data_9HS7
# 
_entry.id   9HS7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9HS7         pdb_00009hs7 10.2210/pdb9hs7/pdb 
WWPDB D_1292144139 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HS7 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              conejero@ugr.es 
_pdbx_contact_author.name_first         Francisco 
_pdbx_contact_author.name_last          Conejero-Lara 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8282-2168 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Camara-Artigas, A.'   1 0000-0003-2197-726X 
'Gavira, J.A.'         2 0000-0002-7386-6484 
'Conejero-Lara, F.'    3 0000-0002-8282-2168 
'Polo-Megias, D.'      4 0000-0002-4019-5506 
'Salinas-Garcia, M.C.' 5 0000-0001-9730-3590 
# 
_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            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            310 
_citation.language                  ? 
_citation.page_first                143157 
_citation.page_last                 143157 
_citation.title                     'Potent HIV-1 miniprotein inhibitors targeting highly conserved gp41 epitopes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2025.143157 
_citation.pdbx_database_id_PubMed   40239787 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Polo-Megias, D.'      1  ? 
primary 'Cano-Munoz, M.'       2  ? 
primary 'Gantner, P.'          3  ? 
primary 'Laumond, G.'          4  ? 
primary 'Decoville, T.'        5  ? 
primary 'Grezzani, J.'         6  ? 
primary 'La Rocchia, I.'       7  ? 
primary 'Salinas-Garcia, M.C.' 8  ? 
primary 'Camara-Artigas, A.'   9  ? 
primary 'Gavira, J.A.'         10 ? 
primary 'Conejero-Lara, F.'    11 ? 
primary 'Moog, C.'             12 ? 
# 
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 'Transmembrane protein gp41' 15447.771 1  ? ? ? ? 
2 non-polymer syn 'DI(HYDROXYETHYL)ETHER'      106.120   1  ? ? ? ? 
3 water       nat water                        18.015    35 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'TM,Glycoprotein 41,gp41' 
# 
_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       
;MTCGAASMTKTVQARQKLSGIVQKQNNLLRKIEAIQHLLQRGLICGPQLLHQIAEIERELNNQEQEIGSLKQRAQVEKTM
SAASGCGMGPASMTLDVQARQLLSGIDQQQNNLKRAIEAIKHLLQLTCWGGGGSHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTCGAASMTKTVQARQKLSGIVQKQNNLLRKIEAIQHLLQRGLICGPQLLHQIAEIERELNNQEQEIGSLKQRAQVEKTM
SAASGCGMGPASMTLDVQARQLLSGIDQQQNNLKRAIEAIKHLLQLTCWGGGGSHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DI(HYDROXYETHYL)ETHER' PEG 
3 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   CYS n 
1 4   GLY n 
1 5   ALA n 
1 6   ALA n 
1 7   SER n 
1 8   MET n 
1 9   THR n 
1 10  LYS n 
1 11  THR n 
1 12  VAL n 
1 13  GLN n 
1 14  ALA n 
1 15  ARG n 
1 16  GLN n 
1 17  LYS n 
1 18  LEU n 
1 19  SER n 
1 20  GLY n 
1 21  ILE n 
1 22  VAL n 
1 23  GLN n 
1 24  LYS n 
1 25  GLN n 
1 26  ASN n 
1 27  ASN n 
1 28  LEU n 
1 29  LEU n 
1 30  ARG n 
1 31  LYS n 
1 32  ILE n 
1 33  GLU n 
1 34  ALA n 
1 35  ILE n 
1 36  GLN n 
1 37  HIS n 
1 38  LEU n 
1 39  LEU n 
1 40  GLN n 
1 41  ARG n 
1 42  GLY n 
1 43  LEU n 
1 44  ILE n 
1 45  CYS n 
1 46  GLY n 
1 47  PRO n 
1 48  GLN n 
1 49  LEU n 
1 50  LEU n 
1 51  HIS n 
1 52  GLN n 
1 53  ILE n 
1 54  ALA n 
1 55  GLU n 
1 56  ILE n 
1 57  GLU n 
1 58  ARG n 
1 59  GLU n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLN n 
1 64  GLU n 
1 65  GLN n 
1 66  GLU n 
1 67  ILE n 
1 68  GLY n 
1 69  SER n 
1 70  LEU n 
1 71  LYS n 
1 72  GLN n 
1 73  ARG n 
1 74  ALA n 
1 75  GLN n 
1 76  VAL n 
1 77  GLU n 
1 78  LYS n 
1 79  THR n 
1 80  MET n 
1 81  SER n 
1 82  ALA n 
1 83  ALA n 
1 84  SER n 
1 85  GLY n 
1 86  CYS n 
1 87  GLY n 
1 88  MET n 
1 89  GLY n 
1 90  PRO n 
1 91  ALA n 
1 92  SER n 
1 93  MET n 
1 94  THR n 
1 95  LEU n 
1 96  ASP n 
1 97  VAL n 
1 98  GLN n 
1 99  ALA n 
1 100 ARG n 
1 101 GLN n 
1 102 LEU n 
1 103 LEU n 
1 104 SER n 
1 105 GLY n 
1 106 ILE n 
1 107 ASP n 
1 108 GLN n 
1 109 GLN n 
1 110 GLN n 
1 111 ASN n 
1 112 ASN n 
1 113 LEU n 
1 114 LYS n 
1 115 ARG n 
1 116 ALA n 
1 117 ILE n 
1 118 GLU n 
1 119 ALA n 
1 120 ILE n 
1 121 LYS n 
1 122 HIS n 
1 123 LEU n 
1 124 LEU n 
1 125 GLN n 
1 126 LEU n 
1 127 THR n 
1 128 CYS n 
1 129 TRP n 
1 130 GLY n 
1 131 GLY n 
1 132 GLY n 
1 133 GLY n 
1 134 SER n 
1 135 HIS n 
1 136 HIS n 
1 137 HIS n 
1 138 HIS n 
1 139 HIS n 
1 140 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1  40  ? ? env ? ? ? ? ? ? 'Human immunodeficiency virus type 1 (BRU ISOLATE)' 11686 ? ? ? ? ? ? 
? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 41 140 ? ? env ? ? ? ? ? ? 'Human immunodeficiency virus type 1 (BRU ISOLATE)' 11686 ? ? ? ? ? ? 
? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                 ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE               ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                 ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE               ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ? 'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'      106.120 
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 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   CYS 3   3   3   CYS CYS A . n 
A 1 4   GLY 4   4   4   GLY GLY A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   MET 8   8   8   MET MET A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  ARG 15  15  15  ARG ARG A . n 
A 1 16  GLN 16  16  16  GLN GLN A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  GLN 23  23  23  GLN GLN A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  GLN 36  36  36  GLN GLN A . n 
A 1 37  HIS 37  37  37  HIS HIS A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  GLN 40  40  40  GLN GLN A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  CYS 45  45  45  CYS CYS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  GLN 52  52  52  GLN GLN A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  MET 80  80  80  MET MET A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  CYS 86  86  86  CYS CYS A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  MET 88  88  88  MET MET A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  MET 93  93  93  MET MET A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 GLN 101 101 101 GLN GLN A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 ASP 107 107 107 ASP ASP A . n 
A 1 108 GLN 108 108 108 GLN GLN A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 ILE 120 120 120 ILE ILE A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 TRP 129 129 ?   ?   ?   A . n 
A 1 130 GLY 130 130 ?   ?   ?   A . n 
A 1 131 GLY 131 131 ?   ?   ?   A . n 
A 1 132 GLY 132 132 ?   ?   ?   A . n 
A 1 133 GLY 133 133 ?   ?   ?   A . n 
A 1 134 SER 134 134 ?   ?   ?   A . n 
A 1 135 HIS 135 135 ?   ?   ?   A . n 
A 1 136 HIS 136 136 ?   ?   ?   A . n 
A 1 137 HIS 137 137 ?   ?   ?   A . n 
A 1 138 HIS 138 138 ?   ?   ?   A . n 
A 1 139 HIS 139 139 ?   ?   ?   A . n 
A 1 140 HIS 140 140 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 PEG 1  201 201 PEG PEG A . 
C 3 HOH 1  301 2   HOH HOH A . 
C 3 HOH 2  302 17  HOH HOH A . 
C 3 HOH 3  303 34  HOH HOH A . 
C 3 HOH 4  304 13  HOH HOH A . 
C 3 HOH 5  305 14  HOH HOH A . 
C 3 HOH 6  306 26  HOH HOH A . 
C 3 HOH 7  307 7   HOH HOH A . 
C 3 HOH 8  308 1   HOH HOH A . 
C 3 HOH 9  309 3   HOH HOH A . 
C 3 HOH 10 310 12  HOH HOH A . 
C 3 HOH 11 311 5   HOH HOH A . 
C 3 HOH 12 312 35  HOH HOH A . 
C 3 HOH 13 313 6   HOH HOH A . 
C 3 HOH 14 314 11  HOH HOH A . 
C 3 HOH 15 315 18  HOH HOH A . 
C 3 HOH 16 316 10  HOH HOH A . 
C 3 HOH 17 317 15  HOH HOH A . 
C 3 HOH 18 318 29  HOH HOH A . 
C 3 HOH 19 319 9   HOH HOH A . 
C 3 HOH 20 320 24  HOH HOH A . 
C 3 HOH 21 321 8   HOH HOH A . 
C 3 HOH 22 322 28  HOH HOH A . 
C 3 HOH 23 323 27  HOH HOH A . 
C 3 HOH 24 324 4   HOH HOH A . 
C 3 HOH 25 325 19  HOH HOH A . 
C 3 HOH 26 326 31  HOH HOH A . 
C 3 HOH 27 327 20  HOH HOH A . 
C 3 HOH 28 328 25  HOH HOH A . 
C 3 HOH 29 329 21  HOH HOH A . 
C 3 HOH 30 330 32  HOH HOH A . 
C 3 HOH 31 331 16  HOH HOH A . 
C 3 HOH 32 332 30  HOH HOH A . 
C 3 HOH 33 333 33  HOH HOH A . 
C 3 HOH 34 334 23  HOH HOH A . 
C 3 HOH 35 335 22  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HS7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.435 
_cell.length_a_esd                 ? 
_cell.length_b                     65.435 
_cell.length_b_esd                 ? 
_cell.length_c                     88.769 
_cell.length_c_esd                 ? 
_cell.volume                       329163.880 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9HS7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
_symmetry.space_group_name_Hall            'P 65' 
_symmetry.space_group_name_H-M             'P 65' 
_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                   9HS7 
_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             3.55 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          66.20 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M sodium phosphate monobasic monohydrate, 0.1M potassium phosphate monobasic, 2M NaCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-12-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979260 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979260 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          25.17 
_reflns.entry_id                                       9HS7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.698 
_reflns.d_resolution_low                               19.290 
_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                                     11436 
_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                           94.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.9 
_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                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.075 
_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                                    1.698 
_reflns_shell.d_res_low                                     1.908 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             572 
_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                               10.0 
_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                               0.330 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.752 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          86.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.991 
_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                               52.62 
_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                                 9HS7 
_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                            1.698 
_refine.ls_d_res_low                             19.29 
_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                     11432 
_refine.ls_number_reflns_R_free                  551 
_refine.ls_number_reflns_R_work                  10881 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.9 
_refine.ls_percent_reflns_R_free                 4.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2027 
_refine.ls_R_factor_R_free                       0.2391 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2008 
_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                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 36.0149 
_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                            0.1752 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.698 
_refine_hist.d_res_low                        19.29 
_refine_hist.number_atoms_solvent             35 
_refine_hist.number_atoms_total               1006 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        964 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         7 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0139  ? 996  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.4013  ? 1333 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0605  ? 155  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0209  ? 177  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.5585 ? 399  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.70 1.87  . . 18  416  86.9  . . . . 0.2777 . . . . . . . . . . . 0.3414 
'X-RAY DIFFRACTION' 1.87 2.14  . . 54  1064 18.98 . . . . 0.2521 . . . . . . . . . . . 0.2418 
'X-RAY DIFFRACTION' 2.14 2.69  . . 188 3701 65.44 . . . . 0.2651 . . . . . . . . . . . 0.2962 
'X-RAY DIFFRACTION' 2.69 19.29 . . 291 5700 99.95 . . . . 0.1784 . . . . . . . . . . . 0.2219 
# 
_struct.entry_id                     9HS7 
_struct.title                        
'Anti-HIV-1 chimeric miniprotein mimicking the N-terminal half of gp41 NHR with an extended region targeting the MPER' 
_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        9HS7 
_struct_keywords.text            'HEPTAD-REPEAT REGION OF GP41, ANTIVIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'ANTIVIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ENV_HV1MF P19551 ? 1 TMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQ     527 
2 UNP ENV_HV1MF P19551 ? 1 MGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWG 528 
# 
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 9HS7 A 2  ? 40  ? P19551 527 ? 565 ? 2  40  
2 2 9HS7 A 88 ? 130 ? P19551 528 ? 570 ? 88 130 
# 
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 9HS7 MET A 1   ? UNP P19551 ?   ?   'initiating methionine' 1   1  
1 9HS7 CYS A 3   ? UNP P19551 MET 528 'engineered mutation'   3   2  
1 9HS7 LYS A 10  ? UNP P19551 LEU 535 'engineered mutation'   10  3  
1 9HS7 LYS A 17  ? UNP P19551 LEU 542 'engineered mutation'   17  4  
1 9HS7 LYS A 24  ? UNP P19551 GLN 549 'engineered mutation'   24  5  
1 9HS7 LYS A 31  ? UNP P19551 ALA 556 'engineered mutation'   31  6  
1 9HS7 ILE A 35  ? UNP P19551 GLN 560 'engineered mutation'   35  7  
1 9HS7 ARG A 41  ? UNP P19551 ?   ?   linker                  41  8  
1 9HS7 GLY A 42  ? UNP P19551 ?   ?   linker                  42  9  
1 9HS7 LEU A 43  ? UNP P19551 ?   ?   linker                  43  10 
1 9HS7 ILE A 44  ? UNP P19551 ?   ?   linker                  44  11 
1 9HS7 CYS A 45  ? UNP P19551 ?   ?   linker                  45  12 
1 9HS7 GLY A 46  ? UNP P19551 ?   ?   linker                  46  13 
1 9HS7 PRO A 47  ? UNP P19551 ?   ?   linker                  47  14 
1 9HS7 GLN A 48  ? UNP P19551 ?   ?   linker                  48  15 
1 9HS7 LEU A 49  ? UNP P19551 ?   ?   linker                  49  16 
1 9HS7 LEU A 50  ? UNP P19551 ?   ?   linker                  50  17 
1 9HS7 HIS A 51  ? UNP P19551 ?   ?   linker                  51  18 
1 9HS7 GLN A 52  ? UNP P19551 ?   ?   linker                  52  19 
1 9HS7 ILE A 53  ? UNP P19551 ?   ?   linker                  53  20 
1 9HS7 ALA A 54  ? UNP P19551 ?   ?   linker                  54  21 
1 9HS7 GLU A 55  ? UNP P19551 ?   ?   linker                  55  22 
1 9HS7 ILE A 56  ? UNP P19551 ?   ?   linker                  56  23 
1 9HS7 GLU A 57  ? UNP P19551 ?   ?   linker                  57  24 
1 9HS7 ARG A 58  ? UNP P19551 ?   ?   linker                  58  25 
1 9HS7 GLU A 59  ? UNP P19551 ?   ?   linker                  59  26 
1 9HS7 LEU A 60  ? UNP P19551 ?   ?   linker                  60  27 
1 9HS7 ASN A 61  ? UNP P19551 ?   ?   linker                  61  28 
1 9HS7 ASN A 62  ? UNP P19551 ?   ?   linker                  62  29 
1 9HS7 GLN A 63  ? UNP P19551 ?   ?   linker                  63  30 
1 9HS7 GLU A 64  ? UNP P19551 ?   ?   linker                  64  31 
1 9HS7 GLN A 65  ? UNP P19551 ?   ?   linker                  65  32 
1 9HS7 GLU A 66  ? UNP P19551 ?   ?   linker                  66  33 
1 9HS7 ILE A 67  ? UNP P19551 ?   ?   linker                  67  34 
1 9HS7 GLY A 68  ? UNP P19551 ?   ?   linker                  68  35 
1 9HS7 SER A 69  ? UNP P19551 ?   ?   linker                  69  36 
1 9HS7 LEU A 70  ? UNP P19551 ?   ?   linker                  70  37 
1 9HS7 LYS A 71  ? UNP P19551 ?   ?   linker                  71  38 
1 9HS7 GLN A 72  ? UNP P19551 ?   ?   linker                  72  39 
1 9HS7 ARG A 73  ? UNP P19551 ?   ?   linker                  73  40 
1 9HS7 ALA A 74  ? UNP P19551 ?   ?   linker                  74  41 
1 9HS7 GLN A 75  ? UNP P19551 ?   ?   linker                  75  42 
1 9HS7 VAL A 76  ? UNP P19551 ?   ?   linker                  76  43 
1 9HS7 GLU A 77  ? UNP P19551 ?   ?   linker                  77  44 
1 9HS7 LYS A 78  ? UNP P19551 ?   ?   linker                  78  45 
1 9HS7 THR A 79  ? UNP P19551 ?   ?   linker                  79  46 
1 9HS7 MET A 80  ? UNP P19551 ?   ?   linker                  80  47 
1 9HS7 SER A 81  ? UNP P19551 ?   ?   linker                  81  48 
1 9HS7 ALA A 82  ? UNP P19551 ?   ?   linker                  82  49 
1 9HS7 ALA A 83  ? UNP P19551 ?   ?   linker                  83  50 
1 9HS7 SER A 84  ? UNP P19551 ?   ?   linker                  84  51 
1 9HS7 GLY A 85  ? UNP P19551 ?   ?   linker                  85  52 
1 9HS7 CYS A 86  ? UNP P19551 ?   ?   linker                  86  53 
1 9HS7 GLY A 87  ? UNP P19551 ?   ?   linker                  87  54 
2 9HS7 PRO A 90  ? UNP P19551 ALA 530 'engineered mutation'   90  55 
2 9HS7 ASP A 96  ? UNP P19551 THR 536 'engineered mutation'   96  56 
2 9HS7 ASP A 107 ? UNP P19551 VAL 547 'engineered mutation'   107 57 
2 9HS7 LYS A 114 ? UNP P19551 LEU 554 'engineered mutation'   114 58 
2 9HS7 ILE A 120 ? UNP P19551 GLN 560 'engineered mutation'   120 59 
2 9HS7 LYS A 121 ? UNP P19551 GLN 561 'engineered mutation'   121 60 
2 9HS7 CYS A 128 ? UNP P19551 VAL 568 'engineered mutation'   128 61 
2 9HS7 GLY A 131 ? UNP P19551 ?   ?   'expression tag'        131 62 
2 9HS7 GLY A 132 ? UNP P19551 ?   ?   'expression tag'        132 63 
2 9HS7 GLY A 133 ? UNP P19551 ?   ?   'expression tag'        133 64 
2 9HS7 SER A 134 ? UNP P19551 ?   ?   'expression tag'        134 65 
2 9HS7 HIS A 135 ? UNP P19551 ?   ?   'expression tag'        135 66 
2 9HS7 HIS A 136 ? UNP P19551 ?   ?   'expression tag'        136 67 
2 9HS7 HIS A 137 ? UNP P19551 ?   ?   'expression tag'        137 68 
2 9HS7 HIS A 138 ? UNP P19551 ?   ?   'expression tag'        138 69 
2 9HS7 HIS A 139 ? UNP P19551 ?   ?   'expression tag'        139 70 
2 9HS7 HIS A 140 ? UNP P19551 ?   ?   'expression tag'        140 71 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 130  ? 
1 MORE         1    ? 
1 'SSA (A^2)'  8060 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_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 SER A 7  ? GLY A 42  ? SER A 7  GLY A 42  1 ? 36 
HELX_P HELX_P2 AA2 GLY A 46 ? GLY A 85  ? GLY A 46 GLY A 85  1 ? 40 
HELX_P HELX_P3 AA3 ASP A 96 ? CYS A 128 ? ASP A 96 CYS A 128 1 ? 33 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 3  SG ? ? ? 1_555 A CYS 86  SG ? ? A CYS 3  A CYS 86  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf2 disulf ? ? A CYS 45 SG ? ? ? 1_555 A CYS 128 SG ? ? A CYS 45 A CYS 128 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 3  ? CYS A 86  ? CYS A 3  ? 1_555 CYS A 86  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 45 ? CYS A 128 ? CYS A 45 ? 1_555 CYS A 128 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_pdbx_entry_details.entry_id                   9HS7 
_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     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 CYS A 86 ? ? -144.56 -2.26   
2 1 MET A 88 ? ? -141.79 -124.56 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     41 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.140 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z         
2 x-y,x,z+5/6   
3 y,-x+y,z+1/6  
4 -y,x-y,z+2/3  
5 -x+y,-x,z+1/3 
6 -x,-y,z+1/2   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A TRP 129 ? A TRP 129 
4  1 Y 1 A GLY 130 ? A GLY 130 
5  1 Y 1 A GLY 131 ? A GLY 131 
6  1 Y 1 A GLY 132 ? A GLY 132 
7  1 Y 1 A GLY 133 ? A GLY 133 
8  1 Y 1 A SER 134 ? A SER 134 
9  1 Y 1 A HIS 135 ? A HIS 135 
10 1 Y 1 A HIS 136 ? A HIS 136 
11 1 Y 1 A HIS 137 ? A HIS 137 
12 1 Y 1 A HIS 138 ? A HIS 138 
13 1 Y 1 A HIS 139 ? A HIS 139 
14 1 Y 1 A HIS 140 ? A HIS 140 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PEG C1   C N N 250 
PEG O1   O N N 251 
PEG C2   C N N 252 
PEG O2   O N N 253 
PEG C3   C N N 254 
PEG C4   C N N 255 
PEG O4   O N N 256 
PEG H11  H N N 257 
PEG H12  H N N 258 
PEG HO1  H N N 259 
PEG H21  H N N 260 
PEG H22  H N N 261 
PEG H31  H N N 262 
PEG H32  H N N 263 
PEG H41  H N N 264 
PEG H42  H N N 265 
PEG HO4  H N N 266 
PRO N    N N N 267 
PRO CA   C N S 268 
PRO C    C N N 269 
PRO O    O N N 270 
PRO CB   C N N 271 
PRO CG   C N N 272 
PRO CD   C N N 273 
PRO OXT  O N N 274 
PRO H    H N N 275 
PRO HA   H N N 276 
PRO HB2  H N N 277 
PRO HB3  H N N 278 
PRO HG2  H N N 279 
PRO HG3  H N N 280 
PRO HD2  H N N 281 
PRO HD3  H N N 282 
PRO HXT  H N N 283 
SER N    N N N 284 
SER CA   C N S 285 
SER C    C N N 286 
SER O    O N N 287 
SER CB   C N N 288 
SER OG   O N N 289 
SER OXT  O N N 290 
SER H    H N N 291 
SER H2   H N N 292 
SER HA   H N N 293 
SER HB2  H N N 294 
SER HB3  H N N 295 
SER HG   H N N 296 
SER HXT  H N N 297 
THR N    N N N 298 
THR CA   C N S 299 
THR C    C N N 300 
THR O    O N N 301 
THR CB   C N R 302 
THR OG1  O N N 303 
THR CG2  C N N 304 
THR OXT  O N N 305 
THR H    H N N 306 
THR H2   H N N 307 
THR HA   H N N 308 
THR HB   H N N 309 
THR HG1  H N N 310 
THR HG21 H N N 311 
THR HG22 H N N 312 
THR HG23 H N N 313 
THR HXT  H N N 314 
TRP N    N N N 315 
TRP CA   C N S 316 
TRP C    C N N 317 
TRP O    O N N 318 
TRP CB   C N N 319 
TRP CG   C Y N 320 
TRP CD1  C Y N 321 
TRP CD2  C Y N 322 
TRP NE1  N Y N 323 
TRP CE2  C Y N 324 
TRP CE3  C Y N 325 
TRP CZ2  C Y N 326 
TRP CZ3  C Y N 327 
TRP CH2  C Y N 328 
TRP OXT  O N N 329 
TRP H    H N N 330 
TRP H2   H N N 331 
TRP HA   H N N 332 
TRP HB2  H N N 333 
TRP HB3  H N N 334 
TRP HD1  H N N 335 
TRP HE1  H N N 336 
TRP HE3  H N N 337 
TRP HZ2  H N N 338 
TRP HZ3  H N N 339 
TRP HH2  H N N 340 
TRP HXT  H N N 341 
VAL N    N N N 342 
VAL CA   C N S 343 
VAL C    C N N 344 
VAL O    O N N 345 
VAL CB   C N N 346 
VAL CG1  C N N 347 
VAL CG2  C N N 348 
VAL OXT  O N N 349 
VAL H    H N N 350 
VAL H2   H N N 351 
VAL HA   H N N 352 
VAL HB   H N N 353 
VAL HG11 H N N 354 
VAL HG12 H N N 355 
VAL HG13 H N N 356 
VAL HG21 H N N 357 
VAL HG22 H N N 358 
VAL HG23 H N N 359 
VAL HXT  H N N 360 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PEG C1  O1   sing N N 237 
PEG C1  C2   sing N N 238 
PEG C1  H11  sing N N 239 
PEG C1  H12  sing N N 240 
PEG O1  HO1  sing N N 241 
PEG C2  O2   sing N N 242 
PEG C2  H21  sing N N 243 
PEG C2  H22  sing N N 244 
PEG O2  C3   sing N N 245 
PEG C3  C4   sing N N 246 
PEG C3  H31  sing N N 247 
PEG C3  H32  sing N N 248 
PEG C4  O4   sing N N 249 
PEG C4  H41  sing N N 250 
PEG C4  H42  sing N N 251 
PEG O4  HO4  sing N N 252 
PRO N   CA   sing N N 253 
PRO N   CD   sing N N 254 
PRO N   H    sing N N 255 
PRO CA  C    sing N N 256 
PRO CA  CB   sing N N 257 
PRO CA  HA   sing N N 258 
PRO C   O    doub N N 259 
PRO C   OXT  sing N N 260 
PRO CB  CG   sing N N 261 
PRO CB  HB2  sing N N 262 
PRO CB  HB3  sing N N 263 
PRO CG  CD   sing N N 264 
PRO CG  HG2  sing N N 265 
PRO CG  HG3  sing N N 266 
PRO CD  HD2  sing N N 267 
PRO CD  HD3  sing N N 268 
PRO OXT HXT  sing N N 269 
SER N   CA   sing N N 270 
SER N   H    sing N N 271 
SER N   H2   sing N N 272 
SER CA  C    sing N N 273 
SER CA  CB   sing N N 274 
SER CA  HA   sing N N 275 
SER C   O    doub N N 276 
SER C   OXT  sing N N 277 
SER CB  OG   sing N N 278 
SER CB  HB2  sing N N 279 
SER CB  HB3  sing N N 280 
SER OG  HG   sing N N 281 
SER OXT HXT  sing N N 282 
THR N   CA   sing N N 283 
THR N   H    sing N N 284 
THR N   H2   sing N N 285 
THR CA  C    sing N N 286 
THR CA  CB   sing N N 287 
THR CA  HA   sing N N 288 
THR C   O    doub N N 289 
THR C   OXT  sing N N 290 
THR CB  OG1  sing N N 291 
THR CB  CG2  sing N N 292 
THR CB  HB   sing N N 293 
THR OG1 HG1  sing N N 294 
THR CG2 HG21 sing N N 295 
THR CG2 HG22 sing N N 296 
THR CG2 HG23 sing N N 297 
THR OXT HXT  sing N N 298 
TRP N   CA   sing N N 299 
TRP N   H    sing N N 300 
TRP N   H2   sing N N 301 
TRP CA  C    sing N N 302 
TRP CA  CB   sing N N 303 
TRP CA  HA   sing N N 304 
TRP C   O    doub N N 305 
TRP C   OXT  sing N N 306 
TRP CB  CG   sing N N 307 
TRP CB  HB2  sing N N 308 
TRP CB  HB3  sing N N 309 
TRP CG  CD1  doub Y N 310 
TRP CG  CD2  sing Y N 311 
TRP CD1 NE1  sing Y N 312 
TRP CD1 HD1  sing N N 313 
TRP CD2 CE2  doub Y N 314 
TRP CD2 CE3  sing Y N 315 
TRP NE1 CE2  sing Y N 316 
TRP NE1 HE1  sing N N 317 
TRP CE2 CZ2  sing Y N 318 
TRP CE3 CZ3  doub Y N 319 
TRP CE3 HE3  sing N N 320 
TRP CZ2 CH2  doub Y N 321 
TRP CZ2 HZ2  sing N N 322 
TRP CZ3 CH2  sing Y N 323 
TRP CZ3 HZ3  sing N N 324 
TRP CH2 HH2  sing N N 325 
TRP OXT HXT  sing N N 326 
VAL N   CA   sing N N 327 
VAL N   H    sing N N 328 
VAL N   H2   sing N N 329 
VAL CA  C    sing N N 330 
VAL CA  CB   sing N N 331 
VAL CA  HA   sing N N 332 
VAL C   O    doub N N 333 
VAL C   OXT  sing N N 334 
VAL CB  CG1  sing N N 335 
VAL CB  CG2  sing N N 336 
VAL CB  HB   sing N N 337 
VAL CG1 HG11 sing N N 338 
VAL CG1 HG12 sing N N 339 
VAL CG1 HG13 sing N N 340 
VAL CG2 HG21 sing N N 341 
VAL CG2 HG22 sing N N 342 
VAL CG2 HG23 sing N N 343 
VAL OXT HXT  sing N N 344 
# 
_pdbx_audit_support.funding_organization   'Ministerio de Ciencia e Innovacion (MCIN)' 
_pdbx_audit_support.country                Spain 
_pdbx_audit_support.grant_number           PID2019.107515RB.C21 
_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   6r2g 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 65' 
_space_group.name_Hall        'P 65' 
_space_group.IT_number        170 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9HS7 
_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]   0.015282 
_atom_sites.fract_transf_matrix[1][2]   0.008823 
_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]   0.017647 
_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]   0.011265 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . CYS A 1 3   ? 2.09100   25.94600 -19.01400 1.000 143.89620 ? 3   CYS A N    1 
ATOM   2    C CA   . CYS A 1 3   ? 0.74600   26.08600 -19.63400 1.000 166.39627 ? 3   CYS A CA   1 
ATOM   3    C C    . CYS A 1 3   ? 0.42700   24.84300 -20.47700 1.000 170.24936 ? 3   CYS A C    1 
ATOM   4    O O    . CYS A 1 3   ? 1.37800   24.26600 -21.05000 1.000 151.94717 ? 3   CYS A O    1 
ATOM   5    C CB   . CYS A 1 3   ? 0.67100   27.33100 -20.50900 1.000 158.40583 ? 3   CYS A CB   1 
ATOM   6    S SG   . CYS A 1 3   ? -1.02800  27.84000 -20.86700 1.000 158.66113 ? 3   CYS A SG   1 
ATOM   7    H HA   . CYS A 1 3   ? 0.07700   26.16200 -18.93600 1.000 200.30000 ? 3   CYS A HA   1 
ATOM   8    H HB2  . CYS A 1 3   ? 1.11300   28.06400 -20.05300 1.000 190.71000 ? 3   CYS A HB2  1 
ATOM   9    H HB3  . CYS A 1 3   ? 1.11400   27.15000 -21.35300 1.000 190.71000 ? 3   CYS A HB3  1 
ATOM   10   N N    . GLY A 1 4   ? -0.84900  24.45300 -20.55600 1.000 147.56506 ? 4   GLY A N    1 
ATOM   11   C CA   . GLY A 1 4   ? -1.26600  23.27600 -21.34400 1.000 116.94823 ? 4   GLY A CA   1 
ATOM   12   C C    . GLY A 1 4   ? -2.75300  23.01800 -21.21900 1.000 147.04658 ? 4   GLY A C    1 
ATOM   13   O O    . GLY A 1 4   ? -3.53000  23.92900 -21.57500 1.000 139.46409 ? 4   GLY A O    1 
ATOM   14   H H    . GLY A 1 4   ? -1.50000  24.85300 -20.16100 1.000 177.70000 ? 4   GLY A H    1 
ATOM   15   H HA2  . GLY A 1 4   ? -1.05400  23.41900 -22.28000 1.000 140.96000 ? 4   GLY A HA2  1 
ATOM   16   H HA3  . GLY A 1 4   ? -0.78800  22.49100 -21.03400 1.000 140.96000 ? 4   GLY A HA3  1 
ATOM   17   N N    . ALA A 1 5   ? -3.14700  21.83300 -20.74100 1.000 152.93939 ? 5   ALA A N    1 
ATOM   18   C CA   . ALA A 1 5   ? -4.57000  21.44300 -20.59100 1.000 156.66615 ? 5   ALA A CA   1 
ATOM   19   C C    . ALA A 1 5   ? -4.71200  20.45400 -19.43300 1.000 159.90075 ? 5   ALA A C    1 
ATOM   20   O O    . ALA A 1 5   ? -3.67000  19.95700 -18.95300 1.000 161.31408 ? 5   ALA A O    1 
ATOM   21   C CB   . ALA A 1 5   ? -5.07400  20.85700 -21.89000 1.000 135.10567 ? 5   ALA A CB   1 
ATOM   22   H H    . ALA A 1 5   ? -2.60000  21.21900 -20.48900 1.000 184.16000 ? 5   ALA A H    1 
ATOM   23   H HA   . ALA A 1 5   ? -5.09900  22.23000 -20.38600 1.000 188.62000 ? 5   ALA A HA   1 
ATOM   24   H HB1  . ALA A 1 5   ? -5.98100  20.53900 -21.76400 1.000 162.75000 ? 5   ALA A HB1  1 
ATOM   25   H HB2  . ALA A 1 5   ? -5.05500  21.54300 -22.57500 1.000 162.75000 ? 5   ALA A HB2  1 
ATOM   26   H HB3  . ALA A 1 5   ? -4.50000  20.11700 -22.14400 1.000 162.75000 ? 5   ALA A HB3  1 
ATOM   27   N N    . ALA A 1 6   ? -5.94200  20.16300 -19.00100 1.000 137.86653 ? 6   ALA A N    1 
ATOM   28   C CA   . ALA A 1 6   ? -6.20600  19.25600 -17.85800 1.000 123.80695 ? 6   ALA A CA   1 
ATOM   29   C C    . ALA A 1 6   ? -5.82800  17.81300 -18.20000 1.000 124.78601 ? 6   ALA A C    1 
ATOM   30   O O    . ALA A 1 6   ? -5.81900  17.49400 -19.41000 1.000 135.06356 ? 6   ALA A O    1 
ATOM   31   C CB   . ALA A 1 6   ? -7.66200  19.35600 -17.45800 1.000 88.59746  ? 6   ALA A CB   1 
ATOM   32   H H    . ALA A 1 6   ? -6.65800  20.48100 -19.35500 1.000 166.07000 ? 6   ALA A H    1 
ATOM   33   H HA   . ALA A 1 6   ? -5.66700  19.53600 -17.10200 1.000 149.19000 ? 6   ALA A HA   1 
ATOM   34   H HB1  . ALA A 1 6   ? -8.21500  19.10000 -18.21300 1.000 106.94000 ? 6   ALA A HB1  1 
ATOM   35   H HB2  . ALA A 1 6   ? -7.82500  18.76000 -16.71000 1.000 106.94000 ? 6   ALA A HB2  1 
ATOM   36   H HB3  . ALA A 1 6   ? -7.85600  20.27100 -17.20100 1.000 106.94000 ? 6   ALA A HB3  1 
ATOM   37   N N    . SER A 1 7   ? -5.54800  16.97100 -17.19400 1.000 123.37532 ? 7   SER A N    1 
ATOM   38   C CA   . SER A 1 7   ? -5.21600  15.56100 -17.36600 1.000 120.61973 ? 7   SER A CA   1 
ATOM   39   C C    . SER A 1 7   ? -6.37700  14.66400 -16.93400 1.000 117.01140 ? 7   SER A C    1 
ATOM   40   O O    . SER A 1 7   ? -7.39600  15.12500 -16.40300 1.000 120.00386 ? 7   SER A O    1 
ATOM   41   C CB   . SER A 1 7   ? -3.95200  15.18900 -16.57300 1.000 104.60465 ? 7   SER A CB   1 
ATOM   42   O OG   . SER A 1 7   ? -4.27000  14.80500 -15.24000 1.000 103.55715 ? 7   SER A OG   1 
ATOM   43   H H    . SER A 1 7   ? -5.54600  17.21300 -16.36900 1.000 148.68000 ? 7   SER A H    1 
ATOM   44   H HA   . SER A 1 7   ? -5.04000  15.39100 -18.30500 1.000 145.37000 ? 7   SER A HA   1 
ATOM   45   H HB2  . SER A 1 7   ? -3.51000  14.44800 -17.01600 1.000 126.15000 ? 7   SER A HB2  1 
ATOM   46   H HB3  . SER A 1 7   ? -3.36100  15.95800 -16.54600 1.000 126.15000 ? 7   SER A HB3  1 
ATOM   47   H HG   . SER A 1 7   ? -3.56800  14.60600 -14.82300 1.000 124.90000 ? 7   SER A HG   1 
ATOM   48   N N    . MET A 1 8   ? -6.20400  13.35300 -17.17200 1.000 112.93986 ? 8   MET A N    1 
ATOM   49   C CA   . MET A 1 8   ? -7.28100  12.40100 -16.91800 1.000 106.87334 ? 8   MET A CA   1 
ATOM   50   C C    . MET A 1 8   ? -7.43700  12.10400 -15.43300 1.000 119.80910 ? 8   MET A C    1 
ATOM   51   O O    . MET A 1 8   ? -8.55900  11.86100 -14.97500 1.000 122.63839 ? 8   MET A O    1 
ATOM   52   C CB   . MET A 1 8   ? -7.04900  11.09000 -17.67500 1.000 103.62032 ? 8   MET A CB   1 
ATOM   53   C CG   . MET A 1 8   ? -7.39700  11.14400 -19.15600 1.000 128.79965 ? 8   MET A CG   1 
ATOM   54   S SD   . MET A 1 8   ? -9.09700  11.69300 -19.47100 1.000 157.07936 ? 8   MET A SD   1 
ATOM   55   C CE   . MET A 1 8   ? -10.09000 10.32900 -18.85600 1.000 111.05279 ? 8   MET A CE   1 
ATOM   56   H H    . MET A 1 8   ? -5.48100  13.00100 -17.47600 1.000 136.15000 ? 8   MET A H    1 
ATOM   57   H HA   . MET A 1 8   ? -8.11000  12.79000 -17.23400 1.000 128.87000 ? 8   MET A HA   1 
ATOM   58   H HB2  . MET A 1 8   ? -6.11200  10.85200 -17.60200 1.000 124.97000 ? 8   MET A HB2  1 
ATOM   59   H HB3  . MET A 1 8   ? -7.59400  10.39800 -17.27000 1.000 124.97000 ? 8   MET A HB3  1 
ATOM   60   H HG2  . MET A 1 8   ? -6.79600  11.76400 -19.59800 1.000 155.19000 ? 8   MET A HG2  1 
ATOM   61   H HG3  . MET A 1 8   ? -7.29400  10.25700 -19.53600 1.000 155.19000 ? 8   MET A HG3  1 
ATOM   62   H HE1  . MET A 1 8   ? -11.02800 10.53800 -18.98600 1.000 133.89000 ? 8   MET A HE1  1 
ATOM   63   H HE2  . MET A 1 8   ? -9.85900  9.52500  -19.34600 1.000 133.89000 ? 8   MET A HE2  1 
ATOM   64   H HE3  . MET A 1 8   ? -9.90600  10.20600 -17.91200 1.000 133.89000 ? 8   MET A HE3  1 
ATOM   65   N N    . THR A 1 9   ? -6.33800  12.12000 -14.66500 1.000 119.10112 ? 9   THR A N    1 
ATOM   66   C CA   . THR A 1 9   ? -6.44000  11.86700 -13.22700 1.000 117.21669 ? 9   THR A CA   1 
ATOM   67   C C    . THR A 1 9   ? -7.09600  13.03600 -12.49100 1.000 111.76603 ? 9   THR A C    1 
ATOM   68   O O    . THR A 1 9   ? -7.73100  12.83500 -11.44000 1.000 99.16452  ? 9   THR A O    1 
ATOM   69   C CB   . THR A 1 9   ? -5.05200  11.57800 -12.64200 1.000 107.80240 ? 9   THR A CB   1 
ATOM   70   O OG1  . THR A 1 9   ? -4.59600  10.29500 -13.09200 1.000 107.48657 ? 9   THR A OG1  1 
ATOM   71   C CG2  . THR A 1 9   ? -5.09800  11.60500 -11.12100 1.000 103.93878 ? 9   THR A CG2  1 
ATOM   72   H H    . THR A 1 9   ? -5.54000  12.27200 -14.94800 1.000 143.55000 ? 9   THR A H    1 
ATOM   73   H HA   . THR A 1 9   ? -6.99100  11.08100 -13.08600 1.000 141.29000 ? 9   THR A HA   1 
ATOM   74   H HB   . THR A 1 9   ? -4.43100  12.26100 -12.94000 1.000 129.99000 ? 9   THR A HB   1 
ATOM   75   H HG1  . THR A 1 9   ? -3.83600  10.13200 -12.77400 1.000 129.61000 ? 9   THR A HG1  1 
ATOM   76   H HG21 . THR A 1 9   ? -5.08100  12.52100 -10.80100 1.000 125.36000 ? 9   THR A HG21 1 
ATOM   77   H HG22 . THR A 1 9   ? -4.33000  11.13400 -10.76100 1.000 125.36000 ? 9   THR A HG22 1 
ATOM   78   H HG23 . THR A 1 9   ? -5.90600  11.17200 -10.80500 1.000 125.36000 ? 9   THR A HG23 1 
ATOM   79   N N    . LYS A 1 10  ? -6.94700  14.25800 -13.02200 1.000 107.43657 ? 10  LYS A N    1 
ATOM   80   C CA   . LYS A 1 10  ? -7.66100  15.41200 -12.48600 1.000 102.76232 ? 10  LYS A CA   1 
ATOM   81   C C    . LYS A 1 10  ? -9.11300  15.42600 -12.94400 1.000 96.09047  ? 10  LYS A C    1 
ATOM   82   O O    . LYS A 1 10  ? -10.02200 15.70700 -12.15100 1.000 86.26034  ? 10  LYS A O    1 
ATOM   83   C CB   . LYS A 1 10  ? -6.97900  16.71100 -12.92100 1.000 106.28643 ? 10  LYS A CB   1 
ATOM   84   C CG   . LYS A 1 10  ? -5.90600  17.21800 -11.96900 1.000 117.91940 ? 10  LYS A CG   1 
ATOM   85   C CD   . LYS A 1 10  ? -6.01500  18.74000 -11.74300 1.000 124.49651 ? 10  LYS A CD   1 
ATOM   86   C CE   . LYS A 1 10  ? -5.12300  19.55200 -12.69400 1.000 129.23655 ? 10  LYS A CE   1 
ATOM   87   N NZ   . LYS A 1 10  ? -5.15500  21.02100 -12.40400 1.000 104.64676 ? 10  LYS A NZ   1 
ATOM   88   H H    . LYS A 1 10  ? -6.43800  14.43800 -13.69100 1.000 129.55000 ? 10  LYS A H    1 
ATOM   89   H HA   . LYS A 1 10  ? -7.65200  15.37000 -11.51700 1.000 123.94000 ? 10  LYS A HA   1 
ATOM   90   H HB2  . LYS A 1 10  ? -6.55700  16.56300 -13.78200 1.000 128.17000 ? 10  LYS A HB2  1 
ATOM   91   H HB3  . LYS A 1 10  ? -7.65800  17.39700 -13.00800 1.000 128.17000 ? 10  LYS A HB3  1 
ATOM   92   H HG2  . LYS A 1 10  ? -6.00100  16.77800 -11.11000 1.000 142.13000 ? 10  LYS A HG2  1 
ATOM   93   H HG3  . LYS A 1 10  ? -5.03200  17.03000 -12.34600 1.000 142.13000 ? 10  LYS A HG3  1 
ATOM   94   H HD2  . LYS A 1 10  ? -6.93200  19.02700 -11.87300 1.000 150.02000 ? 10  LYS A HD2  1 
ATOM   95   H HD3  . LYS A 1 10  ? -5.73600  18.93900 -10.83600 1.000 150.02000 ? 10  LYS A HD3  1 
ATOM   96   H HE2  . LYS A 1 10  ? -4.20600  19.24800 -12.60400 1.000 155.71000 ? 10  LYS A HE2  1 
ATOM   97   H HE3  . LYS A 1 10  ? -5.42900  19.41900 -13.60500 1.000 155.71000 ? 10  LYS A HE3  1 
ATOM   98   H HZ1  . LYS A 1 10  ? -5.98600  21.32900 -12.48700 1.000 126.20000 ? 10  LYS A HZ1  1 
ATOM   99   H HZ2  . LYS A 1 10  ? -4.62700  21.45500 -12.97400 1.000 126.20000 ? 10  LYS A HZ2  1 
ATOM   100  H HZ3  . LYS A 1 10  ? -4.87100  21.17300 -11.57400 1.000 126.20000 ? 10  LYS A HZ3  1 
ATOM   101  N N    . THR A 1 11  ? -9.34000  15.13300 -14.22700 1.000 80.05697  ? 11  THR A N    1 
ATOM   102  C CA   . THR A 1 11  ? -10.69300 15.13600 -14.77000 1.000 71.43488  ? 11  THR A CA   1 
ATOM   103  C C    . THR A 1 11  ? -11.60100 14.12800 -14.07400 1.000 77.54351  ? 11  THR A C    1 
ATOM   104  O O    . THR A 1 11  ? -12.81600 14.37000 -13.95900 1.000 84.06534  ? 11  THR A O    1 
ATOM   105  C CB   . THR A 1 11  ? -10.61800 14.85400 -16.27000 1.000 74.89319  ? 11  THR A CB   1 
ATOM   106  O OG1  . THR A 1 11  ? -10.01600 15.97600 -16.92800 1.000 77.73564  ? 11  THR A OG1  1 
ATOM   107  C CG2  . THR A 1 11  ? -11.98900 14.58000 -16.82900 1.000 90.97933  ? 11  THR A CG2  1 
ATOM   108  H H    . THR A 1 11  ? -8.72900  14.93100 -14.79800 1.000 96.69000  ? 11  THR A H    1 
ATOM   109  H HA   . THR A 1 11  ? -11.07900 16.01800 -14.65000 1.000 86.35000  ? 11  THR A HA   1 
ATOM   110  H HB   . THR A 1 11  ? -10.07000 14.06800 -16.41800 1.000 90.50000  ? 11  THR A HB   1 
ATOM   111  H HG1  . THR A 1 11  ? -9.96900  15.83300 -17.75400 1.000 93.91000  ? 11  THR A HG1  1 
ATOM   112  H HG21 . THR A 1 11  ? -12.25300 13.66700 -16.63700 1.000 109.80000 ? 11  THR A HG21 1 
ATOM   113  H HG22 . THR A 1 11  ? -11.98300 14.70800 -17.79100 1.000 109.80000 ? 11  THR A HG22 1 
ATOM   114  H HG23 . THR A 1 11  ? -12.63500 15.18800 -16.43700 1.000 109.80000 ? 11  THR A HG23 1 
ATOM   115  N N    . VAL A 1 12  ? -11.04100 12.99500 -13.61800 1.000 97.56170  ? 12  VAL A N    1 
ATOM   116  C CA   . VAL A 1 12  ? -11.82900 12.01300 -12.86800 1.000 100.61470 ? 12  VAL A CA   1 
ATOM   117  C C    . VAL A 1 12  ? -11.97200 12.44500 -11.40800 1.000 87.77105  ? 12  VAL A C    1 
ATOM   118  O O    . VAL A 1 12  ? -13.03800 12.27200 -10.79800 1.000 85.81555  ? 12  VAL A O    1 
ATOM   119  C CB   . VAL A 1 12  ? -11.22400 10.59200 -12.97000 1.000 84.37854  ? 12  VAL A CB   1 
ATOM   120  C CG1  . VAL A 1 12  ? -11.11400 10.12200 -14.43800 1.000 77.71984  ? 12  VAL A CG1  1 
ATOM   121  C CG2  . VAL A 1 12  ? -9.87000  10.52200 -12.25600 1.000 90.09501  ? 12  VAL A CG2  1 
ATOM   122  H H    . VAL A 1 12  ? -10.21700 12.77800 -13.73100 1.000 117.70000 ? 12  VAL A H    1 
ATOM   123  H HA   . VAL A 1 12  ? -12.72000 11.97700 -13.25000 1.000 121.36000 ? 12  VAL A HA   1 
ATOM   124  H HB   . VAL A 1 12  ? -11.82000 9.97600  -12.51600 1.000 101.88000 ? 12  VAL A HB   1 
ATOM   125  H HG11 . VAL A 1 12  ? -10.57200 9.31800  -14.47200 1.000 93.89000  ? 12  VAL A HG11 1 
ATOM   126  H HG12 . VAL A 1 12  ? -12.00400 9.93400  -14.77500 1.000 93.89000  ? 12  VAL A HG12 1 
ATOM   127  H HG13 . VAL A 1 12  ? -10.70100 10.82100 -14.96700 1.000 93.89000  ? 12  VAL A HG13 1 
ATOM   128  H HG21 . VAL A 1 12  ? -9.32000  11.26500 -12.54800 1.000 108.74000 ? 12  VAL A HG21 1 
ATOM   129  H HG22 . VAL A 1 12  ? -9.43800  9.68300  -12.48200 1.000 108.74000 ? 12  VAL A HG22 1 
ATOM   130  H HG23 . VAL A 1 12  ? -10.01300 10.57200 -11.29800 1.000 108.74000 ? 12  VAL A HG23 1 
ATOM   131  N N    . GLN A 1 13  ? -10.90500 13.00400 -10.82200 1.000 87.96318  ? 13  GLN A N    1 
ATOM   132  C CA   . GLN A 1 13  ? -11.00400 13.57800 -9.48200  1.000 98.54076  ? 13  GLN A CA   1 
ATOM   133  C C    . GLN A 1 13  ? -12.16700 14.56600 -9.39500  1.000 88.26058  ? 13  GLN A C    1 
ATOM   134  O O    . GLN A 1 13  ? -13.02000 14.48100 -8.49200  1.000 68.35556  ? 13  GLN A O    1 
ATOM   135  C CB   . GLN A 1 13  ? -9.67700  14.25400 -9.12300  1.000 110.38692 ? 13  GLN A CB   1 
ATOM   136  C CG   . GLN A 1 13  ? -9.64800  14.93600 -7.75500  1.000 123.41743 ? 13  GLN A CG   1 
ATOM   137  C CD   . GLN A 1 13  ? -8.23600  15.34000 -7.33000  1.000 120.54340 ? 13  GLN A CD   1 
ATOM   138  O OE1  . GLN A 1 13  ? -7.24000  14.94200 -7.95900  1.000 106.46540 ? 13  GLN A OE1  1 
ATOM   139  N NE2  . GLN A 1 13  ? -8.14500  16.13500 -6.25900  1.000 115.23487 ? 13  GLN A NE2  1 
ATOM   140  H H    . GLN A 1 13  ? -10.12400 13.06100 -11.17700 1.000 106.18000 ? 13  GLN A H    1 
ATOM   141  H HA   . GLN A 1 13  ? -11.16400 12.86700 -8.84200  1.000 118.88000 ? 13  GLN A HA   1 
ATOM   142  H HB2  . GLN A 1 13  ? -8.97800  13.58200 -9.13000  1.000 133.09000 ? 13  GLN A HB2  1 
ATOM   143  H HB3  . GLN A 1 13  ? -9.48500  14.93000 -9.79100  1.000 133.09000 ? 13  GLN A HB3  1 
ATOM   144  H HG2  . GLN A 1 13  ? -10.19200 15.73800 -7.78900  1.000 148.73000 ? 13  GLN A HG2  1 
ATOM   145  H HG3  . GLN A 1 13  ? -9.99900  14.32400 -7.08900  1.000 148.73000 ? 13  GLN A HG3  1 
ATOM   146  H HE21 . GLN A 1 13  ? -8.85800  16.38900 -5.85100  1.000 138.91000 ? 13  GLN A HE21 1 
ATOM   147  H HE22 . GLN A 1 13  ? -7.37400  16.39200 -5.97800  1.000 138.91000 ? 13  GLN A HE22 1 
ATOM   148  N N    . ALA A 1 14  ? -12.23500 15.49000 -10.36300 1.000 68.57401  ? 14  ALA A N    1 
ATOM   149  C CA   . ALA A 1 14  ? -13.27100 16.51900 -10.33600 1.000 76.32757  ? 14  ALA A CA   1 
ATOM   150  C C    . ALA A 1 14  ? -14.65100 15.95500 -10.66900 1.000 60.62569  ? 14  ALA A C    1 
ATOM   151  O O    . ALA A 1 14  ? -15.64200 16.33300 -10.03400 1.000 59.01497  ? 14  ALA A O    1 
ATOM   152  C CB   . ALA A 1 14  ? -12.90900 17.64100 -11.30600 1.000 79.91748  ? 14  ALA A CB   1 
ATOM   153  H H    . ALA A 1 14  ? -11.70000 15.53900 -11.03400 1.000 82.92000  ? 14  ALA A H    1 
ATOM   154  H HA   . ALA A 1 14  ? -13.31200 16.89800 -9.44400  1.000 92.22000  ? 14  ALA A HA   1 
ATOM   155  H HB1  . ALA A 1 14  ? -12.94100 17.29800 -12.21300 1.000 96.53000  ? 14  ALA A HB1  1 
ATOM   156  H HB2  . ALA A 1 14  ? -12.01600 17.96100 -11.10200 1.000 96.53000  ? 14  ALA A HB2  1 
ATOM   157  H HB3  . ALA A 1 14  ? -13.55100 18.35700 -11.19900 1.000 96.53000  ? 14  ALA A HB3  1 
ATOM   158  N N    . ARG A 1 15  ? -14.75200 15.08100 -11.68100 1.000 64.06031  ? 15  ARG A N    1 
ATOM   159  C CA   . ARG A 1 15  ? -16.03100 14.41500 -11.91400 1.000 47.48464  ? 15  ARG A CA   1 
ATOM   160  C C    . ARG A 1 15  ? -16.48100 13.70400 -10.64800 1.000 56.02251  ? 15  ARG A C    1 
ATOM   161  O O    . ARG A 1 15  ? -17.61400 13.88500 -10.18700 1.000 63.39181  ? 15  ARG A O    1 
ATOM   162  C CB   . ARG A 1 15  ? -15.94700 13.42800 -13.08400 1.000 58.88074  ? 15  ARG A CB   1 
ATOM   163  C CG   . ARG A 1 15  ? -17.17400 12.43400 -13.19300 1.000 70.92429  ? 15  ARG A CG   1 
ATOM   164  C CD   . ARG A 1 15  ? -18.59700 13.09300 -13.46800 1.000 92.11631  ? 15  ARG A CD   1 
ATOM   165  N NE   . ARG A 1 15  ? -19.70100 12.15500 -13.21700 1.000 87.93423  ? 15  ARG A NE   1 
ATOM   166  C CZ   . ARG A 1 15  ? -20.46200 11.57200 -14.14600 1.000 72.75609  ? 15  ARG A CZ   1 
ATOM   167  N NH1  . ARG A 1 15  ? -20.42600 11.94700 -15.41700 1.000 64.78935  ? 15  ARG A NH1  1 
ATOM   168  N NH2  . ARG A 1 15  ? -21.27500 10.57500 -13.79200 1.000 71.53226  ? 15  ARG A NH2  1 
ATOM   169  H H    . ARG A 1 15  ? -14.12000 14.86600 -12.22400 1.000 77.50000  ? 15  ARG A H    1 
ATOM   170  H HA   . ARG A 1 15  ? -16.69800 15.08400 -12.13500 1.000 56.21000  ? 15  ARG A HA   1 
ATOM   171  H HB2  . ARG A 1 15  ? -15.90200 13.93100 -13.91200 1.000 71.28000  ? 15  ARG A HB2  1 
ATOM   172  H HB3  . ARG A 1 15  ? -15.14400 12.89400 -12.98200 1.000 71.28000  ? 15  ARG A HB3  1 
ATOM   173  H HG2  . ARG A 1 15  ? -16.99900 11.82600 -13.92800 1.000 85.73000  ? 15  ARG A HG2  1 
ATOM   174  H HG3  . ARG A 1 15  ? -17.24200 11.92300 -12.37200 1.000 85.73000  ? 15  ARG A HG3  1 
ATOM   175  H HD2  . ARG A 1 15  ? -18.71100 13.85200 -12.87500 1.000 111.17000 ? 15  ARG A HD2  1 
ATOM   176  H HD3  . ARG A 1 15  ? -18.63500 13.38800 -14.39000 1.000 111.17000 ? 15  ARG A HD3  1 
ATOM   177  H HE   . ARG A 1 15  ? -19.87200 11.96400 -12.39600 1.000 106.15000 ? 15  ARG A HE   1 
ATOM   178  H HH11 . ARG A 1 15  ? -19.91200 12.58700 -15.66800 1.000 78.37000  ? 15  ARG A HH11 1 
ATOM   179  H HH12 . ARG A 1 15  ? -20.93700 11.55900 -15.98900 1.000 78.37000  ? 15  ARG A HH12 1 
ATOM   180  H HH21 . ARG A 1 15  ? -21.29500 10.31300 -12.97500 1.000 86.47000  ? 15  ARG A HH21 1 
ATOM   181  H HH22 . ARG A 1 15  ? -21.77300 10.19400 -14.38100 1.000 86.47000  ? 15  ARG A HH22 1 
ATOM   182  N N    . GLN A 1 16  ? -15.59000 12.91100 -10.05100 1.000 66.28163  ? 16  GLN A N    1 
ATOM   183  C CA   . GLN A 1 16  ? -15.95100 12.21400 -8.82500  1.000 63.97609  ? 16  GLN A CA   1 
ATOM   184  C C    . GLN A 1 16  ? -16.33800 13.18400 -7.71700  1.000 55.89354  ? 16  GLN A C    1 
ATOM   185  O O    . GLN A 1 16  ? -17.24700 12.88300 -6.92800  1.000 51.16666  ? 16  GLN A O    1 
ATOM   186  C CB   . GLN A 1 16  ? -14.80500 11.29800 -8.41600  1.000 53.83540  ? 16  GLN A CB   1 
ATOM   187  C CG   . GLN A 1 16  ? -15.08500 9.85300  -8.84200  1.000 68.70034  ? 16  GLN A CG   1 
ATOM   188  C CD   . GLN A 1 16  ? -13.82300 9.01200  -9.01900  1.000 90.84247  ? 16  GLN A CD   1 
ATOM   189  O OE1  . GLN A 1 16  ? -13.00600 8.87900  -8.09700  1.000 89.11332  ? 16  GLN A OE1  1 
ATOM   190  N NE2  . GLN A 1 16  ? -13.65900 8.43600  -10.21400 1.000 81.28343  ? 16  GLN A NE2  1 
ATOM   191  H H    . GLN A 1 16  ? -14.79000 12.76500 -10.33100 1.000 80.16000  ? 16  GLN A H    1 
ATOM   192  H HA   . GLN A 1 16  ? -16.72400 11.65600 -9.00400  1.000 77.40000  ? 16  GLN A HA   1 
ATOM   193  H HB2  . GLN A 1 16  ? -13.98100 11.59000 -8.83100  1.000 65.23000  ? 16  GLN A HB2  1 
ATOM   194  H HB3  . GLN A 1 16  ? -14.71500 11.31500 -7.45000  1.000 65.23000  ? 16  GLN A HB3  1 
ATOM   195  H HG2  . GLN A 1 16  ? -15.63300 9.42700  -8.16500  1.000 83.07000  ? 16  GLN A HG2  1 
ATOM   196  H HG3  . GLN A 1 16  ? -15.55600 9.86100  -9.69000  1.000 83.07000  ? 16  GLN A HG3  1 
ATOM   197  H HE21 . GLN A 1 16  ? -14.24700 8.55000  -10.83100 1.000 98.17000  ? 16  GLN A HE21 1 
ATOM   198  H HE22 . GLN A 1 16  ? -12.96500 7.95200  -10.36600 1.000 98.17000  ? 16  GLN A HE22 1 
ATOM   199  N N    . LYS A 1 17  ? -15.70800 14.35900 -7.66500  1.000 48.05050  ? 17  LYS A N    1 
ATOM   200  C CA   . LYS A 1 17  ? -16.12100 15.36800 -6.69400  1.000 47.51359  ? 17  LYS A CA   1 
ATOM   201  C C    . LYS A 1 17  ? -17.55100 15.82700 -6.94900  1.000 59.73348  ? 17  LYS A C    1 
ATOM   202  O O    . LYS A 1 17  ? -18.39000 15.84100 -6.03500  1.000 48.15841  ? 17  LYS A O    1 
ATOM   203  C CB   . LYS A 1 17  ? -15.17500 16.56500 -6.74400  1.000 66.15530  ? 17  LYS A CB   1 
ATOM   204  C CG   . LYS A 1 17  ? -15.38900 17.54600 -5.58900  1.000 70.53740  ? 17  LYS A CG   1 
ATOM   205  C CD   . LYS A 1 17  ? -14.09400 17.75800 -4.77900  1.000 70.94535  ? 17  LYS A CD   1 
ATOM   206  C CE   . LYS A 1 17  ? -14.35900 18.61800 -3.54200  1.000 82.52568  ? 17  LYS A CE   1 
ATOM   207  N NZ   . LYS A 1 17  ? -15.10100 19.86600 -3.90900  1.000 82.96521  ? 17  LYS A NZ   1 
ATOM   208  H H    . LYS A 1 17  ? -15.05200 14.59200 -8.17000  1.000 58.29000  ? 17  LYS A H    1 
ATOM   209  H HA   . LYS A 1 17  ? -16.08000 14.98700 -5.80300  1.000 57.64000  ? 17  LYS A HA   1 
ATOM   210  H HB2  . LYS A 1 17  ? -14.26000 16.24600 -6.70000  1.000 80.01000  ? 17  LYS A HB2  1 
ATOM   211  H HB3  . LYS A 1 17  ? -15.31800 17.04500 -7.57500  1.000 80.01000  ? 17  LYS A HB3  1 
ATOM   212  H HG2  . LYS A 1 17  ? -15.66900 18.40300 -5.94800  1.000 85.27000  ? 17  LYS A HG2  1 
ATOM   213  H HG3  . LYS A 1 17  ? -16.06700 17.19500 -4.99100  1.000 85.27000  ? 17  LYS A HG3  1 
ATOM   214  H HD2  . LYS A 1 17  ? -13.75300 16.89800 -4.48600  1.000 85.76000  ? 17  LYS A HD2  1 
ATOM   215  H HD3  . LYS A 1 17  ? -13.43900 18.21100 -5.33200  1.000 85.76000  ? 17  LYS A HD3  1 
ATOM   216  H HE2  . LYS A 1 17  ? -14.89800 18.11600 -2.91000  1.000 99.66000  ? 17  LYS A HE2  1 
ATOM   217  H HE3  . LYS A 1 17  ? -13.51400 18.87200 -3.13900  1.000 99.66000  ? 17  LYS A HE3  1 
ATOM   218  H HZ1  . LYS A 1 17  ? -15.09700 20.43300 -3.22300  1.000 100.19000 ? 17  LYS A HZ1  1 
ATOM   219  H HZ2  . LYS A 1 17  ? -15.94300 19.66900 -4.12100  1.000 100.19000 ? 17  LYS A HZ2  1 
ATOM   220  H HZ3  . LYS A 1 17  ? -14.71000 20.25700 -4.60700  1.000 100.19000 ? 17  LYS A HZ3  1 
ATOM   221  N N    . LEU A 1 18  ? -17.84400 16.24100 -8.18400  1.000 56.84629  ? 18  LEU A N    1 
ATOM   222  C CA   . LEU A 1 18  ? -19.23400 16.51400 -8.54400  1.000 46.99248  ? 18  LEU A CA   1 
ATOM   223  C C    . LEU A 1 18  ? -20.14800 15.35400 -8.14500  1.000 39.92584  ? 18  LEU A C    1 
ATOM   224  O O    . LEU A 1 18  ? -21.25700 15.56100 -7.63800  1.000 42.09978  ? 18  LEU A O    1 
ATOM   225  C CB   . LEU A 1 18  ? -19.34600 16.76000 -10.04200 1.000 43.23150  ? 18  LEU A CB   1 
ATOM   226  C CG   . LEU A 1 18  ? -18.67600 18.00800 -10.59400 1.000 45.09488  ? 18  LEU A CG   1 
ATOM   227  C CD1  . LEU A 1 18  ? -18.78400 18.07200 -12.09400 1.000 46.86351  ? 18  LEU A CD1  1 
ATOM   228  C CD2  . LEU A 1 18  ? -19.39300 19.17400 -9.94400  1.000 45.88708  ? 18  LEU A CD2  1 
ATOM   229  H H    . LEU A 1 18  ? -17.27300 16.36800 -8.81400  1.000 68.84000  ? 18  LEU A H    1 
ATOM   230  H HA   . LEU A 1 18  ? -19.53600 17.30600 -8.07300  1.000 57.02000  ? 18  LEU A HA   1 
ATOM   231  H HB2  . LEU A 1 18  ? -18.95100 16.00100 -10.50000 1.000 52.51000  ? 18  LEU A HB2  1 
ATOM   232  H HB3  . LEU A 1 18  ? -20.28700 16.81300 -10.27000 1.000 52.51000  ? 18  LEU A HB3  1 
ATOM   233  H HG   . LEU A 1 18  ? -17.74000 18.02700 -10.33900 1.000 54.74000  ? 18  LEU A HG   1 
ATOM   234  H HD11 . LEU A 1 18  ? -18.30900 18.85600 -12.41100 1.000 56.86000  ? 18  LEU A HD11 1 
ATOM   235  H HD12 . LEU A 1 18  ? -18.39000 17.27100 -12.47300 1.000 56.86000  ? 18  LEU A HD12 1 
ATOM   236  H HD13 . LEU A 1 18  ? -19.72000 18.12900 -12.34100 1.000 56.86000  ? 18  LEU A HD13 1 
ATOM   237  H HD21 . LEU A 1 18  ? -19.18200 19.98100 -10.43900 1.000 55.69000  ? 18  LEU A HD21 1 
ATOM   238  H HD22 . LEU A 1 18  ? -20.34900 19.01400 -9.96600  1.000 55.69000  ? 18  LEU A HD22 1 
ATOM   239  H HD23 . LEU A 1 18  ? -19.09200 19.26100 -9.02600  1.000 55.69000  ? 18  LEU A HD23 1 
ATOM   240  N N    . SER A 1 19  ? -19.71000 14.11800 -8.36400  1.000 41.66026  ? 19  SER A N    1 
ATOM   241  C CA   . SER A 1 19  ? -20.61700 13.00600 -8.09800  1.000 34.82786  ? 19  SER A CA   1 
ATOM   242  C C    . SER A 1 19  ? -20.89900 12.88900 -6.60700  1.000 36.14644  ? 19  SER A C    1 
ATOM   243  O O    . SER A 1 19  ? -22.01700 12.55500 -6.20400  1.000 54.05385  ? 19  SER A O    1 
ATOM   244  C CB   . SER A 1 19  ? -20.05100 11.69900 -8.66100  1.000 46.34766  ? 19  SER A CB   1 
ATOM   245  O OG   . SER A 1 19  ? -20.93600 10.63200 -8.34400  1.000 73.00086  ? 19  SER A OG   1 
ATOM   246  H H    . SER A 1 19  ? -18.92900 13.90200 -8.65300  1.000 50.62000  ? 19  SER A H    1 
ATOM   247  H HA   . SER A 1 19  ? -21.46000 13.17900 -8.54500  1.000 42.07000  ? 19  SER A HA   1 
ATOM   248  H HB2  . SER A 1 19  ? -19.97000 11.77300 -9.62500  1.000 56.25000  ? 19  SER A HB2  1 
ATOM   249  H HB3  . SER A 1 19  ? -19.18400 11.52600 -8.26200  1.000 56.25000  ? 19  SER A HB3  1 
ATOM   250  H HG   . SER A 1 19  ? -20.63500 9.90900  -8.64800  1.000 88.23000  ? 19  SER A HG   1 
ATOM   251  N N    . GLY A 1 20  ? -19.90100 13.17300 -5.76700  1.000 41.81028  ? 20  GLY A N    1 
ATOM   252  C CA   . GLY A 1 20  ? -20.09300 13.06600 -4.32900  1.000 41.90502  ? 20  GLY A CA   1 
ATOM   253  C C    . GLY A 1 20  ? -21.02200 14.13000 -3.78300  1.000 37.05707  ? 20  GLY A C    1 
ATOM   254  O O    . GLY A 1 20  ? -21.80500 13.86200 -2.86500  1.000 39.76529  ? 20  GLY A O    1 
ATOM   255  H H    . GLY A 1 20  ? -19.11400 13.42600 -6.00500  1.000 50.80000  ? 20  GLY A H    1 
ATOM   256  H HA2  . GLY A 1 20  ? -20.46600 12.19600 -4.11800  1.000 50.91000  ? 20  GLY A HA2  1 
ATOM   257  H HA3  . GLY A 1 20  ? -19.23600 13.14900 -3.88200  1.000 50.91000  ? 20  GLY A HA3  1 
ATOM   258  N N    . ILE A 1 21  ? -20.97400 15.33600 -4.36500  1.000 34.23568  ? 21  ILE A N    1 
ATOM   259  C CA   . ILE A 1 21  ? -21.90300 16.39800 -3.99900  1.000 36.35173  ? 21  ILE A CA   1 
ATOM   260  C C    . ILE A 1 21  ? -23.33200 15.99600 -4.32400  1.000 30.86159  ? 21  ILE A C    1 
ATOM   261  O O    . ILE A 1 21  ? -24.24700 16.16000 -3.51000  1.000 38.50462  ? 21  ILE A O    1 
ATOM   262  C CB   . ILE A 1 21  ? -21.53800 17.69300 -4.74000  1.000 32.69339  ? 21  ILE A CB   1 
ATOM   263  C CG1  . ILE A 1 21  ? -20.22100 18.21800 -4.23400  1.000 37.83612  ? 21  ILE A CG1  1 
ATOM   264  C CG2  . ILE A 1 21  ? -22.66600 18.69400 -4.60800  1.000 36.19381  ? 21  ILE A CG2  1 
ATOM   265  C CD1  . ILE A 1 21  ? -19.71400 19.32400 -5.10600  1.000 43.00779  ? 21  ILE A CD1  1 
ATOM   266  H H    . ILE A 1 21  ? -20.41000 15.55900 -4.97500  1.000 41.71000  ? 21  ILE A H    1 
ATOM   267  H HA   . ILE A 1 21  ? -21.84200 16.56400 -3.04500  1.000 44.25000  ? 21  ILE A HA   1 
ATOM   268  H HB   . ILE A 1 21  ? -21.43500 17.48000 -5.68100  1.000 39.86000  ? 21  ILE A HB   1 
ATOM   269  H HG12 . ILE A 1 21  ? -20.33700 18.56600 -3.33600  1.000 46.03000  ? 21  ILE A HG12 1 
ATOM   270  H HG13 . ILE A 1 21  ? -19.56500 17.50300 -4.23700  1.000 46.03000  ? 21  ILE A HG13 1 
ATOM   271  H HG21 . ILE A 1 21  ? -22.33100 19.58400 -4.79100  1.000 44.06000  ? 21  ILE A HG21 1 
ATOM   272  H HG22 . ILE A 1 21  ? -23.36400 18.47400 -5.24500  1.000 44.06000  ? 21  ILE A HG22 1 
ATOM   273  H HG23 . ILE A 1 21  ? -23.01600 18.65700 -3.70400  1.000 44.06000  ? 21  ILE A HG23 1 
ATOM   274  H HD11 . ILE A 1 21  ? -18.76800 19.45200 -4.93300  1.000 52.24000  ? 21  ILE A HD11 1 
ATOM   275  H HD12 . ILE A 1 21  ? -19.84900 19.08100 -6.03500  1.000 52.24000  ? 21  ILE A HD12 1 
ATOM   276  H HD13 . ILE A 1 21  ? -20.20000 20.13800 -4.90300  1.000 52.24000  ? 21  ILE A HD13 1 
ATOM   277  N N    . VAL A 1 22  ? -23.56200 15.53900 -5.54900  1.000 32.03279  ? 22  VAL A N    1 
ATOM   278  C CA   . VAL A 1 22  ? -24.87900 15.02600 -5.91000  1.000 27.73227  ? 22  VAL A CA   1 
ATOM   279  C C    . VAL A 1 22  ? -25.35400 14.05800 -4.83700  1.000 27.89019  ? 22  VAL A C    1 
ATOM   280  O O    . VAL A 1 22  ? -26.51200 14.10200 -4.38000  1.000 32.82236  ? 22  VAL A O    1 
ATOM   281  C CB   . VAL A 1 22  ? -24.83200 14.34900 -7.29100  1.000 27.35328  ? 22  VAL A CB   1 
ATOM   282  C CG1  . VAL A 1 22  ? -26.15600 13.66500 -7.57500  1.000 28.84820  ? 22  VAL A CG1  1 
ATOM   283  C CG2  . VAL A 1 22  ? -24.55000 15.34500 -8.36400  1.000 28.53763  ? 22  VAL A CG2  1 
ATOM   284  H H    . VAL A 1 22  ? -22.98100 15.51400 -6.18200  1.000 39.06000  ? 22  VAL A H    1 
ATOM   285  H HA   . VAL A 1 22  ? -25.50800 15.76300 -5.95400  1.000 33.91000  ? 22  VAL A HA   1 
ATOM   286  H HB   . VAL A 1 22  ? -24.13100 13.67900 -7.30000  1.000 29.69000  ? 22  VAL A HB   1 
ATOM   287  H HG11 . VAL A 1 22  ? -26.21900 13.48500 -8.52600  1.000 35.24000  ? 22  VAL A HG11 1 
ATOM   288  H HG12 . VAL A 1 22  ? -26.19800 12.83200 -7.07900  1.000 35.24000  ? 22  VAL A HG12 1 
ATOM   289  H HG13 . VAL A 1 22  ? -26.87900 14.25200 -7.30300  1.000 35.24000  ? 22  VAL A HG13 1 
ATOM   290  H HG21 . VAL A 1 22  ? -24.52000 14.88800 -9.21900  1.000 32.24000  ? 22  VAL A HG21 1 
ATOM   291  H HG22 . VAL A 1 22  ? -25.25500 16.01100 -8.36900  1.000 32.24000  ? 22  VAL A HG22 1 
ATOM   292  H HG23 . VAL A 1 22  ? -23.69600 15.76800 -8.18600  1.000 32.24000  ? 22  VAL A HG23 1 
ATOM   293  N N    . GLN A 1 23  ? -24.47500 13.14300 -4.43600  1.000 37.29658  ? 23  GLN A N    1 
ATOM   294  C CA   . GLN A 1 23  ? -24.85200 12.15300 -3.43800  1.000 37.62556  ? 23  GLN A CA   1 
ATOM   295  C C    . GLN A 1 23  ? -25.14000 12.80700 -2.09100  1.000 36.95969  ? 23  GLN A C    1 
ATOM   296  O O    . GLN A 1 23  ? -26.09300 12.42700 -1.39200  1.000 31.21427  ? 23  GLN A O    1 
ATOM   297  C CB   . GLN A 1 23  ? -23.73500 11.10500 -3.32600  1.000 40.72067  ? 23  GLN A CB   1 
ATOM   298  C CG   . GLN A 1 23  ? -24.08200 9.75400  -3.98900  1.000 76.71709  ? 23  GLN A CG   1 
ATOM   299  C CD   . GLN A 1 23  ? -25.18400 8.97700  -3.22900  1.000 103.37555 ? 23  GLN A CD   1 
ATOM   300  O OE1  . GLN A 1 23  ? -24.98400 8.55300  -2.07900  1.000 92.58478  ? 23  GLN A OE1  1 
ATOM   301  N NE2  . GLN A 1 23  ? -26.35500 8.80800  -3.86900  1.000 96.23785  ? 23  GLN A NE2  1 
ATOM   302  H H    . GLN A 1 23  ? -23.66700 13.07800 -4.72400  1.000 45.38000  ? 23  GLN A H    1 
ATOM   303  H HA   . GLN A 1 23  ? -25.65900 11.70200 -3.73000  1.000 45.78000  ? 23  GLN A HA   1 
ATOM   304  H HB2  . GLN A 1 23  ? -22.93400 11.44700 -3.75200  1.000 49.49000  ? 23  GLN A HB2  1 
ATOM   305  H HB3  . GLN A 1 23  ? -23.56000 10.93600 -2.38700  1.000 49.49000  ? 23  GLN A HB3  1 
ATOM   306  H HG2  . GLN A 1 23  ? -24.39800 9.91700  -4.89100  1.000 92.69000  ? 23  GLN A HG2  1 
ATOM   307  H HG3  . GLN A 1 23  ? -23.28600 9.20000  -4.01200  1.000 92.69000  ? 23  GLN A HG3  1 
ATOM   308  H HE21 . GLN A 1 23  ? -26.45900 9.11800  -4.66400  1.000 116.11000 ? 23  GLN A HE21 1 
ATOM   309  H HE22 . GLN A 1 23  ? -26.99700 8.38400  -3.48600  1.000 116.11000 ? 23  GLN A HE22 1 
ATOM   310  N N    . LYS A 1 24  ? -24.33000 13.78000 -1.69200  1.000 35.51215  ? 24  LYS A N    1 
ATOM   311  C CA   . LYS A 1 24  ? -24.59900 14.41900 -0.41100  1.000 36.88600  ? 24  LYS A CA   1 
ATOM   312  C C    . LYS A 1 24  ? -25.93000 15.15900 -0.46800  1.000 28.47710  ? 24  LYS A C    1 
ATOM   313  O O    . LYS A 1 24  ? -26.71500 15.13200 0.49700   1.000 31.14584  ? 24  LYS A O    1 
ATOM   314  C CB   . LYS A 1 24  ? -23.46800 15.38000 -0.03100  1.000 44.79221  ? 24  LYS A CB   1 
ATOM   315  C CG   . LYS A 1 24  ? -22.10500 14.73200 0.11800   1.000 78.31465  ? 24  LYS A CG   1 
ATOM   316  C CD   . LYS A 1 24  ? -20.94400 15.73800 0.04600   1.000 90.76088  ? 24  LYS A CD   1 
ATOM   317  C CE   . LYS A 1 24  ? -19.58700 15.01400 0.17000   1.000 74.32996  ? 24  LYS A CE   1 
ATOM   318  N NZ   . LYS A 1 24  ? -18.51300 15.96500 0.59700   1.000 90.13712  ? 24  LYS A NZ   1 
ATOM   319  H H    . LYS A 1 24  ? -23.64800 14.07800 -2.12200  1.000 43.24000  ? 24  LYS A H    1 
ATOM   320  H HA   . LYS A 1 24  ? -24.66100 13.73800 0.27700   1.000 44.89000  ? 24  LYS A HA   1 
ATOM   321  H HB2  . LYS A 1 24  ? -23.39600 16.06200 -0.71700  1.000 54.38000  ? 24  LYS A HB2  1 
ATOM   322  H HB3  . LYS A 1 24  ? -23.68800 15.79200 0.81900   1.000 54.38000  ? 24  LYS A HB3  1 
ATOM   323  H HG2  . LYS A 1 24  ? -22.06200 14.29500 0.98300   1.000 94.61000  ? 24  LYS A HG2  1 
ATOM   324  H HG3  . LYS A 1 24  ? -21.98300 14.07700 -0.58400  1.000 94.61000  ? 24  LYS A HG3  1 
ATOM   325  H HD2  . LYS A 1 24  ? -20.96900 16.19900 -0.80700  1.000 109.54000 ? 24  LYS A HD2  1 
ATOM   326  H HD3  . LYS A 1 24  ? -21.02100 16.37200 0.77600   1.000 109.54000 ? 24  LYS A HD3  1 
ATOM   327  H HE2  . LYS A 1 24  ? -19.65600 14.31200 0.83500   1.000 89.82000  ? 24  LYS A HE2  1 
ATOM   328  H HE3  . LYS A 1 24  ? -19.34100 14.64100 -0.69100  1.000 89.82000  ? 24  LYS A HE3  1 
ATOM   329  H HZ1  . LYS A 1 24  ? -17.73600 15.53600 0.66500   1.000 108.79000 ? 24  LYS A HZ1  1 
ATOM   330  H HZ2  . LYS A 1 24  ? -18.43100 16.61900 -0.00100  1.000 108.79000 ? 24  LYS A HZ2  1 
ATOM   331  H HZ3  . LYS A 1 24  ? -18.71800 16.32000 1.38700   1.000 108.79000 ? 24  LYS A HZ3  1 
ATOM   332  N N    . GLN A 1 25  ? -26.19500 15.83700 -1.58400  1.000 30.60367  ? 25  GLN A N    1 
ATOM   333  C CA   . GLN A 1 25  ? -27.45200 16.56100 -1.69300  1.000 21.28676  ? 25  GLN A CA   1 
ATOM   334  C C    . GLN A 1 25  ? -28.60900 15.59100 -1.58900  1.000 22.96328  ? 25  GLN A C    1 
ATOM   335  O O    . GLN A 1 25  ? -29.70800 15.94100 -1.12000  1.000 29.00874  ? 25  GLN A O    1 
ATOM   336  C CB   . GLN A 1 25  ? -27.55500 17.31000 -3.00800  1.000 26.12418  ? 25  GLN A CB   1 
ATOM   337  C CG   . GLN A 1 25  ? -26.54000 18.41900 -3.23700  1.000 29.99570  ? 25  GLN A CG   1 
ATOM   338  C CD   . GLN A 1 25  ? -26.95500 19.32600 -4.37000  1.000 22.26056  ? 25  GLN A CD   1 
ATOM   339  O OE1  . GLN A 1 25  ? -27.33200 18.87600 -5.48600  1.000 27.02692  ? 25  GLN A OE1  1 
ATOM   340  N NE2  . GLN A 1 25  ? -26.86700 20.62300 -4.13800  1.000 32.15912  ? 25  GLN A NE2  1 
ATOM   341  H H    . GLN A 1 25  ? -25.68000 15.89100 -2.27000  1.000 37.35000  ? 25  GLN A H    1 
ATOM   342  H HA   . GLN A 1 25  ? -27.52100 17.20100 -0.96800  1.000 26.17000  ? 25  GLN A HA   1 
ATOM   343  H HB2  . GLN A 1 25  ? -27.45000 16.67100 -3.73000  1.000 31.98000  ? 25  GLN A HB2  1 
ATOM   344  H HB3  . GLN A 1 25  ? -28.43600 17.71200 -3.06000  1.000 31.98000  ? 25  GLN A HB3  1 
ATOM   345  H HG2  . GLN A 1 25  ? -26.47100 18.95400 -2.43300  1.000 36.62000  ? 25  GLN A HG2  1 
ATOM   346  H HG3  . GLN A 1 25  ? -25.68000 18.03100 -3.45800  1.000 36.62000  ? 25  GLN A HG3  1 
ATOM   347  H HE21 . GLN A 1 25  ? -26.60200 20.90600 -3.37000  1.000 39.22000  ? 25  GLN A HE21 1 
ATOM   348  H HE22 . GLN A 1 25  ? -27.08800 21.18500 -4.75000  1.000 39.22000  ? 25  GLN A HE22 1 
ATOM   349  N N    . ASN A 1 26  ? -28.43200 14.39600 -2.15200  1.000 29.00085  ? 26  ASN A N    1 
ATOM   350  C CA   . ASN A 1 26  ? -29.56300 13.46800 -2.16200  1.000 22.18950  ? 26  ASN A CA   1 
ATOM   351  C C    . ASN A 1 26  ? -29.80300 12.88600 -0.77400  1.000 23.14751  ? 26  ASN A C    1 
ATOM   352  O O    . ASN A 1 26  ? -30.95400 12.72700 -0.34000  1.000 33.94091  ? 26  ASN A O    1 
ATOM   353  C CB   . ASN A 1 26  ? -29.33000 12.36000 -3.17700  1.000 23.63178  ? 26  ASN A CB   1 
ATOM   354  C CG   . ASN A 1 26  ? -29.28400 12.86700 -4.58100  1.000 28.15864  ? 26  ASN A CG   1 
ATOM   355  O OD1  . ASN A 1 26  ? -29.73000 13.99500 -4.86800  1.000 31.60379  ? 26  ASN A OD1  1 
ATOM   356  N ND2  . ASN A 1 26  ? -28.80000 12.02100 -5.49800  1.000 36.27277  ? 26  ASN A ND2  1 
ATOM   357  H H    . ASN A 1 26  ? -27.70800 14.10900 -2.51700  1.000 35.43000  ? 26  ASN A H    1 
ATOM   358  H HA   . ASN A 1 26  ? -30.36300 13.94900 -2.42600  1.000 27.26000  ? 26  ASN A HA   1 
ATOM   359  H HB2  . ASN A 1 26  ? -28.48300 11.92900 -2.98600  1.000 28.98000  ? 26  ASN A HB2  1 
ATOM   360  H HB3  . ASN A 1 26  ? -30.05300 11.71600 -3.11400  1.000 28.98000  ? 26  ASN A HB3  1 
ATOM   361  H HD21 . ASN A 1 26  ? -28.51100 11.24700 -5.25900  1.000 44.16000  ? 26  ASN A HD21 1 
ATOM   362  H HD22 . ASN A 1 26  ? -28.75600 12.26000 -6.32300  1.000 44.16000  ? 26  ASN A HD22 1 
ATOM   363  N N    . ASN A 1 27  ? -28.73900 12.62600 -0.03500  1.000 33.80932  ? 27  ASN A N    1 
ATOM   364  C CA   . ASN A 1 27  ? -28.91100 12.22700 1.35600   1.000 32.73287  ? 27  ASN A CA   1 
ATOM   365  C C    . ASN A 1 27  ? -29.55100 13.33500 2.19300   1.000 29.38510  ? 27  ASN A C    1 
ATOM   366  O O    . ASN A 1 27  ? -30.48500 13.07500 2.95900   1.000 35.90957  ? 27  ASN A O    1 
ATOM   367  C CB   . ASN A 1 27  ? -27.56900 11.79600 1.92400   1.000 43.14728  ? 27  ASN A CB   1 
ATOM   368  C CG   . ASN A 1 27  ? -27.05200 10.50300 1.27500   1.000 44.31321  ? 27  ASN A CG   1 
ATOM   369  O OD1  . ASN A 1 27  ? -27.83100 9.61400  0.91100   1.000 57.65428  ? 27  ASN A OD1  1 
ATOM   370  N ND2  . ASN A 1 27  ? -25.74000 10.41600 1.09800   1.000 63.59973  ? 27  ASN A ND2  1 
ATOM   371  H H    . ASN A 1 27  ? -27.92300 12.67000 -0.30300  1.000 41.20000  ? 27  ASN A H    1 
ATOM   372  H HA   . ASN A 1 27  ? -29.50300 11.45900 1.38600   1.000 39.91000  ? 27  ASN A HA   1 
ATOM   373  H HB2  . ASN A 1 27  ? -26.91700 12.49600 1.76400   1.000 52.40000  ? 27  ASN A HB2  1 
ATOM   374  H HB3  . ASN A 1 27  ? -27.66300 11.63900 2.87700   1.000 52.40000  ? 27  ASN A HB3  1 
ATOM   375  H HD21 . ASN A 1 27  ? -25.22800 11.05600 1.35800   1.000 76.94000  ? 27  ASN A HD21 1 
ATOM   376  H HD22 . ASN A 1 27  ? -25.40100 9.71300  0.73600   1.000 76.94000  ? 27  ASN A HD22 1 
ATOM   377  N N    . LEU A 1 28  ? -29.10300 14.58200 2.03100   1.000 30.94318  ? 28  LEU A N    1 
ATOM   378  C CA   . LEU A 1 28  ? -29.74900 15.65400 2.78400   1.000 23.49492  ? 28  LEU A CA   1 
ATOM   379  C C    . LEU A 1 28  ? -31.23700 15.73900 2.45700   1.000 25.37409  ? 28  LEU A C    1 
ATOM   380  O O    . LEU A 1 28  ? -32.07000 16.03000 3.32300   1.000 25.81889  ? 28  LEU A O    1 
ATOM   381  C CB   . LEU A 1 28  ? -29.08100 16.98100 2.47300   1.000 27.61384  ? 28  LEU A CB   1 
ATOM   382  C CG   . LEU A 1 28  ? -27.77200 17.16000 3.23100   1.000 32.12490  ? 28  LEU A CG   1 
ATOM   383  C CD1  . LEU A 1 28  ? -27.14700 18.41800 2.72900   1.000 40.29430  ? 28  LEU A CD1  1 
ATOM   384  C CD2  . LEU A 1 28  ? -28.03200 17.22000 4.71900   1.000 34.59625  ? 28  LEU A CD2  1 
ATOM   385  H H    . LEU A 1 28  ? -28.45800 14.82400 1.51700   1.000 37.76000  ? 28  LEU A H    1 
ATOM   386  H HA   . LEU A 1 28  ? -29.66500 15.47000 3.73100   1.000 28.82000  ? 28  LEU A HA   1 
ATOM   387  H HB2  . LEU A 1 28  ? -28.88800 17.02400 1.52300   1.000 33.76000  ? 28  LEU A HB2  1 
ATOM   388  H HB3  . LEU A 1 28  ? -29.67700 17.70400 2.72400   1.000 33.76000  ? 28  LEU A HB3  1 
ATOM   389  H HG   . LEU A 1 28  ? -27.17700 16.41700 3.04400   1.000 39.18000  ? 28  LEU A HG   1 
ATOM   390  H HD11 . LEU A 1 28  ? -26.31400 18.56700 3.20300   1.000 48.98000  ? 28  LEU A HD11 1 
ATOM   391  H HD12 . LEU A 1 28  ? -26.97500 18.32800 1.77900   1.000 48.98000  ? 28  LEU A HD12 1 
ATOM   392  H HD13 . LEU A 1 28  ? -27.75500 19.15700 2.88700   1.000 48.98000  ? 28  LEU A HD13 1 
ATOM   393  H HD21 . LEU A 1 28  ? -28.85100 17.71500 4.87700   1.000 42.14000  ? 28  LEU A HD21 1 
ATOM   394  H HD22 . LEU A 1 28  ? -27.28800 17.66800 5.15100   1.000 42.14000  ? 28  LEU A HD22 1 
ATOM   395  H HD23 . LEU A 1 28  ? -28.11900 16.31800 5.06300   1.000 42.14000  ? 28  LEU A HD23 1 
ATOM   396  N N    . LEU A 1 29  ? -31.58100 15.53600 1.20200   1.000 24.89509  ? 29  LEU A N    1 
ATOM   397  C CA   . LEU A 1 29  ? -32.96900 15.62800 0.80300   1.000 22.09475  ? 29  LEU A CA   1 
ATOM   398  C C    . LEU A 1 29  ? -33.76000 14.56200 1.50500   1.000 22.40005  ? 29  LEU A C    1 
ATOM   399  O O    . LEU A 1 29  ? -34.89200 14.79100 1.93200   1.000 27.11115  ? 29  LEU A O    1 
ATOM   400  C CB   . LEU A 1 29  ? -33.08500 15.48200 -0.69800  1.000 25.41884  ? 29  LEU A CB   1 
ATOM   401  C CG   . LEU A 1 29  ? -34.46600 15.33700 -1.28500  1.000 24.49504  ? 29  LEU A CG   1 
ATOM   402  C CD1  . LEU A 1 29  ? -35.26900 16.55300 -0.92600  1.000 26.60582  ? 29  LEU A CD1  1 
ATOM   403  C CD2  . LEU A 1 29  ? -34.46200 15.19300 -2.80600  1.000 35.46741  ? 29  LEU A CD2  1 
ATOM   404  H H    . LEU A 1 29  ? -31.03500 15.34500 0.56500   1.000 30.50000  ? 29  LEU A H    1 
ATOM   405  H HA   . LEU A 1 29  ? -33.32300 16.49400 1.05800   1.000 27.14000  ? 29  LEU A HA   1 
ATOM   406  H HB2  . LEU A 1 29  ? -32.68300 16.26400 -1.10700  1.000 31.13000  ? 29  LEU A HB2  1 
ATOM   407  H HB3  . LEU A 1 29  ? -32.58300 14.69500 -0.96000  1.000 31.13000  ? 29  LEU A HB3  1 
ATOM   408  H HG   . LEU A 1 29  ? -34.90300 14.55800 -0.90800  1.000 30.02000  ? 29  LEU A HG   1 
ATOM   409  H HD11 . LEU A 1 29  ? -35.42900 16.55700 0.03100   1.000 32.55000  ? 29  LEU A HD11 1 
ATOM   410  H HD12 . LEU A 1 29  ? -36.11400 16.52300 -1.40200  1.000 32.55000  ? 29  LEU A HD12 1 
ATOM   411  H HD13 . LEU A 1 29  ? -34.77300 17.34600 -1.18300  1.000 32.55000  ? 29  LEU A HD13 1 
ATOM   412  H HD21 . LEU A 1 29  ? -34.06500 15.98700 -3.19700  1.000 43.19000  ? 29  LEU A HD21 1 
ATOM   413  H HD22 . LEU A 1 29  ? -35.37600 15.09200 -3.11600  1.000 43.19000  ? 29  LEU A HD22 1 
ATOM   414  H HD23 . LEU A 1 29  ? -33.94200 14.41000 -3.04700  1.000 43.19000  ? 29  LEU A HD23 1 
ATOM   415  N N    . ARG A 1 30  ? -33.18000 13.37900 1.65200   1.000 23.20805  ? 30  ARG A N    1 
ATOM   416  C CA   . ARG A 1 30  ? -33.91500 12.32100 2.34200   1.000 27.66911  ? 30  ARG A CA   1 
ATOM   417  C C    . ARG A 1 30  ? -34.09100 12.64000 3.82000   1.000 28.41920  ? 30  ARG A C    1 
ATOM   418  O O    . ARG A 1 30  ? -35.11500 12.29000 4.42300   1.000 29.35878  ? 30  ARG A O    1 
ATOM   419  C CB   . ARG A 1 30  ? -33.21000 10.97600 2.20000   1.000 40.70751  ? 30  ARG A CB   1 
ATOM   420  C CG   . ARG A 1 30  ? -33.28000 10.37300 0.81200   1.000 51.92991  ? 30  ARG A CG   1 
ATOM   421  C CD   . ARG A 1 30  ? -32.25600 9.21800  0.63300   1.000 63.37865  ? 30  ARG A CD   1 
ATOM   422  N NE   . ARG A 1 30  ? -32.05400 8.88400  -0.77700  1.000 90.65034  ? 30  ARG A NE   1 
ATOM   423  C CZ   . ARG A 1 30  ? -30.88900 8.92700  -1.41700  1.000 62.67594  ? 30  ARG A CZ   1 
ATOM   424  N NH1  . ARG A 1 30  ? -29.75100 9.16200  -0.77500  1.000 63.34707  ? 30  ARG A NH1  1 
ATOM   425  N NH2  . ARG A 1 30  ? -30.86800 8.72800  -2.73700  1.000 73.33774  ? 30  ARG A NH2  1 
ATOM   426  H H    . ARG A 1 30  ? -32.39400 13.16500 1.37500   1.000 28.48000  ? 30  ARG A H    1 
ATOM   427  H HA   . ARG A 1 30  ? -34.79700 12.24000 1.94600   1.000 33.83000  ? 30  ARG A HA   1 
ATOM   428  H HB2  . ARG A 1 30  ? -32.27300 11.09200 2.42400   1.000 49.48000  ? 30  ARG A HB2  1 
ATOM   429  H HB3  . ARG A 1 30  ? -33.61700 10.34600 2.81500   1.000 49.48000  ? 30  ARG A HB3  1 
ATOM   430  H HG2  . ARG A 1 30  ? -34.16900 10.01500 0.66400   1.000 62.94000  ? 30  ARG A HG2  1 
ATOM   431  H HG3  . ARG A 1 30  ? -33.08100 11.05900 0.15600   1.000 62.94000  ? 30  ARG A HG3  1 
ATOM   432  H HD2  . ARG A 1 30  ? -31.41300 9.48600  1.02600   1.000 76.68000  ? 30  ARG A HD2  1 
ATOM   433  H HD3  . ARG A 1 30  ? -32.59300 8.42700  1.08200   1.000 76.68000  ? 30  ARG A HD3  1 
ATOM   434  H HE   . ARG A 1 30  ? -32.74400 8.64000  -1.22800  1.000 109.41000 ? 30  ARG A HE   1 
ATOM   435  H HH11 . ARG A 1 30  ? -29.74600 9.29600  0.07300   1.000 76.64000  ? 30  ARG A HH11 1 
ATOM   436  H HH12 . ARG A 1 30  ? -29.01100 9.18100  -1.21300  1.000 76.64000  ? 30  ARG A HH12 1 
ATOM   437  H HH21 . ARG A 1 30  ? -31.60000 8.57100  -3.16000  1.000 88.63000  ? 30  ARG A HH21 1 
ATOM   438  H HH22 . ARG A 1 30  ? -30.12100 8.74500  -3.16300  1.000 88.63000  ? 30  ARG A HH22 1 
ATOM   439  N N    . LYS A 1 31  ? -33.10200 13.28200 4.43000   1.000 32.83025  ? 31  LYS A N    1 
ATOM   440  C CA   . LYS A 1 31  ? -33.26700 13.70200 5.81900   1.000 29.14297  ? 31  LYS A CA   1 
ATOM   441  C C    . LYS A 1 31  ? -34.31000 14.81700 5.95800   1.000 22.90011  ? 31  LYS A C    1 
ATOM   442  O O    . LYS A 1 31  ? -35.08300 14.83100 6.92500   1.000 28.59290  ? 31  LYS A O    1 
ATOM   443  C CB   . LYS A 1 31  ? -31.93000 14.14300 6.37800   1.000 30.90897  ? 31  LYS A CB   1 
ATOM   444  C CG   . LYS A 1 31  ? -30.90500 13.00700 6.59200   1.000 33.10134  ? 31  LYS A CG   1 
ATOM   445  C CD   . LYS A 1 31  ? -29.51000 13.64600 6.66800   1.000 52.02203  ? 31  LYS A CD   1 
ATOM   446  C CE   . LYS A 1 31  ? -28.46000 12.89500 7.49100   1.000 60.59148  ? 31  LYS A CE   1 
ATOM   447  N NZ   . LYS A 1 31  ? -27.24300 13.81100 7.68000   1.000 57.83588  ? 31  LYS A NZ   1 
ATOM   448  H H    . LYS A 1 31  ? -32.34500 13.48300 4.07500   1.000 40.02000  ? 31  LYS A H    1 
ATOM   449  H HA   . LYS A 1 31  ? -33.57200 12.94400 6.34100   1.000 35.60000  ? 31  LYS A HA   1 
ATOM   450  H HB2  . LYS A 1 31  ? -31.53500 14.78200 5.76400   1.000 37.72000  ? 31  LYS A HB2  1 
ATOM   451  H HB3  . LYS A 1 31  ? -32.08000 14.56800 7.23700   1.000 37.72000  ? 31  LYS A HB3  1 
ATOM   452  H HG2  . LYS A 1 31  ? -31.08800 12.54800 7.42600   1.000 40.35000  ? 31  LYS A HG2  1 
ATOM   453  H HG3  . LYS A 1 31  ? -30.93000 12.39200 5.84300   1.000 40.35000  ? 31  LYS A HG3  1 
ATOM   454  H HD2  . LYS A 1 31  ? -29.16400 13.72700 5.76600   1.000 63.06000  ? 31  LYS A HD2  1 
ATOM   455  H HD3  . LYS A 1 31  ? -29.60200 14.53000 7.05700   1.000 63.06000  ? 31  LYS A HD3  1 
ATOM   456  H HE2  . LYS A 1 31  ? -28.82200 12.67200 8.36300   1.000 73.34000  ? 31  LYS A HE2  1 
ATOM   457  H HE3  . LYS A 1 31  ? -28.18000 12.09600 7.01800   1.000 73.34000  ? 31  LYS A HE3  1 
ATOM   458  H HZ1  . LYS A 1 31  ? -26.90200 14.03100 6.88800   1.000 70.03000  ? 31  LYS A HZ1  1 
ATOM   459  H HZ2  . LYS A 1 31  ? -27.48500 14.55300 8.10700   1.000 70.03000  ? 31  LYS A HZ2  1 
ATOM   460  H HZ3  . LYS A 1 31  ? -26.61900 13.39300 8.15700   1.000 70.03000  ? 31  LYS A HZ3  1 
ATOM   461  N N    . ILE A 1 32  ? -34.38100 15.73400 5.00600   1.000 23.34490  ? 32  ILE A N    1 
ATOM   462  C CA   . ILE A 1 32  ? -35.40500 16.77100 5.06300   1.000 16.07298  ? 32  ILE A CA   1 
ATOM   463  C C    . ILE A 1 32  ? -36.78500 16.17900 4.81100   1.000 17.51526  ? 32  ILE A C    1 
ATOM   464  O O    . ILE A 1 32  ? -37.73800 16.46400 5.54900   1.000 23.44492  ? 32  ILE A O    1 
ATOM   465  C CB   . ILE A 1 32  ? -35.03600 17.83300 4.03500   1.000 16.22300  ? 32  ILE A CB   1 
ATOM   466  C CG1  . ILE A 1 32  ? -33.75100 18.51200 4.46800   1.000 23.92655  ? 32  ILE A CG1  1 
ATOM   467  C CG2  . ILE A 1 32  ? -36.02200 18.94700 3.97400   1.000 18.77594  ? 32  ILE A CG2  1 
ATOM   468  C CD1  . ILE A 1 32  ? -33.07100 19.25200 3.34100   1.000 24.28712  ? 32  ILE A CD1  1 
ATOM   469  H H    . ILE A 1 32  ? -33.85800 15.78100 4.32500   1.000 28.64000  ? 32  ILE A H    1 
ATOM   470  H HA   . ILE A 1 32  ? -35.40200 17.18000 5.94200   1.000 19.91000  ? 32  ILE A HA   1 
ATOM   471  H HB   . ILE A 1 32  ? -34.92600 17.43200 3.15900   1.000 20.09000  ? 32  ILE A HB   1 
ATOM   472  H HG12 . ILE A 1 32  ? -33.95100 19.15100 5.16700   1.000 29.34000  ? 32  ILE A HG12 1 
ATOM   473  H HG13 . ILE A 1 32  ? -33.12900 17.84700 4.80000   1.000 29.34000  ? 32  ILE A HG13 1 
ATOM   474  H HG21 . ILE A 1 32  ? -35.70800 19.62300 3.35500   1.000 23.16000  ? 32  ILE A HG21 1 
ATOM   475  H HG22 . ILE A 1 32  ? -36.87300 18.59800 3.66800   1.000 23.16000  ? 32  ILE A HG22 1 
ATOM   476  H HG23 . ILE A 1 32  ? -36.12400 19.33100 4.85900   1.000 23.16000  ? 32  ILE A HG23 1 
ATOM   477  H HD11 . ILE A 1 32  ? -32.15900 19.45400 3.60300   1.000 29.77000  ? 32  ILE A HD11 1 
ATOM   478  H HD12 . ILE A 1 32  ? -33.07100 18.69100 2.55000   1.000 29.77000  ? 32  ILE A HD12 1 
ATOM   479  H HD13 . ILE A 1 32  ? -33.55300 20.07400 3.16300   1.000 29.77000  ? 32  ILE A HD13 1 
ATOM   480  N N    . GLU A 1 33  ? -36.91000 15.29000 3.82900   1.000 21.42889  ? 33  GLU A N    1 
ATOM   481  C CA   . GLU A 1 33  ? -38.18300 14.59900 3.63900   1.000 20.00240  ? 33  GLU A CA   1 
ATOM   482  C C    . GLU A 1 33  ? -38.62200 13.85900 4.89900   1.000 20.36560  ? 33  GLU A C    1 
ATOM   483  O O    . GLU A 1 33  ? -39.82000 13.77200 5.20000   1.000 27.14799  ? 33  GLU A O    1 
ATOM   484  C CB   . GLU A 1 33  ? -38.09200 13.61100 2.47500   1.000 24.76876  ? 33  GLU A CB   1 
ATOM   485  C CG   . GLU A 1 33  ? -37.84000 14.22300 1.09700   1.000 42.34192  ? 33  GLU A CG   1 
ATOM   486  C CD   . GLU A 1 33  ? -37.61400 13.18600 -0.02800  1.000 48.62688  ? 33  GLU A CD   1 
ATOM   487  O OE1  . GLU A 1 33  ? -37.35700 12.00000 0.29200   1.000 56.58836  ? 33  GLU A OE1  1 
ATOM   488  O OE2  . GLU A 1 33  ? -37.68700 13.57700 -1.23700  1.000 55.10398  ? 33  GLU A OE2  1 
ATOM   489  H H    . GLU A 1 33  ? -36.29100 15.07300 3.27300   1.000 26.34000  ? 33  GLU A H    1 
ATOM   490  H HA   . GLU A 1 33  ? -38.86600 15.25300 3.42300   1.000 24.63000  ? 33  GLU A HA   1 
ATOM   491  H HB2  . GLU A 1 33  ? -37.36600 12.99400 2.65500   1.000 30.35000  ? 33  GLU A HB2  1 
ATOM   492  H HB3  . GLU A 1 33  ? -38.92700 13.12000 2.42500   1.000 30.35000  ? 33  GLU A HB3  1 
ATOM   493  H HG2  . GLU A 1 33  ? -38.61400 14.75300 0.85100   1.000 51.44000  ? 33  GLU A HG2  1 
ATOM   494  H HG3  . GLU A 1 33  ? -37.05900 14.79300 1.14000   1.000 51.44000  ? 33  GLU A HG3  1 
ATOM   495  N N    . ALA A 1 34  ? -37.69800 13.28100 5.62800   1.000 20.84987  ? 34  ALA A N    1 
ATOM   496  C CA   . ALA A 1 34  ? -38.09400 12.58000 6.83900   1.000 23.93708  ? 34  ALA A CA   1 
ATOM   497  C C    . ALA A 1 34  ? -38.65300 13.53000 7.88700   1.000 26.87164  ? 34  ALA A C    1 
ATOM   498  O O    . ALA A 1 34  ? -39.65700 13.23700 8.55800   1.000 29.68251  ? 34  ALA A O    1 
ATOM   499  C CB   . ALA A 1 34  ? -36.90700 11.81500 7.40600   1.000 27.88492  ? 34  ALA A CB   1 
ATOM   500  H H    . ALA A 1 34  ? -36.85500 13.27400 5.45700   1.000 25.65000  ? 34  ALA A H    1 
ATOM   501  H HA   . ALA A 1 34  ? -38.78600 11.93700 6.61900   1.000 29.35000  ? 34  ALA A HA   1 
ATOM   502  H HB1  . ALA A 1 34  ? -37.18600 11.35300 8.21200   1.000 34.09000  ? 34  ALA A HB1  1 
ATOM   503  H HB2  . ALA A 1 34  ? -36.60100 11.17400 6.74600   1.000 34.09000  ? 34  ALA A HB2  1 
ATOM   504  H HB3  . ALA A 1 34  ? -36.19700 12.44300 7.61200   1.000 34.09000  ? 34  ALA A HB3  1 
ATOM   505  N N    . ILE A 1 35  ? -38.02800 14.67400 8.06900   1.000 23.07908  ? 35  ILE A N    1 
ATOM   506  C CA   . ILE A 1 35  ? -38.62600 15.63100 8.98100   1.000 24.74507  ? 35  ILE A CA   1 
ATOM   507  C C    . ILE A 1 35  ? -39.98500 16.04100 8.47900   1.000 27.03745  ? 35  ILE A C    1 
ATOM   508  O O    . ILE A 1 35  ? -40.93900 16.13500 9.25800   1.000 29.02980  ? 35  ILE A O    1 
ATOM   509  C CB   . ILE A 1 35  ? -37.70000 16.83000 9.16000   1.000 25.80836  ? 35  ILE A CB   1 
ATOM   510  C CG1  . ILE A 1 35  ? -36.50300 16.34100 9.94000   1.000 26.79269  ? 35  ILE A CG1  1 
ATOM   511  C CG2  . ILE A 1 35  ? -38.38600 17.89600 9.97500   1.000 23.78706  ? 35  ILE A CG2  1 
ATOM   512  C CD1  . ILE A 1 35  ? -35.40400 17.27100 10.01900  1.000 31.85908  ? 35  ILE A CD1  1 
ATOM   513  H H    . ILE A 1 35  ? -37.29100 14.91600 7.69800   1.000 28.32000  ? 35  ILE A H    1 
ATOM   514  H HA   . ILE A 1 35  ? -38.74200 15.21100 9.84800   1.000 30.32000  ? 35  ILE A HA   1 
ATOM   515  H HB   . ILE A 1 35  ? -37.42600 17.18100 8.29900   1.000 31.60000  ? 35  ILE A HB   1 
ATOM   516  H HG12 . ILE A 1 35  ? -36.78600 16.14600 10.84700  1.000 32.78000  ? 35  ILE A HG12 1 
ATOM   517  H HG13 . ILE A 1 35  ? -36.16700 15.53200 9.52400   1.000 32.78000  ? 35  ILE A HG13 1 
ATOM   518  H HG21 . ILE A 1 35  ? -39.06900 18.32200 9.43400   1.000 29.17000  ? 35  ILE A HG21 1 
ATOM   519  H HG22 . ILE A 1 35  ? -37.73400 18.55700 10.25200  1.000 29.17000  ? 35  ILE A HG22 1 
ATOM   520  H HG23 . ILE A 1 35  ? -38.79000 17.48500 10.75500  1.000 29.17000  ? 35  ILE A HG23 1 
ATOM   521  H HD11 . ILE A 1 35  ? -34.61200 16.79700 10.31700  1.000 38.86000  ? 35  ILE A HD11 1 
ATOM   522  H HD12 . ILE A 1 35  ? -35.25000 17.65200 9.14000   1.000 38.86000  ? 35  ILE A HD12 1 
ATOM   523  H HD13 . ILE A 1 35  ? -35.62600 17.97300 10.65000  1.000 38.86000  ? 35  ILE A HD13 1 
ATOM   524  N N    . GLN A 1 36  ? -40.12000 16.29100 7.18800   1.000 36.31225  ? 36  GLN A N    1 
ATOM   525  C CA   . GLN A 1 36  ? -41.42300 16.72700 6.68900   1.000 24.89509  ? 36  GLN A CA   1 
ATOM   526  C C    . GLN A 1 36  ? -42.50900 15.70100 7.02200   1.000 28.62712  ? 36  GLN A C    1 
ATOM   527  O O    . GLN A 1 36  ? -43.65900 16.05300 7.31900   1.000 38.89414  ? 36  GLN A O    1 
ATOM   528  C CB   . GLN A 1 36  ? -41.36900 16.94300 5.16900   1.000 27.95072  ? 36  GLN A CB   1 
ATOM   529  C CG   . GLN A 1 36  ? -42.68800 17.31900 4.56500   1.000 38.95730  ? 36  GLN A CG   1 
ATOM   530  C CD   . GLN A 1 36  ? -42.75900 17.06600 3.06900   1.000 36.33594  ? 36  GLN A CD   1 
ATOM   531  O OE1  . GLN A 1 36  ? -41.95300 16.29600 2.49400   1.000 28.51131  ? 36  GLN A OE1  1 
ATOM   532  N NE2  . GLN A 1 36  ? -43.74600 17.68300 2.42700   1.000 42.98410  ? 36  GLN A NE2  1 
ATOM   533  H H    . GLN A 1 36  ? -39.50100 16.22100 6.59500   1.000 44.20000  ? 36  GLN A H    1 
ATOM   534  H HA   . GLN A 1 36  ? -41.66100 17.56900 7.10800   1.000 30.50000  ? 36  GLN A HA   1 
ATOM   535  H HB2  . GLN A 1 36  ? -40.74000 17.65600 4.97700   1.000 34.17000  ? 36  GLN A HB2  1 
ATOM   536  H HB3  . GLN A 1 36  ? -41.07200 16.12100 4.74900   1.000 34.17000  ? 36  GLN A HB3  1 
ATOM   537  H HG2  . GLN A 1 36  ? -43.40400 16.81100 4.97200   1.000 47.37000  ? 36  GLN A HG2  1 
ATOM   538  H HG3  . GLN A 1 36  ? -42.83700 18.26600 4.71000   1.000 47.37000  ? 36  GLN A HG3  1 
ATOM   539  H HE21 . GLN A 1 36  ? -44.28200 18.19900 2.85800   1.000 52.21000  ? 36  GLN A HE21 1 
ATOM   540  H HE22 . GLN A 1 36  ? -43.84000 17.57700 1.57900   1.000 52.21000  ? 36  GLN A HE22 1 
ATOM   541  N N    . HIS A 1 37  ? -42.18500 14.43200 6.87000   1.000 34.83576  ? 37  HIS A N    1 
ATOM   542  C CA   . HIS A 1 37  ? -43.15500 13.39000 7.13100   1.000 31.03530  ? 37  HIS A CA   1 
ATOM   543  C C    . HIS A 1 37  ? -43.43600 13.26900 8.61900   1.000 36.45700  ? 37  HIS A C    1 
ATOM   544  O O    . HIS A 1 37  ? -44.57700 13.01700 9.02200   1.000 52.51945  ? 37  HIS A O    1 
ATOM   545  C CB   . HIS A 1 37  ? -42.63900 12.06600 6.54800   1.000 39.85215  ? 37  HIS A CB   1 
ATOM   546  C CG   . HIS A 1 37  ? -42.50900 12.07900 5.04800   1.000 47.71362  ? 37  HIS A CG   1 
ATOM   547  N ND1  . HIS A 1 37  ? -41.63900 11.24900 4.36700   1.000 50.07706  ? 37  HIS A ND1  1 
ATOM   548  C CD2  . HIS A 1 37  ? -43.14300 12.82000 4.10000   1.000 48.90060  ? 37  HIS A CD2  1 
ATOM   549  C CE1  . HIS A 1 37  ? -41.73800 11.48500 3.06700   1.000 60.07562  ? 37  HIS A CE1  1 
ATOM   550  N NE2  . HIS A 1 37  ? -42.64200 12.43400 2.87800   1.000 56.27517  ? 37  HIS A NE2  1 
ATOM   551  H H    . HIS A 1 37  ? -41.41300 14.14800 6.61800   1.000 42.43000  ? 37  HIS A H    1 
ATOM   552  H HA   . HIS A 1 37  ? -43.98700 13.61200 6.68500   1.000 37.87000  ? 37  HIS A HA   1 
ATOM   553  H HB2  . HIS A 1 37  ? -41.76300 11.88100 6.92000   1.000 48.45000  ? 37  HIS A HB2  1 
ATOM   554  H HB3  . HIS A 1 37  ? -43.25500 11.35700 6.78800   1.000 48.45000  ? 37  HIS A HB3  1 
ATOM   555  H HD2  . HIS A 1 37  ? -43.78900 13.47200 4.25000   1.000 59.31000  ? 37  HIS A HD2  1 
ATOM   556  H HE1  . HIS A 1 37  ? -41.25500 11.05400 2.39900   1.000 72.72000  ? 37  HIS A HE1  1 
ATOM   557  H HE2  . HIS A 1 37  ? -42.88100 12.75300 2.11600   1.000 56.28000  ? 37  HIS A HE2  1 
ATOM   558  N N    . LEU A 1 38  ? -42.42000 13.45200 9.45300   1.000 34.27516  ? 38  LEU A N    1 
ATOM   559  C CA   . LEU A 1 38  ? -42.66900 13.45500 10.89000  1.000 37.53871  ? 38  LEU A CA   1 
ATOM   560  C C    . LEU A 1 38  ? -43.72200 14.49200 11.24900  1.000 41.19178  ? 38  LEU A C    1 
ATOM   561  O O    . LEU A 1 38  ? -44.67900 14.20800 11.97900  1.000 52.63526  ? 38  LEU A O    1 
ATOM   562  C CB   . LEU A 1 38  ? -41.37200 13.72500 11.64400  1.000 33.68035  ? 38  LEU A CB   1 
ATOM   563  C CG   . LEU A 1 38  ? -40.59300 12.44300 11.86500  1.000 42.02609  ? 38  LEU A CG   1 
ATOM   564  C CD1  . LEU A 1 38  ? -39.16500 12.78400 12.24400  1.000 34.52782  ? 38  LEU A CD1  1 
ATOM   565  C CD2  . LEU A 1 38  ? -41.34000 11.64600 12.93200  1.000 43.51574  ? 38  LEU A CD2  1 
ATOM   566  H H    . LEU A 1 38  ? -41.60000 13.57300 9.22300   1.000 41.75000  ? 38  LEU A H    1 
ATOM   567  H HA   . LEU A 1 38  ? -43.01000 12.58600 11.14800  1.000 45.67000  ? 38  LEU A HA   1 
ATOM   568  H HB2  . LEU A 1 38  ? -40.82000 14.32800 11.12300  1.000 41.04000  ? 38  LEU A HB2  1 
ATOM   569  H HB3  . LEU A 1 38  ? -41.57600 14.11900 12.50600  1.000 41.04000  ? 38  LEU A HB3  1 
ATOM   570  H HG   . LEU A 1 38  ? -40.58000 11.92500 11.04500  1.000 51.06000  ? 38  LEU A HG   1 
ATOM   571  H HD11 . LEU A 1 38  ? -38.71300 11.97700 12.53300  1.000 42.06000  ? 38  LEU A HD11 1 
ATOM   572  H HD12 . LEU A 1 38  ? -38.71400 13.15800 11.47100  1.000 42.06000  ? 38  LEU A HD12 1 
ATOM   573  H HD13 . LEU A 1 38  ? -39.17700 13.43100 12.96700  1.000 42.06000  ? 38  LEU A HD13 1 
ATOM   574  H HD21 . LEU A 1 38  ? -40.73500 10.99000 13.31100  1.000 52.85000  ? 38  LEU A HD21 1 
ATOM   575  H HD22 . LEU A 1 38  ? -41.64700 12.24900 13.62700  1.000 52.85000  ? 38  LEU A HD22 1 
ATOM   576  H HD23 . LEU A 1 38  ? -42.09700 11.19700 12.52600  1.000 52.85000  ? 38  LEU A HD23 1 
ATOM   577  N N    . LEU A 1 39  ? -43.56800 15.70500 10.72600  1.000 40.18113  ? 39  LEU A N    1 
ATOM   578  C CA   . LEU A 1 39  ? -44.50000 16.77200 11.07300  1.000 47.36621  ? 39  LEU A CA   1 
ATOM   579  C C    . LEU A 1 39  ? -45.88700 16.56200 10.46500  1.000 47.81626  ? 39  LEU A C    1 
ATOM   580  O O    . LEU A 1 39  ? -46.85900 17.16400 10.93700  1.000 49.69017  ? 39  LEU A O    1 
ATOM   581  C CB   . LEU A 1 39  ? -43.91400 18.11600 10.62800  1.000 38.26511  ? 39  LEU A CB   1 
ATOM   582  C CG   . LEU A 1 39  ? -42.54900 18.51000 11.19800  1.000 38.35986  ? 39  LEU A CG   1 
ATOM   583  C CD1  . LEU A 1 39  ? -42.23500 19.96000 10.82100  1.000 35.43320  ? 39  LEU A CD1  1 
ATOM   584  C CD2  . LEU A 1 39  ? -42.53400 18.31000 12.71800  1.000 53.64854  ? 39  LEU A CD2  1 
ATOM   585  H H    . LEU A 1 39  ? -42.94500 15.93300 10.17900  1.000 48.85000  ? 39  LEU A H    1 
ATOM   586  H HA   . LEU A 1 39  ? -44.60600 16.79300 12.03700  1.000 57.47000  ? 39  LEU A HA   1 
ATOM   587  H HB2  . LEU A 1 39  ? -43.82500 18.10000 9.66200   1.000 46.54000  ? 39  LEU A HB2  1 
ATOM   588  H HB3  . LEU A 1 39  ? -44.53900 18.81400 10.87900  1.000 46.54000  ? 39  LEU A HB3  1 
ATOM   589  H HG   . LEU A 1 39  ? -41.86500 17.94100 10.81100  1.000 46.66000  ? 39  LEU A HG   1 
ATOM   590  H HD11 . LEU A 1 39  ? -41.36800 20.19900 11.18400  1.000 43.15000  ? 39  LEU A HD11 1 
ATOM   591  H HD12 . LEU A 1 39  ? -42.22300 20.03900 9.85400   1.000 43.15000  ? 39  LEU A HD12 1 
ATOM   592  H HD13 . LEU A 1 39  ? -42.92000 20.53800 11.19200  1.000 43.15000  ? 39  LEU A HD13 1 
ATOM   593  H HD21 . LEU A 1 39  ? -43.31900 18.73300 13.09900  1.000 65.01000  ? 39  LEU A HD21 1 
ATOM   594  H HD22 . LEU A 1 39  ? -41.73100 18.71500 13.08100  1.000 65.01000  ? 39  LEU A HD22 1 
ATOM   595  H HD23 . LEU A 1 39  ? -42.54200 17.36000 12.91300  1.000 65.01000  ? 39  LEU A HD23 1 
ATOM   596  N N    . GLN A 1 40  ? -46.00200 15.74300 9.42200   1.000 50.85347  ? 40  GLN A N    1 
ATOM   597  C CA   . GLN A 1 40  ? -47.32600 15.36400 8.94300   1.000 49.56121  ? 40  GLN A CA   1 
ATOM   598  C C    . GLN A 1 40  ? -47.97000 14.33600 9.86500   1.000 51.31142  ? 40  GLN A C    1 
ATOM   599  O O    . GLN A 1 40  ? -49.20000 14.26600 9.92900   1.000 82.45462  ? 40  GLN A O    1 
ATOM   600  C CB   . GLN A 1 40  ? -47.25300 14.81100 7.51000   1.000 44.62114  ? 40  GLN A CB   1 
ATOM   601  C CG   . GLN A 1 40  ? -46.86300 15.84300 6.47300   1.000 44.23162  ? 40  GLN A CG   1 
ATOM   602  C CD   . GLN A 1 40  ? -46.49600 15.22200 5.15900   1.000 48.58214  ? 40  GLN A CD   1 
ATOM   603  O OE1  . GLN A 1 40  ? -46.43100 14.00300 5.04400   1.000 56.71469  ? 40  GLN A OE1  1 
ATOM   604  N NE2  . GLN A 1 40  ? -46.23300 16.05800 4.15800   1.000 51.32721  ? 40  GLN A NE2  1 
ATOM   605  H H    . GLN A 1 40  ? -45.34600 15.40100 8.98400   1.000 61.65000  ? 40  GLN A H    1 
ATOM   606  H HA   . GLN A 1 40  ? -47.89400 16.15100 8.93000   1.000 60.10000  ? 40  GLN A HA   1 
ATOM   607  H HB2  . GLN A 1 40  ? -46.59300 14.10000 7.48500   1.000 54.17000  ? 40  GLN A HB2  1 
ATOM   608  H HB3  . GLN A 1 40  ? -48.12400 14.46000 7.26600   1.000 54.17000  ? 40  GLN A HB3  1 
ATOM   609  H HG2  . GLN A 1 40  ? -47.61200 16.44200 6.32400   1.000 53.70000  ? 40  GLN A HG2  1 
ATOM   610  H HG3  . GLN A 1 40  ? -46.09600 16.34200 6.79500   1.000 53.70000  ? 40  GLN A HG3  1 
ATOM   611  H HE21 . GLN A 1 40  ? -46.28700 16.90700 4.28200   1.000 62.22000  ? 40  GLN A HE21 1 
ATOM   612  H HE22 . GLN A 1 40  ? -46.01600 15.74900 3.38500   1.000 62.22000  ? 40  GLN A HE22 1 
ATOM   613  N N    . ARG A 1 41  ? -47.13900 13.55000 10.55500  1.000 76.98555  ? 41  ARG A N    1 
ATOM   614  C CA   . ARG A 1 41  ? -47.63000 12.47800 11.45600  1.000 78.69365  ? 41  ARG A CA   1 
ATOM   615  C C    . ARG A 1 41  ? -48.19600 13.07800 12.75400  1.000 77.31453  ? 41  ARG A C    1 
ATOM   616  O O    . ARG A 1 41  ? -48.95100 12.34100 13.42500  1.000 82.68886  ? 41  ARG A O    1 
ATOM   617  C CB   . ARG A 1 41  ? -46.53500 11.50500 11.76300  1.000 78.16727  ? 41  ARG A CB   1 
ATOM   618  C CG   . ARG A 1 41  ? -46.96600 10.05700 11.21500  1.000 80.84917  ? 41  ARG A CG   1 
ATOM   619  C CD   . ARG A 1 41  ? -47.24500 10.07600 9.70800   1.000 113.03197 ? 41  ARG A CD   1 
ATOM   620  N NE   . ARG A 1 41  ? -46.04700 10.04400 8.92100   1.000 127.92586 ? 41  ARG A NE   1 
ATOM   621  C CZ   . ARG A 1 41  ? -45.93100 10.15200 7.62300   1.000 101.57007 ? 41  ARG A CZ   1 
ATOM   622  N NH1  . ARG A 1 41  ? -46.82500 10.82600 6.93200   1.000 104.02037 ? 41  ARG A NH1  1 
ATOM   623  N NH2  . ARG A 1 41  ? -44.97700 9.52500  6.99100   1.000 88.13952  ? 41  ARG A NH2  1 
ATOM   624  H H    . ARG A 1 41  ? -46.28200 13.61100 10.52400  1.000 76.99000  ? 41  ARG A H    1 
ATOM   625  H HA   . ARG A 1 41  ? -48.36300 12.01100 11.03100  1.000 78.69000  ? 41  ARG A HA   1 
ATOM   626  H HB2  . ARG A 1 41  ? -45.69000 11.77900 11.37400  1.000 78.17000  ? 41  ARG A HB2  1 
ATOM   627  H HB3  . ARG A 1 41  ? -46.49100 11.42300 12.71700  1.000 78.17000  ? 41  ARG A HB3  1 
ATOM   628  H HG2  . ARG A 1 41  ? -46.24800 9.42600  11.38200  1.000 80.85000  ? 41  ARG A HG2  1 
ATOM   629  H HG3  . ARG A 1 41  ? -47.77400 9.77200  11.66900  1.000 80.85000  ? 41  ARG A HG3  1 
ATOM   630  H HD2  . ARG A 1 41  ? -47.76100 9.28600  9.48300   1.000 113.03000 ? 41  ARG A HD2  1 
ATOM   631  H HD3  . ARG A 1 41  ? -47.74000 10.86700 9.45300   1.000 113.03000 ? 41  ARG A HD3  1 
ATOM   632  H HE   . ARG A 1 41  ? -45.31300 9.94100  9.35700   1.000 127.93000 ? 41  ARG A HE   1 
ATOM   633  H HH11 . ARG A 1 41  ? -47.47500 11.21900 7.33600   1.000 104.02000 ? 41  ARG A HH11 1 
ATOM   634  H HH12 . ARG A 1 41  ? -46.74400 10.89700 6.07900   1.000 104.02000 ? 41  ARG A HH12 1 
ATOM   635  H HH21 . ARG A 1 41  ? -44.38600 9.08600  7.43500   1.000 88.14000  ? 41  ARG A HH21 1 
ATOM   636  H HH22 . ARG A 1 41  ? -44.89300 9.61800  6.14000   1.000 88.14000  ? 41  ARG A HH22 1 
ATOM   637  N N    . GLY A 1 42  ? -47.87900 14.33700 13.09900  1.000 74.45893  ? 42  GLY A N    1 
ATOM   638  C CA   . GLY A 1 42  ? -48.35400 14.92300 14.33100  1.000 73.31142  ? 42  GLY A CA   1 
ATOM   639  C C    . GLY A 1 42  ? -47.36500 15.93100 14.87200  1.000 72.93506  ? 42  GLY A C    1 
ATOM   640  O O    . GLY A 1 42  ? -46.39600 16.30500 14.21800  1.000 66.70537  ? 42  GLY A O    1 
ATOM   641  H H    . GLY A 1 42  ? -47.38800 14.86200 12.62700  1.000 86.22000  ? 42  GLY A H    1 
ATOM   642  H HA2  . GLY A 1 42  ? -49.20100 15.37000 14.17600  1.000 84.84000  ? 42  GLY A HA2  1 
ATOM   643  H HA3  . GLY A 1 42  ? -48.48500 14.22800 14.99500  1.000 84.84000  ? 42  GLY A HA3  1 
ATOM   644  N N    . LEU A 1 43  ? -47.64700 16.36800 16.08800  1.000 96.40103  ? 43  LEU A N    1 
ATOM   645  C CA   . LEU A 1 43  ? -46.92900 17.47100 16.69700  1.000 100.47257 ? 43  LEU A CA   1 
ATOM   646  C C    . LEU A 1 43  ? -45.68100 16.93900 17.37700  1.000 99.22242  ? 43  LEU A C    1 
ATOM   647  O O    . LEU A 1 43  ? -45.77600 16.10400 18.28000  1.000 98.39864  ? 43  LEU A O    1 
ATOM   648  C CB   . LEU A 1 43  ? -47.81600 18.18900 17.71200  1.000 112.02659 ? 43  LEU A CB   1 
ATOM   649  C CG   . LEU A 1 43  ? -49.05600 18.90400 17.15700  1.000 130.83674 ? 43  LEU A CG   1 
ATOM   650  C CD1  . LEU A 1 43  ? -49.90700 19.43900 18.33200  1.000 165.25929 ? 43  LEU A CD1  1 
ATOM   651  C CD2  . LEU A 1 43  ? -48.75300 20.02500 16.14500  1.000 141.55908 ? 43  LEU A CD2  1 
ATOM   652  H H    . LEU A 1 43  ? -48.26200 16.03500 16.58900  1.000 116.31000 ? 43  LEU A H    1 
ATOM   653  H HA   . LEU A 1 43  ? -46.66300 18.10500 16.01300  1.000 121.19000 ? 43  LEU A HA   1 
ATOM   654  H HB2  . LEU A 1 43  ? -48.12700 17.53600 18.35800  1.000 135.06000 ? 43  LEU A HB2  1 
ATOM   655  H HB3  . LEU A 1 43  ? -47.27800 18.85700 18.16500  1.000 135.06000 ? 43  LEU A HB3  1 
ATOM   656  H HG   . LEU A 1 43  ? -49.59700 18.24500 16.69400  1.000 157.63000 ? 43  LEU A HG   1 
ATOM   657  H HD11 . LEU A 1 43  ? -50.68900 19.89000 17.97600  1.000 198.94000 ? 43  LEU A HD11 1 
ATOM   658  H HD12 . LEU A 1 43  ? -50.18000 18.69300 18.88900  1.000 198.94000 ? 43  LEU A HD12 1 
ATOM   659  H HD13 . LEU A 1 43  ? -49.37300 20.06100 18.85000  1.000 198.94000 ? 43  LEU A HD13 1 
ATOM   660  H HD21 . LEU A 1 43  ? -49.58800 20.42600 15.85900  1.000 170.50000 ? 43  LEU A HD21 1 
ATOM   661  H HD22 . LEU A 1 43  ? -48.19500 20.69100 16.57500  1.000 170.50000 ? 43  LEU A HD22 1 
ATOM   662  H HD23 . LEU A 1 43  ? -48.28900 19.64600 15.38200  1.000 170.50000 ? 43  LEU A HD23 1 
ATOM   663  N N    . ILE A 1 44  ? -44.50900 17.47900 17.00600  1.000 82.53095  ? 44  ILE A N    1 
ATOM   664  C CA   . ILE A 1 44  ? -43.20200 17.10000 17.62000  1.000 66.57640  ? 44  ILE A CA   1 
ATOM   665  C C    . ILE A 1 44  ? -42.47500 18.40600 17.97400  1.000 55.73563  ? 44  ILE A C    1 
ATOM   666  O O    . ILE A 1 44  ? -41.58100 18.79900 17.20800  1.000 63.60236  ? 44  ILE A O    1 
ATOM   667  C CB   . ILE A 1 44  ? -42.36200 16.23200 16.66500  1.000 67.99499  ? 44  ILE A CB   1 
ATOM   668  C CG1  . ILE A 1 44  ? -43.13800 15.03900 16.11300  1.000 69.76100  ? 44  ILE A CG1  1 
ATOM   669  C CG2  . ILE A 1 44  ? -41.06200 15.79400 17.33900  1.000 60.23617  ? 44  ILE A CG2  1 
ATOM   670  C CD1  . ILE A 1 44  ? -43.64100 14.07200 17.16800  1.000 106.40486 ? 44  ILE A CD1  1 
ATOM   671  H H    . ILE A 1 44  ? -44.43500 18.07700 16.39200  1.000 99.66000  ? 44  ILE A H    1 
ATOM   672  H HA   . ILE A 1 44  ? -43.35700 16.60100 18.43700  1.000 80.52000  ? 44  ILE A HA   1 
ATOM   673  H HB   . ILE A 1 44  ? -42.12000 16.78900 15.90900  1.000 82.22000  ? 44  ILE A HB   1 
ATOM   674  H HG12 . ILE A 1 44  ? -43.90800 15.36700 15.62300  1.000 84.34000  ? 44  ILE A HG12 1 
ATOM   675  H HG13 . ILE A 1 44  ? -42.55800 14.54300 15.51400  1.000 84.34000  ? 44  ILE A HG13 1 
ATOM   676  H HG21 . ILE A 1 44  ? -40.65600 15.09000 16.81000  1.000 72.91000  ? 44  ILE A HG21 1 
ATOM   677  H HG22 . ILE A 1 44  ? -40.46200 16.55400 17.39300  1.000 72.91000  ? 44  ILE A HG22 1 
ATOM   678  H HG23 . ILE A 1 44  ? -41.26100 15.46500 18.23000  1.000 72.91000  ? 44  ILE A HG23 1 
ATOM   679  H HD11 . ILE A 1 44  ? -43.56700 13.16500 16.84900  1.000 128.32000 ? 44  ILE A HD11 1 
ATOM   680  H HD12 . ILE A 1 44  ? -44.53700 14.31200 17.43600  1.000 128.32000 ? 44  ILE A HD12 1 
ATOM   681  H HD13 . ILE A 1 44  ? -43.06500 14.15900 17.94300  1.000 128.32000 ? 44  ILE A HD13 1 
ATOM   682  N N    . CYS A 1 45  ? -42.87400 19.09500 19.04300  1.000 55.99092  ? 45  CYS A N    1 
ATOM   683  C CA   . CYS A 1 45  ? -42.21500 20.32700 19.43400  1.000 45.33965  ? 45  CYS A CA   1 
ATOM   684  C C    . CYS A 1 45  ? -41.03200 20.01300 20.31900  1.000 41.85502  ? 45  CYS A C    1 
ATOM   685  O O    . CYS A 1 45  ? -41.10200 19.12200 21.16100  1.000 55.91460  ? 45  CYS A O    1 
ATOM   686  C CB   . CYS A 1 45  ? -43.18400 21.23300 20.15900  1.000 45.84234  ? 45  CYS A CB   1 
ATOM   687  S SG   . CYS A 1 45  ? -44.48800 21.70400 19.03000  1.000 50.97190  ? 45  CYS A SG   1 
ATOM   688  H H    . CYS A 1 45  ? -43.52500 18.86500 19.55600  1.000 67.82000  ? 45  CYS A H    1 
ATOM   689  H HA   . CYS A 1 45  ? -41.89200 20.78700 18.64400  1.000 51.27000  ? 45  CYS A HA   1 
ATOM   690  H HB2  . CYS A 1 45  ? -43.57600 20.76100 20.91000  1.000 55.30000  ? 45  CYS A HB2  1 
ATOM   691  H HB3  . CYS A 1 45  ? -42.72500 22.03400 20.45700  1.000 55.30000  ? 45  CYS A HB3  1 
ATOM   692  N N    . GLY A 1 46  ? -39.91900 20.70400 20.08400  1.000 38.65463  ? 46  GLY A N    1 
ATOM   693  C CA   . GLY A 1 46  ? -38.84700 20.68300 21.03200  1.000 35.05420  ? 46  GLY A CA   1 
ATOM   694  C C    . GLY A 1 46  ? -37.52000 20.77500 20.36500  1.000 32.61444  ? 46  GLY A C    1 
ATOM   695  O O    . GLY A 1 46  ? -37.40600 20.85800 19.14200  1.000 33.71983  ? 46  GLY A O    1 
ATOM   696  H H    . GLY A 1 46  ? -39.77400 21.18500 19.38600  1.000 44.48000  ? 46  GLY A H    1 
ATOM   697  H HA2  . GLY A 1 46  ? -38.94000 21.43100 21.64200  1.000 38.93000  ? 46  GLY A HA2  1 
ATOM   698  H HA3  . GLY A 1 46  ? -38.87800 19.86000 21.54400  1.000 38.93000  ? 46  GLY A HA3  1 
ATOM   699  N N    . PRO A 1 47  ? -36.46800 20.72000 21.16900  1.000 25.11091  ? 47  PRO A N    1 
ATOM   700  C CA   . PRO A 1 47  ? -35.11300 20.89900 20.61900  1.000 23.08961  ? 47  PRO A CA   1 
ATOM   701  C C    . PRO A 1 47  ? -34.64800 19.71100 19.82200  1.000 21.38151  ? 47  PRO A C    1 
ATOM   702  O O    . PRO A 1 47  ? -33.68000 19.82700 19.07000  1.000 23.47387  ? 47  PRO A O    1 
ATOM   703  C CB   . PRO A 1 47  ? -34.25700 21.11100 21.87800  1.000 22.56850  ? 47  PRO A CB   1 
ATOM   704  C CG   . PRO A 1 47  ? -35.18700 21.17200 23.01500  1.000 23.29753  ? 47  PRO A CG   1 
ATOM   705  C CD   . PRO A 1 47  ? -36.44300 20.48500 22.59900  1.000 23.16857  ? 47  PRO A CD   1 
ATOM   706  H HA   . PRO A 1 47  ? -35.07500 21.69500 20.06500  1.000 28.33000  ? 47  PRO A HA   1 
ATOM   707  H HB2  . PRO A 1 47  ? -33.64500 20.36600 21.98100  1.000 26.42000  ? 47  PRO A HB2  1 
ATOM   708  H HB3  . PRO A 1 47  ? -33.76600 21.94400 21.79700  1.000 26.42000  ? 47  PRO A HB3  1 
ATOM   709  H HG2  . PRO A 1 47  ? -34.79200 20.71900 23.77600  1.000 28.59000  ? 47  PRO A HG2  1 
ATOM   710  H HG3  . PRO A 1 47  ? -35.36700 22.10000 23.23200  1.000 28.59000  ? 47  PRO A HG3  1 
ATOM   711  H HD2  . PRO A 1 47  ? -36.38900 19.53500 22.78700  1.000 28.43000  ? 47  PRO A HD2  1 
ATOM   712  H HD3  . PRO A 1 47  ? -37.20500 20.89500 23.03600  1.000 28.43000  ? 47  PRO A HD3  1 
ATOM   713  N N    . GLN A 1 48  ? -35.29400 18.55600 19.96400  1.000 25.86363  ? 48  GLN A N    1 
ATOM   714  C CA   . GLN A 1 48  ? -34.88500 17.36900 19.20700  1.000 25.60570  ? 48  GLN A CA   1 
ATOM   715  C C    . GLN A 1 48  ? -34.83000 17.63100 17.71700  1.000 22.45006  ? 48  GLN A C    1 
ATOM   716  O O    . GLN A 1 48  ? -33.77700 17.45400 17.08400  1.000 32.85394  ? 48  GLN A O    1 
ATOM   717  C CB   . GLN A 1 48  ? -35.84000 16.21400 19.60200  1.000 25.02142  ? 48  GLN A CB   1 
ATOM   718  C CG   . GLN A 1 48  ? -35.76900 15.85700 21.07000  1.000 31.02214  ? 48  GLN A CG   1 
ATOM   719  C CD   . GLN A 1 48  ? -36.77200 16.64500 21.94000  1.000 21.50258  ? 48  GLN A CD   1 
ATOM   720  O OE1  . GLN A 1 48  ? -37.49100 17.49500 21.41700  1.000 30.37733  ? 48  GLN A OE1  1 
ATOM   721  N NE2  . GLN A 1 48  ? -36.84300 16.35000 23.20100  1.000 25.23987  ? 48  GLN A NE2  1 
ATOM   722  H H    . GLN A 1 48  ? -35.96800 18.43500 20.48100  1.000 31.67000  ? 48  GLN A H    1 
ATOM   723  H HA   . GLN A 1 48  ? -33.99200 17.11700 19.48900  1.000 31.35000  ? 48  GLN A HA   1 
ATOM   724  H HB2  . GLN A 1 48  ? -36.75100 16.46900 19.39800  1.000 30.65000  ? 48  GLN A HB2  1 
ATOM   725  H HB3  . GLN A 1 48  ? -35.59900 15.42400 19.09400  1.000 30.65000  ? 48  GLN A HB3  1 
ATOM   726  H HG2  . GLN A 1 48  ? -35.96300 14.91200 21.17300  1.000 37.86000  ? 48  GLN A HG2  1 
ATOM   727  H HG3  . GLN A 1 48  ? -34.87600 16.04800 21.39700  1.000 37.86000  ? 48  GLN A HG3  1 
ATOM   728  H HE21 . GLN A 1 48  ? -36.32800 15.74500 23.53100  1.000 30.91000  ? 48  GLN A HE21 1 
ATOM   729  H HE22 . GLN A 1 48  ? -37.39400 16.77000 23.71000  1.000 30.91000  ? 48  GLN A HE22 1 
ATOM   730  N N    . LEU A 1 49  ? -35.93300 18.09100 17.09600  1.000 24.46872  ? 49  LEU A N    1 
ATOM   731  C CA   . LEU A 1 49  ? -35.88500 18.37500 15.69800  1.000 20.92356  ? 49  LEU A CA   1 
ATOM   732  C C    . LEU A 1 49  ? -35.15300 19.68000 15.35700  1.000 20.54720  ? 49  LEU A C    1 
ATOM   733  O O    . LEU A 1 49  ? -34.65600 19.82200 14.24800  1.000 29.26667  ? 49  LEU A O    1 
ATOM   734  C CB   . LEU A 1 49  ? -37.28500 18.43200 15.12300  1.000 32.42757  ? 49  LEU A CB   1 
ATOM   735  C CG   . LEU A 1 49  ? -37.98500 17.07300 15.09000  1.000 30.74579  ? 49  LEU A CG   1 
ATOM   736  C CD1  . LEU A 1 49  ? -39.34100 17.24300 14.47900  1.000 42.52615  ? 49  LEU A CD1  1 
ATOM   737  C CD2  . LEU A 1 49  ? -37.19000 16.03300 14.31600  1.000 43.09727  ? 49  LEU A CD2  1 
ATOM   738  H H    . LEU A 1 49  ? -36.69300 18.23600 17.47200  1.000 29.99000  ? 49  LEU A H    1 
ATOM   739  H HA   . LEU A 1 49  ? -35.40400 17.66000 15.25600  1.000 25.73000  ? 49  LEU A HA   1 
ATOM   740  H HB2  . LEU A 1 49  ? -37.82300 19.03100 15.66500  1.000 39.54000  ? 49  LEU A HB2  1 
ATOM   741  H HB3  . LEU A 1 49  ? -37.23700 18.76400 14.21300  1.000 39.54000  ? 49  LEU A HB3  1 
ATOM   742  H HG   . LEU A 1 49  ? -38.10000 16.75200 15.99800  1.000 37.52000  ? 49  LEU A HG   1 
ATOM   743  H HD11 . LEU A 1 49  ? -39.79600 16.38600 14.47700  1.000 51.66000  ? 49  LEU A HD11 1 
ATOM   744  H HD12 . LEU A 1 49  ? -39.84500 17.88400 15.00400  1.000 51.66000  ? 49  LEU A HD12 1 
ATOM   745  H HD13 . LEU A 1 49  ? -39.23900 17.56600 13.57000  1.000 51.66000  ? 49  LEU A HD13 1 
ATOM   746  H HD21 . LEU A 1 49  ? -37.77200 15.28800 14.09900  1.000 52.34000  ? 49  LEU A HD21 1 
ATOM   747  H HD22 . LEU A 1 49  ? -36.85200 16.43700 13.50200  1.000 52.34000  ? 49  LEU A HD22 1 
ATOM   748  H HD23 . LEU A 1 49  ? -36.45100 15.72600 14.86400  1.000 52.34000  ? 49  LEU A HD23 1 
ATOM   749  N N    . LEU A 1 50  ? -35.03700 20.63300 16.28100  1.000 25.58201  ? 50  LEU A N    1 
ATOM   750  C CA   . LEU A 1 50  ? -34.24100 21.80600 15.92300  1.000 27.38486  ? 50  LEU A CA   1 
ATOM   751  C C    . LEU A 1 50  ? -32.76900 21.45900 15.75900  1.000 26.36106  ? 50  LEU A C    1 
ATOM   752  O O    . LEU A 1 50  ? -32.09700 21.99900 14.86500  1.000 30.77474  ? 50  LEU A O    1 
ATOM   753  C CB   . LEU A 1 50  ? -34.38500 22.88900 16.97100  1.000 24.72139  ? 50  LEU A CB   1 
ATOM   754  C CG   . LEU A 1 50  ? -35.80700 23.47400 16.92500  1.000 29.61145  ? 50  LEU A CG   1 
ATOM   755  C CD1  . LEU A 1 50  ? -35.89000 24.41700 18.10900  1.000 35.85956  ? 50  LEU A CD1  1 
ATOM   756  C CD2  . LEU A 1 50  ? -36.09600 24.12200 15.62400  1.000 36.19908  ? 50  LEU A CD2  1 
ATOM   757  H H    . LEU A 1 50  ? -35.38200 20.63100 17.06900  1.000 31.33000  ? 50  LEU A H    1 
ATOM   758  H HA   . LEU A 1 50  ? -34.55100 22.14900 15.07200  1.000 33.49000  ? 50  LEU A HA   1 
ATOM   759  H HB2  . LEU A 1 50  ? -34.23400 22.51100 17.85200  1.000 30.29000  ? 50  LEU A HB2  1 
ATOM   760  H HB3  . LEU A 1 50  ? -33.75100 23.60100 16.79200  1.000 30.29000  ? 50  LEU A HB3  1 
ATOM   761  H HG   . LEU A 1 50  ? -36.45100 22.76100 17.05900  1.000 36.16000  ? 50  LEU A HG   1 
ATOM   762  H HD11 . LEU A 1 50  ? -35.75500 23.91100 18.92600  1.000 43.66000  ? 50  LEU A HD11 1 
ATOM   763  H HD12 . LEU A 1 50  ? -36.76600 24.83400 18.11900  1.000 43.66000  ? 50  LEU A HD12 1 
ATOM   764  H HD13 . LEU A 1 50  ? -35.20200 25.09500 18.02100  1.000 43.66000  ? 50  LEU A HD13 1 
ATOM   765  H HD21 . LEU A 1 50  ? -35.29900 24.58100 15.31700  1.000 44.07000  ? 50  LEU A HD21 1 
ATOM   766  H HD22 . LEU A 1 50  ? -36.81900 24.75800 15.74300  1.000 44.07000  ? 50  LEU A HD22 1 
ATOM   767  H HD23 . LEU A 1 50  ? -36.35500 23.44300 14.98100  1.000 44.07000  ? 50  LEU A HD23 1 
ATOM   768  N N    . HIS A 1 51  ? -32.23400 20.58900 16.61900  1.000 26.86375  ? 51  HIS A N    1 
ATOM   769  C CA   . HIS A 1 51  ? -30.84300 20.14500 16.44500  1.000 21.46836  ? 51  HIS A CA   1 
ATOM   770  C C    . HIS A 1 51  ? -30.62300 19.49700 15.09100  1.000 21.33940  ? 51  HIS A C    1 
ATOM   771  O O    . HIS A 1 51  ? -29.58300 19.69600 14.45500  1.000 28.84556  ? 51  HIS A O    1 
ATOM   772  C CB   . HIS A 1 51  ? -30.47700 19.15900 17.55900  1.000 29.20877  ? 51  HIS A CB   1 
ATOM   773  C CG   . HIS A 1 51  ? -30.55800 19.72000 18.93900  1.000 30.34574  ? 51  HIS A CG   1 
ATOM   774  N ND1  . HIS A 1 51  ? -30.92000 18.95600 20.02900  1.000 36.73598  ? 51  HIS A ND1  1 
ATOM   775  C CD2  . HIS A 1 51  ? -30.27200 20.95700 19.41300  1.000 39.18101  ? 51  HIS A CD2  1 
ATOM   776  C CE1  . HIS A 1 51  ? -30.86400 19.70600 21.12200  1.000 35.30686  ? 51  HIS A CE1  1 
ATOM   777  N NE2  . HIS A 1 51  ? -30.46700 20.92500 20.77100  1.000 39.24155  ? 51  HIS A NE2  1 
ATOM   778  H H    . HIS A 1 51  ? -32.64100 20.24700 17.29500  1.000 32.86000  ? 51  HIS A H    1 
ATOM   779  H HA   . HIS A 1 51  ? -30.26100 20.91500 16.51800  1.000 26.39000  ? 51  HIS A HA   1 
ATOM   780  H HB2  . HIS A 1 51  ? -31.08200 18.40200 17.51400  1.000 35.68000  ? 51  HIS A HB2  1 
ATOM   781  H HB3  . HIS A 1 51  ? -29.56600 18.85700 17.41800  1.000 35.68000  ? 51  HIS A HB3  1 
ATOM   782  H HD2  . HIS A 1 51  ? -29.99100 21.68400 18.92300  1.000 47.65000  ? 51  HIS A HD2  1 
ATOM   783  H HE1  . HIS A 1 51  ? -31.06800 19.43800 21.97800  1.000 42.99000  ? 51  HIS A HE1  1 
ATOM   784  H HE2  . HIS A 1 51  ? -30.36700 21.59100 21.30600  1.000 47.72000  ? 51  HIS A HE2  1 
ATOM   785  N N    . GLN A 1 52  ? -31.57500 18.72300 14.60400  1.000 26.21104  ? 52  GLN A N    1 
ATOM   786  C CA   . GLN A 1 52  ? -31.35000 18.10800 13.31200  1.000 24.68191  ? 52  GLN A CA   1 
ATOM   787  C C    . GLN A 1 52  ? -31.46000 19.12400 12.19500  1.000 21.70260  ? 52  GLN A C    1 
ATOM   788  O O    . GLN A 1 52  ? -30.71200 19.06800 11.21900  1.000 30.89581  ? 52  GLN A O    1 
ATOM   789  C CB   . GLN A 1 52  ? -32.35700 16.99200 13.06300  1.000 31.09320  ? 52  GLN A CB   1 
ATOM   790  C CG   . GLN A 1 52  ? -32.32900 15.95900 14.12200  1.000 28.71397  ? 52  GLN A CG   1 
ATOM   791  C CD   . GLN A 1 52  ? -33.25200 14.81700 13.78300  1.000 38.32302  ? 52  GLN A CD   1 
ATOM   792  O OE1  . GLN A 1 52  ? -34.08600 14.92000 12.88100  1.000 55.36716  ? 52  GLN A OE1  1 
ATOM   793  N NE2  . GLN A 1 52  ? -33.13400 13.71600 14.53100  1.000 47.74520  ? 52  GLN A NE2  1 
ATOM   794  H H    . GLN A 1 52  ? -32.32700 18.54300 14.98100  1.000 32.08000  ? 52  GLN A H    1 
ATOM   795  H HA   . GLN A 1 52  ? -30.45900 17.72400 13.28900  1.000 30.25000  ? 52  GLN A HA   1 
ATOM   796  H HB2  . GLN A 1 52  ? -33.25000 17.37100 13.03600  1.000 37.94000  ? 52  GLN A HB2  1 
ATOM   797  H HB3  . GLN A 1 52  ? -32.15200 16.56200 12.21800  1.000 37.94000  ? 52  GLN A HB3  1 
ATOM   798  H HG2  . GLN A 1 52  ? -31.42800 15.60900 14.20700  1.000 35.08000  ? 52  GLN A HG2  1 
ATOM   799  H HG3  . GLN A 1 52  ? -32.62100 16.34800 14.96100  1.000 35.08000  ? 52  GLN A HG3  1 
ATOM   800  H HE21 . GLN A 1 52  ? -32.54400 13.68200 15.15600  1.000 57.92000  ? 52  GLN A HE21 1 
ATOM   801  H HE22 . GLN A 1 52  ? -33.64000 13.03700 14.38000  1.000 57.92000  ? 52  GLN A HE22 1 
ATOM   802  N N    . ILE A 1 53  ? -32.40900 20.05100 12.32100  1.000 25.93206  ? 53  ILE A N    1 
ATOM   803  C CA   . ILE A 1 53  ? -32.50500 21.11400 11.33500  1.000 26.47686  ? 53  ILE A CA   1 
ATOM   804  C C    . ILE A 1 53  ? -31.19900 21.86900 11.30000  1.000 23.03697  ? 53  ILE A C    1 
ATOM   805  O O    . ILE A 1 53  ? -30.67200 22.18100 10.22500  1.000 24.34502  ? 53  ILE A O    1 
ATOM   806  C CB   . ILE A 1 53  ? -33.69500 22.04400 11.64200  1.000 20.41561  ? 53  ILE A CB   1 
ATOM   807  C CG1  . ILE A 1 53  ? -34.98200 21.37000 11.20200  1.000 32.06700  ? 53  ILE A CG1  1 
ATOM   808  C CG2  . ILE A 1 53  ? -33.50400 23.37400 10.85900  1.000 27.71648  ? 53  ILE A CG2  1 
ATOM   809  C CD1  . ILE A 1 53  ? -36.19400 21.68600 12.04200  1.000 26.85848  ? 53  ILE A CD1  1 
ATOM   810  H H    . ILE A 1 53  ? -32.99300 20.08400 12.95200  1.000 31.75000  ? 53  ILE A H    1 
ATOM   811  H HA   . ILE A 1 53  ? -32.64900 20.72200 10.46000  1.000 32.40000  ? 53  ILE A HA   1 
ATOM   812  H HB   . ILE A 1 53  ? -33.73000 22.22700 12.59400  1.000 22.68000  ? 53  ILE A HB   1 
ATOM   813  H HG12 . ILE A 1 53  ? -35.17800 21.64500 10.29300  1.000 39.11000  ? 53  ILE A HG12 1 
ATOM   814  H HG13 . ILE A 1 53  ? -34.85100 20.40900 11.22900  1.000 39.11000  ? 53  ILE A HG13 1 
ATOM   815  H HG21 . ILE A 1 53  ? -34.36100 23.82300 10.79600  1.000 33.89000  ? 53  ILE A HG21 1 
ATOM   816  H HG22 . ILE A 1 53  ? -32.87300 23.93800 11.33300  1.000 33.89000  ? 53  ILE A HG22 1 
ATOM   817  H HG23 . ILE A 1 53  ? -33.17300 23.17400 9.96900   1.000 33.89000  ? 53  ILE A HG23 1 
ATOM   818  H HD11 . ILE A 1 53  ? -36.01600 21.43300 12.96100  1.000 32.86000  ? 53  ILE A HD11 1 
ATOM   819  H HD12 . ILE A 1 53  ? -36.95300 21.18600 11.70200  1.000 32.86000  ? 53  ILE A HD12 1 
ATOM   820  H HD13 . ILE A 1 53  ? -36.37400 22.63800 11.99000  1.000 32.86000  ? 53  ILE A HD13 1 
ATOM   821  N N    . ALA A 1 54  ? -30.62600 22.11600 12.46200  1.000 28.94031  ? 54  ALA A N    1 
ATOM   822  C CA   . ALA A 1 54  ? -29.36700 22.86400 12.52200  1.000 22.49480  ? 54  ALA A CA   1 
ATOM   823  C C    . ALA A 1 54  ? -28.22100 22.08900 11.87900  1.000 20.83671  ? 54  ALA A C    1 
ATOM   824  O O    . ALA A 1 54  ? -27.42000 22.65800 11.13800  1.000 28.83240  ? 54  ALA A O    1 
ATOM   825  C CB   . ALA A 1 54  ? -29.07300 23.22400 13.96200  1.000 34.83576  ? 54  ALA A CB   1 
ATOM   826  H H    . ALA A 1 54  ? -30.93400 21.86900 13.22600  1.000 35.35000  ? 54  ALA A H    1 
ATOM   827  H HA   . ALA A 1 54  ? -29.47500 23.69200 12.02800  1.000 27.62000  ? 54  ALA A HA   1 
ATOM   828  H HB1  . ALA A 1 54  ? -28.13100 23.43300 14.05800  1.000 42.43000  ? 54  ALA A HB1  1 
ATOM   829  H HB2  . ALA A 1 54  ? -29.31200 22.47300 14.52200  1.000 42.43000  ? 54  ALA A HB2  1 
ATOM   830  H HB3  . ALA A 1 54  ? -29.61700 23.98900 14.20200  1.000 42.43000  ? 54  ALA A HB3  1 
ATOM   831  N N    A GLU A 1 55  ? -28.11100 20.78800 12.14500  0.700 27.83492  ? 55  GLU A N    1 
ATOM   832  N N    B GLU A 1 55  ? -28.14400 20.78300 12.14200  0.300 27.94019  ? 55  GLU A N    1 
ATOM   833  C CA   A GLU A 1 55  ? -27.10100 20.01000 11.42300  0.700 25.96364  ? 55  GLU A CA   1 
ATOM   834  C CA   B GLU A 1 55  ? -27.16000 19.94600 11.45800  0.300 26.69794  ? 55  GLU A CA   1 
ATOM   835  C C    A GLU A 1 55  ? -27.33900 20.00600 9.91600   0.700 33.84090  ? 55  GLU A C    1 
ATOM   836  C C    B GLU A 1 55  ? -27.34600 19.98400 9.94000   0.300 33.75668  ? 55  GLU A C    1 
ATOM   837  O O    A GLU A 1 55  ? -26.37900 19.98700 9.14000   0.700 30.58261  ? 55  GLU A O    1 
ATOM   838  O O    B GLU A 1 55  ? -26.36400 19.97500 9.18900   0.300 30.55103  ? 55  GLU A O    1 
ATOM   839  C CB   A GLU A 1 55  ? -27.08700 18.58000 11.99100  0.700 34.91734  ? 55  GLU A CB   1 
ATOM   840  C CB   B GLU A 1 55  ? -27.26300 18.51100 11.99800  0.300 34.49624  ? 55  GLU A CB   1 
ATOM   841  C CG   A GLU A 1 55  ? -26.06600 17.64300 11.32900  0.700 39.61264  ? 55  GLU A CG   1 
ATOM   842  C CG   B GLU A 1 55  ? -26.88100 18.35700 13.47800  0.300 33.84353  ? 55  GLU A CG   1 
ATOM   843  C CD   A GLU A 1 55  ? -24.62200 18.06700 11.59400  0.700 53.80908  ? 55  GLU A CD   1 
ATOM   844  C CD   B GLU A 1 55  ? -27.19800 16.97500 14.07300  0.300 31.15637  ? 55  GLU A CD   1 
ATOM   845  O OE1  A GLU A 1 55  ? -24.30400 18.31300 12.78800  0.700 52.61420  ? 55  GLU A OE1  1 
ATOM   846  O OE1  B GLU A 1 55  ? -27.92600 16.19000 13.44800  0.300 22.71851  ? 55  GLU A OE1  1 
ATOM   847  O OE2  A GLU A 1 55  ? -23.81700 18.16500 10.61600  0.700 53.14848  ? 55  GLU A OE2  1 
ATOM   848  O OE2  B GLU A 1 55  ? -26.70700 16.68500 15.18700  0.300 40.65751  ? 55  GLU A OE2  1 
ATOM   849  H H    A GLU A 1 55  ? -28.58500 20.34700 12.71200  0.700 34.03000  ? 55  GLU A H    1 
ATOM   850  H H    B GLU A 1 55  ? -28.64200 20.36400 12.70400  0.300 34.15000  ? 55  GLU A H    1 
ATOM   851  H HA   A GLU A 1 55  ? -26.22900 20.40300 11.58400  0.700 31.78000  ? 55  GLU A HA   1 
ATOM   852  H HA   B GLU A 1 55  ? -26.27100 20.27800 11.65800  0.300 32.66000  ? 55  GLU A HA   1 
ATOM   853  H HB2  A GLU A 1 55  ? -26.87600 18.62400 12.93700  0.700 42.53000  ? 55  GLU A HB2  1 
ATOM   854  H HB2  B GLU A 1 55  ? -28.17900 18.20700 11.89700  0.300 42.02000  ? 55  GLU A HB2  1 
ATOM   855  H HB3  A GLU A 1 55  ? -27.96700 18.18900 11.87000  0.700 42.53000  ? 55  GLU A HB3  1 
ATOM   856  H HB3  B GLU A 1 55  ? -26.67200 17.94200 11.48100  0.300 42.02000  ? 55  GLU A HB3  1 
ATOM   857  H HG2  A GLU A 1 55  ? -26.18400 16.74900 11.68500  0.700 48.16000  ? 55  GLU A HG2  1 
ATOM   858  H HG2  B GLU A 1 55  ? -25.92600 18.50200 13.56700  0.300 41.24000  ? 55  GLU A HG2  1 
ATOM   859  H HG3  A GLU A 1 55  ? -26.20800 17.63700 10.37000  0.700 48.16000  ? 55  GLU A HG3  1 
ATOM   860  H HG3  B GLU A 1 55  ? -27.36100 19.02100 13.99600  0.300 41.24000  ? 55  GLU A HG3  1 
ATOM   861  N N    . ILE A 1 56  ? -28.59400 20.02500 9.46500   1.000 29.82726  ? 56  ILE A N    1 
ATOM   862  C CA   . ILE A 1 56  ? -28.86000 20.04000 8.03400   1.000 30.61946  ? 56  ILE A CA   1 
ATOM   863  C C    . ILE A 1 56  ? -28.44300 21.37200 7.43600   1.000 25.58201  ? 56  ILE A C    1 
ATOM   864  O O    . ILE A 1 56  ? -27.76800 21.42800 6.39900   1.000 31.20901  ? 56  ILE A O    1 
ATOM   865  C CB   . ILE A 1 56  ? -30.34600 19.76600 7.74900   1.000 22.65008  ? 56  ILE A CB   1 
ATOM   866  C CG1  . ILE A 1 56  ? -30.69100 18.31900 8.08300   1.000 24.57663  ? 56  ILE A CG1  1 
ATOM   867  C CG2  . ILE A 1 56  ? -30.70500 20.01700 6.28900   1.000 28.98505  ? 56  ILE A CG2  1 
ATOM   868  C CD1  . ILE A 1 56  ? -32.19800 18.01700 8.20700   1.000 23.28437  ? 56  ILE A CD1  1 
ATOM   869  H H    . ILE A 1 56  ? -29.29700 20.03700 9.96000   1.000 36.42000  ? 56  ILE A H    1 
ATOM   870  H HA   . ILE A 1 56  ? -28.33800 19.34200 7.60800   1.000 37.37000  ? 56  ILE A HA   1 
ATOM   871  H HB   . ILE A 1 56  ? -30.88300 20.35100 8.30700   1.000 27.81000  ? 56  ILE A HB   1 
ATOM   872  H HG12 . ILE A 1 56  ? -30.33600 17.74900 7.38300   1.000 30.12000  ? 56  ILE A HG12 1 
ATOM   873  H HG13 . ILE A 1 56  ? -30.27700 18.09000 8.93000   1.000 30.12000  ? 56  ILE A HG13 1 
ATOM   874  H HG21 . ILE A 1 56  ? -30.74500 20.97300 6.13100   1.000 35.41000  ? 56  ILE A HG21 1 
ATOM   875  H HG22 . ILE A 1 56  ? -31.56800 19.61900 6.10000   1.000 35.41000  ? 56  ILE A HG22 1 
ATOM   876  H HG23 . ILE A 1 56  ? -30.02700 19.61400 5.72400   1.000 35.41000  ? 56  ILE A HG23 1 
ATOM   877  H HD11 . ILE A 1 56  ? -32.31100 17.12300 8.56600   1.000 28.57000  ? 56  ILE A HD11 1 
ATOM   878  H HD12 . ILE A 1 56  ? -32.60100 18.66700 8.80400   1.000 28.57000  ? 56  ILE A HD12 1 
ATOM   879  H HD13 . ILE A 1 56  ? -32.60700 18.07500 7.33000   1.000 28.57000  ? 56  ILE A HD13 1 
ATOM   880  N N    . GLU A 1 57  ? -28.80500 22.47800 8.08700   1.000 24.10289  ? 57  GLU A N    1 
ATOM   881  C CA   . GLU A 1 57  ? -28.32200 23.74600 7.55200   1.000 27.83228  ? 57  GLU A CA   1 
ATOM   882  C C    . GLU A 1 57  ? -26.80200 23.75100 7.52700   1.000 38.46251  ? 57  GLU A C    1 
ATOM   883  O O    . GLU A 1 57  ? -26.17600 24.33000 6.63300   1.000 32.39336  ? 57  GLU A O    1 
ATOM   884  C CB   . GLU A 1 57  ? -28.82200 24.89100 8.41600   1.000 24.50557  ? 57  GLU A CB   1 
ATOM   885  C CG   . GLU A 1 57  ? -30.28400 25.06600 8.37500   1.000 32.54074  ? 57  GLU A CG   1 
ATOM   886  C CD   . GLU A 1 57  ? -30.73100 26.05700 9.40800   1.000 45.74759  ? 57  GLU A CD   1 
ATOM   887  O OE1  . GLU A 1 57  ? -30.44900 25.84200 10.62400  1.000 55.31189  ? 57  GLU A OE1  1 
ATOM   888  O OE2  . GLU A 1 57  ? -31.35700 27.05700 8.99000   1.000 52.82739  ? 57  GLU A OE2  1 
ATOM   889  H H    . GLU A 1 57  ? -29.29500 22.52200 8.79200   1.000 29.55000  ? 57  GLU A H    1 
ATOM   890  H HA   . GLU A 1 57  ? -28.65100 23.86900 6.64800   1.000 34.02000  ? 57  GLU A HA   1 
ATOM   891  H HB2  . GLU A 1 57  ? -28.56900 24.72200 9.33700   1.000 30.03000  ? 57  GLU A HB2  1 
ATOM   892  H HB3  . GLU A 1 57  ? -28.41500 25.71600 8.10900   1.000 30.03000  ? 57  GLU A HB3  1 
ATOM   893  H HG2  . GLU A 1 57  ? -30.54500 25.39600 7.50100   1.000 39.67000  ? 57  GLU A HG2  1 
ATOM   894  H HG3  . GLU A 1 57  ? -30.71600 24.21700 8.55800   1.000 39.67000  ? 57  GLU A HG3  1 
ATOM   895  N N    A ARG A 1 58  ? -26.19400 23.12200 8.52200   0.700 38.58094  ? 58  ARG A N    1 
ATOM   896  N N    B ARG A 1 58  ? -26.17400 23.13500 8.53100   0.300 38.50988  ? 58  ARG A N    1 
ATOM   897  C CA   A ARG A 1 58  ? -24.74300 23.10700 8.61900   0.700 34.98841  ? 58  ARG A CA   1 
ATOM   898  C CA   B ARG A 1 58  ? -24.71500 23.16000 8.58900   0.300 35.18843  ? 58  ARG A CA   1 
ATOM   899  C C    A ARG A 1 58  ? -24.16300 22.48600 7.36900   0.700 34.78575  ? 58  ARG A C    1 
ATOM   900  C C    B ARG A 1 58  ? -24.13000 22.48500 7.36100   0.300 35.05157  ? 58  ARG A C    1 
ATOM   901  O O    A ARG A 1 58  ? -23.41400 23.12400 6.63200   0.700 38.40724  ? 58  ARG A O    1 
ATOM   902  O O    B ARG A 1 58  ? -23.29900 23.06300 6.65500   0.300 38.58357  ? 58  ARG A O    1 
ATOM   903  C CB   A ARG A 1 58  ? -24.33600 22.33200 9.87600   0.700 44.50534  ? 58  ARG A CB   1 
ATOM   904  C CB   B ARG A 1 58  ? -24.19700 22.48500 9.86600   0.300 42.64459  ? 58  ARG A CB   1 
ATOM   905  C CG   A ARG A 1 58  ? -22.99000 22.67400 10.51600  0.700 40.35484  ? 58  ARG A CG   1 
ATOM   906  C CG   B ARG A 1 58  ? -22.68000 22.68300 10.10400  0.300 39.60475  ? 58  ARG A CG   1 
ATOM   907  C CD   A ARG A 1 58  ? -22.90500 22.05400 11.95300  0.700 44.98697  ? 58  ARG A CD   1 
ATOM   908  C CD   B ARG A 1 58  ? -22.09600 21.80500 11.23100  0.300 38.67306  ? 58  ARG A CD   1 
ATOM   909  N NE   A ARG A 1 58  ? -23.61100 22.85200 12.96000  0.700 50.73240  ? 58  ARG A NE   1 
ATOM   910  N NE   B ARG A 1 58  ? -22.21900 20.37600 10.96600  0.300 31.93014  ? 58  ARG A NE   1 
ATOM   911  C CZ   A ARG A 1 58  ? -24.49900 22.38800 13.84000  0.700 41.40760  ? 58  ARG A CZ   1 
ATOM   912  C CZ   B ARG A 1 58  ? -21.52800 19.73100 10.04200  0.300 36.17013  ? 58  ARG A CZ   1 
ATOM   913  N NH1  A ARG A 1 58  ? -24.87200 21.11200 13.86000  0.700 40.53118  ? 58  ARG A NH1  1 
ATOM   914  N NH1  B ARG A 1 58  ? -20.69500 20.36800 9.24300   0.300 40.64435  ? 58  ARG A NH1  1 
ATOM   915  N NH2  A ARG A 1 58  ? -25.01100 23.22300 14.74300  0.700 47.46359  ? 58  ARG A NH2  1 
ATOM   916  N NH2  B ARG A 1 58  ? -21.68100 18.41700 9.91400   0.300 36.25435  ? 58  ARG A NH2  1 
ATOM   917  H H    A ARG A 1 58  ? -26.59700 22.69700 9.15200   0.700 46.92000  ? 58  ARG A H    1 
ATOM   918  H H    B ARG A 1 58  ? -26.55700 22.70900 9.17200   0.300 46.84000  ? 58  ARG A H    1 
ATOM   919  H HA   A ARG A 1 58  ? -24.41200 24.01600 8.69500   0.700 42.62000  ? 58  ARG A HA   1 
ATOM   920  H HA   B ARG A 1 58  ? -24.41500 24.08300 8.59500   0.300 42.85000  ? 58  ARG A HA   1 
ATOM   921  H HB2  A ARG A 1 58  ? -25.01500 22.48100 10.55200  0.700 54.03000  ? 58  ARG A HB2  1 
ATOM   922  H HB2  B ARG A 1 58  ? -24.66800 22.85600 10.62900  0.300 51.80000  ? 58  ARG A HB2  1 
ATOM   923  H HB3  A ARG A 1 58  ? -24.31200 21.38800 9.65400   0.700 54.03000  ? 58  ARG A HB3  1 
ATOM   924  H HB3  B ARG A 1 58  ? -24.36600 21.53200 9.80600   0.300 51.80000  ? 58  ARG A HB3  1 
ATOM   925  H HG2  A ARG A 1 58  ? -22.27200 22.30600 9.97800   0.700 49.05000  ? 58  ARG A HG2  1 
ATOM   926  H HG2  B ARG A 1 58  ? -22.20600 22.47300 9.28500   0.300 48.15000  ? 58  ARG A HG2  1 
ATOM   927  H HG3  A ARG A 1 58  ? -22.90100 23.63700 10.59000  0.700 49.05000  ? 58  ARG A HG3  1 
ATOM   928  H HG3  B ARG A 1 58  ? -22.52300 23.61000 10.34300  0.300 48.15000  ? 58  ARG A HG3  1 
ATOM   929  H HD2  A ARG A 1 58  ? -23.28900 21.16600 11.92800  0.700 54.61000  ? 58  ARG A HD2  1 
ATOM   930  H HD2  B ARG A 1 58  ? -21.15300 22.01000 11.33300  0.300 47.04000  ? 58  ARG A HD2  1 
ATOM   931  H HD3  A ARG A 1 58  ? -21.97300 22.00200 12.21600  0.700 54.61000  ? 58  ARG A HD3  1 
ATOM   932  H HD3  B ARG A 1 58  ? -22.56800 21.99700 12.05600  0.300 47.04000  ? 58  ARG A HD3  1 
ATOM   933  H HE   A ARG A 1 58  ? -23.43700 23.69400 12.98500  0.700 61.50000  ? 58  ARG A HE   1 
ATOM   934  H HE   B ARG A 1 58  ? -22.77600 19.92500 11.44100  0.300 38.94000  ? 58  ARG A HE   1 
ATOM   935  H HH11 A ARG A 1 58  ? -24.54800 20.55700 13.29000  0.700 49.27000  ? 58  ARG A HH11 1 
ATOM   936  H HH11 B ARG A 1 58  ? -20.58500 21.21700 9.31800   0.300 49.40000  ? 58  ARG A HH11 1 
ATOM   937  H HH12 A ARG A 1 58  ? -25.44100 20.83700 14.43900  0.700 49.27000  ? 58  ARG A HH12 1 
ATOM   938  H HH12 B ARG A 1 58  ? -20.25500 19.93100 8.64700   0.300 49.40000  ? 58  ARG A HH12 1 
ATOM   939  H HH21 A ARG A 1 58  ? -24.77600 24.05000 14.74100  0.700 57.58000  ? 58  ARG A HH21 1 
ATOM   940  H HH21 B ARG A 1 58  ? -22.22500 17.99500 10.43000  0.300 44.13000  ? 58  ARG A HH21 1 
ATOM   941  H HH22 A ARG A 1 58  ? -25.58200 22.94400 15.31900  0.700 57.58000  ? 58  ARG A HH22 1 
ATOM   942  H HH22 B ARG A 1 58  ? -21.23900 17.98900 9.31300   0.300 44.13000  ? 58  ARG A HH22 1 
ATOM   943  N N    . GLU A 1 59  ? -24.56300 21.25600 7.08200   1.000 33.27504  ? 59  GLU A N    1 
ATOM   944  C CA   . GLU A 1 59  ? -24.08400 20.57200 5.89600   1.000 35.38582  ? 59  GLU A CA   1 
ATOM   945  C C    . GLU A 1 59  ? -24.45900 21.31700 4.62000   1.000 30.39312  ? 59  GLU A C    1 
ATOM   946  O O    . GLU A 1 59  ? -23.65900 21.38400 3.68500   1.000 37.62556  ? 59  GLU A O    1 
ATOM   947  C CB   . GLU A 1 59  ? -24.62100 19.14400 5.92900   1.000 36.13591  ? 59  GLU A CB   1 
ATOM   948  C CG   . GLU A 1 59  ? -24.09600 18.41500 7.18500   1.000 48.76901  ? 59  GLU A CG   1 
ATOM   949  C CD   . GLU A 1 59  ? -24.43200 16.92500 7.23300   1.000 71.41646  ? 59  GLU A CD   1 
ATOM   950  O OE1  . GLU A 1 59  ? -24.75200 16.33000 6.17600   1.000 64.70513  ? 59  GLU A OE1  1 
ATOM   951  O OE2  . GLU A 1 59  ? -24.37600 16.34500 8.34300   1.000 77.60667  ? 59  GLU A OE2  1 
ATOM   952  H H    . GLU A 1 59  ? -25.11800 20.80600 7.56000   1.000 40.55000  ? 59  GLU A H    1 
ATOM   953  H HA   . GLU A 1 59  ? -23.11600 20.52400 5.93400   1.000 43.09000  ? 59  GLU A HA   1 
ATOM   954  H HB2  . GLU A 1 59  ? -25.59000 19.16200 5.96400   1.000 43.99000  ? 59  GLU A HB2  1 
ATOM   955  H HB3  . GLU A 1 59  ? -24.31700 18.66400 5.14300   1.000 43.99000  ? 59  GLU A HB3  1 
ATOM   956  H HG2  . GLU A 1 59  ? -23.13000 18.50000 7.21300   1.000 59.15000  ? 59  GLU A HG2  1 
ATOM   957  H HG3  . GLU A 1 59  ? -24.48400 18.82800 7.97200   1.000 59.15000  ? 59  GLU A HG3  1 
ATOM   958  N N    . LEU A 1 60  ? -25.64600 21.92800 4.56800   1.000 29.04032  ? 60  LEU A N    1 
ATOM   959  C CA   . LEU A 1 60  ? -25.99200 22.71800 3.39400   1.000 31.88803  ? 60  LEU A CA   1 
ATOM   960  C C    . LEU A 1 60  ? -25.01300 23.86300 3.19400   1.000 39.66002  ? 60  LEU A C    1 
ATOM   961  O O    . LEU A 1 60  ? -24.58400 24.12800 2.06000   1.000 32.95395  ? 60  LEU A O    1 
ATOM   962  C CB   . LEU A 1 60  ? -27.41500 23.24400 3.52100   1.000 29.17455  ? 60  LEU A CB   1 
ATOM   963  C CG   . LEU A 1 60  ? -28.46600 22.21300 3.09400   1.000 37.75979  ? 60  LEU A CG   1 
ATOM   964  C CD1  . LEU A 1 60  ? -29.88000 22.74600 3.37700   1.000 40.88648  ? 60  LEU A CD1  1 
ATOM   965  C CD2  . LEU A 1 60  ? -28.31200 21.84100 1.63400   1.000 40.72330  ? 60  LEU A CD2  1 
ATOM   966  H H    . LEU A 1 60  ? -26.24900 21.90100 5.18100   1.000 35.48000  ? 60  LEU A H    1 
ATOM   967  H HA   . LEU A 1 60  ? -25.93700 22.15000 2.61100   1.000 38.89000  ? 60  LEU A HA   1 
ATOM   968  H HB2  . LEU A 1 60  ? -27.58400 23.47900 4.44700   1.000 35.64000  ? 60  LEU A HB2  1 
ATOM   969  H HB3  . LEU A 1 60  ? -27.51500 24.02600 2.95600   1.000 35.64000  ? 60  LEU A HB3  1 
ATOM   970  H HG   . LEU A 1 60  ? -28.34300 21.40700 3.61900   1.000 45.94000  ? 60  LEU A HG   1 
ATOM   971  H HD11 . LEU A 1 60  ? -30.53000 22.08000 3.10300   1.000 49.69000  ? 60  LEU A HD11 1 
ATOM   972  H HD12 . LEU A 1 60  ? -29.96400 22.92000 4.32700   1.000 49.69000  ? 60  LEU A HD12 1 
ATOM   973  H HD13 . LEU A 1 60  ? -30.01500 23.56600 2.87700   1.000 49.69000  ? 60  LEU A HD13 1 
ATOM   974  H HD21 . LEU A 1 60  ? -29.15200 21.48100 1.31000   1.000 49.49000  ? 60  LEU A HD21 1 
ATOM   975  H HD22 . LEU A 1 60  ? -28.07700 22.63600 1.13000   1.000 49.49000  ? 60  LEU A HD22 1 
ATOM   976  H HD23 . LEU A 1 60  ? -27.61200 21.17500 1.54800   1.000 49.49000  ? 60  LEU A HD23 1 
ATOM   977  N N    . ASN A 1 61  ? -24.62800 24.54300 4.26800   1.000 40.59171  ? 61  ASN A N    1 
ATOM   978  C CA   . ASN A 1 61  ? -23.70800 25.67800 4.11500   1.000 38.87045  ? 61  ASN A CA   1 
ATOM   979  C C    . ASN A 1 61  ? -22.31600 25.21900 3.70100   1.000 41.12072  ? 61  ASN A C    1 
ATOM   980  O O    . ASN A 1 61  ? -21.65800 25.86500 2.87400   1.000 37.04392  ? 61  ASN A O    1 
ATOM   981  C CB   . ASN A 1 61  ? -23.62000 26.48500 5.40300   1.000 42.46562  ? 61  ASN A CB   1 
ATOM   982  C CG   . ASN A 1 61  ? -24.95000 27.08800 5.78600   1.000 55.32242  ? 61  ASN A CG   1 
ATOM   983  O OD1  . ASN A 1 61  ? -25.77600 27.40900 4.92300   1.000 61.20207  ? 61  ASN A OD1  1 
ATOM   984  N ND2  . ASN A 1 61  ? -25.18300 27.21400 7.08300   1.000 65.13149  ? 61  ASN A ND2  1 
ATOM   985  H H    . ASN A 1 61  ? -24.87300 24.37900 5.07600   1.000 49.34000  ? 61  ASN A H    1 
ATOM   986  H HA   . ASN A 1 61  ? -24.04700 26.26400 3.42000   1.000 47.27000  ? 61  ASN A HA   1 
ATOM   987  H HB2  . ASN A 1 61  ? -23.33300 25.90300 6.12400   1.000 51.59000  ? 61  ASN A HB2  1 
ATOM   988  H HB3  . ASN A 1 61  ? -22.98400 27.20700 5.28300   1.000 51.59000  ? 61  ASN A HB3  1 
ATOM   989  H HD21 . ASN A 1 61  ? -24.58500 26.97400 7.65300   1.000 78.79000  ? 61  ASN A HD21 1 
ATOM   990  H HD22 . ASN A 1 61  ? -25.92700 27.54900 7.35600   1.000 78.79000  ? 61  ASN A HD22 1 
ATOM   991  N N    . ASN A 1 62  ? -21.85400 24.09800 4.25200   1.000 35.33055  ? 62  ASN A N    1 
ATOM   992  C CA   . ASN A 1 62  ? -20.63900 23.49400 3.72000   1.000 29.80621  ? 62  ASN A CA   1 
ATOM   993  C C    . ASN A 1 62  ? -20.74600 23.24500 2.22700   1.000 38.15194  ? 62  ASN A C    1 
ATOM   994  O O    . ASN A 1 62  ? -19.81200 23.52500 1.46800   1.000 50.41394  ? 62  ASN A O    1 
ATOM   995  C CB   . ASN A 1 62  ? -20.35100 22.15900 4.40400   1.000 35.60690  ? 62  ASN A CB   1 
ATOM   996  C CG   . ASN A 1 62  ? -20.01100 22.31800 5.87900   1.000 50.03758  ? 62  ASN A CG   1 
ATOM   997  O OD1  . ASN A 1 62  ? -19.90300 21.32800 6.62900   1.000 45.40018  ? 62  ASN A OD1  1 
ATOM   998  N ND2  . ASN A 1 62  ? -19.84500 23.57300 6.30600   1.000 50.81925  ? 62  ASN A ND2  1 
ATOM   999  H H    . ASN A 1 62  ? -22.21300 23.68000 4.91300   1.000 43.02000  ? 62  ASN A H    1 
ATOM   1000 H HA   . ASN A 1 62  ? -19.88700 24.09000 3.85800   1.000 36.40000  ? 62  ASN A HA   1 
ATOM   1001 H HB2  . ASN A 1 62  ? -21.13600 21.59300 4.33600   1.000 43.36000  ? 62  ASN A HB2  1 
ATOM   1002 H HB3  . ASN A 1 62  ? -19.59600 21.73500 3.96600   1.000 43.36000  ? 62  ASN A HB3  1 
ATOM   1003 H HD21 . ASN A 1 62  ? -19.92300 24.24500 5.78200   1.000 61.61000  ? 62  ASN A HD21 1 
ATOM   1004 H HD22 . ASN A 1 62  ? -19.65200 23.71000 7.13300   1.000 61.61000  ? 62  ASN A HD22 1 
ATOM   1005 N N    . GLN A 1 63  ? -21.86300 22.69100 1.78600   1.000 40.24693  ? 63  GLN A N    1 
ATOM   1006 C CA   . GLN A 1 63  ? -21.97000 22.43600 0.36300   1.000 30.95108  ? 63  GLN A CA   1 
ATOM   1007 C C    . GLN A 1 63  ? -21.99100 23.73300 -0.43600  1.000 28.85083  ? 63  GLN A C    1 
ATOM   1008 O O    . GLN A 1 63  ? -21.50700 23.77000 -1.57000  1.000 35.01999  ? 63  GLN A O    1 
ATOM   1009 C CB   . GLN A 1 63  ? -23.22000 21.63900 0.04400   1.000 38.16773  ? 63  GLN A CB   1 
ATOM   1010 C CG   . GLN A 1 63  ? -23.12300 20.18400 0.35000   1.000 39.81793  ? 63  GLN A CG   1 
ATOM   1011 C CD   . GLN A 1 63  ? -24.35600 19.47400 -0.09700  1.000 52.00624  ? 63  GLN A CD   1 
ATOM   1012 O OE1  . GLN A 1 63  ? -25.18700 20.05000 -0.80900  1.000 58.62545  ? 63  GLN A OE1  1 
ATOM   1013 N NE2  . GLN A 1 63  ? -24.49600 18.22100 0.30400   1.000 79.31740  ? 63  GLN A NE2  1 
ATOM   1014 H H    . GLN A 1 63  ? -22.54200 22.46300 2.26300   1.000 48.92000  ? 63  GLN A H    1 
ATOM   1015 H HA   . GLN A 1 63  ? -21.20200 21.91800 0.07600   1.000 37.77000  ? 63  GLN A HA   1 
ATOM   1016 H HB2  . GLN A 1 63  ? -23.95800 22.00000 0.56000   1.000 46.43000  ? 63  GLN A HB2  1 
ATOM   1017 H HB3  . GLN A 1 63  ? -23.40900 21.72900 -0.90300  1.000 46.43000  ? 63  GLN A HB3  1 
ATOM   1018 H HG2  . GLN A 1 63  ? -22.36300 19.80500 -0.11900  1.000 48.41000  ? 63  GLN A HG2  1 
ATOM   1019 H HG3  . GLN A 1 63  ? -23.02700 20.06000 1.30700   1.000 48.41000  ? 63  GLN A HG3  1 
ATOM   1020 H HE21 . GLN A 1 63  ? -23.89300 17.86000 0.79900   1.000 95.81000  ? 63  GLN A HE21 1 
ATOM   1021 H HE22 . GLN A 1 63  ? -25.19000 17.77000 0.07200   1.000 95.81000  ? 63  GLN A HE22 1 
ATOM   1022 N N    . GLU A 1 64  ? -22.57600 24.80200 0.11100   1.000 34.04356  ? 64  GLU A N    1 
ATOM   1023 C CA   . GLU A 1 64  ? -22.53800 26.06300 -0.62000  1.000 39.85478  ? 64  GLU A CA   1 
ATOM   1024 C C    . GLU A 1 64  ? -21.09200 26.44300 -0.93400  1.000 46.37661  ? 64  GLU A C    1 
ATOM   1025 O O    . GLU A 1 64  ? -20.77400 26.82500 -2.06700  1.000 45.04487  ? 64  GLU A O    1 
ATOM   1026 C CB   . GLU A 1 64  ? -23.25000 27.12900 0.19900   1.000 36.50964  ? 64  GLU A CB   1 
ATOM   1027 C CG   . GLU A 1 64  ? -23.66400 28.39200 -0.54400  1.000 41.97872  ? 64  GLU A CG   1 
ATOM   1028 C CD   . GLU A 1 64  ? -24.33200 29.40500 0.40700   1.000 60.77044  ? 64  GLU A CD   1 
ATOM   1029 O OE1  . GLU A 1 64  ? -23.92600 29.50000 1.59600   1.000 81.17552  ? 64  GLU A OE1  1 
ATOM   1030 O OE2  . GLU A 1 64  ? -25.27400 30.10900 -0.02400  1.000 84.29958  ? 64  GLU A OE2  1 
ATOM   1031 H H    . GLU A 1 64  ? -22.98300 24.82300 0.86900   1.000 41.48000  ? 64  GLU A H    1 
ATOM   1032 H HA   . GLU A 1 64  ? -23.01300 25.95900 -1.46000  1.000 48.45000  ? 64  GLU A HA   1 
ATOM   1033 H HB2  . GLU A 1 64  ? -24.05600 26.73800 0.57200   1.000 44.44000  ? 64  GLU A HB2  1 
ATOM   1034 H HB3  . GLU A 1 64  ? -22.66200 27.40000 0.92100   1.000 44.44000  ? 64  GLU A HB3  1 
ATOM   1035 H HG2  . GLU A 1 64  ? -22.87800 28.80900 -0.93100  1.000 51.00000  ? 64  GLU A HG2  1 
ATOM   1036 H HG3  . GLU A 1 64  ? -24.30000 28.16200 -1.23900  1.000 51.00000  ? 64  GLU A HG3  1 
ATOM   1037 N N    . GLN A 1 65  ? -20.18900 26.24500 0.02900   1.000 42.86303  ? 65  GLN A N    1 
ATOM   1038 C CA   . GLN A 1 65  ? -18.77700 26.55100 -0.17700  1.000 39.37577  ? 65  GLN A CA   1 
ATOM   1039 C C    . GLN A 1 65  ? -18.12300 25.59500 -1.17000  1.000 31.74328  ? 65  GLN A C    1 
ATOM   1040 O O    . GLN A 1 65  ? -17.48700 26.01900 -2.13100  1.000 44.08950  ? 65  GLN A O    1 
ATOM   1041 C CB   . GLN A 1 65  ? -18.02300 26.49700 1.15100   1.000 52.93266  ? 65  GLN A CB   1 
ATOM   1042 C CG   . GLN A 1 65  ? -18.23500 27.70400 2.04200   1.000 81.82034  ? 65  GLN A CG   1 
ATOM   1043 C CD   . GLN A 1 65  ? -17.68300 27.48100 3.46000   1.000 117.26143 ? 65  GLN A CD   1 
ATOM   1044 O OE1  . GLN A 1 65  ? -17.04500 26.45000 3.73400   1.000 105.78110 ? 65  GLN A OE1  1 
ATOM   1045 N NE2  . GLN A 1 65  ? -17.93800 28.43900 4.36600   1.000 118.57738 ? 65  GLN A NE2  1 
ATOM   1046 H H    . GLN A 1 65  ? -20.37100 25.93400 0.81000   1.000 52.06000  ? 65  GLN A H    1 
ATOM   1047 H HA   . GLN A 1 65  ? -18.69800 27.45100 -0.53100  1.000 47.88000  ? 65  GLN A HA   1 
ATOM   1048 H HB2  . GLN A 1 65  ? -18.31600 25.71300 1.64200   1.000 64.14000  ? 65  GLN A HB2  1 
ATOM   1049 H HB3  . GLN A 1 65  ? -17.07300 26.43100 0.96600   1.000 64.14000  ? 65  GLN A HB3  1 
ATOM   1050 H HG2  . GLN A 1 65  ? -17.77800 28.46800 1.65700   1.000 98.81000  ? 65  GLN A HG2  1 
ATOM   1051 H HG3  . GLN A 1 65  ? -19.18500 27.88400 2.11300   1.000 98.81000  ? 65  GLN A HG3  1 
ATOM   1052 H HE21 . GLN A 1 65  ? -18.38500 29.13800 4.13900   1.000 142.92000 ? 65  GLN A HE21 1 
ATOM   1053 H HE22 . GLN A 1 65  ? -17.65000 28.35600 5.17200   1.000 142.92000 ? 65  GLN A HE22 1 
ATOM   1054 N N    . GLU A 1 66  ? -18.19400 24.29300 -0.90600  1.000 30.75895  ? 66  GLU A N    1 
ATOM   1055 C CA   . GLU A 1 66  ? -17.65600 23.33600 -1.87100  1.000 26.52950  ? 66  GLU A CA   1 
ATOM   1056 C C    . GLU A 1 66  ? -18.07000 23.68100 -3.29800  1.000 44.12898  ? 66  GLU A C    1 
ATOM   1057 O O    . GLU A 1 66  ? -17.27900 23.53600 -4.23400  1.000 45.87129  ? 66  GLU A O    1 
ATOM   1058 C CB   . GLU A 1 66  ? -18.14300 21.94200 -1.45600  1.000 40.53644  ? 66  GLU A CB   1 
ATOM   1059 C CG   . GLU A 1 66  ? -17.21200 20.77400 -1.76700  1.000 42.51299  ? 66  GLU A CG   1 
ATOM   1060 C CD   . GLU A 1 66  ? -17.79400 19.40200 -1.30000  1.000 72.87716  ? 66  GLU A CD   1 
ATOM   1061 O OE1  . GLU A 1 66  ? -18.63600 19.35600 -0.36000  1.000 64.54721  ? 66  GLU A OE1  1 
ATOM   1062 O OE2  . GLU A 1 66  ? -17.40900 18.36100 -1.89500  1.000 74.31681  ? 66  GLU A OE2  1 
ATOM   1063 H H    . GLU A 1 66  ? -18.53800 23.94700 -0.19800  1.000 37.54000  ? 66  GLU A H    1 
ATOM   1064 H HA   . GLU A 1 66  ? -16.68700 23.34600 -1.82500  1.000 32.46000  ? 66  GLU A HA   1 
ATOM   1065 H HB2  . GLU A 1 66  ? -18.28900 21.94100 -0.49700  1.000 49.27000  ? 66  GLU A HB2  1 
ATOM   1066 H HB3  . GLU A 1 66  ? -18.98300 21.76800 -1.90800  1.000 49.27000  ? 66  GLU A HB3  1 
ATOM   1067 H HG2  . GLU A 1 66  ? -17.08800 20.73200 -2.72600  1.000 51.64000  ? 66  GLU A HG2  1 
ATOM   1068 H HG3  . GLU A 1 66  ? -16.36100 20.91300 -1.32200  1.000 51.64000  ? 66  GLU A HG3  1 
ATOM   1069 N N    . ILE A 1 67  ? -19.29700 24.17400 -3.47300  1.000 44.63956  ? 67  ILE A N    1 
ATOM   1070 C CA   . ILE A 1 67  ? -19.82900 24.43400 -4.80600  1.000 39.96269  ? 67  ILE A CA   1 
ATOM   1071 C C    . ILE A 1 67  ? -19.32100 25.76500 -5.32800  1.000 30.90107  ? 67  ILE A C    1 
ATOM   1072 O O    . ILE A 1 67  ? -19.02800 25.90500 -6.51900  1.000 36.32278  ? 67  ILE A O    1 
ATOM   1073 C CB   . ILE A 1 67  ? -21.37000 24.41100 -4.79800  1.000 36.86495  ? 67  ILE A CB   1 
ATOM   1074 C CG1  . ILE A 1 67  ? -21.88700 22.98300 -4.73600  1.000 28.13758  ? 67  ILE A CG1  1 
ATOM   1075 C CG2  . ILE A 1 67  ? -21.96100 25.08700 -6.06900  1.000 34.58573  ? 67  ILE A CG2  1 
ATOM   1076 C CD1  . ILE A 1 67  ? -23.31900 22.85900 -4.18100  1.000 23.57914  ? 67  ILE A CD1  1 
ATOM   1077 H H    . ILE A 1 67  ? -19.84000 24.36600 -2.83400  1.000 54.20000  ? 67  ILE A H    1 
ATOM   1078 H HA   . ILE A 1 67  ? -19.52200 23.73900 -5.40900  1.000 48.58000  ? 67  ILE A HA   1 
ATOM   1079 H HB   . ILE A 1 67  ? -21.68400 24.89000 -4.01600  1.000 44.86000  ? 67  ILE A HB   1 
ATOM   1080 H HG12 . ILE A 1 67  ? -21.88400 22.61100 -5.63200  1.000 34.39000  ? 67  ILE A HG12 1 
ATOM   1081 H HG13 . ILE A 1 67  ? -21.30200 22.46400 -4.16300  1.000 34.39000  ? 67  ILE A HG13 1 
ATOM   1082 H HG21 . ILE A 1 67  ? -22.88600 24.81300 -6.16900  1.000 42.13000  ? 67  ILE A HG21 1 
ATOM   1083 H HG22 . ILE A 1 67  ? -21.91300 26.05100 -5.96900  1.000 42.13000  ? 67  ILE A HG22 1 
ATOM   1084 H HG23 . ILE A 1 67  ? -21.44900 24.80600 -6.84300  1.000 42.13000  ? 67  ILE A HG23 1 
ATOM   1085 H HD11 . ILE A 1 67  ? -23.34600 23.24300 -3.29100  1.000 28.92000  ? 67  ILE A HD11 1 
ATOM   1086 H HD12 . ILE A 1 67  ? -23.56300 21.92100 -4.14500  1.000 28.92000  ? 67  ILE A HD12 1 
ATOM   1087 H HD13 . ILE A 1 67  ? -23.92800 23.33700 -4.76600  1.000 28.92000  ? 67  ILE A HD13 1 
ATOM   1088 N N    . GLY A 1 68  ? -19.27300 26.78200 -4.47700  1.000 33.73562  ? 68  GLY A N    1 
ATOM   1089 C CA   . GLY A 1 68  ? -18.69800 28.03100 -4.91700  1.000 35.13053  ? 68  GLY A CA   1 
ATOM   1090 C C    . GLY A 1 68  ? -17.22000 27.88300 -5.18700  1.000 38.92835  ? 68  GLY A C    1 
ATOM   1091 O O    . GLY A 1 68  ? -16.66900 28.55700 -6.05800  1.000 36.93074  ? 68  GLY A O    1 
ATOM   1092 H H    . GLY A 1 68  ? -19.55800 26.77200 -3.66600  1.000 41.11000  ? 68  GLY A H    1 
ATOM   1093 H HA2  . GLY A 1 68  ? -19.13600 28.32500 -5.73100  1.000 42.79000  ? 68  GLY A HA2  1 
ATOM   1094 H HA3  . GLY A 1 68  ? -18.82400 28.70800 -4.23400  1.000 42.79000  ? 68  GLY A HA3  1 
ATOM   1095 N N    . SER A 1 69  ? -16.55300 26.99200 -4.46900  1.000 41.00492  ? 69  SER A N    1 
ATOM   1096 C CA   . SER A 1 69  ? -15.13300 26.81600 -4.74500  1.000 45.66337  ? 69  SER A CA   1 
ATOM   1097 C C    . SER A 1 69  ? -14.92300 26.25600 -6.13500  1.000 43.28414  ? 69  SER A C    1 
ATOM   1098 O O    . SER A 1 69  ? -14.02500 26.70400 -6.86200  1.000 46.09237  ? 69  SER A O    1 
ATOM   1099 C CB   . SER A 1 69  ? -14.47900 25.89900 -3.72000  1.000 44.79748  ? 69  SER A CB   1 
ATOM   1100 O OG   . SER A 1 69  ? -14.19700 26.65100 -2.57100  1.000 53.63275  ? 69  SER A OG   1 
ATOM   1101 H H    . SER A 1 69  ? -16.87800 26.49700 -3.84500  1.000 49.83000  ? 69  SER A H    1 
ATOM   1102 H HA   . SER A 1 69  ? -14.69300 27.67900 -4.69900  1.000 55.42000  ? 69  SER A HA   1 
ATOM   1103 H HB2  . SER A 1 69  ? -15.08900 25.17900 -3.49400  1.000 54.38000  ? 69  SER A HB2  1 
ATOM   1104 H HB3  . SER A 1 69  ? -13.65400 25.54300 -4.08400  1.000 54.38000  ? 69  SER A HB3  1 
ATOM   1105 H HG   . SER A 1 69  ? -13.83500 26.16400 -1.99000  1.000 64.98000  ? 69  SER A HG   1 
ATOM   1106 N N    . LEU A 1 70  ? -15.72100 25.25400 -6.50900  1.000 46.21080  ? 70  LEU A N    1 
ATOM   1107 C CA   . LEU A 1 70  ? -15.56200 24.66500 -7.82500  1.000 33.40401  ? 70  LEU A CA   1 
ATOM   1108 C C    . LEU A 1 70  ? -15.84500 25.69100 -8.90500  1.000 42.61037  ? 70  LEU A C    1 
ATOM   1109 O O    . LEU A 1 70  ? -15.20500 25.70800 -9.96300  1.000 38.46777  ? 70  LEU A O    1 
ATOM   1110 C CB   . LEU A 1 70  ? -16.49800 23.47800 -8.00600  1.000 42.09978  ? 70  LEU A CB   1 
ATOM   1111 C CG   . LEU A 1 70  ? -15.96000 22.16500 -7.47000  1.000 47.65045  ? 70  LEU A CG   1 
ATOM   1112 C CD1  . LEU A 1 70  ? -17.10400 21.24100 -7.16900  1.000 59.62820  ? 70  LEU A CD1  1 
ATOM   1113 C CD2  . LEU A 1 70  ? -15.06400 21.48100 -8.48500  1.000 60.84151  ? 70  LEU A CD2  1 
ATOM   1114 H H    . LEU A 1 70  ? -16.34500 24.90900 -6.02800  1.000 56.08000  ? 70  LEU A H    1 
ATOM   1115 H HA   . LEU A 1 70  ? -14.64900 24.35400 -7.93000  1.000 40.71000  ? 70  LEU A HA   1 
ATOM   1116 H HB2  . LEU A 1 70  ? -17.33000 23.66600 -7.54400  1.000 51.15000  ? 70  LEU A HB2  1 
ATOM   1117 H HB3  . LEU A 1 70  ? -16.67000 23.36100 -8.95300  1.000 51.15000  ? 70  LEU A HB3  1 
ATOM   1118 H HG   . LEU A 1 70  ? -15.45600 22.31900 -6.65600  1.000 57.81000  ? 70  LEU A HG   1 
ATOM   1119 H HD11 . LEU A 1 70  ? -16.75000 20.39100 -6.86300  1.000 72.18000  ? 70  LEU A HD11 1 
ATOM   1120 H HD12 . LEU A 1 70  ? -17.65700 21.63800 -6.47800  1.000 72.18000  ? 70  LEU A HD12 1 
ATOM   1121 H HD13 . LEU A 1 70  ? -17.62500 21.11100 -7.97700  1.000 72.18000  ? 70  LEU A HD13 1 
ATOM   1122 H HD21 . LEU A 1 70  ? -14.73000 20.65400 -8.10400  1.000 73.64000  ? 70  LEU A HD21 1 
ATOM   1123 H HD22 . LEU A 1 70  ? -15.58000 21.29300 -9.28500  1.000 73.64000  ? 70  LEU A HD22 1 
ATOM   1124 H HD23 . LEU A 1 70  ? -14.32300 22.07000 -8.69900  1.000 73.64000  ? 70  LEU A HD23 1 
ATOM   1125 N N    . LYS A 1 71  ? -16.84800 26.51400 -8.68600  1.000 37.37027  ? 71  LYS A N    1 
ATOM   1126 C CA   . LYS A 1 71  ? -17.17800 27.47900 -9.71200  1.000 33.15134  ? 71  LYS A CA   1 
ATOM   1127 C C    . LYS A 1 71  ? -16.04400 28.45200 -9.86900  1.000 34.64363  ? 71  LYS A C    1 
ATOM   1128 O O    . LYS A 1 71  ? -15.69200 28.83600 -10.99000 1.000 35.47004  ? 71  LYS A O    1 
ATOM   1129 C CB   . LYS A 1 71  ? -18.45300 28.23200 -9.35000  1.000 34.53572  ? 71  LYS A CB   1 
ATOM   1130 C CG   . LYS A 1 71  ? -19.69100 27.42300 -9.49700  1.000 44.61588  ? 71  LYS A CG   1 
ATOM   1131 C CD   . LYS A 1 71  ? -20.93100 28.32900 -9.46100  1.000 53.60643  ? 71  LYS A CD   1 
ATOM   1132 C CE   . LYS A 1 71  ? -21.31200 28.74600 -8.05200  1.000 57.14106  ? 71  LYS A CE   1 
ATOM   1133 N NZ   . LYS A 1 71  ? -22.63200 29.46000 -8.07000  1.000 55.61456  ? 71  LYS A NZ   1 
ATOM   1134 H H    . LYS A 1 71  ? -17.33800 26.53700 -7.98000  1.000 45.47000  ? 71  LYS A H    1 
ATOM   1135 H HA   . LYS A 1 71  ? -17.31600 27.02300 -10.55700 1.000 40.41000  ? 71  LYS A HA   1 
ATOM   1136 H HB2  . LYS A 1 71  ? -18.39400 28.51900 -8.42500  1.000 42.07000  ? 71  LYS A HB2  1 
ATOM   1137 H HB3  . LYS A 1 71  ? -18.53100 29.00600 -9.92900  1.000 42.07000  ? 71  LYS A HB3  1 
ATOM   1138 H HG2  . LYS A 1 71  ? -19.67500 26.95800 -10.34800 1.000 54.17000  ? 71  LYS A HG2  1 
ATOM   1139 H HG3  . LYS A 1 71  ? -19.75200 26.78900 -8.76600  1.000 54.17000  ? 71  LYS A HG3  1 
ATOM   1140 H HD2  . LYS A 1 71  ? -20.75500 29.13300 -9.97500  1.000 64.96000  ? 71  LYS A HD2  1 
ATOM   1141 H HD3  . LYS A 1 71  ? -21.68200 27.84900 -9.84400  1.000 64.96000  ? 71  LYS A HD3  1 
ATOM   1142 H HE2  . LYS A 1 71  ? -21.39400 27.95900 -7.49100  1.000 69.20000  ? 71  LYS A HE2  1 
ATOM   1143 H HE3  . LYS A 1 71  ? -20.63900 29.34900 -7.69800  1.000 69.20000  ? 71  LYS A HE3  1 
ATOM   1144 H HZ1  . LYS A 1 71  ? -23.25900 28.93200 -8.41600  1.000 67.37000  ? 71  LYS A HZ1  1 
ATOM   1145 H HZ2  . LYS A 1 71  ? -22.57100 30.19800 -8.56300  1.000 67.37000  ? 71  LYS A HZ2  1 
ATOM   1146 H HZ3  . LYS A 1 71  ? -22.86800 29.68400 -7.24200  1.000 67.37000  ? 71  LYS A HZ3  1 
ATOM   1147 N N    . GLN A 1 72  ? -15.47400 28.87400 -8.75800  1.000 40.53644  ? 72  GLN A N    1 
ATOM   1148 C CA   . GLN A 1 72  ? -14.44500 29.90700 -8.75800  1.000 37.75189  ? 72  GLN A CA   1 
ATOM   1149 C C    . GLN A 1 72  ? -13.11100 29.34200 -9.21800  1.000 41.42076  ? 72  GLN A C    1 
ATOM   1150 O O    . GLN A 1 72  ? -12.35300 30.03800 -9.89000  1.000 40.07323  ? 72  GLN A O    1 
ATOM   1151 C CB   . GLN A 1 72  ? -14.35000 30.51400 -7.35700  1.000 31.16953  ? 72  GLN A CB   1 
ATOM   1152 C CG   . GLN A 1 72  ? -13.52700 31.78700 -7.26400  1.000 38.43882  ? 72  GLN A CG   1 
ATOM   1153 C CD   . GLN A 1 72  ? -13.86600 32.79000 -8.35200  1.000 38.35460  ? 72  GLN A CD   1 
ATOM   1154 O OE1  . GLN A 1 72  ? -15.01700 32.87700 -8.79300  1.000 37.60977  ? 72  GLN A OE1  1 
ATOM   1155 N NE2  . GLN A 1 72  ? -12.86100 33.54700 -8.79900  1.000 36.40700  ? 72  GLN A NE2  1 
ATOM   1156 H H    . GLN A 1 72  ? -15.66600 28.57600 -7.97400  1.000 49.27000  ? 72  GLN A H    1 
ATOM   1157 H HA   . GLN A 1 72  ? -14.70800 30.59700 -9.38500  1.000 45.93000  ? 72  GLN A HA   1 
ATOM   1158 H HB2  . GLN A 1 72  ? -15.24600 30.72300 -7.05000  1.000 38.03000  ? 72  GLN A HB2  1 
ATOM   1159 H HB3  . GLN A 1 72  ? -13.94800 29.86100 -6.76400  1.000 38.03000  ? 72  GLN A HB3  1 
ATOM   1160 H HG2  . GLN A 1 72  ? -13.69200 32.20800 -6.40600  1.000 46.76000  ? 72  GLN A HG2  1 
ATOM   1161 H HG3  . GLN A 1 72  ? -12.58800 31.56200 -7.34800  1.000 46.76000  ? 72  GLN A HG3  1 
ATOM   1162 H HE21 . GLN A 1 72  ? -12.07300 33.45500 -8.46700  1.000 44.32000  ? 72  GLN A HE21 1 
ATOM   1163 H HE22 . GLN A 1 72  ? -13.00300 34.12900 -9.41600  1.000 44.32000  ? 72  GLN A HE22 1 
ATOM   1164 N N    . ARG A 1 73  ? -12.82400 28.09200 -8.87600  1.000 32.97501  ? 73  ARG A N    1 
ATOM   1165 C CA   . ARG A 1 73  ? -11.66200 27.40500 -9.42800  1.000 25.33988  ? 73  ARG A CA   1 
ATOM   1166 C C    . ARG A 1 73  ? -11.73500 27.31600 -10.94500 1.000 30.73263  ? 73  ARG A C    1 
ATOM   1167 O O    . ARG A 1 73  ? -10.70800 27.40100 -11.63300 1.000 42.20506  ? 73  ARG A O    1 
ATOM   1168 C CB   . ARG A 1 73  ? -11.58100 26.02500 -8.77800  1.000 37.29658  ? 73  ARG A CB   1 
ATOM   1169 C CG   . ARG A 1 73  ? -10.23200 25.39200 -8.69100  1.000 53.86698  ? 73  ARG A CG   1 
ATOM   1170 C CD   . ARG A 1 73  ? -10.33400 24.11600 -7.83000  1.000 70.86639  ? 73  ARG A CD   1 
ATOM   1171 N NE   . ARG A 1 73  ? -10.44100 24.38200 -6.39400  1.000 72.85347  ? 73  ARG A NE   1 
ATOM   1172 C CZ   . ARG A 1 73  ? -9.41000  24.69700 -5.61200  1.000 93.02694  ? 73  ARG A CZ   1 
ATOM   1173 N NH1  . ARG A 1 73  ? -8.18600  24.87800 -6.10900  1.000 72.03758  ? 73  ARG A NH1  1 
ATOM   1174 N NH2  . ARG A 1 73  ? -9.61000  24.83800 -4.29900  1.000 73.16140  ? 73  ARG A NH2  1 
ATOM   1175 H H    . ARG A 1 73  ? -13.28700 27.61900 -8.32700  1.000 40.20000  ? 73  ARG A H    1 
ATOM   1176 H HA   . ARG A 1 73  ? -10.86000 27.89700 -9.19300  1.000 31.03000  ? 73  ARG A HA   1 
ATOM   1177 H HB2  . ARG A 1 73  ? -11.91600 26.09800 -7.87100  1.000 45.38000  ? 73  ARG A HB2  1 
ATOM   1178 H HB3  . ARG A 1 73  ? -12.14900 25.42100 -9.28100  1.000 45.38000  ? 73  ARG A HB3  1 
ATOM   1179 H HG2  . ARG A 1 73  ? -9.92700  25.14600 -9.57800  1.000 65.27000  ? 73  ARG A HG2  1 
ATOM   1180 H HG3  . ARG A 1 73  ? -9.60900  26.00400 -8.26900  1.000 65.27000  ? 73  ARG A HG3  1 
ATOM   1181 H HD2  . ARG A 1 73  ? -11.12300 23.62000 -8.09900  1.000 85.67000  ? 73  ARG A HD2  1 
ATOM   1182 H HD3  . ARG A 1 73  ? -9.54100  23.57600 -7.97500  1.000 85.67000  ? 73  ARG A HD3  1 
ATOM   1183 H HE   . ARG A 1 73  ? -11.22000 24.33200 -6.03200  1.000 88.05000  ? 73  ARG A HE   1 
ATOM   1184 H HH11 . ARG A 1 73  ? -8.04400  24.78700 -6.95200  1.000 87.07000  ? 73  ARG A HH11 1 
ATOM   1185 H HH12 . ARG A 1 73  ? -7.53600  25.08300 -5.58400  1.000 87.07000  ? 73  ARG A HH12 1 
ATOM   1186 H HH21 . ARG A 1 73  ? -10.39600 24.72600 -3.96900  1.000 88.42000  ? 73  ARG A HH21 1 
ATOM   1187 H HH22 . ARG A 1 73  ? -8.95400  25.04700 -3.78400  1.000 88.42000  ? 73  ARG A HH22 1 
ATOM   1188 N N    . ALA A 1 74  ? -12.92900 27.14800 -11.50200 1.000 44.33163  ? 74  ALA A N    1 
ATOM   1189 C CA   . ALA A 1 74  ? -13.02600 27.17500 -12.95800 1.000 42.68670  ? 74  ALA A CA   1 
ATOM   1190 C C    . ALA A 1 74  ? -12.66200 28.55200 -13.47500 1.000 25.35567  ? 74  ALA A C    1 
ATOM   1191 O O    . ALA A 1 74  ? -12.02700 28.69900 -14.53000 1.000 33.12766  ? 74  ALA A O    1 
ATOM   1192 C CB   . ALA A 1 74  ? -14.43000 26.80800 -13.43100 1.000 39.96005  ? 74  ALA A CB   1 
ATOM   1193 H H    . ALA A 1 74  ? -13.66900 27.02200 -11.08200 1.000 53.83000  ? 74  ALA A H    1 
ATOM   1194 H HA   . ALA A 1 74  ? -12.40200 26.53400 -13.33300 1.000 51.85000  ? 74  ALA A HA   1 
ATOM   1195 H HB1  . ALA A 1 74  ? -14.64400 25.91400 -13.12100 1.000 48.58000  ? 74  ALA A HB1  1 
ATOM   1196 H HB2  . ALA A 1 74  ? -15.06300 27.44600 -13.06500 1.000 48.58000  ? 74  ALA A HB2  1 
ATOM   1197 H HB3  . ALA A 1 74  ? -14.45400 26.83700 -14.40000 1.000 48.58000  ? 74  ALA A HB3  1 
ATOM   1198 N N    . GLN A 1 75  ? -13.06100 29.57200 -12.72500 1.000 35.08052  ? 75  GLN A N    1 
ATOM   1199 C CA   . GLN A 1 75  ? -12.72800 30.93200 -13.09000 1.000 29.85095  ? 75  GLN A CA   1 
ATOM   1200 C C    . GLN A 1 75  ? -11.22800 31.16600 -12.99000 1.000 29.21403  ? 75  GLN A C    1 
ATOM   1201 O O    . GLN A 1 75  ? -10.64600 31.91600 -13.79100 1.000 34.72522  ? 75  GLN A O    1 
ATOM   1202 C CB   . GLN A 1 75  ? -13.49700 31.87400 -12.17200 1.000 41.58130  ? 75  GLN A CB   1 
ATOM   1203 C CG   . GLN A 1 75  ? -13.49200 33.32300 -12.61700 1.000 50.44026  ? 75  GLN A CG   1 
ATOM   1204 C CD   . GLN A 1 75  ? -14.10400 33.51800 -14.00700 1.000 81.98088  ? 75  GLN A CD   1 
ATOM   1205 O OE1  . GLN A 1 75  ? -14.88400 32.66800 -14.51700 1.000 58.46227  ? 75  GLN A OE1  1 
ATOM   1206 N NE2  . GLN A 1 75  ? -13.74200 34.64400 -14.63900 1.000 53.51431  ? 75  GLN A NE2  1 
ATOM   1207 H H    . GLN A 1 75  ? -13.52400 29.50000 -12.00400 1.000 42.72000  ? 75  GLN A H    1 
ATOM   1208 H HA   . GLN A 1 75  ? -13.00300 31.09300 -14.00600 1.000 36.45000  ? 75  GLN A HA   1 
ATOM   1209 H HB2  . GLN A 1 75  ? -14.42100 31.58200 -12.12900 1.000 50.53000  ? 75  GLN A HB2  1 
ATOM   1210 H HB3  . GLN A 1 75  ? -13.10200 31.83900 -11.28800 1.000 50.53000  ? 75  GLN A HB3  1 
ATOM   1211 H HG2  . GLN A 1 75  ? -14.00800 33.84900 -11.98600 1.000 61.15000  ? 75  GLN A HG2  1 
ATOM   1212 H HG3  . GLN A 1 75  ? -12.57600 33.64200 -12.64500 1.000 61.15000  ? 75  GLN A HG3  1 
ATOM   1213 H HE21 . GLN A 1 75  ? -13.20600 35.19800 -14.25800 1.000 64.84000  ? 75  GLN A HE21 1 
ATOM   1214 H HE22 . GLN A 1 75  ? -14.04900 34.81400 -15.42400 1.000 64.84000  ? 75  GLN A HE22 1 
ATOM   1215 N N    . VAL A 1 76  ? -10.57300 30.55800 -12.00800 1.000 31.61432  ? 76  VAL A N    1 
ATOM   1216 C CA   . VAL A 1 76  ? -9.13200  30.73200 -11.93300 1.000 24.35029  ? 76  VAL A CA   1 
ATOM   1217 C C    . VAL A 1 76  ? -8.45200  30.07400 -13.11700 1.000 26.51107  ? 76  VAL A C    1 
ATOM   1218 O O    . VAL A 1 76  ? -7.52300  30.63600 -13.70900 1.000 27.48751  ? 76  VAL A O    1 
ATOM   1219 C CB   . VAL A 1 76  ? -8.57800  30.18300 -10.62300 1.000 27.15589  ? 76  VAL A CB   1 
ATOM   1220 C CG1  . VAL A 1 76  ? -7.02000  30.02000 -10.79700 1.000 28.19285  ? 76  VAL A CG1  1 
ATOM   1221 C CG2  . VAL A 1 76  ? -8.91900  31.10200 -9.50000  1.000 23.13698  ? 76  VAL A CG2  1 
ATOM   1222 H H    . VAL A 1 76  ? -10.92200 30.06100 -11.39900 1.000 38.56000  ? 76  VAL A H    1 
ATOM   1223 H HA   . VAL A 1 76  ? -8.93000  31.68000 -11.96500 1.000 29.85000  ? 76  VAL A HA   1 
ATOM   1224 H HB   . VAL A 1 76  ? -8.96500  29.31200 -10.44300 1.000 33.21000  ? 76  VAL A HB   1 
ATOM   1225 H HG11 . VAL A 1 76  ? -6.83100  29.19700 -11.27500 1.000 34.46000  ? 76  VAL A HG11 1 
ATOM   1226 H HG12 . VAL A 1 76  ? -6.61400  29.98400 -9.91700  1.000 34.46000  ? 76  VAL A HG12 1 
ATOM   1227 H HG13 . VAL A 1 76  ? -6.67000  30.78200 -11.28500 1.000 34.46000  ? 76  VAL A HG13 1 
ATOM   1228 H HG21 . VAL A 1 76  ? -8.51900  31.96900 -9.66900  1.000 28.39000  ? 76  VAL A HG21 1 
ATOM   1229 H HG22 . VAL A 1 76  ? -8.57100  30.73200 -8.67400  1.000 28.39000  ? 76  VAL A HG22 1 
ATOM   1230 H HG23 . VAL A 1 76  ? -9.88400  31.18700 -9.44400  1.000 28.39000  ? 76  VAL A HG23 1 
ATOM   1231 N N    . GLU A 1 77  ? -8.91600  28.88300 -13.51600 1.000 29.06927  ? 77  GLU A N    1 
ATOM   1232 C CA   . GLU A 1 77  ? -8.26600  28.18900 -14.62100 1.000 31.78276  ? 77  GLU A CA   1 
ATOM   1233 C C    . GLU A 1 77  ? -8.44500  28.95000 -15.92200 1.000 22.75273  ? 77  GLU A C    1 
ATOM   1234 O O    . GLU A 1 77  ? -7.51000  29.07400 -16.71300 1.000 35.86219  ? 77  GLU A O    1 
ATOM   1235 C CB   . GLU A 1 77  ? -8.83300  26.76900 -14.76300 1.000 35.04894  ? 77  GLU A CB   1 
ATOM   1236 C CG   . GLU A 1 77  ? -8.55200  25.91800 -13.55300 1.000 41.68921  ? 77  GLU A CG   1 
ATOM   1237 C CD   . GLU A 1 77  ? -9.38800  24.64800 -13.46100 1.000 56.61731  ? 77  GLU A CD   1 
ATOM   1238 O OE1  . GLU A 1 77  ? -10.31100 24.40000 -14.29700 1.000 60.30723  ? 77  GLU A OE1  1 
ATOM   1239 O OE2  . GLU A 1 77  ? -9.11500  23.88400 -12.50900 1.000 75.29587  ? 77  GLU A OE2  1 
ATOM   1240 H H    . GLU A 1 77  ? -9.58700  28.47000 -13.17100 1.000 35.51000  ? 77  GLU A H    1 
ATOM   1241 H HA   . GLU A 1 77  ? -7.31600  28.11900 -14.43900 1.000 38.77000  ? 77  GLU A HA   1 
ATOM   1242 H HB2  . GLU A 1 77  ? -9.79500  26.82100 -14.87800 1.000 42.69000  ? 77  GLU A HB2  1 
ATOM   1243 H HB3  . GLU A 1 77  ? -8.42800  26.34100 -15.53300 1.000 42.69000  ? 77  GLU A HB3  1 
ATOM   1244 H HG2  . GLU A 1 77  ? -7.61900  25.65400 -13.57200 1.000 50.66000  ? 77  GLU A HG2  1 
ATOM   1245 H HG3  . GLU A 1 77  ? -8.72600  26.44100 -12.75500 1.000 50.66000  ? 77  GLU A HG3  1 
ATOM   1246 N N    . LYS A 1 78  ? -9.66200  29.41300 -16.18600 1.000 32.47231  ? 78  LYS A N    1 
ATOM   1247 C CA   . LYS A 1 78  ? -9.93900  30.18900 -17.38700 1.000 28.03494  ? 78  LYS A CA   1 
ATOM   1248 C C    . LYS A 1 78  ? -9.02700  31.39400 -17.47400 1.000 31.89593  ? 78  LYS A C    1 
ATOM   1249 O O    . LYS A 1 78  ? -8.43400  31.65900 -18.51500 1.000 32.76182  ? 78  LYS A O    1 
ATOM   1250 C CB   . LYS A 1 78  ? -11.42100 30.59800 -17.34400 1.000 34.47255  ? 78  LYS A CB   1 
ATOM   1251 C CG   . LYS A 1 78  ? -12.03400 31.28300 -18.58200 1.000 48.01102  ? 78  LYS A CG   1 
ATOM   1252 C CD   . LYS A 1 78  ? -13.29400 32.09800 -18.13800 1.000 72.07443  ? 78  LYS A CD   1 
ATOM   1253 C CE   . LYS A 1 78  ? -14.19000 32.58500 -19.29200 1.000 88.19215  ? 78  LYS A CE   1 
ATOM   1254 N NZ   . LYS A 1 78  ? -15.15400 33.64700 -18.82600 1.000 81.51240  ? 78  LYS A NZ   1 
ATOM   1255 H H    . LYS A 1 78  ? -10.34800 29.29000 -15.68200 1.000 39.59000  ? 78  LYS A H    1 
ATOM   1256 H HA   . LYS A 1 78  ? -9.79400  29.63600 -18.17100 1.000 34.27000  ? 78  LYS A HA   1 
ATOM   1257 H HB2  . LYS A 1 78  ? -11.94400 29.79800 -17.17900 1.000 42.00000  ? 78  LYS A HB2  1 
ATOM   1258 H HB3  . LYS A 1 78  ? -11.53800 31.20900 -16.60000 1.000 42.00000  ? 78  LYS A HB3  1 
ATOM   1259 H HG2  . LYS A 1 78  ? -11.39000 31.89500 -18.96900 1.000 58.24000  ? 78  LYS A HG2  1 
ATOM   1260 H HG3  . LYS A 1 78  ? -12.30600 30.61300 -19.22900 1.000 58.24000  ? 78  LYS A HG3  1 
ATOM   1261 H HD2  . LYS A 1 78  ? -13.83700 31.53800 -17.56200 1.000 87.12000  ? 78  LYS A HD2  1 
ATOM   1262 H HD3  . LYS A 1 78  ? -12.99800 32.88000 -17.64600 1.000 87.12000  ? 78  LYS A HD3  1 
ATOM   1263 H HE2  . LYS A 1 78  ? -13.63500 32.96300 -19.99200 1.000 106.46000 ? 78  LYS A HE2  1 
ATOM   1264 H HE3  . LYS A 1 78  ? -14.70300 31.83800 -19.63700 1.000 106.46000 ? 78  LYS A HE3  1 
ATOM   1265 H HZ1  . LYS A 1 78  ? -15.66200 33.91500 -19.50600 1.000 98.44000  ? 78  LYS A HZ1  1 
ATOM   1266 H HZ2  . LYS A 1 78  ? -15.67800 33.32200 -18.18400 1.000 98.44000  ? 78  LYS A HZ2  1 
ATOM   1267 H HZ3  . LYS A 1 78  ? -14.70500 34.34600 -18.50700 1.000 98.44000  ? 78  LYS A HZ3  1 
ATOM   1268 N N    . THR A 1 79  ? -8.90000  32.14200 -16.39400 1.000 25.36883  ? 79  THR A N    1 
ATOM   1269 C CA   . THR A 1 79  ? -8.15300  33.39300 -16.46500 1.000 25.54780  ? 79  THR A CA   1 
ATOM   1270 C C    . THR A 1 79  ? -6.65800  33.16700 -16.53000 1.000 24.61611  ? 79  THR A C    1 
ATOM   1271 O O    . THR A 1 79  ? -5.92000  33.93200 -17.18500 1.000 22.84221  ? 79  THR A O    1 
ATOM   1272 C CB   . THR A 1 79  ? -8.46200  34.26100 -15.24900 1.000 29.76409  ? 79  THR A CB   1 
ATOM   1273 O OG1  . THR A 1 79  ? -8.25700  33.50400 -14.04400 1.000 21.27097  ? 79  THR A OG1  1 
ATOM   1274 C CG2  . THR A 1 79  ? -9.90100  34.72600 -15.31100 1.000 24.54768  ? 79  THR A CG2  1 
ATOM   1275 H H    . THR A 1 79  ? -9.22800  31.95700 -15.62100 1.000 31.07000  ? 79  THR A H    1 
ATOM   1276 H HA   . THR A 1 79  ? -8.42100  33.87900 -17.26000 1.000 31.29000  ? 79  THR A HA   1 
ATOM   1277 H HB   . THR A 1 79  ? -7.88400  35.04000 -15.24800 1.000 36.34000  ? 79  THR A HB   1 
ATOM   1278 H HG1  . THR A 1 79  ? -8.82200  32.88500 -13.99200 1.000 25.53000  ? 79  THR A HG1  1 
ATOM   1279 H HG21 . THR A 1 79  ? -10.10000 35.29000 -14.54700 1.000 30.08000  ? 79  THR A HG21 1 
ATOM   1280 H HG22 . THR A 1 79  ? -10.05000 35.23300 -16.12400 1.000 30.08000  ? 79  THR A HG22 1 
ATOM   1281 H HG23 . THR A 1 79  ? -10.49800 33.96100 -15.30200 1.000 30.08000  ? 79  THR A HG23 1 
ATOM   1282 N N    . MET A 1 80  ? -6.18500  32.18400 -15.77200 1.000 22.98433  ? 80  MET A N    1 
ATOM   1283 C CA   . MET A 1 80  ? -4.77600  31.83600 -15.86900 1.000 21.81314  ? 80  MET A CA   1 
ATOM   1284 C C    . MET A 1 80  ? -4.43500  31.37900 -17.25800 1.000 21.99211  ? 80  MET A C    1 
ATOM   1285 O O    . MET A 1 80  ? -3.42900  31.76600 -17.80900 1.000 25.33198  ? 80  MET A O    1 
ATOM   1286 C CB   . MET A 1 80  ? -4.45300  30.77200 -14.82100 1.000 23.86602  ? 80  MET A CB   1 
ATOM   1287 C CG   . MET A 1 80  ? -4.55400  31.23900 -13.40600 1.000 25.29777  ? 80  MET A CG   1 
ATOM   1288 S SD   . MET A 1 80  ? -3.35600  32.51900 -13.01900 1.000 25.36620  ? 80  MET A SD   1 
ATOM   1289 C CE   . MET A 1 80  ? -1.76600  31.90500 -13.55900 1.000 22.80010  ? 80  MET A CE   1 
ATOM   1290 H H    . MET A 1 80  ? -6.64200  31.71800 -15.21200 1.000 28.21000  ? 80  MET A H    1 
ATOM   1291 H HA   . MET A 1 80  ? -4.24800  32.62300 -15.66600 1.000 24.55000  ? 80  MET A HA   1 
ATOM   1292 H HB2  . MET A 1 80  ? -5.07500  30.03600 -14.92900 1.000 29.26000  ? 80  MET A HB2  1 
ATOM   1293 H HB3  . MET A 1 80  ? -3.54800  30.45500 -14.96700 1.000 29.26000  ? 80  MET A HB3  1 
ATOM   1294 H HG2  . MET A 1 80  ? -5.43700  31.60700 -13.25400 1.000 30.98000  ? 80  MET A HG2  1 
ATOM   1295 H HG3  . MET A 1 80  ? -4.39800  30.49000 -12.81100 1.000 30.98000  ? 80  MET A HG3  1 
ATOM   1296 H HE1  . MET A 1 80  ? -1.60900  31.03800 -13.15400 1.000 24.22000  ? 80  MET A HE1  1 
ATOM   1297 H HE2  . MET A 1 80  ? -1.07700  32.52900 -13.28300 1.000 24.22000  ? 80  MET A HE2  1 
ATOM   1298 H HE3  . MET A 1 80  ? -1.77000  31.82300 -14.52500 1.000 24.22000  ? 80  MET A HE3  1 
ATOM   1299 N N    . SER A 1 81  ? -5.26500  30.58300 -17.86700 1.000 24.42924  ? 81  SER A N    1 
ATOM   1300 C CA   . SER A 1 81  ? -4.95200  30.12700 -19.21100 1.000 26.62688  ? 81  SER A CA   1 
ATOM   1301 C C    . SER A 1 81  ? -4.84700  31.30800 -20.18100 1.000 23.06856  ? 81  SER A C    1 
ATOM   1302 O O    . SER A 1 81  ? -3.91000  31.38700 -20.98400 1.000 30.02728  ? 81  SER A O    1 
ATOM   1303 C CB   . SER A 1 81  ? -6.01400  29.12300 -19.66700 1.000 25.73466  ? 81  SER A CB   1 
ATOM   1304 O OG   . SER A 1 81  ? -5.71200  28.58100 -20.94900 1.000 51.40616  ? 81  SER A OG   1 
ATOM   1305 H H    . SER A 1 81  ? -6.00600  30.29000 -17.54300 1.000 29.94000  ? 81  SER A H    1 
ATOM   1306 H HA   . SER A 1 81  ? -4.09500  29.67200 -19.19900 1.000 32.58000  ? 81  SER A HA   1 
ATOM   1307 H HB2  . SER A 1 81  ? -6.05700  28.39900 -19.02300 1.000 31.51000  ? 81  SER A HB2  1 
ATOM   1308 H HB3  . SER A 1 81  ? -6.87200  29.57400 -19.71200 1.000 31.51000  ? 81  SER A HB3  1 
ATOM   1309 H HG   . SER A 1 81  ? -6.33700  28.08200 -21.20500 1.000 62.31000  ? 81  SER A HG   1 
ATOM   1310 N N    . ALA A 1 82  ? -5.79100  32.26100 -20.09300 1.000 25.32672  ? 82  ALA A N    1 
ATOM   1311 C CA   . ALA A 1 82  ? -5.73200  33.43700 -20.95900 1.000 22.63692  ? 82  ALA A CA   1 
ATOM   1312 C C    . ALA A 1 82  ? -4.45300  34.18700 -20.73700 1.000 22.36058  ? 82  ALA A C    1 
ATOM   1313 O O    . ALA A 1 82  ? -3.86000  34.70200 -21.67800 1.000 28.95874  ? 82  ALA A O    1 
ATOM   1314 C CB   . ALA A 1 82  ? -6.90600  34.36000 -20.65700 1.000 23.43439  ? 82  ALA A CB   1 
ATOM   1315 H H    . ALA A 1 82  ? -6.45900  32.24600 -19.55100 1.000 31.02000  ? 82  ALA A H    1 
ATOM   1316 H HA   . ALA A 1 82  ? -5.77800  33.16400 -21.88900 1.000 27.79000  ? 82  ALA A HA   1 
ATOM   1317 H HB1  . ALA A 1 82  ? -6.85800  34.63800 -19.72900 1.000 28.75000  ? 82  ALA A HB1  1 
ATOM   1318 H HB2  . ALA A 1 82  ? -6.85500  35.13500 -21.23800 1.000 28.75000  ? 82  ALA A HB2  1 
ATOM   1319 H HB3  . ALA A 1 82  ? -7.73400  33.88000 -20.81700 1.000 28.75000  ? 82  ALA A HB3  1 
ATOM   1320 N N    . ALA A 1 83  ? -4.03200  34.27600 -19.50300 1.000 22.82379  ? 83  ALA A N    1 
ATOM   1321 C CA   . ALA A 1 83  ? -2.84700  35.04600 -19.13700 1.000 21.95790  ? 83  ALA A CA   1 
ATOM   1322 C C    . ALA A 1 83  ? -1.59100  34.33800 -19.57100 1.000 22.18687  ? 83  ALA A C    1 
ATOM   1323 O O    . ALA A 1 83  ? -0.53000  34.97000 -19.67900 1.000 32.42494  ? 83  ALA A O    1 
ATOM   1324 C CB   . ALA A 1 83  ? -2.78800  35.29700 -17.62900 1.000 27.45329  ? 83  ALA A CB   1 
ATOM   1325 H H    . ALA A 1 83  ? -4.41600  33.89500 -18.83500 1.000 28.02000  ? 83  ALA A H    1 
ATOM   1326 H HA   . ALA A 1 83  ? -2.87800  35.90600 -19.58400 1.000 24.02000  ? 83  ALA A HA   1 
ATOM   1327 H HB1  . ALA A 1 83  ? -3.57700  35.79300 -17.36100 1.000 33.57000  ? 83  ALA A HB1  1 
ATOM   1328 H HB2  . ALA A 1 83  ? -2.76000  34.44400 -17.16800 1.000 33.57000  ? 83  ALA A HB2  1 
ATOM   1329 H HB3  . ALA A 1 83  ? -1.99000  35.80900 -17.42600 1.000 33.57000  ? 83  ALA A HB3  1 
ATOM   1330 N N    . SER A 1 84  ? -1.67500  33.04800 -19.83500 1.000 32.45126  ? 84  SER A N    1 
ATOM   1331 C CA   . SER A 1 84  ? -0.47100  32.31300 -20.21300 1.000 33.27504  ? 84  SER A CA   1 
ATOM   1332 C C    . SER A 1 84  ? -0.31400  32.18400 -21.70600 1.000 24.20817  ? 84  SER A C    1 
ATOM   1333 O O    . SER A 1 84  ? 0.76100   31.78000 -22.17600 1.000 34.65942  ? 84  SER A O    1 
ATOM   1334 C CB   . SER A 1 84  ? -0.47700  30.94500 -19.53900 1.000 44.71852  ? 84  SER A CB   1 
ATOM   1335 O OG   . SER A 1 84  ? -0.46200  31.11700 -18.10500 1.000 52.41418  ? 84  SER A OG   1 
ATOM   1336 H H    . SER A 1 84  ? -2.39400  32.57700 -19.80500 1.000 39.57000  ? 84  SER A H    1 
ATOM   1337 H HA   . SER A 1 84  ? 0.30400   32.79100 -19.88100 1.000 40.56000  ? 84  SER A HA   1 
ATOM   1338 H HB2  . SER A 1 84  ? -1.28100  30.46700 -19.79500 1.000 54.29000  ? 84  SER A HB2  1 
ATOM   1339 H HB3  . SER A 1 84  ? 0.31100   30.44900 -19.81100 1.000 54.29000  ? 84  SER A HB3  1 
ATOM   1340 H HG   . SER A 1 84  ? -0.46500  30.36800 -17.72600 1.000 63.52000  ? 84  SER A HG   1 
ATOM   1341 N N    . GLY A 1 85  ? -1.29400  32.59900 -22.47100 1.000 60.13353  ? 85  GLY A N    1 
ATOM   1342 C CA   . GLY A 1 85  ? -1.13300  32.45100 -23.89300 1.000 59.81243  ? 85  GLY A CA   1 
ATOM   1343 C C    . GLY A 1 85  ? -1.46600  31.02600 -24.26000 1.000 75.03531  ? 85  GLY A C    1 
ATOM   1344 O O    . GLY A 1 85  ? -0.64800  30.29300 -24.82900 1.000 77.58562  ? 85  GLY A O    1 
ATOM   1345 H H    . GLY A 1 85  ? -2.03200  32.95400 -22.21000 1.000 69.03000  ? 85  GLY A H    1 
ATOM   1346 H HA2  . GLY A 1 85  ? -1.73600  33.04900 -24.36200 1.000 68.64000  ? 85  GLY A HA2  1 
ATOM   1347 H HA3  . GLY A 1 85  ? -0.22100  32.64800 -24.15700 1.000 68.64000  ? 85  GLY A HA3  1 
ATOM   1348 N N    . CYS A 1 86  ? -2.68200  30.62500 -23.88400 1.000 61.18628  ? 86  CYS A N    1 
ATOM   1349 C CA   . CYS A 1 86  ? -3.23100  29.33300 -24.25700 1.000 62.12324  ? 86  CYS A CA   1 
ATOM   1350 C C    . CYS A 1 86  ? -4.72600  29.47200 -24.49100 1.000 85.44446  ? 86  CYS A C    1 
ATOM   1351 O O    . CYS A 1 86  ? -5.37000  28.48300 -24.88100 1.000 97.94859  ? 86  CYS A O    1 
ATOM   1352 C CB   . CYS A 1 86  ? -2.92100  28.27000 -23.17900 1.000 64.83935  ? 86  CYS A CB   1 
ATOM   1353 S SG   . CYS A 1 86  ? -1.09800  28.02300 -22.88800 1.000 72.36657  ? 86  CYS A SG   1 
ATOM   1354 H H    . CYS A 1 86  ? -3.20300  31.09500 -23.38900 1.000 70.29000  ? 86  CYS A H    1 
ATOM   1355 H HA   . CYS A 1 86  ? -2.82300  29.04400 -25.08800 1.000 73.31000  ? 86  CYS A HA   1 
ATOM   1356 H HB2  . CYS A 1 86  ? -3.32200  28.54700 -22.34000 1.000 78.44000  ? 86  CYS A HB2  1 
ATOM   1357 H HB3  . CYS A 1 86  ? -3.29600  27.42000 -23.45900 1.000 78.44000  ? 86  CYS A HB3  1 
ATOM   1358 N N    . GLY A 1 87  ? -5.29800  30.68000 -24.28500 1.000 62.52592  ? 87  GLY A N    1 
ATOM   1359 C CA   . GLY A 1 87  ? -6.68100  30.92300 -24.72100 1.000 83.70740  ? 87  GLY A CA   1 
ATOM   1360 C C    . GLY A 1 87  ? -7.70100  30.33600 -23.75500 1.000 81.43082  ? 87  GLY A C    1 
ATOM   1361 O O    . GLY A 1 87  ? -7.60200  30.53800 -22.55400 1.000 66.41586  ? 87  GLY A O    1 
ATOM   1362 H H    . GLY A 1 87  ? -4.92200  31.35300 -23.90600 1.000 71.90000  ? 87  GLY A H    1 
ATOM   1363 H HA2  . GLY A 1 87  ? -6.83600  31.87800 -24.79200 1.000 101.08000 ? 87  GLY A HA2  1 
ATOM   1364 H HA3  . GLY A 1 87  ? -6.82000  30.52200 -25.59300 1.000 101.08000 ? 87  GLY A HA3  1 
ATOM   1365 N N    . MET A 1 88  ? -8.70700  29.62400 -24.27500 1.000 108.39984 ? 88  MET A N    1 
ATOM   1366 C CA   . MET A 1 88  ? -9.72200  29.00900 -23.41600 1.000 116.35606 ? 88  MET A CA   1 
ATOM   1367 C C    . MET A 1 88  ? -10.13000 27.63900 -23.93900 1.000 118.42999 ? 88  MET A C    1 
ATOM   1368 O O    . MET A 1 88  ? -9.28000  26.77100 -24.15600 1.000 120.75658 ? 88  MET A O    1 
ATOM   1369 C CB   . MET A 1 88  ? -10.98500 29.88300 -23.28200 1.000 110.94488 ? 88  MET A CB   1 
ATOM   1370 C CG   . MET A 1 88  ? -10.80900 31.39200 -23.03600 1.000 106.11535 ? 88  MET A CG   1 
ATOM   1371 S SD   . MET A 1 88  ? -10.09400 31.92200 -21.45600 1.000 91.61362  ? 88  MET A SD   1 
ATOM   1372 C CE   . MET A 1 88  ? -10.57200 33.65700 -21.36600 1.000 91.80311  ? 88  MET A CE   1 
ATOM   1373 H H    . MET A 1 88  ? -8.82300  29.48400 -25.11600 1.000 108.40000 ? 88  MET A H    1 
ATOM   1374 H HA   . MET A 1 88  ? -9.35000  28.89800 -22.52700 1.000 116.36000 ? 88  MET A HA   1 
ATOM   1375 H HB2  . MET A 1 88  ? -11.47300 29.84000 -24.11800 1.000 110.94000 ? 88  MET A HB2  1 
ATOM   1376 H HB3  . MET A 1 88  ? -11.53300 29.53000 -22.56300 1.000 110.94000 ? 88  MET A HB3  1 
ATOM   1377 H HG2  . MET A 1 88  ? -10.23700 31.74300 -23.73600 1.000 106.12000 ? 88  MET A HG2  1 
ATOM   1378 H HG3  . MET A 1 88  ? -11.68300 31.80800 -23.10300 1.000 106.12000 ? 88  MET A HG3  1 
ATOM   1379 H HE1  . MET A 1 88  ? -10.23000 34.03600 -20.54100 1.000 91.80000  ? 88  MET A HE1  1 
ATOM   1380 H HE2  . MET A 1 88  ? -10.19700 34.12700 -22.12700 1.000 91.80000  ? 88  MET A HE2  1 
ATOM   1381 H HE3  . MET A 1 88  ? -11.54000 33.71900 -21.38200 1.000 91.80000  ? 88  MET A HE3  1 
ATOM   1382 N N    . GLY A 1 89  ? -11.43000 27.45800 -24.16400 1.000 113.59783 ? 89  GLY A N    1 
ATOM   1383 C CA   . GLY A 1 89  ? -12.00300 26.18800 -24.54000 1.000 108.26298 ? 89  GLY A CA   1 
ATOM   1384 C C    . GLY A 1 89  ? -12.16400 25.32600 -23.31000 1.000 114.16369 ? 89  GLY A C    1 
ATOM   1385 O O    . GLY A 1 89  ? -11.87800 25.76500 -22.19400 1.000 127.51003 ? 89  GLY A O    1 
ATOM   1386 H H    . GLY A 1 89  ? -12.03500 28.06000 -24.10700 1.000 113.60000 ? 89  GLY A H    1 
ATOM   1387 H HA2  . GLY A 1 89  ? -12.87200 26.32300 -24.94900 1.000 108.26000 ? 89  GLY A HA2  1 
ATOM   1388 H HA3  . GLY A 1 89  ? -11.42300 25.73500 -25.17100 1.000 108.26000 ? 89  GLY A HA3  1 
ATOM   1389 N N    . PRO A 1 90  ? -12.63400 24.08900 -23.47300 1.000 146.79918 ? 90  PRO A N    1 
ATOM   1390 C CA   . PRO A 1 90  ? -12.67500 23.14800 -22.34200 1.000 146.81760 ? 90  PRO A CA   1 
ATOM   1391 C C    . PRO A 1 90  ? -11.42500 22.28900 -22.19200 1.000 137.74020 ? 90  PRO A C    1 
ATOM   1392 O O    . PRO A 1 90  ? -11.39700 21.42200 -21.30700 1.000 124.94656 ? 90  PRO A O    1 
ATOM   1393 C CB   . PRO A 1 90  ? -13.89700 22.28400 -22.67600 1.000 126.39937 ? 90  PRO A CB   1 
ATOM   1394 C CG   . PRO A 1 90  ? -13.87600 22.21600 -24.19000 1.000 136.63744 ? 90  PRO A CG   1 
ATOM   1395 C CD   . PRO A 1 90  ? -13.23400 23.51600 -24.69100 1.000 130.82095 ? 90  PRO A CD   1 
ATOM   1396 H HA   . PRO A 1 90  ? -12.83800 23.62400 -21.51300 1.000 176.81000 ? 90  PRO A HA   1 
ATOM   1397 H HB2  . PRO A 1 90  ? -13.79000 21.40300 -22.28400 1.000 152.31000 ? 90  PRO A HB2  1 
ATOM   1398 H HB3  . PRO A 1 90  ? -14.70600 22.71400 -22.35700 1.000 152.31000 ? 90  PRO A HB3  1 
ATOM   1399 H HG2  . PRO A 1 90  ? -13.35000 21.45000 -24.47000 1.000 164.59000 ? 90  PRO A HG2  1 
ATOM   1400 H HG3  . PRO A 1 90  ? -14.78500 22.14100 -24.52100 1.000 164.59000 ? 90  PRO A HG3  1 
ATOM   1401 H HD2  . PRO A 1 90  ? -12.54700 23.32300 -25.34800 1.000 157.61000 ? 90  PRO A HD2  1 
ATOM   1402 H HD3  . PRO A 1 90  ? -13.91100 24.11200 -25.04800 1.000 157.61000 ? 90  PRO A HD3  1 
ATOM   1403 N N    . ALA A 1 91  ? -10.40100 22.51600 -23.03200 1.000 112.32399 ? 91  ALA A N    1 
ATOM   1404 C CA   . ALA A 1 91  ? -9.09400  21.89100 -22.82200 1.000 112.68720 ? 91  ALA A CA   1 
ATOM   1405 C C    . ALA A 1 91  ? -8.37800  22.51300 -21.62700 1.000 114.75586 ? 91  ALA A C    1 
ATOM   1406 O O    . ALA A 1 91  ? -7.76900  21.79700 -20.81900 1.000 124.34649 ? 91  ALA A O    1 
ATOM   1407 C CB   . ALA A 1 91  ? -8.23200  22.01600 -24.08400 1.000 93.80335  ? 91  ALA A CB   1 
ATOM   1408 H H    . ALA A 1 91  ? -10.44100 23.02400 -23.72400 1.000 135.41000 ? 91  ALA A H    1 
ATOM   1409 H HA   . ALA A 1 91  ? -9.22100  20.94700 -22.63800 1.000 135.85000 ? 91  ALA A HA   1 
ATOM   1410 H HB1  . ALA A 1 91  ? -7.37300  21.59600 -23.92200 1.000 113.19000 ? 91  ALA A HB1  1 
ATOM   1411 H HB2  . ALA A 1 91  ? -8.68400  21.57300 -24.81900 1.000 113.19000 ? 91  ALA A HB2  1 
ATOM   1412 H HB3  . ALA A 1 91  ? -8.10800  22.95600 -24.28900 1.000 113.19000 ? 91  ALA A HB3  1 
ATOM   1413 N N    . SER A 1 92  ? -8.47100  23.84800 -21.48600 1.000 118.94584 ? 92  SER A N    1 
ATOM   1414 C CA   . SER A 1 92  ? -7.93100  24.62600 -20.36500 1.000 108.45248 ? 92  SER A CA   1 
ATOM   1415 C C    . SER A 1 92  ? -8.69800  24.42900 -19.05500 1.000 101.03317 ? 92  SER A C    1 
ATOM   1416 O O    . SER A 1 92  ? -8.35300  25.04700 -18.04000 1.000 66.66852  ? 92  SER A O    1 
ATOM   1417 C CB   . SER A 1 92  ? -7.93700  26.12800 -20.72100 1.000 106.74438 ? 92  SER A CB   1 
ATOM   1418 O OG   . SER A 1 92  ? -9.25600  26.66900 -20.86800 1.000 86.38931  ? 92  SER A OG   1 
ATOM   1419 H H    . SER A 1 92  ? -8.86700  24.34600 -22.06500 1.000 143.36000 ? 92  SER A H    1 
ATOM   1420 H HA   . SER A 1 92  ? -7.01100  24.35900 -20.21400 1.000 130.77000 ? 92  SER A HA   1 
ATOM   1421 H HB2  . SER A 1 92  ? -7.48200  26.61400 -20.01500 1.000 128.72000 ? 92  SER A HB2  1 
ATOM   1422 H HB3  . SER A 1 92  ? -7.46000  26.24800 -21.55700 1.000 128.72000 ? 92  SER A HB3  1 
ATOM   1423 H HG   . SER A 1 92  ? -9.63700  26.70200 -20.12100 1.000 104.29000 ? 92  SER A HG   1 
ATOM   1424 N N    . MET A 1 93  ? -9.72200  23.58600 -19.04800 1.000 98.78290  ? 93  MET A N    1 
ATOM   1425 C CA   . MET A 1 93  ? -10.66500 23.50600 -17.94800 1.000 79.80957  ? 93  MET A CA   1 
ATOM   1426 C C    . MET A 1 93  ? -10.80500 22.05300 -17.52400 1.000 77.03292  ? 93  MET A C    1 
ATOM   1427 O O    . MET A 1 93  ? -11.09700 21.17900 -18.34900 1.000 91.28726  ? 93  MET A O    1 
ATOM   1428 C CB   . MET A 1 93  ? -12.01300 24.12400 -18.37000 1.000 99.29612  ? 93  MET A CB   1 
ATOM   1429 C CG   . MET A 1 93  ? -11.93400 25.64700 -18.70200 1.000 109.64999 ? 93  MET A CG   1 
ATOM   1430 S SD   . MET A 1 93  ? -12.61000 26.79600 -17.46600 1.000 89.31597  ? 93  MET A SD   1 
ATOM   1431 C CE   . MET A 1 93  ? -14.38800 26.53300 -17.69900 1.000 84.12324  ? 93  MET A CE   1 
ATOM   1432 H H    . MET A 1 93  ? -9.89600  23.03700 -19.68600 1.000 119.17000 ? 93  MET A H    1 
ATOM   1433 H HA   . MET A 1 93  ? -10.32600 24.01900 -17.19800 1.000 96.40000  ? 93  MET A HA   1 
ATOM   1434 H HB2  . MET A 1 93  ? -12.33300 23.66400 -19.16200 1.000 119.79000 ? 93  MET A HB2  1 
ATOM   1435 H HB3  . MET A 1 93  ? -12.64800 24.01100 -17.64600 1.000 119.79000 ? 93  MET A HB3  1 
ATOM   1436 H HG2  . MET A 1 93  ? -11.00200 25.88100 -18.82500 1.000 132.21000 ? 93  MET A HG2  1 
ATOM   1437 H HG3  . MET A 1 93  ? -12.41500 25.80100 -19.53000 1.000 132.21000 ? 93  MET A HG3  1 
ATOM   1438 H HE1  . MET A 1 93  ? -14.86600 26.92100 -16.94900 1.000 101.57000 ? 93  MET A HE1  1 
ATOM   1439 H HE2  . MET A 1 93  ? -14.66500 26.95900 -18.52500 1.000 101.57000 ? 93  MET A HE2  1 
ATOM   1440 H HE3  . MET A 1 93  ? -14.55800 25.58000 -17.74400 1.000 101.57000 ? 93  MET A HE3  1 
ATOM   1441 N N    . THR A 1 94  ? -10.58200 21.81100 -16.22600 1.000 73.12193  ? 94  THR A N    1 
ATOM   1442 C CA   . THR A 1 94  ? -10.78400 20.48100 -15.66100 1.000 74.38260  ? 94  THR A CA   1 
ATOM   1443 C C    . THR A 1 94  ? -12.20800 19.98100 -15.86100 1.000 70.99272  ? 94  THR A C    1 
ATOM   1444 O O    . THR A 1 94  ? -12.42900 18.77300 -16.01600 1.000 80.67020  ? 94  THR A O    1 
ATOM   1445 C CB   . THR A 1 94  ? -10.48100 20.46800 -14.16200 1.000 71.95863  ? 94  THR A CB   1 
ATOM   1446 O OG1  . THR A 1 94  ? -9.13800  20.87900 -13.93200 1.000 75.29587  ? 94  THR A OG1  1 
ATOM   1447 C CG2  . THR A 1 94  ? -10.69300 19.06200 -13.62500 1.000 73.46407  ? 94  THR A CG2  1 
ATOM   1448 H H    . THR A 1 94  ? -10.31500 22.39900 -15.65900 1.000 88.37000  ? 94  THR A H    1 
ATOM   1449 H HA   . THR A 1 94  ? -10.18200 19.85700 -16.09600 1.000 89.89000  ? 94  THR A HA   1 
ATOM   1450 H HB   . THR A 1 94  ? -11.08800 21.06900 -13.70300 1.000 83.22000  ? 94  THR A HB   1 
ATOM   1451 H HG1  . THR A 1 94  ? -8.97200  20.87200 -13.10900 1.000 90.98000  ? 94  THR A HG1  1 
ATOM   1452 H HG21 . THR A 1 94  ? -10.21700 18.95500 -12.78700 1.000 85.97000  ? 94  THR A HG21 1 
ATOM   1453 H HG22 . THR A 1 94  ? -11.63700 18.90000 -13.47100 1.000 85.97000  ? 94  THR A HG22 1 
ATOM   1454 H HG23 . THR A 1 94  ? -10.35800 18.41000 -14.26100 1.000 85.97000  ? 94  THR A HG23 1 
ATOM   1455 N N    . LEU A 1 95  ? -13.19100 20.87400 -15.77000 1.000 70.59004  ? 95  LEU A N    1 
ATOM   1456 C CA   . LEU A 1 95  ? -14.59800 20.54300 -15.99000 1.000 80.88338  ? 95  LEU A CA   1 
ATOM   1457 C C    . LEU A 1 95  ? -14.99800 20.98500 -17.40300 1.000 70.54267  ? 95  LEU A C    1 
ATOM   1458 O O    . LEU A 1 95  ? -14.81700 22.15600 -17.76500 1.000 76.05386  ? 95  LEU A O    1 
ATOM   1459 C CB   . LEU A 1 95  ? -15.46900 21.22300 -14.93000 1.000 76.06175  ? 95  LEU A CB   1 
ATOM   1460 C CG   . LEU A 1 95  ? -15.76000 20.61500 -13.55600 1.000 72.60081  ? 95  LEU A CG   1 
ATOM   1461 C CD1  . LEU A 1 95  ? -14.58900 20.21400 -12.73800 1.000 73.17719  ? 95  LEU A CD1  1 
ATOM   1462 C CD2  . LEU A 1 95  ? -16.53500 21.67300 -12.75300 1.000 73.37196  ? 95  LEU A CD2  1 
ATOM   1463 H H    . LEU A 1 95  ? -13.06400 21.70200 -15.57600 1.000 81.57000  ? 95  LEU A H    1 
ATOM   1464 H HA   . LEU A 1 95  ? -14.72300 19.58400 -15.92100 1.000 97.69000  ? 95  LEU A HA   1 
ATOM   1465 H HB2  . LEU A 1 95  ? -15.06600 22.08700 -14.75300 1.000 91.90000  ? 95  LEU A HB2  1 
ATOM   1466 H HB3  . LEU A 1 95  ? -16.33600 21.37300 -15.33800 1.000 91.90000  ? 95  LEU A HB3  1 
ATOM   1467 H HG   . LEU A 1 95  ? -16.33200 19.84000 -13.66500 1.000 83.99000  ? 95  LEU A HG   1 
ATOM   1468 H HD11 . LEU A 1 95  ? -13.96600 20.95600 -12.69500 1.000 85.85000  ? 95  LEU A HD11 1 
ATOM   1469 H HD12 . LEU A 1 95  ? -14.89400 19.98600 -11.84600 1.000 85.85000  ? 95  LEU A HD12 1 
ATOM   1470 H HD13 . LEU A 1 95  ? -14.16300 19.44700 -13.15100 1.000 85.85000  ? 95  LEU A HD13 1 
ATOM   1471 H HD21 . LEU A 1 95  ? -17.33000 21.92500 -13.24900 1.000 84.91000  ? 95  LEU A HD21 1 
ATOM   1472 H HD22 . LEU A 1 95  ? -16.78600 21.29700 -11.89500 1.000 84.91000  ? 95  LEU A HD22 1 
ATOM   1473 H HD23 . LEU A 1 95  ? -15.96700 22.44800 -12.62200 1.000 84.91000  ? 95  LEU A HD23 1 
ATOM   1474 N N    . ASP A 1 96  ? -15.51400 20.05500 -18.20600 1.000 71.14537  ? 96  ASP A N    1 
ATOM   1475 C CA   . ASP A 1 96  ? -15.87800 20.39000 -19.57400 1.000 71.39014  ? 96  ASP A CA   1 
ATOM   1476 C C    . ASP A 1 96  ? -17.28800 20.97000 -19.61700 1.000 72.05601  ? 96  ASP A C    1 
ATOM   1477 O O    . ASP A 1 96  ? -17.92400 21.20600 -18.59000 1.000 72.19023  ? 96  ASP A O    1 
ATOM   1478 C CB   . ASP A 1 96  ? -15.77000 19.17700 -20.49400 1.000 72.39289  ? 96  ASP A CB   1 
ATOM   1479 C CG   . ASP A 1 96  ? -16.37400 17.93100 -19.89700 1.000 73.25878  ? 96  ASP A CG   1 
ATOM   1480 O OD1  . ASP A 1 96  ? -17.35900 18.01400 -19.11700 1.000 73.29826  ? 96  ASP A OD1  1 
ATOM   1481 O OD2  . ASP A 1 96  ? -15.81900 16.85300 -20.19800 1.000 82.20722  ? 96  ASP A OD2  1 
ATOM   1482 H H    . ASP A 1 96  ? -15.65900 19.23900 -17.97900 1.000 82.24000  ? 96  ASP A H    1 
ATOM   1483 H HA   . ASP A 1 96  ? -15.26800 21.06700 -19.90500 1.000 82.53000  ? 96  ASP A HA   1 
ATOM   1484 H HB2  . ASP A 1 96  ? -16.26200 19.35500 -21.30500 1.000 83.74000  ? 96  ASP A HB2  1 
ATOM   1485 H HB3  . ASP A 1 96  ? -14.83700 19.00300 -20.69300 1.000 83.74000  ? 96  ASP A HB3  1 
ATOM   1486 N N    . VAL A 1 97  ? -17.78800 21.29100 -20.79900 1.000 52.36681  ? 97  VAL A N    1 
ATOM   1487 C CA   . VAL A 1 97  ? -19.11000 21.96000 -20.88800 1.000 60.05720  ? 97  VAL A CA   1 
ATOM   1488 C C    . VAL A 1 97  ? -20.17300 21.06500 -20.23800 1.000 52.96161  ? 97  VAL A C    1 
ATOM   1489 O O    . VAL A 1 97  ? -21.14900 21.61800 -19.71500 1.000 52.83265  ? 97  VAL A O    1 
ATOM   1490 C CB   . VAL A 1 97  ? -19.40800 22.25900 -22.36300 1.000 64.98674  ? 97  VAL A CB   1 
ATOM   1491 C CG1  . VAL A 1 97  ? -20.88400 22.51900 -22.62100 1.000 74.78002  ? 97  VAL A CG1  1 
ATOM   1492 C CG2  . VAL A 1 97  ? -18.56900 23.42600 -22.85700 1.000 74.80371  ? 97  VAL A CG2  1 
ATOM   1493 H H    . VAL A 1 97  ? -17.40600 21.14400 -21.55500 1.000 63.47000  ? 97  VAL A H    1 
ATOM   1494 H HA   . VAL A 1 97  ? -19.08000 22.80100 -20.40500 1.000 72.69000  ? 97  VAL A HA   1 
ATOM   1495 H HB   . VAL A 1 97  ? -19.15700 21.48200 -22.88700 1.000 78.61000  ? 97  VAL A HB   1 
ATOM   1496 H HG11 . VAL A 1 97  ? -21.36600 21.67800 -22.58800 1.000 90.36000  ? 97  VAL A HG11 1 
ATOM   1497 H HG12 . VAL A 1 97  ? -20.98300 22.92100 -23.49800 1.000 90.36000  ? 97  VAL A HG12 1 
ATOM   1498 H HG13 . VAL A 1 97  ? -21.22100 23.12300 -21.94100 1.000 90.36000  ? 97  VAL A HG13 1 
ATOM   1499 H HG21 . VAL A 1 97  ? -18.79100 24.21600 -22.33900 1.000 90.39000  ? 97  VAL A HG21 1 
ATOM   1500 H HG22 . VAL A 1 97  ? -18.76300 23.57900 -23.79500 1.000 90.39000  ? 97  VAL A HG22 1 
ATOM   1501 H HG23 . VAL A 1 97  ? -17.63000 23.20900 -22.74400 1.000 90.39000  ? 97  VAL A HG23 1 
ATOM   1502 N N    . GLN A 1 98  ? -19.97700 19.74700 -20.24900 1.000 56.60942  ? 98  GLN A N    1 
ATOM   1503 C CA   . GLN A 1 98  ? -20.97900 18.78400 -19.73300 1.000 45.94235  ? 98  GLN A CA   1 
ATOM   1504 C C    . GLN A 1 98  ? -20.88700 18.72700 -18.20800 1.000 50.14549  ? 98  GLN A C    1 
ATOM   1505 O O    . GLN A 1 98  ? -21.93200 18.64500 -17.57300 1.000 48.76374  ? 98  GLN A O    1 
ATOM   1506 C CB   . GLN A 1 98  ? -20.71200 17.39800 -20.30600 1.000 42.81303  ? 98  GLN A CB   1 
ATOM   1507 C CG   . GLN A 1 98  ? -20.53100 17.37000 -21.81800 1.000 68.39504  ? 98  GLN A CG   1 
ATOM   1508 C CD   . GLN A 1 98  ? -19.08500 17.22500 -22.23200 1.000 75.77224  ? 98  GLN A CD   1 
ATOM   1509 O OE1  . GLN A 1 98  ? -18.48800 16.15000 -22.11400 1.000 68.45031  ? 98  GLN A OE1  1 
ATOM   1510 N NE2  . GLN A 1 98  ? -18.50500 18.31500 -22.71100 1.000 71.52173  ? 98  GLN A NE2  1 
ATOM   1511 H H    . GLN A 1 98  ? -19.26600 19.37100 -20.55200 1.000 68.56000  ? 98  GLN A H    1 
ATOM   1512 H HA   . GLN A 1 98  ? -21.87200 19.06500 -19.98600 1.000 55.76000  ? 98  GLN A HA   1 
ATOM   1513 H HB2  . GLN A 1 98  ? -19.90100 17.04700 -19.90500 1.000 52.00000  ? 98  GLN A HB2  1 
ATOM   1514 H HB3  . GLN A 1 98  ? -21.46100 16.82200 -20.08800 1.000 52.00000  ? 98  GLN A HB3  1 
ATOM   1515 H HG2  . GLN A 1 98  ? -21.02300 16.61700 -22.18100 1.000 82.71000  ? 98  GLN A HG2  1 
ATOM   1516 H HG3  . GLN A 1 98  ? -20.86900 18.19800 -22.19300 1.000 82.71000  ? 98  GLN A HG3  1 
ATOM   1517 H HE21 . GLN A 1 98  ? -18.95200 19.04700 -22.77700 1.000 86.45000  ? 98  GLN A HE21 1 
ATOM   1518 H HE22 . GLN A 1 98  ? -17.68300 18.29000 -22.96100 1.000 86.45000  ? 98  GLN A HE22 1 
ATOM   1519 N N    . ALA A 1 99  ? -19.67800 18.72000 -17.65800 1.000 65.60260  ? 99  ALA A N    1 
ATOM   1520 C CA   . ALA A 1 99  ? -19.44800 18.68700 -16.20200 1.000 40.38116  ? 99  ALA A CA   1 
ATOM   1521 C C    . ALA A 1 99  ? -19.85900 20.03900 -15.64500 1.000 51.37195  ? 99  ALA A C    1 
ATOM   1522 O O    . ALA A 1 99  ? -20.29200 20.07900 -14.49200 1.000 65.58155  ? 99  ALA A O    1 
ATOM   1523 C CB   . ALA A 1 99  ? -18.00900 18.38200 -15.91800 1.000 55.24347  ? 99  ALA A CB   1 
ATOM   1524 H H    . ALA A 1 99  ? -18.95000 18.73400 -18.11500 1.000 79.35000  ? 99  ALA A H    1 
ATOM   1525 H HA   . ALA A 1 99  ? -20.00000 18.00000 -15.79700 1.000 49.09000  ? 99  ALA A HA   1 
ATOM   1526 H HB1  . ALA A 1 99  ? -17.78800 17.51800 -16.30000 1.000 66.92000  ? 99  ALA A HB1  1 
ATOM   1527 H HB2  . ALA A 1 99  ? -17.45600 19.07200 -16.31700 1.000 66.92000  ? 99  ALA A HB2  1 
ATOM   1528 H HB3  . ALA A 1 99  ? -17.87400 18.36400 -14.95800 1.000 66.92000  ? 99  ALA A HB3  1 
ATOM   1529 N N    . ARG A 1 100 ? -19.71600 21.10600 -16.42900 1.000 55.68826  ? 100 ARG A N    1 
ATOM   1530 C CA   . ARG A 1 100 ? -20.17300 22.43100 -15.98700 1.000 49.25591  ? 100 ARG A CA   1 
ATOM   1531 C C    . ARG A 1 100 ? -21.70300 22.50900 -15.95700 1.000 44.88433  ? 100 ARG A C    1 
ATOM   1532 O O    . ARG A 1 100 ? -22.27700 23.25700 -15.15000 1.000 46.54769  ? 100 ARG A O    1 
ATOM   1533 C CB   . ARG A 1 100 ? -19.59600 23.53000 -16.88700 1.000 69.18461  ? 100 ARG A CB   1 
ATOM   1534 C CG   . ARG A 1 100 ? -18.35400 24.27400 -16.33200 1.000 85.08652  ? 100 ARG A CG   1 
ATOM   1535 C CD   . ARG A 1 100 ? -17.16200 24.31100 -17.34300 1.000 94.26130  ? 100 ARG A CD   1 
ATOM   1536 N NE   . ARG A 1 100 ? -17.43700 25.02000 -18.59400 1.000 78.96999  ? 100 ARG A NE   1 
ATOM   1537 C CZ   . ARG A 1 100 ? -16.68900 24.93500 -19.69100 1.000 87.41311  ? 100 ARG A CZ   1 
ATOM   1538 N NH1  . ARG A 1 100 ? -15.61100 24.16600 -19.74200 1.000 98.14861  ? 100 ARG A NH1  1 
ATOM   1539 N NH2  . ARG A 1 100 ? -17.03200 25.64000 -20.76600 1.000 97.67750  ? 100 ARG A NH2  1 
ATOM   1540 H H    . ARG A 1 100 ? -19.36200 21.09500 -17.21200 1.000 67.45000  ? 100 ARG A H    1 
ATOM   1541 H HA   . ARG A 1 100 ? -19.85300 22.58600 -15.08400 1.000 59.73000  ? 100 ARG A HA   1 
ATOM   1542 H HB2  . ARG A 1 100 ? -19.34100 23.13200 -17.73400 1.000 83.65000  ? 100 ARG A HB2  1 
ATOM   1543 H HB3  . ARG A 1 100 ? -20.28700 24.19400 -17.03900 1.000 83.65000  ? 100 ARG A HB3  1 
ATOM   1544 H HG2  . ARG A 1 100 ? -18.60100 25.19000 -16.12700 1.000 102.73000 ? 100 ARG A HG2  1 
ATOM   1545 H HG3  . ARG A 1 100 ? -18.04800 23.82600 -15.52800 1.000 102.73000 ? 100 ARG A HG3  1 
ATOM   1546 H HD2  . ARG A 1 100 ? -16.41100 24.74800 -16.91400 1.000 113.74000 ? 100 ARG A HD2  1 
ATOM   1547 H HD3  . ARG A 1 100 ? -16.92300 23.39900 -17.57000 1.000 113.74000 ? 100 ARG A HD3  1 
ATOM   1548 H HE   . ARG A 1 100 ? -18.13100 25.52700 -18.62200 1.000 95.39000  ? 100 ARG A HE   1 
ATOM   1549 H HH11 . ARG A 1 100 ? -15.37600 23.70500 -19.05500 1.000 118.41000 ? 100 ARG A HH11 1 
ATOM   1550 H HH12 . ARG A 1 100 ? -15.14500 24.12800 -20.46400 1.000 118.41000 ? 100 ARG A HH12 1 
ATOM   1551 H HH21 . ARG A 1 100 ? -17.73000 26.14200 -20.74600 1.000 117.84000 ? 100 ARG A HH21 1 
ATOM   1552 H HH22 . ARG A 1 100 ? -16.55700 25.59200 -21.48100 1.000 117.84000 ? 100 ARG A HH22 1 
ATOM   1553 N N    . GLN A 1 101 ? -22.37600 21.71900 -16.79800 1.000 49.32960  ? 101 GLN A N    1 
ATOM   1554 C CA   . GLN A 1 101 ? -23.83900 21.75000 -16.82300 1.000 50.19023  ? 101 GLN A CA   1 
ATOM   1555 C C    . GLN A 1 101 ? -24.42600 21.03500 -15.61500 1.000 47.25040  ? 101 GLN A C    1 
ATOM   1556 O O    . GLN A 1 101 ? -25.38100 21.50700 -14.98600 1.000 42.99989  ? 101 GLN A O    1 
ATOM   1557 C CB   . GLN A 1 101 ? -24.35200 21.11700 -18.12100 1.000 59.72558  ? 101 GLN A CB   1 
ATOM   1558 C CG   . GLN A 1 101 ? -25.86000 20.93600 -18.09600 1.000 50.14285  ? 101 GLN A CG   1 
ATOM   1559 C CD   . GLN A 1 101 ? -26.47800 20.96000 -19.44700 1.000 42.67354  ? 101 GLN A CD   1 
ATOM   1560 O OE1  . GLN A 1 101 ? -25.99200 21.62500 -20.36600 1.000 54.85658  ? 101 GLN A OE1  1 
ATOM   1561 N NE2  . GLN A 1 101 ? -27.56100 20.23100 -19.58900 1.000 53.12742  ? 101 GLN A NE2  1 
ATOM   1562 H H    . GLN A 1 101 ? -22.01800 21.16800 -17.35300 1.000 59.83000  ? 101 GLN A H    1 
ATOM   1563 H HA   . GLN A 1 101 ? -24.13700 22.67300 -16.80000 1.000 60.85000  ? 101 GLN A HA   1 
ATOM   1564 H HB2  . GLN A 1 101 ? -24.12400 21.69300 -18.86700 1.000 72.30000  ? 101 GLN A HB2  1 
ATOM   1565 H HB3  . GLN A 1 101 ? -23.94300 20.24500 -18.23400 1.000 72.30000  ? 101 GLN A HB3  1 
ATOM   1566 H HG2  . GLN A 1 101 ? -26.06700 20.08100 -17.68900 1.000 60.80000  ? 101 GLN A HG2  1 
ATOM   1567 H HG3  . GLN A 1 101 ? -26.25500 21.65400 -17.57700 1.000 60.80000  ? 101 GLN A HG3  1 
ATOM   1568 H HE21 . GLN A 1 101 ? -27.86700 19.78200 -18.92300 1.000 64.38000  ? 101 GLN A HE21 1 
ATOM   1569 H HE22 . GLN A 1 101 ? -27.96500 20.20400 -20.34800 1.000 64.38000  ? 101 GLN A HE22 1 
ATOM   1570 N N    . LEU A 1 102 ? -23.90000 19.86400 -15.29500 1.000 46.22133  ? 102 LEU A N    1 
ATOM   1571 C CA   . LEU A 1 102 ? -24.23600 19.27000 -14.01100 1.000 35.15421  ? 102 LEU A CA   1 
ATOM   1572 C C    . LEU A 1 102 ? -24.09700 20.28200 -12.87400 1.000 34.22779  ? 102 LEU A C    1 
ATOM   1573 O O    . LEU A 1 102 ? -24.96000 20.38500 -11.98900 1.000 36.93074  ? 102 LEU A O    1 
ATOM   1574 C CB   . LEU A 1 102 ? -23.33100 18.06800 -13.75900 1.000 38.02561  ? 102 LEU A CB   1 
ATOM   1575 C CG   . LEU A 1 102 ? -23.53200 17.26100 -12.47400 1.000 46.69244  ? 102 LEU A CG   1 
ATOM   1576 C CD1  . LEU A 1 102 ? -24.91600 16.63200 -12.45900 1.000 41.67342  ? 102 LEU A CD1  1 
ATOM   1577 C CD2  . LEU A 1 102 ? -22.38900 16.24000 -12.48400 1.000 42.31560  ? 102 LEU A CD2  1 
ATOM   1578 H H    . LEU A 1 102 ? -23.36300 19.40400 -15.78500 1.000 56.09000  ? 102 LEU A H    1 
ATOM   1579 H HA   . LEU A 1 102 ? -25.15500 18.96100 -14.03200 1.000 42.81000  ? 102 LEU A HA   1 
ATOM   1580 H HB2  . LEU A 1 102 ? -23.44500 17.45100 -14.49900 1.000 46.26000  ? 102 LEU A HB2  1 
ATOM   1581 H HB3  . LEU A 1 102 ? -22.41400 18.38500 -13.75200 1.000 46.26000  ? 102 LEU A HB3  1 
ATOM   1582 H HG   . LEU A 1 102 ? -23.43500 17.83800 -11.70000 1.000 56.66000  ? 102 LEU A HG   1 
ATOM   1583 H HD11 . LEU A 1 102 ? -25.58200 17.33500 -12.40500 1.000 50.64000  ? 102 LEU A HD11 1 
ATOM   1584 H HD12 . LEU A 1 102 ? -24.98800 16.04700 -11.68800 1.000 50.64000  ? 102 LEU A HD12 1 
ATOM   1585 H HD13 . LEU A 1 102 ? -25.03900 16.12100 -13.27400 1.000 50.64000  ? 102 LEU A HD13 1 
ATOM   1586 H HD21 . LEU A 1 102 ? -22.47800 15.66100 -11.71100 1.000 51.41000  ? 102 LEU A HD21 1 
ATOM   1587 H HD22 . LEU A 1 102 ? -22.44100 15.71600 -13.29800 1.000 51.41000  ? 102 LEU A HD22 1 
ATOM   1588 H HD23 . LEU A 1 102 ? -21.54300 16.71200 -12.44800 1.000 51.41000  ? 102 LEU A HD23 1 
ATOM   1589 N N    . LEU A 1 103 ? -23.01300 21.05000 -12.87800 1.000 40.79963  ? 103 LEU A N    1 
ATOM   1590 C CA   . LEU A 1 103 ? -22.78000 21.94200 -11.75400 1.000 42.93146  ? 103 LEU A CA   1 
ATOM   1591 C C    . LEU A 1 103 ? -23.84600 23.03600 -11.68800 1.000 40.30483  ? 103 LEU A C    1 
ATOM   1592 O O    . LEU A 1 103 ? -24.20500 23.47300 -10.58900 1.000 37.85454  ? 103 LEU A O    1 
ATOM   1593 C CB   . LEU A 1 103 ? -21.35300 22.49600 -11.84400 1.000 42.20506  ? 103 LEU A CB   1 
ATOM   1594 C CG   . LEU A 1 103 ? -20.79900 23.22200 -10.62900 1.000 41.56025  ? 103 LEU A CG   1 
ATOM   1595 C CD1  . LEU A 1 103 ? -20.79400 22.39900 -9.32500  1.000 47.50570  ? 103 LEU A CD1  1 
ATOM   1596 C CD2  . LEU A 1 103 ? -19.37000 23.73300 -10.89800 1.000 53.66433  ? 103 LEU A CD2  1 
ATOM   1597 H H    . LEU A 1 103 ? -22.41700 21.07400 -13.49700 1.000 49.59000  ? 103 LEU A H    1 
ATOM   1598 H HA   . LEU A 1 103 ? -22.84400 21.42400 -10.93700 1.000 52.14000  ? 103 LEU A HA   1 
ATOM   1599 H HB2  . LEU A 1 103 ? -20.75500 21.75400 -12.02700 1.000 51.27000  ? 103 LEU A HB2  1 
ATOM   1600 H HB3  . LEU A 1 103 ? -21.32100 23.12000 -12.58600 1.000 51.27000  ? 103 LEU A HB3  1 
ATOM   1601 H HG   . LEU A 1 103 ? -21.35300 24.00200 -10.46900 1.000 50.50000  ? 103 LEU A HG   1 
ATOM   1602 H HD11 . LEU A 1 103 ? -20.52800 22.97600 -8.59200  1.000 57.63000  ? 103 LEU A HD11 1 
ATOM   1603 H HD12 . LEU A 1 103 ? -21.68400 22.05100 -9.16300  1.000 57.63000  ? 103 LEU A HD12 1 
ATOM   1604 H HD13 . LEU A 1 103 ? -20.16400 21.67000 -9.41400  1.000 57.63000  ? 103 LEU A HD13 1 
ATOM   1605 H HD21 . LEU A 1 103 ? -19.04500 24.19000 -10.10700 1.000 65.02000  ? 103 LEU A HD21 1 
ATOM   1606 H HD22 . LEU A 1 103 ? -18.79800 22.97700 -11.10200 1.000 65.02000  ? 103 LEU A HD22 1 
ATOM   1607 H HD23 . LEU A 1 103 ? -19.39000 24.34500 -11.65000 1.000 65.02000  ? 103 LEU A HD23 1 
ATOM   1608 N N    . SER A 1 104 ? -24.42900 23.43800 -12.81900 1.000 40.44959  ? 104 SER A N    1 
ATOM   1609 C CA   . SER A 1 104 ? -25.55500 24.37200 -12.74900 1.000 43.04200  ? 104 SER A CA   1 
ATOM   1610 C C    . SER A 1 104 ? -26.74200 23.73700 -12.03900 1.000 44.37637  ? 104 SER A C    1 
ATOM   1611 O O    . SER A 1 104 ? -27.38100 24.37000 -11.19500 1.000 44.49218  ? 104 SER A O    1 
ATOM   1612 C CB   . SER A 1 104 ? -25.98000 24.83400 -14.14400 1.000 42.96305  ? 104 SER A CB   1 
ATOM   1613 O OG   . SER A 1 104 ? -24.91400 25.51900 -14.78100 1.000 64.29192  ? 104 SER A OG   1 
ATOM   1614 H H    . SER A 1 104 ? -24.20200 23.19500 -13.61200 1.000 49.17000  ? 104 SER A H    1 
ATOM   1615 H HA   . SER A 1 104 ? -25.28600 25.15400 -12.24300 1.000 52.28000  ? 104 SER A HA   1 
ATOM   1616 H HB2  . SER A 1 104 ? -26.22200 24.05900 -14.67500 1.000 52.18000  ? 104 SER A HB2  1 
ATOM   1617 H HB3  . SER A 1 104 ? -26.73900 25.43300 -14.06300 1.000 52.18000  ? 104 SER A HB3  1 
ATOM   1618 H HG   . SER A 1 104 ? -25.15100 25.77100 -15.54600 1.000 77.78000  ? 104 SER A HG   1 
ATOM   1619 N N    . GLY A 1 105 ? -27.07100 22.48800 -12.38700 1.000 38.37039  ? 105 GLY A N    1 
ATOM   1620 C CA   . GLY A 1 105 ? -28.16300 21.80400 -11.70100 1.000 39.79951  ? 105 GLY A CA   1 
ATOM   1621 C C    . GLY A 1 105 ? -27.86900 21.51600 -10.24300 1.000 30.52208  ? 105 GLY A C    1 
ATOM   1622 O O    . GLY A 1 105 ? -28.78100 21.51500 -9.40500  1.000 29.66408  ? 105 GLY A O    1 
ATOM   1623 H H    . GLY A 1 105 ? -26.68600 22.02700 -13.00300 1.000 46.67000  ? 105 GLY A H    1 
ATOM   1624 H HA2  . GLY A 1 105 ? -28.96300 22.35100 -11.74800 1.000 48.39000  ? 105 GLY A HA2  1 
ATOM   1625 H HA3  . GLY A 1 105 ? -28.34300 20.96200 -12.14700 1.000 48.39000  ? 105 GLY A HA3  1 
ATOM   1626 N N    . ILE A 1 106 ? -26.59500 21.28400 -9.90900  1.000 34.89103  ? 106 ILE A N    1 
ATOM   1627 C CA   . ILE A 1 106 ? -26.23600 21.08200 -8.52200  1.000 28.54290  ? 106 ILE A CA   1 
ATOM   1628 C C    . ILE A 1 106 ? -26.41900 22.37000 -7.74500  1.000 35.25160  ? 106 ILE A C    1 
ATOM   1629 O O    . ILE A 1 106 ? -26.88900 22.37500 -6.59800  1.000 41.27863  ? 106 ILE A O    1 
ATOM   1630 C CB   . ILE A 1 106 ? -24.78300 20.58900 -8.41100  1.000 29.60355  ? 106 ILE A CB   1 
ATOM   1631 C CG1  . ILE A 1 106 ? -24.69200 19.10600 -8.73500  1.000 36.59649  ? 106 ILE A CG1  1 
ATOM   1632 C CG2  . ILE A 1 106 ? -24.26300 20.86700 -7.03200  1.000 39.71002  ? 106 ILE A CG2  1 
ATOM   1633 C CD1  . ILE A 1 106 ? -23.27800 18.64300 -9.01500  1.000 37.93086  ? 106 ILE A CD1  1 
ATOM   1634 H H    . ILE A 1 106 ? -25.93800 21.24100 -10.46200 1.000 42.50000  ? 106 ILE A H    1 
ATOM   1635 H HA   . ILE A 1 106 ? -26.81700 20.40800 -8.13500  1.000 34.88000  ? 106 ILE A HA   1 
ATOM   1636 H HB   . ILE A 1 106 ? -24.24100 21.07800 -9.05000  1.000 36.15000  ? 106 ILE A HB   1 
ATOM   1637 H HG12 . ILE A 1 106 ? -25.02900 18.59800 -7.98000  1.000 44.54000  ? 106 ILE A HG12 1 
ATOM   1638 H HG13 . ILE A 1 106 ? -25.22800 18.92300 -9.52300  1.000 44.54000  ? 106 ILE A HG13 1 
ATOM   1639 H HG21 . ILE A 1 106 ? -24.01200 21.80200 -6.96300  1.000 48.28000  ? 106 ILE A HG21 1 
ATOM   1640 H HG22 . ILE A 1 106 ? -23.48400 20.31200 -6.87300  1.000 48.28000  ? 106 ILE A HG22 1 
ATOM   1641 H HG23 . ILE A 1 106 ? -24.95000 20.65300 -6.38100  1.000 48.28000  ? 106 ILE A HG23 1 
ATOM   1642 H HD11 . ILE A 1 106 ? -22.87600 19.23700 -9.66800  1.000 46.14000  ? 106 ILE A HD11 1 
ATOM   1643 H HD12 . ILE A 1 106 ? -23.30600 17.73800 -9.36400  1.000 46.14000  ? 106 ILE A HD12 1 
ATOM   1644 H HD13 . ILE A 1 106 ? -22.76700 18.66400 -8.19100  1.000 46.14000  ? 106 ILE A HD13 1 
ATOM   1645 N N    . ASP A 1 107 ? -25.99600 23.47500 -8.34300  1.000 45.26069  ? 107 ASP A N    1 
ATOM   1646 C CA   . ASP A 1 107 ? -26.13700 24.79100 -7.72900  1.000 45.43703  ? 107 ASP A CA   1 
ATOM   1647 C C    . ASP A 1 107 ? -27.60100 25.11500 -7.48500  1.000 36.69387  ? 107 ASP A C    1 
ATOM   1648 O O    . ASP A 1 107 ? -27.99000 25.54900 -6.39200  1.000 47.87679  ? 107 ASP A O    1 
ATOM   1649 C CB   . ASP A 1 107 ? -25.51000 25.80200 -8.67300  1.000 50.11127  ? 107 ASP A CB   1 
ATOM   1650 C CG   . ASP A 1 107 ? -25.07200 27.03500 -8.01300  1.000 38.41513  ? 107 ASP A CG   1 
ATOM   1651 O OD1  . ASP A 1 107 ? -25.20500 27.19200 -6.78200  1.000 53.99068  ? 107 ASP A OD1  1 
ATOM   1652 O OD2  . ASP A 1 107 ? -24.56100 27.86800 -8.76700  1.000 63.96556  ? 107 ASP A OD2  1 
ATOM   1653 H H    . ASP A 1 107 ? -25.61900 23.49000 -9.11600  1.000 54.94000  ? 107 ASP A H    1 
ATOM   1654 H HA   . ASP A 1 107 ? -25.66400 24.81200 -6.88200  1.000 55.15000  ? 107 ASP A HA   1 
ATOM   1655 H HB2  . ASP A 1 107 ? -24.73300 25.40000 -9.09200  1.000 60.76000  ? 107 ASP A HB2  1 
ATOM   1656 H HB3  . ASP A 1 107 ? -26.16100 26.04300 -9.35100  1.000 60.76000  ? 107 ASP A HB3  1 
ATOM   1657 N N    . GLN A 1 108 ? -28.42600 24.89400 -8.50800  1.000 37.11761  ? 108 GLN A N    1 
ATOM   1658 C CA   . GLN A 1 108 ? -29.86600 25.09000 -8.37000  1.000 38.38618  ? 108 GLN A CA   1 
ATOM   1659 C C    . GLN A 1 108 ? -30.44800 24.21700 -7.27400  1.000 38.54936  ? 108 GLN A C    1 
ATOM   1660 O O    . GLN A 1 108 ? -31.29600 24.66300 -6.49400  1.000 38.96257  ? 108 GLN A O    1 
ATOM   1661 C CB   . GLN A 1 108 ? -30.53100 24.75100 -9.71300  1.000 44.37111  ? 108 GLN A CB   1 
ATOM   1662 C CG   . GLN A 1 108 ? -32.05200 24.62100 -9.62200  1.000 53.96436  ? 108 GLN A CG   1 
ATOM   1663 C CD   . GLN A 1 108 ? -32.72100 25.97200 -9.44400  1.000 68.00289  ? 108 GLN A CD   1 
ATOM   1664 O OE1  . GLN A 1 108 ? -32.51100 26.89800 -10.23700 1.000 60.66780  ? 108 GLN A OE1  1 
ATOM   1665 N NE2  . GLN A 1 108 ? -33.51700 26.10300 -8.38200  1.000 85.04967  ? 108 GLN A NE2  1 
ATOM   1666 H H    . GLN A 1 108 ? -28.17700 24.63100 -9.28800  1.000 45.17000  ? 108 GLN A H    1 
ATOM   1667 H HA   . GLN A 1 108 ? -30.05000 26.01800 -8.15800  1.000 46.69000  ? 108 GLN A HA   1 
ATOM   1668 H HB2  . GLN A 1 108 ? -30.33000 25.45500 -10.34900 1.000 53.87000  ? 108 GLN A HB2  1 
ATOM   1669 H HB3  . GLN A 1 108 ? -30.17900 23.90600 -10.03300 1.000 53.87000  ? 108 GLN A HB3  1 
ATOM   1670 H HG2  . GLN A 1 108 ? -32.37600 24.24600 -10.45600 1.000 65.38000  ? 108 GLN A HG2  1 
ATOM   1671 H HG3  . GLN A 1 108 ? -32.31400 24.04600 -8.88900  1.000 65.38000  ? 108 GLN A HG3  1 
ATOM   1672 H HE21 . GLN A 1 108 ? -33.63600 25.43800 -7.84900  1.000 102.69000 ? 108 GLN A HE21 1 
ATOM   1673 H HE22 . GLN A 1 108 ? -33.91800 26.84900 -8.23500  1.000 102.69000 ? 108 GLN A HE22 1 
ATOM   1674 N N    . GLN A 1 109 ? -30.02700 22.96100 -7.20200  1.000 30.83791  ? 109 GLN A N    1 
ATOM   1675 C CA   . GLN A 1 109 ? -30.58600 22.04300 -6.18600  1.000 34.26727  ? 109 GLN A CA   1 
ATOM   1676 C C    . GLN A 1 109 ? -30.14400 22.54300 -4.80900  1.000 33.01185  ? 109 GLN A C    1 
ATOM   1677 O O    . GLN A 1 109 ? -30.87200 22.32100 -3.88500  1.000 37.11761  ? 109 GLN A O    1 
ATOM   1678 C CB   . GLN A 1 109 ? -30.14600 20.59800 -6.38500  1.000 30.27205  ? 109 GLN A CB   1 
ATOM   1679 C CG   . GLN A 1 109 ? -30.64100 19.60100 -5.34000  1.000 30.65104  ? 109 GLN A CG   1 
ATOM   1680 C CD   . GLN A 1 109 ? -32.14500 19.43700 -5.31300  1.000 23.28174  ? 109 GLN A CD   1 
ATOM   1681 O OE1  . GLN A 1 109 ? -32.88700 20.10100 -6.03500  1.000 32.45652  ? 109 GLN A OE1  1 
ATOM   1682 N NE2  . GLN A 1 109 ? -32.61700 18.53000 -4.47700  1.000 32.17491  ? 109 GLN A NE2  1 
ATOM   1683 H H    . GLN A 1 109 ? -29.43100 22.61100 -7.71400  1.000 37.63000  ? 109 GLN A H    1 
ATOM   1684 H HA   . GLN A 1 109 ? -31.55400 22.07700 -6.22500  1.000 41.75000  ? 109 GLN A HA   1 
ATOM   1685 H HB2  . GLN A 1 109 ? -30.46900 20.29700 -7.24900  1.000 36.95000  ? 109 GLN A HB2  1 
ATOM   1686 H HB3  . GLN A 1 109 ? -29.17600 20.57000 -6.37600  1.000 36.95000  ? 109 GLN A HB3  1 
ATOM   1687 H HG2  . GLN A 1 109 ? -30.25400 18.73300 -5.53300  1.000 37.41000  ? 109 GLN A HG2  1 
ATOM   1688 H HG3  . GLN A 1 109 ? -30.35800 19.89600 -4.46000  1.000 37.41000  ? 109 GLN A HG3  1 
ATOM   1689 H HE21 . GLN A 1 109 ? -32.07700 18.07700 -3.98400  1.000 39.24000  ? 109 GLN A HE21 1 
ATOM   1690 H HE22 . GLN A 1 109 ? -33.46500 18.39500 -4.42200  1.000 39.24000  ? 109 GLN A HE22 1 
ATOM   1691 N N    . GLN A 1 110 ? -28.96800 23.14500 -4.69600  1.000 40.21272  ? 110 GLN A N    1 
ATOM   1692 C CA   . GLN A 1 110 ? -28.47300 23.66600 -3.40800  1.000 32.70655  ? 110 GLN A CA   1 
ATOM   1693 C C    . GLN A 1 110 ? -29.45300 24.74700 -2.93600  1.000 28.08758  ? 110 GLN A C    1 
ATOM   1694 O O    . GLN A 1 110 ? -29.75400 24.75200 -1.74400  1.000 33.97249  ? 110 GLN A O    1 
ATOM   1695 C CB   . GLN A 1 110 ? -27.04800 24.18900 -3.55900  1.000 49.58489  ? 110 GLN A CB   1 
ATOM   1696 C CG   . GLN A 1 110 ? -26.45200 24.80200 -2.30000  1.000 45.97393  ? 110 GLN A CG   1 
ATOM   1697 C CD   . GLN A 1 110 ? -26.32300 23.82300 -1.16200  1.000 39.97848  ? 110 GLN A CD   1 
ATOM   1698 O OE1  . GLN A 1 110 ? -26.24300 22.60600 -1.35100  1.000 42.29454  ? 110 GLN A OE1  1 
ATOM   1699 N NE2  . GLN A 1 110 ? -26.28800 24.37300 0.03700   1.000 35.50163  ? 110 GLN A NE2  1 
ATOM   1700 H H    . GLN A 1 110 ? -28.42500 23.27000 -5.35100  1.000 48.88000  ? 110 GLN A H    1 
ATOM   1701 H HA   . GLN A 1 110 ? -28.46800 22.95100 -2.75300  1.000 39.88000  ? 110 GLN A HA   1 
ATOM   1702 H HB2  . GLN A 1 110 ? -26.47600 23.45300 -3.82500  1.000 60.13000  ? 110 GLN A HB2  1 
ATOM   1703 H HB3  . GLN A 1 110 ? -27.04100 24.87200 -4.24700  1.000 60.13000  ? 110 GLN A HB3  1 
ATOM   1704 H HG2  . GLN A 1 110 ? -25.56200 25.12900 -2.49600  1.000 55.80000  ? 110 GLN A HG2  1 
ATOM   1705 H HG3  . GLN A 1 110 ? -27.01500 25.53400 -2.00400  1.000 55.80000  ? 110 GLN A HG3  1 
ATOM   1706 H HE21 . GLN A 1 110 ? -26.34500 25.22700 0.12000   1.000 43.23000  ? 110 GLN A HE21 1 
ATOM   1707 H HE22 . GLN A 1 110 ? -26.21400 23.87700 0.73600   1.000 43.23000  ? 110 GLN A HE22 1 
ATOM   1708 N N    . ASN A 1 111 ? -29.95000 25.60200 -3.82300  1.000 33.65404  ? 111 ASN A N    1 
ATOM   1709 C CA   . ASN A 1 111 ? -30.88400 26.62500 -3.36100  1.000 32.99606  ? 111 ASN A CA   1 
ATOM   1710 C C    . ASN A 1 111 ? -32.24000 25.99500 -3.02500  1.000 33.14082  ? 111 ASN A C    1 
ATOM   1711 O O    . ASN A 1 111 ? -32.79500 26.25500 -1.95900  1.000 38.72833  ? 111 ASN A O    1 
ATOM   1712 C CB   . ASN A 1 111 ? -30.93800 27.72900 -4.42400  1.000 44.35532  ? 111 ASN A CB   1 
ATOM   1713 C CG   . ASN A 1 111 ? -29.52100 28.41400 -4.65900  1.000 47.22935  ? 111 ASN A CG   1 
ATOM   1714 O OD1  . ASN A 1 111 ? -29.12100 28.67200 -5.80200  1.000 44.84222  ? 111 ASN A OD1  1 
ATOM   1715 N ND2  . ASN A 1 111 ? -28.78500 28.68400 -3.57600  1.000 54.68024  ? 111 ASN A ND2  1 
ATOM   1716 H H    . ASN A 1 111 ? -29.77300 25.61500 -4.66400  1.000 41.01000  ? 111 ASN A H    1 
ATOM   1717 H HA   . ASN A 1 111 ? -30.53600 27.01800 -2.54500  1.000 40.22000  ? 111 ASN A HA   1 
ATOM   1718 H HB2  . ASN A 1 111 ? -31.23000 27.34500 -5.26600  1.000 53.86000  ? 111 ASN A HB2  1 
ATOM   1719 H HB3  . ASN A 1 111 ? -31.56000 28.41500 -4.13700  1.000 53.86000  ? 111 ASN A HB3  1 
ATOM   1720 H HD21 . ASN A 1 111 ? -29.08400 28.49400 -2.79300  1.000 66.24000  ? 111 ASN A HD21 1 
ATOM   1721 H HD22 . ASN A 1 111 ? -28.01300 29.05300 -3.66300  1.000 66.24000  ? 111 ASN A HD22 1 
ATOM   1722 N N    . ASN A 1 112 ? -32.73900 25.08000 -3.86000  1.000 40.13902  ? 112 ASN A N    1 
ATOM   1723 C CA   . ASN A 1 112 ? -33.97900 24.37700 -3.51000  1.000 29.98254  ? 112 ASN A CA   1 
ATOM   1724 C C    . ASN A 1 112 ? -33.95200 23.77700 -2.12400  1.000 31.70907  ? 112 ASN A C    1 
ATOM   1725 O O    . ASN A 1 112 ? -34.94700 23.87700 -1.39500  1.000 27.89282  ? 112 ASN A O    1 
ATOM   1726 C CB   . ASN A 1 112 ? -34.25500 23.28300 -4.52900  1.000 27.48224  ? 112 ASN A CB   1 
ATOM   1727 C CG   . ASN A 1 112 ? -34.44900 23.82100 -5.89500  1.000 29.45616  ? 112 ASN A CG   1 
ATOM   1728 O OD1  . ASN A 1 112 ? -34.74500 24.99200 -6.06700  1.000 37.47818  ? 112 ASN A OD1  1 
ATOM   1729 N ND2  . ASN A 1 112 ? -34.29200 22.97200 -6.89700  1.000 38.97309  ? 112 ASN A ND2  1 
ATOM   1730 H H    . ASN A 1 112 ? -32.39200 24.85200 -4.61300  1.000 48.79000  ? 112 ASN A H    1 
ATOM   1731 H HA   . ASN A 1 112 ? -34.71500 25.00800 -3.54500  1.000 36.61000  ? 112 ASN A HA   1 
ATOM   1732 H HB2  . ASN A 1 112 ? -33.50200 22.67200 -4.55000  1.000 33.61000  ? 112 ASN A HB2  1 
ATOM   1733 H HB3  . ASN A 1 112 ? -35.06200 22.80900 -4.27500  1.000 33.61000  ? 112 ASN A HB3  1 
ATOM   1734 H HD21 . ASN A 1 112 ? -34.08400 22.15300 -6.73800  1.000 47.39000  ? 112 ASN A HD21 1 
ATOM   1735 H HD22 . ASN A 1 112 ? -34.39500 23.24000 -7.70800  1.000 47.39000  ? 112 ASN A HD22 1 
ATOM   1736 N N    . LEU A 1 113 ? -32.83600 23.13300 -1.73300  1.000 29.22192  ? 113 LEU A N    1 
ATOM   1737 C CA   . LEU A 1 113 ? -32.76100 22.45100 -0.44300  1.000 28.81924  ? 113 LEU A CA   1 
ATOM   1738 C C    . LEU A 1 113 ? -32.74900 23.45700 0.69500   1.000 25.76098  ? 113 LEU A C    1 
ATOM   1739 O O    . LEU A 1 113 ? -33.27400 23.21400 1.78900   1.000 32.53285  ? 113 LEU A O    1 
ATOM   1740 C CB   . LEU A 1 113 ? -31.50100 21.56600 -0.39300  1.000 21.91842  ? 113 LEU A CB   1 
ATOM   1741 C CG   . LEU A 1 113 ? -31.56200 20.29700 -1.26600  1.000 29.52722  ? 113 LEU A CG   1 
ATOM   1742 C CD1  . LEU A 1 113 ? -30.21500 19.59500 -1.36700  1.000 31.40640  ? 113 LEU A CD1  1 
ATOM   1743 C CD2  . LEU A 1 113 ? -32.55500 19.29700 -0.72400  1.000 26.92165  ? 113 LEU A CD2  1 
ATOM   1744 H H    . LEU A 1 113 ? -32.11600 23.08100 -2.20000  1.000 35.69000  ? 113 LEU A H    1 
ATOM   1745 H HA   . LEU A 1 113 ? -33.54000 21.88300 -0.33600  1.000 35.21000  ? 113 LEU A HA   1 
ATOM   1746 H HB2  . LEU A 1 113 ? -30.74300 22.09100 -0.69300  1.000 26.93000  ? 113 LEU A HB2  1 
ATOM   1747 H HB3  . LEU A 1 113 ? -31.35900 21.28400 0.52400   1.000 26.93000  ? 113 LEU A HB3  1 
ATOM   1748 H HG   . LEU A 1 113 ? -31.84100 20.54200 -2.16200  1.000 36.06000  ? 113 LEU A HG   1 
ATOM   1749 H HD11 . LEU A 1 113 ? -29.56700 20.20900 -1.74700  1.000 38.32000  ? 113 LEU A HD11 1 
ATOM   1750 H HD12 . LEU A 1 113 ? -30.30700 18.81600 -1.93800  1.000 38.32000  ? 113 LEU A HD12 1 
ATOM   1751 H HD13 . LEU A 1 113 ? -29.93300 19.32400 -0.47900  1.000 38.32000  ? 113 LEU A HD13 1 
ATOM   1752 H HD21 . LEU A 1 113 ? -32.53100 18.50100 -1.27700  1.000 32.93000  ? 113 LEU A HD21 1 
ATOM   1753 H HD22 . LEU A 1 113 ? -32.31300 19.07500 0.18900   1.000 32.93000  ? 113 LEU A HD22 1 
ATOM   1754 H HD23 . LEU A 1 113 ? -33.44300 19.68700 -0.74600  1.000 32.93000  ? 113 LEU A HD23 1 
ATOM   1755 N N    . LYS A 1 114 ? -32.17800 24.61000 0.43600   1.000 34.56467  ? 114 LYS A N    1 
ATOM   1756 C CA   . LYS A 1 114 ? -32.12200 25.60500 1.46900   1.000 32.12227  ? 114 LYS A CA   1 
ATOM   1757 C C    . LYS A 1 114 ? -33.48900 26.21200 1.67700   1.000 32.65655  ? 114 LYS A C    1 
ATOM   1758 O O    . LYS A 1 114 ? -33.92000 26.43100 2.81700   1.000 32.42494  ? 114 LYS A O    1 
ATOM   1759 C CB   . LYS A 1 114 ? -31.10200 26.66300 1.07800   1.000 33.39611  ? 114 LYS A CB   1 
ATOM   1760 C CG   . LYS A 1 114 ? -30.94800 27.71400 2.10900   1.000 60.64411  ? 114 LYS A CG   1 
ATOM   1761 C CD   . LYS A 1 114 ? -30.21500 27.15400 3.34500   1.000 90.68719  ? 114 LYS A CD   1 
ATOM   1762 C CE   . LYS A 1 114 ? -30.07900 28.17500 4.49600   1.000 69.24778  ? 114 LYS A CE   1 
ATOM   1763 N NZ   . LYS A 1 114 ? -29.34600 27.55300 5.65500   1.000 80.70178  ? 114 LYS A NZ   1 
ATOM   1764 H H    . LYS A 1 114 ? -31.82200 24.83700 -0.31300  1.000 42.10000  ? 114 LYS A H    1 
ATOM   1765 H HA   . LYS A 1 114 ? -31.83800 25.18900 2.29600   1.000 39.17000  ? 114 LYS A HA   1 
ATOM   1766 H HB2  . LYS A 1 114 ? -30.23900 26.23900 0.95000   1.000 40.70000  ? 114 LYS A HB2  1 
ATOM   1767 H HB3  . LYS A 1 114 ? -31.38800 27.08900 0.25500   1.000 40.70000  ? 114 LYS A HB3  1 
ATOM   1768 H HG2  . LYS A 1 114 ? -30.41600 28.44000 1.74600   1.000 73.40000  ? 114 LYS A HG2  1 
ATOM   1769 H HG3  . LYS A 1 114 ? -31.81600 28.04400 2.38800   1.000 73.40000  ? 114 LYS A HG3  1 
ATOM   1770 H HD2  . LYS A 1 114 ? -30.70500 26.39200 3.68900   1.000 109.45000 ? 114 LYS A HD2  1 
ATOM   1771 H HD3  . LYS A 1 114 ? -29.32200 26.88100 3.08300   1.000 109.45000 ? 114 LYS A HD3  1 
ATOM   1772 H HE2  . LYS A 1 114 ? -29.57500 28.94500 4.18900   1.000 83.72000  ? 114 LYS A HE2  1 
ATOM   1773 H HE3  . LYS A 1 114 ? -30.96100 28.44400 4.79700   1.000 83.72000  ? 114 LYS A HE3  1 
ATOM   1774 H HZ1  . LYS A 1 114 ? -29.26900 28.14200 6.31700   1.000 97.47000  ? 114 LYS A HZ1  1 
ATOM   1775 H HZ2  . LYS A 1 114 ? -29.79300 26.84200 5.95100   1.000 97.47000  ? 114 LYS A HZ2  1 
ATOM   1776 H HZ3  . LYS A 1 114 ? -28.53300 27.29700 5.39900   1.000 97.47000  ? 114 LYS A HZ3  1 
ATOM   1777 N N    . ARG A 1 115 ? -34.17400 26.52100 0.59000   1.000 31.66432  ? 115 ARG A N    1 
ATOM   1778 C CA   . ARG A 1 115 ? -35.53800 27.01800 0.72500   1.000 29.40089  ? 115 ARG A CA   1 
ATOM   1779 C C    . ARG A 1 115 ? -36.38300 26.01200 1.48400   1.000 29.73251  ? 115 ARG A C    1 
ATOM   1780 O O    . ARG A 1 115 ? -37.23300 26.37800 2.30500   1.000 31.96962  ? 115 ARG A O    1 
ATOM   1781 C CB   . ARG A 1 115 ? -36.12100 27.27900 -0.65500  1.000 36.82020  ? 115 ARG A CB   1 
ATOM   1782 C CG   . ARG A 1 115 ? -35.72500 28.59200 -1.29300  1.000 40.91280  ? 115 ARG A CG   1 
ATOM   1783 C CD   . ARG A 1 115 ? -36.48900 28.81900 -2.63100  1.000 46.41346  ? 115 ARG A CD   1 
ATOM   1784 N NE   . ARG A 1 115 ? -35.93300 28.07200 -3.75600  1.000 50.10338  ? 115 ARG A NE   1 
ATOM   1785 C CZ   . ARG A 1 115 ? -34.88200 28.46100 -4.46900  1.000 59.27816  ? 115 ARG A CZ   1 
ATOM   1786 N NH1  . ARG A 1 115 ? -34.26600 29.60200 -4.22700  1.000 60.54147  ? 115 ARG A NH1  1 
ATOM   1787 N NH2  . ARG A 1 115 ? -34.42200 27.67000 -5.43200  1.000 64.99990  ? 115 ARG A NH2  1 
ATOM   1788 H H    . ARG A 1 115 ? -33.88600 26.45600 -0.21800  1.000 38.62000  ? 115 ARG A H    1 
ATOM   1789 H HA   . ARG A 1 115 ? -35.53200 27.85200 1.22000   1.000 35.91000  ? 115 ARG A HA   1 
ATOM   1790 H HB2  . ARG A 1 115 ? -35.83300 26.56900 -1.24900  1.000 44.81000  ? 115 ARG A HB2  1 
ATOM   1791 H HB3  . ARG A 1 115 ? -37.08800 27.27000 -0.58500  1.000 44.81000  ? 115 ARG A HB3  1 
ATOM   1792 H HG2  . ARG A 1 115 ? -35.94200 29.32000 -0.69000  1.000 49.72000  ? 115 ARG A HG2  1 
ATOM   1793 H HG3  . ARG A 1 115 ? -34.77400 28.58300 -1.48200  1.000 49.72000  ? 115 ARG A HG3  1 
ATOM   1794 H HD2  . ARG A 1 115 ? -37.41000 28.53700 -2.51600  1.000 56.32000  ? 115 ARG A HD2  1 
ATOM   1795 H HD3  . ARG A 1 115 ? -36.46200 29.76300 -2.85300  1.000 56.32000  ? 115 ARG A HD3  1 
ATOM   1796 H HE   . ARG A 1 115 ? -36.31000 27.32900 -3.97000  1.000 60.75000  ? 115 ARG A HE   1 
ATOM   1797 H HH11 . ARG A 1 115 ? -34.54700 30.12300 -3.60400  1.000 73.28000  ? 115 ARG A HH11 1 
ATOM   1798 H HH12 . ARG A 1 115 ? -33.58600 29.83000 -4.70100  1.000 73.28000  ? 115 ARG A HH12 1 
ATOM   1799 H HH21 . ARG A 1 115 ? -34.81400 26.92300 -5.59900  1.000 78.62000  ? 115 ARG A HH21 1 
ATOM   1800 H HH22 . ARG A 1 115 ? -33.74200 27.91300 -5.90000  1.000 78.62000  ? 115 ARG A HH22 1 
ATOM   1801 N N    . ALA A 1 116 ? -36.15300 24.72600 1.23400   1.000 29.46143  ? 116 ALA A N    1 
ATOM   1802 C CA   . ALA A 1 116 ? -37.01000 23.73100 1.86200   1.000 22.14739  ? 116 ALA A CA   1 
ATOM   1803 C C    . ALA A 1 116 ? -36.70500 23.57900 3.33000   1.000 22.09475  ? 116 ALA A C    1 
ATOM   1804 O O    . ALA A 1 116 ? -37.62000 23.46900 4.15300   1.000 21.47363  ? 116 ALA A O    1 
ATOM   1805 C CB   . ALA A 1 116 ? -36.89300 22.40700 1.09800   1.000 21.24465  ? 116 ALA A CB   1 
ATOM   1806 H H    . ALA A 1 116 ? -35.53300 24.41400 0.72600   1.000 35.98000  ? 116 ALA A H    1 
ATOM   1807 H HA   . ALA A 1 116 ? -37.93000 24.02800 1.78700   1.000 27.21000  ? 116 ALA A HA   1 
ATOM   1808 H HB1  . ALA A 1 116 ? -37.46600 21.74800 1.52000   1.000 26.12000  ? 116 ALA A HB1  1 
ATOM   1809 H HB2  . ALA A 1 116 ? -37.17100 22.54700 0.17900   1.000 26.12000  ? 116 ALA A HB2  1 
ATOM   1810 H HB3  . ALA A 1 116 ? -35.97000 22.10900 1.12300   1.000 26.12000  ? 116 ALA A HB3  1 
ATOM   1811 N N    . ILE A 1 117 ? -35.44100 23.60600 3.71300   1.000 28.51921  ? 117 ILE A N    1 
ATOM   1812 C CA   . ILE A 1 117 ? -35.17500 23.38500 5.11700   1.000 24.18448  ? 117 ILE A CA   1 
ATOM   1813 C C    . ILE A 1 117 ? -35.61800 24.60900 5.89200   1.000 31.64590  ? 117 ILE A C    1 
ATOM   1814 O O    . ILE A 1 117 ? -36.05300 24.51400 7.03600   1.000 35.46215  ? 117 ILE A O    1 
ATOM   1815 C CB   . ILE A 1 117 ? -33.69400 23.03500 5.36500   1.000 37.75979  ? 117 ILE A CB   1 
ATOM   1816 C CG1  . ILE A 1 117 ? -33.50900 22.67700 6.83900   1.000 36.45174  ? 117 ILE A CG1  1 
ATOM   1817 C CG2  . ILE A 1 117 ? -32.75000 24.15700 5.00500   1.000 45.79233  ? 117 ILE A CG2  1 
ATOM   1818 C CD1  . ILE A 1 117 ? -34.22600 21.36100 7.27700   1.000 33.23556  ? 117 ILE A CD1  1 
ATOM   1819 H H    . ILE A 1 117 ? -34.75600 23.74200 3.21100   1.000 34.85000  ? 117 ILE A H    1 
ATOM   1820 H HA   . ILE A 1 117 ? -35.71300 22.63600 5.41500   1.000 29.65000  ? 117 ILE A HA   1 
ATOM   1821 H HB   . ILE A 1 117 ? -33.46800 22.25900 4.82900   1.000 45.94000  ? 117 ILE A HB   1 
ATOM   1822 H HG12 . ILE A 1 117 ? -32.56100 22.56100 7.00900   1.000 44.37000  ? 117 ILE A HG12 1 
ATOM   1823 H HG13 . ILE A 1 117 ? -33.84900 23.39800 7.39100   1.000 44.37000  ? 117 ILE A HG13 1 
ATOM   1824 H HG21 . ILE A 1 117 ? -31.83800 23.85000 5.11800   1.000 55.58000  ? 117 ILE A HG21 1 
ATOM   1825 H HG22 . ILE A 1 117 ? -32.90300 24.41100 4.08200   1.000 55.58000  ? 117 ILE A HG22 1 
ATOM   1826 H HG23 . ILE A 1 117 ? -32.91900 24.91300 5.58900   1.000 55.58000  ? 117 ILE A HG23 1 
ATOM   1827 H HD11 . ILE A 1 117 ? -34.01200 21.18300 8.20600   1.000 40.51000  ? 117 ILE A HD11 1 
ATOM   1828 H HD12 . ILE A 1 117 ? -35.18400 21.46700 7.17500   1.000 40.51000  ? 117 ILE A HD12 1 
ATOM   1829 H HD13 . ILE A 1 117 ? -33.91000 20.63300 6.72300   1.000 40.51000  ? 117 ILE A HD13 1 
ATOM   1830 N N    . GLU A 1 118 ? -35.58400 25.76900 5.26100   1.000 31.72486  ? 118 GLU A N    1 
ATOM   1831 C CA   . GLU A 1 118 ? -36.10500 26.95300 5.91800   1.000 32.76445  ? 118 GLU A CA   1 
ATOM   1832 C C    . GLU A 1 118 ? -37.61900 26.86300 6.05600   1.000 28.85346  ? 118 GLU A C    1 
ATOM   1833 O O    . GLU A 1 118 ? -38.17500 27.14600 7.11100   1.000 37.06760  ? 118 GLU A O    1 
ATOM   1834 C CB   . GLU A 1 118 ? -35.69400 28.19900 5.13900   1.000 39.90478  ? 118 GLU A CB   1 
ATOM   1835 C CG   . GLU A 1 118 ? -34.17800 28.46700 5.14700   1.000 67.20543  ? 118 GLU A CG   1 
ATOM   1836 C CD   . GLU A 1 118 ? -33.57400 28.60100 6.56400   1.000 88.91329  ? 118 GLU A CD   1 
ATOM   1837 O OE1  . GLU A 1 118 ? -33.95200 29.54500 7.31800   1.000 82.99153  ? 118 GLU A OE1  1 
ATOM   1838 O OE2  . GLU A 1 118 ? -32.70800 27.75700 6.91700   1.000 82.47831  ? 118 GLU A OE2  1 
ATOM   1839 H H    . GLU A 1 118 ? -35.27100 25.89900 4.47000   1.000 38.70000  ? 118 GLU A H    1 
ATOM   1840 H HA   . GLU A 1 118 ? -35.72800 27.01300 6.80900   1.000 39.95000  ? 118 GLU A HA   1 
ATOM   1841 H HB2  . GLU A 1 118 ? -35.97200 28.09600 4.21500   1.000 48.51000  ? 118 GLU A HB2  1 
ATOM   1842 H HB3  . GLU A 1 118 ? -36.13300 28.97100 5.53000   1.000 48.51000  ? 118 GLU A HB3  1 
ATOM   1843 H HG2  . GLU A 1 118 ? -33.72600 27.73200 4.70900   1.000 81.27000  ? 118 GLU A HG2  1 
ATOM   1844 H HG3  . GLU A 1 118 ? -34.00300 29.29300 4.67000   1.000 81.27000  ? 118 GLU A HG3  1 
ATOM   1845 N N    . ALA A 1 119 ? -38.30900 26.49200 5.00100   1.000 32.75656  ? 119 ALA A N    1 
ATOM   1846 C CA   . ALA A 1 119 ? -39.75000 26.34800 5.14900   1.000 30.11414  ? 119 ALA A CA   1 
ATOM   1847 C C    . ALA A 1 119 ? -40.07500 25.44400 6.31400   1.000 29.22719  ? 119 ALA A C    1 
ATOM   1848 O O    . ALA A 1 119 ? -41.02000 25.69200 7.05900   1.000 32.80130  ? 119 ALA A O    1 
ATOM   1849 C CB   . ALA A 1 119 ? -40.34900 25.79900 3.86700   1.000 29.69303  ? 119 ALA A CB   1 
ATOM   1850 H H    . ALA A 1 119 ? -37.99200 26.32300 4.22000   1.000 39.93000  ? 119 ALA A H    1 
ATOM   1851 H HA   . ALA A 1 119 ? -40.14300 27.21800 5.32000   1.000 36.77000  ? 119 ALA A HA   1 
ATOM   1852 H HB1  . ALA A 1 119 ? -41.30800 25.70900 3.98100   1.000 36.26000  ? 119 ALA A HB1  1 
ATOM   1853 H HB2  . ALA A 1 119 ? -39.95400 24.93300 3.68000   1.000 36.26000  ? 119 ALA A HB2  1 
ATOM   1854 H HB3  . ALA A 1 119 ? -40.15800 26.41300 3.14100   1.000 36.26000  ? 119 ALA A HB3  1 
ATOM   1855 N N    . ILE A 1 120 ? -39.32000 24.36000 6.45800   1.000 32.62496  ? 120 ILE A N    1 
ATOM   1856 C CA   . ILE A 1 120 ? -39.60000 23.38300 7.49800   1.000 25.72677  ? 120 ILE A CA   1 
ATOM   1857 C C    . ILE A 1 120 ? -39.33600 23.99300 8.85600   1.000 25.00826  ? 120 ILE A C    1 
ATOM   1858 O O    . ILE A 1 120 ? -40.12600 23.87500 9.80000   1.000 31.32744  ? 120 ILE A O    1 
ATOM   1859 C CB   . ILE A 1 120 ? -38.72900 22.12900 7.28200   1.000 29.14823  ? 120 ILE A CB   1 
ATOM   1860 C CG1  . ILE A 1 120 ? -39.07100 21.40100 6.00700   1.000 29.51143  ? 120 ILE A CG1  1 
ATOM   1861 C CG2  . ILE A 1 120 ? -38.82900 21.25700 8.48400   1.000 37.85717  ? 120 ILE A CG2  1 
ATOM   1862 C CD1  . ILE A 1 120 ? -40.03300 20.34100 6.19700   1.000 31.80645  ? 120 ILE A CD1  1 
ATOM   1863 H H    . ILE A 1 120 ? -38.64100 24.16900 5.96600   1.000 39.78000  ? 120 ILE A H    1 
ATOM   1864 H HA   . ILE A 1 120 ? -40.53300 23.12100 7.45400   1.000 31.50000  ? 120 ILE A HA   1 
ATOM   1865 H HB   . ILE A 1 120 ? -37.80700 22.42300 7.21100   1.000 35.60000  ? 120 ILE A HB   1 
ATOM   1866 H HG12 . ILE A 1 120 ? -39.44500 22.03200 5.37200   1.000 36.04000  ? 120 ILE A HG12 1 
ATOM   1867 H HG13 . ILE A 1 120 ? -38.26200 21.00800 5.64400   1.000 36.04000  ? 120 ILE A HG13 1 
ATOM   1868 H HG21 . ILE A 1 120 ? -38.45900 20.38400 8.27900   1.000 46.06000  ? 120 ILE A HG21 1 
ATOM   1869 H HG22 . ILE A 1 120 ? -38.31900 21.65200 9.20800   1.000 46.06000  ? 120 ILE A HG22 1 
ATOM   1870 H HG23 . ILE A 1 120 ? -39.76000 21.17300 8.74300   1.000 46.06000  ? 120 ILE A HG23 1 
ATOM   1871 H HD11 . ILE A 1 120 ? -39.59600 19.57200 6.59400   1.000 38.80000  ? 120 ILE A HD11 1 
ATOM   1872 H HD12 . ILE A 1 120 ? -40.39400 20.09500 5.33100   1.000 38.80000  ? 120 ILE A HD12 1 
ATOM   1873 H HD13 . ILE A 1 120 ? -40.75100 20.65600 6.76900   1.000 38.80000  ? 120 ILE A HD13 1 
ATOM   1874 N N    . LYS A 1 121 ? -38.20600 24.67800 8.97900   1.000 35.38056  ? 121 LYS A N    1 
ATOM   1875 C CA   . LYS A 1 121 ? -37.89900 25.35000 10.22200  1.000 37.65715  ? 121 LYS A CA   1 
ATOM   1876 C C    . LYS A 1 121 ? -39.00300 26.31700 10.61000  1.000 42.88935  ? 121 LYS A C    1 
ATOM   1877 O O    . LYS A 1 121 ? -39.43300 26.34300 11.76500  1.000 43.12886  ? 121 LYS A O    1 
ATOM   1878 C CB   . LYS A 1 121 ? -36.56000 26.08700 10.10400  1.000 34.92524  ? 121 LYS A CB   1 
ATOM   1879 C CG   . LYS A 1 121 ? -35.98200 26.46000 11.43400  1.000 47.51886  ? 121 LYS A CG   1 
ATOM   1880 C CD   . LYS A 1 121 ? -34.51900 26.84500 11.30100  1.000 52.77212  ? 121 LYS A CD   1 
ATOM   1881 C CE   . LYS A 1 121 ? -34.34800 28.01300 10.34200  1.000 69.31621  ? 121 LYS A CE   1 
ATOM   1882 N NZ   . LYS A 1 121 ? -33.04400 28.70300 10.56200  1.000 78.87525  ? 121 LYS A NZ   1 
ATOM   1883 H H    . LYS A 1 121 ? -37.61100 24.76600 8.36400   1.000 43.08000  ? 121 LYS A H    1 
ATOM   1884 H HA   . LYS A 1 121 ? -37.81800 24.68900 10.92700  1.000 45.82000  ? 121 LYS A HA   1 
ATOM   1885 H HB2  . LYS A 1 121 ? -35.92300 25.51400 9.65000   1.000 42.54000  ? 121 LYS A HB2  1 
ATOM   1886 H HB3  . LYS A 1 121 ? -36.69600 26.90100 9.59500   1.000 42.54000  ? 121 LYS A HB3  1 
ATOM   1887 H HG2  . LYS A 1 121 ? -36.46700 27.21900 11.79400  1.000 57.65000  ? 121 LYS A HG2  1 
ATOM   1888 H HG3  . LYS A 1 121 ? -36.04500 25.70300 12.03700  1.000 57.65000  ? 121 LYS A HG3  1 
ATOM   1889 H HD2  . LYS A 1 121 ? -34.17600 27.10900 12.16900  1.000 63.96000  ? 121 LYS A HD2  1 
ATOM   1890 H HD3  . LYS A 1 121 ? -34.01700 26.09100 10.95500  1.000 63.96000  ? 121 LYS A HD3  1 
ATOM   1891 H HE2  . LYS A 1 121 ? -34.36900 27.68500 9.42900   1.000 83.81000  ? 121 LYS A HE2  1 
ATOM   1892 H HE3  . LYS A 1 121 ? -35.06100 28.65500 10.48600  1.000 83.81000  ? 121 LYS A HE3  1 
ATOM   1893 H HZ1  . LYS A 1 121 ? -33.00200 29.01500 11.39400  1.000 95.28000  ? 121 LYS A HZ1  1 
ATOM   1894 H HZ2  . LYS A 1 121 ? -32.96000 29.38300 9.99400   1.000 95.28000  ? 121 LYS A HZ2  1 
ATOM   1895 H HZ3  . LYS A 1 121 ? -32.37300 28.13300 10.43200  1.000 95.28000  ? 121 LYS A HZ3  1 
ATOM   1896 N N    . HIS A 1 122 ? -39.47100 27.13600 9.66400   1.000 34.12514  ? 122 HIS A N    1 
ATOM   1897 C CA   . HIS A 1 122 ? -40.50000 28.12400 10.02600  1.000 39.09153  ? 122 HIS A CA   1 
ATOM   1898 C C    . HIS A 1 122 ? -41.79900 27.41600 10.36500  1.000 30.63525  ? 122 HIS A C    1 
ATOM   1899 O O    . HIS A 1 122 ? -42.53100 27.82700 11.25200  1.000 37.85980  ? 122 HIS A O    1 
ATOM   1900 C CB   . HIS A 1 122 ? -40.76400 29.12200 8.88700   1.000 35.48583  ? 122 HIS A CB   1 
ATOM   1901 C CG   . HIS A 1 122 ? -39.55400 29.89400 8.43900   1.000 67.10805  ? 122 HIS A CG   1 
ATOM   1902 N ND1  . HIS A 1 122 ? -39.42400 30.40200 7.15900   1.000 71.11379  ? 122 HIS A ND1  1 
ATOM   1903 C CD2  . HIS A 1 122 ? -38.42700 30.25400 9.10100   1.000 63.17073  ? 122 HIS A CD2  1 
ATOM   1904 C CE1  . HIS A 1 122 ? -38.26900 31.03500 7.05100   1.000 68.09501  ? 122 HIS A CE1  1 
ATOM   1905 N NE2  . HIS A 1 122 ? -37.64200 30.95500 8.21300   1.000 65.18940  ? 122 HIS A NE2  1 
ATOM   1906 H H    . HIS A 1 122 ? -39.22400 27.14500 8.84000   1.000 41.58000  ? 122 HIS A H    1 
ATOM   1907 H HA   . HIS A 1 122 ? -40.20900 28.62100 10.80700  1.000 47.54000  ? 122 HIS A HA   1 
ATOM   1908 H HB2  . HIS A 1 122 ? -41.10200 28.63400 8.12000   1.000 43.21000  ? 122 HIS A HB2  1 
ATOM   1909 H HB3  . HIS A 1 122 ? -41.42800 29.76300 9.18500   1.000 43.21000  ? 122 HIS A HB3  1 
ATOM   1910 H HD2  . HIS A 1 122 ? -38.21900 30.05600 9.98500   1.000 76.43000  ? 122 HIS A HD2  1 
ATOM   1911 H HE1  . HIS A 1 122 ? -37.94900 31.45900 6.28700   1.000 82.34000  ? 122 HIS A HE1  1 
ATOM   1912 H HE2  . HIS A 1 122 ? -36.87200 31.29500 8.38900   1.000 78.85000  ? 122 HIS A HE2  1 
ATOM   1913 N N    . LEU A 1 123 ? -42.11200 26.33500 9.66700   1.000 31.68538  ? 123 LEU A N    1 
ATOM   1914 C CA   . LEU A 1 123 ? -43.30700 25.59400 10.06100  1.000 29.60092  ? 123 LEU A CA   1 
ATOM   1915 C C    . LEU A 1 123 ? -43.22300 25.15200 11.50800  1.000 36.78336  ? 123 LEU A C    1 
ATOM   1916 O O    . LEU A 1 123 ? -44.12100 25.41600 12.30800  1.000 42.72354  ? 123 LEU A O    1 
ATOM   1917 C CB   . LEU A 1 123 ? -43.49900 24.39000 9.14500   1.000 30.22468  ? 123 LEU A CB   1 
ATOM   1918 C CG   . LEU A 1 123 ? -44.71500 23.56700 9.60200   1.000 30.88265  ? 123 LEU A CG   1 
ATOM   1919 C CD1  . LEU A 1 123 ? -45.96100 24.40000 9.54500   1.000 43.51048  ? 123 LEU A CD1  1 
ATOM   1920 C CD2  . LEU A 1 123 ? -44.89000 22.35900 8.68500   1.000 30.84317  ? 123 LEU A CD2  1 
ATOM   1921 H H    . LEU A 1 123 ? -41.67700 26.01900 8.99500   1.000 38.65000  ? 123 LEU A H    1 
ATOM   1922 H HA   . LEU A 1 123 ? -44.07500 26.17800 9.96800   1.000 36.15000  ? 123 LEU A HA   1 
ATOM   1923 H HB2  . LEU A 1 123 ? -43.65500 24.69300 8.23700   1.000 36.90000  ? 123 LEU A HB2  1 
ATOM   1924 H HB3  . LEU A 1 123 ? -42.71200 23.82400 9.18400   1.000 36.90000  ? 123 LEU A HB3  1 
ATOM   1925 H HG   . LEU A 1 123 ? -44.59200 23.24300 10.50700  1.000 37.69000  ? 123 LEU A HG   1 
ATOM   1926 H HD11 . LEU A 1 123 ? -45.97400 25.00700 10.30100  1.000 52.84000  ? 123 LEU A HD11 1 
ATOM   1927 H HD12 . LEU A 1 123 ? -46.73300 23.81300 9.58100   1.000 52.84000  ? 123 LEU A HD12 1 
ATOM   1928 H HD13 . LEU A 1 123 ? -45.96700 24.90100 8.71400   1.000 52.84000  ? 123 LEU A HD13 1 
ATOM   1929 H HD21 . LEU A 1 123 ? -45.64500 21.83400 8.99500   1.000 37.64000  ? 123 LEU A HD21 1 
ATOM   1930 H HD22 . LEU A 1 123 ? -45.05200 22.67000 7.78100   1.000 37.64000  ? 123 LEU A HD22 1 
ATOM   1931 H HD23 . LEU A 1 123 ? -44.08200 21.82300 8.71100   1.000 37.64000  ? 123 LEU A HD23 1 
ATOM   1932 N N    . LEU A 1 124 ? -42.15100 24.45200 11.86600  1.000 41.84449  ? 124 LEU A N    1 
ATOM   1933 C CA   . LEU A 1 124 ? -42.04200 23.95600 13.22800  1.000 41.02597  ? 124 LEU A CA   1 
ATOM   1934 C C    . LEU A 1 124 ? -42.04200 25.10800 14.21000  1.000 37.84138  ? 124 LEU A C    1 
ATOM   1935 O O    . LEU A 1 124 ? -42.67300 25.03800 15.27500  1.000 47.28198  ? 124 LEU A O    1 
ATOM   1936 C CB   . LEU A 1 124 ? -40.77800 23.10500 13.35100  1.000 36.43595  ? 124 LEU A CB   1 
ATOM   1937 C CG   . LEU A 1 124 ? -40.79800 22.13500 14.52400  1.000 49.62174  ? 124 LEU A CG   1 
ATOM   1938 C CD1  . LEU A 1 124 ? -39.87900 21.01200 14.14900  1.000 62.49697  ? 124 LEU A CD1  1 
ATOM   1939 C CD2  . LEU A 1 124 ? -40.33300 22.81700 15.77000  1.000 79.40426  ? 124 LEU A CD2  1 
ATOM   1940 H H    . LEU A 1 124 ? -41.49000 24.25600 11.35200  1.000 50.84000  ? 124 LEU A H    1 
ATOM   1941 H HA   . LEU A 1 124 ? -42.80700 23.39200 13.42300  1.000 49.86000  ? 124 LEU A HA   1 
ATOM   1942 H HB2  . LEU A 1 124 ? -40.67400 22.58500 12.53900  1.000 44.35000  ? 124 LEU A HB2  1 
ATOM   1943 H HB3  . LEU A 1 124 ? -40.01500 23.69300 13.46300  1.000 44.35000  ? 124 LEU A HB3  1 
ATOM   1944 H HG   . LEU A 1 124 ? -41.69300 21.78700 14.66100  1.000 60.17000  ? 124 LEU A HG   1 
ATOM   1945 H HD11 . LEU A 1 124 ? -40.26000 20.52700 13.40000  1.000 75.62000  ? 124 LEU A HD11 1 
ATOM   1946 H HD12 . LEU A 1 124 ? -39.78000 20.41900 14.91000  1.000 75.62000  ? 124 LEU A HD12 1 
ATOM   1947 H HD13 . LEU A 1 124 ? -39.01600 21.38000 13.90200  1.000 75.62000  ? 124 LEU A HD13 1 
ATOM   1948 H HD21 . LEU A 1 124 ? -40.42000 23.77600 15.67500  1.000 95.91000  ? 124 LEU A HD21 1 
ATOM   1949 H HD22 . LEU A 1 124 ? -39.40300 22.58800 15.92000  1.000 95.91000  ? 124 LEU A HD22 1 
ATOM   1950 H HD23 . LEU A 1 124 ? -40.86900 22.50700 16.51600  1.000 95.91000  ? 124 LEU A HD23 1 
ATOM   1951 N N    . GLN A 1 125 ? -41.41400 26.21900 13.83400  1.000 49.66911  ? 125 GLN A N    1 
ATOM   1952 C CA   . GLN A 1 125 ? -41.42500 27.39800 14.69900  1.000 41.15493  ? 125 GLN A CA   1 
ATOM   1953 C C    . GLN A 1 125 ? -42.84000 27.88100 15.00300  1.000 45.93445  ? 125 GLN A C    1 
ATOM   1954 O O    . GLN A 1 125 ? -43.16600 28.15900 16.16300  1.000 59.14920  ? 125 GLN A O    1 
ATOM   1955 C CB   . GLN A 1 125 ? -40.61900 28.52200 14.05500  1.000 52.60894  ? 125 GLN A CB   1 
ATOM   1956 C CG   . GLN A 1 125 ? -39.11700 28.38700 14.28300  1.000 57.53321  ? 125 GLN A CG   1 
ATOM   1957 C CD   . GLN A 1 125 ? -38.30700 29.33500 13.41600  1.000 66.39480  ? 125 GLN A CD   1 
ATOM   1958 O OE1  . GLN A 1 125 ? -38.85500 30.10100 12.60500  1.000 73.26668  ? 125 GLN A OE1  1 
ATOM   1959 N NE2  . GLN A 1 125 ? -36.99100 29.28600 13.57900  1.000 64.39719  ? 125 GLN A NE2  1 
ATOM   1960 H H    . GLN A 1 125 ? -40.98100 26.31700 13.09700  1.000 60.23000  ? 125 GLN A H    1 
ATOM   1961 H HA   . GLN A 1 125 ? -41.00100 27.17200 15.54200  1.000 50.01000  ? 125 GLN A HA   1 
ATOM   1962 H HB2  . GLN A 1 125 ? -40.77800 28.51500 13.09800  1.000 63.76000  ? 125 GLN A HB2  1 
ATOM   1963 H HB3  . GLN A 1 125 ? -40.90400 29.36900 14.43200  1.000 63.76000  ? 125 GLN A HB3  1 
ATOM   1964 H HG2  . GLN A 1 125 ? -38.91900 28.58600 15.21200  1.000 69.67000  ? 125 GLN A HG2  1 
ATOM   1965 H HG3  . GLN A 1 125 ? -38.84500 27.48000 14.07200  1.000 69.67000  ? 125 GLN A HG3  1 
ATOM   1966 H HE21 . GLN A 1 125 ? -36.64800 28.74200 14.15000  1.000 77.90000  ? 125 GLN A HE21 1 
ATOM   1967 H HE22 . GLN A 1 125 ? -36.48100 29.80000 13.11500  1.000 77.90000  ? 125 GLN A HE22 1 
ATOM   1968 N N    . LEU A 1 126 ? -43.68600 28.02500 13.97100  1.000 52.07203  ? 126 LEU A N    1 
ATOM   1969 C CA   . LEU A 1 126 ? -45.08100 28.41500 14.19900  1.000 38.50198  ? 126 LEU A CA   1 
ATOM   1970 C C    . LEU A 1 126 ? -45.82100 27.35600 15.01900  1.000 41.31285  ? 126 LEU A C    1 
ATOM   1971 O O    . LEU A 1 126 ? -46.34900 27.62700 16.10700  1.000 61.88374  ? 126 LEU A O    1 
ATOM   1972 C CB   . LEU A 1 126 ? -45.80100 28.59000 12.87100  1.000 51.89570  ? 126 LEU A CB   1 
ATOM   1973 C CG   . LEU A 1 126 ? -45.96300 29.94500 12.22000  1.000 58.38595  ? 126 LEU A CG   1 
ATOM   1974 C CD1  . LEU A 1 126 ? -44.63200 30.59500 12.02700  1.000 76.75657  ? 126 LEU A CD1  1 
ATOM   1975 C CD2  . LEU A 1 126 ? -46.68000 29.67800 10.88500  1.000 66.87118  ? 126 LEU A CD2  1 
ATOM   1976 H H    . LEU A 1 126 ? -43.47800 27.90500 13.14500  1.000 63.11000  ? 126 LEU A H    1 
ATOM   1977 H HA   . LEU A 1 126 ? -45.11000 29.25600 14.68100  1.000 46.83000  ? 126 LEU A HA   1 
ATOM   1978 H HB2  . LEU A 1 126 ? -45.34200 28.03400 12.22200  1.000 62.90000  ? 126 LEU A HB2  1 
ATOM   1979 H HB3  . LEU A 1 126 ? -46.69900 28.24200 12.98900  1.000 62.90000  ? 126 LEU A HB3  1 
ATOM   1980 H HG   . LEU A 1 126 ? -46.52000 30.51600 12.77200  1.000 70.69000  ? 126 LEU A HG   1 
ATOM   1981 H HD11 . LEU A 1 126 ? -44.22100 30.73600 12.89400  1.000 92.74000  ? 126 LEU A HD11 1 
ATOM   1982 H HD12 . LEU A 1 126 ? -44.75900 31.44600 11.57900  1.000 92.74000  ? 126 LEU A HD12 1 
ATOM   1983 H HD13 . LEU A 1 126 ? -44.07400 30.01500 11.48500  1.000 92.74000  ? 126 LEU A HD13 1 
ATOM   1984 H HD21 . LEU A 1 126 ? -46.83300 30.52400 10.43500  1.000 80.87000  ? 126 LEU A HD21 1 
ATOM   1985 H HD22 . LEU A 1 126 ? -46.12200 29.10700 10.33500  1.000 80.87000  ? 126 LEU A HD22 1 
ATOM   1986 H HD23 . LEU A 1 126 ? -47.52700 29.24100 11.06400  1.000 80.87000  ? 126 LEU A HD23 1 
ATOM   1987 N N    . THR A 1 127 ? -45.89300 26.13700 14.48500  1.000 45.88708  ? 127 THR A N    1 
ATOM   1988 C CA   . THR A 1 127 ? -46.50300 25.00900 15.19100  1.000 51.60092  ? 127 THR A CA   1 
ATOM   1989 C C    . THR A 1 127 ? -46.05300 24.95500 16.66300  1.000 42.20243  ? 127 THR A C    1 
ATOM   1990 O O    . THR A 1 127 ? -46.78600 24.44400 17.51500  1.000 51.71673  ? 127 THR A O    1 
ATOM   1991 C CB   . THR A 1 127 ? -46.19300 23.71800 14.40700  1.000 43.40784  ? 127 THR A CB   1 
ATOM   1992 O OG1  . THR A 1 127 ? -46.97500 23.68200 13.18800  1.000 57.20423  ? 127 THR A OG1  1 
ATOM   1993 C CG2  . THR A 1 127 ? -46.46800 22.46200 15.20500  1.000 55.12503  ? 127 THR A CG2  1 
ATOM   1994 H H    . THR A 1 127 ? -45.59200 25.93500 13.70500  1.000 55.69000  ? 127 THR A H    1 
ATOM   1995 H HA   . THR A 1 127 ? -47.46600 25.12800 15.18600  1.000 62.55000  ? 127 THR A HA   1 
ATOM   1996 H HB   . THR A 1 127 ? -45.25200 23.71700 14.17200  1.000 52.71000  ? 127 THR A HB   1 
ATOM   1997 H HG1  . THR A 1 127 ? -46.80700 22.97900 12.76000  1.000 69.27000  ? 127 THR A HG1  1 
ATOM   1998 H HG21 . THR A 1 127 ? -45.79000 22.34500 15.88900  1.000 66.78000  ? 127 THR A HG21 1 
ATOM   1999 H HG22 . THR A 1 127 ? -46.46000 21.68900 14.61900  1.000 66.78000  ? 127 THR A HG22 1 
ATOM   2000 H HG23 . THR A 1 127 ? -47.33800 22.52600 15.62900  1.000 66.78000  ? 127 THR A HG23 1 
ATOM   2001 N N    . CYS A 1 128 ? -44.89500 25.53600 16.99800  1.000 62.62593  ? 128 CYS A N    1 
ATOM   2002 C CA   . CYS A 1 128 ? -44.38800 25.51400 18.37500  1.000 56.83576  ? 128 CYS A CA   1 
ATOM   2003 C C    . CYS A 1 128 ? -43.86400 26.88900 18.83800  1.000 49.51120  ? 128 CYS A C    1 
ATOM   2004 O O    . CYS A 1 128 ? -44.47000 27.54400 19.67000  1.000 62.16535  ? 128 CYS A O    1 
ATOM   2005 C CB   . CYS A 1 128 ? -43.24800 24.48400 18.50500  1.000 51.48249  ? 128 CYS A CB   1 
ATOM   2006 S SG   . CYS A 1 128 ? -43.45800 22.85000 17.61700  1.000 47.64519  ? 128 CYS A SG   1 
ATOM   2007 H H    . CYS A 1 128 ? -44.37800 25.94400 16.44600  1.000 75.78000  ? 128 CYS A H    1 
ATOM   2008 H HA   . CYS A 1 128 ? -45.10200 25.24900 18.97600  1.000 68.83000  ? 128 CYS A HA   1 
ATOM   2009 H HB2  . CYS A 1 128 ? -42.43600 24.89000 18.16400  1.000 62.41000  ? 128 CYS A HB2  1 
ATOM   2010 H HB3  . CYS A 1 128 ? -43.13100 24.28300 19.44700  1.000 62.41000  ? 128 CYS A HB3  1 
HETATM 2011 C C1   . PEG B 2 .   ? -5.24700  35.58200 -28.25100 1.000 57.60000  ? 201 PEG A C1   1 
HETATM 2012 O O1   . PEG B 2 .   ? -5.62900  36.94700 -28.03200 1.000 58.61000  ? 201 PEG A O1   1 
HETATM 2013 C C2   . PEG B 2 .   ? -5.14600  34.74500 -26.98200 1.000 57.52000  ? 201 PEG A C2   1 
HETATM 2014 O O2   . PEG B 2 .   ? -4.75600  33.40000 -27.31200 1.000 77.76000  ? 201 PEG A O2   1 
HETATM 2015 C C3   . PEG B 2 .   ? -3.55500  32.98400 -26.66100 1.000 69.13000  ? 201 PEG A C3   1 
HETATM 2016 C C4   . PEG B 2 .   ? -2.93900  31.78800 -27.33800 1.000 56.43000  ? 201 PEG A C4   1 
HETATM 2017 O O4   . PEG B 2 .   ? -1.52600  31.89600 -27.32100 1.000 65.29000  ? 201 PEG A O4   1 
HETATM 2018 H H11  . PEG B 2 .   ? -4.38700  35.57700 -28.68400 1.000 69.74000  ? 201 PEG A H11  1 
HETATM 2019 H H12  . PEG B 2 .   ? -5.88500  35.16600 -28.84300 1.000 69.74000  ? 201 PEG A H12  1 
HETATM 2020 H HO1  . PEG B 2 .   ? -6.16600  37.05600 -27.38200 1.000 70.96000  ? 201 PEG A HO1  1 
HETATM 2021 H H21  . PEG B 2 .   ? -6.01200  34.72600 -26.54500 1.000 69.65000  ? 201 PEG A H21  1 
HETATM 2022 H H22  . PEG B 2 .   ? -4.50100  35.14700 -26.38600 1.000 69.65000  ? 201 PEG A H22  1 
HETATM 2023 H H31  . PEG B 2 .   ? -3.73400  32.78300 -25.72900 1.000 83.58000  ? 201 PEG A H31  1 
HETATM 2024 H H32  . PEG B 2 .   ? -2.90800  33.69700 -26.72800 1.000 83.58000  ? 201 PEG A H32  1 
HETATM 2025 H H41  . PEG B 2 .   ? -3.25100  31.73500 -28.25300 1.000 68.34000  ? 201 PEG A H41  1 
HETATM 2026 H H42  . PEG B 2 .   ? -3.20300  30.98300 -26.86500 1.000 68.34000  ? 201 PEG A H42  1 
HETATM 2027 H HO4  . PEG B 2 .   ? -1.12300  31.19800 -27.59100 1.000 78.97000  ? 201 PEG A HO4  1 
HETATM 2028 O O    . HOH C 3 .   ? -31.12600 21.41700 -10.11400 1.000 38.48000  ? 301 HOH A O    1 
HETATM 2029 O O    . HOH C 3 .   ? -38.34300 28.64500 2.19200   1.000 46.38000  ? 302 HOH A O    1 
HETATM 2030 O O    . HOH C 3 .   ? -37.70700 26.19700 -4.20500  1.000 31.02000  ? 303 HOH A O    1 
HETATM 2031 O O    . HOH C 3 .   ? -24.88500 26.36200 -4.28200  1.000 45.06000  ? 304 HOH A O    1 
HETATM 2032 O O    . HOH C 3 .   ? -39.38300 9.88700  4.89400   1.000 41.73000  ? 305 HOH A O    1 
HETATM 2033 O O    . HOH C 3 .   ? -6.45100  31.37200 -27.82000 1.000 50.92000  ? 306 HOH A O    1 
HETATM 2034 O O    . HOH C 3 .   ? -6.783    36.447   -17.675   1.000 24.24000  ? 307 HOH A O    1 
HETATM 2035 O O    . HOH C 3 .   ? -30.96700 16.53300 -3.65300  1.000 20.55000  ? 308 HOH A O    1 
HETATM 2036 O O    . HOH C 3 .   ? -38.32500 17.90000 18.42200  1.000 31.88000  ? 309 HOH A O    1 
HETATM 2037 O O    . HOH C 3 .   ? -13.95400 23.59900 -11.22000 1.000 39.18000  ? 310 HOH A O    1 
HETATM 2038 O O    . HOH C 3 .   ? -36.73500 10.12800 3.74200   1.000 39.62000  ? 311 HOH A O    1 
HETATM 2039 O O    . HOH C 3 .   ? -16.62300 23.70500 3.08700   1.000 52.55000  ? 312 HOH A O    1 
HETATM 2040 O O    . HOH C 3 .   ? -22.40200 28.19800 -4.00900  1.000 52.19000  ? 313 HOH A O    1 
HETATM 2041 O O    . HOH C 3 .   ? -5.36900  35.07500 -24.10800 1.000 42.79000  ? 314 HOH A O    1 
HETATM 2042 O O    . HOH C 3 .   ? -46.25900 18.93300 4.52500   1.000 32.85000  ? 315 HOH A O    1 
HETATM 2043 O O    . HOH C 3 .   ? -40.482   29.710   4.538     1.000 28.17000  ? 316 HOH A O    1 
HETATM 2044 O O    . HOH C 3 .   ? -41.638   15.132   -0.233    0.500 36.87000  ? 317 HOH A O    1 
HETATM 2045 O O    . HOH C 3 .   ? -18.26500 30.98900 -6.85800  1.000 48.99000  ? 318 HOH A O    1 
HETATM 2046 O O    . HOH C 3 .   ? -0.344    31.651   -30.111   1.000 43.11000  ? 319 HOH A O    1 
HETATM 2047 O O    . HOH C 3 .   ? -31.63700 29.13700 -7.47300  1.000 60.39000  ? 320 HOH A O    1 
HETATM 2048 O O    . HOH C 3 .   ? -17.52300 15.48100 -2.97900  1.000 57.97000  ? 321 HOH A O    1 
HETATM 2049 O O    . HOH C 3 .   ? -31.48700 9.18100  -5.72300  1.000 40.44000  ? 322 HOH A O    1 
HETATM 2050 O O    . HOH C 3 .   ? -44.43400 17.74900 -0.62600  1.000 42.46000  ? 323 HOH A O    1 
HETATM 2051 O O    . HOH C 3 .   ? -29.16400 24.04800 -14.18600 1.000 32.78000  ? 324 HOH A O    1 
HETATM 2052 O O    . HOH C 3 .   ? -35.845   23.573   -9.725    1.000 39.01000  ? 325 HOH A O    1 
HETATM 2053 O O    . HOH C 3 .   ? 3.55600   31.45400 -20.44800 1.000 48.93000  ? 326 HOH A O    1 
HETATM 2054 O O    . HOH C 3 .   ? -29.39500 14.95700 10.42000  1.000 42.45000  ? 327 HOH A O    1 
HETATM 2055 O O    . HOH C 3 .   ? -44.05500 16.73700 21.53600  1.000 51.60000  ? 328 HOH A O    1 
HETATM 2056 O O    . HOH C 3 .   ? -34.13700 29.91600 -8.29400  1.000 47.85000  ? 329 HOH A O    1 
HETATM 2057 O O    . HOH C 3 .   ? -1.70700  24.36100 -16.90100 1.000 66.51000  ? 330 HOH A O    1 
HETATM 2058 O O    . HOH C 3 .   ? -32.55100 11.35000 -4.87400  1.000 46.99000  ? 331 HOH A O    1 
HETATM 2059 O O    . HOH C 3 .   ? -45.629   14.275   0.846     1.000 61.45000  ? 332 HOH A O    1 
HETATM 2060 O O    . HOH C 3 .   ? -43.743   8.924    11.765    1.000 58.63000  ? 333 HOH A O    1 
HETATM 2061 O O    . HOH C 3 .   ? -29.96700 12.97700 11.31000  1.000 47.91000  ? 334 HOH A O    1 
HETATM 2062 O O    . HOH C 3 .   ? -36.25800 30.69800 1.77200   1.000 44.28000  ? 335 HOH A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . CYS A 3   ? 1.28710 2.22750 1.95280 -0.12490 0.56340  0.19660  3   CYS A N   
2    C CA  . CYS A 3   ? 1.63490 2.46450 2.22290 -0.12640 0.58410  0.17680  3   CYS A CA  
3    C C   . CYS A 3   ? 1.68430 2.56260 2.22180 -0.10340 0.58540  0.17320  3   CYS A C   
4    O O   . CYS A 3   ? 1.41630 2.38980 1.96720 -0.10510 0.59610  0.16490  3   CYS A O   
5    C CB  . CYS A 3   ? 1.55720 2.36840 2.09310 -0.15070 0.60320  0.19080  3   CYS A CB  
6    S SG  . CYS A 3   ? 1.62860 2.34460 2.05520 -0.16210 0.59800  0.17590  3   CYS A SG  
10   N N   . GLY A 4   ? 1.44190 2.24100 1.92390 -0.09430 0.58380  0.15630  4   GLY A N   
11   C CA  . GLY A 4   ? 1.06260 1.88440 1.49650 -0.07390 0.58920  0.14450  4   GLY A CA  
12   C C   . GLY A 4   ? 1.49300 2.22620 1.86790 -0.06880 0.57920  0.12830  4   GLY A C   
13   O O   . GLY A 4   ? 1.43550 2.11500 1.74850 -0.08740 0.58040  0.12900  4   GLY A O   
17   N N   . ALA A 5   ? 1.56440 2.29470 1.95190 -0.04780 0.56540  0.11320  5   ALA A N   
18   C CA  . ALA A 5   ? 1.65300 2.31500 1.98460 -0.04720 0.55190  0.09200  5   ALA A CA  
19   C C   . ALA A 5   ? 1.67790 2.33460 2.06300 -0.03670 0.53120  0.07140  5   ALA A C   
20   O O   . ALA A 5   ? 1.65590 2.35860 2.11470 -0.02190 0.53110  0.07970  5   ALA A O   
21   C CB  . ALA A 5   ? 1.40450 2.06850 1.66040 -0.03330 0.56650  0.09030  5   ALA A CB  
27   N N   . ALA A 6   ? 1.42380 2.04370 1.77080 -0.04110 0.50820  0.05200  6   ALA A N   
28   C CA  . ALA A 6   ? 1.22950 1.85460 1.62000 -0.03400 0.48180  0.03090  6   ALA A CA  
29   C C   . ALA A 6   ? 1.23130 1.86650 1.64350 -0.00180 0.49700  0.03050  6   ALA A C   
30   O O   . ALA A 6   ? 1.37200 2.02670 1.73310 0.01880  0.51570  0.04830  6   ALA A O   
31   C CB  . ALA A 6   ? 0.80990 1.41060 1.14580 -0.03780 0.45190  0.02740  6   ALA A CB  
37   N N   . SER A 7   ? 1.18890 1.83450 1.66430 0.00340  0.48080  0.01020  7   SER A N   
38   C CA  . SER A 7   ? 1.13690 1.82420 1.62190 0.05360  0.48000  0.04030  7   SER A CA  
39   C C   . SER A 7   ? 1.11520 1.74630 1.58440 0.04860  0.46780  0.00250  7   SER A C   
40   O O   . SER A 7   ? 1.16860 1.78190 1.60910 0.02610  0.44210  -0.01680 7   SER A O   
41   C CB  . SER A 7   ? 0.85490 1.75900 1.36060 0.04110  0.41650  -0.00180 7   SER A CB  
42   O OG  . SER A 7   ? 0.84430 1.67130 1.41910 0.00240  0.40560  -0.08720 7   SER A OG  
48   N N   . MET A 8   ? 1.04160 1.76620 1.48340 0.09760  0.44730  0.02560  8   MET A N   
49   C CA  . MET A 8   ? 0.99320 1.64750 1.42000 0.10530  0.44550  0.00920  8   MET A CA  
50   C C   . MET A 8   ? 1.14510 1.75340 1.65370 0.07020  0.42620  -0.04600 8   MET A C   
51   O O   . MET A 8   ? 1.19650 1.78980 1.67340 0.07100  0.40150  -0.05110 8   MET A O   
52   C CB  . MET A 8   ? 0.93580 1.66840 1.33290 0.12840  0.44310  -0.01990 8   MET A CB  
53   C CG  . MET A 8   ? 1.28580 1.98780 1.62020 0.12540  0.47690  -0.02930 8   MET A CG  
54   S SD  . MET A 8   ? 1.70420 2.30220 1.96190 0.10930  0.47780  -0.02540 8   MET A SD  
55   C CE  . MET A 8   ? 1.13360 1.69890 1.38700 0.12550  0.45870  -0.04280 8   MET A CE  
65   N N   . THR A 9   ? 1.07650 1.82840 1.62040 0.04900  0.37900  -0.10610 9   THR A N   
66   C CA  . THR A 9   ? 1.04150 1.77840 1.63380 0.05960  0.35050  -0.09630 9   THR A CA  
67   C C   . THR A 9   ? 0.98950 1.67710 1.58000 0.04810  0.33900  -0.06210 9   THR A C   
68   O O   . THR A 9   ? 0.83230 1.51000 1.42550 0.05620  0.30770  -0.05320 9   THR A O   
69   C CB  . THR A 9   ? 0.87520 1.71060 1.51020 0.07930  0.33210  -0.08960 9   THR A CB  
70   O OG1 . THR A 9   ? 0.85800 1.73250 1.49350 0.11830  0.34310  -0.07820 9   THR A OG1 
71   C CG2 . THR A 9   ? 0.81720 1.63480 1.49720 0.08110  0.29980  -0.08410 9   THR A CG2 
79   N N   . LYS A 10  ? 0.94270 1.62450 1.51490 0.03040  0.35550  -0.04680 10  LYS A N   
80   C CA  . LYS A 10  ? 0.89660 1.56630 1.44160 0.01890  0.33520  -0.02350 10  LYS A CA  
81   C C   . LYS A 10  ? 0.84880 1.48040 1.32180 0.02130  0.33420  -0.01500 10  LYS A C   
82   O O   . LYS A 10  ? 0.73540 1.35610 1.18600 0.02110  0.30250  -0.00510 10  LYS A O   
83   C CB  . LYS A 10  ? 0.93630 1.61910 1.48300 -0.00190 0.35100  -0.01350 10  LYS A CB  
84   C CG  . LYS A 10  ? 1.04920 1.77290 1.65830 -0.01020 0.33380  -0.01450 10  LYS A CG  
85   C CD  . LYS A 10  ? 1.13830 1.85980 1.73220 -0.03090 0.32620  0.00590  10  LYS A CD  
86   C CE  . LYS A 10  ? 1.19350 1.92530 1.79160 -0.04860 0.35900  0.00760  10  LYS A CE  
87   N NZ  . LYS A 10  ? 0.88580 1.61690 1.47340 -0.06940 0.35000  0.02650  10  LYS A NZ  
101  N N   . THR A 11  ? 0.66800 1.27740 1.09640 0.02410  0.36460  -0.01900 11  THR A N   
102  C CA  . THR A 11  ? 0.59430 1.17180 0.94810 0.02530  0.36270  -0.01600 11  THR A CA  
103  C C   . THR A 11  ? 0.67720 1.24230 1.02680 0.04060  0.33710  -0.02290 11  THR A C   
104  O O   . THR A 11  ? 0.78450 1.32910 1.08050 0.03810  0.31380  -0.01780 11  THR A O   
105  C CB  . THR A 11  ? 0.66090 1.21720 0.96750 0.02900  0.39850  -0.02010 11  THR A CB  
106  O OG1 . THR A 11  ? 0.69960 1.26050 0.99350 0.01320  0.41750  -0.00860 11  THR A OG1 
107  C CG2 . THR A 11  ? 0.90090 1.42440 1.13150 0.03240  0.39350  -0.02430 11  THR A CG2 
115  N N   . VAL A 12  ? 0.90980 1.48470 1.31240 0.05620  0.33780  -0.03430 12  VAL A N   
116  C CA  . VAL A 12  ? 0.95150 1.51460 1.35680 0.07080  0.31500  -0.03960 12  VAL A CA  
117  C C   . VAL A 12  ? 0.77600 1.35100 1.20790 0.06770  0.27510  -0.02850 12  VAL A C   
118  O O   . VAL A 12  ? 0.76710 1.32360 1.16990 0.07140  0.24840  -0.02330 12  VAL A O   
119  C CB  . VAL A 12  ? 0.73430 1.29540 1.17630 0.08930  0.32720  -0.05490 12  VAL A CB  
120  C CG1 . VAL A 12  ? 0.66970 1.21000 1.07330 0.09750  0.36610  -0.05860 12  VAL A CG1 
121  C CG2 . VAL A 12  ? 0.76930 1.36780 1.28610 0.08830  0.31940  -0.06380 12  VAL A CG2 
131  N N   . GLN A 13  ? 0.75140 1.35560 1.23520 0.06070  0.26990  -0.02510 13  GLN A N   
132  C CA  . GLN A 13  ? 0.87930 1.48870 1.37610 0.05650  0.23210  -0.01190 13  GLN A CA  
133  C C   . GLN A 13  ? 0.77770 1.36440 1.21140 0.04520  0.21360  0.00430  13  GLN A C   
134  O O   . GLN A 13  ? 0.53700 1.10740 0.95280 0.04860  0.18420  0.01110  13  GLN A O   
135  C CB  . GLN A 13  ? 0.99990 1.64430 1.55000 0.04720  0.23300  -0.01110 13  GLN A CB  
136  C CG  . GLN A 13  ? 1.16040 1.80800 1.72090 0.04180  0.19580  0.00270  13  GLN A CG  
137  C CD  . GLN A 13  ? 1.09110 1.77810 1.71090 0.03600  0.19490  -0.00080 13  GLN A CD  
138  O OE1 . GLN A 13  ? 0.89050 1.60710 1.54760 0.03850  0.21870  -0.01580 13  GLN A OE1 
139  N NE2 . GLN A 13  ? 1.02270 1.71030 1.64540 0.02820  0.16600  0.01230  13  GLN A NE2 
148  N N   . ALA A 14  ? 0.54110 1.12560 0.93880 0.03150  0.23130  0.00930  14  ALA A N   
149  C CA  . ALA A 14  ? 0.66420 1.23120 1.00470 0.02010  0.21330  0.02270  14  ALA A CA  
150  C C   . ALA A 14  ? 0.49160 1.03300 0.77890 0.02740  0.20620  0.01790  14  ALA A C   
151  O O   . ALA A 14  ? 0.48470 1.01340 0.74420 0.02530  0.17900  0.02620  14  ALA A O   
152  C CB  . ALA A 14  ? 0.71640 1.28670 1.03340 0.00320  0.23400  0.02900  14  ALA A CB  
158  N N   . ARG A 15  ? 0.54340 1.07610 0.81450 0.03540  0.23090  0.00360  15  ARG A N   
159  C CA  . ARG A 15  ? 0.35620 0.86590 0.58210 0.04300  0.22210  -0.00380 15  ARG A CA  
160  C C   . ARG A 15  ? 0.45700 0.96380 0.70780 0.05420  0.19510  -0.00300 15  ARG A C   
161  O O   . ARG A 15  ? 0.56520 1.05860 0.78480 0.05290  0.17130  0.00190  15  ARG A O   
162  C CB  . ARG A 15  ? 0.50990 1.00820 0.71910 0.05160  0.25280  -0.02140 15  ARG A CB  
163  C CG  . ARG A 15  ? 0.68210 1.15720 0.85550 0.06210  0.24300  -0.03340 15  ARG A CG  
164  C CD  . ARG A 15  ? 0.97840 1.43550 1.08610 0.05240  0.22250  -0.02950 15  ARG A CD  
165  N NE  . ARG A 15  ? 0.93640 1.37780 1.02690 0.06190  0.20760  -0.04000 15  ARG A NE  
166  C CZ  . ARG A 15  ? 0.76730 1.18650 0.81060 0.06370  0.21490  -0.05520 15  ARG A CZ  
167  N NH1 . ARG A 15  ? 0.68670 1.09180 0.68320 0.05540  0.23290  -0.05980 15  ARG A NH1 
168  N NH2 . ARG A 15  ? 0.75640 1.16410 0.79740 0.07330  0.20330  -0.06630 15  ARG A NH2 
182  N N   . GLN A 16  ? 0.56400 1.08230 0.87210 0.06470  0.19810  -0.00750 16  GLN A N   
183  C CA  . GLN A 16  ? 0.53010 1.04100 0.85970 0.07470  0.17250  -0.00570 16  GLN A CA  
184  C C   . GLN A 16  ? 0.43150 0.93940 0.75280 0.06500  0.14130  0.01060  16  GLN A C   
185  O O   . GLN A 16  ? 0.38260 0.87310 0.68840 0.06850  0.11930  0.01360  16  GLN A O   
186  C CB  . GLN A 16  ? 0.37540 0.90060 0.76950 0.08660  0.18000  -0.01350 16  GLN A CB  
187  C CG  . GLN A 16  ? 0.56720 1.07900 0.96410 0.10310  0.19430  -0.02900 16  GLN A CG  
188  C CD  . GLN A 16  ? 0.82160 1.35100 1.27900 0.11440  0.21490  -0.04230 16  GLN A CD  
189  O OE1 . GLN A 16  ? 0.77700 1.32470 1.28420 0.11790  0.19890  -0.04230 16  GLN A OE1 
190  N NE2 . GLN A 16  ? 0.70690 1.22910 1.15240 0.12030  0.24750  -0.05520 16  GLN A NE2 
199  N N   . LYS A 17  ? 0.32530 0.84710 0.65330 0.05210  0.14070  0.02060  17  LYS A N   
200  C CA  . LYS A 17  ? 0.32600 0.84040 0.63890 0.04220  0.11340  0.03520  17  LYS A CA  
201  C C   . LYS A 17  ? 0.50610 1.00220 0.76130 0.03740  0.10310  0.03910  17  LYS A C   
202  O O   . LYS A 17  ? 0.37020 0.84940 0.61020 0.03830  0.08010  0.04410  17  LYS A O   
203  C CB  . LYS A 17  ? 0.55060 1.08320 0.87980 0.02860  0.11780  0.04400  17  LYS A CB  
204  C CG  . LYS A 17  ? 0.61160 1.13570 0.93280 0.01940  0.09010  0.05760  17  LYS A CG  
205  C CD  . LYS A 17  ? 0.59400 1.13560 0.96600 0.01690  0.08410  0.05970  17  LYS A CD  
206  C CE  . LYS A 17  ? 0.75010 1.27700 1.10850 0.00890  0.05650  0.07100  17  LYS A CE  
207  N NZ  . LYS A 17  ? 0.77370 1.29100 1.08760 -0.00420 0.05420  0.08150  17  LYS A NZ  
221  N N   . LEU A 18  ? 0.48010 0.97820 0.70160 0.03150  0.12000  0.03650  18  LEU A N   
222  C CA  . LEU A 18  ? 0.37780 0.86080 0.54690 0.02870  0.11020  0.03700  18  LEU A CA  
223  C C   . LEU A 18  ? 0.29470 0.76380 0.45850 0.04110  0.10000  0.02780  18  LEU A C   
224  O O   . LEU A 18  ? 0.33420 0.79140 0.47400 0.03980  0.08020  0.03170  18  LEU A O   
225  C CB  . LEU A 18  ? 0.34290 0.82440 0.47530 0.02300  0.13230  0.03110  18  LEU A CB  
226  C CG  . LEU A 18  ? 0.36660 0.85530 0.49150 0.00820  0.14310  0.04120  18  LEU A CG  
227  C CD1 . LEU A 18  ? 0.40680 0.88450 0.48930 0.00320  0.16650  0.03410  18  LEU A CD1 
228  C CD2 . LEU A 18  ? 0.38500 0.86820 0.49030 -0.00130 0.11760  0.05620  18  LEU A CD2 
240  N N   . SER A 19  ? 0.30850 0.77830 0.49610 0.05300  0.11450  0.01520  19  SER A N   
241  C CA  . SER A 19  ? 0.22950 0.68440 0.40940 0.06370  0.10690  0.00570  19  SER A CA  
242  C C   . SER A 19  ? 0.24400 0.68810 0.44130 0.06560  0.08150  0.01470  19  SER A C   
243  O O   . SER A 19  ? 0.48260 0.91150 0.65970 0.06760  0.06770  0.01300  19  SER A O   
244  C CB  . SER A 19  ? 0.36800 0.82300 0.57000 0.07670  0.12920  -0.01000 19  SER A CB  
245  O OG  . SER A 19  ? 0.71310 1.15220 0.90840 0.08650  0.12100  -0.01890 19  SER A OG  
251  N N   . GLY A 20  ? 0.30200 0.75180 0.53480 0.06390  0.07550  0.02330  20  GLY A N   
252  C CA  . GLY A 20  ? 0.30540 0.73860 0.54820 0.06430  0.05240  0.03070  20  GLY A CA  
253  C C   . GLY A 20  ? 0.26130 0.67920 0.46750 0.05320  0.03450  0.04060  20  GLY A C   
254  O O   . GLY A 20  ? 0.30720 0.70210 0.50160 0.05350  0.01950  0.04210  20  GLY A O   
258  N N   . ILE A 21  ? 0.22820 0.65700 0.41560 0.04290  0.03780  0.04690  21  ILE A N   
259  C CA  . ILE A 21  ? 0.27130 0.68630 0.42360 0.03330  0.02330  0.05550  21  ILE A CA  
260  C C   . ILE A 21  ? 0.21590 0.62000 0.33670 0.03640  0.01930  0.04910  21  ILE A C   
261  O O   . ILE A 21  ? 0.32650 0.70670 0.42980 0.03370  0.00620  0.05140  21  ILE A O   
262  C CB  . ILE A 21  ? 0.22290 0.65540 0.36390 0.02260  0.02940  0.06360  21  ILE A CB  
263  C CG1 . ILE A 21  ? 0.27420 0.71620 0.44720 0.01730  0.03020  0.07030  21  ILE A CG1 
264  C CG2 . ILE A 21  ? 0.28370 0.70440 0.38710 0.01470  0.01650  0.07100  21  ILE A CG2 
265  C CD1 . ILE A 21  ? 0.33520 0.79600 0.50290 0.00620  0.04100  0.07700  21  ILE A CD1 
277  N N   . VAL A 22  ? 0.22880 0.64820 0.34010 0.04070  0.03260  0.03960  22  VAL A N   
278  C CA  . VAL A 22  ? 0.18490 0.59820 0.27060 0.04430  0.02840  0.03050  22  VAL A CA  
279  C C   . VAL A 22  ? 0.19050 0.58130 0.28790 0.05040  0.01830  0.02710  22  VAL A C   
280  O O   . VAL A 22  ? 0.26520 0.63850 0.34340 0.04780  0.00680  0.02660  22  VAL A O   
281  C CB  . VAL A 22  ? 0.17910 0.60480 0.25540 0.04950  0.04770  0.01590  22  VAL A CB  
282  C CG1 . VAL A 22  ? 0.20790 0.62680 0.26140 0.05360  0.04230  0.00350  22  VAL A CG1 
283  C CG2 . VAL A 22  ? 0.19850 0.63440 0.25140 0.04030  0.05810  0.01950  22  VAL A CG2 
293  N N   . GLN A 23  ? 0.29920 0.68850 0.42940 0.05810  0.02410  0.02440  23  GLN A N   
294  C CA  . GLN A 23  ? 0.30620 0.67470 0.44870 0.06360  0.01530  0.02230  23  GLN A CA  
295  C C   . GLN A 23  ? 0.30870 0.65200 0.44360 0.05480  -0.00070 0.03290  23  GLN A C   
296  O O   . GLN A 23  ? 0.24680 0.56800 0.37120 0.05380  -0.00890 0.03150  23  GLN A O   
297  C CB  . GLN A 23  ? 0.32980 0.70500 0.51240 0.07450  0.02460  0.01840  23  GLN A CB  
298  C CG  . GLN A 23  ? 0.78340 1.16010 0.97140 0.08690  0.03650  0.00340  23  GLN A CG  
299  C CD  . GLN A 23  ? 1.13030 1.48620 1.31130 0.08940  0.02420  0.00130  23  GLN A CD  
300  O OE1 . GLN A 23  ? 0.99230 1.33370 1.19180 0.09110  0.01390  0.00870  23  GLN A OE1 
301  N NE2 . GLN A 23  ? 1.04880 1.40470 1.20310 0.08880  0.02490  -0.00940 23  GLN A NE2 
310  N N   . LYS A 24  ? 0.28790 0.63310 0.42830 0.04820  -0.00330 0.04200  24  LYS A N   
311  C CA  . LYS A 24  ? 0.31750 0.63620 0.44780 0.04020  -0.01550 0.04860  24  LYS A CA  
312  C C   . LYS A 24  ? 0.22820 0.52960 0.32420 0.03300  -0.01810 0.04820  24  LYS A C   
313  O O   . LYS A 24  ? 0.27420 0.54830 0.36090 0.02980  -0.02430 0.04720  24  LYS A O   
314  C CB  . LYS A 24  ? 0.41090 0.73740 0.55360 0.03450  -0.01760 0.05660  24  LYS A CB  
315  C CG  . LYS A 24  ? 0.81610 1.16030 0.99920 0.04120  -0.01580 0.05610  24  LYS A CG  
316  C CD  . LYS A 24  ? 0.96220 1.32520 1.16110 0.03500  -0.01440 0.06260  24  LYS A CD  
317  C CE  . LYS A 24  ? 0.73180 1.11500 0.97740 0.04270  -0.01190 0.05980  24  LYS A CE  
318  N NZ  . LYS A 24  ? 0.92180 1.31790 1.18510 0.03530  -0.01660 0.06600  24  LYS A NZ  
332  N N   . GLN A 25  ? 0.25520 0.57330 0.33430 0.03040  -0.01260 0.04860  25  GLN A N   
333  C CA  . GLN A 25  ? 0.15120 0.45360 0.20400 0.02440  -0.01430 0.04750  25  GLN A CA  
334  C C   . GLN A 25  ? 0.17880 0.46680 0.22690 0.02840  -0.01660 0.03810  25  GLN A C   
335  O O   . GLN A 25  ? 0.26700 0.53040 0.30480 0.02390  -0.01970 0.03590  25  GLN A O   
336  C CB  . GLN A 25  ? 0.20920 0.53710 0.24630 0.02210  -0.00900 0.04950  25  GLN A CB  
337  C CG  . GLN A 25  ? 0.25150 0.59730 0.29090 0.01580  -0.00670 0.06080  25  GLN A CG  
338  C CD  . GLN A 25  ? 0.15300 0.51940 0.17340 0.01050  -0.00270 0.06470  25  GLN A CD  
339  O OE1 . GLN A 25  ? 0.20850 0.59970 0.21870 0.01470  0.00120  0.05870  25  GLN A OE1 
340  N NE2 . GLN A 25  ? 0.28090 0.64090 0.30010 0.00080  -0.00340 0.07400  25  GLN A NE2 
349  N N   . ASN A 26  ? 0.24590 0.55180 0.30420 0.03710  -0.01390 0.03130  26  ASN A N   
350  C CA  . ASN A 26  ? 0.16410 0.46070 0.21830 0.04030  -0.01660 0.02180  26  ASN A CA  
351  C C   . ASN A 26  ? 0.18130 0.45130 0.24690 0.03940  -0.02240 0.02400  26  ASN A C   
352  O O   . ASN A 26  ? 0.32660 0.57850 0.38450 0.03610  -0.02620 0.02080  26  ASN A O   
353  C CB  . ASN A 26  ? 0.16990 0.49450 0.23350 0.05070  -0.01080 0.01090  26  ASN A CB  
354  C CG  . ASN A 26  ? 0.22220 0.57720 0.27050 0.05140  -0.00500 0.00600  26  ASN A CG  
355  O OD1 . ASN A 26  ? 0.27310 0.62720 0.30050 0.04370  -0.00790 0.01150  26  ASN A OD1 
356  N ND2 . ASN A 26  ? 0.31390 0.69210 0.37220 0.06050  0.00710  -0.00590 26  ASN A ND2 
363  N N   . ASN A 27  ? 0.31040 0.57920 0.39500 0.04190  -0.02380 0.02970  27  ASN A N   
364  C CA  . ASN A 27  ? 0.30200 0.54830 0.39340 0.04040  -0.03090 0.03280  27  ASN A CA  
365  C C   . ASN A 27  ? 0.27190 0.50010 0.34450 0.03120  -0.03340 0.03700  27  ASN A C   
366  O O   . ASN A 27  ? 0.36100 0.57570 0.42770 0.02920  -0.03600 0.03620  27  ASN A O   
367  C CB  . ASN A 27  ? 0.42360 0.67610 0.53970 0.04560  -0.03340 0.03760  27  ASN A CB  
368  C CG  . ASN A 27  ? 0.42350 0.69530 0.56490 0.05810  -0.02810 0.03300  27  ASN A CG  
369  O OD1 . ASN A 27  ? 0.59210 0.86530 0.73320 0.06320  -0.02580 0.02630  27  ASN A OD1 
370  N ND2 . ASN A 27  ? 0.65420 0.94200 0.82030 0.06360  -0.02490 0.03500  27  ASN A ND2 
377  N N   . LEU A 28  ? 0.29240 0.52640 0.35690 0.02620  -0.03080 0.04210  28  LEU A N   
378  C CA  . LEU A 28  ? 0.20620 0.42940 0.25710 0.01890  -0.03090 0.04600  28  LEU A CA  
379  C C   . LEU A 28  ? 0.23650 0.45190 0.27570 0.01750  -0.02890 0.03990  28  LEU A C   
380  O O   . LEU A 28  ? 0.24740 0.45160 0.28200 0.01430  -0.02990 0.04030  28  LEU A O   
381  C CB  . LEU A 28  ? 0.25680 0.48830 0.30410 0.01380  -0.02850 0.05180  28  LEU A CB  
382  C CG  . LEU A 28  ? 0.30810 0.54470 0.36780 0.01260  -0.03280 0.05900  28  LEU A CG  
383  C CD1 . LEU A 28  ? 0.40900 0.65550 0.46650 0.00690  -0.03060 0.06440  28  LEU A CD1 
384  C CD2 . LEU A 28  ? 0.34460 0.56720 0.40270 0.00950  -0.03810 0.06190  28  LEU A CD2 
396  N N   . LEU A 29  ? 0.22920 0.45190 0.26480 0.01990  -0.02670 0.03400  29  LEU A N   
397  C CA  . LEU A 29  ? 0.19820 0.41530 0.22600 0.01880  -0.02680 0.02800  29  LEU A CA  
398  C C   . LEU A 29  ? 0.20360 0.41110 0.23640 0.02020  -0.03020 0.02390  29  LEU A C   
399  O O   . LEU A 29  ? 0.26690 0.46660 0.29660 0.01760  -0.03120 0.02210  29  LEU A O   
400  C CB  . LEU A 29  ? 0.23810 0.46610 0.26160 0.02120  -0.02590 0.02210  29  LEU A CB  
401  C CG  . LEU A 29  ? 0.22950 0.45340 0.24780 0.02080  -0.02880 0.01470  29  LEU A CG  
402  C CD1 . LEU A 29  ? 0.26010 0.47670 0.27410 0.01700  -0.02940 0.01810  29  LEU A CD1 
403  C CD2 . LEU A 29  ? 0.36610 0.60370 0.37780 0.02290  -0.02940 0.00890  29  LEU A CD2 
415  N N   . ARG A 30  ? 0.20960 0.41850 0.25370 0.02450  -0.03250 0.02270  30  ARG A N   
416  C CA  . ARG A 30  ? 0.26660 0.46650 0.31820 0.02520  -0.03660 0.01990  30  ARG A CA  
417  C C   . ARG A 30  ? 0.28040 0.46960 0.32980 0.02180  -0.03810 0.02630  30  ARG A C   
418  O O   . ARG A 30  ? 0.29460 0.47660 0.34430 0.01970  -0.04000 0.02450  30  ARG A O   
419  C CB  . ARG A 30  ? 0.42270 0.63310 0.49090 0.03250  -0.03810 0.01860  30  ARG A CB  
420  C CG  . ARG A 30  ? 0.55670 0.78920 0.62720 0.03820  -0.03520 0.00940  30  ARG A CG  
421  C CD  . ARG A 30  ? 0.68900 0.93840 0.78070 0.04950  -0.03300 0.00790  30  ARG A CD  
422  N NE  . ARG A 30  ? 1.02580 1.30040 1.11810 0.05670  -0.02730 -0.00380 30  ARG A NE  
423  C CZ  . ARG A 30  ? 0.66290 0.95480 0.76370 0.06360  -0.02000 -0.00410 30  ARG A CZ  
424  N NH1 . ARG A 30  ? 0.66850 0.95560 0.78280 0.06460  -0.01930 0.00700  30  ARG A NH1 
425  N NH2 . ARG A 30  ? 0.79130 1.10730 0.88790 0.06950  -0.01270 -0.01750 30  ARG A NH2 
439  N N   . LYS A 31  ? 0.33660 0.52610 0.38470 0.02080  -0.03780 0.03360  31  LYS A N   
440  C CA  . LYS A 31  ? 0.29440 0.47480 0.33810 0.01680  -0.03970 0.03910  31  LYS A CA  
441  C C   . LYS A 31  ? 0.21970 0.39700 0.25340 0.01180  -0.03610 0.03790  31  LYS A C   
442  O O   . LYS A 31  ? 0.29510 0.46530 0.32600 0.00930  -0.03710 0.03840  31  LYS A O   
443  C CB  . LYS A 31  ? 0.31490 0.49780 0.36170 0.01630  -0.04210 0.04640  31  LYS A CB  
444  C CG  . LYS A 31  ? 0.33730 0.52220 0.39820 0.02270  -0.04800 0.04870  31  LYS A CG  
445  C CD  . LYS A 31  ? 0.57180 0.76570 0.63910 0.02230  -0.04990 0.05450  31  LYS A CD  
446  C CE  . LYS A 31  ? 0.67580 0.86960 0.75680 0.02740  -0.05880 0.05930  31  LYS A CE  
447  N NZ  . LYS A 31  ? 0.63570 0.83940 0.72240 0.02450  -0.06140 0.06510  31  LYS A NZ  
461  N N   . ILE A 32  ? 0.22480 0.40800 0.25420 0.01090  -0.03250 0.03620  32  ILE A N   
462  C CA  . ILE A 32  ? 0.13560 0.31580 0.15930 0.00800  -0.03080 0.03470  32  ILE A CA  
463  C C   . ILE A 32  ? 0.15390 0.33250 0.17910 0.00930  -0.03180 0.02790  32  ILE A C   
464  O O   . ILE A 32  ? 0.23060 0.40490 0.25530 0.00750  -0.03230 0.02700  32  ILE A O   
465  C CB  . ILE A 32  ? 0.13640 0.32320 0.15680 0.00740  -0.02870 0.03560  32  ILE A CB  
466  C CG1 . ILE A 32  ? 0.23290 0.42190 0.25430 0.00440  -0.02860 0.04280  32  ILE A CG1 
467  C CG2 . ILE A 32  ? 0.17100 0.35440 0.18800 0.00590  -0.02910 0.03430  32  ILE A CG2 
468  C CD1 . ILE A 32  ? 0.23460 0.43330 0.25490 0.00370  -0.02670 0.04500  32  ILE A CD1 
480  N N   . GLU A 33  ? 0.20080 0.38400 0.22940 0.01200  -0.03310 0.02250  33  GLU A N   
481  C CA  . GLU A 33  ? 0.18120 0.36390 0.21490 0.01200  -0.03580 0.01570  33  GLU A CA  
482  C C   . GLU A 33  ? 0.18570 0.36270 0.22540 0.01020  -0.03740 0.01690  33  GLU A C   
483  O O   . GLU A 33  ? 0.26980 0.44700 0.31470 0.00810  -0.03850 0.01330  33  GLU A O   
484  C CB  . GLU A 33  ? 0.23810 0.42670 0.27630 0.01450  -0.03820 0.00940  33  GLU A CB  
485  C CG  . GLU A 33  ? 0.46050 0.65670 0.49160 0.01600  -0.03750 0.00710  33  GLU A CG  
486  C CD  . GLU A 33  ? 0.53690 0.74010 0.57060 0.01860  -0.03990 0.00010  33  GLU A CD  
487  O OE1 . GLU A 33  ? 0.63420 0.83840 0.67750 0.02020  -0.04130 -0.00200 33  GLU A OE1 
488  O OE2 . GLU A 33  ? 0.61910 0.82900 0.64560 0.01920  -0.04090 -0.00330 33  GLU A OE2 
495  N N   . ALA A 34  ? 0.19260 0.36590 0.23370 0.01110  -0.03840 0.02200  34  ALA A N   
496  C CA  . ALA A 34  ? 0.23210 0.40000 0.27740 0.00940  -0.04100 0.02430  34  ALA A CA  
497  C C   . ALA A 34  ? 0.27280 0.43780 0.31040 0.00560  -0.03890 0.02760  34  ALA A C   
498  O O   . ALA A 34  ? 0.30500 0.47670 0.34610 0.00250  -0.03850 0.02750  34  ALA A O   
499  C CB  . ALA A 34  ? 0.28240 0.44730 0.32980 0.01240  -0.04450 0.03060  34  ALA A CB  
505  N N   . ILE A 35  ? 0.22810 0.39170 0.25710 0.00490  -0.03670 0.03170  35  ILE A N   
506  C CA  . ILE A 35  ? 0.25190 0.41310 0.27520 0.00180  -0.03540 0.03320  35  ILE A CA  
507  C C   . ILE A 35  ? 0.27760 0.44410 0.30560 0.00210  -0.03400 0.02660  35  ILE A C   
508  O O   . ILE A 35  ? 0.30150 0.46960 0.33190 0.00020  -0.03380 0.02510  35  ILE A O   
509  C CB  . ILE A 35  ? 0.26810 0.42730 0.28520 0.00060  -0.03480 0.03760  35  ILE A CB  
510  C CG1 . ILE A 35  ? 0.28290 0.43720 0.29790 -0.00030 -0.03850 0.04390  35  ILE A CG1 
511  C CG2 . ILE A 35  ? 0.24530 0.40150 0.25700 -0.00170 -0.03460 0.03730  35  ILE A CG2 
512  C CD1 . ILE A 35  ? 0.34770 0.50200 0.36080 -0.00210 -0.03980 0.04780  35  ILE A CD1 
524  N N   . GLN A 36  ? 0.39280 0.56350 0.42340 0.00450  -0.03390 0.02250  36  GLN A N   
525  C CA  . GLN A 36  ? 0.24440 0.42000 0.28150 0.00530  -0.03510 0.01640  36  GLN A CA  
526  C C   . GLN A 36  ? 0.28540 0.46580 0.33650 0.00330  -0.03630 0.01130  36  GLN A C   
527  O O   . GLN A 36  ? 0.41000 0.59600 0.47180 0.00240  -0.03630 0.00750  36  GLN A O   
528  C CB  . GLN A 36  ? 0.28200 0.46110 0.31890 0.00790  -0.03700 0.01310  36  GLN A CB  
529  C CG  . GLN A 36  ? 0.41670 0.60100 0.46250 0.00910  -0.04110 0.00740  36  GLN A CG  
530  C CD  . GLN A 36  ? 0.38180 0.57050 0.42830 0.01080  -0.04530 0.00350  36  GLN A CD  
531  O OE1 . GLN A 36  ? 0.28390 0.47320 0.32620 0.01090  -0.04430 0.00310  36  GLN A OE1 
532  N NE2 . GLN A 36  ? 0.46260 0.65520 0.51540 0.01230  -0.05120 0.00040  36  GLN A NE2 
541  N N   . HIS A 37  ? 0.36240 0.54250 0.41870 0.00240  -0.03740 0.01040  37  HIS A N   
542  C CA  . HIS A 37  ? 0.30370 0.49830 0.37720 -0.00160 -0.03690 0.00600  37  HIS A CA  
543  C C   . HIS A 37  ? 0.36760 0.57540 0.44220 -0.00680 -0.03210 0.01140  37  HIS A C   
544  O O   . HIS A 37  ? 0.55980 0.78370 0.65200 -0.01250 -0.02730 0.00670  37  HIS A O   
545  C CB  . HIS A 37  ? 0.41240 0.61010 0.49170 -0.00160 -0.03920 0.00420  37  HIS A CB  
546  C CG  . HIS A 37  ? 0.51400 0.70640 0.59250 0.00160  -0.04320 -0.00120 37  HIS A CG  
547  N ND1 . HIS A 37  ? 0.54370 0.73790 0.62110 0.00400  -0.04490 -0.00230 37  HIS A ND1 
548  C CD2 . HIS A 37  ? 0.52950 0.72120 0.60730 0.00250  -0.04570 -0.00520 37  HIS A CD2 
549  C CE1 . HIS A 37  ? 0.67160 0.86540 0.74560 0.00550  -0.04760 -0.00720 37  HIS A CE1 
550  N NE2 . HIS A 37  ? 0.62390 0.81720 0.69710 0.00460  -0.04860 -0.00840 37  HIS A NE2 
558  N N   . LEU A 38  ? 0.34740 0.54970 0.40520 -0.00650 -0.03250 0.02150  38  LEU A N   
559  C CA  . LEU A 38  ? 0.38510 0.60220 0.43900 -0.01360 -0.02950 0.03000  38  LEU A CA  
560  C C   . LEU A 38  ? 0.42570 0.65410 0.48530 -0.01540 -0.02420 0.02470  38  LEU A C   
561  O O   . LEU A 38  ? 0.55950 0.80660 0.63380 -0.02420 -0.01390 0.02250  38  LEU A O   
562  C CB  . LEU A 38  ? 0.34930 0.55040 0.38000 -0.01230 -0.03380 0.04200  38  LEU A CB  
563  C CG  . LEU A 38  ? 0.45690 0.65410 0.48580 -0.01260 -0.03870 0.05090  38  LEU A CG  
564  C CD1 . LEU A 38  ? 0.37530 0.54780 0.38880 -0.00840 -0.04260 0.05630  38  LEU A CD1 
565  C CD2 . LEU A 38  ? 0.48020 0.67120 0.50200 -0.02270 -0.03080 0.05640  38  LEU A CD2 
577  N N   . LEU A 39  ? 0.42040 0.63440 0.47190 -0.00850 -0.02680 0.02160  39  LEU A N   
578  C CA  . LEU A 39  ? 0.50540 0.73070 0.56360 -0.00800 -0.02340 0.01710  39  LEU A CA  
579  C C   . LEU A 39  ? 0.49840 0.73350 0.58490 -0.00770 -0.02000 0.00570  39  LEU A C   
580  O O   . LEU A 39  ? 0.51240 0.76140 0.61420 -0.00820 -0.01320 0.00050  39  LEU A O   
581  C CB  . LEU A 39  ? 0.40100 0.60700 0.44590 -0.00190 -0.02810 0.01810  39  LEU A CB  
582  C CG  . LEU A 39  ? 0.41480 0.60410 0.43860 -0.00310 -0.03000 0.02640  39  LEU A CG  
583  C CD1 . LEU A 39  ? 0.38430 0.55860 0.40340 0.00050  -0.03270 0.02490  39  LEU A CD1 
584  C CD2 . LEU A 39  ? 0.60860 0.81040 0.61940 -0.00990 -0.02850 0.03390  39  LEU A CD2 
596  N N   . GLN A 40  ? 0.53620 0.76400 0.63200 -0.00700 -0.02410 0.00160  40  GLN A N   
597  C CA  . GLN A 40  ? 0.50690 0.74470 0.63150 -0.00900 -0.02210 -0.00740 40  GLN A CA  
598  C C   . GLN A 40  ? 0.51740 0.77190 0.66030 -0.01950 -0.00920 -0.01020 40  GLN A C   
599  O O   . GLN A 40  ? 0.89950 1.16430 1.06910 -0.02290 -0.00190 -0.01710 40  GLN A O   
600  C CB  . GLN A 40  ? 0.44690 0.67430 0.57420 -0.00670 -0.03120 -0.01010 40  GLN A CB  
601  C CG  . GLN A 40  ? 0.45190 0.66300 0.56570 0.00010  -0.03970 -0.00790 40  GLN A CG  
602  C CD  . GLN A 40  ? 0.50970 0.71810 0.61810 0.00080  -0.04560 -0.00980 40  GLN A CD  
603  O OE1 . GLN A 40  ? 0.61000 0.81930 0.72560 -0.00300 -0.04540 -0.01200 40  GLN A OE1 
604  N NE2 . GLN A 40  ? 0.54910 0.75530 0.64580 0.00520  -0.05060 -0.00910 40  GLN A NE2 
613  N N   . ARG A 41  ? 0.51270 1.24350 1.16890 -0.22280 0.07100  -0.51120 41  ARG A N   
614  C CA  . ARG A 41  ? 0.53360 1.23210 1.22430 -0.24650 0.09990  -0.51390 41  ARG A CA  
615  C C   . ARG A 41  ? 0.50940 1.20680 1.22140 -0.23360 0.11660  -0.48300 41  ARG A C   
616  O O   . ARG A 41  ? 0.57380 1.25360 1.31440 -0.25090 0.13620  -0.48180 41  ARG A O   
617  C CB  . ARG A 41  ? 0.55790 1.18510 1.22700 -0.26180 0.12280  -0.52070 41  ARG A CB  
618  C CG  . ARG A 41  ? 0.59470 1.21380 1.26340 -0.28510 0.11710  -0.55340 41  ARG A CG  
619  C CD  . ARG A 41  ? 0.99200 1.66040 1.64230 -0.27920 0.08240  -0.57450 41  ARG A CD  
620  N NE  . ARG A 41  ? 1.20680 1.84000 1.81380 -0.28070 0.07860  -0.58950 41  ARG A NE  
621  C CZ  . ARG A 41  ? 0.87240 1.53570 1.45110 -0.27270 0.05120  -0.60420 41  ARG A CZ  
622  N NH1 . ARG A 41  ? 0.88830 1.60530 1.45870 -0.25280 0.02510  -0.59550 41  ARG A NH1 
623  N NH2 . ARG A 41  ? 0.71890 1.35560 1.27440 -0.28170 0.05020  -0.62370 41  ARG A NH2 
637  N N   . GLY A 42  ? 0.47320 1.18700 1.16890 -0.20330 0.10790  -0.45750 42  GLY A N   
638  C CA  . GLY A 42  ? 0.45520 1.16580 1.16450 -0.18750 0.12110  -0.42760 42  GLY A CA  
639  C C   . GLY A 42  ? 0.47160 1.15440 1.14520 -0.15650 0.12530  -0.39590 42  GLY A C   
640  O O   . GLY A 42  ? 0.40930 1.08080 1.04440 -0.14400 0.11370  -0.39470 42  GLY A O   
644  N N   . LEU A 43  ? 0.77350 1.43820 1.45110 -0.14180 0.14010  -0.36650 43  LEU A N   
645  C CA  . LEU A 43  ? 0.84520 1.48480 1.48750 -0.10770 0.14080  -0.33200 43  LEU A CA  
646  C C   . LEU A 43  ? 0.86740 1.42430 1.47830 -0.11000 0.17010  -0.31530 43  LEU A C   
647  O O   . LEU A 43  ? 0.86880 1.38080 1.48910 -0.12620 0.19530  -0.30870 43  LEU A O   
648  C CB  . LEU A 43  ? 0.98220 1.63600 1.63830 -0.09000 0.14160  -0.30720 43  LEU A CB  
649  C CG  . LEU A 43  ? 1.18690 1.91670 1.86760 -0.08170 0.11240  -0.31700 43  LEU A CG  
650  C CD1 . LEU A 43  ? 1.61560 2.35170 2.31180 -0.06730 0.11990  -0.29220 43  LEU A CD1 
651  C CD2 . LEU A 43  ? 1.32130 2.08460 1.97270 -0.05650 0.07730  -0.31650 43  LEU A CD2 
663  N N   . ILE A 44  ? 0.67980 1.21060 1.24540 -0.09050 0.16460  -0.30340 44  ILE A N   
664  C CA  . ILE A 44  ? 0.52040 0.96480 1.04440 -0.08790 0.19040  -0.28240 44  ILE A CA  
665  C C   . ILE A 44  ? 0.40800 0.82770 0.88200 -0.04860 0.18000  -0.24430 44  ILE A C   
666  O O   . ILE A 44  ? 0.53130 0.93180 0.95350 -0.03470 0.16190  -0.23750 44  ILE A O   
667  C CB  . ILE A 44  ? 0.55920 0.97090 1.05340 -0.10510 0.18870  -0.30270 44  ILE A CB  
668  C CG1 . ILE A 44  ? 0.55550 0.99820 1.09690 -0.14230 0.19110  -0.34340 44  ILE A CG1 
669  C CG2 . ILE A 44  ? 0.50290 0.82740 0.95840 -0.10330 0.21660  -0.28180 44  ILE A CG2 
670  C CD1 . ILE A 44  ? 1.01460 1.43190 1.59640 -0.16630 0.22110  -0.34480 44  ILE A CD1 
682  N N   . CYS A 45  ? 0.41260 0.82560 0.88920 -0.03010 0.18360  -0.21600 45  CYS A N   
683  C CA  . CYS A 45  ? 0.30120 0.68910 0.73240 0.00640  0.17320  -0.17980 45  CYS A CA  
684  C C   . CYS A 45  ? 0.30470 0.59850 0.68710 0.00930  0.19440  -0.14870 45  CYS A C   
685  O O   . CYS A 45  ? 0.49420 0.74670 0.88360 -0.01000 0.21470  -0.14510 45  CYS A O   
686  C CB  . CYS A 45  ? 0.29180 0.71080 0.73920 0.02560  0.16270  -0.16180 45  CYS A CB  
687  S SG  . CYS A 45  ? 0.30720 0.83090 0.79860 0.02490  0.12900  -0.19360 45  CYS A SG  
692  N N   . GLY A 46  ? 0.29280 0.55300 0.62290 0.03240  0.18550  -0.12710 46  GLY A N   
693  C CA  . GLY A 46  ? 0.29320 0.46930 0.56940 0.03970  0.19450  -0.09120 46  GLY A CA  
694  C C   . GLY A 46  ? 0.29210 0.42980 0.51730 0.04770  0.18900  -0.08250 46  GLY A C   
695  O O   . GLY A 46  ? 0.29220 0.46770 0.52130 0.04930  0.18100  -0.10550 46  GLY A O   
699  N N   . PRO A 47  ? 0.25940 0.51510 0.17960 -0.15430 -0.00210 0.00060  47  PRO A N   
700  C CA  . PRO A 47  ? 0.23380 0.48990 0.15360 -0.15410 -0.00110 -0.00080 47  PRO A CA  
701  C C   . PRO A 47  ? 0.21060 0.46760 0.13420 -0.14910 -0.00280 0.00410  47  PRO A C   
702  O O   . PRO A 47  ? 0.23660 0.49460 0.16070 -0.14890 -0.00210 0.00330  47  PRO A O   
703  C CB  . PRO A 47  ? 0.22660 0.48940 0.14150 -0.16020 -0.00020 -0.00250 47  PRO A CB  
704  C CG  . PRO A 47  ? 0.23640 0.50030 0.14850 -0.16410 -0.00030 -0.00340 47  PRO A CG  
705  C CD  . PRO A 47  ? 0.23440 0.49460 0.15130 -0.15840 -0.00230 0.00080  47  PRO A CD  
713  N N   . GLN A 48  ? 0.26640 0.52410 0.19220 -0.14670 -0.00460 0.00850  48  GLN A N   
714  C CA  . GLN A 48  ? 0.26150 0.52140 0.19000 -0.14490 -0.00570 0.01160  48  GLN A CA  
715  C C   . GLN A 48  ? 0.22290 0.47840 0.15170 -0.14380 -0.00480 0.00940  48  GLN A C   
716  O O   . GLN A 48  ? 0.35380 0.61140 0.28310 -0.14430 -0.00440 0.00890  48  GLN A O   
717  C CB  . GLN A 48  ? 0.25350 0.51390 0.18330 -0.14420 -0.00730 0.01510  48  GLN A CB  
718  C CG  . GLN A 48  ? 0.32710 0.59490 0.25670 -0.14590 -0.00870 0.01820  48  GLN A CG  
719  C CD  . GLN A 48  ? 0.20850 0.47280 0.13570 -0.14680 -0.00820 0.01620  48  GLN A CD  
720  O OE1 . GLN A 48  ? 0.32320 0.58120 0.24980 -0.14600 -0.00720 0.01310  48  GLN A OE1 
721  N NE2 . GLN A 48  ? 0.25400 0.52480 0.18020 -0.14910 -0.00930 0.01850  48  GLN A NE2 
730  N N   . LEU A 49  ? 0.24990 0.50130 0.17850 -0.14280 -0.00470 0.00860  49  LEU A N   
731  C CA  . LEU A 49  ? 0.20550 0.45520 0.13430 -0.14240 -0.00410 0.00730  49  LEU A CA  
732  C C   . LEU A 49  ? 0.20110 0.45020 0.12940 -0.14280 -0.00270 0.00410  49  LEU A C   
733  O O   . LEU A 49  ? 0.31160 0.56010 0.24030 -0.14250 -0.00210 0.00290  49  LEU A O   
734  C CB  . LEU A 49  ? 0.35090 0.60120 0.28000 -0.14200 -0.00530 0.00940  49  LEU A CB  
735  C CG  . LEU A 49  ? 0.32980 0.58020 0.25820 -0.14300 -0.00620 0.01140  49  LEU A CG  
736  C CD1 . LEU A 49  ? 0.47770 0.73180 0.40630 -0.14350 -0.00770 0.01410  49  LEU A CD1 
737  C CD2 . LEU A 49  ? 0.48710 0.73650 0.41390 -0.14550 -0.00510 0.00940  49  LEU A CD2 
749  N N   . LEU A 50  ? 0.26500 0.51480 0.19220 -0.14480 -0.00180 0.00170  50  LEU A N   
750  C CA  . LEU A 50  ? 0.28840 0.53780 0.21430 -0.14690 0.00020  -0.00270 50  LEU A CA  
751  C C   . LEU A 50  ? 0.27520 0.52570 0.20070 -0.14690 0.00090  -0.00350 50  LEU A C   
752  O O   . LEU A 50  ? 0.33140 0.58090 0.25700 -0.14700 0.00200  -0.00590 50  LEU A O   
753  C CB  . LEU A 50  ? 0.25540 0.50550 0.17840 -0.15210 0.00210  -0.00720 50  LEU A CB  
754  C CG  . LEU A 50  ? 0.31590 0.56910 0.24010 -0.15420 0.00190  -0.00640 50  LEU A CG  
755  C CD1 . LEU A 50  ? 0.39640 0.65000 0.31610 -0.16230 0.00530  -0.01250 50  LEU A CD1 
756  C CD2 . LEU A 50  ? 0.39700 0.65470 0.32370 -0.15410 0.00190  -0.00520 50  LEU A CD2 
768  N N   . HIS A 51  ? 0.28020 0.53490 0.20560 -0.14740 -0.00010 -0.00080 51  HIS A N   
769  C CA  . HIS A 51  ? 0.20950 0.47040 0.13580 -0.14820 -0.00030 0.00040  51  HIS A CA  
770  C C   . HIS A 51  ? 0.20770 0.46690 0.13620 -0.14620 -0.00060 0.00110  51  HIS A C   
771  O O   . HIS A 51  ? 0.30190 0.56330 0.23080 -0.14690 0.00000  -0.00020 51  HIS A O   
772  C CB  . HIS A 51  ? 0.30400 0.57450 0.23130 -0.14940 -0.00250 0.00560  51  HIS A CB  
773  C CG  . HIS A 51  ? 0.31830 0.59220 0.24250 -0.15280 -0.00210 0.00480  51  HIS A CG  
774  N ND1 . HIS A 51  ? 0.39710 0.67680 0.32190 -0.15320 -0.00400 0.00930  51  HIS A ND1 
775  C CD2 . HIS A 51  ? 0.43200 0.70500 0.35170 -0.15720 0.00030  -0.00050 51  HIS A CD2 
776  C CE1 . HIS A 51  ? 0.37940 0.66260 0.29950 -0.15820 -0.00290 0.00690  51  HIS A CE1 
777  N NE2 . HIS A 51  ? 0.43190 0.71050 0.34860 -0.16120 -0.00010 0.00040  51  HIS A NE2 
785  N N   . GLN A 52  ? 0.27030 0.52610 0.19950 -0.14480 -0.00140 0.00250  52  GLN A N   
786  C CA  . GLN A 52  ? 0.25120 0.50570 0.18090 -0.14510 -0.00100 0.00170  52  GLN A CA  
787  C C   . GLN A 52  ? 0.21530 0.46500 0.14430 -0.14410 0.00030  -0.00130 52  GLN A C   
788  O O   . GLN A 52  ? 0.33180 0.58130 0.26080 -0.14490 0.00120  -0.00320 52  GLN A O   
789  C CB  . GLN A 52  ? 0.33320 0.58600 0.26220 -0.14610 -0.00160 0.00290  52  GLN A CB  
790  C CG  . GLN A 52  ? 0.30080 0.55930 0.23090 -0.14740 -0.00310 0.00620  52  GLN A CG  
791  C CD  . GLN A 52  ? 0.42360 0.68040 0.35210 -0.15020 -0.00300 0.00590  52  GLN A CD  
792  O OE1 . GLN A 52  ? 0.64200 0.89360 0.56810 -0.15100 -0.00210 0.00360  52  GLN A OE1 
793  N NE2 . GLN A 52  ? 0.54030 0.80380 0.47000 -0.15290 -0.00400 0.00870  52  GLN A NE2 
802  N N   . ILE A 53  ? 0.26970 0.51720 0.19840 -0.14300 0.00020  -0.00150 53  ILE A N   
803  C CA  . ILE A 53  ? 0.27680 0.52360 0.20560 -0.14280 0.00080  -0.00320 53  ILE A CA  
804  C C   . ILE A 53  ? 0.23340 0.48000 0.16190 -0.14370 0.00260  -0.00670 53  ILE A C   
805  O O   . ILE A 53  ? 0.25010 0.49600 0.17890 -0.14360 0.00340  -0.00840 53  ILE A O   
806  C CB  . ILE A 53  ? 0.19900 0.44820 0.12850 -0.14310 0.00000  -0.00190 53  ILE A CB  
807  C CG1 . ILE A 53  ? 0.34540 0.59740 0.27560 -0.14240 -0.00220 0.00250  53  ILE A CG1 
808  C CG2 . ILE A 53  ? 0.29020 0.54240 0.22050 -0.14440 0.00080  -0.00390 53  ILE A CG2 
809  C CD1 . ILE A 53  ? 0.27760 0.53400 0.20890 -0.14290 -0.00360 0.00540  53  ILE A CD1 
821  N N   . ALA A 54  ? 0.30800 0.55610 0.23550 -0.14520 0.00320  -0.00800 54  ALA A N   
822  C CA  . ALA A 54  ? 0.22620 0.47590 0.15260 -0.14750 0.00500  -0.01160 54  ALA A CA  
823  C C   . ALA A 54  ? 0.20360 0.45670 0.13140 -0.14700 0.00460  -0.01040 54  ALA A C   
824  O O   . ALA A 54  ? 0.30500 0.55770 0.23280 -0.14760 0.00590  -0.01310 54  ALA A O   
825  C CB  . ALA A 54  ? 0.38230 0.63520 0.30610 -0.15100 0.00570  -0.01290 54  ALA A CB  
831  N N   A GLU A 55  ? 0.29030 0.54780 0.21950 -0.14680 0.00290  -0.00640 55  GLU A N   
832  N N   B GLU A 55  ? 0.29170 0.54900 0.22090 -0.14680 0.00280  -0.00640 55  GLU A N   
833  C CA  A GLU A 55  ? 0.26450 0.52670 0.19530 -0.14770 0.00240  -0.00550 55  GLU A CA  
834  C CA  B GLU A 55  ? 0.27380 0.53600 0.20460 -0.14770 0.00240  -0.00530 55  GLU A CA  
835  C C   A GLU A 55  ? 0.36660 0.62210 0.29710 -0.14700 0.00380  -0.00840 55  GLU A C   
836  C C   B GLU A 55  ? 0.36550 0.62110 0.29600 -0.14700 0.00370  -0.00830 55  GLU A C   
837  O O   A GLU A 55  ? 0.32460 0.58180 0.25560 -0.14800 0.00460  -0.01010 55  GLU A O   
838  O O   B GLU A 55  ? 0.32410 0.58160 0.25510 -0.14810 0.00450  -0.01000 55  GLU A O   
839  C CB  A GLU A 55  ? 0.37480 0.64460 0.30730 -0.14890 0.00030  -0.00080 55  GLU A CB  
840  C CB  B GLU A 55  ? 0.36980 0.63870 0.30220 -0.14880 0.00030  -0.00070 55  GLU A CB  
841  C CG  A GLU A 55  ? 0.43000 0.70460 0.37050 -0.14960 0.00000  0.00080  55  GLU A CG  
842  C CG  B GLU A 55  ? 0.35760 0.63730 0.29100 -0.14980 -0.00180 0.00410  55  GLU A CG  
843  C CD  A GLU A 55  ? 0.60480 0.88890 0.55080 -0.14960 -0.00080 0.00310  55  GLU A CD  
844  C CD  B GLU A 55  ? 0.32010 0.60730 0.25640 -0.15050 -0.00420 0.00980  55  GLU A CD  
845  O OE1 A GLU A 55  ? 0.58690 0.88200 0.53020 -0.15120 -0.00280 0.00710  55  GLU A OE1 
846  O OE1 B GLU A 55  ? 0.21460 0.49380 0.15480 -0.14960 -0.00320 0.00840  55  GLU A OE1 
847  O OE2 A GLU A 55  ? 0.59520 0.87690 0.54730 -0.14890 0.00060  0.00110  55  GLU A OE2 
848  O OE2 B GLU A 55  ? 0.43510 0.73430 0.37540 -0.15080 -0.00650 0.01580  55  GLU A OE2 
861  N N   . ILE A 56  ? 0.31810 0.56770 0.24750 -0.14580 0.00380  -0.00850 56  ILE A N   
862  C CA  . ILE A 56  ? 0.32960 0.57570 0.25810 -0.14620 0.00470  -0.01040 56  ILE A CA  
863  C C   . ILE A 56  ? 0.26610 0.51090 0.19500 -0.14500 0.00560  -0.01260 56  ILE A C   
864  O O   . ILE A 56  ? 0.33760 0.58170 0.26650 -0.14580 0.00670  -0.01480 56  ILE A O   
865  C CB  . ILE A 56  ? 0.22970 0.47410 0.15680 -0.14620 0.00370  -0.00850 56  ILE A CB  
866  C CG1 . ILE A 56  ? 0.25440 0.49930 0.18010 -0.14900 0.00350  -0.00800 56  ILE A CG1 
867  C CG2 . ILE A 56  ? 0.31050 0.55460 0.23620 -0.14740 0.00400  -0.00930 56  ILE A CG2 
868  C CD1 . ILE A 56  ? 0.23860 0.48330 0.16280 -0.14930 0.00220  -0.00560 56  ILE A CD1 
880  N N   . GLU A 57  ? 0.24720 0.49210 0.17650 -0.14410 0.00560  -0.01280 57  GLU A N   
881  C CA  . GLU A 57  ? 0.29450 0.53900 0.22400 -0.14450 0.00700  -0.01590 57  GLU A CA  
882  C C   . GLU A 57  ? 0.42890 0.67410 0.35840 -0.14560 0.00840  -0.01870 57  GLU A C   
883  O O   . GLU A 57  ? 0.35220 0.59660 0.28200 -0.14580 0.00970  -0.02120 57  GLU A O   
884  C CB  . GLU A 57  ? 0.25230 0.49750 0.18130 -0.14610 0.00760  -0.01750 57  GLU A CB  
885  C CG  . GLU A 57  ? 0.35270 0.60110 0.28260 -0.14600 0.00590  -0.01410 57  GLU A CG  
886  C CD  . GLU A 57  ? 0.51960 0.77000 0.44860 -0.14970 0.00730  -0.01670 57  GLU A CD  
887  O OE1 . GLU A 57  ? 0.64230 0.89000 0.56930 -0.15090 0.00810  -0.01860 57  GLU A OE1 
888  O OE2 . GLU A 57  ? 0.60650 0.86230 0.53840 -0.15210 0.00830  -0.01630 57  GLU A OE2 
895  N N   A ARG A 58  ? 0.42910 0.67830 0.35850 -0.14660 0.00790  -0.01740 58  ARG A N   
896  N N   B ARG A 58  ? 0.42820 0.67740 0.35760 -0.14670 0.00790  -0.01750 58  ARG A N   
897  C CA  A ARG A 58  ? 0.38160 0.63640 0.31140 -0.14850 0.00840  -0.01840 58  ARG A CA  
898  C CA  B ARG A 58  ? 0.38420 0.63890 0.31390 -0.14860 0.00850  -0.01860 58  ARG A CA  
899  C C   A ARG A 58  ? 0.37860 0.63340 0.30970 -0.14830 0.00860  -0.01890 58  ARG A C   
900  C C   B ARG A 58  ? 0.38190 0.63690 0.31300 -0.14840 0.00860  -0.01890 58  ARG A C   
901  O O   A ARG A 58  ? 0.42470 0.67870 0.35590 -0.14870 0.01000  -0.02190 58  ARG A O   
902  O O   B ARG A 58  ? 0.42660 0.68140 0.35800 -0.14890 0.01000  -0.02170 58  ARG A O   
903  C CB  A ARG A 58  ? 0.49900 0.76300 0.42900 -0.15030 0.00650  -0.01440 58  ARG A CB  
904  C CB  B ARG A 58  ? 0.47540 0.73970 0.40520 -0.15060 0.00670  -0.01490 58  ARG A CB  
905  C CG  A ARG A 58  ? 0.44300 0.71780 0.37250 -0.15380 0.00630  -0.01390 58  ARG A CG  
906  C CG  B ARG A 58  ? 0.43320 0.70830 0.36330 -0.15370 0.00650  -0.01450 58  ARG A CG  
907  C CD  A ARG A 58  ? 0.49780 0.78420 0.42730 -0.15590 0.00370  -0.00830 58  ARG A CD  
908  C CD  B ARG A 58  ? 0.41580 0.70650 0.34710 -0.15600 0.00340  -0.00770 58  ARG A CD  
909  N NE  A ARG A 58  ? 0.57320 0.85540 0.49900 -0.15770 0.00510  -0.01110 58  ARG A NE  
910  N NE  B ARG A 58  ? 0.32690 0.61960 0.26670 -0.15320 0.00110  -0.00240 58  ARG A NE  
911  C CZ  A ARG A 58  ? 0.45530 0.73720 0.38080 -0.15720 0.00390  -0.00840 58  ARG A CZ  
912  C CZ  B ARG A 58  ? 0.37680 0.66780 0.32970 -0.15060 0.00110  -0.00130 58  ARG A CZ  
913  N NH1 A ARG A 58  ? 0.44210 0.72710 0.37080 -0.15460 0.00140  -0.00280 58  ARG A NH1 
914  N NH1 B ARG A 58  ? 0.43360 0.72330 0.38740 -0.15090 0.00250  -0.00450 58  ARG A NH1 
915  N NH2 A ARG A 58  ? 0.53440 0.81310 0.45590 -0.16010 0.00570  -0.01190 58  ARG A NH2 
916  N NH2 B ARG A 58  ? 0.37360 0.66360 0.34030 -0.14800 0.00090  0.00290  58  ARG A NH2 
943  N N   . GLU A 59  ? 0.35930 0.61430 0.29070 -0.14870 0.00770  -0.01690 59  GLU A N   
944  C CA  . GLU A 59  ? 0.38600 0.63990 0.31860 -0.15020 0.00880  -0.01880 59  GLU A CA  
945  C C   . GLU A 59  ? 0.32580 0.57300 0.25600 -0.14950 0.01030  -0.02200 59  GLU A C   
946  O O   . GLU A 59  ? 0.41750 0.66430 0.34780 -0.15080 0.01180  -0.02490 59  GLU A O   
947  C CB  . GLU A 59  ? 0.39460 0.64630 0.33210 -0.15120 0.00860  -0.01720 59  GLU A CB  
948  C CG  . GLU A 59  ? 0.54880 0.80710 0.49710 -0.14980 0.00690  -0.01190 59  GLU A CG  
949  C CD  . GLU A 59  ? 0.83300 1.08860 0.79190 -0.15060 0.00840  -0.01000 59  GLU A CD  
950  O OE1 . GLU A 59  ? 0.75060 0.99800 0.70990 -0.15330 0.01180  -0.01410 59  GLU A OE1 
951  O OE2 . GLU A 59  ? 0.90660 1.16850 0.87360 -0.14920 0.00700  -0.00440 59  GLU A OE2 
958  N N   . LEU A 60  ? 0.31010 0.55380 0.23950 -0.14750 0.00970  -0.02080 60  LEU A N   
959  C CA  . LEU A 60  ? 0.34700 0.58870 0.27590 -0.14700 0.01010  -0.02170 60  LEU A CA  
960  C C   . LEU A 60  ? 0.44500 0.68670 0.37520 -0.14640 0.01140  -0.02450 60  LEU A C   
961  O O   . LEU A 60  ? 0.36030 0.60130 0.29050 -0.14700 0.01230  -0.02650 60  LEU A O   
962  C CB  . LEU A 60  ? 0.31220 0.55530 0.24100 -0.14580 0.00820  -0.01830 60  LEU A CB  
963  C CG  . LEU A 60  ? 0.42140 0.66530 0.34800 -0.14760 0.00710  -0.01590 60  LEU A CG  
964  C CD1 . LEU A 60  ? 0.45910 0.70800 0.38640 -0.14660 0.00450  -0.01120 60  LEU A CD1 
965  C CD2 . LEU A 60  ? 0.45970 0.70380 0.38380 -0.15070 0.00800  -0.01770 60  LEU A CD2 
977  N N   . ASN A 61  ? 0.45620 0.69910 0.38700 -0.14620 0.01180  -0.02550 61  ASN A N   
978  C CA  . ASN A 61  ? 0.43430 0.67720 0.36540 -0.14720 0.01370  -0.02940 61  ASN A CA  
979  C C   . ASN A 61  ? 0.46180 0.70700 0.39360 -0.14820 0.01450  -0.03110 61  ASN A C   
980  O O   . ASN A 61  ? 0.41040 0.65440 0.34270 -0.14860 0.01610  -0.03410 61  ASN A O   
981  C CB  . ASN A 61  ? 0.47990 0.72380 0.40980 -0.14920 0.01470  -0.03150 61  ASN A CB  
982  C CG  . ASN A 61  ? 0.64330 0.88600 0.57270 -0.14960 0.01450  -0.03100 61  ASN A CG  
983  O OD1 . ASN A 61  ? 0.71710 0.96080 0.64750 -0.14900 0.01360  -0.02940 61  ASN A OD1 
984  N ND2 . ASN A 61  ? 0.76800 1.01110 0.69560 -0.15160 0.01490  -0.03170 61  ASN A ND2 
991  N N   . ASN A 62  ? 0.38660 0.63690 0.31890 -0.14920 0.01340  -0.02870 62  ASN A N   
992  C CA  . ASN A 62  ? 0.31390 0.56690 0.25170 -0.14970 0.01360  -0.02890 62  ASN A CA  
993  C C   . ASN A 62  ? 0.42150 0.66810 0.36000 -0.14950 0.01510  -0.03140 62  ASN A C   
994  O O   . ASN A 62  ? 0.57580 0.82110 0.51860 -0.14930 0.01640  -0.03360 62  ASN A O   
995  C CB  . ASN A 62  ? 0.38270 0.64050 0.32970 -0.14920 0.01160  -0.02390 62  ASN A CB  
996  C CG  . ASN A 62  ? 0.56240 0.83020 0.50860 -0.15040 0.00950  -0.02050 62  ASN A CG  
997  O OD1 . ASN A 62  ? 0.50550 0.77600 0.44350 -0.15280 0.01050  -0.02330 62  ASN A OD1 
998  N ND2 . ASN A 62  ? 0.56720 0.84140 0.52230 -0.14960 0.00720  -0.01460 62  ASN A ND2 
1005 N N   . GLN A 63  ? 0.45060 0.69440 0.38420 -0.15050 0.01500  -0.03110 63  GLN A N   
1006 C CA  . GLN A 63  ? 0.33490 0.57470 0.26640 -0.15250 0.01660  -0.03390 63  GLN A CA  
1007 C C   . GLN A 63  ? 0.30910 0.54780 0.23930 -0.15100 0.01690  -0.03500 63  GLN A C   
1008 O O   . GLN A 63  ? 0.38800 0.62510 0.31750 -0.15260 0.01850  -0.03780 63  GLN A O   
1009 C CB  . GLN A 63  ? 0.42850 0.66660 0.35510 -0.15500 0.01630  -0.03310 63  GLN A CB  
1010 C CG  . GLN A 63  ? 0.44880 0.68480 0.37930 -0.15770 0.01750  -0.03380 63  GLN A CG  
1011 C CD  . GLN A 63  ? 0.60660 0.84210 0.52730 -0.16290 0.01790  -0.03510 63  GLN A CD  
1012 O OE1 . GLN A 63  ? 0.69120 0.92620 0.61010 -0.16200 0.01680  -0.03330 63  GLN A OE1 
1013 N NE2 . GLN A 63  ? 0.95200 1.18370 0.87800 -0.16530 0.01970  -0.03570 63  GLN A NE2 
1022 N N   . GLU A 64  ? 0.37440 0.61370 0.30540 -0.14860 0.01570  -0.03310 64  GLU A N   
1023 C CA  . GLU A 64  ? 0.44770 0.68720 0.37940 -0.14800 0.01620  -0.03430 64  GLU A CA  
1024 C C   . GLU A 64  ? 0.53020 0.76880 0.46310 -0.14870 0.01850  -0.03870 64  GLU A C   
1025 O O   . GLU A 64  ? 0.51360 0.75140 0.44650 -0.14920 0.01940  -0.04050 64  GLU A O   
1026 C CB  . GLU A 64  ? 0.40440 0.64600 0.33680 -0.14750 0.01560  -0.03330 64  GLU A CB  
1027 C CG  . GLU A 64  ? 0.47190 0.71780 0.40530 -0.14870 0.01560  -0.03330 64  GLU A CG  
1028 C CD  . GLU A 64  ? 0.70780 0.95400 0.64720 -0.14870 0.01690  -0.03260 64  GLU A CD  
1029 O OE1 . GLU A 64  ? 0.96820 1.21100 0.90510 -0.15020 0.01840  -0.03650 64  GLU A OE1 
1030 O OE2 . GLU A 64  ? 1.00120 1.25170 0.95010 -0.14730 0.01730  -0.02710 64  GLU A OE2 
1037 N N   . GLN A 65  ? 0.48480 0.72540 0.41840 -0.14920 0.01910  -0.03990 65  GLN A N   
1038 C CA  . GLN A 65  ? 0.43900 0.67980 0.37730 -0.14940 0.02060  -0.04250 65  GLN A CA  
1039 C C   . GLN A 65  ? 0.34120 0.57970 0.28520 -0.14910 0.02120  -0.04260 65  GLN A C   
1040 O O   . GLN A 65  ? 0.49770 0.73370 0.44380 -0.14900 0.02280  -0.04520 65  GLN A O   
1041 C CB  . GLN A 65  ? 0.60800 0.85480 0.54840 -0.15050 0.01990  -0.04150 65  GLN A CB  
1042 C CG  . GLN A 65  ? 0.97550 1.22360 0.90970 -0.15310 0.02130  -0.04450 65  GLN A CG  
1043 C CD  . GLN A 65  ? 1.42180 1.67890 1.35470 -0.15610 0.02020  -0.04280 65  GLN A CD  
1044 O OE1 . GLN A 65  ? 1.27200 1.53570 1.21150 -0.15520 0.01760  -0.03780 65  GLN A OE1 
1045 N NE2 . GLN A 65  ? 1.44000 1.69610 1.36930 -0.15920 0.02200  -0.04590 65  GLN A NE2 
1054 N N   . GLU A 66  ? 0.32720 0.56590 0.27560 -0.14930 0.02040  -0.04010 66  GLU A N   
1055 C CA  . GLU A 66  ? 0.27260 0.50710 0.22830 -0.15030 0.02240  -0.04120 66  GLU A CA  
1056 C C   . GLU A 66  ? 0.49970 0.72960 0.44740 -0.15240 0.02420  -0.04510 66  GLU A C   
1057 O O   . GLU A 66  ? 0.52140 0.74780 0.47370 -0.15330 0.02670  -0.04770 66  GLU A O   
1058 C CB  . GLU A 66  ? 0.44890 0.68220 0.40910 -0.15150 0.02260  -0.03890 66  GLU A CB  
1059 C CG  . GLU A 66  ? 0.46930 0.69960 0.44640 -0.15200 0.02620  -0.03760 66  GLU A CG  
1060 C CD  . GLU A 66  ? 0.85250 1.08040 0.83610 -0.15360 0.02850  -0.03520 66  GLU A CD  
1061 O OE1 . GLU A 66  ? 0.74770 0.97940 0.72540 -0.15310 0.02510  -0.03290 66  GLU A OE1 
1062 O OE2 . GLU A 66  ? 0.86930 1.09000 0.86440 -0.15570 0.03530  -0.03540 66  GLU A OE2 
1069 N N   . ILE A 67  ? 0.50910 0.74100 0.44600 -0.15340 0.02290  -0.04460 67  ILE A N   
1070 C CA  . ILE A 67  ? 0.45240 0.68450 0.38150 -0.15640 0.02340  -0.04630 67  ILE A CA  
1071 C C   . ILE A 67  ? 0.33670 0.56970 0.26770 -0.15430 0.02360  -0.04710 67  ILE A C   
1072 O O   . ILE A 67  ? 0.40610 0.63830 0.33570 -0.15630 0.02480  -0.04930 67  ILE A O   
1073 C CB  . ILE A 67  ? 0.41340 0.64810 0.33920 -0.15650 0.02070  -0.04170 67  ILE A CB  
1074 C CG1 . ILE A 67  ? 0.30470 0.53750 0.22690 -0.16080 0.02160  -0.04270 67  ILE A CG1 
1075 C CG2 . ILE A 67  ? 0.38370 0.62250 0.30790 -0.15770 0.01940  -0.03970 67  ILE A CG2 
1076 C CD1 . ILE A 67  ? 0.24640 0.48230 0.16720 -0.15990 0.01870  -0.03760 67  ILE A CD1 
1088 N N   . GLY A 68  ? 0.37110 0.60560 0.30510 -0.15140 0.02270  -0.04600 68  GLY A N   
1089 C CA  . GLY A 68  ? 0.38780 0.62140 0.32560 -0.15010 0.02390  -0.04790 68  GLY A CA  
1090 C C   . GLY A 68  ? 0.43530 0.66530 0.37850 -0.14960 0.02630  -0.05130 68  GLY A C   
1091 O O   . GLY A 68  ? 0.40980 0.63820 0.35520 -0.14950 0.02780  -0.05350 68  GLY A O   
1095 N N   . SER A 69  ? 0.46010 0.69020 0.40770 -0.14930 0.02630  -0.05080 69  SER A N   
1096 C CA  . SER A 69  ? 0.51660 0.74560 0.47280 -0.14890 0.02780  -0.05230 69  SER A CA  
1097 C C   . SER A 69  ? 0.48770 0.71190 0.44500 -0.15030 0.03000  -0.05440 69  SER A C   
1098 O O   . SER A 69  ? 0.52260 0.74480 0.48390 -0.15000 0.03180  -0.05680 69  SER A O   
1099 C CB  . SER A 69  ? 0.50120 0.73440 0.46650 -0.14830 0.02660  -0.04880 69  SER A CB  
1100 O OG  . SER A 69  ? 0.61150 0.85100 0.57530 -0.14850 0.02520  -0.04810 69  SER A OG  
1106 N N   . LEU A 70  ? 0.52690 0.74900 0.47990 -0.15300 0.03040  -0.05440 70  LEU A N   
1107 C CA  . LEU A 70  ? 0.36690 0.58400 0.31830 -0.15680 0.03360  -0.05800 70  LEU A CA  
1108 C C   . LEU A 70  ? 0.48560 0.70450 0.42890 -0.15790 0.03330  -0.05960 70  LEU A C   
1109 O O   . LEU A 70  ? 0.43400 0.64950 0.37810 -0.15970 0.03590  -0.06290 70  LEU A O   
1110 C CB  . LEU A 70  ? 0.47990 0.69500 0.42470 -0.16180 0.03470  -0.05900 70  LEU A CB  
1111 C CG  . LEU A 70  ? 0.54780 0.75750 0.50520 -0.16230 0.03800  -0.05840 70  LEU A CG  
1112 C CD1 . LEU A 70  ? 0.70220 0.91110 0.65230 -0.16640 0.03820  -0.05880 70  LEU A CD1 
1113 C CD2 . LEU A 70  ? 0.71530 0.91630 0.68010 -0.16550 0.04470  -0.06220 70  LEU A CD2 
1125 N N   . LYS A 71  ? 0.41940 0.64420 0.35630 -0.15710 0.03010  -0.05660 71  LYS A N   
1126 C CA  . LYS A 71  ? 0.36570 0.59470 0.29920 -0.15810 0.02920  -0.05600 71  LYS A CA  
1127 C C   . LYS A 71  ? 0.38300 0.60860 0.32470 -0.15470 0.03100  -0.05800 71  LYS A C   
1128 O O   . LYS A 71  ? 0.39350 0.61900 0.33520 -0.15600 0.03220  -0.05950 71  LYS A O   
1129 C CB  . LYS A 71  ? 0.38120 0.61840 0.31260 -0.15720 0.02540  -0.05040 71  LYS A CB  
1130 C CG  . LYS A 71  ? 0.50920 0.75070 0.43530 -0.16000 0.02300  -0.04650 71  LYS A CG  
1131 C CD  . LYS A 71  ? 0.61880 0.87220 0.54580 -0.15940 0.01870  -0.03920 71  LYS A CD  
1132 C CE  . LYS A 71  ? 0.66250 0.91610 0.59250 -0.15610 0.01790  -0.03760 71  LYS A CE  
1133 N NZ  . LYS A 71  ? 0.63750 0.90340 0.57220 -0.15540 0.01440  -0.02900 71  LYS A NZ  
1147 N N   . GLN A 72  ? 0.45620 0.68010 0.40390 -0.15140 0.03130  -0.05820 72  GLN A N   
1148 C CA  . GLN A 72  ? 0.41960 0.64120 0.37360 -0.14950 0.03330  -0.06060 72  GLN A CA  
1149 C C   . GLN A 72  ? 0.46540 0.68350 0.42490 -0.14950 0.03550  -0.06330 72  GLN A C   
1150 O O   . GLN A 72  ? 0.44790 0.66390 0.41080 -0.14910 0.03740  -0.06570 72  GLN A O   
1151 C CB  . GLN A 72  ? 0.33520 0.55800 0.29110 -0.14840 0.03310  -0.06080 72  GLN A CB  
1152 C CG  . GLN A 72  ? 0.42660 0.64740 0.38650 -0.14850 0.03590  -0.06450 72  GLN A CG  
1153 C CD  . GLN A 72  ? 0.42510 0.64400 0.38820 -0.14810 0.03750  -0.06430 72  GLN A CD  
1154 O OE1 . GLN A 72  ? 0.41460 0.63670 0.37770 -0.14780 0.03600  -0.05980 72  GLN A OE1 
1155 N NE2 . GLN A 72  ? 0.40010 0.61570 0.36750 -0.14830 0.04070  -0.06800 72  GLN A NE2 
1164 N N   . ARG A 73  ? 0.35760 0.57480 0.32050 -0.15010 0.03560  -0.06250 73  ARG A N   
1165 C CA  . ARG A 73  ? 0.25900 0.47270 0.23110 -0.15040 0.03830  -0.06370 73  ARG A CA  
1166 C C   . ARG A 73  ? 0.33050 0.53940 0.29780 -0.15330 0.04100  -0.06720 73  ARG A C   
1167 O O   . ARG A 73  ? 0.47480 0.68030 0.44850 -0.15310 0.04380  -0.06920 73  ARG A O   
1168 C CB  . ARG A 73  ? 0.40780 0.62160 0.38770 -0.15080 0.03860  -0.06070 73  ARG A CB  
1169 C CG  . ARG A 73  ? 0.61170 0.82580 0.60920 -0.14960 0.04110  -0.05800 73  ARG A CG  
1170 C CD  . ARG A 73  ? 0.82270 1.03880 0.83110 -0.14930 0.04180  -0.05250 73  ARG A CD  
1171 N NE  . ARG A 73  ? 0.84420 1.07030 0.85360 -0.14730 0.03680  -0.04790 73  ARG A NE  
1172 C CZ  . ARG A 73  ? 1.09270 1.32920 1.11270 -0.14550 0.03480  -0.04320 73  ARG A CZ  
1173 N NH1 . ARG A 73  ? 0.82230 1.06100 0.85380 -0.14460 0.03710  -0.04180 73  ARG A NH1 
1174 N NH2 . ARG A 73  ? 0.83850 1.08490 0.85640 -0.14540 0.03060  -0.03970 73  ARG A NH2 
1188 N N   . ALA A 74  ? 0.50620 0.71630 0.46190 -0.15670 0.04020  -0.06760 74  ALA A N   
1189 C CA  . ALA A 74  ? 0.48810 0.69680 0.43700 -0.16110 0.04220  -0.07080 74  ALA A CA  
1190 C C   . ALA A 74  ? 0.26720 0.47810 0.21810 -0.15850 0.04150  -0.07050 74  ALA A C   
1191 O O   . ALA A 74  ? 0.36640 0.57440 0.31790 -0.16020 0.04400  -0.07340 74  ALA A O   
1192 C CB  . ALA A 74  ? 0.45640 0.67060 0.39130 -0.16680 0.04020  -0.07020 74  ALA A CB  
1198 N N   . GLN A 75  ? 0.38830 0.60350 0.34110 -0.15500 0.03880  -0.06730 75  GLN A N   
1199 C CA  . GLN A 75  ? 0.32020 0.53610 0.27790 -0.15280 0.03940  -0.06700 75  GLN A CA  
1200 C C   . GLN A 75  ? 0.31140 0.52170 0.27690 -0.15070 0.04240  -0.07080 75  GLN A C   
1201 O O   . GLN A 75  ? 0.38080 0.58920 0.34940 -0.15040 0.04430  -0.07240 75  GLN A O   
1202 C CB  . GLN A 75  ? 0.46670 0.68630 0.42690 -0.15040 0.03770  -0.06350 75  GLN A CB  
1203 C CG  . GLN A 75  ? 0.57610 0.79640 0.54400 -0.14890 0.03950  -0.06190 75  GLN A CG  
1204 C CD  . GLN A 75  ? 0.97320 1.20070 0.94100 -0.15050 0.03850  -0.05730 75  GLN A CD  
1205 O OE1 . GLN A 75  ? 0.67600 0.91020 0.63510 -0.15410 0.03530  -0.05500 75  GLN A OE1 
1206 N NE2 . GLN A 75  ? 0.60970 0.83690 0.58670 -0.14870 0.04190  -0.05560 75  GLN A NE2 
1215 N N   . VAL A 76  ? 0.34060 0.55000 0.31060 -0.14960 0.04250  -0.07110 76  VAL A N   
1216 C CA  . VAL A 76  ? 0.24620 0.45400 0.22500 -0.14830 0.04450  -0.07290 76  VAL A CA  
1217 C C   . VAL A 76  ? 0.27400 0.47700 0.25630 -0.14950 0.04740  -0.07460 76  VAL A C   
1218 O O   . VAL A 76  ? 0.28550 0.48640 0.27250 -0.14890 0.04950  -0.07670 76  VAL A O   
1219 C CB  . VAL A 76  ? 0.27810 0.49040 0.26330 -0.14750 0.04300  -0.07030 76  VAL A CB  
1220 C CG1 . VAL A 76  ? 0.28670 0.50030 0.28420 -0.14700 0.04460  -0.06990 76  VAL A CG1 
1221 C CG2 . VAL A 76  ? 0.22730 0.44370 0.20810 -0.14780 0.04150  -0.07060 76  VAL A CG2 
1231 N N   . GLU A 77  ? 0.30820 0.50850 0.28780 -0.15220 0.04840  -0.07460 77  GLU A N   
1232 C CA  . GLU A 77  ? 0.34360 0.53750 0.32650 -0.15480 0.05300  -0.07740 77  GLU A CA  
1233 C C   . GLU A 77  ? 0.23240 0.42520 0.20690 -0.15700 0.05390  -0.08070 77  GLU A C   
1234 O O   . GLU A 77  ? 0.39830 0.58670 0.37760 -0.15720 0.05730  -0.08310 77  GLU A O   
1235 C CB  . GLU A 77  ? 0.38750 0.57690 0.36730 -0.15920 0.05560  -0.07840 77  GLU A CB  
1236 C CG  . GLU A 77  ? 0.46700 0.65770 0.45930 -0.15670 0.05560  -0.07360 77  GLU A CG  
1237 C CD  . GLU A 77  ? 0.65890 0.84520 0.64710 -0.16110 0.05810  -0.07430 77  GLU A CD  
1238 O OE1 . GLU A 77  ? 0.71190 0.89530 0.68420 -0.16730 0.05930  -0.07940 77  GLU A OE1 
1239 O OE2 . GLU A 77  ? 0.89070 1.07810 0.89210 -0.15880 0.05920  -0.06910 77  GLU A OE2 
1246 N N   . LYS A 78  ? 0.35740 0.55560 0.32080 -0.15900 0.05080  -0.07960 78  LYS A N   
1247 C CA  . LYS A 78  ? 0.30200 0.50330 0.25990 -0.16130 0.05050  -0.08000 78  LYS A CA  
1248 C C   . LYS A 78  ? 0.34840 0.54820 0.31530 -0.15690 0.05160  -0.08010 78  LYS A C   
1249 O O   . LYS A 78  ? 0.35990 0.55720 0.32770 -0.15810 0.05410  -0.08230 78  LYS A O   
1250 C CB  . LYS A 78  ? 0.38260 0.59440 0.33280 -0.16290 0.04580  -0.07510 78  LYS A CB  
1251 C CG  . LYS A 78  ? 0.55240 0.77350 0.49830 -0.16640 0.04390  -0.07190 78  LYS A CG  
1252 C CD  . LYS A 78  ? 0.85220 1.08550 0.80080 -0.16430 0.03930  -0.06320 78  LYS A CD  
1253 C CE  . LYS A 78  ? 1.05170 1.30100 0.99820 -0.16820 0.03610  -0.05610 78  LYS A CE  
1254 N NZ  . LYS A 78  ? 0.95950 1.21990 0.91770 -0.16310 0.03430  -0.04510 78  LYS A NZ  
1268 N N   . THR A 79  ? 0.26340 0.46430 0.23620 -0.15260 0.05030  -0.07830 79  THR A N   
1269 C CA  . THR A 79  ? 0.26390 0.46310 0.24370 -0.15000 0.05220  -0.07940 79  THR A CA  
1270 C C   . THR A 79  ? 0.25150 0.44580 0.23800 -0.14910 0.05510  -0.08280 79  THR A C   
1271 O O   . THR A 79  ? 0.22860 0.42030 0.21900 -0.14850 0.05760  -0.08480 79  THR A O   
1272 C CB  . THR A 79  ? 0.31590 0.51680 0.29820 -0.14800 0.05150  -0.07820 79  THR A CB  
1273 O OG1 . THR A 79  ? 0.20810 0.41010 0.19000 -0.14770 0.05000  -0.07850 79  THR A OG1 
1274 C CG2 . THR A 79  ? 0.24860 0.45480 0.22930 -0.14810 0.04960  -0.07290 79  THR A CG2 
1282 N N   . MET A 80  ? 0.22950 0.42390 0.21990 -0.14880 0.05480  -0.08220 80  MET A N   
1283 C CA  . MET A 80  ? 0.21170 0.40440 0.21270 -0.14790 0.05720  -0.08280 80  MET A CA  
1284 C C   . MET A 80  ? 0.21610 0.40240 0.21710 -0.14980 0.06100  -0.08520 80  MET A C   
1285 O O   . MET A 80  ? 0.25720 0.44100 0.26430 -0.14900 0.06360  -0.08670 80  MET A O   
1286 C CB  . MET A 80  ? 0.23360 0.43020 0.24300 -0.14730 0.05600  -0.07870 80  MET A CB  
1287 C CG  . MET A 80  ? 0.24920 0.45360 0.25840 -0.14650 0.05240  -0.07670 80  MET A CG  
1288 S SD  . MET A 80  ? 0.24720 0.45640 0.26020 -0.14700 0.05300  -0.07880 80  MET A SD  
1289 C CE  . MET A 80  ? 0.20830 0.41980 0.23820 -0.14610 0.05520  -0.07550 80  MET A CE  
1299 N N   . SER A 81  ? 0.25050 0.43420 0.24350 -0.15330 0.06180  -0.08620 81  SER A N   
1300 C CA  . SER A 81  ? 0.28140 0.45860 0.27170 -0.15710 0.06640  -0.08990 81  SER A CA  
1301 C C   . SER A 81  ? 0.23730 0.41530 0.22390 -0.15710 0.06630  -0.09160 81  SER A C   
1302 O O   . SER A 81  ? 0.32570 0.49860 0.31660 -0.15740 0.07020  -0.09420 81  SER A O   
1303 C CB  . SER A 81  ? 0.27480 0.45020 0.25280 -0.16340 0.06740  -0.09210 81  SER A CB  
1304 O OG  . SER A 81  ? 0.60410 0.77210 0.57700 -0.16930 0.07310  -0.09740 81  SER A OG  
1310 N N   . ALA A 82  ? 0.26550 0.45030 0.24650 -0.15650 0.06240  -0.08920 82  ALA A N   
1311 C CA  . ALA A 82  ? 0.23060 0.41730 0.21220 -0.15610 0.06280  -0.08860 82  ALA A CA  
1312 C C   . ALA A 82  ? 0.22520 0.40740 0.21700 -0.15210 0.06540  -0.09040 82  ALA A C   
1313 O O   . ALA A 82  ? 0.30890 0.48840 0.30300 -0.15230 0.06810  -0.09200 82  ALA A O   
1314 C CB  . ALA A 82  ? 0.23820 0.43340 0.21880 -0.15490 0.05920  -0.08310 82  ALA A CB  
1320 N N   . ALA A 83  ? 0.22910 0.41180 0.22630 -0.14930 0.06450  -0.09010 83  ALA A N   
1321 C CA  . ALA A 83  ? 0.21590 0.39720 0.22120 -0.14730 0.06650  -0.09200 83  ALA A CA  
1322 C C   . ALA A 83  ? 0.21740 0.39550 0.23010 -0.14720 0.06920  -0.09310 83  ALA A C   
1323 O O   . ALA A 83  ? 0.34510 0.52260 0.36430 -0.14620 0.07130  -0.09460 83  ALA A O   
1324 C CB  . ALA A 83  ? 0.28350 0.46920 0.29040 -0.14650 0.06450  -0.09140 83  ALA A CB  
1330 N N   . SER A 84  ? 0.34800 0.52380 0.36120 -0.14860 0.07020  -0.09220 84  SER A N   
1331 C CA  . SER A 84  ? 0.35590 0.52810 0.38030 -0.14830 0.07440  -0.09160 84  SER A CA  
1332 C C   . SER A 84  ? 0.24520 0.40930 0.26530 -0.15100 0.07910  -0.09560 84  SER A C   
1333 O O   . SER A 84  ? 0.37590 0.53540 0.40560 -0.15060 0.08390  -0.09540 84  SER A O   
1334 C CB  . SER A 84  ? 0.49800 0.67110 0.53000 -0.14840 0.07520  -0.08720 84  SER A CB  
1335 O OG  . SER A 84  ? 0.59050 0.77330 0.62770 -0.14620 0.07050  -0.08280 84  SER A OG  
1341 N N   . GLY A 85  ? 0.72740 0.86780 0.68960 -0.34890 -0.10570 -0.04670 85  GLY A N   
1342 C CA  . GLY A 85  ? 0.72220 0.85770 0.69270 -0.33920 -0.10150 -0.05540 85  GLY A CA  
1343 C C   . GLY A 85  ? 0.90090 1.04620 0.90390 -0.34990 -0.07370 -0.06580 85  GLY A C   
1344 O O   . GLY A 85  ? 0.93000 1.05930 0.95860 -0.35610 -0.05400 -0.05340 85  GLY A O   
1348 N N   . CYS A 86  ? 0.71620 0.88600 0.72260 -0.35330 -0.06780 -0.08970 86  CYS A N   
1349 C CA  . CYS A 86  ? 0.71500 0.89710 0.74830 -0.36470 -0.04070 -0.10700 86  CYS A CA  
1350 C C   . CYS A 86  ? 1.00410 1.21680 1.02560 -0.36260 -0.04640 -0.14080 86  CYS A C   
1351 O O   . CYS A 86  ? 1.15250 1.38000 1.18910 -0.37450 -0.02600 -0.16070 86  CYS A O   
1352 C CB  . CYS A 86  ? 0.73740 0.91900 0.80720 -0.37680 -0.02160 -0.08530 86  CYS A CB  
1353 S SG  . CYS A 86  ? 0.83040 0.98390 0.93530 -0.38180 -0.01540 -0.03070 86  CYS A SG  
1358 N N   . GLY A 87  ? 0.71720 0.94010 0.71840 -0.34910 -0.07120 -0.14650 87  GLY A N   
1359 C CA  . GLY A 87  ? 0.97380 1.22960 0.97710 -0.34550 -0.07840 -0.17100 87  GLY A CA  
1360 C C   . GLY A 87  ? 0.93390 1.20800 0.95210 -0.35010 -0.06630 -0.18630 87  GLY A C   
1361 O O   . GLY A 87  ? 0.74800 1.01220 0.76330 -0.35010 -0.06480 -0.18030 87  GLY A O   
1365 N N   . MET A 88  ? 1.26180 1.56460 1.29230 -0.35840 -0.05770 -0.20670 88  MET A N   
1366 C CA  . MET A 88  ? 1.35110 1.67250 1.39740 -0.36280 -0.04530 -0.22230 88  MET A CA  
1367 C C   . MET A 88  ? 1.36830 1.70480 1.42670 -0.38090 -0.02340 -0.23810 88  MET A C   
1368 O O   . MET A 88  ? 1.40240 1.71890 1.46690 -0.39260 -0.00300 -0.23190 88  MET A O   
1369 C CB  . MET A 88  ? 1.26980 1.61810 1.32750 -0.35050 -0.05890 -0.23440 88  MET A CB  
1370 C CG  . MET A 88  ? 1.21340 1.54920 1.26930 -0.33260 -0.07580 -0.22430 88  MET A CG  
1371 S SD  . MET A 88  ? 1.04860 1.34750 1.08480 -0.33420 -0.06760 -0.21850 88  MET A SD  
1372 C CE  . MET A 88  ? 1.04760 1.34170 1.09880 -0.31510 -0.07610 -0.22230 88  MET A CE  
1382 N N   . GLY A 89  ? 1.29240 1.66390 1.35990 -0.38460 -0.02480 -0.25770 89  GLY A N   
1383 C CA  . GLY A 89  ? 1.21600 1.60480 1.29270 -0.40490 -0.00280 -0.27710 89  GLY A CA  
1384 C C   . GLY A 89  ? 1.28640 1.66900 1.38230 -0.40670 0.01790  -0.27980 89  GLY A C   
1385 O O   . GLY A 89  ? 1.45990 1.82890 1.55600 -0.39640 0.01240  -0.26650 89  GLY A O   
1389 N N   . PRO A 90  ? 1.69110 2.08500 1.80160 -0.42410 0.04280  -0.29680 90  PRO A N   
1390 C CA  . PRO A 90  ? 1.68500 2.07350 1.81990 -0.42800 0.06410  -0.29430 90  PRO A CA  
1391 C C   . PRO A 90  ? 1.57210 1.92990 1.73150 -0.43640 0.08970  -0.27380 90  PRO A C   
1392 O O   . PRO A 90  ? 1.40010 1.75760 1.58970 -0.44230 0.10760  -0.26410 90  PRO A O   
1393 C CB  . PRO A 90  ? 1.41310 1.83180 1.55770 -0.44210 0.07890  -0.32290 90  PRO A CB  
1394 C CG  . PRO A 90  ? 1.54650 1.97180 1.67330 -0.45870 0.08150  -0.33660 90  PRO A CG  
1395 C CD  . PRO A 90  ? 1.48350 1.89980 1.58730 -0.44580 0.05240  -0.31940 90  PRO A CD  
1403 N N   . ALA A 91  ? 1.25990 1.59390 1.41400 -0.43760 0.09240  -0.26360 91  ALA A N   
1404 C CA  . ALA A 91  ? 1.26290 1.56600 1.45270 -0.44170 0.11550  -0.23520 91  ALA A CA  
1405 C C   . ALA A 91  ? 1.29120 1.58660 1.48240 -0.43070 0.09320  -0.19660 91  ALA A C   
1406 O O   . ALA A 91  ? 1.40070 1.69070 1.63320 -0.43740 0.10720  -0.16560 91  ALA A O   
1407 C CB  . ALA A 91  ? 1.03410 1.31260 1.21740 -0.44780 0.12720  -0.23780 91  ALA A CB  
1413 N N   . SER A 92  ? 1.35750 1.65540 1.50650 -0.41770 0.05920  -0.19600 92  SER A N   
1414 C CA  . SER A 92  ? 1.23150 1.52340 1.36580 -0.41420 0.03730  -0.16760 92  SER A CA  
1415 C C   . SER A 92  ? 1.13130 1.44350 1.26400 -0.42320 0.03570  -0.16970 92  SER A C   
1416 O O   . SER A 92  ? 0.70360 1.01370 0.81580 -0.43010 0.02060  -0.15060 92  SER A O   
1417 C CB  . SER A 92  ? 1.22580 1.51160 1.31840 -0.39940 0.00910  -0.17490 92  SER A CB  
1418 O OG  . SER A 92  ? 0.96570 1.27340 1.04330 -0.39140 0.00000  -0.20640 92  SER A OG  
1424 N N   . MET A 93  ? 1.09050 1.42240 1.24040 -0.42760 0.05240  -0.19360 93  MET A N   
1425 C CA  . MET A 93  ? 0.84560 1.19810 0.98870 -0.43510 0.05130  -0.20450 93  MET A CA  
1426 C C   . MET A 93  ? 0.79220 1.15690 0.97780 -0.44940 0.07580  -0.19600 93  MET A C   
1427 O O   . MET A 93  ? 0.96300 1.32970 1.17580 -0.44910 0.09770  -0.21260 93  MET A O   
1428 C CB  . MET A 93  ? 1.09280 1.46210 1.21790 -0.42290 0.04450  -0.24440 93  MET A CB  
1429 C CG  . MET A 93  ? 1.23690 1.59610 1.33320 -0.40750 0.02190  -0.24830 93  MET A CG  
1430 S SD  . MET A 93  ? 0.98670 1.34620 1.06070 -0.40820 0.01570  -0.26110 93  MET A SD  
1431 C CE  . MET A 93  ? 0.90150 1.29370 1.00110 -0.40020 0.02500  -0.29670 93  MET A CE  
1441 N N   . THR A 94  ? 0.73790 1.11190 0.92850 -0.46650 0.07280  -0.16900 94  THR A N   
1442 C CA  . THR A 94  ? 0.73380 1.12350 0.96890 -0.47970 0.09330  -0.15490 94  THR A CA  
1443 C C   . THR A 94  ? 0.68580 1.09110 0.92050 -0.47330 0.10700  -0.19800 94  THR A C   
1444 O O   . THR A 94  ? 0.79600 1.20080 1.06830 -0.46980 0.12980  -0.19600 94  THR A O   
1445 C CB  . THR A 94  ? 0.70370 1.10230 0.92810 -0.49600 0.07970  -0.11650 94  THR A CB  
1446 O OG1 . THR A 94  ? 0.74960 1.13630 0.97500 -0.50260 0.06420  -0.06960 94  THR A OG1 
1447 C CG2 . THR A 94  ? 0.70360 1.11140 0.97630 -0.49620 0.09670  -0.09430 94  THR A CG2 
1455 N N   . LEU A 95  ? 0.68970 1.10650 0.88590 -0.46970 0.09420  -0.23310 95  LEU A N   
1456 C CA  . LEU A 95  ? 0.81320 1.24880 1.01120 -0.46330 0.10370  -0.27150 95  LEU A CA  
1457 C C   . LEU A 95  ? 0.68410 1.12100 0.87520 -0.44920 0.09950  -0.29850 95  LEU A C   
1458 O O   . LEU A 95  ? 0.76510 1.19330 0.93130 -0.43710 0.07990  -0.29940 95  LEU A O   
1459 C CB  . LEU A 95  ? 0.75740 1.20460 0.92800 -0.46760 0.09570  -0.28730 95  LEU A CB  
1460 C CG  . LEU A 95  ? 0.71220 1.16680 0.87950 -0.48240 0.10340  -0.27480 95  LEU A CG  
1461 C CD1 . LEU A 95  ? 0.72110 1.16800 0.89130 -0.49880 0.09860  -0.22580 95  LEU A CD1 
1462 C CD2 . LEU A 95  ? 0.73280 1.19010 0.86490 -0.48840 0.09950  -0.29980 95  LEU A CD2 
1474 N N   . ASP A 96  ? 0.68310 1.12800 0.89210 -0.44980 0.11750  -0.31570 96  ASP A N   
1475 C CA  . ASP A 96  ? 0.68790 1.14010 0.88450 -0.44600 0.11190  -0.33640 96  ASP A CA  
1476 C C   . ASP A 96  ? 0.68900 1.17170 0.87710 -0.43830 0.09740  -0.35900 96  ASP A C   
1477 O O   . ASP A 96  ? 0.68630 1.17870 0.87790 -0.43500 0.09500  -0.36380 96  ASP A O   
1478 C CB  . ASP A 96  ? 0.69950 1.14230 0.90880 -0.45480 0.14060  -0.34440 96  ASP A CB  
1479 C CG  . ASP A 96  ? 0.70170 1.14820 0.93360 -0.45740 0.16490  -0.34970 96  ASP A CG  
1480 O OD1 . ASP A 96  ? 0.69580 1.16380 0.92540 -0.45330 0.15700  -0.35850 96  ASP A OD1 
1481 O OD2 . ASP A 96  ? 0.81490 1.23840 1.07020 -0.46240 0.19440  -0.34380 96  ASP A OD2 
1486 N N   . VAL A 97  ? 0.81010 0.71780 0.46180 -0.24360 0.20510  -0.08670 97  VAL A N   
1487 C CA  . VAL A 97  ? 0.93440 0.81100 0.53650 -0.20470 0.20630  -0.06330 97  VAL A CA  
1488 C C   . VAL A 97  ? 0.81560 0.74960 0.44710 -0.18530 0.16970  -0.06460 97  VAL A C   
1489 O O   . VAL A 97  ? 0.82830 0.74300 0.43610 -0.16510 0.16580  -0.05550 97  VAL A O   
1490 C CB  . VAL A 97  ? 1.02130 0.87700 0.57090 -0.16850 0.22120  -0.04000 97  VAL A CB  
1491 C CG1 . VAL A 97  ? 1.15700 1.01860 0.66570 -0.11830 0.20860  -0.01940 97  VAL A CG1 
1492 C CG2 . VAL A 97  ? 1.18330 0.96240 0.69650 -0.18280 0.26430  -0.03380 97  VAL A CG2 
1502 N N   . GLN A 98  ? 0.82310 0.82120 0.50660 -0.19140 0.14680  -0.07640 98  GLN A N   
1503 C CA  . GLN A 98  ? 0.65850 0.70880 0.37830 -0.17340 0.11670  -0.07940 98  GLN A CA  
1504 C C   . GLN A 98  ? 0.69460 0.75900 0.45170 -0.19630 0.10740  -0.08900 98  GLN A C   
1505 O O   . GLN A 98  ? 0.67470 0.74500 0.43310 -0.17630 0.09370  -0.08420 98  GLN A O   
1506 C CB  . GLN A 98  ? 0.58200 0.69250 0.35220 -0.17710 0.10240  -0.09010 98  GLN A CB  
1507 C CG  . GLN A 98  ? 0.91760 1.02360 0.65750 -0.16070 0.11170  -0.08560 98  GLN A CG  
1508 C CD  . GLN A 98  ? 1.00880 1.10950 0.76070 -0.19300 0.12790  -0.09300 98  GLN A CD  
1509 O OE1 . GLN A 98  ? 0.94770 0.99750 0.65560 -0.19710 0.15270  -0.08470 98  GLN A OE1 
1510 N NE2 . GLN A 98  ? 0.91770 1.06930 0.73050 -0.21510 0.11540  -0.10970 98  GLN A NE2 
1519 N N   . ALA A 99  ? 0.87710 0.95200 0.66350 -0.23390 0.11310  -0.10450 99  ALA A N   
1520 C CA  . ALA A 99  ? 0.53830 0.63800 0.35800 -0.25410 0.10360  -0.11680 99  ALA A CA  
1521 C C   . ALA A 99  ? 0.71030 0.75410 0.48750 -0.25550 0.11880  -0.11310 99  ALA A C   
1522 O O   . ALA A 99  ? 0.87860 0.94000 0.67320 -0.25630 0.10870  -0.11490 99  ALA A O   
1523 C CB  . ALA A 99  ? 0.71250 0.83250 0.55400 -0.26600 0.10340  -0.13310 99  ALA A CB  
1529 N N   . ARG A 100 ? 0.80480 0.78220 0.52890 -0.25460 0.14570  -0.10710 100 ARG A N   
1530 C CA  . ARG A 100 ? 0.75930 0.67290 0.43930 -0.25350 0.16590  -0.10290 100 ARG A CA  
1531 C C   . ARG A 100 ? 0.71580 0.62090 0.36870 -0.21080 0.15150  -0.08190 100 ARG A C   
1532 O O   . ARG A 100 ? 0.75290 0.62790 0.38780 -0.20890 0.15590  -0.08110 100 ARG A O   
1533 C CB  . ARG A 100 ? 1.05220 0.89130 0.68520 -0.26010 0.20490  -0.09930 100 ARG A CB  
1534 C CG  . ARG A 100 ? 1.25860 1.07160 0.90270 -0.30510 0.23160  -0.13030 100 ARG A CG  
1535 C CD  . ARG A 100 ? 1.38050 1.17730 1.02370 -0.31960 0.25350  -0.13900 100 ARG A CD  
1536 N NE  . ARG A 100 ? 1.22760 0.95520 0.81770 -0.29490 0.28310  -0.11140 100 ARG A NE  
1537 C CZ  . ARG A 100 ? 1.34120 1.05610 0.92400 -0.29600 0.29960  -0.10800 100 ARG A CZ  
1538 N NH1 . ARG A 100 ? 1.44670 1.21020 1.07230 -0.32090 0.28920  -0.13140 100 ARG A NH1 
1539 N NH2 . ARG A 100 ? 1.50950 1.16320 1.03860 -0.26760 0.32690  -0.07990 100 ARG A NH2 
1553 N N   . GLN A 101 ? 0.76180 0.69790 0.41460 -0.17660 0.13360  -0.06960 101 GLN A N   
1554 C CA  . GLN A 101 ? 0.77930 0.71770 0.41000 -0.13350 0.11780  -0.05650 101 GLN A CA  
1555 C C   . GLN A 101 ? 0.71200 0.69340 0.38990 -0.13340 0.09180  -0.06510 101 GLN A C   
1556 O O   . GLN A 101 ? 0.66880 0.63430 0.33070 -0.11570 0.08600  -0.06040 101 GLN A O   
1557 C CB  . GLN A 101 ? 0.89460 0.86150 0.51320 -0.09720 0.10770  -0.04860 101 GLN A CB  
1558 C CG  . GLN A 101 ? 0.77000 0.75720 0.37800 -0.05310 0.08660  -0.04420 101 GLN A CG  
1559 C CD  . GLN A 101 ? 0.68340 0.68600 0.25200 -0.01000 0.08530  -0.03510 101 GLN A CD  
1560 O OE1 . GLN A 101 ? 0.85330 0.84360 0.38740 -0.01100 0.10570  -0.02280 101 GLN A OE1 
1561 N NE2 . GLN A 101 ? 0.81890 0.81390 0.38580 0.01390  0.06400  -0.04200 101 GLN A NE2 
1570 N N   . LEU A 102 ? 0.66050 0.69740 0.39830 -0.15040 0.07800  -0.07580 102 LEU A N   
1571 C CA  . LEU A 102 ? 0.49250 0.56640 0.27680 -0.15340 0.06170  -0.08040 102 LEU A CA  
1572 C C   . LEU A 102 ? 0.49510 0.54070 0.26470 -0.17090 0.07010  -0.08380 102 LEU A C   
1573 O O   . LEU A 102 ? 0.52820 0.57400 0.30100 -0.15610 0.05970  -0.08100 102 LEU A O   
1574 C CB  . LEU A 102 ? 0.48780 0.62230 0.33470 -0.17440 0.05730  -0.08840 102 LEU A CB  
1575 C CG  . LEU A 102 ? 0.56530 0.74640 0.46240 -0.17200 0.04840  -0.08790 102 LEU A CG  
1576 C CD1 . LEU A 102 ? 0.49610 0.68420 0.40310 -0.13990 0.03550  -0.08350 102 LEU A CD1 
1577 C CD2 . LEU A 102 ? 0.48610 0.70280 0.41890 -0.17500 0.05150  -0.08970 102 LEU A CD2 
1589 N N   . LEU A 103 ? 0.59170 0.61210 0.34640 -0.20420 0.09130  -0.09310 103 LEU A N   
1590 C CA  . LEU A 103 ? 0.62640 0.62880 0.37600 -0.22710 0.10220  -0.10350 103 LEU A CA  
1591 C C   . LEU A 103 ? 0.63280 0.57050 0.32810 -0.20710 0.11130  -0.09430 103 LEU A C   
1592 O O   . LEU A 103 ? 0.60180 0.53620 0.30030 -0.21160 0.10950  -0.09960 103 LEU A O   
1593 C CB  . LEU A 103 ? 0.62010 0.61200 0.37150 -0.27110 0.12710  -0.12340 103 LEU A CB  
1594 C CG  . LEU A 103 ? 0.60350 0.60530 0.37030 -0.30140 0.14150  -0.14190 103 LEU A CG  
1595 C CD1 . LEU A 103 ? 0.63440 0.71890 0.45170 -0.28230 0.12000  -0.13780 103 LEU A CD1 
1596 C CD2 . LEU A 103 ? 0.75780 0.75350 0.52770 -0.31940 0.16300  -0.16150 103 LEU A CD2 
1608 N N   . SER A 104 ? 0.66540 0.55870 0.31280 -0.17980 0.12030  -0.07840 104 SER A N   
1609 C CA  . SER A 104 ? 0.73170 0.57280 0.33090 -0.15300 0.12760  -0.06550 104 SER A CA  
1610 C C   . SER A 104 ? 0.72640 0.60930 0.35040 -0.12530 0.09640  -0.06290 104 SER A C   
1611 O O   . SER A 104 ? 0.74040 0.59900 0.35110 -0.12180 0.09790  -0.06320 104 SER A O   
1612 C CB  . SER A 104 ? 0.76090 0.56320 0.30830 -0.12050 0.14130  -0.04470 104 SER A CB  
1613 O OG  . SER A 104 ? 1.05600 0.80760 0.57920 -0.14340 0.17580  -0.04500 104 SER A OG  
1619 N N   . GLY A 105 ? 0.61870 0.55950 0.27970 -0.10550 0.07170  -0.06210 105 GLY A N   
1620 C CA  . GLY A 105 ? 0.61570 0.59050 0.30600 -0.08120 0.04750  -0.06290 105 GLY A CA  
1621 C C   . GLY A 105 ? 0.47640 0.47460 0.20870 -0.10210 0.04080  -0.07080 105 GLY A C   
1622 O O   . GLY A 105 ? 0.46260 0.46300 0.20150 -0.08640 0.03030  -0.07000 105 GLY A O   
1626 N N   . ILE A 106 ? 0.51460 0.53580 0.27530 -0.13530 0.04780  -0.07860 106 ILE A N   
1627 C CA  . ILE A 106 ? 0.41130 0.46510 0.20810 -0.14980 0.04340  -0.08480 106 ILE A CA  
1628 C C   . ILE A 106 ? 0.52010 0.53410 0.28520 -0.16100 0.05450  -0.09100 106 ILE A C   
1629 O O   . ILE A 106 ? 0.58700 0.61490 0.36650 -0.15400 0.04580  -0.09220 106 ILE A O   
1630 C CB  . ILE A 106 ? 0.39780 0.49640 0.23060 -0.17840 0.05060  -0.09270 106 ILE A CB  
1631 C CG1 . ILE A 106 ? 0.45540 0.60380 0.33130 -0.16550 0.04090  -0.08630 106 ILE A CG1 
1632 C CG2 . ILE A 106 ? 0.50990 0.63690 0.36200 -0.19240 0.05370  -0.10120 106 ILE A CG2 
1633 C CD1 . ILE A 106 ? 0.45090 0.63860 0.35170 -0.18860 0.05250  -0.09200 106 ILE A CD1 
1645 N N   . ASP A 107 ? 0.67950 0.63950 0.40070 -0.18040 0.07850  -0.09610 107 ASP A N   
1646 C CA  . ASP A 107 ? 0.71030 0.61860 0.39750 -0.19560 0.09900  -0.10470 107 ASP A CA  
1647 C C   . ASP A 107 ? 0.61850 0.49690 0.27880 -0.16210 0.08990  -0.09290 107 ASP A C   
1648 O O   . ASP A 107 ? 0.75970 0.63550 0.42390 -0.16500 0.08860  -0.09940 107 ASP A O   
1649 C CB  . ASP A 107 ? 0.80800 0.64740 0.44860 -0.21670 0.13520  -0.10850 107 ASP A CB  
1650 C CG  . ASP A 107 ? 0.68020 0.47450 0.30490 -0.25010 0.16790  -0.12720 107 ASP A CG  
1651 O OD1 . ASP A 107 ? 0.85900 0.68340 0.50900 -0.25840 0.16070  -0.13860 107 ASP A OD1 
1652 O OD2 . ASP A 107 ? 1.03790 0.76540 0.62710 -0.26670 0.20500  -0.13080 107 ASP A OD2 
1657 N N   . GLN A 108 ? 0.63670 0.50080 0.27280 -0.12830 0.08320  -0.07680 108 GLN A N   
1658 C CA  . GLN A 108 ? 0.66340 0.51420 0.28090 -0.09300 0.07240  -0.06680 108 GLN A CA  
1659 C C   . GLN A 108 ? 0.63080 0.53630 0.29760 -0.08210 0.04630  -0.07160 108 GLN A C   
1660 O O   . GLN A 108 ? 0.64340 0.53480 0.30220 -0.07210 0.04360  -0.07200 108 GLN A O   
1661 C CB  . GLN A 108 ? 0.74350 0.60040 0.34200 -0.05760 0.06560  -0.05290 108 GLN A CB  
1662 C CG  . GLN A 108 ? 0.85680 0.73470 0.45890 -0.02230 0.04730  -0.04840 108 GLN A CG  
1663 C CD  . GLN A 108 ? 1.07610 0.88190 0.62580 -0.01180 0.06440  -0.03850 108 GLN A CD  
1664 O OE1 . GLN A 108 ? 0.98090 0.78490 0.53930 -0.00740 0.05720  -0.04250 108 GLN A OE1 
1665 N NE2 . GLN A 108 ? 1.33240 1.07250 0.82660 -0.00470 0.09090  -0.02390 108 GLN A NE2 
1674 N N   . GLN A 109 ? 0.49850 0.45890 0.21430 -0.08250 0.03080  -0.07350 109 GLN A N   
1675 C CA  . GLN A 109 ? 0.51550 0.51340 0.27310 -0.06930 0.01320  -0.07360 109 GLN A CA  
1676 C C   . GLN A 109 ? 0.49530 0.49750 0.26150 -0.08940 0.01750  -0.08060 109 GLN A C   
1677 O O   . GLN A 109 ? 0.54050 0.55140 0.31840 -0.07550 0.00850  -0.07950 109 GLN A O   
1678 C CB  . GLN A 109 ? 0.43400 0.47800 0.23820 -0.06990 0.00520  -0.07170 109 GLN A CB  
1679 C CG  . GLN A 109 ? 0.41540 0.49090 0.25830 -0.06090 -0.00320 -0.06960 109 GLN A CG  
1680 C CD  . GLN A 109 ? 0.33020 0.38870 0.16570 -0.03660 -0.01110 -0.06800 109 GLN A CD  
1681 O OE1 . GLN A 109 ? 0.47040 0.49400 0.26880 -0.02200 -0.01300 -0.06790 109 GLN A OE1 
1682 N NE2 . GLN A 109 ? 0.42180 0.50910 0.29160 -0.03200 -0.01300 -0.06740 109 GLN A NE2 
1691 N N   . GLN A 110 ? 0.58840 0.58870 0.35080 -0.12150 0.03190  -0.08990 110 GLN A N   
1692 C CA  . GLN A 110 ? 0.48650 0.49860 0.25760 -0.14050 0.03730  -0.10160 110 GLN A CA  
1693 C C   . GLN A 110 ? 0.45450 0.42050 0.19220 -0.13400 0.04290  -0.10420 110 GLN A C   
1694 O O   . GLN A 110 ? 0.51940 0.50190 0.26950 -0.12980 0.03620  -0.10840 110 GLN A O   
1695 C CB  . GLN A 110 ? 0.70060 0.71360 0.46980 -0.17840 0.05790  -0.11700 110 GLN A CB  
1696 C CG  . GLN A 110 ? 0.64340 0.67820 0.42520 -0.19850 0.06580  -0.13500 110 GLN A CG  
1697 C CD  . GLN A 110 ? 0.52850 0.63660 0.35390 -0.18500 0.04690  -0.13260 110 GLN A CD  
1698 O OE1 . GLN A 110 ? 0.54420 0.68170 0.38110 -0.19240 0.04810  -0.14580 110 GLN A OE1 
1699 N NE2 . GLN A 110 ? 0.45470 0.59140 0.30280 -0.16480 0.03300  -0.11650 110 GLN A NE2 
1708 N N   . ASN A 111 ? 0.56150 0.46520 0.25200 -0.13200 0.05830  -0.10070 111 ASN A N   
1709 C CA  . ASN A 111 ? 0.58150 0.43460 0.23760 -0.12520 0.06840  -0.10160 111 ASN A CA  
1710 C C   . ASN A 111 ? 0.57200 0.44630 0.24090 -0.08820 0.04500  -0.09150 111 ASN A C   
1711 O O   . ASN A 111 ? 0.64010 0.51660 0.31480 -0.08470 0.04120  -0.09620 111 ASN A O   
1712 C CB  . ASN A 111 ? 0.77370 0.54270 0.36890 -0.12870 0.09890  -0.09620 111 ASN A CB  
1713 C CG  . ASN A 111 ? 0.82140 0.56430 0.40880 -0.17210 0.13150  -0.11180 111 ASN A CG  
1714 O OD1 . ASN A 111 ? 0.81600 0.51610 0.37170 -0.17440 0.15190  -0.10460 111 ASN A OD1 
1715 N ND2 . ASN A 111 ? 0.89380 0.66950 0.51430 -0.20340 0.13710  -0.13370 111 ASN A ND2 
1722 N N   . ASN A 112 ? 0.64830 0.54750 0.32930 -0.06240 0.03000  -0.08120 112 ASN A N   
1723 C CA  . ASN A 112 ? 0.50190 0.43140 0.20590 -0.03230 0.01170  -0.07820 112 ASN A CA  
1724 C C   . ASN A 112 ? 0.50280 0.46190 0.24010 -0.03290 0.00150  -0.08190 112 ASN A C   
1725 O O   . ASN A 112 ? 0.45350 0.41330 0.19300 -0.01840 -0.00330 -0.08340 112 ASN A O   
1726 C CB  . ASN A 112 ? 0.45140 0.41650 0.17630 -0.01140 -0.00040 -0.07440 112 ASN A CB  
1727 C CG  . ASN A 112 ? 0.49410 0.43970 0.18540 -0.00700 0.00820  -0.06860 112 ASN A CG  
1728 O OD1 . ASN A 112 ? 0.63200 0.51740 0.27460 -0.00560 0.02220  -0.06170 112 ASN A OD1 
1729 N ND2 . ASN A 112 ? 0.59570 0.57960 0.30550 0.00050  0.00160  -0.06920 112 ASN A ND2 
1736 N N   . LEU A 113 ? 0.45320 0.44060 0.21650 -0.05020 0.00020  -0.08250 113 LEU A N   
1737 C CA  . LEU A 113 ? 0.42890 0.44700 0.21910 -0.04980 -0.00630 -0.08170 113 LEU A CA  
1738 C C   . LEU A 113 ? 0.39750 0.40710 0.17420 -0.06020 -0.00140 -0.09150 113 LEU A C   
1739 O O   . LEU A 113 ? 0.47790 0.49730 0.26090 -0.05030 -0.00670 -0.09040 113 LEU A O   
1740 C CB  . LEU A 113 ? 0.31510 0.37960 0.13810 -0.06470 -0.00560 -0.08050 113 LEU A CB  
1741 C CG  . LEU A 113 ? 0.39680 0.48080 0.24430 -0.05540 -0.00890 -0.07210 113 LEU A CG  
1742 C CD1 . LEU A 113 ? 0.39540 0.52580 0.27210 -0.07050 -0.00490 -0.07240 113 LEU A CD1 
1743 C CD2 . LEU A 113 ? 0.35190 0.45130 0.21970 -0.03780 -0.01260 -0.06650 113 LEU A CD2 
1755 N N   . LYS A 114 ? 0.52390 0.51010 0.27930 -0.08310 0.01250  -0.10220 114 LYS A N   
1756 C CA  . LYS A 114 ? 0.49960 0.47630 0.24460 -0.09820 0.02120  -0.11580 114 LYS A CA  
1757 C C   . LYS A 114 ? 0.52760 0.46460 0.24860 -0.08060 0.02220  -0.11370 114 LYS A C   
1758 O O   . LYS A 114 ? 0.52140 0.46530 0.24530 -0.07680 0.01920  -0.11920 114 LYS A O   
1759 C CB  . LYS A 114 ? 0.52810 0.48280 0.25800 -0.13360 0.04380  -0.13120 114 LYS A CB  
1760 C CG  . LYS A 114 ? 0.87710 0.82490 0.60220 -0.15380 0.05740  -0.15060 114 LYS A CG  
1761 C CD  . LYS A 114 ? 1.22100 1.24230 0.98240 -0.15750 0.04510  -0.16010 114 LYS A CD  
1762 C CE  . LYS A 114 ? 0.94730 0.97510 0.70870 -0.17620 0.05680  -0.18370 114 LYS A CE  
1763 N NZ  . LYS A 114 ? 1.05540 1.16260 0.84830 -0.17500 0.04380  -0.19210 114 LYS A NZ  
1777 N N   . ARG A 115 ? 0.53690 0.43380 0.23240 -0.06940 0.02770  -0.10580 115 ARG A N   
1778 C CA  . ARG A 115 ? 0.52570 0.39000 0.20140 -0.05020 0.02880  -0.10210 115 ARG A CA  
1779 C C   . ARG A 115 ? 0.50250 0.41450 0.21270 -0.02690 0.00970  -0.09950 115 ARG A C   
1780 O O   . ARG A 115 ? 0.53430 0.43830 0.24210 -0.02050 0.01030  -0.10290 115 ARG A O   
1781 C CB  . ARG A 115 ? 0.64470 0.46670 0.28760 -0.03470 0.03510  -0.08980 115 ARG A CB  
1782 C CG  . ARG A 115 ? 0.74190 0.48340 0.32920 -0.04820 0.06440  -0.08820 115 ARG A CG  
1783 C CD  . ARG A 115 ? 0.84040 0.53730 0.38580 -0.01630 0.06890  -0.06920 115 ARG A CD  
1784 N NE  . ARG A 115 ? 0.87390 0.60140 0.42840 -0.01290 0.06110  -0.06310 115 ARG A NE  
1785 C CZ  . ARG A 115 ? 1.00880 0.70500 0.53850 -0.03120 0.08140  -0.06190 115 ARG A CZ  
1786 N NH1 . ARG A 115 ? 1.05820 0.68840 0.55370 -0.05640 0.11510  -0.06790 115 ARG A NH1 
1787 N NH2 . ARG A 115 ? 1.06400 0.79730 0.60840 -0.02710 0.07130  -0.05720 115 ARG A NH2 
1801 N N   . ALA A 116 ? 0.47580 0.42880 0.21480 -0.01460 -0.00360 -0.09360 116 ALA A N   
1802 C CA  . ALA A 116 ? 0.36730 0.34150 0.13270 0.00630  -0.01390 -0.08700 116 ALA A CA  
1803 C C   . ALA A 116 ? 0.37280 0.33880 0.12790 -0.00130 -0.01460 -0.08610 116 ALA A C   
1804 O O   . ALA A 116 ? 0.37110 0.32180 0.12300 0.00290  -0.01320 -0.08130 116 ALA A O   
1805 C CB  . ALA A 116 ? 0.36250 0.31660 0.12810 -0.00180 -0.01560 -0.07160 116 ALA A CB  
1811 N N   . ILE A 117 ? 0.44350 0.43430 0.20580 -0.02130 -0.01220 -0.09040 117 ILE A N   
1812 C CA  . ILE A 117 ? 0.37690 0.39480 0.14720 -0.02650 -0.01240 -0.09200 117 ILE A CA  
1813 C C   . ILE A 117 ? 0.48550 0.48220 0.23470 -0.02890 -0.00860 -0.10470 117 ILE A C   
1814 O O   . ILE A 117 ? 0.53280 0.53600 0.27860 -0.02360 -0.00940 -0.10460 117 ILE A O   
1815 C CB  . ILE A 117 ? 0.52440 0.59310 0.31720 -0.04360 -0.01170 -0.09580 117 ILE A CB  
1816 C CG1 . ILE A 117 ? 0.49020 0.60190 0.29290 -0.04030 -0.01330 -0.09680 117 ILE A CG1 
1817 C CG2 . ILE A 117 ? 0.63010 0.69460 0.41520 -0.06830 -0.00430 -0.11200 117 ILE A CG2 
1818 C CD1 . ILE A 117 ? 0.43700 0.56970 0.25610 -0.01880 -0.01410 -0.08070 117 ILE A CD1 
1830 N N   . GLU A 118 ? 0.50000 0.47020 0.23520 -0.04000 -0.00000 -0.11560 118 GLU A N   
1831 C CA  . GLU A 118 ? 0.52710 0.47240 0.24540 -0.04670 0.00920  -0.12840 118 GLU A CA  
1832 C C   . GLU A 118 ? 0.48240 0.41490 0.19900 -0.02140 0.00520  -0.12300 118 GLU A C   
1833 O O   . GLU A 118 ? 0.58760 0.52000 0.30080 -0.01640 0.00520  -0.12860 118 GLU A O   
1834 C CB  . GLU A 118 ? 0.63870 0.54110 0.33640 -0.07200 0.02950  -0.13860 118 GLU A CB  
1835 C CG  . GLU A 118 ? 0.97440 0.89800 0.68110 -0.10400 0.03900  -0.15220 118 GLU A CG  
1836 C CD  . GLU A 118 ? 1.22840 1.19800 0.95190 -0.11700 0.03700  -0.16910 118 GLU A CD  
1837 O OE1 . GLU A 118 ? 1.16280 1.11430 0.87620 -0.12600 0.04760  -0.18370 118 GLU A OE1 
1838 O OE2 . GLU A 118 ? 1.12020 1.14650 0.86710 -0.11800 0.02620  -0.16810 118 GLU A OE2 
1845 N N   . ALA A 119 ? 0.53010 0.46020 0.25430 -0.00970 0.00400  -0.11490 119 ALA A N   
1846 C CA  . ALA A 119 ? 0.49460 0.42180 0.22780 0.00040  0.00570  -0.11160 119 ALA A CA  
1847 C C   . ALA A 119 ? 0.45980 0.42950 0.22120 -0.00040 0.00360  -0.10990 119 ALA A C   
1848 O O   . ALA A 119 ? 0.51370 0.46560 0.26700 0.00290  0.00810  -0.11250 119 ALA A O   
1849 C CB  . ALA A 119 ? 0.49270 0.40690 0.22860 0.00970  0.00370  -0.09940 119 ALA A CB  
1855 N N   . ILE A 120 ? 0.51790 0.46010 0.26160 -0.01680 0.00430  -0.08950 120 ILE A N   
1856 C CA  . ILE A 120 ? 0.41980 0.38660 0.17110 -0.00100 0.00110  -0.08650 120 ILE A CA  
1857 C C   . ILE A 120 ? 0.41940 0.38170 0.14910 -0.00060 0.00090  -0.09200 120 ILE A C   
1858 O O   . ILE A 120 ? 0.49450 0.46740 0.22840 0.00410  0.00630  -0.09350 120 ILE A O   
1859 C CB  . ILE A 120 ? 0.43980 0.44950 0.21820 0.00770  -0.00430 -0.07780 120 ILE A CB  
1860 C CG1 . ILE A 120 ? 0.43460 0.44990 0.23680 0.01500  -0.00540 -0.07430 120 ILE A CG1 
1861 C CG2 . ILE A 120 ? 0.52870 0.58250 0.32720 0.02310  -0.00140 -0.07250 120 ILE A CG2 
1862 C CD1 . ILE A 120 ? 0.44490 0.48410 0.27950 0.03920  -0.00190 -0.07260 120 ILE A CD1 
1874 N N   . LYS A 121 ? 0.55180 0.52170 0.27080 -0.00320 -0.00530 -0.10200 121 LYS A N   
1875 C CA  . LYS A 121 ? 0.57670 0.56500 0.28910 -0.00990 -0.00380 -0.11480 121 LYS A CA  
1876 C C   . LYS A 121 ? 0.66240 0.61250 0.35470 -0.00000 -0.00040 -0.12360 121 LYS A C   
1877 O O   . LYS A 121 ? 0.66780 0.62050 0.35040 0.00080  0.00320  -0.12510 121 LYS A O   
1878 C CB  . LYS A 121 ? 0.53050 0.54540 0.25110 -0.03180 -0.00290 -0.13170 121 LYS A CB  
1879 C CG  . LYS A 121 ? 0.67540 0.73150 0.39860 -0.04350 -0.00150 -0.14690 121 LYS A CG  
1880 C CD  . LYS A 121 ? 0.72200 0.82030 0.46280 -0.06870 0.00120  -0.16440 121 LYS A CD  
1881 C CE  . LYS A 121 ? 0.94790 1.00400 0.68180 -0.09030 0.01380  -0.17880 121 LYS A CE  
1882 N NZ  . LYS A 121 ? 1.05070 1.14550 0.80070 -0.12260 0.02420  -0.20510 121 LYS A NZ  
1896 N N   . HIS A 122 ? 0.55080 0.49070 0.25510 0.00420  0.00120  -0.13270 122 HIS A N   
1897 C CA  . HIS A 122 ? 0.61810 0.54430 0.32290 0.00330  0.00990  -0.14620 122 HIS A CA  
1898 C C   . HIS A 122 ? 0.49210 0.44410 0.22780 0.00950  0.01320  -0.13900 122 HIS A C   
1899 O O   . HIS A 122 ? 0.58800 0.53140 0.31910 0.01090  0.01850  -0.14550 122 HIS A O   
1900 C CB  . HIS A 122 ? 0.59340 0.46780 0.28710 -0.01050 0.02430  -0.14660 122 HIS A CB  
1901 C CG  . HIS A 122 ? 1.00710 0.85870 0.68400 -0.03540 0.03530  -0.15450 122 HIS A CG  
1902 N ND1 . HIS A 122 ? 1.07990 0.88410 0.73800 -0.04270 0.04840  -0.14800 122 HIS A ND1 
1903 C CD2 . HIS A 122 ? 0.95100 0.82130 0.62790 -0.05810 0.03940  -0.16960 122 HIS A CD2 
1904 C CE1 . HIS A 122 ? 1.04740 0.84200 0.69790 -0.07070 0.06270  -0.16000 122 HIS A CE1 
1905 N NE2 . HIS A 122 ? 0.98990 0.83000 0.65700 -0.08240 0.05700  -0.17520 122 HIS A NE2 
1913 N N   . LEU A 123 ? 0.50180 0.45380 0.24830 0.00430  0.01650  -0.12410 123 LEU A N   
1914 C CA  . LEU A 123 ? 0.48010 0.41390 0.23070 0.02190  0.01800  -0.11330 123 LEU A CA  
1915 C C   . LEU A 123 ? 0.56820 0.51860 0.31080 0.02130  0.02230  -0.11180 123 LEU A C   
1916 O O   . LEU A 123 ? 0.64630 0.58780 0.38920 0.03100  0.02650  -0.11520 123 LEU A O   
1917 C CB  . LEU A 123 ? 0.47970 0.41800 0.25070 0.03830  0.01200  -0.09970 123 LEU A CB  
1918 C CG  . LEU A 123 ? 0.48040 0.41910 0.27390 0.06320  0.01380  -0.09460 123 LEU A CG  
1919 C CD1 . LEU A 123 ? 0.65040 0.55910 0.44370 0.07130  0.01450  -0.09870 123 LEU A CD1 
1920 C CD2 . LEU A 123 ? 0.46430 0.41920 0.28840 0.07700  0.01110  -0.08900 123 LEU A CD2 
1932 N N   . LEU A 124 ? 0.62860 0.59930 0.36200 0.01790  0.01920  -0.10350 124 LEU A N   
1933 C CA  . LEU A 124 ? 0.60940 0.60900 0.34040 0.03050  0.02030  -0.09890 124 LEU A CA  
1934 C C   . LEU A 124 ? 0.58680 0.56590 0.28510 0.01720  0.02410  -0.11250 124 LEU A C   
1935 O O   . LEU A 124 ? 0.70250 0.69330 0.40070 0.02750  0.02930  -0.11330 124 LEU A O   
1936 C CB  . LEU A 124 ? 0.53250 0.57850 0.27340 0.03540  0.01380  -0.08950 124 LEU A CB  
1937 C CG  . LEU A 124 ? 0.67930 0.77330 0.43280 0.06000  0.01770  -0.07740 124 LEU A CG  
1938 C CD1 . LEU A 124 ? 0.82030 0.95740 0.59690 0.07140  0.01520  -0.06340 124 LEU A CD1 
1939 C CD2 . LEU A 124 ? 1.05660 1.17110 0.78930 0.05370  0.01540  -0.08700 124 LEU A CD2 
1951 N N   . GLN A 125 ? 0.75760 0.69980 0.42980 0.00600  0.01980  -0.12190 125 GLN A N   
1952 C CA  . GLN A 125 ? 0.66100 0.59090 0.31180 0.00980  0.01830  -0.13890 125 GLN A CA  
1953 C C   . GLN A 125 ? 0.73490 0.62620 0.38420 0.01910  0.02580  -0.13630 125 GLN A C   
1954 O O   . GLN A 125 ? 0.90490 0.80090 0.54160 0.01790  0.03170  -0.14420 125 GLN A O   
1955 C CB  . GLN A 125 ? 0.80310 0.73730 0.45850 0.00130  0.01360  -0.16020 125 GLN A CB  
1956 C CG  . GLN A 125 ? 0.84560 0.82810 0.51230 -0.02140 0.01190  -0.16800 125 GLN A CG  
1957 C CD  . GLN A 125 ? 0.95630 0.93300 0.63340 -0.04500 0.01800  -0.18490 125 GLN A CD  
1958 O OE1 . GLN A 125 ? 1.05870 0.99200 0.73310 -0.04730 0.02660  -0.18820 125 GLN A OE1 
1959 N NE2 . GLN A 125 ? 0.91030 0.93430 0.60220 -0.06550 0.01780  -0.19610 125 GLN A NE2 
1968 N N   . LEU A 126 ? 0.76010 0.72690 0.49150 0.00960  0.02970  -0.15610 126 LEU A N   
1969 C CA  . LEU A 126 ? 0.60510 0.52890 0.32890 0.01940  0.03760  -0.15850 126 LEU A CA  
1970 C C   . LEU A 126 ? 0.64130 0.56410 0.36430 0.02940  0.04380  -0.14470 126 LEU A C   
1971 O O   . LEU A 126 ? 0.90390 0.82710 0.62030 0.03130  0.05040  -0.15120 126 LEU A O   
1972 C CB  . LEU A 126 ? 0.79050 0.66470 0.51660 0.03120  0.03610  -0.14610 126 LEU A CB  
1973 C CG  . LEU A 126 ? 0.89540 0.71920 0.60380 0.03050  0.04050  -0.15020 126 LEU A CG  
1974 C CD1 . LEU A 126 ? 1.13310 0.95800 0.82530 0.01400  0.04180  -0.16160 126 LEU A CD1 
1975 C CD2 . LEU A 126 ? 1.01220 0.80580 0.72280 0.04720  0.03720  -0.13210 126 LEU A CD2 
1987 N N   . THR A 127 ? 0.69420 0.61920 0.43010 0.04550  0.03940  -0.12570 127 THR A N   
1988 C CA  . THR A 127 ? 0.75900 0.69470 0.50690 0.06930  0.04350  -0.11260 127 THR A CA  
1989 C C   . THR A 127 ? 0.63860 0.60020 0.36470 0.06810  0.04900  -0.11360 127 THR A C   
1990 O O   . THR A 127 ? 0.75590 0.72140 0.48770 0.08760  0.05680  -0.10650 127 THR A O   
1991 C CB  . THR A 127 ? 0.64270 0.59450 0.41210 0.08330  0.04030  -0.09800 127 THR A CB  
1992 O OG1 . THR A 127 ? 0.81700 0.74630 0.61020 0.08820  0.03650  -0.09800 127 THR A OG1 
1993 C CG2 . THR A 127 ? 0.77900 0.75220 0.56330 0.10680  0.05070  -0.08370 127 THR A CG2 
2001 N N   . CYS A 128 ? 0.90220 0.87640 0.60090 0.04540  0.04620  -0.12220 128 CYS A N   
2002 C CA  . CYS A 128 ? 0.82690 0.82900 0.50360 0.04850  0.04710  -0.12290 128 CYS A CA  
2003 C C   . CYS A 128 ? 0.75590 0.73140 0.39390 0.02620  0.04680  -0.14300 128 CYS A C   
2004 O O   . CYS A 128 ? 0.92790 0.88550 0.54860 0.02470  0.05460  -0.15340 128 CYS A O   
2005 C CB  . CYS A 128 ? 0.73810 0.79390 0.42410 0.06150  0.03870  -0.10810 128 CYS A CB  
2006 S SG  . CYS A 128 ? 0.67200 0.74260 0.39570 0.08940  0.04070  -0.08270 128 CYS A SG  
# 
