9.666   1.00 21.99  ? 147 ILE   B C   1 
ATOM   1158 O  O   . ILE   B 1 47 ? 25.621 20.850 10.393  1.00 26.12  ? 147 ILE   B O   1 
ATOM   1159 C  CB  . ILE   B 1 47 ? 24.990 17.661 10.524  1.00 26.56  ? 147 ILE   B CB  1 
ATOM   1160 C  CG1 . ILE   B 1 47 ? 24.083 18.369 11.534  1.00 22.96  ? 147 ILE   B CG1 1 
ATOM   1161 C  CG2 . ILE   B 1 47 ? 25.428 16.268 10.976  1.00 26.09  ? 147 ILE   B CG2 1 
ATOM   1162 C  CD1 . ILE   B 1 47 ? 22.730 17.644 11.710  1.00 29.53  ? 147 ILE   B CD1 1 
ATOM   1163 N  N   . GLY   B 1 48 ? 25.608 19.881 8.358   1.00 29.17  ? 148 GLY   B N   1 
ATOM   1164 C  CA  . GLY   B 1 48 ? 25.481 21.117 7.612   1.00 32.97  ? 148 GLY   B CA  1 
ATOM   1165 C  C   . GLY   B 1 48 ? 24.150 21.138 6.894   1.00 26.98  ? 148 GLY   B C   1 
ATOM   1166 O  O   . GLY   B 1 48 ? 23.704 20.124 6.342   1.00 33.27  ? 148 GLY   B O   1 
ATOM   1167 N  N   . GLY   B 1 49 ? 23.495 22.255 6.979   1.00 29.16  ? 149 GLY   B N   1 
ATOM   1168 C  CA  . GLY   B 1 49 ? 22.291 22.448 6.208   1.00 37.13  ? 149 GLY   B CA  1 
ATOM   1169 C  C   . GLY   B 1 49 ? 22.366 23.767 5.488   1.00 31.86  ? 149 GLY   B C   1 
ATOM   1170 O  O   . GLY   B 1 49 ? 23.442 24.321 5.270   1.00 34.93  ? 149 GLY   B O   1 
ATOM   1171 N  N   A ILE   B 1 50 ? 21.199 24.249 5.099   0.64 29.99  ? 150 ILE   B N   1 
ATOM   1172 N  N   B ILE   B 1 50 ? 21.205 24.317 5.168   0.36 30.12  ? 150 ILE   B N   1 
ATOM   1173 C  CA  A ILE   B 1 50 ? 21.078 25.638 4.727   0.64 36.21  ? 150 ILE   B CA  1 
ATOM   1174 C  CA  B ILE   B 1 50 ? 21.216 25.522 4.352   0.36 35.66  ? 150 ILE   B CA  1 
ATOM   1175 C  C   A ILE   B 1 50 ? 21.343 26.478 5.967   0.64 34.19  ? 150 ILE   B C   1 
ATOM   1176 C  C   B ILE   B 1 50 ? 21.874 26.686 5.094   0.36 34.59  ? 150 ILE   B C   1 
ATOM   1177 O  O   A ILE   B 1 50 ? 20.820 26.199 7.059   0.64 29.09  ? 150 ILE   B O   1 
ATOM   1178 O  O   B ILE   B 1 50 ? 22.627 27.465 4.496   0.36 41.81  ? 150 ILE   B O   1 
ATOM   1179 C  CB  A ILE   B 1 50 ? 19.692 25.898 4.129   0.64 36.57  ? 150 ILE   B CB  1 
ATOM   1180 C  CB  B ILE   B 1 50 ? 19.790 25.842 3.870   0.36 38.42  ? 150 ILE   B CB  1 
ATOM   1181 C  CG1 A ILE   B 1 50 ? 19.801 25.786 2.605   0.64 37.78  ? 150 ILE   B CG1 1 
ATOM   1182 C  CG1 B ILE   B 1 50 ? 19.663 25.333 2.432   0.36 35.75  ? 150 ILE   B CG1 1 
ATOM   1183 C  CG2 A ILE   B 1 50 ? 19.212 27.290 4.530   0.64 44.22  ? 150 ILE   B CG2 1 
ATOM   1184 C  CG2 B ILE   B 1 50 ? 19.496 27.332 3.978   0.36 43.75  ? 150 ILE   B CG2 1 
ATOM   1185 C  CD1 A ILE   B 1 50 ? 18.492 25.617 1.896   0.64 43.99  ? 150 ILE   B CD1 1 
ATOM   1186 C  CD1 B ILE   B 1 50 ? 18.277 25.309 1.874   0.36 43.58  ? 150 ILE   B CD1 1 
ATOM   1187 N  N   A GLY   B 1 51 ? 22.190 27.484 5.816   0.64 31.13  ? 151 GLY   B N   1 
ATOM   1188 N  N   B GLY   B 1 51 ? 21.657 26.794 6.404   0.36 35.50  ? 151 GLY   B N   1 
ATOM   1189 C  CA  A GLY   B 1 51 ? 22.508 28.377 6.898   0.64 36.55  ? 151 GLY   B CA  1 
ATOM   1190 C  CA  B GLY   B 1 51 ? 22.140 27.926 7.173   0.36 36.17  ? 151 GLY   B CA  1 
ATOM   1191 C  C   A GLY   B 1 51 ? 23.775 28.024 7.636   0.64 43.88  ? 151 GLY   B C   1 
ATOM   1192 C  C   B GLY   B 1 51 ? 23.499 27.781 7.837   0.36 42.61  ? 151 GLY   B C   1 
ATOM   1193 O  O   A GLY   B 1 51 ? 24.262 28.845 8.418   0.64 45.55  ? 151 GLY   B O   1 
ATOM   1194 O  O   B GLY   B 1 51 ? 23.812 28.569 8.736   0.36 43.57  ? 151 GLY   B O   1 
ATOM   1195 N  N   . GLY   B 1 52 ? 24.326 26.834 7.413   1.00 28.94  ? 152 GLY   B N   1 
ATOM   1196 C  CA  . GLY   B 1 52 ? 25.578 26.522 8.073   1.00 34.92  ? 152 GLY   B CA  1 
ATOM   1197 C  C   . GLY   B 1 52 ? 25.491 25.231 8.855   1.00 32.33  ? 152 GLY   B C   1 
ATOM   1198 O  O   . GLY   B 1 52 ? 24.584 24.423 8.643   1.00 29.32  ? 152 GLY   B O   1 
ATOM   1199 N  N   . PHE   B 1 53 ? 26.442 25.039 9.768   1.00 30.26  ? 153 PHE   B N   1 
ATOM   1200 C  CA  . PHE   B 1 53 ? 26.617 23.765 10.460  1.00 25.37  ? 153 PHE   B CA  1 
ATOM   1201 C  C   . PHE   B 1 53 ? 26.242 23.908 11.927  1.00 25.52  ? 153 PHE   B C   1 
ATOM   1202 O  O   . PHE   B 1 53 ? 26.309 24.995 12.506  1.00 31.47  ? 153 PHE   B O   1 
ATOM   1203 C  CB  . PHE   B 1 53 ? 28.076 23.272 10.365  1.00 26.47  ? 153 PHE   B CB  1 
ATOM   1204 C  CG  . PHE   B 1 53 ? 28.462 22.712 9.031   1.00 25.44  ? 153 PHE   B CG  1 
ATOM   1205 C  CD1 . PHE   B 1 53 ? 28.629 23.554 7.942   1.00 30.73  ? 153 PHE   B CD1 1 
ATOM   1206 C  CD2 . PHE   B 1 53 ? 28.669 21.346 8.863   1.00 29.68  ? 153 PHE   B CD2 1 
ATOM   1207 C  CE1 . PHE   B 1 53 ? 29.000 23.040 6.712   1.00 31.21  ? 153 PHE   B CE1 1 
ATOM   1208 C  CE2 . PHE   B 1 53 ? 29.026 20.831 7.635   1.00 33.13  ? 153 PHE   B CE2 1 
ATOM   1209 C  CZ  . PHE   B 1 53 ? 29.183 21.696 6.546   1.00 27.73  ? 153 PHE   B CZ  1 
ATOM   1210 N  N   . ILE   B 1 54 ? 25.871 22.781 12.546  1.00 24.04  ? 154 ILE   B N   1 
ATOM   1211 C  CA  . ILE   B 1 54 ? 25.667 22.717 13.989  1.00 23.54  ? 154 ILE   B CA  1 
ATOM   1212 C  C   . ILE   B 1 54 ? 26.408 21.498 14.510  1.00 24.37  ? 154 ILE   B C   1 
ATOM   1213 O  O   . ILE   B 1 54 ? 26.636 20.532 13.792  1.00 23.44  ? 154 ILE   B O   1 
ATOM   1214 C  CB  . ILE   B 1 54 ? 24.181 22.645 14.403  1.00 25.05  ? 154 ILE   B CB  1 
ATOM   1215 C  CG1 . ILE   B 1 54 ? 23.543 21.349 13.870  1.00 26.28  ? 154 ILE   B CG1 1 
ATOM   1216 C  CG2 . ILE   B 1 54 ? 23.426 23.884 13.911  1.00 29.27  ? 154 ILE   B CG2 1 
ATOM   1217 C  CD1 . ILE   B 1 54 ? 22.164 21.050 14.459  1.00 33.25  ? 154 ILE   B CD1 1 
ATOM   1218 N  N   . LYS   B 1 55 ? 26.764 21.546 15.792  1.00 25.28  ? 155 LYS   B N   1 
ATOM   1219 C  CA  . LYS   B 1 55 ? 27.403 20.406 16.448  1.00 24.82  ? 155 LYS   B CA  1 
ATOM   1220 C  C   . LYS   B 1 55 ? 26.328 19.542 17.087  1.00 22.55  ? 155 LYS   B C   1 
ATOM   1221 O  O   . LYS   B 1 55 ? 25.414 20.066 17.727  1.00 25.90  ? 155 LYS   B O   1 
ATOM   1222 C  CB  . LYS   B 1 55 ? 28.392 20.887 17.512  1.00 26.03  ? 155 LYS   B CB  1 
ATOM   1223 C  CG  . LYS   B 1 55 ? 29.257 19.788 18.136  1.00 33.27  ? 155 LYS   B CG  1 
ATOM   1224 C  CD  . LYS   B 1 55 ? 30.033 20.351 19.331  1.00 48.16  ? 155 LYS   B CD  1 
ATOM   1225 C  CE  . LYS   B 1 55 ? 31.220 19.456 19.677  1.00 60.56  ? 155 LYS   B CE  1 
ATOM   1226 N  NZ  . LYS   B 1 55 ? 31.516 19.425 21.132  1.00 75.17  ? 155 LYS   B NZ  1 
ATOM   1227 N  N   . VAL   B 1 56 ? 26.438 18.230 16.903  1.00 21.50  ? 156 VAL   B N   1 
ATOM   1228 C  CA  . VAL   B 1 56 ? 25.498 17.253 17.448  1.00 22.05  ? 156 VAL   B CA  1 
ATOM   1229 C  C   . VAL   B 1 56 ? 26.263 16.107 18.114  1.00 23.23  ? 156 VAL   B C   1 
ATOM   1230 O  O   . VAL   B 1 56 ? 27.452 15.893 17.887  1.00 25.37  ? 156 VAL   B O   1 
ATOM   1231 C  CB  . VAL   B 1 56 ? 24.557 16.692 16.345  1.00 23.60  ? 156 VAL   B CB  1 
ATOM   1232 C  CG1 . VAL   B 1 56 ? 23.713 17.801 15.729  1.00 24.85  ? 156 VAL   B CG1 1 
ATOM   1233 C  CG2 . VAL   B 1 56 ? 25.367 16.000 15.278  1.00 25.18  ? 156 VAL   B CG2 1 
ATOM   1234 N  N   . ARG   B 1 57 ? 25.549 15.344 18.932  1.00 21.95  ? 157 ARG   B N   1 
ATOM   1235 C  CA  . ARG   B 1 57 ? 26.086 14.129 19.522  1.00 23.62  ? 157 ARG   B CA  1 
ATOM   1236 C  C   . ARG   B 1 57 ? 25.525 12.942 18.764  1.00 21.31  ? 157 ARG   B C   1 
ATOM   1237 O  O   . ARG   B 1 57 ? 24.312 12.833 18.592  1.00 24.56  ? 157 ARG   B O   1 
ATOM   1238 C  CB  . ARG   B 1 57 ? 25.714 14.018 21.003  1.00 28.91  ? 157 ARG   B CB  1 
ATOM   1239 C  CG  . ARG   B 1 57 ? 25.846 15.341 21.757  1.00 32.02  ? 157 ARG   B CG  1 
ATOM   1240 C  CD  . ARG   B 1 57 ? 25.959 15.109 23.269  1.00 48.33  ? 157 ARG   B CD  1 
ATOM   1241 N  NE  . ARG   B 1 57 ? 24.707 14.638 23.861  1.00 64.98  ? 157 ARG   B NE  1 
ATOM   1242 C  CZ  . ARG   B 1 57 ? 23.600 15.359 24.013  1.00 87.39  ? 157 ARG   B CZ  1 
ATOM   1243 N  NH1 . ARG   B 1 57 ? 23.544 16.636 23.656  1.00 61.94  ? 157 ARG   B NH1 1 
ATOM   1244 N  NH2 . ARG   B 1 57 ? 22.524 14.789 24.556  1.00 70.01  ? 157 ARG   B NH2 1 
ATOM   1245 N  N   . GLN   B 1 58 ? 26.412 12.078 18.308  1.00 25.21  ? 158 GLN   B N   1 
ATOM   1246 C  CA  . GLN   B 1 58 ? 26.035 10.897 17.557  1.00 23.38  ? 158 GLN   B CA  1 
ATOM   1247 C  C   . GLN   B 1 58 ? 25.902 9.702  18.488  1.00 27.58  ? 158 GLN   B C   1 
ATOM   1248 O  O   . GLN   B 1 58 ? 26.902 9.236  19.051  1.00 28.38  ? 158 GLN   B O   1 
ATOM   1249 C  CB  . GLN   B 1 58 ? 27.089 10.603 16.501  1.00 23.78  ? 158 GLN   B CB  1 
ATOM   1250 C  CG  . GLN   B 1 58 ? 26.750 9.357  15.684  1.00 26.63  ? 158 GLN   B CG  1 
ATOM   1251 C  CD  . GLN   B 1 58 ? 27.887 8.961  14.767  1.00 38.15  ? 158 GLN   B CD  1 
ATOM   1252 O  OE1 . GLN   B 1 58 ? 28.483 9.818  14.108  1.00 41.85  ? 158 GLN   B OE1 1 
ATOM   1253 N  NE2 . GLN   B 1 58 ? 28.172 7.665  14.686  1.00 43.36  ? 158 GLN   B NE2 1 
ATOM   1254 N  N   . TYR   B 1 59 ? 24.691 9.168  18.593  1.00 25.16  ? 159 TYR   B N   1 
ATOM   1255 C  CA  . TYR   B 1 59 ? 24.438 7.924  19.318  1.00 27.65  ? 159 TYR   B CA  1 
ATOM   1256 C  C   . TYR   B 1 59 ? 24.190 6.782  18.343  1.00 31.41  ? 159 TYR   B C   1 
ATOM   1257 O  O   . TYR   B 1 59 ? 23.415 6.923  17.400  1.00 29.07  ? 159 TYR   B O   1 
ATOM   1258 C  CB  . TYR   B 1 59 ? 23.238 8.062  20.238  1.00 26.94  ? 159 TYR   B CB  1 
ATOM   1259 C  CG  . TYR   B 1 59 ? 23.413 9.002  21.406  1.00 29.17  ? 159 TYR   B CG  1 
ATOM   1260 C  CD1 . TYR   B 1 59 ? 23.201 10.367 21.272  1.00 33.45  ? 159 TYR   B CD1 1 
ATOM   1261 C  CD2 . TYR   B 1 59 ? 23.772 8.508  22.666  1.00 31.11  ? 159 TYR   B CD2 1 
ATOM   1262 C  CE1 . TYR   B 1 59 ? 23.340 11.221 22.360  1.00 33.45  ? 159 TYR   B CE1 1 
ATOM   1263 C  CE2 . TYR   B 1 59 ? 23.920 9.348  23.755  1.00 32.20  ? 159 TYR   B CE2 1 
ATOM   1264 C  CZ  . TYR   B 1 59 ? 23.708 10.698 23.604  1.00 34.24  ? 159 TYR   B CZ  1 
ATOM   1265 O  OH  . TYR   B 1 59 ? 23.850 11.554 24.674  1.00 40.68  ? 159 TYR   B OH  1 
ATOM   1266 N  N   . ASP   B 1 60 ? 24.800 5.626  18.593  1.00 28.04  ? 160 ASP   B N   1 
ATOM   1267 C  CA  . ASP   B 1 60 ? 24.570 4.472  17.731  1.00 33.93  ? 160 ASP   B CA  1 
ATOM   1268 C  C   . ASP   B 1 60 ? 23.606 3.465  18.371  1.00 31.43  ? 160 ASP   B C   1 
ATOM   1269 O  O   . ASP   B 1 60 ? 23.376 3.460  19.583  1.00 30.10  ? 160 ASP   B O   1 
ATOM   1270 C  CB  . ASP   B 1 60 ? 25.909 3.811  17.388  1.00 34.89  ? 160 ASP   B CB  1 
ATOM   1271 C  CG  . ASP   B 1 60 ? 26.807 4.712  16.535  1.00 52.72  ? 160 ASP   B CG  1 
ATOM   1272 O  OD1 . ASP   B 1 60 ? 26.266 5.523  15.744  1.00 43.82  ? 160 ASP   B OD1 1 
ATOM   1273 O  OD2 . ASP   B 1 60 ? 28.048 4.626  16.659  1.00 61.22  ? 160 ASP   B OD2 1 
ATOM   1274 N  N   . GLN   B 1 61 ? 22.980 2.659  17.516  1.00 32.69  ? 161 GLN   B N   1 
ATOM   1275 C  CA  . GLN   B 1 61 ? 22.162 1.518  17.951  1.00 33.31  ? 161 GLN   B CA  1 
ATOM   1276 C  C   . GLN   B 1 61 ? 21.001 1.939  18.859  1.00 31.50  ? 161 GLN   B C   1 
ATOM   1277 O  O   . GLN   B 1 61 ? 20.746 1.326  19.892  1.00 35.60  ? 161 GLN   B O   1 
ATOM   1278 C  CB  . GLN   B 1 61 ? 23.045 0.480  18.654  1.00 39.02  ? 161 GLN   B CB  1 
ATOM   1279 C  CG  . GLN   B 1 61 ? 24.009 -0.331 17.767  1.00 47.17  ? 161 GLN   B CG  1 
ATOM   1280 C  CD  . GLN   B 1 61 ? 23.427 -0.754 16.421  1.00 79.07  ? 161 GLN   B CD  1 
ATOM   1281 O  OE1 . GLN   B 1 61 ? 23.436 0.007  15.450  1.00 87.69  ? 161 GLN   B OE1 1 
ATOM   1282 N  NE2 . GLN   B 1 61 ? 22.931 -1.989 16.357  1.00 71.22  ? 161 GLN   B NE2 1 
ATOM   1283 N  N   . ILE   B 1 62 ? 20.278 2.995  18.467  1.00 26.98  ? 162 ILE   B N   1 
ATOM   1284 C  CA  . ILE   B 1 62 ? 19.155 3.515  19.238  1.00 30.64  ? 162 ILE   B CA  1 
ATOM   1285 C  C   . ILE   B 1 62 ? 17.862 2.961  18.655  1.00 35.87  ? 162 ILE   B C   1 
ATOM   1286 O  O   . ILE   B 1 62 ? 17.673 2.943  17.431  1.00 29.23  ? 162 ILE   B O   1 
ATOM   1287 C  CB  . ILE   B 1 62 ? 19.153 5.064  19.232  1.00 29.55  ? 162 ILE   B CB  1 
ATOM   1288 C  CG1 . ILE   B 1 62 ? 20.441 5.602  19.870  1.00 27.37  ? 162 ILE   B CG1 1 
ATOM   1289 C  CG2 . ILE   B 1 62 ? 17.894 5.626  19.932  1.00 28.44  ? 162 ILE   B CG2 1 
ATOM   1290 C  CD1 . ILE   B 1 62 ? 20.560 5.308  21.362  1.00 34.75  ? 162 ILE   B CD1 1 
ATOM   1291 N  N   . ILE   B 1 63 ? 16.965 2.505  19.521  1.00 31.04  ? 163 ILE   B N   1 
ATOM   1292 C  CA  . ILE   B 1 63 ? 15.678 1.992  19.071  1.00 29.58  ? 163 ILE   B CA  1 
ATOM   1293 C  C   . ILE   B 1 63 ? 14.679 3.139  19.055  1.00 33.35  ? 163 ILE   B C   1 
ATOM   1294 O  O   . ILE   B 1 63 ? 14.606 3.936  19.999  1.00 37.00  ? 163 ILE   B O   1 
ATOM   1295 C  CB  . ILE   B 1 63 ? 15.188 0.853  19.981  1.00 32.15  ? 163 ILE   B CB  1 
ATOM   1296 C  CG1 . ILE   B 1 63 ? 15.993 -0.405 19.719  1.00 39.92  ? 163 ILE   B CG1 1 
ATOM   1297 C  CG2 . ILE   B 1 63 ? 13.751 0.522  19.656  1.00 39.44  ? 163 ILE   B CG2 1 
ATOM   1298 C  CD1 . ILE   B 1 63 ? 16.331 -1.145 20.999  1.00 53.85  ? 163 ILE   B CD1 1 
ATOM   1299 N  N   A ILE   B 1 64 ? 13.886 3.204  17.995  0.40 32.99  ? 164 ILE   B N   1 
ATOM   1300 N  N   B ILE   B 1 64 ? 13.942 3.253  17.954  0.60 32.91  ? 164 ILE   B N   1 
ATOM   1301 C  CA  A ILE   B 1 64 ? 12.918 4.270  17.811  0.40 33.38  ? 164 ILE   B CA  1 
ATOM   1302 C  CA  B ILE   B 1 64 ? 12.921 4.270  17.758  0.60 33.35  ? 164 ILE   B CA  1 
ATOM   1303 C  C   A ILE   B 1 64 ? 11.682 3.668  17.155  0.40 34.85  ? 164 ILE   B C   1 
ATOM   1304 C  C   B ILE   B 1 64 ? 11.681 3.577  17.214  0.60 34.87  ? 164 ILE   B C   1 
ATOM   1305 O  O   A ILE   B 1 64 ? 11.789 2.899  16.194  0.40 37.43  ? 164 ILE   B O   1 
ATOM   1306 O  O   B ILE   B 1 64 ? 11.785 2.695  16.357  0.60 38.36  ? 164 ILE   B O   1 
ATOM   1307 C  CB  A ILE   B 1 64 ? 13.523 5.413  16.972  0.40 35.54  ? 164 ILE   B CB  1 
ATOM   1308 C  CB  B ILE   B 1 64 ? 13.380 5.368  16.772  0.60 35.07  ? 164 ILE   B CB  1 
ATOM   1309 C  CG1 A ILE   B 1 64 ? 12.607 6.633  16.929  0.40 38.97  ? 164 ILE   B CG1 1 
ATOM   1310 C  CG1 B ILE   B 1 64 ? 14.707 5.987  17.211  0.60 37.43  ? 164 ILE   B CG1 1 
ATOM   1311 C  CG2 A ILE   B 1 64 ? 13.888 4.916  15.585  0.40 31.80  ? 164 ILE   B CG2 1 
ATOM   1312 C  CG2 B ILE   B 1 64 ? 12.303 6.441  16.629  0.60 41.41  ? 164 ILE   B CG2 1 
ATOM   1313 C  CD1 A ILE   B 1 64 ? 13.312 7.868  16.396  0.40 29.51  ? 164 ILE   B CD1 1 
ATOM   1314 C  CD1 B ILE   B 1 64 ? 14.824 7.451  16.886  0.60 34.75  ? 164 ILE   B CD1 1 
ATOM   1315 N  N   . GLU   B 1 65 ? 10.516 3.970  17.705  1.00 28.63  ? 165 GLU   B N   1 
ATOM   1316 C  CA  . GLU   B 1 65 ? 9.244  3.535  17.141  1.00 29.40  ? 165 GLU   B CA  1 
ATOM   1317 C  C   . GLU   B 1 65 ? 8.702  4.676  16.296  1.00 36.31  ? 165 GLU   B C   1 
ATOM   1318 O  O   . GLU   B 1 65 ? 8.532  5.784  16.804  1.00 35.46  ? 165 GLU   B O   1 
ATOM   1319 C  CB  . GLU   B 1 65 ? 8.245  3.194  18.238  1.00 35.70  ? 165 GLU   B CB  1 
ATOM   1320 C  CG  . GLU   B 1 65 ? 7.481  1.953  17.985  1.00 64.50  ? 165 GLU   B CG  1 
ATOM   1321 C  CD  . GLU   B 1 65 ? 6.711  1.549  19.205  1.00 83.53  ? 165 GLU   B CD  1 
ATOM   1322 O  OE1 . GLU   B 1 65 ? 7.280  0.818  20.045  1.00 81.93  ? 165 GLU   B OE1 1 
ATOM   1323 O  OE2 . GLU   B 1 65 ? 5.546  1.981  19.323  1.00 83.80  ? 165 GLU   B OE2 1 
ATOM   1324 N  N   . ILE   B 1 66 ? 8.471  4.419  15.011  1.00 29.91  ? 166 ILE   B N   1 
ATOM   1325 C  CA  . ILE   B 1 66 ? 8.030  5.445  14.068  1.00 28.57  ? 166 ILE   B CA  1 
ATOM   1326 C  C   . ILE   B 1 66 ? 6.635  5.076  13.591  1.00 38.00  ? 166 ILE   B C   1 
ATOM   1327 O  O   . ILE   B 1 66 ? 6.471  4.113  12.832  1.00 34.12  ? 166 ILE   B O   1 
ATOM   1328 C  CB  . ILE   B 1 66 ? 8.996  5.581  12.880  1.00 30.36  ? 166 ILE   B CB  1 
ATOM   1329 C  CG1 . ILE   B 1 66 ? 10.421 5.822  13.399  1.00 38.82  ? 166 ILE   B CG1 1 
ATOM   1330 C  CG2 . ILE   B 1 66 ? 8.545  6.706  11.930  1.00 33.17  ? 166 ILE   B CG2 1 
ATOM   1331 C  CD1 . ILE   B 1 66 ? 11.516 5.528  12.419  1.00 37.37  ? 166 ILE   B CD1 1 
ATOM   1332 N  N   . ALA   B 1 67 ? 5.634  5.847  14.021  1.00 39.74  ? 167 ALA   B N   1 
ATOM   1333 C  CA  . ALA   B 1 67 ? 4.239  5.557  13.706  1.00 49.58  ? 167 ALA   B CA  1 
ATOM   1334 C  C   . ALA   B 1 67 ? 3.948  4.075  13.928  1.00 47.42  ? 167 ALA   B C   1 
ATOM   1335 O  O   . ALA   B 1 67 ? 3.379  3.388  13.077  1.00 46.81  ? 167 ALA   B O   1 
ATOM   1336 C  CB  . ALA   B 1 67 ? 3.894  5.982  12.274  1.00 55.32  ? 167 ALA   B CB  1 
ATOM   1337 N  N   . GLY   B 1 68 ? 4.399  3.572  15.072  1.00 38.44  ? 168 GLY   B N   1 
ATOM   1338 C  CA  . GLY   B 1 68 ? 4.152  2.192  15.443  1.00 44.96  ? 168 GLY   B CA  1 
ATOM   1339 C  C   . GLY   B 1 68 ? 5.070  1.162  14.824  1.00 55.18  ? 168 GLY   B C   1 
ATOM   1340 O  O   . GLY   B 1 68 ? 4.849  -0.036 15.033  1.00 54.30  ? 168 GLY   B O   1 
ATOM   1341 N  N   . HIS   B 1 69 ? 6.083  1.568  14.084  1.00 43.64  ? 169 HIS   B N   1 
ATOM   1342 C  CA  . HIS   B 1 69 ? 7.020  0.635  13.470  1.00 42.03  ? 169 HIS   B CA  1 
ATOM   1343 C  C   . HIS   B 1 69 ? 8.378  0.769  14.150  1.00 40.73  ? 169 HIS   B C   1 
ATOM   1344 O  O   . HIS   B 1 69 ? 8.940  1.869  14.212  1.00 35.81  ? 169 HIS   B O   1 
ATOM   1345 C  CB  . HIS   B 1 69 ? 7.166  0.902  11.968  1.00 40.60  ? 169 HIS   B CB  1 
ATOM   1346 C  CG  . HIS   B 1 69 ? 5.882  0.812  11.203  1.00 54.13  ? 169 HIS   B CG  1 
ATOM   1347 N  ND1 . HIS   B 1 69 ? 4.859  1.725  11.352  1.00 63.11  ? 169 HIS   B ND1 1 
ATOM   1348 C  CD2 . HIS   B 1 69 ? 5.442  -0.102 10.307  1.00 53.04  ? 169 HIS   B CD2 1 
ATOM   1349 C  CE1 . HIS   B 1 69 ? 3.850  1.384  10.568  1.00 63.84  ? 169 HIS   B CE1 1 
ATOM   1350 N  NE2 . HIS   B 1 69 ? 4.179  0.280  9.922   1.00 64.87  ? 169 HIS   B NE2 1 
ATOM   1351 N  N   . LYS   B 1 70 ? 8.916  -0.345 14.633  1.00 36.22  ? 170 LYS   B N   1 
ATOM   1352 C  CA  . LYS   B 1 70 ? 10.192 -0.350 15.335  1.00 40.16  ? 170 LYS   B CA  1 
ATOM   1353 C  C   . LYS   B 1 70 ? 11.357 -0.304 14.345  1.00 44.33  ? 170 LYS   B C   1 
ATOM   1354 O  O   . LYS   B 1 70 ? 11.328 -0.949 13.293  1.00 42.89  ? 170 LYS   B O   1 
ATOM   1355 C  CB  . LYS   B 1 70 ? 10.277 -1.596 16.218  1.00 45.31  ? 170 LYS   B CB  1 
ATOM   1356 C  CG  . LYS   B 1 70 ? 11.270 -1.517 17.348  1.00 57.57  ? 170 LYS   B CG  1 
ATOM   1357 C  CD  . LYS   B 1 70 ? 11.296 -2.818 18.149  1.00 88.20  ? 170 LYS   B CD  1 
ATOM   1358 C  CE  . LYS   B 1 70 ? 10.089 -2.925 19.084  1.00 94.81  ? 170 LYS   B CE  1 
ATOM   1359 N  NZ  . LYS   B 1 70 ? 10.460 -3.459 20.429  1.00 88.05  ? 170 LYS   B NZ  1 
ATOM   1360 N  N   . ALA   B 1 71 ? 12.385 0.477  14.677  1.00 31.04  ? 171 ALA   B N   1 
ATOM   1361 C  CA  . ALA   B 1 71 ? 13.554 0.560  13.817  1.00 31.80  ? 171 ALA   B CA  1 
ATOM   1362 C  C   . ALA   B 1 71 ? 14.754 0.862  14.694  1.00 37.20  ? 171 ALA   B C   1 
ATOM   1363 O  O   . ALA   B 1 71 ? 14.608 1.392  15.803  1.00 38.58  ? 171 ALA   B O   1 
ATOM   1364 C  CB  . ALA   B 1 71 ? 13.383 1.627  12.731  1.00 32.24  ? 171 ALA   B CB  1 
ATOM   1365 N  N   . ILE   B 1 72 ? 15.946 0.504  14.216  1.00 26.56  ? 172 ILE   B N   1 
ATOM   1366 C  CA  . ILE   B 1 72 ? 17.156 0.763  14.991  1.00 27.85  ? 172 ILE   B CA  1 
ATOM   1367 C  C   . ILE   B 1 72 ? 18.210 1.427  14.106  1.00 28.06  ? 172 ILE   B C   1 
ATOM   1368 O  O   . ILE   B 1 72 ? 18.343 1.101  12.920  1.00 26.12  ? 172 ILE   B O   1 
ATOM   1369 C  CB  . ILE   B 1 72 ? 17.708 -0.522 15.666  1.00 32.05  ? 172 ILE   B CB  1 
ATOM   1370 C  CG1 . ILE   B 1 72 ? 18.818 -0.162 16.652  1.00 38.76  ? 172 ILE   B CG1 1 
ATOM   1371 C  CG2 . ILE   B 1 72 ? 18.250 -1.513 14.650  1.00 36.78  ? 172 ILE   B CG2 1 
ATOM   1372 C  CD1 . ILE   B 1 72 ? 19.236 -1.305 17.580  1.00 49.54  ? 172 ILE   B CD1 1 
ATOM   1373 N  N   . GLY   B 1 73 ? 18.942 2.376  14.681  1.00 27.82  ? 173 GLY   B N   1 
ATOM   1374 C  CA  . GLY   B 1 73 ? 20.009 3.018  13.943  1.00 27.72  ? 173 GLY   B CA  1 
ATOM   1375 C  C   . GLY   B 1 73 ? 20.604 4.178  14.723  1.00 26.81  ? 173 GLY   B C   1 
ATOM   1376 O  O   . GLY   B 1 73 ? 20.301 4.391  15.905  1.00 26.89  ? 173 GLY   B O   1 
ATOM   1377 N  N   . THR   B 1 74 ? 21.447 4.931  14.012  1.00 25.81  ? 174 THR   B N   1 
ATOM   1378 C  CA  . THR   B 1 74 ? 22.135 6.094  14.568  1.00 25.73  ? 174 THR   B CA  1 
ATOM   1379 C  C   . THR   B 1 74 ? 21.179 7.279  14.666  1.00 28.41  ? 174 THR   B C   1 
ATOM   1380 O  O   . THR   B 1 74 ? 20.363 7.528  13.765  1.00 26.26  ? 174 THR   B O   1 
ATOM   1381 C  CB  . THR   B 1 74 ? 23.342 6.429  13.682  1.00 32.44  ? 174 THR   B CB  1 
ATOM   1382 O  OG1 . THR   B 1 74 ? 24.315 5.378  13.802  1.00 34.45  ? 174 THR   B OG1 1 
ATOM   1383 C  CG2 . THR   B 1 74 ? 24.002 7.762  14.069  1.00 28.38  ? 174 THR   B CG2 1 
ATOM   1384 N  N   . VAL   B 1 75 ? 21.278 8.026  15.773  1.00 21.97  ? 175 VAL   B N   1 
ATOM   1385 C  CA  . VAL   B 1 75 ? 20.451 9.196  16.003  1.00 21.44  ? 175 VAL   B CA  1 
ATOM   1386 C  C   . VAL   B 1 75 ? 21.396 10.325 16.387  1.00 22.45  ? 175 VAL   B C   1 
ATOM   1387 O  O   . VAL   B 1 75 ? 22.325 10.112 17.170  1.00 25.45  ? 175 VAL   B O   1 
ATOM   1388 C  CB  . VAL   B 1 75 ? 19.397 8.919  17.099  1.00 24.41  ? 175 VAL   B CB  1 
ATOM   1389 C  CG1 . VAL   B 1 75 ? 18.700 10.184 17.523  1.00 27.39  ? 175 VAL   B CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 75 ? 18.372 7.913  16.565  1.00 27.35  ? 175 VAL   B CG2 1 
ATOM   1391 N  N   . LEU   B 1 76 ? 21.231 11.489 15.771  1.00 20.94  ? 176 LEU   B N   1 
ATOM   1392 C  CA  . LEU   B 1 76 ? 22.052 12.653 16.101  1.00 18.93  ? 176 LEU   B CA  1 
ATOM   1393 C  C   . LEU   B 1 76 ? 21.214 13.545 17.003  1.00 23.33  ? 176 LEU   B C   1 
ATOM   1394 O  O   . LEU   B 1 76 ? 20.046 13.785 16.700  1.00 24.69  ? 176 LEU   B O   1 
ATOM   1395 C  CB  . LEU   B 1 76 ? 22.444 13.429 14.839  1.00 19.68  ? 176 LEU   B CB  1 
ATOM   1396 C  CG  . LEU   B 1 76 ? 23.096 12.563 13.777  1.00 20.79  ? 176 LEU   B CG  1 
ATOM   1397 C  CD1 . LEU   B 1 76 ? 23.427 13.425 12.573  1.00 21.70  ? 176 LEU   B CD1 1 
ATOM   1398 C  CD2 . LEU   B 1 76 ? 24.343 11.837 14.322  1.00 24.02  ? 176 LEU   B CD2 1 
ATOM   1399 N  N   . VAL   B 1 77 ? 21.799 14.032 18.101  1.00 22.64  ? 177 VAL   B N   1 
ATOM   1400 C  CA  . VAL   B 1 77 ? 21.073 14.852 19.070  1.00 19.04  ? 177 VAL   B CA  1 
ATOM   1401 C  C   . VAL   B 1 77 ? 21.732 16.219 19.130  1.00 19.37  ? 177 VAL   B C   1 
ATOM   1402 O  O   . VAL   B 1 77 ? 22.950 16.315 19.316  1.00 24.33  ? 177 VAL   B O   1 
ATOM   1403 C  CB  . VAL   B 1 77 ? 21.069 14.202 20.469  1.00 22.86  ? 177 VAL   B CB  1 
ATOM   1404 C  CG1 . VAL   B 1 77 ? 20.298 15.091 21.425  1.00 26.22  ? 177 VAL   B CG1 1 
ATOM   1405 C  CG2 . VAL   B 1 77 ? 20.452 12.818 20.391  1.00 27.71  ? 177 VAL   B CG2 1 
ATOM   1406 N  N   . GLY   B 1 78 ? 20.926 17.274 18.964  1.00 22.67  ? 178 GLY   B N   1 
ATOM   1407 C  CA  . GLY   B 1 78 ? 21.461 18.610 18.962  1.00 24.10  ? 178 GLY   B CA  1 
ATOM   1408 C  C   . GLY   B 1 78 ? 20.384 19.667 18.831  1.00 24.24  ? 178 GLY   B C   1 
ATOM   1409 O  O   . GLY   B 1 78 ? 19.179 19.383 18.853  1.00 28.35  ? 178 GLY   B O   1 
ATOM   1410 N  N   . PRO   B 1 79 ? 20.809 20.923 18.682  1.00 24.93  ? 179 PRO   B N   1 
ATOM   1411 C  CA  . PRO   B 1 79 ? 19.869 22.063 18.664  1.00 26.94  ? 179 PRO   B CA  1 
ATOM   1412 C  C   . PRO   B 1 79 ? 19.148 22.229 17.328  1.00 34.85  ? 179 PRO   B C   1 
ATOM   1413 O  O   . PRO   B 1 79 ? 19.272 23.247 16.635  1.00 37.04  ? 179 PRO   B O   1 
ATOM   1414 C  CB  . PRO   B 1 79 ? 20.791 23.247 18.983  1.00 29.36  ? 179 PRO   B CB  1 
ATOM   1415 C  CG  . PRO   B 1 79 ? 22.128 22.837 18.368  1.00 39.67  ? 179 PRO   B CG  1 
ATOM   1416 C  CD  . PRO   B 1 79 ? 22.222 21.340 18.584  1.00 28.82  ? 179 PRO   B CD  1 
ATOM   1417 N  N   . THR   B 1 80 ? 18.362 21.219 16.958  1.00 29.40  ? 180 THR   B N   1 
ATOM   1418 C  CA  . THR   B 1 80 ? 17.533 21.361 15.771  1.00 27.85  ? 180 THR   B CA  1 
ATOM   1419 C  C   . THR   B 1 80 ? 16.170 21.941 16.152  1.00 30.94  ? 180 THR   B C   1 
ATOM   1420 O  O   . THR   B 1 80 ? 15.626 21.615 17.214  1.00 35.95  ? 180 THR   B O   1 
ATOM   1421 C  CB  . THR   B 1 80 ? 17.363 19.992 15.081  1.00 29.69  ? 180 THR   B CB  1 
ATOM   1422 O  OG1 . THR   B 1 80 ? 16.467 20.117 13.977  1.00 28.18  ? 180 THR   B OG1 1 
ATOM   1423 C  CG2 . THR   B 1 80 ? 16.798 18.929 16.064  1.00 25.17  ? 180 THR   B CG2 1 
ATOM   1424 N  N   . PRO   B 1 81 ? 15.561 22.786 15.302  1.00 33.20  ? 181 PRO   B N   1 
ATOM   1425 C  CA  . PRO   B 1 81 ? 14.226 23.319 15.636  1.00 35.07  ? 181 PRO   B CA  1 
ATOM   1426 C  C   . PRO   B 1 81 ? 13.114 22.324 15.442  1.00 43.74  ? 181 PRO   B C   1 
ATOM   1427 O  O   . PRO   B 1 81 ? 12.009 22.540 15.963  1.00 37.75  ? 181 PRO   B O   1 
ATOM   1428 C  CB  . PRO   B 1 81 ? 14.049 24.503 14.667  1.00 43.79  ? 181 PRO   B CB  1 
ATOM   1429 C  CG  . PRO   B 1 81 ? 15.089 24.332 13.596  1.00 41.70  ? 181 PRO   B CG  1 
ATOM   1430 C  CD  . PRO   B 1 81 ? 16.011 23.189 13.957  1.00 38.00  ? 181 PRO   B CD  1 
ATOM   1431 N  N   A VAL   B 1 82 ? 13.352 21.240 14.716  0.49 28.41  ? 182 VAL   B N   1 
ATOM   1432 N  N   B VAL   B 1 82 ? 13.362 21.245 14.697  0.51 28.39  ? 182 VAL   B N   1 
ATOM   1433 C  CA  A VAL   B 1 82 ? 12.318 20.248 14.499  0.49 26.59  ? 182 VAL   B CA  1 
ATOM   1434 C  CA  B VAL   B 1 82 ? 12.350 20.258 14.344  0.51 26.66  ? 182 VAL   B CA  1 
ATOM   1435 C  C   A VAL   B 1 82 ? 13.002 18.889 14.511  0.49 25.24  ? 182 VAL   B C   1 
ATOM   1436 C  C   B VAL   B 1 82 ? 13.004 18.879 14.448  0.51 25.25  ? 182 VAL   B C   1 
ATOM   1437 O  O   A VAL   B 1 82 ? 14.171 18.758 14.136  0.49 28.11  ? 182 VAL   B O   1 
ATOM   1438 O  O   B VAL   B 1 82 ? 14.172 18.720 14.073  0.51 28.18  ? 182 VAL   B O   1 
ATOM   1439 C  CB  A VAL   B 1 82 ? 11.581 20.494 13.171  0.49 32.85  ? 182 VAL   B CB  1 
ATOM   1440 C  CB  B VAL   B 1 82 ? 11.802 20.510 12.916  0.51 32.71  ? 182 VAL   B CB  1 
ATOM   1441 C  CG1 A VAL   B 1 82 ? 12.576 20.460 12.059  0.49 29.05  ? 182 VAL   B CG1 1 
ATOM   1442 C  CG1 B VAL   B 1 82 ? 10.811 19.434 12.507  0.51 31.75  ? 182 VAL   B CG1 1 
ATOM   1443 C  CG2 A VAL   B 1 82 ? 10.455 19.496 12.952  0.49 32.95  ? 182 VAL   B CG2 1 
ATOM   1444 C  CG2 B VAL   B 1 82 ? 11.185 21.915 12.776  0.51 30.12  ? 182 VAL   B CG2 1 
ATOM   1445 N  N   . ASN   B 1 83 ? 12.272 17.886 14.974  1.00 24.29  ? 183 ASN   B N   1 
ATOM   1446 C  CA  . ASN   B 1 83 ? 12.774 16.515 14.977  1.00 19.73  ? 183 ASN   B CA  1 
ATOM   1447 C  C   . ASN   B 1 83 ? 12.632 15.965 13.565  1.00 22.30  ? 183 ASN   B C   1 
ATOM   1448 O  O   . ASN   B 1 83 ? 11.561 16.104 12.953  1.00 23.89  ? 183 ASN   B O   1 
ATOM   1449 C  CB  . ASN   B 1 83 ? 11.980 15.632 15.947  1.00 23.83  ? 183 ASN   B CB  1 
ATOM   1450 C  CG  . ASN   B 1 83 ? 12.157 16.074 17.397  1.00 33.85  ? 183 ASN   B CG  1 
ATOM   1451 O  OD1 . ASN   B 1 83 ? 13.255 16.424 17.811  1.00 30.39  ? 183 ASN   B OD1 1 
ATOM   1452 N  ND2 . ASN   B 1 83 ? 11.050 16.176 18.127  1.00 31.68  ? 183 ASN   B ND2 1 
ATOM   1453 N  N   . ILE   B 1 84 ? 13.695 15.325 13.069  1.00 20.07  ? 184 ILE   B N   1 
ATOM   1454 C  CA  . ILE   B 1 84 ? 13.825 14.929 11.663  1.00 20.35  ? 184 ILE   B CA  1 
ATOM   1455 C  C   . ILE   B 1 84 ? 14.096 13.424 11.616  1.00 17.77  ? 184 ILE   B C   1 
ATOM   1456 O  O   . ILE   B 1 84 ? 15.115 12.970 12.148  1.00 21.24  ? 184 ILE   B O   1 
ATOM   1457 C  CB  . ILE   B 1 84 ? 14.998 15.672 10.996  1.00 21.99  ? 184 ILE   B CB  1 
ATOM   1458 C  CG1 . ILE   B 1 84 ? 14.718 17.172 10.880  1.00 24.97  ? 184 ILE   B CG1 1 
ATOM   1459 C  CG2 . ILE   B 1 84 ? 15.260 15.103 9.603   1.00 27.73  ? 184 ILE   B CG2 1 
ATOM   1460 C  CD1 . ILE   B 1 84 ? 13.314 17.494 10.559  1.00 36.57  ? 184 ILE   B CD1 1 
ATOM   1461 N  N   . ILE   B 1 85 ? 13.227 12.662 10.949  1.00 17.55  ? 185 ILE   B N   1 
ATOM   1462 C  CA  . ILE   B 1 85 ? 13.470 11.247 10.684  1.00 18.55  ? 185 ILE   B CA  1 
ATOM   1463 C  C   . ILE   B 1 85 ? 14.081 11.174 9.290   1.00 18.90  ? 185 ILE   B C   1 
ATOM   1464 O  O   . ILE   B 1 85 ? 13.407 11.482 8.300   1.00 20.95  ? 185 ILE   B O   1 
ATOM   1465 C  CB  . ILE   B 1 85 ? 12.175 10.424 10.743  1.00 20.93  ? 185 ILE   B CB  1 
ATOM   1466 C  CG1 . ILE   B 1 85 ? 11.515 10.517 12.116  1.00 22.70  ? 185 ILE   B CG1 1 
ATOM   1467 C  CG2 . ILE   B 1 85 ? 12.481 8.973  10.342  1.00 24.21  ? 185 ILE   B CG2 1 
ATOM   1468 C  CD1 . ILE   B 1 85 ? 12.440 10.153 13.258  1.00 27.73  ? 185 ILE   B CD1 1 
ATOM   1469 N  N   . GLY   B 1 86 ? 15.353 10.775 9.196   1.00 18.21  ? 186 GLY   B N   1 
ATOM   1470 C  CA  . GLY   B 1 86 ? 16.064 10.770 7.934   1.00 17.55  ? 186 GLY   B CA  1 
ATOM   1471 C  C   . GLY   B 1 86 ? 16.073 9.390  7.276   1.00 18.70  ? 186 GLY   B C   1 
ATOM   1472 O  O   . GLY   B 1 86 ? 15.507 8.433  7.793   1.00 19.15  ? 186 GLY   B O   1 
ATOM   1473 N  N   . ARG   B 1 87 ? 16.783 9.313  6.147   1.00 17.96  ? 187 ARG   B N   1 
ATOM   1474 C  CA  . ARG   B 1 87 ? 16.766 8.102  5.319   1.00 16.85  ? 187 ARG   B CA  1 
ATOM   1475 C  C   . ARG   B 1 87 ? 17.279 6.874  6.064   1.00 21.16  ? 187 ARG   B C   1 
ATOM   1476 O  O   . ARG   B 1 87 ? 16.801 5.767  5.800   1.00 21.11  ? 187 ARG   B O   1 
ATOM   1477 C  CB  . ARG   B 1 87 ? 17.589 8.303  4.050   1.00 17.46  ? 187 ARG   B CB  1 
ATOM   1478 C  CG  . ARG   B 1 87 ? 16.937 9.296  3.053   1.00 17.24  ? 187 ARG   B CG  1 
ATOM   1479 C  CD  . ARG   B 1 87 ? 17.692 9.282  1.709   1.00 17.05  ? 187 ARG   B CD  1 
ATOM   1480 N  NE  . ARG   B 1 87 ? 19.089 9.697  1.829   1.00 20.93  ? 187 ARG   B NE  1 
ATOM   1481 C  CZ  . ARG   B 1 87 ? 20.137 8.875  1.855   1.00 24.41  ? 187 ARG   B CZ  1 
ATOM   1482 N  NH1 . ARG   B 1 87 ? 20.003 7.562  1.707   1.00 23.12  ? 187 ARG   B NH1 1 
ATOM   1483 N  NH2 . ARG   B 1 87 ? 21.356 9.381  2.028   1.00 25.93  ? 187 ARG   B NH2 1 
ATOM   1484 N  N   . ASN   B 1 88 ? 18.217 7.045  6.997   1.00 19.00  ? 188 ASN   B N   1 
ATOM   1485 C  CA  . ASN   B 1 88 ? 18.795 5.890  7.691   1.00 19.16  ? 188 ASN   B CA  1 
ATOM   1486 C  C   . ASN   B 1 88 ? 17.742 5.114  8.466   1.00 24.19  ? 188 ASN   B C   1 
ATOM   1487 O  O   . ASN   B 1 88 ? 17.903 3.910  8.661   1.00 23.85  ? 188 ASN   B O   1 
ATOM   1488 C  CB  . ASN   B 1 88 ? 19.937 6.347  8.604   1.00 18.46  ? 188 ASN   B CB  1 
ATOM   1489 C  CG  . ASN   B 1 88 ? 19.437 7.063  9.862   1.00 27.51  ? 188 ASN   B CG  1 
ATOM   1490 O  OD1 . ASN   B 1 88 ? 18.629 8.000  9.793   1.00 23.20  ? 188 ASN   B OD1 1 
ATOM   1491 N  ND2 . ASN   B 1 88 ? 19.932 6.619  11.025  1.00 26.28  ? 188 ASN   B ND2 1 
ATOM   1492 N  N   . LEU   B 1 89 ? 16.672 5.772  8.934   1.00 19.37  ? 189 LEU   B N   1 
ATOM   1493 C  CA  . LEU   B 1 89 ? 15.548 5.064  9.553   1.00 20.08  ? 189 LEU   B CA  1 
ATOM   1494 C  C   . LEU   B 1 89 ? 14.342 4.897  8.627   1.00 25.30  ? 189 LEU   B C   1 
ATOM   1495 O  O   . LEU   B 1 89 ? 13.576 3.939  8.803   1.00 22.13  ? 189 LEU   B O   1 
ATOM   1496 C  CB  . LEU   B 1 89 ? 15.101 5.767  10.855  1.00 18.84  ? 189 LEU   B CB  1 
ATOM   1497 C  CG  . LEU   B 1 89 ? 16.215 5.732  11.905  1.00 27.39  ? 189 LEU   B CG  1 
ATOM   1498 C  CD1 . LEU   B 1 89 ? 15.772 6.503  13.142  1.00 30.19  ? 189 LEU   B CD1 1 
ATOM   1499 C  CD2 . LEU   B 1 89 ? 16.520 4.266  12.280  1.00 28.68  ? 189 LEU   B CD2 1 
ATOM   1500 N  N   . LEU   B 1 90 ? 14.133 5.787  7.636   1.00 18.34  ? 190 LEU   B N   1 
ATOM   1501 C  CA  . LEU   B 1 90 ? 13.005 5.578  6.715   1.00 17.36  ? 190 LEU   B CA  1 
ATOM   1502 C  C   . LEU   B 1 90 ? 13.151 4.262  5.949   1.00 21.23  ? 190 LEU   B C   1 
ATOM   1503 O  O   . LEU   B 1 90 ? 12.145 3.610  5.641   1.00 21.80  ? 190 LEU   B O   1 
ATOM   1504 C  CB  . LEU   B 1 90 ? 12.867 6.743  5.695   1.00 18.06  ? 190 LEU   B CB  1 
ATOM   1505 C  CG  . LEU   B 1 90 ? 12.517 8.096  6.369   1.00 22.21  ? 190 LEU   B CG  1 
ATOM   1506 C  CD1 . LEU   B 1 90 ? 12.704 9.239  5.348   1.00 23.98  ? 190 LEU   B CD1 1 
ATOM   1507 C  CD2 . LEU   B 1 90 ? 11.108 8.059  6.927   1.00 27.71  ? 190 LEU   B CD2 1 
ATOM   1508 N  N   . THR   B 1 91 ? 14.374 3.903  5.572   1.00 19.48  ? 191 THR   B N   1 
ATOM   1509 C  CA  . THR   B 1 91 ? 14.560 2.634  4.850   1.00 18.89  ? 191 THR   B CA  1 
ATOM   1510 C  C   . THR   B 1 91 ? 14.085 1.455  5.706   1.00 24.48  ? 191 THR   B C   1 
ATOM   1511 O  O   . THR   B 1 91 ? 13.552 0.476  5.176   1.00 23.99  ? 191 THR   B O   1 
ATOM   1512 C  CB  . THR   B 1 91 ? 16.024 2.407  4.476   1.00 22.14  ? 191 THR   B CB  1 
ATOM   1513 O  OG1 . THR   B 1 91 ? 16.817 2.499  5.659   1.00 23.02  ? 191 THR   B OG1 1 
ATOM   1514 C  CG2 . THR   B 1 91 ? 16.570 3.453  3.447   1.00 23.31  ? 191 THR   B CG2 1 
ATOM   1515 N  N   . GLN   B 1 92 ? 14.296 1.527  7.028   1.00 20.64  ? 192 GLN   B N   1 
ATOM   1516 C  CA  . GLN   B 1 92 ? 14.000 0.381  7.894   1.00 20.15  ? 192 GLN   B CA  1 
ATOM   1517 C  C   . GLN   B 1 92 ? 12.514 0.143  8.057   1.00 28.94  ? 192 GLN   B C   1 
ATOM   1518 O  O   . GLN   B 1 92 ? 12.116 -0.988 8.382   1.00 28.16  ? 192 GLN   B O   1 
ATOM   1519 C  CB  . GLN   B 1 92 ? 14.651 0.583  9.267   1.00 22.18  ? 192 GLN   B CB  1 
ATOM   1520 C  CG  . GLN   B 1 92 ? 16.152 0.736  9.194   1.00 19.40  ? 192 GLN   B CG  1 
ATOM   1521 C  CD  . GLN   B 1 92 ? 16.841 -0.530 8.655   1.00 25.74  ? 192 GLN   B CD  1 
ATOM   1522 O  OE1 . GLN   B 1 92 ? 16.920 -1.547 9.350   1.00 22.50  ? 192 GLN   B OE1 1 
ATOM   1523 N  NE2 . GLN   B 1 92 ? 17.268 -0.485 7.409   1.00 21.52  ? 192 GLN   B NE2 1 
ATOM   1524 N  N   . ILE   B 1 93 ? 11.677 1.171  7.876   1.00 24.56  ? 193 ILE   B N   1 
ATOM   1525 C  CA  . ILE   B 1 93 ? 10.232 0.987  7.936   1.00 25.09  ? 193 ILE   B CA  1 
ATOM   1526 C  C   . ILE   B 1 93 ? 9.626  0.808  6.549   1.00 27.51  ? 193 ILE   B C   1 
ATOM   1527 O  O   . ILE   B 1 93 ? 8.399  0.738  6.416   1.00 28.38  ? 193 ILE   B O   1 
ATOM   1528 C  CB  . ILE   B 1 93 ? 9.544  2.131  8.708   1.00 26.39  ? 193 ILE   B CB  1 
ATOM   1529 C  CG1 . ILE   B 1 93 ? 9.599  3.442  7.925   1.00 26.26  ? 193 ILE   B CG1 1 
ATOM   1530 C  CG2 . ILE   B 1 93 ? 10.194 2.335  10.080  1.00 32.32  ? 193 ILE   B CG2 1 
ATOM   1531 C  CD1 . ILE   B 1 93 ? 8.616  4.506  8.503   1.00 29.02  ? 193 ILE   B CD1 1 
ATOM   1532 N  N   . GLY   B 1 94 ? 10.457 0.718  5.514   1.00 24.58  ? 194 GLY   B N   1 
ATOM   1533 C  CA  . GLY   B 1 94 ? 9.982  0.405  4.184   1.00 26.22  ? 194 GLY   B CA  1 
ATOM   1534 C  C   . GLY   B 1 94 ? 9.377  1.572  3.439   1.00 32.62  ? 194 GLY   B C   1 
ATOM   1535 O  O   . GLY   B 1 94 ? 8.572  1.367  2.522   1.00 32.55  ? 194 GLY   B O   1 
ATOM   1536 N  N   . ALA   B 1 95 ? 9.764  2.797  3.790   1.00 22.93  ? 195 ALA   B N   1 
ATOM   1537 C  CA  . ALA   B 1 95 ? 9.163  3.987  3.201   1.00 26.17  ? 195 ALA   B CA  1 
ATOM   1538 C  C   . ALA   B 1 95 ? 9.686  4.221  1.794   1.00 25.34  ? 195 ALA   B C   1 
ATOM   1539 O  O   . ALA   B 1 95 ? 10.886 4.113  1.543   1.00 32.95  ? 195 ALA   B O   1 
ATOM   1540 C  CB  . ALA   B 1 95 ? 9.467  5.207  4.068   1.00 25.25  ? 195 ALA   B CB  1 
ATOM   1541 N  N   . THR   B 1 96 ? 8.784  4.584  0.879   1.00 21.94  ? 196 THR   B N   1 
ATOM   1542 C  CA  . THR   B 1 96 ? 9.145  4.917  -0.489  1.00 19.31  ? 196 THR   B CA  1 
ATOM   1543 C  C   . THR   B 1 96 ? 8.443  6.214  -0.898  1.00 22.48  ? 196 THR   B C   1 
ATOM   1544 O  O   . THR   B 1 96 ? 7.401  6.592  -0.345  1.00 25.94  ? 196 THR   B O   1 
ATOM   1545 C  CB  . THR   B 1 96 ? 8.740  3.830  -1.498  1.00 25.78  ? 196 THR   B CB  1 
ATOM   1546 O  OG1 . THR   B 1 96 ? 7.323  3.634  -1.413  1.00 29.78  ? 196 THR   B OG1 1 
ATOM   1547 C  CG2 . THR   B 1 96 ? 9.504  2.519  -1.229  1.00 30.78  ? 196 THR   B CG2 1 
ATOM   1548 N  N   A LEU   B 1 97 ? 9.049  6.888  -1.867  0.48 23.62  ? 197 LEU   B N   1 
ATOM   1549 N  N   B LEU   B 1 97 ? 9.049  6.899  -1.869  0.52 23.60  ? 197 LEU   B N   1 
ATOM   1550 C  CA  A LEU   B 1 97 ? 8.458  8.048  -2.510  0.48 22.31  ? 197 LEU   B CA  1 
ATOM   1551 C  CA  B LEU   B 1 97 ? 8.465  8.068  -2.516  0.52 22.28  ? 197 LEU   B CA  1 
ATOM   1552 C  C   A LEU   B 1 97 ? 7.861  7.557  -3.819  0.48 27.41  ? 197 LEU   B C   1 
ATOM   1553 C  C   B LEU   B 1 97 ? 7.885  7.618  -3.849  0.52 27.40  ? 197 LEU   B C   1 
ATOM   1554 O  O   A LEU   B 1 97 ? 8.518  6.814  -4.555  0.48 30.28  ? 197 LEU   B O   1 
ATOM   1555 O  O   B LEU   B 1 97 ? 8.592  7.001  -4.651  0.52 30.76  ? 197 LEU   B O   1 
ATOM   1556 C  CB  A LEU   B 1 97 ? 9.525  9.114  -2.762  0.48 26.79  ? 197 LEU   B CB  1 
ATOM   1557 C  CB  B LEU   B 1 97 ? 9.524  9.151  -2.756  0.52 26.75  ? 197 LEU   B CB  1 
ATOM   1558 C  CG  A LEU   B 1 97 ? 9.620  10.338 -1.872  0.48 30.68  ? 197 LEU   B CG  1 
ATOM   1559 C  CG  B LEU   B 1 97 ? 9.200  10.640 -2.862  0.52 31.51  ? 197 LEU   B CG  1 
ATOM   1560 C  CD1 A LEU   B 1 97 ? 10.774 11.201 -2.379  0.48 31.42  ? 197 LEU   B CD1 1 
ATOM   1561 C  CD1 B LEU   B 1 97 ? 8.080  11.065 -1.928  0.52 32.06  ? 197 LEU   B CD1 1 
ATOM   1562 C  CD2 A LEU   B 1 97 ? 8.322  11.127 -1.893  0.48 31.73  ? 197 LEU   B CD2 1 
ATOM   1563 C  CD2 B LEU   B 1 97 ? 10.470 11.467 -2.647  0.52 34.76  ? 197 LEU   B CD2 1 
ATOM   1564 N  N   . ASN   B 1 98 ? 6.610  7.931  -4.088  1.00 24.99  ? 198 ASN   B N   1 
ATOM   1565 C  CA  . ASN   B 1 98 ? 5.904  7.451  -5.280  1.00 23.72  ? 198 ASN   B CA  1 
ATOM   1566 C  C   . ASN   B 1 98 ? 5.285  8.606  -6.050  1.00 27.12  ? 198 ASN   B C   1 
ATOM   1567 O  O   . ASN   B 1 98 ? 4.625  9.463  -5.453  1.00 28.99  ? 198 ASN   B O   1 
ATOM   1568 C  CB  . ASN   B 1 98 ? 4.796  6.456  -4.912  1.00 26.94  ? 198 ASN   B CB  1 
ATOM   1569 C  CG  . ASN   B 1 98 ? 5.344  5.207  -4.261  1.00 35.03  ? 198 ASN   B CG  1 
ATOM   1570 O  OD1 . ASN   B 1 98 ? 5.799  5.230  -3.127  1.00 40.14  ? 198 ASN   B OD1 1 
ATOM   1571 N  ND2 . ASN   B 1 98 ? 5.336  4.117  -4.999  1.00 45.20  ? 198 ASN   B ND2 1 
ATOM   1572 N  N   . PHE   B 1 99 ? 5.499  8.625  -7.360  1.00 25.72  ? 199 PHE   B N   1 
ATOM   1573 C  CA  . PHE   B 1 99 ? 4.784  9.553  -8.228  1.00 29.83  ? 199 PHE   B CA  1 
ATOM   1574 C  C   . PHE   B 1 99 ? 4.703  8.985  -9.644  1.00 44.80  ? 199 PHE   B C   1 
ATOM   1575 O  O   . PHE   B 1 99 ? 4.218  9.638  -10.565 1.00 37.41  ? 199 PHE   B O   1 
ATOM   1576 C  CB  . PHE   B 1 99 ? 5.442  10.949 -8.224  1.00 29.62  ? 199 PHE   B CB  1 
ATOM   1577 C  CG  . PHE   B 1 99 ? 6.884  10.976 -8.708  1.00 32.35  ? 199 PHE   B CG  1 
ATOM   1578 C  CD1 . PHE   B 1 99 ? 7.939  10.752 -7.825  1.00 33.65  ? 199 PHE   B CD1 1 
ATOM   1579 C  CD2 . PHE   B 1 99 ? 7.187  11.254 -10.028 1.00 33.90  ? 199 PHE   B CD2 1 
ATOM   1580 C  CE1 . PHE   B 1 99 ? 9.259  10.781 -8.262  1.00 35.90  ? 199 PHE   B CE1 1 
ATOM   1581 C  CE2 . PHE   B 1 99 ? 8.512  11.284 -10.474 1.00 41.42  ? 199 PHE   B CE2 1 
ATOM   1582 C  CZ  . PHE   B 1 99 ? 9.549  11.055 -9.586  1.00 47.32  ? 199 PHE   B CZ  1 
ATOM   1583 O  OXT . PHE   B 1 99 ? 5.115  7.854  -9.887  1.00 37.50  ? 199 PHE   B OXT 1 
HETATM 1584 C  C2  . A1BHV C 2 .  ? 14.729 22.710 5.506   1.00 43.35  ? 401 A1BHV B C2  1 
HETATM 1585 C  C4  . A1BHV C 2 .  ? 15.363 20.378 6.075   1.00 28.72  ? 401 A1BHV B C4  1 
HETATM 1586 C  C5  . A1BHV C 2 .  ? 15.742 19.297 5.023   1.00 25.30  ? 401 A1BHV B C5  1 
HETATM 1587 C  C9  . A1BHV C 2 .  ? 14.734 19.787 7.354   1.00 29.46  ? 401 A1BHV B C9  1 
HETATM 1588 C  C12 . A1BHV C 2 .  ? 19.150 18.637 4.503   1.00 31.31  ? 401 A1BHV B C12 1 
HETATM 1589 C  C13 . A1BHV C 2 .  ? 18.978 19.263 3.104   1.00 38.42  ? 401 A1BHV B C13 1 
HETATM 1590 C  C14 . A1BHV C 2 .  ? 18.880 20.788 3.259   1.00 37.22  ? 401 A1BHV B C14 1 
HETATM 1591 O  O16 . A1BHV C 2 .  ? 19.773 20.531 6.947   1.00 33.53  ? 401 A1BHV B O16 1 
HETATM 1592 C  C18 . A1BHV C 2 .  ? 19.856 17.918 7.398   1.00 28.40  ? 401 A1BHV B C18 1 
HETATM 1593 C  C21 . A1BHV C 2 .  ? 21.390 15.659 7.908   1.00 31.11  ? 401 A1BHV B C21 1 
HETATM 1594 C  C22 . A1BHV C 2 .  ? 21.987 16.782 7.303   1.00 24.66  ? 401 A1BHV B C22 1 
HETATM 1595 C  C23 . A1BHV C 2 .  ? 21.214 17.916 7.048   1.00 28.24  ? 401 A1BHV B C23 1 
HETATM 1596 C  C25 . A1BHV C 2 .  ? 14.313 20.878 8.309   1.00 29.10  ? 401 A1BHV B C25 1 
HETATM 1597 C  C26 . A1BHV C 2 .  ? 12.988 21.337 8.347   1.00 29.22  ? 401 A1BHV B C26 1 
HETATM 1598 C  C15 . A1BHV C 2 .  ? 20.116 18.882 2.150   1.00 31.74  ? 401 A1BHV B C15 1 
HETATM 1599 C  C19 . A1BHV C 2 .  ? 19.260 16.804 8.008   1.00 27.49  ? 401 A1BHV B C19 1 
HETATM 1600 C  C20 . A1BHV C 2 .  ? 20.029 15.675 8.258   1.00 29.30  ? 401 A1BHV B C20 1 
HETATM 1601 C  C27 . A1BHV C 2 .  ? 12.612 22.358 9.225   1.00 67.78  ? 401 A1BHV B C27 1 
HETATM 1602 C  C28 . A1BHV C 2 .  ? 13.557 22.939 10.075  1.00 62.29  ? 401 A1BHV B C28 1 
HETATM 1603 C  C29 . A1BHV C 2 .  ? 14.882 22.492 10.044  1.00 46.64  ? 401 A1BHV B C29 1 
HETATM 1604 C  C30 . A1BHV C 2 .  ? 15.256 21.475 9.163   1.00 39.34  ? 401 A1BHV B C30 1 
HETATM 1605 C  C31 . A1BHV C 2 .  ? 23.430 14.403 7.794   1.00 34.22  ? 401 A1BHV B C31 1 
HETATM 1606 C  C32 . A1BHV C 2 .  ? 13.430 24.766 5.708   1.00 40.95  ? 401 A1BHV B C32 1 
HETATM 1607 C  C33 . A1BHV C 2 .  ? 12.103 24.924 6.468   1.00 43.99  ? 401 A1BHV B C33 1 
HETATM 1608 C  C34 . A1BHV C 2 .  ? 11.594 26.376 6.470   1.00 37.93  ? 401 A1BHV B C34 1 
HETATM 1609 C  C35 . A1BHV C 2 .  ? 11.714 26.902 5.037   1.00 76.30  ? 401 A1BHV B C35 1 
HETATM 1610 C  C36 . A1BHV C 2 .  ? 11.153 25.863 3.988   1.00 52.76  ? 401 A1BHV B C36 1 
HETATM 1611 C  C37 . A1BHV C 2 .  ? 12.440 25.346 3.346   1.00 32.40  ? 401 A1BHV B C37 1 
HETATM 1612 C  C38 . A1BHV C 2 .  ? 13.513 25.682 4.419   1.00 57.46  ? 401 A1BHV B C38 1 
HETATM 1613 C  C39 . A1BHV C 2 .  ? 13.096 25.657 2.009   1.00 43.20  ? 401 A1BHV B C39 1 
HETATM 1614 C  C41 . A1BHV C 2 .  ? 14.812 25.427 3.663   1.00 50.71  ? 401 A1BHV B C41 1 
HETATM 1615 C  C43 . A1BHV C 2 .  ? 16.037 26.087 4.274   1.00 66.88  ? 401 A1BHV B C43 1 
HETATM 1616 C  C6  . A1BHV C 2 .  ? 16.872 18.431 5.576   1.00 30.40  ? 401 A1BHV B C6  1 
HETATM 1617 N  N3  . A1BHV C 2 .  ? 14.503 21.387 5.466   1.00 27.74  ? 401 A1BHV B N3  1 
HETATM 1618 N  N7  . A1BHV C 2 .  ? 18.188 19.122 5.529   1.00 30.25  ? 401 A1BHV B N7  1 
HETATM 1619 O  O1  . A1BHV C 2 .  ? 13.538 23.366 5.350   1.00 49.04  ? 401 A1BHV B O1  1 
HETATM 1620 O  O10 . A1BHV C 2 .  ? 14.615 18.458 4.753   1.00 29.88  ? 401 A1BHV B O10 1 
HETATM 1621 O  O17 . A1BHV C 2 .  ? 17.826 19.443 8.124   1.00 29.41  ? 401 A1BHV B O17 1 
HETATM 1622 O  O24 . A1BHV C 2 .  ? 22.055 14.509 8.193   1.00 34.23  ? 401 A1BHV B O24 1 
HETATM 1623 O  O40 . A1BHV C 2 .  ? 14.480 25.978 2.356   1.00 62.80  ? 401 A1BHV B O40 1 
HETATM 1624 O  O42 . A1BHV C 2 .  ? 13.157 27.028 4.769   1.00 44.60  ? 401 A1BHV B O42 1 
HETATM 1625 O  O8  . A1BHV C 2 .  ? 15.835 23.243 5.647   1.00 29.84  ? 401 A1BHV B O8  1 
HETATM 1626 S  S11 . A1BHV C 2 .  ? 18.871 19.367 7.077   1.00 28.50  ? 401 A1BHV B S11 1 
HETATM 1627 CL CL  . CL    D 3 .  ? 22.004 4.090  10.896  1.00 33.30  ? 402 CL    B CL  1 
HETATM 1628 O  O   . HOH   E 4 .  ? 19.931 25.303 14.457  1.00 46.66  ? 101 HOH   A O   1 
HETATM 1629 O  O   . HOH   E 4 .  ? 16.536 38.358 -11.557 1.00 44.13  ? 102 HOH   A O   1 
HETATM 1630 O  O   . HOH   E 4 .  ? 12.239 27.380 -16.828 1.00 34.39  ? 103 HOH   A O   1 
HETATM 1631 O  O   . HOH   E 4 .  ? 15.138 38.459 -13.706 1.00 51.08  ? 104 HOH   A O   1 
HETATM 1632 O  O   . HOH   E 4 .  ? 7.857  24.059 -21.287 1.00 67.34  ? 105 HOH   A O   1 
HETATM 1633 O  O   . HOH   E 4 .  ? 16.871 7.177  -3.622  1.00 35.91  ? 106 HOH   A O   1 
HETATM 1634 O  O   . HOH   E 4 .  ? 13.526 16.354 -16.243 1.00 39.76  ? 107 HOH   A O   1 
HETATM 1635 O  O   . HOH   E 4 .  ? 1.088  14.938 -2.317  1.00 31.55  ? 108 HOH   A O   1 
HETATM 1636 O  O   . HOH   E 4 .  ? 23.718 15.274 -3.249  1.00 48.54  ? 109 HOH   A O   1 
HETATM 1637 O  O   . HOH   E 4 .  ? 21.293 8.828  -5.662  1.00 44.50  ? 110 HOH   A O   1 
HETATM 1638 O  O   . HOH   E 4 .  ? 4.603  24.209 0.460   1.00 36.25  ? 111 HOH   A O   1 
HETATM 1639 O  O   . HOH   E 4 .  ? 7.824  19.660 4.777   1.00 23.75  ? 112 HOH   A O   1 
HETATM 1640 O  O   . HOH   E 4 .  ? 8.520  36.239 -10.279 1.00 39.29  ? 113 HOH   A O   1 
HETATM 1641 O  O   . HOH   E 4 .  ? 1.433  27.906 -11.214 1.00 30.73  ? 114 HOH   A O   1 
HETATM 1642 O  O   . HOH   E 4 .  ? 9.405  27.488 -3.456  1.00 26.15  ? 115 HOH   A O   1 
HETATM 1643 O  O   . HOH   E 4 .  ? -1.427 16.108 -6.554  1.00 52.80  ? 116 HOH   A O   1 
HETATM 1644 O  O   . HOH   E 4 .  ? 2.902  17.402 -13.370 1.00 53.02  ? 117 HOH   A O   1 
HETATM 1645 O  O   . HOH   E 4 .  ? 8.422  36.443 0.088   1.00 55.11  ? 118 HOH   A O   1 
HETATM 1646 O  O   . HOH   E 4 .  ? 9.175  21.391 6.573   1.00 34.08  ? 119 HOH   A O   1 
HETATM 1647 O  O   . HOH   E 4 .  ? 25.487 27.196 -3.719  1.00 44.04  ? 120 HOH   A O   1 
HETATM 1648 O  O   . HOH   E 4 .  ? 21.934 19.515 -6.405  1.00 32.02  ? 121 HOH   A O   1 
HETATM 1649 O  O   . HOH   E 4 .  ? 10.693 36.157 4.740   1.00 44.17  ? 122 HOH   A O   1 
HETATM 1650 O  O   . HOH   E 4 .  ? 0.906  22.747 -2.907  1.00 47.75  ? 123 HOH   A O   1 
HETATM 1651 O  O   . HOH   E 4 .  ? 4.231  30.614 -8.421  1.00 36.08  ? 124 HOH   A O   1 
HETATM 1652 O  O   . HOH   E 4 .  ? 13.727 24.904 -19.479 1.00 50.18  ? 125 HOH   A O   1 
HETATM 1653 O  O   . HOH   E 4 .  ? 1.430  9.083  -5.529  1.00 37.51  ? 126 HOH   A O   1 
HETATM 1654 O  O   . HOH   E 4 .  ? 18.714 23.284 -23.672 1.00 55.23  ? 127 HOH   A O   1 
HETATM 1655 O  O   . HOH   E 4 .  ? 2.400  24.723 -5.937  1.00 40.22  ? 128 HOH   A O   1 
HETATM 1656 O  O   . HOH   E 4 .  ? 20.251 34.885 -3.256  1.00 47.91  ? 129 HOH   A O   1 
HETATM 1657 O  O   . HOH   E 4 .  ? 8.950  42.364 -6.847  1.00 42.43  ? 130 HOH   A O   1 
HETATM 1658 O  O   . HOH   E 4 .  ? 8.162  37.065 -7.196  1.00 48.73  ? 131 HOH   A O   1 
HETATM 1659 O  O   . HOH   E 4 .  ? 4.446  30.834 -16.274 1.00 42.96  ? 132 HOH   A O   1 
HETATM 1660 O  O   . HOH   E 4 .  ? 22.127 21.509 -19.714 1.00 44.20  ? 133 HOH   A O   1 
HETATM 1661 O  O   . HOH   E 4 .  ? 24.739 29.354 -5.436  1.00 41.57  ? 134 HOH   A O   1 
HETATM 1662 O  O   . HOH   E 4 .  ? 23.332 20.168 -10.659 1.00 34.04  ? 135 HOH   A O   1 
HETATM 1663 O  O   . HOH   E 4 .  ? 21.996 35.208 3.422   1.00 51.31  ? 136 HOH   A O   1 
HETATM 1664 O  O   . HOH   E 4 .  ? 3.969  16.408 -17.147 1.00 53.40  ? 137 HOH   A O   1 
HETATM 1665 O  O   . HOH   E 4 .  ? 9.709  30.078 -16.521 1.00 36.94  ? 138 HOH   A O   1 
HETATM 1666 O  O   . HOH   E 4 .  ? 23.480 8.622  -1.870  1.00 37.72  ? 139 HOH   A O   1 
HETATM 1667 O  O   . HOH   E 4 .  ? 17.702 3.764  -3.174  1.00 33.23  ? 140 HOH   A O   1 
HETATM 1668 O  O   . HOH   E 4 .  ? 15.349 11.938 -13.312 1.00 33.75  ? 141 HOH   A O   1 
HETATM 1669 O  O   . HOH   E 4 .  ? 7.554  39.226 -12.900 1.00 51.74  ? 142 HOH   A O   1 
HETATM 1670 O  O   . HOH   E 4 .  ? 4.295  26.985 -5.864  1.00 20.82  ? 143 HOH   A O   1 
HETATM 1671 O  O   . HOH   E 4 .  ? 13.517 -1.848 0.089   1.00 26.55  ? 144 HOH   A O   1 
HETATM 1672 O  O   . HOH   E 4 .  ? 18.828 8.625  -7.433  1.00 51.42  ? 145 HOH   A O   1 
HETATM 1673 O  O   . HOH   E 4 .  ? 14.561 3.399  -6.295  1.00 43.76  ? 146 HOH   A O   1 
HETATM 1674 O  O   . HOH   E 4 .  ? 25.654 28.753 -8.491  1.00 55.42  ? 147 HOH   A O   1 
HETATM 1675 O  O   . HOH   E 4 .  ? 8.417  44.755 -5.487  1.00 50.00  ? 148 HOH   A O   1 
HETATM 1676 O  O   . HOH   E 4 .  ? 23.306 16.940 -5.604  1.00 52.12  ? 149 HOH   A O   1 
HETATM 1677 O  O   . HOH   E 4 .  ? 2.301  22.316 -0.474  1.00 48.66  ? 150 HOH   A O   1 
HETATM 1678 O  O   . HOH   E 4 .  ? 17.103 7.226  -6.147  1.00 45.62  ? 151 HOH   A O   1 
HETATM 1679 O  O   . HOH   E 4 .  ? 23.931 35.524 -1.860  1.00 62.25  ? 152 HOH   A O   1 
HETATM 1680 O  O   . HOH   E 4 .  ? 14.891 -1.771 -2.825  1.00 48.63  ? 153 HOH   A O   1 
HETATM 1681 O  O   . HOH   E 4 .  ? 2.769  14.942 -13.447 1.00 44.98  ? 154 HOH   A O   1 
HETATM 1682 O  O   . HOH   E 4 .  ? 2.378  25.373 -2.266  1.00 55.82  ? 155 HOH   A O   1 
HETATM 1683 O  O   . HOH   E 4 .  ? 13.732 9.619  -12.004 1.00 59.06  ? 156 HOH   A O   1 
HETATM 1684 O  O   . HOH   F 4 .  ? 29.492 9.120  11.246  1.00 53.66  ? 501 HOH   B O   1 
HETATM 1685 O  O   . HOH   F 4 .  ? 25.238 9.292  27.284  1.00 50.90  ? 502 HOH   B O   1 
HETATM 1686 O  O   . HOH   F 4 .  ? 14.677 4.505  22.477  1.00 40.36  ? 503 HOH   B O   1 
HETATM 1687 O  O   . HOH   F 4 .  ? 1.716  15.198 5.049   1.00 39.60  ? 504 HOH   B O   1 
HETATM 1688 O  O   . HOH   F 4 .  ? 18.642 22.842 6.628   1.00 30.54  ? 505 HOH   B O   1 
HETATM 1689 O  O   . HOH   F 4 .  ? 23.689 2.532  14.754  1.00 43.13  ? 506 HOH   B O   1 
HETATM 1690 O  O   . HOH   F 4 .  ? 25.165 12.865 1.529   1.00 55.16  ? 507 HOH   B O   1 
HETATM 1691 O  O   . HOH   F 4 .  ? 13.239 2.893  1.267   1.00 26.01  ? 508 HOH   B O   1 
HETATM 1692 O  O   . HOH   F 4 .  ? 15.787 -1.693 11.828  1.00 35.13  ? 509 HOH   B O   1 
HETATM 1693 O  O   . HOH   F 4 .  ? 21.398 7.444  5.259   1.00 34.67  ? 510 HOH   B O   1 
HETATM 1694 O  O   . HOH   F 4 .  ? 18.743 12.459 1.400   1.00 22.47  ? 511 HOH   B O   1 
HETATM 1695 O  O   . HOH   F 4 .  ? 21.453 9.553  12.110  1.00 33.20  ? 512 HOH   B O   1 
HETATM 1696 O  O   . HOH   F 4 .  ? 23.749 7.587  7.128   1.00 61.93  ? 513 HOH   B O   1 
HETATM 1697 O  O   . HOH   F 4 .  ? 19.614 3.069  5.472   1.00 30.79  ? 514 HOH   B O   1 
HETATM 1698 O  O   . HOH   F 4 .  ? -1.306 16.264 3.481   1.00 40.37  ? 515 HOH   B O   1 
HETATM 1699 O  O   . HOH   F 4 .  ? 6.567  1.570  0.442   1.00 34.54  ? 516 HOH   B O   1 
HETATM 1700 O  O   . HOH   F 4 .  ? 1.827  8.748  13.859  1.00 48.94  ? 517 HOH   B O   1 
HETATM 1701 O  O   . HOH   F 4 .  ? 20.504 14.512 1.550   1.00 40.76  ? 518 HOH   B O   1 
HETATM 1702 O  O   . HOH   F 4 .  ? 1.119  18.428 9.511   1.00 49.02  ? 519 HOH   B O   1 
HETATM 1703 O  O   . HOH   F 4 .  ? -2.277 12.310 3.751   1.00 50.19  ? 520 HOH   B O   1 
HETATM 1704 O  O   . HOH   F 4 .  ? 17.551 2.352  22.369  1.00 47.68  ? 521 HOH   B O   1 
HETATM 1705 O  O   . HOH   F 4 .  ? -3.733 9.561  1.816   1.00 54.28  ? 522 HOH   B O   1 
HETATM 1706 O  O   . HOH   F 4 .  ? 10.316 25.387 10.321  1.00 52.41  ? 523 HOH   B O   1 
HETATM 1707 O  O   . HOH   F 4 .  ? 13.022 0.372  2.304   1.00 29.76  ? 524 HOH   B O   1 
HETATM 1708 O  O   . HOH   F 4 .  ? 21.072 15.389 4.461   1.00 31.74  ? 525 HOH   B O   1 
HETATM 1709 O  O   . HOH   F 4 .  ? 0.349  12.024 11.896  1.00 56.92  ? 526 HOH   B O   1 
HETATM 1710 O  O   . HOH   F 4 .  ? 28.633 6.875  18.774  1.00 46.50  ? 527 HOH   B O   1 
HETATM 1711 O  O   . HOH   F 4 .  ? -3.405 5.759  3.764   1.00 49.08  ? 528 HOH   B O   1 
HETATM 1712 O  O   . HOH   F 4 .  ? 9.364  18.329 15.810  1.00 33.04  ? 529 HOH   B O   1 
HETATM 1713 O  O   . HOH   F 4 .  ? 4.881  5.846  17.252  1.00 43.16  ? 530 HOH   B O   1 
HETATM 1714 O  O   . HOH   F 4 .  ? 22.996 6.847  1.883   1.00 42.15  ? 531 HOH   B O   1 
HETATM 1715 O  O   . HOH   F 4 .  ? 12.973 -2.558 11.325  1.00 40.38  ? 532 HOH   B O   1 
HETATM 1716 O  O   . HOH   F 4 .  ? 26.128 24.154 17.244  1.00 36.49  ? 533 HOH   B O   1 
HETATM 1717 O  O   . HOH   F 4 .  ? 7.684  16.984 19.928  1.00 45.81  ? 534 HOH   B O   1 
HETATM 1718 O  O   . HOH   F 4 .  ? 6.568  21.563 12.116  1.00 46.12  ? 535 HOH   B O   1 
HETATM 1719 O  O   . HOH   F 4 .  ? 25.472 22.474 19.640  1.00 50.03  ? 536 HOH   B O   1 
HETATM 1720 O  O   . HOH   F 4 .  ? 26.125 12.338 5.180   1.00 51.88  ? 537 HOH   B O   1 
HETATM 1721 O  O   . HOH   F 4 .  ? 1.066  3.991  11.117  1.00 67.59  ? 538 HOH   B O   1 
HETATM 1722 O  O   . HOH   F 4 .  ? 28.724 27.128 9.615   1.00 42.84  ? 539 HOH   B O   1 
HETATM 1723 O  O   . HOH   F 4 .  ? 26.429 17.253 6.789   1.00 42.51  ? 540 HOH   B O   1 
HETATM 1724 O  O   . HOH   F 4 .  ? 11.444 4.092  23.784  1.00 53.95  ? 541 HOH   B O   1 
HETATM 1725 O  O   . HOH   F 4 .  ? 15.503 14.253 28.294  1.00 36.55  ? 542 HOH   B O   1 
HETATM 1726 O  O   . HOH   F 4 .  ? 23.793 6.440  9.849   1.00 54.19  ? 543 HOH   B O   1 
HETATM 1727 O  O   . HOH   F 4 .  ? 17.225 21.567 21.289  1.00 41.20  ? 544 HOH   B O   1 
HETATM 1728 O  O   . HOH   F 4 .  ? 1.966  22.035 7.655   1.00 38.26  ? 545 HOH   B O   1 
HETATM 1729 O  O   . HOH   F 4 .  ? 20.101 5.390  4.155   1.00 41.21  ? 546 HOH   B O   1 
HETATM 1730 O  O   . HOH   F 4 .  ? 25.364 30.911 10.717  1.00 61.82  ? 547 HOH   B O   1 
HETATM 1731 O  O   . HOH   F 4 .  ? 14.764 12.283 30.541  1.00 58.97  ? 548 HOH   B O   1 
HETATM 1732 O  O   . HOH   F 4 .  ? 0.644  14.325 7.356   1.00 46.61  ? 549 HOH   B O   1 
HETATM 1733 O  O   . HOH   F 4 .  ? 28.526 24.934 17.004  1.00 61.67  ? 550 HOH   B O   1 
HETATM 1734 O  O   . HOH   F 4 .  ? 31.039 13.699 9.423   1.00 62.42  ? 551 HOH   B O   1 
HETATM 1735 O  O   . HOH   F 4 .  ? 28.090 12.557 3.803   1.00 75.23  ? 552 HOH   B O   1 
HETATM 1736 O  O   . HOH   F 4 .  ? 27.793 10.853 2.222   1.00 68.79  ? 553 HOH   B O   1 
HETATM 1737 O  O   . HOH   F 4 .  ? 0.759  8.100  11.126  1.00 65.79  ? 554 HOH   B O   1 
# 
