data_9FZF
# 
_entry.id   9FZF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9FZF         pdb_00009fzf 10.2210/pdb9fzf/pdb 
WWPDB D_1292139779 ?            ?                   
# 
_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       2025-03-19 
_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                        9FZF 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-05 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  . 9FVR      unspecified       
PDB  . 9FXK      unspecified       
EMDB . EMD-50819 'other EM volume' 
EMDB . EMD-50849 'other EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              derek.logan@biochemistry.lu.se 
_pdbx_contact_author.name_first         Derek 
_pdbx_contact_author.name_last          Logan 
_pdbx_contact_author.name_mi            T. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0098-8560 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bimai, O.'           1 0000-0003-0562-7251 
'Rozman Grinberg, I.' 2 0000-0003-3094-1998 
'Sjoberg, B.M.'       3 0000-0001-5953-3360 
'Logan, D.T.'         4 0000-0002-0098-8560 
# 
_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            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Bacterial transcriptional repressor NrdR - a flexible multifactorial nucleotide sensor.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.70037 
_citation.pdbx_database_id_PubMed   40029022 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rozman Grinberg, I.'   1  ?                   
primary 'Bimai, O.'             2  ?                   
primary 'Shahid, S.'            3  ?                   
primary 'Philipp, L.'           4  ?                   
primary 'Martinez-Carranza, M.' 5  ?                   
primary 'Banerjee, I.'          6  ?                   
primary 'Lundin, D.'            7  ?                   
primary 'Stenmark, P.'          8  0000-0003-4777-3417 
primary 'Sjoberg, B.M.'         9  ?                   
primary 'Logan, D.T.'           10 0000-0002-0098-8560 
# 
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 'Transcriptional repressor NrdR'    18769.650 2   ? ? ? ? 
2 non-polymer syn 
;2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
;
491.182   2   ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"          427.201   2   ? ? ? ? 
4 non-polymer syn 'ZINC ION'                          65.409    2   ? ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                     24.305    2   ? ? ? ? 
6 water       nat water                               18.015    161 ? ? ? ? 
# 
_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       
;MHCPFCFAVDTKVIDSRLVGEGSSVRRRRQCLVCNERFTTFEVAELVMPRVVKSNDVREPFNEEKLRSGMLRALEKRPVS
SDDVEMAINHIKSQLRATGEREVPSKMIGNLVMEQLKKLDKVAYIRFASVYRSFEDIKDFGEEIARLEDKLAAALEHHHH
HH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHCPFCFAVDTKVIDSRLVGEGSSVRRRRQCLVCNERFTTFEVAELVMPRVVKSNDVREPFNEEKLRSGMLRALEKRPVS
SDDVEMAINHIKSQLRATGEREVPSKMIGNLVMEQLKKLDKVAYIRFASVYRSFEDIKDFGEEIARLEDKLAAALEHHHH
HH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
;
DTP 
3 "ADENOSINE-5'-DIPHOSPHATE"          ADP 
4 'ZINC ION'                          ZN  
5 'MAGNESIUM ION'                     MG  
6 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   HIS n 
1 3   CYS n 
1 4   PRO n 
1 5   PHE n 
1 6   CYS n 
1 7   PHE n 
1 8   ALA n 
1 9   VAL n 
1 10  ASP n 
1 11  THR n 
1 12  LYS n 
1 13  VAL n 
1 14  ILE n 
1 15  ASP n 
1 16  SER n 
1 17  ARG n 
1 18  LEU n 
1 19  VAL n 
1 20  GLY n 
1 21  GLU n 
1 22  GLY n 
1 23  SER n 
1 24  SER n 
1 25  VAL n 
1 26  ARG n 
1 27  ARG n 
1 28  ARG n 
1 29  ARG n 
1 30  GLN n 
1 31  CYS n 
1 32  LEU n 
1 33  VAL n 
1 34  CYS n 
1 35  ASN n 
1 36  GLU n 
1 37  ARG n 
1 38  PHE n 
1 39  THR n 
1 40  THR n 
1 41  PHE n 
1 42  GLU n 
1 43  VAL n 
1 44  ALA n 
1 45  GLU n 
1 46  LEU n 
1 47  VAL n 
1 48  MET n 
1 49  PRO n 
1 50  ARG n 
1 51  VAL n 
1 52  VAL n 
1 53  LYS n 
1 54  SER n 
1 55  ASN n 
1 56  ASP n 
1 57  VAL n 
1 58  ARG n 
1 59  GLU n 
1 60  PRO n 
1 61  PHE n 
1 62  ASN n 
1 63  GLU n 
1 64  GLU n 
1 65  LYS n 
1 66  LEU n 
1 67  ARG n 
1 68  SER n 
1 69  GLY n 
1 70  MET n 
1 71  LEU n 
1 72  ARG n 
1 73  ALA n 
1 74  LEU n 
1 75  GLU n 
1 76  LYS n 
1 77  ARG n 
1 78  PRO n 
1 79  VAL n 
1 80  SER n 
1 81  SER n 
1 82  ASP n 
1 83  ASP n 
1 84  VAL n 
1 85  GLU n 
1 86  MET n 
1 87  ALA n 
1 88  ILE n 
1 89  ASN n 
1 90  HIS n 
1 91  ILE n 
1 92  LYS n 
1 93  SER n 
1 94  GLN n 
1 95  LEU n 
1 96  ARG n 
1 97  ALA n 
1 98  THR n 
1 99  GLY n 
1 100 GLU n 
1 101 ARG n 
1 102 GLU n 
1 103 VAL n 
1 104 PRO n 
1 105 SER n 
1 106 LYS n 
1 107 MET n 
1 108 ILE n 
1 109 GLY n 
1 110 ASN n 
1 111 LEU n 
1 112 VAL n 
1 113 MET n 
1 114 GLU n 
1 115 GLN n 
1 116 LEU n 
1 117 LYS n 
1 118 LYS n 
1 119 LEU n 
1 120 ASP n 
1 121 LYS n 
1 122 VAL n 
1 123 ALA n 
1 124 TYR n 
1 125 ILE n 
1 126 ARG n 
1 127 PHE n 
1 128 ALA n 
1 129 SER n 
1 130 VAL n 
1 131 TYR n 
1 132 ARG n 
1 133 SER n 
1 134 PHE n 
1 135 GLU n 
1 136 ASP n 
1 137 ILE n 
1 138 LYS n 
1 139 ASP n 
1 140 PHE n 
1 141 GLY n 
1 142 GLU n 
1 143 GLU n 
1 144 ILE n 
1 145 ALA n 
1 146 ARG n 
1 147 LEU n 
1 148 GLU n 
1 149 ASP n 
1 150 LYS n 
1 151 LEU n 
1 152 ALA n 
1 153 ALA n 
1 154 ALA n 
1 155 LEU n 
1 156 GLU n 
1 157 HIS n 
1 158 HIS n 
1 159 HIS n 
1 160 HIS n 
1 161 HIS n 
1 162 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   162 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'nrdR, ybaD, b0413, JW0403' 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"          ? 'C10 H15 N5 O10 P2' 427.201 
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 
DTP non-polymer         . 
;2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
;
? 'C10 H16 N5 O12 P3' 491.182 
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 
MG  non-polymer         . 'MAGNESIUM ION'                     ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE                       ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                             ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                              ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                           ? 'C4 H9 N O3'        119.119 
TYR 'L-peptide linking' y TYROSINE                            ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                              ? 'C5 H11 N O2'       117.146 
ZN  non-polymer         . 'ZINC ION'                          ? 'Zn 2'              65.409  
# 
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   1   MET MET A . n 
A 1 2   HIS 2   2   2   HIS HIS A . n 
A 1 3   CYS 3   3   3   CYS CYS A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  ARG 26  26  26  ARG ARG A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  CYS 31  31  31  CYS CYS A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  CYS 34  34  34  CYS CYS A . n 
A 1 35  ASN 35  35  35  ASN ASN A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  PHE 41  41  41  PHE PHE A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  MET 48  48  48  MET MET A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  VAL 57  57  57  VAL VAL 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  PRO 60  60  60  PRO PRO A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  MET 70  70  70  MET MET A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ARG 77  77  77  ARG ARG A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  MET 86  86  86  MET MET A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ARG 101 101 101 ARG ARG A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 MET 107 107 107 MET MET A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 MET 113 113 113 MET MET A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 GLN 115 115 115 GLN GLN A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 TYR 124 124 124 TYR TYR A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 GLU 142 142 142 GLU GLU A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 LYS 150 150 ?   ?   ?   A . n 
A 1 151 LEU 151 151 ?   ?   ?   A . n 
A 1 152 ALA 152 152 ?   ?   ?   A . n 
A 1 153 ALA 153 153 ?   ?   ?   A . n 
A 1 154 ALA 154 154 ?   ?   ?   A . n 
A 1 155 LEU 155 155 ?   ?   ?   A . n 
A 1 156 GLU 156 156 ?   ?   ?   A . n 
A 1 157 HIS 157 157 ?   ?   ?   A . n 
A 1 158 HIS 158 158 ?   ?   ?   A . n 
A 1 159 HIS 159 159 ?   ?   ?   A . n 
A 1 160 HIS 160 160 ?   ?   ?   A . n 
A 1 161 HIS 161 161 ?   ?   ?   A . n 
A 1 162 HIS 162 162 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   HIS 2   2   2   HIS HIS B . n 
B 1 3   CYS 3   3   3   CYS CYS B . n 
B 1 4   PRO 4   4   4   PRO PRO B . n 
B 1 5   PHE 5   5   5   PHE PHE B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   ALA 8   8   8   ALA ALA B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  THR 11  11  11  THR THR B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  ILE 14  14  14  ILE ILE B . n 
B 1 15  ASP 15  15  15  ASP ASP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  ARG 17  17  17  ARG ARG B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  SER 24  24  24  SER SER B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  ARG 26  26  26  ARG ARG B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  ARG 28  28  28  ARG ARG B . n 
B 1 29  ARG 29  29  29  ARG ARG B . n 
B 1 30  GLN 30  30  30  GLN GLN B . n 
B 1 31  CYS 31  31  31  CYS CYS B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  CYS 34  34  34  CYS CYS B . n 
B 1 35  ASN 35  35  35  ASN ASN B . n 
B 1 36  GLU 36  36  36  GLU GLU B . n 
B 1 37  ARG 37  37  37  ARG ARG B . n 
B 1 38  PHE 38  38  38  PHE PHE B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  PHE 41  41  41  PHE PHE B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  VAL 43  43  43  VAL VAL B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  GLU 45  45  45  GLU GLU B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  MET 48  48  48  MET MET B . n 
B 1 49  PRO 49  49  49  PRO PRO B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  LYS 53  53  53  LYS LYS B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  GLU 59  59  59  GLU GLU B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  PHE 61  61  61  PHE PHE B . n 
B 1 62  ASN 62  62  62  ASN ASN B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  LYS 65  65  65  LYS LYS B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  ARG 67  67  67  ARG ARG B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  MET 70  70  70  MET MET B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ARG 72  72  72  ARG ARG B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  ARG 77  77  77  ARG ARG B . n 
B 1 78  PRO 78  78  78  PRO PRO B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  VAL 84  84  84  VAL VAL B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  MET 86  86  86  MET MET B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  ILE 88  88  88  ILE ILE B . n 
B 1 89  ASN 89  89  89  ASN ASN B . n 
B 1 90  HIS 90  90  90  HIS HIS B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  GLN 94  94  94  GLN GLN B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ARG 101 101 101 ARG ARG B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 PRO 104 104 104 PRO PRO B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LYS 106 106 106 LYS LYS B . n 
B 1 107 MET 107 107 107 MET MET B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 MET 113 113 113 MET MET B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 GLN 115 115 115 GLN GLN B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 LYS 117 117 117 LYS LYS B . n 
B 1 118 LYS 118 118 118 LYS LYS B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 TYR 124 124 124 TYR TYR B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 ARG 126 126 126 ARG ARG B . n 
B 1 127 PHE 127 127 127 PHE PHE B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 VAL 130 130 130 VAL VAL B . n 
B 1 131 TYR 131 131 131 TYR TYR B . n 
B 1 132 ARG 132 132 132 ARG ARG B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 GLU 142 142 142 GLU GLU B . n 
B 1 143 GLU 143 143 143 GLU GLU B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 ARG 146 146 146 ARG ARG B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 ASP 149 149 149 ASP ASP B . n 
B 1 150 LYS 150 150 ?   ?   ?   B . n 
B 1 151 LEU 151 151 ?   ?   ?   B . n 
B 1 152 ALA 152 152 ?   ?   ?   B . n 
B 1 153 ALA 153 153 ?   ?   ?   B . n 
B 1 154 ALA 154 154 ?   ?   ?   B . n 
B 1 155 LEU 155 155 ?   ?   ?   B . n 
B 1 156 GLU 156 156 ?   ?   ?   B . n 
B 1 157 HIS 157 157 ?   ?   ?   B . n 
B 1 158 HIS 158 158 ?   ?   ?   B . n 
B 1 159 HIS 159 159 ?   ?   ?   B . n 
B 1 160 HIS 160 160 ?   ?   ?   B . n 
B 1 161 HIS 161 161 ?   ?   ?   B . n 
B 1 162 HIS 162 162 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 DTP ? ? DTP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 DTP 1   200 200 DTP DTP A . 
D 3 ADP 1   201 201 ADP ADP A . 
E 4 ZN  1   202 202 ZN  ZN  A . 
F 5 MG  1   203 203 MG  MG  A . 
G 2 DTP 1   200 200 DTP DTP B . 
H 3 ADP 1   201 201 ADP ADP B . 
I 4 ZN  1   202 202 ZN  ZN  B . 
J 5 MG  1   203 203 MG  MG  B . 
K 6 HOH 1   301 151 HOH HOH A . 
K 6 HOH 2   302 98  HOH HOH A . 
K 6 HOH 3   303 5   HOH HOH A . 
K 6 HOH 4   304 125 HOH HOH A . 
K 6 HOH 5   305 60  HOH HOH A . 
K 6 HOH 6   306 100 HOH HOH A . 
K 6 HOH 7   307 49  HOH HOH A . 
K 6 HOH 8   308 177 HOH HOH A . 
K 6 HOH 9   309 44  HOH HOH A . 
K 6 HOH 10  310 23  HOH HOH A . 
K 6 HOH 11  311 61  HOH HOH A . 
K 6 HOH 12  312 84  HOH HOH A . 
K 6 HOH 13  313 160 HOH HOH A . 
K 6 HOH 14  314 21  HOH HOH A . 
K 6 HOH 15  315 43  HOH HOH A . 
K 6 HOH 16  316 85  HOH HOH A . 
K 6 HOH 17  317 101 HOH HOH A . 
K 6 HOH 18  318 14  HOH HOH A . 
K 6 HOH 19  319 78  HOH HOH A . 
K 6 HOH 20  320 83  HOH HOH A . 
K 6 HOH 21  321 86  HOH HOH A . 
K 6 HOH 22  322 104 HOH HOH A . 
K 6 HOH 23  323 20  HOH HOH A . 
K 6 HOH 24  324 73  HOH HOH A . 
K 6 HOH 25  325 9   HOH HOH A . 
K 6 HOH 26  326 2   HOH HOH A . 
K 6 HOH 27  327 167 HOH HOH A . 
K 6 HOH 28  328 72  HOH HOH A . 
K 6 HOH 29  329 82  HOH HOH A . 
K 6 HOH 30  330 52  HOH HOH A . 
K 6 HOH 31  331 17  HOH HOH A . 
K 6 HOH 32  332 63  HOH HOH A . 
K 6 HOH 33  333 120 HOH HOH A . 
K 6 HOH 34  334 161 HOH HOH A . 
K 6 HOH 35  335 107 HOH HOH A . 
K 6 HOH 36  336 162 HOH HOH A . 
K 6 HOH 37  337 163 HOH HOH A . 
K 6 HOH 38  338 166 HOH HOH A . 
K 6 HOH 39  339 95  HOH HOH A . 
K 6 HOH 40  340 194 HOH HOH A . 
K 6 HOH 41  341 188 HOH HOH A . 
K 6 HOH 42  342 115 HOH HOH A . 
K 6 HOH 43  343 155 HOH HOH A . 
K 6 HOH 44  344 164 HOH HOH A . 
K 6 HOH 45  345 51  HOH HOH A . 
K 6 HOH 46  346 128 HOH HOH A . 
K 6 HOH 47  347 156 HOH HOH A . 
K 6 HOH 48  348 71  HOH HOH A . 
K 6 HOH 49  349 126 HOH HOH A . 
K 6 HOH 50  350 159 HOH HOH A . 
K 6 HOH 51  351 62  HOH HOH A . 
K 6 HOH 52  352 131 HOH HOH A . 
K 6 HOH 53  353 64  HOH HOH A . 
K 6 HOH 54  354 118 HOH HOH A . 
L 6 HOH 1   301 199 HOH HOH B . 
L 6 HOH 2   302 145 HOH HOH B . 
L 6 HOH 3   303 42  HOH HOH B . 
L 6 HOH 4   304 149 HOH HOH B . 
L 6 HOH 5   305 30  HOH HOH B . 
L 6 HOH 6   306 33  HOH HOH B . 
L 6 HOH 7   307 197 HOH HOH B . 
L 6 HOH 8   308 76  HOH HOH B . 
L 6 HOH 9   309 133 HOH HOH B . 
L 6 HOH 10  310 191 HOH HOH B . 
L 6 HOH 11  311 66  HOH HOH B . 
L 6 HOH 12  312 46  HOH HOH B . 
L 6 HOH 13  313 113 HOH HOH B . 
L 6 HOH 14  314 56  HOH HOH B . 
L 6 HOH 15  315 22  HOH HOH B . 
L 6 HOH 16  316 8   HOH HOH B . 
L 6 HOH 17  317 70  HOH HOH B . 
L 6 HOH 18  318 68  HOH HOH B . 
L 6 HOH 19  319 3   HOH HOH B . 
L 6 HOH 20  320 39  HOH HOH B . 
L 6 HOH 21  321 178 HOH HOH B . 
L 6 HOH 22  322 31  HOH HOH B . 
L 6 HOH 23  323 124 HOH HOH B . 
L 6 HOH 24  324 48  HOH HOH B . 
L 6 HOH 25  325 29  HOH HOH B . 
L 6 HOH 26  326 88  HOH HOH B . 
L 6 HOH 27  327 90  HOH HOH B . 
L 6 HOH 28  328 28  HOH HOH B . 
L 6 HOH 29  329 184 HOH HOH B . 
L 6 HOH 30  330 134 HOH HOH B . 
L 6 HOH 31  331 146 HOH HOH B . 
L 6 HOH 32  332 40  HOH HOH B . 
L 6 HOH 33  333 108 HOH HOH B . 
L 6 HOH 34  334 170 HOH HOH B . 
L 6 HOH 35  335 59  HOH HOH B . 
L 6 HOH 36  336 200 HOH HOH B . 
L 6 HOH 37  337 15  HOH HOH B . 
L 6 HOH 38  338 54  HOH HOH B . 
L 6 HOH 39  339 26  HOH HOH B . 
L 6 HOH 40  340 96  HOH HOH B . 
L 6 HOH 41  341 47  HOH HOH B . 
L 6 HOH 42  342 102 HOH HOH B . 
L 6 HOH 43  343 67  HOH HOH B . 
L 6 HOH 44  344 190 HOH HOH B . 
L 6 HOH 45  345 157 HOH HOH B . 
L 6 HOH 46  346 79  HOH HOH B . 
L 6 HOH 47  347 137 HOH HOH B . 
L 6 HOH 48  348 169 HOH HOH B . 
L 6 HOH 49  349 181 HOH HOH B . 
L 6 HOH 50  350 93  HOH HOH B . 
L 6 HOH 51  351 53  HOH HOH B . 
L 6 HOH 52  352 193 HOH HOH B . 
L 6 HOH 53  353 103 HOH HOH B . 
L 6 HOH 54  354 80  HOH HOH B . 
L 6 HOH 55  355 41  HOH HOH B . 
L 6 HOH 56  356 37  HOH HOH B . 
L 6 HOH 57  357 65  HOH HOH B . 
L 6 HOH 58  358 179 HOH HOH B . 
L 6 HOH 59  359 174 HOH HOH B . 
L 6 HOH 60  360 138 HOH HOH B . 
L 6 HOH 61  361 19  HOH HOH B . 
L 6 HOH 62  362 150 HOH HOH B . 
L 6 HOH 63  363 114 HOH HOH B . 
L 6 HOH 64  364 152 HOH HOH B . 
L 6 HOH 65  365 38  HOH HOH B . 
L 6 HOH 66  366 185 HOH HOH B . 
L 6 HOH 67  367 12  HOH HOH B . 
L 6 HOH 68  368 92  HOH HOH B . 
L 6 HOH 69  369 112 HOH HOH B . 
L 6 HOH 70  370 172 HOH HOH B . 
L 6 HOH 71  371 171 HOH HOH B . 
L 6 HOH 72  372 109 HOH HOH B . 
L 6 HOH 73  373 186 HOH HOH B . 
L 6 HOH 74  374 187 HOH HOH B . 
L 6 HOH 75  375 154 HOH HOH B . 
L 6 HOH 76  376 55  HOH HOH B . 
L 6 HOH 77  377 35  HOH HOH B . 
L 6 HOH 78  378 58  HOH HOH B . 
L 6 HOH 79  379 144 HOH HOH B . 
L 6 HOH 80  380 36  HOH HOH B . 
L 6 HOH 81  381 87  HOH HOH B . 
L 6 HOH 82  382 129 HOH HOH B . 
L 6 HOH 83  383 111 HOH HOH B . 
L 6 HOH 84  384 195 HOH HOH B . 
L 6 HOH 85  385 168 HOH HOH B . 
L 6 HOH 86  386 91  HOH HOH B . 
L 6 HOH 87  387 180 HOH HOH B . 
L 6 HOH 88  388 45  HOH HOH B . 
L 6 HOH 89  389 25  HOH HOH B . 
L 6 HOH 90  390 110 HOH HOH B . 
L 6 HOH 91  391 32  HOH HOH B . 
L 6 HOH 92  392 34  HOH HOH B . 
L 6 HOH 93  393 196 HOH HOH B . 
L 6 HOH 94  394 27  HOH HOH B . 
L 6 HOH 95  395 153 HOH HOH B . 
L 6 HOH 96  396 198 HOH HOH B . 
L 6 HOH 97  397 13  HOH HOH B . 
L 6 HOH 98  398 132 HOH HOH B . 
L 6 HOH 99  399 74  HOH HOH B . 
L 6 HOH 100 400 89  HOH HOH B . 
L 6 HOH 101 401 69  HOH HOH B . 
L 6 HOH 102 402 176 HOH HOH B . 
L 6 HOH 103 403 57  HOH HOH B . 
L 6 HOH 104 404 192 HOH HOH B . 
L 6 HOH 105 405 16  HOH HOH B . 
L 6 HOH 106 406 130 HOH HOH B . 
L 6 HOH 107 407 182 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? 2.11.8      1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 15-Mar-2019 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FZF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     147.126 
_cell.length_a_esd                 ? 
_cell.length_b                     147.126 
_cell.length_b_esd                 ? 
_cell.length_c                     85.805 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9FZF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                180 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 62 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FZF 
_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             3.57 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          65.55 
_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              5.5 
_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    '0.1 M Bis-Tris pH 5.5, 0.2 M ammonium acetate, 45% (v/v) MPD' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-01-19 
_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   0.9795 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FZF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.444 
_reflns.d_resolution_low                               127.42 
_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                                     10132 
_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                           95.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                39.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.315 
_reflns.pdbx_Rpim_I_all                                0.05 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.310 
_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                                    2.444 
_reflns_shell.d_res_low                                     2.699 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             517 
_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                               41.2 
_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                               2.667 
_reflns_shell.pdbx_Rpim_I_all                               0.413 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.912 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          84.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.635 
_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]                            3.3756 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            3.3756 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -6.7511 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.34 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.897 
_refine.correlation_coeff_Fo_to_Fc_free          0.795 
_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                                 9FZF 
_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                            2.444 
_refine.ls_d_res_low                             127.42 
_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                     10312 
_refine.ls_number_reflns_R_free                  494 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    49.6 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2181 
_refine.ls_R_factor_R_free                       0.2831 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2149 
_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                    ? 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.458 
_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                            ? 
_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_analyze.entry_id                        9FZF 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.36 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.444 
_refine_hist.d_res_low                        127.42 
_refine_hist.number_atoms_solvent             161 
_refine_hist.number_atoms_total               2683 
_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        2404 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         118 
_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' ? 0.007 ? 2558 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.85  ? 3452 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 980  ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 442  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2558 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 322  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 2106 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.76  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 18.14 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.444 
_refine_ls_shell.d_res_low                        2.67 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             11 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               9.1 
_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                  0.2723 
_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                  0.3244 
# 
_struct.entry_id                     9FZF 
_struct.title                        'Transcriptional repressor NrdR from E. coli, ADP/dATP bound state' 
_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        9FZF 
_struct_keywords.text            
'ribonucleotide reductase, transcriptional repressor, ATP-cone domain, Zn-ribbon domain, DNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'DNA BINDING 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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 6 ? 
L N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NRDR_ECOLI 
_struct_ref.pdbx_db_accession          P0A8D0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MHCPFCFAVDTKVIDSRLVGEGSSVRRRRQCLVCNERFTTFEVAELVMPRVVKSNDVREPFNEEKLRSGMLRALEKRPVS
SDDVEMAINHIKSQLRATGEREVPSKMIGNLVMEQLKKLDKVAYIRFASVYRSFEDIKEFGEEIARLED
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FZF A 1 ? 149 ? P0A8D0 1 ? 149 ? 1 149 
2 1 9FZF B 1 ? 149 ? P0A8D0 1 ? 149 ? 1 149 
# 
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 9FZF ASP A 139 ? UNP P0A8D0 GLU 139 conflict         139 1  
1 9FZF LYS A 150 ? UNP P0A8D0 ?   ?   'expression tag' 150 2  
1 9FZF LEU A 151 ? UNP P0A8D0 ?   ?   'expression tag' 151 3  
1 9FZF ALA A 152 ? UNP P0A8D0 ?   ?   'expression tag' 152 4  
1 9FZF ALA A 153 ? UNP P0A8D0 ?   ?   'expression tag' 153 5  
1 9FZF ALA A 154 ? UNP P0A8D0 ?   ?   'expression tag' 154 6  
1 9FZF LEU A 155 ? UNP P0A8D0 ?   ?   'expression tag' 155 7  
1 9FZF GLU A 156 ? UNP P0A8D0 ?   ?   'expression tag' 156 8  
1 9FZF HIS A 157 ? UNP P0A8D0 ?   ?   'expression tag' 157 9  
1 9FZF HIS A 158 ? UNP P0A8D0 ?   ?   'expression tag' 158 10 
1 9FZF HIS A 159 ? UNP P0A8D0 ?   ?   'expression tag' 159 11 
1 9FZF HIS A 160 ? UNP P0A8D0 ?   ?   'expression tag' 160 12 
1 9FZF HIS A 161 ? UNP P0A8D0 ?   ?   'expression tag' 161 13 
1 9FZF HIS A 162 ? UNP P0A8D0 ?   ?   'expression tag' 162 14 
2 9FZF ASP B 139 ? UNP P0A8D0 GLU 139 conflict         139 15 
2 9FZF LYS B 150 ? UNP P0A8D0 ?   ?   'expression tag' 150 16 
2 9FZF LEU B 151 ? UNP P0A8D0 ?   ?   'expression tag' 151 17 
2 9FZF ALA B 152 ? UNP P0A8D0 ?   ?   'expression tag' 152 18 
2 9FZF ALA B 153 ? UNP P0A8D0 ?   ?   'expression tag' 153 19 
2 9FZF ALA B 154 ? UNP P0A8D0 ?   ?   'expression tag' 154 20 
2 9FZF LEU B 155 ? UNP P0A8D0 ?   ?   'expression tag' 155 21 
2 9FZF GLU B 156 ? UNP P0A8D0 ?   ?   'expression tag' 156 22 
2 9FZF HIS B 157 ? UNP P0A8D0 ?   ?   'expression tag' 157 23 
2 9FZF HIS B 158 ? UNP P0A8D0 ?   ?   'expression tag' 158 24 
2 9FZF HIS B 159 ? UNP P0A8D0 ?   ?   'expression tag' 159 25 
2 9FZF HIS B 160 ? UNP P0A8D0 ?   ?   'expression tag' 160 26 
2 9FZF HIS B 161 ? UNP P0A8D0 ?   ?   'expression tag' 161 27 
2 9FZF HIS B 162 ? UNP P0A8D0 ?   ?   'expression tag' 162 28 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric    2 
2 author_defined_assembly ? tetrameric 4 
# 
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)' 5550  ? 
1 MORE         -40   ? 
1 'SSA (A^2)'  17160 ? 
2 'ABSA (A^2)' 16610 ? 
2 MORE         -105  ? 
2 'SSA (A^2)'  28170 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,5     A,C,D,E,F,K 
2 1,2,3,4 B,G,H,I,J,L 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 none ? 
2 2 none ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000  0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 4_655  -x+1,-y,z      -1.0000000000 0.0000000000 0.0000000000 147.1260000000 0.0000000000 
-1.0000000000 0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000  
3 'crystal symmetry operation' 8_556  x-y,-y,-z+1    1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
-1.0000000000 0.0000000000 0.0000000000    0.0000000000 0.0000000000 -1.0000000000 85.8050000000 
4 'crystal symmetry operation' 11_656 -x+y+1,y,-z+1  -1.0000000000 0.0000000000 0.0000000000 147.1260000000 0.0000000000 
1.0000000000  0.0000000000 0.0000000000    0.0000000000 0.0000000000 -1.0000000000 85.8050000000 
5 'crystal symmetry operation' 12_545 x,x-y-1,-z+1/3 0.5000000000  0.8660254038 0.0000000000 73.5630000000  0.8660254038 
-0.5000000000 0.0000000000 -127.4148535572 0.0000000000 0.0000000000 -1.0000000000 28.6016666667 
# 
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 ASN A 62  ? LEU A 74  ? ASN A 62  LEU A 74  1 ? 13 
HELX_P HELX_P2  AA2 SER A 80  ? THR A 98  ? SER A 80  THR A 98  1 ? 19 
HELX_P HELX_P3  AA3 SER A 105 ? ASP A 120 ? SER A 105 ASP A 120 1 ? 16 
HELX_P HELX_P4  AA4 ASP A 120 ? ARG A 132 ? ASP A 120 ARG A 132 1 ? 13 
HELX_P HELX_P5  AA5 ILE A 137 ? ASP A 149 ? ILE A 137 ASP A 149 1 ? 13 
HELX_P HELX_P6  AA6 GLY B 20  ? SER B 23  ? GLY B 20  SER B 23  5 ? 4  
HELX_P HELX_P7  AA7 ASN B 62  ? LEU B 74  ? ASN B 62  LEU B 74  1 ? 13 
HELX_P HELX_P8  AA8 SER B 80  ? GLY B 99  ? SER B 80  GLY B 99  1 ? 20 
HELX_P HELX_P9  AA9 SER B 105 ? ASP B 120 ? SER B 105 ASP B 120 1 ? 16 
HELX_P HELX_P10 AB1 ASP B 120 ? ARG B 132 ? ASP B 120 ARG B 132 1 ? 13 
HELX_P HELX_P11 AB2 ASP B 136 ? LEU B 147 ? ASP B 136 LEU B 147 1 ? 12 
# 
_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 
metalc1  metalc ? ? A CYS 3  SG  ? ? ? 1_555 E ZN  . ZN ? ? A CYS 3   A ZN  202 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
metalc2  metalc ? ? A CYS 6  SG  ? ? ? 1_555 E ZN  . ZN ? ? A CYS 6   A ZN  202 1_555 ? ? ? ? ? ? ? 2.453 ? ? 
metalc3  metalc ? ? A CYS 31 SG  ? ? ? 1_555 E ZN  . ZN ? ? A CYS 31  A ZN  202 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc4  metalc ? ? A CYS 34 SG  ? ? ? 1_555 E ZN  . ZN ? ? A CYS 34  A ZN  202 1_555 ? ? ? ? ? ? ? 2.381 ? ? 
metalc5  metalc ? ? C DTP .  O2G ? ? ? 1_555 F MG  . MG ? ? A DTP 200 A MG  203 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc6  metalc ? ? C DTP .  O2B ? ? ? 1_555 F MG  . MG ? ? A DTP 200 A MG  203 1_555 ? ? ? ? ? ? ? 1.931 ? ? 
metalc7  metalc ? ? C DTP .  O2A ? ? ? 1_555 F MG  . MG ? ? A DTP 200 A MG  203 1_555 ? ? ? ? ? ? ? 1.926 ? ? 
metalc8  metalc ? ? D ADP .  O3B ? ? ? 1_555 F MG  . MG ? ? A ADP 201 A MG  203 1_555 ? ? ? ? ? ? ? 2.498 ? ? 
metalc9  metalc ? ? D ADP .  O2A ? ? ? 1_555 F MG  . MG ? ? A ADP 201 A MG  203 1_555 ? ? ? ? ? ? ? 2.563 ? ? 
metalc10 metalc ? ? F MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  203 A HOH 301 1_555 ? ? ? ? ? ? ? 1.944 ? ? 
metalc11 metalc ? ? B CYS 3  SG  ? ? ? 1_555 I ZN  . ZN ? ? B CYS 3   B ZN  202 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
metalc12 metalc ? ? B CYS 6  SG  ? ? ? 1_555 I ZN  . ZN ? ? B CYS 6   B ZN  202 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
metalc13 metalc ? ? B CYS 31 SG  ? ? ? 1_555 I ZN  . ZN ? ? B CYS 31  B ZN  202 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc14 metalc ? ? B CYS 34 SG  ? ? ? 1_555 I ZN  . ZN ? ? B CYS 34  B ZN  202 1_555 ? ? ? ? ? ? ? 2.436 ? ? 
metalc15 metalc ? ? G DTP .  O3G ? ? ? 1_555 J MG  . MG ? ? B DTP 200 B MG  203 1_555 ? ? ? ? ? ? ? 1.938 ? ? 
metalc16 metalc ? ? G DTP .  O2B ? ? ? 1_555 J MG  . MG ? ? B DTP 200 B MG  203 1_555 ? ? ? ? ? ? ? 1.931 ? ? 
metalc17 metalc ? ? G DTP .  O2A ? ? ? 1_555 J MG  . MG ? ? B DTP 200 B MG  203 1_555 ? ? ? ? ? ? ? 1.937 ? ? 
metalc18 metalc ? ? H ADP .  O1B ? ? ? 1_555 J MG  . MG ? ? B ADP 201 B MG  203 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
metalc19 metalc ? ? H ADP .  O2A ? ? ? 1_555 J MG  . MG ? ? B ADP 201 B MG  203 1_555 ? ? ? ? ? ? ? 2.582 ? ? 
metalc20 metalc ? ? J MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  203 B HOH 302 1_555 ? ? ? ? ? ? ? 1.926 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 3  ? A CYS 3   ? 1_555 ZN ? E ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 6  ? A CYS 6   ? 1_555 111.3 ? 
2  SG  ? A CYS 3  ? A CYS 3   ? 1_555 ZN ? E ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 31 ? A CYS 31  ? 1_555 110.0 ? 
3  SG  ? A CYS 6  ? A CYS 6   ? 1_555 ZN ? E ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 31 ? A CYS 31  ? 1_555 100.4 ? 
4  SG  ? A CYS 3  ? A CYS 3   ? 1_555 ZN ? E ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 34 ? A CYS 34  ? 1_555 111.3 ? 
5  SG  ? A CYS 6  ? A CYS 6   ? 1_555 ZN ? E ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 34 ? A CYS 34  ? 1_555 108.7 ? 
6  SG  ? A CYS 31 ? A CYS 31  ? 1_555 ZN ? E ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 34 ? A CYS 34  ? 1_555 114.6 ? 
7  O2G ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2B ? C DTP .  ? A DTP 200 ? 1_555 96.2  ? 
8  O2G ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2A ? C DTP .  ? A DTP 200 ? 1_555 105.8 ? 
9  O2B ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2A ? C DTP .  ? A DTP 200 ? 1_555 98.7  ? 
10 O2G ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O3B ? D ADP .  ? A ADP 201 ? 1_555 87.4  ? 
11 O2B ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O3B ? D ADP .  ? A ADP 201 ? 1_555 82.9  ? 
12 O2A ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O3B ? D ADP .  ? A ADP 201 ? 1_555 166.4 ? 
13 O2G ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2A ? D ADP .  ? A ADP 201 ? 1_555 166.2 ? 
14 O2B ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2A ? D ADP .  ? A ADP 201 ? 1_555 97.2  ? 
15 O2A ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2A ? D ADP .  ? A ADP 201 ? 1_555 75.1  ? 
16 O3B ? D ADP .  ? A ADP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2A ? D ADP .  ? A ADP 201 ? 1_555 91.3  ? 
17 O2G ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 301 ? 1_555 67.6  ? 
18 O2B ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 301 ? 1_555 156.0 ? 
19 O2A ? C DTP .  ? A DTP 200 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 301 ? 1_555 102.6 ? 
20 O3B ? D ADP .  ? A ADP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 301 ? 1_555 78.9  ? 
21 O2A ? D ADP .  ? A ADP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 301 ? 1_555 98.7  ? 
22 SG  ? B CYS 3  ? B CYS 3   ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 SG  ? B CYS 6  ? B CYS 6   ? 1_555 120.0 ? 
23 SG  ? B CYS 3  ? B CYS 3   ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 SG  ? B CYS 31 ? B CYS 31  ? 1_555 103.7 ? 
24 SG  ? B CYS 6  ? B CYS 6   ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 SG  ? B CYS 31 ? B CYS 31  ? 1_555 101.1 ? 
25 SG  ? B CYS 3  ? B CYS 3   ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 SG  ? B CYS 34 ? B CYS 34  ? 1_555 109.1 ? 
26 SG  ? B CYS 6  ? B CYS 6   ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 SG  ? B CYS 34 ? B CYS 34  ? 1_555 115.0 ? 
27 SG  ? B CYS 31 ? B CYS 31  ? 1_555 ZN ? I ZN . ? B ZN 202 ? 1_555 SG  ? B CYS 34 ? B CYS 34  ? 1_555 105.7 ? 
28 O3G ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O2B ? G DTP .  ? B DTP 200 ? 1_555 97.3  ? 
29 O3G ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O2A ? G DTP .  ? B DTP 200 ? 1_555 113.4 ? 
30 O2B ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O2A ? G DTP .  ? B DTP 200 ? 1_555 94.8  ? 
31 O3G ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O1B ? H ADP .  ? B ADP 201 ? 1_555 82.3  ? 
32 O2B ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O1B ? H ADP .  ? B ADP 201 ? 1_555 101.1 ? 
33 O2A ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O1B ? H ADP .  ? B ADP 201 ? 1_555 156.1 ? 
34 O3G ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O2A ? H ADP .  ? B ADP 201 ? 1_555 163.5 ? 
35 O2B ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O2A ? H ADP .  ? B ADP 201 ? 1_555 96.5  ? 
36 O2A ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O2A ? H ADP .  ? B ADP 201 ? 1_555 74.4  ? 
37 O1B ? H ADP .  ? B ADP 201 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O2A ? H ADP .  ? B ADP 201 ? 1_555 86.1  ? 
38 O3G ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 302 ? 1_555 82.3  ? 
39 O2B ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 302 ? 1_555 179.0 ? 
40 O2A ? G DTP .  ? B DTP 200 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 302 ? 1_555 86.2  ? 
41 O1B ? H ADP .  ? B ADP 201 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 302 ? 1_555 77.9  ? 
42 O2A ? H ADP .  ? B ADP 201 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 302 ? 1_555 83.7  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 11  ? ARG A 17  ? THR A 11  ARG A 17  
AA1 2 SER A 24  ? CYS A 31  ? SER A 24  CYS A 31  
AA1 3 ARG A 37  ? VAL A 43  ? ARG A 37  VAL A 43  
AA2 1 ARG A 58  ? GLU A 59  ? ARG A 58  GLU A 59  
AA2 2 ARG A 50  ? VAL A 52  ? ARG A 50  VAL A 52  
AA2 3 GLU A 102 ? PRO A 104 ? GLU A 102 PRO A 104 
AA3 1 LYS B 12  ? VAL B 19  ? LYS B 12  VAL B 19  
AA3 2 SER B 24  ? GLN B 30  ? SER B 24  GLN B 30  
AA3 3 ARG B 37  ? GLU B 42  ? ARG B 37  GLU B 42  
AA4 1 ARG B 58  ? GLU B 59  ? ARG B 58  GLU B 59  
AA4 2 ARG B 50  ? VAL B 52  ? ARG B 50  VAL B 52  
AA4 3 GLU B 102 ? PRO B 104 ? GLU B 102 PRO B 104 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 14 ? N ILE A 14 O ARG A 28  ? O ARG A 28  
AA1 2 3 N ARG A 27 ? N ARG A 27 O THR A 40  ? O THR A 40  
AA2 1 2 O GLU A 59 ? O GLU A 59 N VAL A 51  ? N VAL A 51  
AA2 2 3 N ARG A 50 ? N ARG A 50 O VAL A 103 ? O VAL A 103 
AA3 1 2 N ARG B 17 ? N ARG B 17 O ARG B 26  ? O ARG B 26  
AA3 2 3 N ARG B 27 ? N ARG B 27 O THR B 40  ? O THR B 40  
AA4 1 2 O GLU B 59 ? O GLU B 59 N VAL B 51  ? N VAL B 51  
AA4 2 3 N ARG B 50 ? N ARG B 50 O VAL B 103 ? O VAL B 103 
# 
_pdbx_entry_details.entry_id                   9FZF 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     322 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     369 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_655 
_pdbx_validate_symm_contact.dist              2.15 
# 
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 PHE A 7   ? ? 100.37  31.38  
2 1 LEU A 74  ? ? -94.27  34.06  
3 1 SER A 133 ? ? 55.75   81.44  
4 1 CYS B 6   ? ? -93.71  -61.85 
5 1 PHE B 7   ? ? 153.65  -9.98  
6 1 ASP B 15  ? ? 173.63  142.83 
7 1 ARG B 17  ? ? -171.72 141.53 
8 1 LEU B 74  ? ? -93.84  33.76  
9 1 SER B 133 ? ? 42.75   82.80  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? ? 94.2246 -14.8104 29.8501 -0.0364 ? 0.2693  ? 0.1086 ? -0.0705 ? -0.0155 ? -0.3897 ? 1.7521 ? 0.4756 ? 
0.8193  ? 4.615 ? 4.0234 ? 6.3823 ? 0.0548 ? 0.1916 ? 0.3258 ? 0.1916 ? -0.0944 ? 0.4474  ? 0.3258 ? 0.4474  ? 0.0396 ? 
2 'X-RAY DIFFRACTION' ? ? 70.1451 -8.953   26.4595 0.1485  ? -0.0443 ? 0.0044 ? -0.2552 ? -0.0554 ? -0.1894 ? 1.8558 ? 0.2014 ? 
-1.1447 ? 1.715 ? -0.365 ? 5.7767 ? -0.051 ? 0.2282 ? 0.5019 ? 0.2282 ? 0.0156  ? -0.3817 ? 0.5019 ? -0.3817 ? 0.0354 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 1   ? ? ? A 149 ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 1 ? ? A 200 ? ? ? A 203 ? ? '{ A|* }' 
3 'X-RAY DIFFRACTION' 2 ? ? B 1   ? ? ? B 149 ? ? '{ B|* }' 
4 'X-RAY DIFFRACTION' 2 ? ? B 200 ? ? ? B 203 ? ? '{ B|* }' 
# 
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 LYS 150 ? A LYS 150 
2  1 Y 1 A LEU 151 ? A LEU 151 
3  1 Y 1 A ALA 152 ? A ALA 152 
4  1 Y 1 A ALA 153 ? A ALA 153 
5  1 Y 1 A ALA 154 ? A ALA 154 
6  1 Y 1 A LEU 155 ? A LEU 155 
7  1 Y 1 A GLU 156 ? A GLU 156 
8  1 Y 1 A HIS 157 ? A HIS 157 
9  1 Y 1 A HIS 158 ? A HIS 158 
10 1 Y 1 A HIS 159 ? A HIS 159 
11 1 Y 1 A HIS 160 ? A HIS 160 
12 1 Y 1 A HIS 161 ? A HIS 161 
13 1 Y 1 A HIS 162 ? A HIS 162 
14 1 Y 1 B LYS 150 ? B LYS 150 
15 1 Y 1 B LEU 151 ? B LEU 151 
16 1 Y 1 B ALA 152 ? B ALA 152 
17 1 Y 1 B ALA 153 ? B ALA 153 
18 1 Y 1 B ALA 154 ? B ALA 154 
19 1 Y 1 B LEU 155 ? B LEU 155 
20 1 Y 1 B GLU 156 ? B GLU 156 
21 1 Y 1 B HIS 157 ? B HIS 157 
22 1 Y 1 B HIS 158 ? B HIS 158 
23 1 Y 1 B HIS 159 ? B HIS 159 
24 1 Y 1 B HIS 160 ? B HIS 160 
25 1 Y 1 B HIS 161 ? B HIS 161 
26 1 Y 1 B HIS 162 ? B HIS 162 
# 
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 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
CYS N      N  N N 116 
CYS CA     C  N R 117 
CYS C      C  N N 118 
CYS O      O  N N 119 
CYS CB     C  N N 120 
CYS SG     S  N N 121 
CYS OXT    O  N N 122 
CYS H      H  N N 123 
CYS H2     H  N N 124 
CYS HA     H  N N 125 
CYS HB2    H  N N 126 
CYS HB3    H  N N 127 
CYS HG     H  N N 128 
CYS HXT    H  N N 129 
DTP PG     P  N N 130 
DTP O1G    O  N N 131 
DTP O2G    O  N N 132 
DTP O3G    O  N N 133 
DTP PB     P  N S 134 
DTP O1B    O  N N 135 
DTP O2B    O  N N 136 
DTP O3B    O  N N 137 
DTP PA     P  N S 138 
DTP O1A    O  N N 139 
DTP O2A    O  N N 140 
DTP O3A    O  N N 141 
DTP "O5'"  O  N N 142 
DTP "C5'"  C  N N 143 
DTP "C4'"  C  N R 144 
DTP "O4'"  O  N N 145 
DTP "C3'"  C  N S 146 
DTP "O3'"  O  N N 147 
DTP "C2'"  C  N N 148 
DTP "C1'"  C  N R 149 
DTP N9     N  Y N 150 
DTP C8     C  Y N 151 
DTP N7     N  Y N 152 
DTP C5     C  Y N 153 
DTP C6     C  Y N 154 
DTP N6     N  N N 155 
DTP N1     N  Y N 156 
DTP C2     C  Y N 157 
DTP N3     N  Y N 158 
DTP C4     C  Y N 159 
DTP HOG2   H  N N 160 
DTP HOG3   H  N N 161 
DTP HOB2   H  N N 162 
DTP HOA2   H  N N 163 
DTP "H5'1" H  N N 164 
DTP "H5'2" H  N N 165 
DTP "H4'"  H  N N 166 
DTP "H3'"  H  N N 167 
DTP "HO3'" H  N N 168 
DTP "H2'1" H  N N 169 
DTP "H2'2" H  N N 170 
DTP "H1'"  H  N N 171 
DTP H8     H  N N 172 
DTP HN61   H  N N 173 
DTP HN62   H  N N 174 
DTP H2     H  N N 175 
GLN N      N  N N 176 
GLN CA     C  N S 177 
GLN C      C  N N 178 
GLN O      O  N N 179 
GLN CB     C  N N 180 
GLN CG     C  N N 181 
GLN CD     C  N N 182 
GLN OE1    O  N N 183 
GLN NE2    N  N N 184 
GLN OXT    O  N N 185 
GLN H      H  N N 186 
GLN H2     H  N N 187 
GLN HA     H  N N 188 
GLN HB2    H  N N 189 
GLN HB3    H  N N 190 
GLN HG2    H  N N 191 
GLN HG3    H  N N 192 
GLN HE21   H  N N 193 
GLN HE22   H  N N 194 
GLN HXT    H  N N 195 
GLU N      N  N N 196 
GLU CA     C  N S 197 
GLU C      C  N N 198 
GLU O      O  N N 199 
GLU CB     C  N N 200 
GLU CG     C  N N 201 
GLU CD     C  N N 202 
GLU OE1    O  N N 203 
GLU OE2    O  N N 204 
GLU OXT    O  N N 205 
GLU H      H  N N 206 
GLU H2     H  N N 207 
GLU HA     H  N N 208 
GLU HB2    H  N N 209 
GLU HB3    H  N N 210 
GLU HG2    H  N N 211 
GLU HG3    H  N N 212 
GLU HE2    H  N N 213 
GLU HXT    H  N N 214 
GLY N      N  N N 215 
GLY CA     C  N N 216 
GLY C      C  N N 217 
GLY O      O  N N 218 
GLY OXT    O  N N 219 
GLY H      H  N N 220 
GLY H2     H  N N 221 
GLY HA2    H  N N 222 
GLY HA3    H  N N 223 
GLY HXT    H  N N 224 
HIS N      N  N N 225 
HIS CA     C  N S 226 
HIS C      C  N N 227 
HIS O      O  N N 228 
HIS CB     C  N N 229 
HIS CG     C  Y N 230 
HIS ND1    N  Y N 231 
HIS CD2    C  Y N 232 
HIS CE1    C  Y N 233 
HIS NE2    N  Y N 234 
HIS OXT    O  N N 235 
HIS H      H  N N 236 
HIS H2     H  N N 237 
HIS HA     H  N N 238 
HIS HB2    H  N N 239 
HIS HB3    H  N N 240 
HIS HD1    H  N N 241 
HIS HD2    H  N N 242 
HIS HE1    H  N N 243 
HIS HE2    H  N N 244 
HIS HXT    H  N N 245 
HOH O      O  N N 246 
HOH H1     H  N N 247 
HOH H2     H  N N 248 
ILE N      N  N N 249 
ILE CA     C  N S 250 
ILE C      C  N N 251 
ILE O      O  N N 252 
ILE CB     C  N S 253 
ILE CG1    C  N N 254 
ILE CG2    C  N N 255 
ILE CD1    C  N N 256 
ILE OXT    O  N N 257 
ILE H      H  N N 258 
ILE H2     H  N N 259 
ILE HA     H  N N 260 
ILE HB     H  N N 261 
ILE HG12   H  N N 262 
ILE HG13   H  N N 263 
ILE HG21   H  N N 264 
ILE HG22   H  N N 265 
ILE HG23   H  N N 266 
ILE HD11   H  N N 267 
ILE HD12   H  N N 268 
ILE HD13   H  N N 269 
ILE HXT    H  N N 270 
LEU N      N  N N 271 
LEU CA     C  N S 272 
LEU C      C  N N 273 
LEU O      O  N N 274 
LEU CB     C  N N 275 
LEU CG     C  N N 276 
LEU CD1    C  N N 277 
LEU CD2    C  N N 278 
LEU OXT    O  N N 279 
LEU H      H  N N 280 
LEU H2     H  N N 281 
LEU HA     H  N N 282 
LEU HB2    H  N N 283 
LEU HB3    H  N N 284 
LEU HG     H  N N 285 
LEU HD11   H  N N 286 
LEU HD12   H  N N 287 
LEU HD13   H  N N 288 
LEU HD21   H  N N 289 
LEU HD22   H  N N 290 
LEU HD23   H  N N 291 
LEU HXT    H  N N 292 
LYS N      N  N N 293 
LYS CA     C  N S 294 
LYS C      C  N N 295 
LYS O      O  N N 296 
LYS CB     C  N N 297 
LYS CG     C  N N 298 
LYS CD     C  N N 299 
LYS CE     C  N N 300 
LYS NZ     N  N N 301 
LYS OXT    O  N N 302 
LYS H      H  N N 303 
LYS H2     H  N N 304 
LYS HA     H  N N 305 
LYS HB2    H  N N 306 
LYS HB3    H  N N 307 
LYS HG2    H  N N 308 
LYS HG3    H  N N 309 
LYS HD2    H  N N 310 
LYS HD3    H  N N 311 
LYS HE2    H  N N 312 
LYS HE3    H  N N 313 
LYS HZ1    H  N N 314 
LYS HZ2    H  N N 315 
LYS HZ3    H  N N 316 
LYS HXT    H  N N 317 
MET N      N  N N 318 
MET CA     C  N S 319 
MET C      C  N N 320 
MET O      O  N N 321 
MET CB     C  N N 322 
MET CG     C  N N 323 
MET SD     S  N N 324 
MET CE     C  N N 325 
MET OXT    O  N N 326 
MET H      H  N N 327 
MET H2     H  N N 328 
MET HA     H  N N 329 
MET HB2    H  N N 330 
MET HB3    H  N N 331 
MET HG2    H  N N 332 
MET HG3    H  N N 333 
MET HE1    H  N N 334 
MET HE2    H  N N 335 
MET HE3    H  N N 336 
MET HXT    H  N N 337 
MG  MG     MG N N 338 
PHE N      N  N N 339 
PHE CA     C  N S 340 
PHE C      C  N N 341 
PHE O      O  N N 342 
PHE CB     C  N N 343 
PHE CG     C  Y N 344 
PHE CD1    C  Y N 345 
PHE CD2    C  Y N 346 
PHE CE1    C  Y N 347 
PHE CE2    C  Y N 348 
PHE CZ     C  Y N 349 
PHE OXT    O  N N 350 
PHE H      H  N N 351 
PHE H2     H  N N 352 
PHE HA     H  N N 353 
PHE HB2    H  N N 354 
PHE HB3    H  N N 355 
PHE HD1    H  N N 356 
PHE HD2    H  N N 357 
PHE HE1    H  N N 358 
PHE HE2    H  N N 359 
PHE HZ     H  N N 360 
PHE HXT    H  N N 361 
PRO N      N  N N 362 
PRO CA     C  N S 363 
PRO C      C  N N 364 
PRO O      O  N N 365 
PRO CB     C  N N 366 
PRO CG     C  N N 367 
PRO CD     C  N N 368 
PRO OXT    O  N N 369 
PRO H      H  N N 370 
PRO HA     H  N N 371 
PRO HB2    H  N N 372 
PRO HB3    H  N N 373 
PRO HG2    H  N N 374 
PRO HG3    H  N N 375 
PRO HD2    H  N N 376 
PRO HD3    H  N N 377 
PRO HXT    H  N N 378 
SER N      N  N N 379 
SER CA     C  N S 380 
SER C      C  N N 381 
SER O      O  N N 382 
SER CB     C  N N 383 
SER OG     O  N N 384 
SER OXT    O  N N 385 
SER H      H  N N 386 
SER H2     H  N N 387 
SER HA     H  N N 388 
SER HB2    H  N N 389 
SER HB3    H  N N 390 
SER HG     H  N N 391 
SER HXT    H  N N 392 
THR N      N  N N 393 
THR CA     C  N S 394 
THR C      C  N N 395 
THR O      O  N N 396 
THR CB     C  N R 397 
THR OG1    O  N N 398 
THR CG2    C  N N 399 
THR OXT    O  N N 400 
THR H      H  N N 401 
THR H2     H  N N 402 
THR HA     H  N N 403 
THR HB     H  N N 404 
THR HG1    H  N N 405 
THR HG21   H  N N 406 
THR HG22   H  N N 407 
THR HG23   H  N N 408 
THR HXT    H  N N 409 
TYR N      N  N N 410 
TYR CA     C  N S 411 
TYR C      C  N N 412 
TYR O      O  N N 413 
TYR CB     C  N N 414 
TYR CG     C  Y N 415 
TYR CD1    C  Y N 416 
TYR CD2    C  Y N 417 
TYR CE1    C  Y N 418 
TYR CE2    C  Y N 419 
TYR CZ     C  Y N 420 
TYR OH     O  N N 421 
TYR OXT    O  N N 422 
TYR H      H  N N 423 
TYR H2     H  N N 424 
TYR HA     H  N N 425 
TYR HB2    H  N N 426 
TYR HB3    H  N N 427 
TYR HD1    H  N N 428 
TYR HD2    H  N N 429 
TYR HE1    H  N N 430 
TYR HE2    H  N N 431 
TYR HH     H  N N 432 
TYR HXT    H  N N 433 
VAL N      N  N N 434 
VAL CA     C  N S 435 
VAL C      C  N N 436 
VAL O      O  N N 437 
VAL CB     C  N N 438 
VAL CG1    C  N N 439 
VAL CG2    C  N N 440 
VAL OXT    O  N N 441 
VAL H      H  N N 442 
VAL H2     H  N N 443 
VAL HA     H  N N 444 
VAL HB     H  N N 445 
VAL HG11   H  N N 446 
VAL HG12   H  N N 447 
VAL HG13   H  N N 448 
VAL HG21   H  N N 449 
VAL HG22   H  N N 450 
VAL HG23   H  N N 451 
VAL HXT    H  N N 452 
ZN  ZN     ZN N N 453 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
CYS N     CA     sing N N 114 
CYS N     H      sing N N 115 
CYS N     H2     sing N N 116 
CYS CA    C      sing N N 117 
CYS CA    CB     sing N N 118 
CYS CA    HA     sing N N 119 
CYS C     O      doub N N 120 
CYS C     OXT    sing N N 121 
CYS CB    SG     sing N N 122 
CYS CB    HB2    sing N N 123 
CYS CB    HB3    sing N N 124 
CYS SG    HG     sing N N 125 
CYS OXT   HXT    sing N N 126 
DTP PG    O1G    doub N N 127 
DTP PG    O2G    sing N N 128 
DTP PG    O3G    sing N N 129 
DTP PG    O3B    sing N N 130 
DTP O2G   HOG2   sing N N 131 
DTP O3G   HOG3   sing N N 132 
DTP PB    O1B    doub N N 133 
DTP PB    O2B    sing N N 134 
DTP PB    O3B    sing N N 135 
DTP PB    O3A    sing N N 136 
DTP O2B   HOB2   sing N N 137 
DTP PA    O1A    doub N N 138 
DTP PA    O2A    sing N N 139 
DTP PA    O3A    sing N N 140 
DTP PA    "O5'"  sing N N 141 
DTP O2A   HOA2   sing N N 142 
DTP "O5'" "C5'"  sing N N 143 
DTP "C5'" "C4'"  sing N N 144 
DTP "C5'" "H5'1" sing N N 145 
DTP "C5'" "H5'2" sing N N 146 
DTP "C4'" "O4'"  sing N N 147 
DTP "C4'" "C3'"  sing N N 148 
DTP "C4'" "H4'"  sing N N 149 
DTP "O4'" "C1'"  sing N N 150 
DTP "C3'" "O3'"  sing N N 151 
DTP "C3'" "C2'"  sing N N 152 
DTP "C3'" "H3'"  sing N N 153 
DTP "O3'" "HO3'" sing N N 154 
DTP "C2'" "C1'"  sing N N 155 
DTP "C2'" "H2'1" sing N N 156 
DTP "C2'" "H2'2" sing N N 157 
DTP "C1'" N9     sing N N 158 
DTP "C1'" "H1'"  sing N N 159 
DTP N9    C8     sing Y N 160 
DTP N9    C4     sing Y N 161 
DTP C8    N7     doub Y N 162 
DTP C8    H8     sing N N 163 
DTP N7    C5     sing Y N 164 
DTP C5    C6     sing Y N 165 
DTP C5    C4     doub Y N 166 
DTP C6    N6     sing N N 167 
DTP C6    N1     doub Y N 168 
DTP N6    HN61   sing N N 169 
DTP N6    HN62   sing N N 170 
DTP N1    C2     sing Y N 171 
DTP C2    N3     doub Y N 172 
DTP C2    H2     sing N N 173 
DTP N3    C4     sing Y N 174 
GLN N     CA     sing N N 175 
GLN N     H      sing N N 176 
GLN N     H2     sing N N 177 
GLN CA    C      sing N N 178 
GLN CA    CB     sing N N 179 
GLN CA    HA     sing N N 180 
GLN C     O      doub N N 181 
GLN C     OXT    sing N N 182 
GLN CB    CG     sing N N 183 
GLN CB    HB2    sing N N 184 
GLN CB    HB3    sing N N 185 
GLN CG    CD     sing N N 186 
GLN CG    HG2    sing N N 187 
GLN CG    HG3    sing N N 188 
GLN CD    OE1    doub N N 189 
GLN CD    NE2    sing N N 190 
GLN NE2   HE21   sing N N 191 
GLN NE2   HE22   sing N N 192 
GLN OXT   HXT    sing N N 193 
GLU N     CA     sing N N 194 
GLU N     H      sing N N 195 
GLU N     H2     sing N N 196 
GLU CA    C      sing N N 197 
GLU CA    CB     sing N N 198 
GLU CA    HA     sing N N 199 
GLU C     O      doub N N 200 
GLU C     OXT    sing N N 201 
GLU CB    CG     sing N N 202 
GLU CB    HB2    sing N N 203 
GLU CB    HB3    sing N N 204 
GLU CG    CD     sing N N 205 
GLU CG    HG2    sing N N 206 
GLU CG    HG3    sing N N 207 
GLU CD    OE1    doub N N 208 
GLU CD    OE2    sing N N 209 
GLU OE2   HE2    sing N N 210 
GLU OXT   HXT    sing N N 211 
GLY N     CA     sing N N 212 
GLY N     H      sing N N 213 
GLY N     H2     sing N N 214 
GLY CA    C      sing N N 215 
GLY CA    HA2    sing N N 216 
GLY CA    HA3    sing N N 217 
GLY C     O      doub N N 218 
GLY C     OXT    sing N N 219 
GLY OXT   HXT    sing N N 220 
HIS N     CA     sing N N 221 
HIS N     H      sing N N 222 
HIS N     H2     sing N N 223 
HIS CA    C      sing N N 224 
HIS CA    CB     sing N N 225 
HIS CA    HA     sing N N 226 
HIS C     O      doub N N 227 
HIS C     OXT    sing N N 228 
HIS CB    CG     sing N N 229 
HIS CB    HB2    sing N N 230 
HIS CB    HB3    sing N N 231 
HIS CG    ND1    sing Y N 232 
HIS CG    CD2    doub Y N 233 
HIS ND1   CE1    doub Y N 234 
HIS ND1   HD1    sing N N 235 
HIS CD2   NE2    sing Y N 236 
HIS CD2   HD2    sing N N 237 
HIS CE1   NE2    sing Y N 238 
HIS CE1   HE1    sing N N 239 
HIS NE2   HE2    sing N N 240 
HIS OXT   HXT    sing N N 241 
HOH O     H1     sing N N 242 
HOH O     H2     sing N N 243 
ILE N     CA     sing N N 244 
ILE N     H      sing N N 245 
ILE N     H2     sing N N 246 
ILE CA    C      sing N N 247 
ILE CA    CB     sing N N 248 
ILE CA    HA     sing N N 249 
ILE C     O      doub N N 250 
ILE C     OXT    sing N N 251 
ILE CB    CG1    sing N N 252 
ILE CB    CG2    sing N N 253 
ILE CB    HB     sing N N 254 
ILE CG1   CD1    sing N N 255 
ILE CG1   HG12   sing N N 256 
ILE CG1   HG13   sing N N 257 
ILE CG2   HG21   sing N N 258 
ILE CG2   HG22   sing N N 259 
ILE CG2   HG23   sing N N 260 
ILE CD1   HD11   sing N N 261 
ILE CD1   HD12   sing N N 262 
ILE CD1   HD13   sing N N 263 
ILE OXT   HXT    sing N N 264 
LEU N     CA     sing N N 265 
LEU N     H      sing N N 266 
LEU N     H2     sing N N 267 
LEU CA    C      sing N N 268 
LEU CA    CB     sing N N 269 
LEU CA    HA     sing N N 270 
LEU C     O      doub N N 271 
LEU C     OXT    sing N N 272 
LEU CB    CG     sing N N 273 
LEU CB    HB2    sing N N 274 
LEU CB    HB3    sing N N 275 
LEU CG    CD1    sing N N 276 
LEU CG    CD2    sing N N 277 
LEU CG    HG     sing N N 278 
LEU CD1   HD11   sing N N 279 
LEU CD1   HD12   sing N N 280 
LEU CD1   HD13   sing N N 281 
LEU CD2   HD21   sing N N 282 
LEU CD2   HD22   sing N N 283 
LEU CD2   HD23   sing N N 284 
LEU OXT   HXT    sing N N 285 
LYS N     CA     sing N N 286 
LYS N     H      sing N N 287 
LYS N     H2     sing N N 288 
LYS CA    C      sing N N 289 
LYS CA    CB     sing N N 290 
LYS CA    HA     sing N N 291 
LYS C     O      doub N N 292 
LYS C     OXT    sing N N 293 
LYS CB    CG     sing N N 294 
LYS CB    HB2    sing N N 295 
LYS CB    HB3    sing N N 296 
LYS CG    CD     sing N N 297 
LYS CG    HG2    sing N N 298 
LYS CG    HG3    sing N N 299 
LYS CD    CE     sing N N 300 
LYS CD    HD2    sing N N 301 
LYS CD    HD3    sing N N 302 
LYS CE    NZ     sing N N 303 
LYS CE    HE2    sing N N 304 
LYS CE    HE3    sing N N 305 
LYS NZ    HZ1    sing N N 306 
LYS NZ    HZ2    sing N N 307 
LYS NZ    HZ3    sing N N 308 
LYS OXT   HXT    sing N N 309 
MET N     CA     sing N N 310 
MET N     H      sing N N 311 
MET N     H2     sing N N 312 
MET CA    C      sing N N 313 
MET CA    CB     sing N N 314 
MET CA    HA     sing N N 315 
MET C     O      doub N N 316 
MET C     OXT    sing N N 317 
MET CB    CG     sing N N 318 
MET CB    HB2    sing N N 319 
MET CB    HB3    sing N N 320 
MET CG    SD     sing N N 321 
MET CG    HG2    sing N N 322 
MET CG    HG3    sing N N 323 
MET SD    CE     sing N N 324 
MET CE    HE1    sing N N 325 
MET CE    HE2    sing N N 326 
MET CE    HE3    sing N N 327 
MET OXT   HXT    sing N N 328 
PHE N     CA     sing N N 329 
PHE N     H      sing N N 330 
PHE N     H2     sing N N 331 
PHE CA    C      sing N N 332 
PHE CA    CB     sing N N 333 
PHE CA    HA     sing N N 334 
PHE C     O      doub N N 335 
PHE C     OXT    sing N N 336 
PHE CB    CG     sing N N 337 
PHE CB    HB2    sing N N 338 
PHE CB    HB3    sing N N 339 
PHE CG    CD1    doub Y N 340 
PHE CG    CD2    sing Y N 341 
PHE CD1   CE1    sing Y N 342 
PHE CD1   HD1    sing N N 343 
PHE CD2   CE2    doub Y N 344 
PHE CD2   HD2    sing N N 345 
PHE CE1   CZ     doub Y N 346 
PHE CE1   HE1    sing N N 347 
PHE CE2   CZ     sing Y N 348 
PHE CE2   HE2    sing N N 349 
PHE CZ    HZ     sing N N 350 
PHE OXT   HXT    sing N N 351 
PRO N     CA     sing N N 352 
PRO N     CD     sing N N 353 
PRO N     H      sing N N 354 
PRO CA    C      sing N N 355 
PRO CA    CB     sing N N 356 
PRO CA    HA     sing N N 357 
PRO C     O      doub N N 358 
PRO C     OXT    sing N N 359 
PRO CB    CG     sing N N 360 
PRO CB    HB2    sing N N 361 
PRO CB    HB3    sing N N 362 
PRO CG    CD     sing N N 363 
PRO CG    HG2    sing N N 364 
PRO CG    HG3    sing N N 365 
PRO CD    HD2    sing N N 366 
PRO CD    HD3    sing N N 367 
PRO OXT   HXT    sing N N 368 
SER N     CA     sing N N 369 
SER N     H      sing N N 370 
SER N     H2     sing N N 371 
SER CA    C      sing N N 372 
SER CA    CB     sing N N 373 
SER CA    HA     sing N N 374 
SER C     O      doub N N 375 
SER C     OXT    sing N N 376 
SER CB    OG     sing N N 377 
SER CB    HB2    sing N N 378 
SER CB    HB3    sing N N 379 
SER OG    HG     sing N N 380 
SER OXT   HXT    sing N N 381 
THR N     CA     sing N N 382 
THR N     H      sing N N 383 
THR N     H2     sing N N 384 
THR CA    C      sing N N 385 
THR CA    CB     sing N N 386 
THR CA    HA     sing N N 387 
THR C     O      doub N N 388 
THR C     OXT    sing N N 389 
THR CB    OG1    sing N N 390 
THR CB    CG2    sing N N 391 
THR CB    HB     sing N N 392 
THR OG1   HG1    sing N N 393 
THR CG2   HG21   sing N N 394 
THR CG2   HG22   sing N N 395 
THR CG2   HG23   sing N N 396 
THR OXT   HXT    sing N N 397 
TYR N     CA     sing N N 398 
TYR N     H      sing N N 399 
TYR N     H2     sing N N 400 
TYR CA    C      sing N N 401 
TYR CA    CB     sing N N 402 
TYR CA    HA     sing N N 403 
TYR C     O      doub N N 404 
TYR C     OXT    sing N N 405 
TYR CB    CG     sing N N 406 
TYR CB    HB2    sing N N 407 
TYR CB    HB3    sing N N 408 
TYR CG    CD1    doub Y N 409 
TYR CG    CD2    sing Y N 410 
TYR CD1   CE1    sing Y N 411 
TYR CD1   HD1    sing N N 412 
TYR CD2   CE2    doub Y N 413 
TYR CD2   HD2    sing N N 414 
TYR CE1   CZ     doub Y N 415 
TYR CE1   HE1    sing N N 416 
TYR CE2   CZ     sing Y N 417 
TYR CE2   HE2    sing N N 418 
TYR CZ    OH     sing N N 419 
TYR OH    HH     sing N N 420 
TYR OXT   HXT    sing N N 421 
VAL N     CA     sing N N 422 
VAL N     H      sing N N 423 
VAL N     H2     sing N N 424 
VAL CA    C      sing N N 425 
VAL CA    CB     sing N N 426 
VAL CA    HA     sing N N 427 
VAL C     O      doub N N 428 
VAL C     OXT    sing N N 429 
VAL CB    CG1    sing N N 430 
VAL CB    CG2    sing N N 431 
VAL CB    HB     sing N N 432 
VAL CG1   HG11   sing N N 433 
VAL CG1   HG12   sing N N 434 
VAL CG1   HG13   sing N N 435 
VAL CG2   HG21   sing N N 436 
VAL CG2   HG22   sing N N 437 
VAL CG2   HG23   sing N N 438 
VAL OXT   HXT    sing N N 439 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Carl Trygger Foundation'  Sweden          'CTS 20:361' 1 
Cancerfonden               Sweden          201210PJF    2 
'Wenner-Gren Foundation'   'United States' ?            3 
'Swedish Research Council' Sweden          2016-04855   4 
'Swedish Research Council' Sweden          2019-03681   5 
'Swedish Research Council' Sweden          2023-05074   6 
# 
_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   7P3F 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FZF 
_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]   0.006797 
_atom_sites.fract_transf_matrix[1][2]   0.003924 
_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]   0.007848 
_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]   0.011654 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
ZN 
# 
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     . MET A 1 1   ? 110.336 9.017   42.108 1    70.85  ? 1   MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? 108.991 9.539   41.877 1    71.24  ? 1   MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? 108.731 10.889  42.561 1    71.83  ? 1   MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? 109.449 11.266  43.487 1    71.97  ? 1   MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? 107.911 8.506   42.25  1    71.41  ? 1   MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? 107.802 8.242   43.728 1    72.74  ? 1   MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? 106.171 7.621   44.198 1    73.25  ? 1   MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? 106.328 5.956   43.773 1    70.33  ? 1   MET A CE    1 
ATOM   9    N  N     . HIS A 1 2   ? 107.714 11.621  42.078 1    72.12  ? 2   HIS A N     1 
ATOM   10   C  CA    . HIS A 1 2   ? 107.323 12.924  42.594 1    72.91  ? 2   HIS A CA    1 
ATOM   11   C  C     . HIS A 1 2   ? 106.89  12.812  44.018 1    73.01  ? 2   HIS A C     1 
ATOM   12   O  O     . HIS A 1 2   ? 106.108 11.924  44.357 1    73.28  ? 2   HIS A O     1 
ATOM   13   C  CB    . HIS A 1 2   ? 106.124 13.478  41.816 1    74.62  ? 2   HIS A CB    1 
ATOM   14   C  CG    . HIS A 1 2   ? 106.435 14.629  40.916 1    78.73  ? 2   HIS A CG    1 
ATOM   15   N  ND1   . HIS A 1 2   ? 107.138 14.455  39.728 1    81.01  ? 2   HIS A ND1   1 
ATOM   16   C  CD2   . HIS A 1 2   ? 106.082 15.931  41.028 1    80.43  ? 2   HIS A CD2   1 
ATOM   17   C  CE1   . HIS A 1 2   ? 107.199 15.653  39.166 1    81.75  ? 2   HIS A CE1   1 
ATOM   18   N  NE2   . HIS A 1 2   ? 106.582 16.576  39.912 1    81.88  ? 2   HIS A NE2   1 
ATOM   19   N  N     . CYS A 1 3   ? 107.358 13.743  44.852 1    72.59  ? 3   CYS A N     1 
ATOM   20   C  CA    . CYS A 1 3   ? 106.925 13.857  46.239 1    72.44  ? 3   CYS A CA    1 
ATOM   21   C  C     . CYS A 1 3   ? 105.444 14.24   46.246 1    71.51  ? 3   CYS A C     1 
ATOM   22   O  O     . CYS A 1 3   ? 105.052 15.222  45.616 1    71.45  ? 3   CYS A O     1 
ATOM   23   C  CB    . CYS A 1 3   ? 107.765 14.89   46.982 1    73.83  ? 3   CYS A CB    1 
ATOM   24   S  SG    . CYS A 1 3   ? 107.125 15.337  48.62  1    79.73  ? 3   CYS A SG    1 
ATOM   25   N  N     . PRO A 1 4   ? 104.612 13.473  46.958 1    70.68  ? 4   PRO A N     1 
ATOM   26   C  CA    . PRO A 1 4   ? 103.178 13.784  46.994 1    70.49  ? 4   PRO A CA    1 
ATOM   27   C  C     . PRO A 1 4   ? 102.803 15.02   47.805 1    70.97  ? 4   PRO A C     1 
ATOM   28   O  O     . PRO A 1 4   ? 101.63  15.369  47.846 1    71.14  ? 4   PRO A O     1 
ATOM   29   C  CB    . PRO A 1 4   ? 102.565 12.524  47.605 1    70.86  ? 4   PRO A CB    1 
ATOM   30   C  CG    . PRO A 1 4   ? 103.638 11.966  48.457 1    71.29  ? 4   PRO A CG    1 
ATOM   31   C  CD    . PRO A 1 4   ? 104.932 12.279  47.761 1    69.92  ? 4   PRO A CD    1 
ATOM   32   N  N     . PHE A 1 5   ? 103.775 15.681  48.446 1    71.02  ? 5   PHE A N     1 
ATOM   33   C  CA    . PHE A 1 5   ? 103.494 16.843  49.27  1    71.47  ? 5   PHE A CA    1 
ATOM   34   C  C     . PHE A 1 5   ? 104.052 18.148  48.688 1    73.03  ? 5   PHE A C     1 
ATOM   35   O  O     . PHE A 1 5   ? 103.284 19.08   48.455 1    73.04  ? 5   PHE A O     1 
ATOM   36   C  CB    . PHE A 1 5   ? 103.986 16.618  50.713 1    70.64  ? 5   PHE A CB    1 
ATOM   37   C  CG    . PHE A 1 5   ? 103.673 15.256  51.286 1    70.36  ? 5   PHE A CG    1 
ATOM   38   C  CD1   . PHE A 1 5   ? 102.366 14.821  51.407 1    70.45  ? 5   PHE A CD1   1 
ATOM   39   C  CD2   . PHE A 1 5   ? 104.688 14.408  51.692 1    70.79  ? 5   PHE A CD2   1 
ATOM   40   C  CE1   . PHE A 1 5   ? 102.082 13.569  51.927 1    70.78  ? 5   PHE A CE1   1 
ATOM   41   C  CE2   . PHE A 1 5   ? 104.4   13.158  52.219 1    71.08  ? 5   PHE A CE2   1 
ATOM   42   C  CZ    . PHE A 1 5   ? 103.1   12.744  52.325 1    70.62  ? 5   PHE A CZ    1 
ATOM   43   N  N     . CYS A 1 6   ? 105.374 18.227  48.45  1    74.23  ? 6   CYS A N     1 
ATOM   44   C  CA    . CYS A 1 6   ? 105.976 19.478  47.975 1    75.84  ? 6   CYS A CA    1 
ATOM   45   C  C     . CYS A 1 6   ? 106.004 19.569  46.464 1    77.05  ? 6   CYS A C     1 
ATOM   46   O  O     . CYS A 1 6   ? 105.691 20.617  45.908 1    77.11  ? 6   CYS A O     1 
ATOM   47   C  CB    . CYS A 1 6   ? 107.351 19.723  48.599 1    76.75  ? 6   CYS A CB    1 
ATOM   48   S  SG    . CYS A 1 6   ? 108.699 18.743  47.883 1    80.25  ? 6   CYS A SG    1 
ATOM   49   N  N     . PHE A 1 7   ? 106.331 18.414  45.835 1    77.96  ? 7   PHE A N     1 
ATOM   50   C  CA    . PHE A 1 7   ? 106.355 18.054  44.422 1    79.52  ? 7   PHE A CA    1 
ATOM   51   C  C     . PHE A 1 7   ? 107.758 18.075  43.754 1    81.08  ? 7   PHE A C     1 
ATOM   52   O  O     . PHE A 1 7   ? 107.842 18.248  42.534 1    81.29  ? 7   PHE A O     1 
ATOM   53   C  CB    . PHE A 1 7   ? 105.321 18.823  43.59  1    79.53  ? 7   PHE A CB    1 
ATOM   54   C  CG    . PHE A 1 7   ? 103.91  18.34   43.854 1    80.08  ? 7   PHE A CG    1 
ATOM   55   C  CD1   . PHE A 1 7   ? 103.434 17.186  43.265 1    80.8   ? 7   PHE A CD1   1 
ATOM   56   C  CD2   . PHE A 1 7   ? 103.071 19.031  44.712 1    80.77  ? 7   PHE A CD2   1 
ATOM   57   C  CE1   . PHE A 1 7   ? 102.145 16.739  43.52  1    81.44  ? 7   PHE A CE1   1 
ATOM   58   C  CE2   . PHE A 1 7   ? 101.786 18.579  44.968 1    81.36  ? 7   PHE A CE2   1 
ATOM   59   C  CZ    . PHE A 1 7   ? 101.329 17.44   44.368 1    81.16  ? 7   PHE A CZ    1 
ATOM   60   N  N     . ALA A 1 8   ? 108.842 17.768  44.53  1    81.99  ? 8   ALA A N     1 
ATOM   61   C  CA    . ALA A 1 8   ? 110.2   17.47   44.075 1    83.31  ? 8   ALA A CA    1 
ATOM   62   C  C     . ALA A 1 8   ? 110.052 16.244  43.166 1    84.45  ? 8   ALA A C     1 
ATOM   63   O  O     . ALA A 1 8   ? 109.34  15.303  43.519 1    84.57  ? 8   ALA A O     1 
ATOM   64   C  CB    . ALA A 1 8   ? 111.071 17.097  45.271 1    83.53  ? 8   ALA A CB    1 
ATOM   65   N  N     . VAL A 1 9   ? 110.633 16.292  41.974 1    85.18  ? 9   VAL A N     1 
ATOM   66   C  CA    . VAL A 1 9   ? 110.486 15.217  40.99  1    86.41  ? 9   VAL A CA    1 
ATOM   67   C  C     . VAL A 1 9   ? 111.163 13.885  41.38  1    87.37  ? 9   VAL A C     1 
ATOM   68   O  O     . VAL A 1 9   ? 110.927 12.868  40.719 1    87.3   ? 9   VAL A O     1 
ATOM   69   C  CB    . VAL A 1 9   ? 110.967 15.706  39.61  1    87.13  ? 9   VAL A CB    1 
ATOM   70   C  CG1   . VAL A 1 9   ? 110.03  16.781  39.073 1    87.68  ? 9   VAL A CG1   1 
ATOM   71   C  CG2   . VAL A 1 9   ? 112.398 16.231  39.69  1    87.63  ? 9   VAL A CG2   1 
ATOM   72   N  N     . ASP A 1 10  ? 111.967 13.892  42.474 1    87.82  ? 10  ASP A N     1 
ATOM   73   C  CA    . ASP A 1 10  ? 112.745 12.744  42.941 1    88.63  ? 10  ASP A CA    1 
ATOM   74   C  C     . ASP A 1 10  ? 112.704 12.559  44.466 1    88.57  ? 10  ASP A C     1 
ATOM   75   O  O     . ASP A 1 10  ? 112.944 13.516  45.202 1    88.89  ? 10  ASP A O     1 
ATOM   76   C  CB    . ASP A 1 10  ? 114.209 12.935  42.454 1    91.13  ? 10  ASP A CB    1 
ATOM   77   C  CG    . ASP A 1 10  ? 115.313 12.176  43.179 1    96.61  ? 10  ASP A CG    1 
ATOM   78   O  OD1   . ASP A 1 10  ? 115.203 10.934  43.298 1    97.75  ? 10  ASP A OD1   1 
ATOM   79   O  OD2   . ASP A 1 10  ? 116.296 12.825  43.608 1    98.79  ? 10  ASP A OD2   1 
ATOM   80   N  N     . THR A 1 11  ? 112.454 11.315  44.937 1    88.06  ? 11  THR A N     1 
ATOM   81   C  CA    . THR A 1 11  ? 112.512 10.983  46.359 1    88.03  ? 11  THR A CA    1 
ATOM   82   C  C     . THR A 1 11  ? 113.444 9.773   46.571 1    88.03  ? 11  THR A C     1 
ATOM   83   O  O     . THR A 1 11  ? 113.493 8.88    45.725 1    88.06  ? 11  THR A O     1 
ATOM   84   C  CB    . THR A 1 11  ? 111.125 10.774  46.967 1    89     ? 11  THR A CB    1 
ATOM   85   O  OG1   . THR A 1 11  ? 110.466 9.747   46.243 1    89.97  ? 11  THR A OG1   1 
ATOM   86   C  CG2   . THR A 1 11  ? 110.271 12.034  46.964 1    89.27  ? 11  THR A CG2   1 
ATOM   87   N  N     . LYS A 1 12  ? 114.204 9.751   47.673 1    87.89  ? 12  LYS A N     1 
ATOM   88   C  CA    . LYS A 1 12  ? 115.135 8.65    47.943 1    88.26  ? 12  LYS A CA    1 
ATOM   89   C  C     . LYS A 1 12  ? 114.419 7.472   48.607 1    88.34  ? 12  LYS A C     1 
ATOM   90   O  O     . LYS A 1 12  ? 113.519 7.682   49.414 1    88.34  ? 12  LYS A O     1 
ATOM   91   C  CB    . LYS A 1 12  ? 116.306 9.134   48.82  1    90.04  ? 12  LYS A CB    1 
ATOM   92   C  CG    . LYS A 1 12  ? 117.499 8.177   48.869 1    94.05  ? 12  LYS A CG    1 
ATOM   93   C  CD    . LYS A 1 12  ? 118.545 8.637   49.881 1    98.45  ? 12  LYS A CD    1 
ATOM   94   C  CE    . LYS A 1 12  ? 119.705 7.676   50.039 1    102.2  ? 12  LYS A CE    1 
ATOM   95   N  NZ    . LYS A 1 12  ? 120.581 8.046   51.193 1    104.5  ? 12  LYS A NZ    1 
ATOM   96   N  N     . VAL A 1 13  ? 114.814 6.234   48.275 1    88.16  ? 13  VAL A N     1 
ATOM   97   C  CA    . VAL A 1 13  ? 114.205 5.04    48.861 1    88.34  ? 13  VAL A CA    1 
ATOM   98   C  C     . VAL A 1 13  ? 114.866 4.661   50.199 1    88.31  ? 13  VAL A C     1 
ATOM   99   O  O     . VAL A 1 13  ? 116.08  4.495   50.264 1    88.41  ? 13  VAL A O     1 
ATOM   100  C  CB    . VAL A 1 13  ? 114.183 3.873   47.845 1    89.09  ? 13  VAL A CB    1 
ATOM   101  C  CG1   . VAL A 1 13  ? 113.834 2.55    48.518 1    89.79  ? 13  VAL A CG1   1 
ATOM   102  C  CG2   . VAL A 1 13  ? 113.216 4.171   46.704 1    89.38  ? 13  VAL A CG2   1 
ATOM   103  N  N     . ILE A 1 14  ? 114.055 4.538   51.261 1    88.06  ? 14  ILE A N     1 
ATOM   104  C  CA    . ILE A 1 14  ? 114.479 4.226   52.631 1    88.23  ? 14  ILE A CA    1 
ATOM   105  C  C     . ILE A 1 14  ? 114.419 2.718   52.96  1    88.73  ? 14  ILE A C     1 
ATOM   106  O  O     . ILE A 1 14  ? 115.311 2.214   53.647 1    89.06  ? 14  ILE A O     1 
ATOM   107  C  CB    . ILE A 1 14  ? 113.657 5.066   53.648 1    88.2   ? 14  ILE A CB    1 
ATOM   108  C  CG1   . ILE A 1 14  ? 113.682 6.563   53.303 1    88.79  ? 14  ILE A CG1   1 
ATOM   109  C  CG2   . ILE A 1 14  ? 114.107 4.819   55.08  1    88.63  ? 14  ILE A CG2   1 
ATOM   110  C  CD1   . ILE A 1 14  ? 115.039 7.173   53.319 1    89.99  ? 14  ILE A CD1   1 
ATOM   111  N  N     . ASP A 1 15  ? 113.382 1.998   52.485 1    88.58  ? 15  ASP A N     1 
ATOM   112  C  CA    . ASP A 1 15  ? 113.26  0.566   52.778 1    88.97  ? 15  ASP A CA    1 
ATOM   113  C  C     . ASP A 1 15  ? 112.557 -0.235  51.665 1    89.58  ? 15  ASP A C     1 
ATOM   114  O  O     . ASP A 1 15  ? 111.879 0.35    50.825 1    89.83  ? 15  ASP A O     1 
ATOM   115  C  CB    . ASP A 1 15  ? 112.563 0.352   54.13  1    90.07  ? 15  ASP A CB    1 
ATOM   116  C  CG    . ASP A 1 15  ? 113.039 -0.892  54.841 1    93.76  ? 15  ASP A CG    1 
ATOM   117  O  OD1   . ASP A 1 15  ? 114.131 -0.847  55.45  1    94.4   ? 15  ASP A OD1   1 
ATOM   118  O  OD2   . ASP A 1 15  ? 112.333 -1.912  54.778 1    95.62  ? 15  ASP A OD2   1 
ATOM   119  N  N     . SER A 1 16  ? 112.721 -1.572  51.654 1    89.58  ? 16  SER A N     1 
ATOM   120  C  CA    . SER A 1 16  ? 112.106 -2.433  50.64  1    89.94  ? 16  SER A CA    1 
ATOM   121  C  C     . SER A 1 16  ? 111.766 -3.821  51.206 1    90.23  ? 16  SER A C     1 
ATOM   122  O  O     . SER A 1 16  ? 112.665 -4.631  51.421 1    90.54  ? 16  SER A O     1 
ATOM   123  C  CB    . SER A 1 16  ? 113.035 -2.571  49.436 1    91.12  ? 16  SER A CB    1 
ATOM   124  O  OG    . SER A 1 16  ? 112.564 -3.505  48.478 1    93.23  ? 16  SER A OG    1 
ATOM   125  N  N     . ARG A 1 17  ? 110.478 -4.103  51.439 1    90.01  ? 17  ARG A N     1 
ATOM   126  C  CA    . ARG A 1 17  ? 110.06  -5.402  51.969 1    90.39  ? 17  ARG A CA    1 
ATOM   127  C  C     . ARG A 1 17  ? 109.002 -6.077  51.092 1    90.28  ? 17  ARG A C     1 
ATOM   128  O  O     . ARG A 1 17  ? 108.259 -5.394  50.39  1    90.46  ? 17  ARG A O     1 
ATOM   129  C  CB    . ARG A 1 17  ? 109.535 -5.252  53.401 1    92.11  ? 17  ARG A CB    1 
ATOM   130  C  CG    . ARG A 1 17  ? 110.633 -4.973  54.416 1    96.23  ? 17  ARG A CG    1 
ATOM   131  C  CD    . ARG A 1 17  ? 110.085 -4.93   55.831 1    100.08 ? 17  ARG A CD    1 
ATOM   132  N  NE    . ARG A 1 17  ? 110.381 -3.666  56.507 1    103.49 ? 17  ARG A NE    1 
ATOM   133  C  CZ    . ARG A 1 17  ? 109.646 -2.562  56.394 1    106.42 ? 17  ARG A CZ    1 
ATOM   134  N  NH1   . ARG A 1 17  ? 108.583 -2.541  55.599 1    106.34 ? 17  ARG A NH1   1 
ATOM   135  N  NH2   . ARG A 1 17  ? 109.989 -1.461  57.049 1    106.76 ? 17  ARG A NH2   1 
ATOM   136  N  N     . LEU A 1 18  ? 108.915 -7.412  51.14  1    89.83  ? 18  LEU A N     1 
ATOM   137  C  CA    . LEU A 1 18  ? 107.91  -8.146  50.364 1    89.89  ? 18  LEU A CA    1 
ATOM   138  C  C     . LEU A 1 18  ? 106.677 -8.375  51.242 1    90.05  ? 18  LEU A C     1 
ATOM   139  O  O     . LEU A 1 18  ? 106.515 -9.456  51.808 1    90.23  ? 18  LEU A O     1 
ATOM   140  C  CB    . LEU A 1 18  ? 108.475 -9.493  49.881 1    89.96  ? 18  LEU A CB    1 
ATOM   141  C  CG    . LEU A 1 18  ? 109.053 -9.532  48.469 1    91.34  ? 18  LEU A CG    1 
ATOM   142  C  CD1   . LEU A 1 18  ? 108.04  -9.069  47.448 1    91.98  ? 18  LEU A CD1   1 
ATOM   143  C  CD2   . LEU A 1 18  ? 110.32  -8.716  48.365 1    91.96  ? 18  LEU A CD2   1 
ATOM   144  N  N     . VAL A 1 19  ? 105.812 -7.355  51.367 1    89.76  ? 19  VAL A N     1 
ATOM   145  C  CA    . VAL A 1 19  ? 104.656 -7.414  52.261 1    89.85  ? 19  VAL A CA    1 
ATOM   146  C  C     . VAL A 1 19  ? 103.428 -8.139  51.702 1    89.83  ? 19  VAL A C     1 
ATOM   147  O  O     . VAL A 1 19  ? 102.703 -8.754  52.485 1    90.09  ? 19  VAL A O     1 
ATOM   148  C  CB    . VAL A 1 19  ? 104.261 -6.02   52.785 1    90.45  ? 19  VAL A CB    1 
ATOM   149  C  CG1   . VAL A 1 19  ? 105.438 -5.358  53.489 1    91.01  ? 19  VAL A CG1   1 
ATOM   150  C  CG2   . VAL A 1 19  ? 103.723 -5.138  51.665 1    90.85  ? 19  VAL A CG2   1 
ATOM   151  N  N     . GLY A 1 20  ? 103.19  -8.074  50.393 1    89.31  ? 20  GLY A N     1 
ATOM   152  C  CA    . GLY A 1 20  ? 102.034 -8.743  49.804 1    89.39  ? 20  GLY A CA    1 
ATOM   153  C  C     . GLY A 1 20  ? 102.231 -10.239 49.648 1    89.37  ? 20  GLY A C     1 
ATOM   154  O  O     . GLY A 1 20  ? 101.606 -10.861 48.784 1    89.5   ? 20  GLY A O     1 
ATOM   155  N  N     . GLU A 1 21  ? 103.114 -10.826 50.491 1    89.05  ? 21  GLU A N     1 
ATOM   156  C  CA    . GLU A 1 21  ? 103.519 -12.229 50.473 1    89.06  ? 21  GLU A CA    1 
ATOM   157  C  C     . GLU A 1 21  ? 104.053 -12.592 49.091 1    88.35  ? 21  GLU A C     1 
ATOM   158  O  O     . GLU A 1 21  ? 103.629 -13.571 48.48  1    88.55  ? 21  GLU A O     1 
ATOM   159  C  CB    . GLU A 1 21  ? 102.401 -13.158 50.966 1    91.73  ? 21  GLU A CB    1 
ATOM   160  C  CG    . GLU A 1 21  ? 102.488 -13.453 52.454 1    97.54  ? 21  GLU A CG    1 
ATOM   161  C  CD    . GLU A 1 21  ? 102.512 -12.257 53.391 1    105.19 ? 21  GLU A CD    1 
ATOM   162  O  OE1   . GLU A 1 21  ? 101.825 -11.252 53.097 1    106.5  ? 21  GLU A OE1   1 
ATOM   163  O  OE2   . GLU A 1 21  ? 103.201 -12.335 54.435 1    107.74 ? 21  GLU A OE2   1 
ATOM   164  N  N     . GLY A 1 22  ? 104.95  -11.739 48.601 1    87.24  ? 22  GLY A N     1 
ATOM   165  C  CA    . GLY A 1 22  ? 105.576 -11.865 47.296 1    86.45  ? 22  GLY A CA    1 
ATOM   166  C  C     . GLY A 1 22  ? 104.864 -11.095 46.206 1    85.28  ? 22  GLY A C     1 
ATOM   167  O  O     . GLY A 1 22  ? 105.495 -10.571 45.284 1    85.57  ? 22  GLY A O     1 
ATOM   168  N  N     . SER A 1 23  ? 103.542 -11.028 46.296 1    83.78  ? 23  SER A N     1 
ATOM   169  C  CA    . SER A 1 23  ? 102.708 -10.356 45.309 1    82.7   ? 23  SER A CA    1 
ATOM   170  C  C     . SER A 1 23  ? 102.962 -8.834  45.204 1    81.13  ? 23  SER A C     1 
ATOM   171  O  O     . SER A 1 23  ? 102.715 -8.251  44.149 1    81.12  ? 23  SER A O     1 
ATOM   172  C  CB    . SER A 1 23  ? 101.239 -10.647 45.605 1    83.98  ? 23  SER A CB    1 
ATOM   173  O  OG    . SER A 1 23  ? 100.408 -10.54  44.462 1    86.16  ? 23  SER A OG    1 
ATOM   174  N  N     . SER A 1 24  ? 103.475 -8.197  46.275 1    79.63  ? 24  SER A N     1 
ATOM   175  C  CA    . SER A 1 24  ? 103.712 -6.752  46.257 1    78.6   ? 24  SER A CA    1 
ATOM   176  C  C     . SER A 1 24  ? 104.979 -6.303  47.01  1    77.34  ? 24  SER A C     1 
ATOM   177  O  O     . SER A 1 24  ? 105.344 -6.9    48.021 1    77.57  ? 24  SER A O     1 
ATOM   178  C  CB    . SER A 1 24  ? 102.49  -6.023  46.808 1    79.75  ? 24  SER A CB    1 
ATOM   179  O  OG    . SER A 1 24  ? 102.698 -4.623  46.878 1    81.99  ? 24  SER A OG    1 
ATOM   180  N  N     . VAL A 1 25  ? 105.622 -5.223  46.529 1    75.89  ? 25  VAL A N     1 
ATOM   181  C  CA    . VAL A 1 25  ? 106.815 -4.637  47.141 1    75.04  ? 25  VAL A CA    1 
ATOM   182  C  C     . VAL A 1 25  ? 106.451 -3.334  47.837 1    74.08  ? 25  VAL A C     1 
ATOM   183  O  O     . VAL A 1 25  ? 105.944 -2.411  47.202 1    73.94  ? 25  VAL A O     1 
ATOM   184  C  CB    . VAL A 1 25  ? 107.949 -4.429  46.107 1    75.65  ? 25  VAL A CB    1 
ATOM   185  C  CG1   . VAL A 1 25  ? 109.052 -3.514  46.646 1    76.32  ? 25  VAL A CG1   1 
ATOM   186  C  CG2   . VAL A 1 25  ? 108.528 -5.762  45.668 1    76.06  ? 25  VAL A CG2   1 
ATOM   187  N  N     . ARG A 1 26  ? 106.718 -3.256  49.139 1    73.26  ? 26  ARG A N     1 
ATOM   188  C  CA    . ARG A 1 26  ? 106.431 -2.053  49.898 1    73.03  ? 26  ARG A CA    1 
ATOM   189  C  C     . ARG A 1 26  ? 107.707 -1.266  50.069 1    72.6   ? 26  ARG A C     1 
ATOM   190  O  O     . ARG A 1 26  ? 108.738 -1.829  50.426 1    72.56  ? 26  ARG A O     1 
ATOM   191  C  CB    . ARG A 1 26  ? 105.847 -2.414  51.261 1    74.54  ? 26  ARG A CB    1 
ATOM   192  C  CG    . ARG A 1 26  ? 105.611 -1.231  52.179 1    77.7   ? 26  ARG A CG    1 
ATOM   193  C  CD    . ARG A 1 26  ? 105.531 -1.705  53.604 1    81     ? 26  ARG A CD    1 
ATOM   194  N  NE    . ARG A 1 26  ? 104.355 -1.165  54.28  1    83.97  ? 26  ARG A NE    1 
ATOM   195  C  CZ    . ARG A 1 26  ? 104.381 -0.136  55.121 1    86.03  ? 26  ARG A CZ    1 
ATOM   196  N  NH1   . ARG A 1 26  ? 105.531 0.468   55.411 1    84.97  ? 26  ARG A NH1   1 
ATOM   197  N  NH2   . ARG A 1 26  ? 103.26  0.294   55.688 1    86.27  ? 26  ARG A NH2   1 
ATOM   198  N  N     . ARG A 1 27  ? 107.647 0.034   49.808 1    72.26  ? 27  ARG A N     1 
ATOM   199  C  CA    . ARG A 1 27  ? 108.804 0.895   49.952 1    72.59  ? 27  ARG A CA    1 
ATOM   200  C  C     . ARG A 1 27  ? 108.482 2.095   50.818 1    73.39  ? 27  ARG A C     1 
ATOM   201  O  O     . ARG A 1 27  ? 107.343 2.553   50.881 1    73.29  ? 27  ARG A O     1 
ATOM   202  C  CB    . ARG A 1 27  ? 109.297 1.39    48.582 1    73.23  ? 27  ARG A CB    1 
ATOM   203  C  CG    . ARG A 1 27  ? 109.739 0.298   47.642 1    75.05  ? 27  ARG A CG    1 
ATOM   204  C  CD    . ARG A 1 27  ? 110.265 0.886   46.342 1    76.62  ? 27  ARG A CD    1 
ATOM   205  N  NE    . ARG A 1 27  ? 110.097 -0.036  45.211 1    77.2   ? 27  ARG A NE    1 
ATOM   206  C  CZ    . ARG A 1 27  ? 110.965 -0.99   44.89  1    78.29  ? 27  ARG A CZ    1 
ATOM   207  N  NH1   . ARG A 1 27  ? 112.098 -1.124  45.57  1    78.26  ? 27  ARG A NH1   1 
ATOM   208  N  NH2   . ARG A 1 27  ? 110.736 -1.782  43.858 1    77.64  ? 27  ARG A NH2   1 
ATOM   209  N  N     . ARG A 1 28  ? 109.502 2.61    51.474 1    73.96  ? 28  ARG A N     1 
ATOM   210  C  CA    . ARG A 1 28  ? 109.397 3.846   52.214 1    75.04  ? 28  ARG A CA    1 
ATOM   211  C  C     . ARG A 1 28  ? 110.237 4.844   51.412 1    75.74  ? 28  ARG A C     1 
ATOM   212  O  O     . ARG A 1 28  ? 111.283 4.474   50.869 1    75.75  ? 28  ARG A O     1 
ATOM   213  C  CB    . ARG A 1 28  ? 109.952 3.683   53.623 1    76.86  ? 28  ARG A CB    1 
ATOM   214  C  CG    . ARG A 1 28  ? 109.264 4.582   54.623 1    80.77  ? 28  ARG A CG    1 
ATOM   215  C  CD    . ARG A 1 28  ? 107.859 4.111   54.931 1    84.51  ? 28  ARG A CD    1 
ATOM   216  N  NE    . ARG A 1 28  ? 107.464 4.5     56.286 1    87.8   ? 28  ARG A NE    1 
ATOM   217  C  CZ    . ARG A 1 28  ? 106.877 5.651   56.596 1    90.16  ? 28  ARG A CZ    1 
ATOM   218  N  NH1   . ARG A 1 28  ? 106.583 6.532   55.647 1    89.68  ? 28  ARG A NH1   1 
ATOM   219  N  NH2   . ARG A 1 28  ? 106.567 5.926   57.857 1    90.33  ? 28  ARG A NH2   1 
ATOM   220  N  N     . ARG A 1 29  ? 109.755 6.076   51.261 1    76.07  ? 29  ARG A N     1 
ATOM   221  C  CA    . ARG A 1 29  ? 110.487 7.086   50.499 1    76.79  ? 29  ARG A CA    1 
ATOM   222  C  C     . ARG A 1 29  ? 110.568 8.386   51.287 1    77.63  ? 29  ARG A C     1 
ATOM   223  O  O     . ARG A 1 29  ? 109.628 8.738   51.992 1    77.64  ? 29  ARG A O     1 
ATOM   224  C  CB    . ARG A 1 29  ? 109.871 7.303   49.102 1    77.66  ? 29  ARG A CB    1 
ATOM   225  C  CG    . ARG A 1 29  ? 110.384 6.348   48.025 1    79.66  ? 29  ARG A CG    1 
ATOM   226  C  CD    . ARG A 1 29  ? 109.577 6.451   46.735 1    81.7   ? 29  ARG A CD    1 
ATOM   227  N  NE    . ARG A 1 29  ? 110.174 5.698   45.626 1    83.02  ? 29  ARG A NE    1 
ATOM   228  C  CZ    . ARG A 1 29  ? 110.94  6.234   44.679 1    84.62  ? 29  ARG A CZ    1 
ATOM   229  N  NH1   . ARG A 1 29  ? 111.216 7.532   44.694 1    84.01  ? 29  ARG A NH1   1 
ATOM   230  N  NH2   . ARG A 1 29  ? 111.433 5.477   43.708 1    84.68  ? 29  ARG A NH2   1 
ATOM   231  N  N     . GLN A 1 30  ? 111.699 9.083   51.191 1    78.2   ? 30  GLN A N     1 
ATOM   232  C  CA    . GLN A 1 30  ? 111.879 10.345  51.898 1    79.23  ? 30  GLN A CA    1 
ATOM   233  C  C     . GLN A 1 30  ? 112.151 11.44   50.901 1    79.69  ? 30  GLN A C     1 
ATOM   234  O  O     . GLN A 1 30  ? 112.95  11.248  49.982 1    80.23  ? 30  GLN A O     1 
ATOM   235  C  CB    . GLN A 1 30  ? 113.029 10.265  52.905 1    81.49  ? 30  GLN A CB    1 
ATOM   236  C  CG    . GLN A 1 30  ? 113.266 11.577  53.644 1    86.48  ? 30  GLN A CG    1 
ATOM   237  C  CD    . GLN A 1 30  ? 114.195 11.411  54.813 1    93.29  ? 30  GLN A CD    1 
ATOM   238  O  OE1   . GLN A 1 30  ? 114.254 10.347  55.441 1    95.55  ? 30  GLN A OE1   1 
ATOM   239  N  NE2   . GLN A 1 30  ? 114.937 12.464  55.143 1    94.7   ? 30  GLN A NE2   1 
ATOM   240  N  N     . CYS A 1 31  ? 111.487 12.585  51.066 1    79.24  ? 31  CYS A N     1 
ATOM   241  C  CA    . CYS A 1 31  ? 111.699 13.7    50.167 1    79.31  ? 31  CYS A CA    1 
ATOM   242  C  C     . CYS A 1 31  ? 112.935 14.47   50.58  1    79.24  ? 31  CYS A C     1 
ATOM   243  O  O     . CYS A 1 31  ? 113.186 14.667  51.763 1    79.27  ? 31  CYS A O     1 
ATOM   244  C  CB    . CYS A 1 31  ? 110.474 14.599  50.085 1    79.73  ? 31  CYS A CB    1 
ATOM   245  S  SG    . CYS A 1 31  ? 110.628 15.92   48.858 1    81.74  ? 31  CYS A SG    1 
ATOM   246  N  N     . LEU A 1 32  ? 113.725 14.87   49.604 1    79.02  ? 32  LEU A N     1 
ATOM   247  C  CA    . LEU A 1 32  ? 114.959 15.596  49.86  1    79.39  ? 32  LEU A CA    1 
ATOM   248  C  C     . LEU A 1 32  ? 114.655 17.071  50.162 1    79.4   ? 32  LEU A C     1 
ATOM   249  O  O     . LEU A 1 32  ? 115.278 17.655  51.048 1    79.74  ? 32  LEU A O     1 
ATOM   250  C  CB    . LEU A 1 32  ? 115.901 15.45   48.651 1    79.81  ? 32  LEU A CB    1 
ATOM   251  C  CG    . LEU A 1 32  ? 116.79  14.19   48.551 1    81.54  ? 32  LEU A CG    1 
ATOM   252  C  CD1   . LEU A 1 32  ? 116.049 12.897  48.865 1    82.04  ? 32  LEU A CD1   1 
ATOM   253  C  CD2   . LEU A 1 32  ? 117.372 14.059  47.15  1    82.41  ? 32  LEU A CD2   1 
ATOM   254  N  N     . VAL A 1 33  ? 113.656 17.65   49.471 1    78.93  ? 33  VAL A N     1 
ATOM   255  C  CA    . VAL A 1 33  ? 113.252 19.044  49.636 1    79.02  ? 33  VAL A CA    1 
ATOM   256  C  C     . VAL A 1 33  ? 112.483 19.321  50.939 1    78.81  ? 33  VAL A C     1 
ATOM   257  O  O     . VAL A 1 33  ? 112.915 20.175  51.715 1    79.1   ? 33  VAL A O     1 
ATOM   258  C  CB    . VAL A 1 33  ? 112.463 19.555  48.405 1    79.98  ? 33  VAL A CB    1 
ATOM   259  C  CG1   . VAL A 1 33  ? 112.11  21.032  48.563 1    80.65  ? 33  VAL A CG1   1 
ATOM   260  C  CG2   . VAL A 1 33  ? 113.236 19.311  47.113 1    80.44  ? 33  VAL A CG2   1 
ATOM   261  N  N     . CYS A 1 34  ? 111.359 18.618  51.189 1    78.15  ? 34  CYS A N     1 
ATOM   262  C  CA    . CYS A 1 34  ? 110.551 18.875  52.383 1    78.03  ? 34  CYS A CA    1 
ATOM   263  C  C     . CYS A 1 34  ? 110.785 17.895  53.54  1    77.4   ? 34  CYS A C     1 
ATOM   264  O  O     . CYS A 1 34  ? 110.1   18.003  54.556 1    77.31  ? 34  CYS A O     1 
ATOM   265  C  CB    . CYS A 1 34  ? 109.069 18.959  52.025 1    79.03  ? 34  CYS A CB    1 
ATOM   266  S  SG    . CYS A 1 34  ? 108.323 17.376  51.548 1    83     ? 34  CYS A SG    1 
ATOM   267  N  N     . ASN A 1 35  ? 111.729 16.949  53.392 1    76.82  ? 35  ASN A N     1 
ATOM   268  C  CA    . ASN A 1 35  ? 112.109 15.932  54.388 1    76.75  ? 35  ASN A CA    1 
ATOM   269  C  C     . ASN A 1 35  ? 110.951 15.057  54.879 1    75.76  ? 35  ASN A C     1 
ATOM   270  O  O     . ASN A 1 35  ? 111.033 14.502  55.975 1    76.05  ? 35  ASN A O     1 
ATOM   271  C  CB    . ASN A 1 35  ? 112.863 16.53   55.577 1    78.68  ? 35  ASN A CB    1 
ATOM   272  C  CG    . ASN A 1 35  ? 113.855 17.613  55.221 1    83.21  ? 35  ASN A CG    1 
ATOM   273  O  OD1   . ASN A 1 35  ? 114.748 17.459  54.365 1    84.91  ? 35  ASN A OD1   1 
ATOM   274  N  ND2   . ASN A 1 35  ? 113.718 18.744  55.883 1    84.08  ? 35  ASN A ND2   1 
ATOM   275  N  N     . GLU A 1 36  ? 109.892 14.909  54.07  1    74.4   ? 36  GLU A N     1 
ATOM   276  C  CA    . GLU A 1 36  ? 108.737 14.107  54.466 1    73.45  ? 36  GLU A CA    1 
ATOM   277  C  C     . GLU A 1 36  ? 108.849 12.658  54.043 1    72.03  ? 36  GLU A C     1 
ATOM   278  O  O     . GLU A 1 36  ? 109.472 12.364  53.03  1    72.04  ? 36  GLU A O     1 
ATOM   279  C  CB    . GLU A 1 36  ? 107.44  14.705  53.909 1    75.51  ? 36  GLU A CB    1 
ATOM   280  C  CG    . GLU A 1 36  ? 106.991 15.976  54.603 1    79.66  ? 36  GLU A CG    1 
ATOM   281  C  CD    . GLU A 1 36  ? 106.524 15.82   56.037 1    84.26  ? 36  GLU A CD    1 
ATOM   282  O  OE1   . GLU A 1 36  ? 106.231 14.676  56.457 1    85.58  ? 36  GLU A OE1   1 
ATOM   283  O  OE2   . GLU A 1 36  ? 106.433 16.855  56.737 1    84.97  ? 36  GLU A OE2   1 
ATOM   284  N  N     . ARG A 1 37  ? 108.211 11.752  54.793 1    70.64  ? 37  ARG A N     1 
ATOM   285  C  CA    . ARG A 1 37  ? 108.236 10.333  54.458 1    69.86  ? 37  ARG A CA    1 
ATOM   286  C  C     . ARG A 1 37  ? 106.865 9.816   54.005 1    68.06  ? 37  ARG A C     1 
ATOM   287  O  O     . ARG A 1 37  ? 105.833 10.329  54.435 1    68.32  ? 37  ARG A O     1 
ATOM   288  C  CB    . ARG A 1 37  ? 108.802 9.504   55.623 1    71.88  ? 37  ARG A CB    1 
ATOM   289  C  CG    . ARG A 1 37  ? 110.232 9.891   55.991 1    75.96  ? 37  ARG A CG    1 
ATOM   290  C  CD    . ARG A 1 37  ? 110.805 8.992   57.075 1    80.22  ? 37  ARG A CD    1 
ATOM   291  N  NE    . ARG A 1 37  ? 112.214 9.28    57.331 1    84.47  ? 37  ARG A NE    1 
ATOM   292  C  CZ    . ARG A 1 37  ? 112.826 9.115   58.498 1    87.93  ? 37  ARG A CZ    1 
ATOM   293  N  NH1   . ARG A 1 37  ? 112.151 8.672   59.553 1    87.86  ? 37  ARG A NH1   1 
ATOM   294  N  NH2   . ARG A 1 37  ? 114.116 9.406   58.626 1    88.36  ? 37  ARG A NH2   1 
ATOM   295  N  N     . PHE A 1 38  ? 106.857 8.819   53.116 1    66.06  ? 38  PHE A N     1 
ATOM   296  C  CA    . PHE A 1 38  ? 105.62  8.234   52.6   1    64.52  ? 38  PHE A CA    1 
ATOM   297  C  C     . PHE A 1 38  ? 105.83  6.802   52.16  1    62.81  ? 38  PHE A C     1 
ATOM   298  O  O     . PHE A 1 38  ? 106.938 6.417   51.803 1    62.94  ? 38  PHE A O     1 
ATOM   299  C  CB    . PHE A 1 38  ? 105.006 9.072   51.469 1    64.2   ? 38  PHE A CB    1 
ATOM   300  C  CG    . PHE A 1 38  ? 105.878 9.261   50.252 1    64.71  ? 38  PHE A CG    1 
ATOM   301  C  CD1   . PHE A 1 38  ? 106.874 10.221  50.237 1    65.31  ? 38  PHE A CD1   1 
ATOM   302  C  CD2   . PHE A 1 38  ? 105.656 8.526   49.096 1    65.37  ? 38  PHE A CD2   1 
ATOM   303  C  CE1   . PHE A 1 38  ? 107.662 10.409  49.111 1    65.83  ? 38  PHE A CE1   1 
ATOM   304  C  CE2   . PHE A 1 38  ? 106.439 8.726   47.968 1    65.85  ? 38  PHE A CE2   1 
ATOM   305  C  CZ    . PHE A 1 38  ? 107.43  9.67    47.98  1    65.58  ? 38  PHE A CZ    1 
ATOM   306  N  N     . THR A 1 39  ? 104.768 6.006   52.207 1    61.16  ? 39  THR A N     1 
ATOM   307  C  CA    . THR A 1 39  ? 104.819 4.597   51.843 1    60.15  ? 39  THR A CA    1 
ATOM   308  C  C     . THR A 1 39  ? 104.316 4.381   50.411 1    58.81  ? 39  THR A C     1 
ATOM   309  O  O     . THR A 1 39  ? 103.396 5.065   49.971 1    58.97  ? 39  THR A O     1 
ATOM   310  C  CB    . THR A 1 39  ? 103.98  3.821   52.864 1    61.21  ? 39  THR A CB    1 
ATOM   311  O  OG1   . THR A 1 39  ? 104.646 3.856   54.126 1    62.2   ? 39  THR A OG1   1 
ATOM   312  C  CG2   . THR A 1 39  ? 103.703 2.385   52.444 1    61.37  ? 39  THR A CG2   1 
ATOM   313  N  N     . THR A 1 40  ? 104.94  3.467   49.664 1    57.29  ? 40  THR A N     1 
ATOM   314  C  CA    . THR A 1 40  ? 104.482 3.13    48.321 1    56.33  ? 40  THR A CA    1 
ATOM   315  C  C     . THR A 1 40  ? 104.351 1.613   48.165 1    55.26  ? 40  THR A C     1 
ATOM   316  O  O     . THR A 1 40  ? 105.05  0.848   48.827 1    55.4   ? 40  THR A O     1 
ATOM   317  C  CB    . THR A 1 40  ? 105.365 3.732   47.204 1    57.41  ? 40  THR A CB    1 
ATOM   318  O  OG1   . THR A 1 40  ? 106.54  2.95    47.053 1    57.99  ? 40  THR A OG1   1 
ATOM   319  C  CG2   . THR A 1 40  ? 105.724 5.192   47.43  1    58.07  ? 40  THR A CG2   1 
ATOM   320  N  N     . PHE A 1 41  ? 103.487 1.185   47.256 1    54.12  ? 41  PHE A N     1 
ATOM   321  C  CA    . PHE A 1 41  ? 103.31  -0.228  46.966 1    53.34  ? 41  PHE A CA    1 
ATOM   322  C  C     . PHE A 1 41  ? 103.487 -0.433  45.473 1    52.19  ? 41  PHE A C     1 
ATOM   323  O  O     . PHE A 1 41  ? 102.945 0.326   44.682 1    52.21  ? 41  PHE A O     1 
ATOM   324  C  CB    . PHE A 1 41  ? 101.941 -0.735  47.447 1    53.24  ? 41  PHE A CB    1 
ATOM   325  C  CG    . PHE A 1 41  ? 101.804 -0.78   48.957 1    53.77  ? 41  PHE A CG    1 
ATOM   326  C  CD1   . PHE A 1 41  ? 102.331 -1.831  49.688 1    54.56  ? 41  PHE A CD1   1 
ATOM   327  C  CD2   . PHE A 1 41  ? 101.137 0.223   49.643 1    54.34  ? 41  PHE A CD2   1 
ATOM   328  C  CE1   . PHE A 1 41  ? 102.199 -1.871  51.077 1    55.01  ? 41  PHE A CE1   1 
ATOM   329  C  CE2   . PHE A 1 41  ? 101.014 0.181   51.032 1    54.81  ? 41  PHE A CE2   1 
ATOM   330  C  CZ    . PHE A 1 41  ? 101.546 -0.864  51.737 1    54.57  ? 41  PHE A CZ    1 
ATOM   331  N  N     . GLU A 1 42  ? 104.296 -1.421  45.092 1    51.12  ? 42  GLU A N     1 
ATOM   332  C  CA    . GLU A 1 42  ? 104.566 -1.763  43.7   1    50.48  ? 42  GLU A CA    1 
ATOM   333  C  C     . GLU A 1 42  ? 103.848 -3.061  43.407 1    49.94  ? 42  GLU A C     1 
ATOM   334  O  O     . GLU A 1 42  ? 104.101 -4.069  44.062 1    49.93  ? 42  GLU A O     1 
ATOM   335  C  CB    . GLU A 1 42  ? 106.067 -1.923  43.465 1    52.06  ? 42  GLU A CB    1 
ATOM   336  C  CG    . GLU A 1 42  ? 106.402 -2.274  42.035 1    55.77  ? 42  GLU A CG    1 
ATOM   337  C  CD    . GLU A 1 42  ? 107.836 -2.709  41.8   1    60.94  ? 42  GLU A CD    1 
ATOM   338  O  OE1   . GLU A 1 42  ? 108.671 -2.505  42.706 1    61.45  ? 42  GLU A OE1   1 
ATOM   339  O  OE2   . GLU A 1 42  ? 108.127 -3.268  40.718 1    62.93  ? 42  GLU A OE2   1 
ATOM   340  N  N     . VAL A 1 43  ? 102.89  -3.021  42.477 1    49.48  ? 43  VAL A N     1 
ATOM   341  C  CA    . VAL A 1 43  ? 102.048 -4.174  42.15  1    49.34  ? 43  VAL A CA    1 
ATOM   342  C  C     . VAL A 1 43  ? 102.101 -4.505  40.661 1    48.71  ? 43  VAL A C     1 
ATOM   343  O  O     . VAL A 1 43  ? 102.257 -3.598  39.85  1    49.23  ? 43  VAL A O     1 
ATOM   344  C  CB    . VAL A 1 43  ? 100.59  -3.91   42.586 1    50.31  ? 43  VAL A CB    1 
ATOM   345  C  CG1   . VAL A 1 43  ? 99.753  -5.163  42.397 1    51.12  ? 43  VAL A CG1   1 
ATOM   346  C  CG2   . VAL A 1 43  ? 100.513 -3.424  44.035 1    50.83  ? 43  VAL A CG2   1 
ATOM   347  N  N     . ALA A 1 44  ? 101.934 -5.783  40.287 1    47.46  ? 44  ALA A N     1 
ATOM   348  C  CA    . ALA A 1 44  ? 101.962 -6.195  38.882 1    46.61  ? 44  ALA A CA    1 
ATOM   349  C  C     . ALA A 1 44  ? 100.631 -6.012  38.14  1    45.24  ? 44  ALA A C     1 
ATOM   350  O  O     . ALA A 1 44  ? 99.593  -6.492  38.601 1    44.97  ? 44  ALA A O     1 
ATOM   351  C  CB    . ALA A 1 44  ? 102.415 -7.64   38.781 1    46.87  ? 44  ALA A CB    1 
ATOM   352  N  N     . GLU A 1 45  ? 100.672 -5.339  36.973 1    44.43  ? 45  GLU A N     1 
ATOM   353  C  CA    . GLU A 1 45  ? 99.491  -5.123  36.126 1    44.04  ? 45  GLU A CA    1 
ATOM   354  C  C     . GLU A 1 45  ? 99.55   -5.984  34.891 1    43.41  ? 45  GLU A C     1 
ATOM   355  O  O     . GLU A 1 45  ? 100.358 -5.727  34.002 1    43.36  ? 45  GLU A O     1 
ATOM   356  C  CB    . GLU A 1 45  ? 99.329  -3.654  35.705 1    46.12  ? 45  GLU A CB    1 
ATOM   357  C  CG    . GLU A 1 45  ? 98.496  -2.83   36.671 1    51.62  ? 45  GLU A CG    1 
ATOM   358  C  CD    . GLU A 1 45  ? 97.121  -3.384  37.006 1    59.12  ? 45  GLU A CD    1 
ATOM   359  O  OE1   . GLU A 1 45  ? 96.726  -3.309  38.197 1    61.08  ? 45  GLU A OE1   1 
ATOM   360  O  OE2   . GLU A 1 45  ? 96.442  -3.895  36.082 1    60.1   ? 45  GLU A OE2   1 
ATOM   361  N  N     . LEU A 1 46  ? 98.688  -7.007  34.829 1    42.95  ? 46  LEU A N     1 
ATOM   362  C  CA    . LEU A 1 46  ? 98.617  -7.929  33.695 1    42.8   ? 46  LEU A CA    1 
ATOM   363  C  C     . LEU A 1 46  ? 97.736  -7.372  32.579 1    42.85  ? 46  LEU A C     1 
ATOM   364  O  O     . LEU A 1 46  ? 96.634  -6.867  32.844 1    43.1   ? 46  LEU A O     1 
ATOM   365  C  CB    . LEU A 1 46  ? 98.063  -9.291  34.137 1    42.6   ? 46  LEU A CB    1 
ATOM   366  C  CG    . LEU A 1 46  ? 98.861  -10.057 35.17  1    43.44  ? 46  LEU A CG    1 
ATOM   367  C  CD1   . LEU A 1 46  ? 98.158  -11.338 35.535 1    43.83  ? 46  LEU A CD1   1 
ATOM   368  C  CD2   . LEU A 1 46  ? 100.264 -10.344 34.68  1    43.97  ? 46  LEU A CD2   1 
ATOM   369  N  N     . VAL A 1 47  ? 98.225  -7.483  31.327 1    42.33  ? 47  VAL A N     1 
ATOM   370  C  CA    . VAL A 1 47  ? 97.528  -7.03   30.103 1    42.03  ? 47  VAL A CA    1 
ATOM   371  C  C     . VAL A 1 47  ? 96.28   -7.875  29.852 1    41.6   ? 47  VAL A C     1 
ATOM   372  O  O     . VAL A 1 47  ? 95.267  -7.378  29.362 1    41.94  ? 47  VAL A O     1 
ATOM   373  C  CB    . VAL A 1 47  ? 98.405  -7.027  28.828 1    42.53  ? 47  VAL A CB    1 
ATOM   374  C  CG1   . VAL A 1 47  ? 97.929  -5.946  27.877 1    43.27  ? 47  VAL A CG1   1 
ATOM   375  C  CG2   . VAL A 1 47  ? 99.898  -6.869  29.128 1    42.98  ? 47  VAL A CG2   1 
ATOM   376  N  N     . MET A 1 48  ? 96.402  -9.174  30.126 1    40.63  ? 48  MET A N     1 
ATOM   377  C  CA    . MET A 1 48  ? 95.375  -10.2   30.041 1    40.04  ? 48  MET A CA    1 
ATOM   378  C  C     . MET A 1 48  ? 95.53   -11.069 31.286 1    39.97  ? 48  MET A C     1 
ATOM   379  O  O     . MET A 1 48  ? 96.649  -11.194 31.818 1    39.73  ? 48  MET A O     1 
ATOM   380  C  CB    . MET A 1 48  ? 95.588  -11.061 28.785 1    39.81  ? 48  MET A CB    1 
ATOM   381  C  CG    . MET A 1 48  ? 95.137  -10.386 27.519 1    40.09  ? 48  MET A CG    1 
ATOM   382  S  SD    . MET A 1 48  ? 93.351  -10.214 27.472 1    38.86  ? 48  MET A SD    1 
ATOM   383  C  CE    . MET A 1 48  ? 92.894  -11.898 27.232 1    35.33  ? 48  MET A CE    1 
ATOM   384  N  N     . PRO A 1 49  ? 94.447  -11.713 31.77  1    39.81  ? 49  PRO A N     1 
ATOM   385  C  CA    . PRO A 1 49  ? 94.609  -12.563 32.939 1    39.84  ? 49  PRO A CA    1 
ATOM   386  C  C     . PRO A 1 49  ? 95.589  -13.707 32.708 1    40.65  ? 49  PRO A C     1 
ATOM   387  O  O     . PRO A 1 49  ? 95.768  -14.158 31.575 1    41.41  ? 49  PRO A O     1 
ATOM   388  C  CB    . PRO A 1 49  ? 93.186  -13.074 33.212 1    40.36  ? 49  PRO A CB    1 
ATOM   389  C  CG    . PRO A 1 49  ? 92.477  -12.963 31.945 1    40.93  ? 49  PRO A CG    1 
ATOM   390  C  CD    . PRO A 1 49  ? 93.043  -11.715 31.306 1    39.38  ? 49  PRO A CD    1 
ATOM   391  N  N     . ARG A 1 50  ? 96.265  -14.143 33.771 1    40.83  ? 50  ARG A N     1 
ATOM   392  C  CA    . ARG A 1 50  ? 97.144  -15.294 33.672 1    41.42  ? 50  ARG A CA    1 
ATOM   393  C  C     . ARG A 1 50  ? 96.233  -16.529 33.587 1    41.59  ? 50  ARG A C     1 
ATOM   394  O  O     . ARG A 1 50  ? 95.113  -16.518 34.096 1    42.1   ? 50  ARG A O     1 
ATOM   395  C  CB    . ARG A 1 50  ? 98.131  -15.368 34.856 1    43.22  ? 50  ARG A CB    1 
ATOM   396  C  CG    . ARG A 1 50  ? 97.51   -15.686 36.208 1    45.67  ? 50  ARG A CG    1 
ATOM   397  C  CD    . ARG A 1 50  ? 98.543  -15.95  37.292 1    48.39  ? 50  ARG A CD    1 
ATOM   398  N  NE    . ARG A 1 50  ? 97.931  -16.104 38.619 1    50.77  ? 50  ARG A NE    1 
ATOM   399  C  CZ    . ARG A 1 50  ? 97.889  -15.147 39.547 1    52.55  ? 50  ARG A CZ    1 
ATOM   400  N  NH1   . ARG A 1 50  ? 98.426  -13.958 39.309 1    52.41  ? 50  ARG A NH1   1 
ATOM   401  N  NH2   . ARG A 1 50  ? 97.312  -15.376 40.72  1    52.06  ? 50  ARG A NH2   1 
ATOM   402  N  N     . VAL A 1 51  ? 96.684  -17.561 32.907 1    41.17  ? 51  VAL A N     1 
ATOM   403  C  CA    . VAL A 1 51  ? 95.903  -18.766 32.699 1    41.8   ? 51  VAL A CA    1 
ATOM   404  C  C     . VAL A 1 51  ? 96.25   -19.852 33.705 1    42.93  ? 51  VAL A C     1 
ATOM   405  O  O     . VAL A 1 51  ? 97.423  -20.174 33.884 1    43.05  ? 51  VAL A O     1 
ATOM   406  C  CB    . VAL A 1 51  ? 96.125  -19.273 31.261 1    42.57  ? 51  VAL A CB    1 
ATOM   407  C  CG1   . VAL A 1 51  ? 95.295  -20.522 30.985 1    43.07  ? 51  VAL A CG1   1 
ATOM   408  C  CG2   . VAL A 1 51  ? 95.835  -18.175 30.235 1    43.07  ? 51  VAL A CG2   1 
ATOM   409  N  N     . VAL A 1 52  ? 95.234  -20.422 34.363 1    43.53  ? 52  VAL A N     1 
ATOM   410  C  CA    . VAL A 1 52  ? 95.446  -21.549 35.252 1    44.67  ? 52  VAL A CA    1 
ATOM   411  C  C     . VAL A 1 52  ? 95.231  -22.779 34.383 1    45.78  ? 52  VAL A C     1 
ATOM   412  O  O     . VAL A 1 52  ? 94.12   -23.006 33.905 1    46.02  ? 52  VAL A O     1 
ATOM   413  C  CB    . VAL A 1 52  ? 94.473  -21.568 36.452 1    45.74  ? 52  VAL A CB    1 
ATOM   414  C  CG1   . VAL A 1 52  ? 94.848  -22.675 37.427 1    46.48  ? 52  VAL A CG1   1 
ATOM   415  C  CG2   . VAL A 1 52  ? 94.427  -20.223 37.154 1    46.06  ? 52  VAL A CG2   1 
ATOM   416  N  N     . LYS A 1 53  ? 96.29   -23.539 34.118 1    46.27  ? 53  LYS A N     1 
ATOM   417  C  CA    . LYS A 1 53  ? 96.195  -24.734 33.281 1    47.05  ? 53  LYS A CA    1 
ATOM   418  C  C     . LYS A 1 53  ? 95.489  -25.895 34.01  1    48.12  ? 53  LYS A C     1 
ATOM   419  O  O     . LYS A 1 53  ? 95.29   -25.828 35.227 1    47.84  ? 53  LYS A O     1 
ATOM   420  C  CB    . LYS A 1 53  ? 97.597  -25.153 32.821 1    48.49  ? 53  LYS A CB    1 
ATOM   421  C  CG    . LYS A 1 53  ? 98.33   -24.066 32.065 1    52.19  ? 53  LYS A CG    1 
ATOM   422  C  CD    . LYS A 1 53  ? 98.731  -24.543 30.688 1    55.41  ? 53  LYS A CD    1 
ATOM   423  C  CE    . LYS A 1 53  ? 97.715  -24.172 29.654 1    58.04  ? 53  LYS A CE    1 
ATOM   424  N  NZ    . LYS A 1 53  ? 98.174  -24.559 28.301 1    59.72  ? 53  LYS A NZ    1 
ATOM   425  N  N     . SER A 1 54  ? 95.115  -26.961 33.273 1    49.02  ? 54  SER A N     1 
ATOM   426  C  CA    . SER A 1 54  ? 94.449  -28.15  33.815 1    50.51  ? 54  SER A CA    1 
ATOM   427  C  C     . SER A 1 54  ? 95.199  -28.739 35.004 1    51.78  ? 54  SER A C     1 
ATOM   428  O  O     . SER A 1 54  ? 94.576  -29.242 35.937 1    51.95  ? 54  SER A O     1 
ATOM   429  C  CB    . SER A 1 54  ? 94.305  -29.215 32.734 1    52.42  ? 54  SER A CB    1 
ATOM   430  O  OG    . SER A 1 54  ? 93.482  -28.778 31.659 1    55.61  ? 54  SER A OG    1 
ATOM   431  N  N     . ASN A 1 55  ? 96.535  -28.665 34.979 1    52.48  ? 55  ASN A N     1 
ATOM   432  C  CA    . ASN A 1 55  ? 97.378  -29.176 36.053 1    53.68  ? 55  ASN A CA    1 
ATOM   433  C  C     . ASN A 1 55  ? 97.736  -28.115 37.102 1    54.76  ? 55  ASN A C     1 
ATOM   434  O  O     . ASN A 1 55  ? 98.766  -28.227 37.763 1    55.19  ? 55  ASN A O     1 
ATOM   435  C  CB    . ASN A 1 55  ? 98.638  -29.829 35.488 1    55.21  ? 55  ASN A CB    1 
ATOM   436  C  CG    . ASN A 1 55  ? 99.529  -28.908 34.692 1    58.77  ? 55  ASN A CG    1 
ATOM   437  O  OD1   . ASN A 1 55  ? 99.144  -27.802 34.305 1    60.9   ? 55  ASN A OD1   1 
ATOM   438  N  ND2   . ASN A 1 55  ? 100.747 -29.353 34.417 1    58.85  ? 55  ASN A ND2   1 
ATOM   439  N  N     . ASP A 1 56  ? 96.891  -27.083 37.24  1    54.8   ? 56  ASP A N     1 
ATOM   440  C  CA    . ASP A 1 56  ? 97.001  -25.97  38.185 1    54.55  ? 56  ASP A CA    1 
ATOM   441  C  C     . ASP A 1 56  ? 98.278  -25.131 38.029 1    52.96  ? 56  ASP A C     1 
ATOM   442  O  O     . ASP A 1 56  ? 98.558  -24.295 38.877 1    52.91  ? 56  ASP A O     1 
ATOM   443  C  CB    . ASP A 1 56  ? 96.814  -26.467 39.614 1    57.91  ? 56  ASP A CB    1 
ATOM   444  C  CG    . ASP A 1 56  ? 95.476  -27.16  39.761 1    65.24  ? 56  ASP A CG    1 
ATOM   445  O  OD1   . ASP A 1 56  ? 94.44   -26.491 39.554 1    67.64  ? 56  ASP A OD1   1 
ATOM   446  O  OD2   . ASP A 1 56  ? 95.466  -28.385 40.03  1    67.03  ? 56  ASP A OD2   1 
ATOM   447  N  N     . VAL A 1 57  ? 99.003  -25.293 36.916 1    51.69  ? 57  VAL A N     1 
ATOM   448  C  CA    . VAL A 1 57  ? 100.188 -24.491 36.644 1    50.74  ? 57  VAL A CA    1 
ATOM   449  C  C     . VAL A 1 57  ? 99.713  -23.139 36.12  1    50.16  ? 57  VAL A C     1 
ATOM   450  O  O     . VAL A 1 57  ? 98.893  -23.098 35.201 1    50.52  ? 57  VAL A O     1 
ATOM   451  C  CB    . VAL A 1 57  ? 101.11  -25.19  35.614 1    50.73  ? 57  VAL A CB    1 
ATOM   452  C  CG1   . VAL A 1 57  ? 102.175 -24.237 35.081 1    51.15  ? 57  VAL A CG1   1 
ATOM   453  C  CG2   . VAL A 1 57  ? 101.754 -26.426 36.21  1    50.88  ? 57  VAL A CG2   1 
ATOM   454  N  N     . ARG A 1 58  ? 100.213 -22.041 36.695 1    49.07  ? 58  ARG A N     1 
ATOM   455  C  CA    . ARG A 1 58  ? 99.844  -20.717 36.206 1    48.63  ? 58  ARG A CA    1 
ATOM   456  C  C     . ARG A 1 58  ? 100.829 -20.322 35.086 1    48.22  ? 58  ARG A C     1 
ATOM   457  O  O     . ARG A 1 58  ? 102.032 -20.546 35.213 1    48.5   ? 58  ARG A O     1 
ATOM   458  C  CB    . ARG A 1 58  ? 99.82   -19.675 37.344 1    49.22  ? 58  ARG A CB    1 
ATOM   459  C  CG    . ARG A 1 58  ? 98.484  -19.567 38.08  1    50.6   ? 58  ARG A CG    1 
ATOM   460  C  CD    . ARG A 1 58  ? 98.193  -20.777 38.955 1    52.58  ? 58  ARG A CD    1 
ATOM   461  N  NE    . ARG A 1 58  ? 97.053  -20.552 39.847 1    53.73  ? 58  ARG A NE    1 
ATOM   462  C  CZ    . ARG A 1 58  ? 96.42   -21.51  40.52  1    53.95  ? 58  ARG A CZ    1 
ATOM   463  N  NH1   . ARG A 1 58  ? 96.796  -22.777 40.399 1    53.38  ? 58  ARG A NH1   1 
ATOM   464  N  NH2   . ARG A 1 58  ? 95.393  -21.21  41.301 1    52.61  ? 58  ARG A NH2   1 
ATOM   465  N  N     . GLU A 1 59  ? 100.318 -19.797 33.973 1    47.18  ? 59  GLU A N     1 
ATOM   466  C  CA    . GLU A 1 59  ? 101.167 -19.356 32.868 1    46.96  ? 59  GLU A CA    1 
ATOM   467  C  C     . GLU A 1 59  ? 100.564 -18.11  32.216 1    47     ? 59  GLU A C     1 
ATOM   468  O  O     . GLU A 1 59  ? 99.372  -17.872 32.389 1    47.56  ? 59  GLU A O     1 
ATOM   469  C  CB    . GLU A 1 59  ? 101.404 -20.486 31.85  1    48.46  ? 59  GLU A CB    1 
ATOM   470  C  CG    . GLU A 1 59  ? 100.173 -20.896 31.076 1    51.25  ? 59  GLU A CG    1 
ATOM   471  C  CD    . GLU A 1 59  ? 100.468 -21.706 29.833 1    55.68  ? 59  GLU A CD    1 
ATOM   472  O  OE1   . GLU A 1 59  ? 99.757  -21.503 28.822 1    56.86  ? 59  GLU A OE1   1 
ATOM   473  O  OE2   . GLU A 1 59  ? 101.411 -22.527 29.859 1    56.58  ? 59  GLU A OE2   1 
ATOM   474  N  N     . PRO A 1 60  ? 101.345 -17.262 31.516 1    46.19  ? 60  PRO A N     1 
ATOM   475  C  CA    . PRO A 1 60  ? 100.754 -16.047 30.935 1    45.98  ? 60  PRO A CA    1 
ATOM   476  C  C     . PRO A 1 60  ? 99.803  -16.337 29.791 1    46.19  ? 60  PRO A C     1 
ATOM   477  O  O     . PRO A 1 60  ? 99.878  -17.402 29.17  1    46.69  ? 60  PRO A O     1 
ATOM   478  C  CB    . PRO A 1 60  ? 101.969 -15.257 30.46  1    46.54  ? 60  PRO A CB    1 
ATOM   479  C  CG    . PRO A 1 60  ? 102.98  -16.278 30.2   1    47.06  ? 60  PRO A CG    1 
ATOM   480  C  CD    . PRO A 1 60  ? 102.784 -17.347 31.223 1    45.55  ? 60  PRO A CD    1 
ATOM   481  N  N     . PHE A 1 61  ? 98.916  -15.38  29.486 1    45.66  ? 61  PHE A N     1 
ATOM   482  C  CA    . PHE A 1 61  ? 97.979  -15.549 28.388 1    45.53  ? 61  PHE A CA    1 
ATOM   483  C  C     . PHE A 1 61  ? 98.751  -15.513 27.101 1    46.16  ? 61  PHE A C     1 
ATOM   484  O  O     . PHE A 1 61  ? 99.481  -14.556 26.85  1    46.98  ? 61  PHE A O     1 
ATOM   485  C  CB    . PHE A 1 61  ? 96.926  -14.446 28.394 1    45.13  ? 61  PHE A CB    1 
ATOM   486  C  CG    . PHE A 1 61  ? 95.945  -14.542 27.252 1    45.47  ? 61  PHE A CG    1 
ATOM   487  C  CD1   . PHE A 1 61  ? 94.883  -15.424 27.304 1    46.1   ? 61  PHE A CD1   1 
ATOM   488  C  CD2   . PHE A 1 61  ? 96.087  -13.751 26.125 1    46.13  ? 61  PHE A CD2   1 
ATOM   489  C  CE1   . PHE A 1 61  ? 93.976  -15.501 26.263 1    46.6   ? 61  PHE A CE1   1 
ATOM   490  C  CE2   . PHE A 1 61  ? 95.191  -13.85  25.074 1    46.63  ? 61  PHE A CE2   1 
ATOM   491  C  CZ    . PHE A 1 61  ? 94.142  -14.722 25.153 1    46.4   ? 61  PHE A CZ    1 
ATOM   492  N  N     . ASN A 1 62  ? 98.601  -16.563 26.295 1    45.41  ? 62  ASN A N     1 
ATOM   493  C  CA    . ASN A 1 62  ? 99.304  -16.705 25.041 1    44.51  ? 62  ASN A CA    1 
ATOM   494  C  C     . ASN A 1 62  ? 98.317  -16.663 23.895 1    43.71  ? 62  ASN A C     1 
ATOM   495  O  O     . ASN A 1 62  ? 97.624  -17.64  23.658 1    44.07  ? 62  ASN A O     1 
ATOM   496  C  CB    . ASN A 1 62  ? 100.006 -18.034 25.052 1    45.42  ? 62  ASN A CB    1 
ATOM   497  C  CG    . ASN A 1 62  ? 101.127 -18.101 24.079 1    48.51  ? 62  ASN A CG    1 
ATOM   498  O  OD1   . ASN A 1 62  ? 100.956 -17.892 22.871 1    48.9   ? 62  ASN A OD1   1 
ATOM   499  N  ND2   . ASN A 1 62  ? 102.305 -18.392 24.602 1    49.53  ? 62  ASN A ND2   1 
ATOM   500  N  N     . GLU A 1 63  ? 98.274  -15.555 23.16  1    42.43  ? 63  GLU A N     1 
ATOM   501  C  CA    . GLU A 1 63  ? 97.347  -15.376 22.043 1    41.62  ? 63  GLU A CA    1 
ATOM   502  C  C     . GLU A 1 63  ? 97.546  -16.421 20.936 1    41.62  ? 63  GLU A C     1 
ATOM   503  O  O     . GLU A 1 63  ? 96.572  -16.86  20.322 1    42.06  ? 63  GLU A O     1 
ATOM   504  C  CB    . GLU A 1 63  ? 97.51   -13.966 21.476 1    42.9   ? 63  GLU A CB    1 
ATOM   505  C  CG    . GLU A 1 63  ? 96.341  -13.504 20.638 1    48.25  ? 63  GLU A CG    1 
ATOM   506  C  CD    . GLU A 1 63  ? 96.551  -12.134 20.021 1    55.39  ? 63  GLU A CD    1 
ATOM   507  O  OE1   . GLU A 1 63  ? 96.179  -11.134 20.677 1    57.35  ? 63  GLU A OE1   1 
ATOM   508  O  OE2   . GLU A 1 63  ? 97.088  -12.058 18.89  1    55.67  ? 63  GLU A OE2   1 
ATOM   509  N  N     . GLU A 1 64  ? 98.817  -16.811 20.689 1    40.73  ? 64  GLU A N     1 
ATOM   510  C  CA    . GLU A 1 64  ? 99.196  -17.812 19.702 1    39.98  ? 64  GLU A CA    1 
ATOM   511  C  C     . GLU A 1 64  ? 98.639  -19.176 20.07  1    38.49  ? 64  GLU A C     1 
ATOM   512  O  O     . GLU A 1 64  ? 98.116  -19.857 19.201 1    38.43  ? 64  GLU A O     1 
ATOM   513  C  CB    . GLU A 1 64  ? 100.719 -17.881 19.558 1    43.45  ? 64  GLU A CB    1 
ATOM   514  C  CG    . GLU A 1 64  ? 101.339 -16.621 18.98  1    51.6   ? 64  GLU A CG    1 
ATOM   515  C  CD    . GLU A 1 64  ? 102.829 -16.471 19.245 1    61.84  ? 64  GLU A CD    1 
ATOM   516  O  OE1   . GLU A 1 64  ? 103.21  -16.386 20.438 1    64.77  ? 64  GLU A OE1   1 
ATOM   517  O  OE2   . GLU A 1 64  ? 103.613 -16.425 18.265 1    63.4   ? 64  GLU A OE2   1 
ATOM   518  N  N     . LYS A 1 65  ? 98.698  -19.57  21.355 1    37.55  ? 65  LYS A N     1 
ATOM   519  C  CA    . LYS A 1 65  ? 98.151  -20.856 21.811 1    37.15  ? 65  LYS A CA    1 
ATOM   520  C  C     . LYS A 1 65  ? 96.651  -20.92  21.502 1    37.34  ? 65  LYS A C     1 
ATOM   521  O  O     . LYS A 1 65  ? 96.16   -21.915 20.982 1    37.27  ? 65  LYS A O     1 
ATOM   522  C  CB    . LYS A 1 65  ? 98.37   -21.043 23.318 1    37.66  ? 65  LYS A CB    1 
ATOM   523  C  CG    . LYS A 1 65  ? 99.761  -21.466 23.715 1    39.8   ? 65  LYS A CG    1 
ATOM   524  C  CD    . LYS A 1 65  ? 99.788  -21.986 25.144 1    41.22  ? 65  LYS A CD    1 
ATOM   525  C  CE    . LYS A 1 65  ? 101.208 -22.287 25.568 1    43.67  ? 65  LYS A CE    1 
ATOM   526  N  NZ    . LYS A 1 65  ? 101.282 -23.264 26.685 1    45.68  ? 65  LYS A NZ    1 
ATOM   527  N  N     . LEU A 1 66  ? 95.951  -19.824 21.772 1    37.55  ? 66  LEU A N     1 
ATOM   528  C  CA    . LEU A 1 66  ? 94.529  -19.67  21.516 1    38.26  ? 66  LEU A CA    1 
ATOM   529  C  C     . LEU A 1 66  ? 94.228  -19.766 20.007 1    39.92  ? 66  LEU A C     1 
ATOM   530  O  O     . LEU A 1 66  ? 93.334  -20.514 19.605 1    40.55  ? 66  LEU A O     1 
ATOM   531  C  CB    . LEU A 1 66  ? 94.074  -18.299 22.071 1    37.69  ? 66  LEU A CB    1 
ATOM   532  C  CG    . LEU A 1 66  ? 92.661  -17.88  21.738 1    37.97  ? 66  LEU A CG    1 
ATOM   533  C  CD1   . LEU A 1 66  ? 91.68   -18.813 22.374 1    38.59  ? 66  LEU A CD1   1 
ATOM   534  C  CD2   . LEU A 1 66  ? 92.4    -16.49  22.197 1    38.12  ? 66  LEU A CD2   1 
ATOM   535  N  N     . ARG A 1 67  ? 94.981  -19.013 19.181 1    40.15  ? 67  ARG A N     1 
ATOM   536  C  CA    . ARG A 1 67  ? 94.817  -18.95  17.737 1    40.37  ? 67  ARG A CA    1 
ATOM   537  C  C     . ARG A 1 67  ? 95.056  -20.287 17.052 1    40.53  ? 67  ARG A C     1 
ATOM   538  O  O     . ARG A 1 67  ? 94.23   -20.702 16.241 1    41     ? 67  ARG A O     1 
ATOM   539  C  CB    . ARG A 1 67  ? 95.734  -17.865 17.164 1    41.9   ? 67  ARG A CB    1 
ATOM   540  C  CG    . ARG A 1 67  ? 95.719  -17.749 15.636 1    45.72  ? 67  ARG A CG    1 
ATOM   541  C  CD    . ARG A 1 67  ? 95.996  -16.335 15.159 1    49.31  ? 67  ARG A CD    1 
ATOM   542  N  NE    . ARG A 1 67  ? 97.12   -15.729 15.87  1    53.37  ? 67  ARG A NE    1 
ATOM   543  C  CZ    . ARG A 1 67  ? 97.066  -14.563 16.503 1    57.12  ? 67  ARG A CZ    1 
ATOM   544  N  NH1   . ARG A 1 67  ? 95.956  -13.833 16.476 1    56.99  ? 67  ARG A NH1   1 
ATOM   545  N  NH2   . ARG A 1 67  ? 98.129  -14.106 17.155 1    58.02  ? 67  ARG A NH2   1 
ATOM   546  N  N     . SER A 1 68  ? 96.176  -20.957 17.376 1    40.12  ? 68  SER A N     1 
ATOM   547  C  CA    . SER A 1 68  ? 96.568  -22.233 16.784 1    40.28  ? 68  SER A CA    1 
ATOM   548  C  C     . SER A 1 68  ? 95.519  -23.304 16.953 1    40.27  ? 68  SER A C     1 
ATOM   549  O  O     . SER A 1 68  ? 95.293  -24.08  16.027 1    40.86  ? 68  SER A O     1 
ATOM   550  C  CB    . SER A 1 68  ? 97.886  -22.731 17.377 1    41.67  ? 68  SER A CB    1 
ATOM   551  O  OG    . SER A 1 68  ? 98.872  -21.716 17.423 1    44.2   ? 68  SER A OG    1 
ATOM   552  N  N     . GLY A 1 69  ? 94.902  -23.359 18.123 1    39.55  ? 69  GLY A N     1 
ATOM   553  C  CA    . GLY A 1 69  ? 93.877  -24.349 18.403 1    39.77  ? 69  GLY A CA    1 
ATOM   554  C  C     . GLY A 1 69  ? 92.666  -24.166 17.522 1    40.16  ? 69  GLY A C     1 
ATOM   555  O  O     . GLY A 1 69  ? 92.098  -25.145 17.032 1    40.72  ? 69  GLY A O     1 
ATOM   556  N  N     . MET A 1 70  ? 92.307  -22.904 17.266 1    39.92  ? 70  MET A N     1 
ATOM   557  C  CA    . MET A 1 70  ? 91.192  -22.561 16.395 1    40.19  ? 70  MET A CA    1 
ATOM   558  C  C     . MET A 1 70  ? 91.559  -22.866 14.966 1    40.5   ? 70  MET A C     1 
ATOM   559  O  O     . MET A 1 70  ? 90.787  -23.525 14.282 1    41.12  ? 70  MET A O     1 
ATOM   560  C  CB    . MET A 1 70  ? 90.813  -21.081 16.535 1    40.86  ? 70  MET A CB    1 
ATOM   561  C  CG    . MET A 1 70  ? 90.423  -20.693 17.945 1    43.36  ? 70  MET A CG    1 
ATOM   562  S  SD    . MET A 1 70  ? 89.909  -18.968 18.118 1    45.9   ? 70  MET A SD    1 
ATOM   563  C  CE    . MET A 1 70  ? 88.431  -18.992 17.097 1    43.83  ? 70  MET A CE    1 
ATOM   564  N  N     . LEU A 1 71  ? 92.746  -22.435 14.516 1    40.12  ? 71  LEU A N     1 
ATOM   565  C  CA    . LEU A 1 71  ? 93.185  -22.669 13.142 1    40.01  ? 71  LEU A CA    1 
ATOM   566  C  C     . LEU A 1 71  ? 93.265  -24.143 12.768 1    40.24  ? 71  LEU A C     1 
ATOM   567  O  O     . LEU A 1 71  ? 93.02   -24.482 11.624 1    41.11  ? 71  LEU A O     1 
ATOM   568  C  CB    . LEU A 1 71  ? 94.521  -21.968 12.863 1    40.09  ? 71  LEU A CB    1 
ATOM   569  C  CG    . LEU A 1 71  ? 94.485  -20.458 12.749 1    41.16  ? 71  LEU A CG    1 
ATOM   570  C  CD1   . LEU A 1 71  ? 95.874  -19.901 12.48  1    41.11  ? 71  LEU A CD1   1 
ATOM   571  C  CD2   . LEU A 1 71  ? 93.574  -20.034 11.63  1    42.04  ? 71  LEU A CD2   1 
ATOM   572  N  N     . ARG A 1 72  ? 93.608  -25.012 13.723 1    40.02  ? 72  ARG A N     1 
ATOM   573  C  CA    . ARG A 1 72  ? 93.682  -26.451 13.539 1    40.26  ? 72  ARG A CA    1 
ATOM   574  C  C     . ARG A 1 72  ? 92.294  -26.99  13.27  1    41.01  ? 72  ARG A C     1 
ATOM   575  O  O     . ARG A 1 72  ? 92.112  -27.753 12.337 1    41.52  ? 72  ARG A O     1 
ATOM   576  C  CB    . ARG A 1 72  ? 94.279  -27.108 14.788 1    40.51  ? 72  ARG A CB    1 
ATOM   577  C  CG    . ARG A 1 72  ? 95.703  -27.509 14.581 1    42.01  ? 72  ARG A CG    1 
ATOM   578  C  CD    . ARG A 1 72  ? 96.559  -27.168 15.752 1    41.68  ? 72  ARG A CD    1 
ATOM   579  N  NE    . ARG A 1 72  ? 96.804  -28.344 16.568 1    43.03  ? 72  ARG A NE    1 
ATOM   580  C  CZ    . ARG A 1 72  ? 97.996  -28.906 16.732 1    45.07  ? 72  ARG A CZ    1 
ATOM   581  N  NH1   . ARG A 1 72  ? 99.07   -28.388 16.146 1    45.59  ? 72  ARG A NH1   1 
ATOM   582  N  NH2   . ARG A 1 72  ? 98.123  -30.001 17.472 1    44.88  ? 72  ARG A NH2   1 
ATOM   583  N  N     . ALA A 1 73  ? 91.316  -26.584 14.069 1    41.7   ? 73  ALA A N     1 
ATOM   584  C  CA    . ALA A 1 73  ? 89.937  -27.015 13.925 1    42.97  ? 73  ALA A CA    1 
ATOM   585  C  C     . ALA A 1 73  ? 89.295  -26.437 12.667 1    44.83  ? 73  ALA A C     1 
ATOM   586  O  O     . ALA A 1 73  ? 88.425  -27.08  12.09  1    45.57  ? 73  ALA A O     1 
ATOM   587  C  CB    . ALA A 1 73  ? 89.146  -26.61  15.151 1    43     ? 73  ALA A CB    1 
ATOM   588  N  N     . LEU A 1 74  ? 89.74   -25.245 12.216 1    45.5   ? 74  LEU A N     1 
ATOM   589  C  CA    . LEU A 1 74  ? 89.229  -24.558 11.017 1    46.33  ? 74  LEU A CA    1 
ATOM   590  C  C     . LEU A 1 74  ? 90.059  -24.861 9.752  1    48.05  ? 74  LEU A C     1 
ATOM   591  O  O     . LEU A 1 74  ? 90.214  -23.992 8.886  1    48.93  ? 74  LEU A O     1 
ATOM   592  C  CB    . LEU A 1 74  ? 89.205  -23.041 11.246 1    46.06  ? 74  LEU A CB    1 
ATOM   593  C  CG    . LEU A 1 74  ? 88.275  -22.52  12.32  1    46.92  ? 74  LEU A CG    1 
ATOM   594  C  CD1   . LEU A 1 74  ? 88.732  -21.176 12.794 1    47.33  ? 74  LEU A CD1   1 
ATOM   595  C  CD2   . LEU A 1 74  ? 86.864  -22.42  11.801 1    47.07  ? 74  LEU A CD2   1 
ATOM   596  N  N     . GLU A 1 75  ? 90.595  -26.083 9.64   1    48.52  ? 75  GLU A N     1 
ATOM   597  C  CA    . GLU A 1 75  ? 91.373  -26.471 8.467  1    49.12  ? 75  GLU A CA    1 
ATOM   598  C  C     . GLU A 1 75  ? 90.413  -26.804 7.344  1    49.7   ? 75  GLU A C     1 
ATOM   599  O  O     . GLU A 1 75  ? 89.454  -27.536 7.575  1    49.84  ? 75  GLU A O     1 
ATOM   600  C  CB    . GLU A 1 75  ? 92.273  -27.673 8.782  1    51.33  ? 75  GLU A CB    1 
ATOM   601  C  CG    . GLU A 1 75  ? 93.63   -27.266 9.331  1    56.58  ? 75  GLU A CG    1 
ATOM   602  C  CD    . GLU A 1 75  ? 94.564  -26.64  8.309  1    63.21  ? 75  GLU A CD    1 
ATOM   603  O  OE1   . GLU A 1 75  ? 95.341  -25.731 8.676  1    65.46  ? 75  GLU A OE1   1 
ATOM   604  O  OE2   . GLU A 1 75  ? 94.526  -27.065 7.137  1    65.15  ? 75  GLU A OE2   1 
ATOM   605  N  N     . LYS A 1 76  ? 90.644  -26.223 6.141  1    49.86  ? 76  LYS A N     1 
ATOM   606  C  CA    . LYS A 1 76  ? 89.84   -26.411 4.924  1    50.34  ? 76  LYS A CA    1 
ATOM   607  C  C     . LYS A 1 76  ? 88.379  -25.94  5.056  1    50.9   ? 76  LYS A C     1 
ATOM   608  O  O     . LYS A 1 76  ? 87.533  -26.308 4.236  1    51.54  ? 76  LYS A O     1 
ATOM   609  C  CB    . LYS A 1 76  ? 89.913  -27.864 4.412  1    51.51  ? 76  LYS A CB    1 
ATOM   610  C  CG    . LYS A 1 76  ? 91.309  -28.256 3.927  1    54.45  ? 76  LYS A CG    1 
ATOM   611  C  CD    . LYS A 1 76  ? 91.363  -29.696 3.377  1    58.1   ? 76  LYS A CD    1 
ATOM   612  C  CE    . LYS A 1 76  ? 92.657  -30.044 2.634  1    60.14  ? 76  LYS A CE    1 
ATOM   613  N  NZ    . LYS A 1 76  ? 93.585  -30.969 3.38   1    60.76  ? 76  LYS A NZ    1 
ATOM   614  N  N     . ARG A 1 77  ? 88.099  -25.11  6.064  1    50.61  ? 77  ARG A N     1 
ATOM   615  C  CA    . ARG A 1 77  ? 86.767  -24.589 6.331  1    50.65  ? 77  ARG A CA    1 
ATOM   616  C  C     . ARG A 1 77  ? 86.603  -23.199 5.748  1    51.62  ? 77  ARG A C     1 
ATOM   617  O  O     . ARG A 1 77  ? 87.565  -22.427 5.705  1    52.03  ? 77  ARG A O     1 
ATOM   618  C  CB    . ARG A 1 77  ? 86.507  -24.564 7.845  1    50.29  ? 77  ARG A CB    1 
ATOM   619  C  CG    . ARG A 1 77  ? 86.681  -25.915 8.525  1    50.75  ? 77  ARG A CG    1 
ATOM   620  C  CD    . ARG A 1 77  ? 85.845  -27.044 7.943  1    51.79  ? 77  ARG A CD    1 
ATOM   621  N  NE    . ARG A 1 77  ? 84.464  -26.651 7.663  1    53.09  ? 77  ARG A NE    1 
ATOM   622  C  CZ    . ARG A 1 77  ? 83.742  -27.118 6.648  1    55.02  ? 77  ARG A CZ    1 
ATOM   623  N  NH1   . ARG A 1 77  ? 82.501  -26.695 6.46   1    54.26  ? 77  ARG A NH1   1 
ATOM   624  N  NH2   . ARG A 1 77  ? 84.258  -28.015 5.813  1    55.46  ? 77  ARG A NH2   1 
ATOM   625  N  N     . PRO A 1 78  ? 85.376  -22.836 5.33   1    51.8   ? 78  PRO A N     1 
ATOM   626  C  CA    . PRO A 1 78  ? 85.179  -21.504 4.735  1    52.08  ? 78  PRO A CA    1 
ATOM   627  C  C     . PRO A 1 78  ? 84.996  -20.378 5.759  1    52.57  ? 78  PRO A C     1 
ATOM   628  O  O     . PRO A 1 78  ? 83.926  -19.784 5.865  1    53.11  ? 78  PRO A O     1 
ATOM   629  C  CB    . PRO A 1 78  ? 83.964  -21.698 3.829  1    52.36  ? 78  PRO A CB    1 
ATOM   630  C  CG    . PRO A 1 78  ? 83.198  -22.802 4.457  1    52.64  ? 78  PRO A CG    1 
ATOM   631  C  CD    . PRO A 1 78  ? 84.139  -23.642 5.292  1    51.14  ? 78  PRO A CD    1 
ATOM   632  N  N     . VAL A 1 79  ? 86.057  -20.104 6.513  1    52.24  ? 79  VAL A N     1 
ATOM   633  C  CA    . VAL A 1 79  ? 86.127  -19.078 7.54   1    52.6   ? 79  VAL A CA    1 
ATOM   634  C  C     . VAL A 1 79  ? 87.37   -18.269 7.174  1    53.06  ? 79  VAL A C     1 
ATOM   635  O  O     . VAL A 1 79  ? 88.458  -18.838 7.061  1    53.62  ? 79  VAL A O     1 
ATOM   636  C  CB    . VAL A 1 79  ? 86.265  -19.758 8.926  1    53.23  ? 79  VAL A CB    1 
ATOM   637  C  CG1   . VAL A 1 79  ? 86.58   -18.743 10.022 1    54.02  ? 79  VAL A CG1   1 
ATOM   638  C  CG2   . VAL A 1 79  ? 85.018  -20.571 9.264  1    53.49  ? 79  VAL A CG2   1 
ATOM   639  N  N     . SER A 1 80  ? 87.207  -16.976 6.888  1    52.67  ? 80  SER A N     1 
ATOM   640  C  CA    . SER A 1 80  ? 88.341  -16.141 6.488  1    52.6   ? 80  SER A CA    1 
ATOM   641  C  C     . SER A 1 80  ? 89.273  -15.835 7.673  1    52.02  ? 80  SER A C     1 
ATOM   642  O  O     . SER A 1 80  ? 88.898  -16.035 8.824  1    51.85  ? 80  SER A O     1 
ATOM   643  C  CB    . SER A 1 80  ? 87.861  -14.859 5.802  1    53.81  ? 80  SER A CB    1 
ATOM   644  O  OG    . SER A 1 80  ? 87.34   -13.904 6.714  1    56.31  ? 80  SER A OG    1 
ATOM   645  N  N     . SER A 1 81  ? 90.497  -15.372 7.386  1    51.62  ? 81  SER A N     1 
ATOM   646  C  CA    . SER A 1 81  ? 91.457  -14.981 8.424  1    51.65  ? 81  SER A CA    1 
ATOM   647  C  C     . SER A 1 81  ? 90.905  -13.837 9.31   1    50.16  ? 81  SER A C     1 
ATOM   648  O  O     . SER A 1 81  ? 91.281  -13.722 10.469 1    50.31  ? 81  SER A O     1 
ATOM   649  C  CB    . SER A 1 81  ? 92.785  -14.573 7.78   1    54.08  ? 81  SER A CB    1 
ATOM   650  O  OG    . SER A 1 81  ? 93.596  -13.805 8.656  1    57.95  ? 81  SER A OG    1 
ATOM   651  N  N     . ASP A 1 82  ? 90.026  -13.002 8.743  1    48.9   ? 82  ASP A N     1 
ATOM   652  C  CA    . ASP A 1 82  ? 89.371  -11.904 9.425  1    48.21  ? 82  ASP A CA    1 
ATOM   653  C  C     . ASP A 1 82  ? 88.378  -12.461 10.441 1    47.5   ? 82  ASP A C     1 
ATOM   654  O  O     . ASP A 1 82  ? 88.363  -11.988 11.559 1    47.71  ? 82  ASP A O     1 
ATOM   655  C  CB    . ASP A 1 82  ? 88.678  -11.015 8.401  1    49.57  ? 82  ASP A CB    1 
ATOM   656  C  CG    . ASP A 1 82  ? 87.634  -10.102 8.99   1    53.22  ? 82  ASP A CG    1 
ATOM   657  O  OD1   . ASP A 1 82  ? 88.008  -9.212  9.763  1    52.38  ? 82  ASP A OD1   1 
ATOM   658  O  OD2   . ASP A 1 82  ? 86.436  -10.298 8.684  1    56.44  ? 82  ASP A OD2   1 
ATOM   659  N  N     . ASP A 1 83  ? 87.575  -13.463 10.065 1    46.76  ? 83  ASP A N     1 
ATOM   660  C  CA    . ASP A 1 83  ? 86.612  -14.118 10.948 1    46.6   ? 83  ASP A CA    1 
ATOM   661  C  C     . ASP A 1 83  ? 87.3    -14.688 12.176 1    46.43  ? 83  ASP A C     1 
ATOM   662  O  O     . ASP A 1 83  ? 86.741  -14.632 13.27  1    46.65  ? 83  ASP A O     1 
ATOM   663  C  CB    . ASP A 1 83  ? 85.915  -15.266 10.217 1    48.39  ? 83  ASP A CB    1 
ATOM   664  C  CG    . ASP A 1 83  ? 85.018  -14.817 9.096  1    53.51  ? 83  ASP A CG    1 
ATOM   665  O  OD1   . ASP A 1 83  ? 84.372  -13.755 9.247  1    53.95  ? 83  ASP A OD1   1 
ATOM   666  O  OD2   . ASP A 1 83  ? 84.949  -15.537 8.062  1    56.31  ? 83  ASP A OD2   1 
ATOM   667  N  N     . VAL A 1 84  ? 88.501  -15.254 11.993 1    45.9   ? 84  VAL A N     1 
ATOM   668  C  CA    . VAL A 1 84  ? 89.283  -15.825 13.082 1    45.88  ? 84  VAL A CA    1 
ATOM   669  C  C     . VAL A 1 84  ? 89.747  -14.712 14.005 1    45.77  ? 84  VAL A C     1 
ATOM   670  O  O     . VAL A 1 84  ? 89.539  -14.811 15.209 1    45.99  ? 84  VAL A O     1 
ATOM   671  C  CB    . VAL A 1 84  ? 90.476  -16.669 12.558 1    46.39  ? 84  VAL A CB    1 
ATOM   672  C  CG1   . VAL A 1 84  ? 91.425  -17.051 13.698 1    47.06  ? 84  VAL A CG1   1 
ATOM   673  C  CG2   . VAL A 1 84  ? 89.987  -17.909 11.806 1    46.4   ? 84  VAL A CG2   1 
ATOM   674  N  N     . GLU A 1 85  ? 90.321  -13.629 13.45  1    45.41  ? 85  GLU A N     1 
ATOM   675  C  CA    . GLU A 1 85  ? 90.808  -12.515 14.271 1    45.51  ? 85  GLU A CA    1 
ATOM   676  C  C     . GLU A 1 85  ? 89.715  -11.801 15.031 1    44.65  ? 85  GLU A C     1 
ATOM   677  O  O     . GLU A 1 85  ? 89.928  -11.427 16.176 1    45.18  ? 85  GLU A O     1 
ATOM   678  C  CB    . GLU A 1 85  ? 91.637  -11.53  13.446 1    48.6   ? 85  GLU A CB    1 
ATOM   679  C  CG    . GLU A 1 85  ? 92.855  -12.176 12.814 1    55.15  ? 85  GLU A CG    1 
ATOM   680  C  CD    . GLU A 1 85  ? 93.74   -12.984 13.75  1    62.53  ? 85  GLU A CD    1 
ATOM   681  O  OE1   . GLU A 1 85  ? 93.979  -12.532 14.897 1    61.23  ? 85  GLU A OE1   1 
ATOM   682  O  OE2   . GLU A 1 85  ? 94.198  -14.072 13.326 1    66.24  ? 85  GLU A OE2   1 
ATOM   683  N  N     . MET A 1 86  ? 88.53   -11.693 14.415 1    43.39  ? 86  MET A N     1 
ATOM   684  C  CA    . MET A 1 86  ? 87.275  -11.143 14.915 1    42.86  ? 86  MET A CA    1 
ATOM   685  C  C     . MET A 1 86  ? 86.786  -11.98  16.105 1    42.11  ? 86  MET A C     1 
ATOM   686  O  O     . MET A 1 86  ? 86.297  -11.422 17.082 1    42.76  ? 86  MET A O     1 
ATOM   687  C  CB    . MET A 1 86  ? 86.249  -11.21  13.777 1    44.15  ? 86  MET A CB    1 
ATOM   688  C  CG    . MET A 1 86  ? 84.933  -10.58  14.063 1    48.16  ? 86  MET A CG    1 
ATOM   689  S  SD    . MET A 1 86  ? 84.234  -9.865  12.54  1    59.17  ? 86  MET A SD    1 
ATOM   690  C  CE    . MET A 1 86  ? 83.897  -11.328 11.551 1    56.46  ? 86  MET A CE    1 
ATOM   691  N  N     . ALA A 1 87  ? 86.95   -13.311 16.043 1    40.79  ? 87  ALA A N     1 
ATOM   692  C  CA    . ALA A 1 87  ? 86.572  -14.229 17.116 1    40.06  ? 87  ALA A CA    1 
ATOM   693  C  C     . ALA A 1 87  ? 87.582  -14.167 18.241 1    39.41  ? 87  ALA A C     1 
ATOM   694  O  O     . ALA A 1 87  ? 87.189  -14.231 19.398 1    39.87  ? 87  ALA A O     1 
ATOM   695  C  CB    . ALA A 1 87  ? 86.47   -15.654 16.593 1    40.08  ? 87  ALA A CB    1 
ATOM   696  N  N     . ILE A 1 88  ? 88.88   -14.051 17.922 1    38.38  ? 88  ILE A N     1 
ATOM   697  C  CA    . ILE A 1 88  ? 89.923  -13.964 18.943 1    37.95  ? 88  ILE A CA    1 
ATOM   698  C  C     . ILE A 1 88  ? 89.763  -12.686 19.757 1    38.02  ? 88  ILE A C     1 
ATOM   699  O  O     . ILE A 1 88  ? 89.761  -12.763 20.98  1    38.63  ? 88  ILE A O     1 
ATOM   700  C  CB    . ILE A 1 88  ? 91.345  -14.119 18.349 1    37.91  ? 88  ILE A CB    1 
ATOM   701  C  CG1   . ILE A 1 88  ? 91.551  -15.54  17.809 1    38.06  ? 88  ILE A CG1   1 
ATOM   702  C  CG2   . ILE A 1 88  ? 92.432  -13.741 19.369 1    38.44  ? 88  ILE A CG2   1 
ATOM   703  C  CD1   . ILE A 1 88  ? 92.717  -15.669 16.962 1    38.98  ? 88  ILE A CD1   1 
ATOM   704  N  N     . ASN A 1 89  ? 89.543  -11.529 19.102 1    37.31  ? 89  ASN A N     1 
ATOM   705  C  CA    . ASN A 1 89  ? 89.358  -10.259 19.829 1    36.85  ? 89  ASN A CA    1 
ATOM   706  C  C     . ASN A 1 89  ? 88.15   -10.278 20.76  1    35     ? 89  ASN A C     1 
ATOM   707  O  O     . ASN A 1 89  ? 88.168  -9.634  21.807 1    34.87  ? 89  ASN A O     1 
ATOM   708  C  CB    . ASN A 1 89  ? 89.251  -9.075  18.856 1    39.12  ? 89  ASN A CB    1 
ATOM   709  C  CG    . ASN A 1 89  ? 90.495  -8.857  18.032 1    43.74  ? 89  ASN A CG    1 
ATOM   710  O  OD1   . ASN A 1 89  ? 91.614  -9.109  18.47  1    45.2   ? 89  ASN A OD1   1 
ATOM   711  N  ND2   . ASN A 1 89  ? 90.327  -8.4    16.804 1    45.72  ? 89  ASN A ND2   1 
ATOM   712  N  N     . HIS A 1 90  ? 87.1    -11.005 20.37  1    33.76  ? 90  HIS A N     1 
ATOM   713  C  CA    . HIS A 1 90  ? 85.9    -11.108 21.181 1    33.17  ? 90  HIS A CA    1 
ATOM   714  C  C     . HIS A 1 90  ? 86.151  -11.988 22.393 1    32.56  ? 90  HIS A C     1 
ATOM   715  O  O     . HIS A 1 90  ? 85.665  -11.667 23.478 1    32.6   ? 90  HIS A O     1 
ATOM   716  C  CB    . HIS A 1 90  ? 84.716  -11.632 20.364 1    33.63  ? 90  HIS A CB    1 
ATOM   717  C  CG    . HIS A 1 90  ? 83.403  -11.5   21.058 1    34.63  ? 90  HIS A CG    1 
ATOM   718  N  ND1   . HIS A 1 90  ? 82.343  -12.322 20.736 1    36.43  ? 90  HIS A ND1   1 
ATOM   719  C  CD2   . HIS A 1 90  ? 83.011  -10.629 22.014 1    35.29  ? 90  HIS A CD2   1 
ATOM   720  C  CE1   . HIS A 1 90  ? 81.346  -11.928 21.505 1    37.01  ? 90  HIS A CE1   1 
ATOM   721  N  NE2   . HIS A 1 90  ? 81.708  -10.916 22.296 1    36.65  ? 90  HIS A NE2   1 
ATOM   722  N  N     . ILE A 1 91  ? 86.947  -13.078 22.228 1    31.58  ? 91  ILE A N     1 
ATOM   723  C  CA    . ILE A 1 91  ? 87.32   -13.965 23.345 1    31.04  ? 91  ILE A CA    1 
ATOM   724  C  C     . ILE A 1 91  ? 88.188  -13.201 24.34  1    30.63  ? 91  ILE A C     1 
ATOM   725  O  O     . ILE A 1 91  ? 87.952  -13.296 25.531 1    31.55  ? 91  ILE A O     1 
ATOM   726  C  CB    . ILE A 1 91  ? 88.007  -15.272 22.868 1    31.05  ? 91  ILE A CB    1 
ATOM   727  C  CG1   . ILE A 1 91  ? 87.025  -16.148 22.072 1    31.65  ? 91  ILE A CG1   1 
ATOM   728  C  CG2   . ILE A 1 91  ? 88.615  -16.048 24.041 1    31.26  ? 91  ILE A CG2   1 
ATOM   729  C  CD1   . ILE A 1 91  ? 87.662  -17.286 21.332 1    32.54  ? 91  ILE A CD1   1 
ATOM   730  N  N     . LYS A 1 92  ? 89.118  -12.377 23.856 1    29.63  ? 92  LYS A N     1 
ATOM   731  C  CA    . LYS A 1 92  ? 89.975  -11.555 24.701 1    29.44  ? 92  LYS A CA    1 
ATOM   732  C  C     . LYS A 1 92  ? 89.154  -10.563 25.499 1    29.55  ? 92  LYS A C     1 
ATOM   733  O  O     . LYS A 1 92  ? 89.382  -10.407 26.697 1    29.78  ? 92  LYS A O     1 
ATOM   734  C  CB    . LYS A 1 92  ? 91.022  -10.825 23.857 1    30.92  ? 92  LYS A CB    1 
ATOM   735  C  CG    . LYS A 1 92  ? 92.05   -11.761 23.261 1    34.62  ? 92  LYS A CG    1 
ATOM   736  C  CD    . LYS A 1 92  ? 92.964  -11.042 22.305 1    40.13  ? 92  LYS A CD    1 
ATOM   737  C  CE    . LYS A 1 92  ? 93.816  -10.011 23.002 1    45.18  ? 92  LYS A CE    1 
ATOM   738  N  NZ    . LYS A 1 92  ? 94.606  -9.214  22.031 1    48.69  ? 92  LYS A NZ    1 
ATOM   739  N  N     . SER A 1 93  ? 88.155  -9.944  24.851 1    29.28  ? 93  SER A N     1 
ATOM   740  C  CA    . SER A 1 93  ? 87.244  -8.99   25.473 1    29.56  ? 93  SER A CA    1 
ATOM   741  C  C     . SER A 1 93  ? 86.416  -9.646  26.57  1    28.99  ? 93  SER A C     1 
ATOM   742  O  O     . SER A 1 93  ? 86.212  -9.045  27.629 1    29.46  ? 93  SER A O     1 
ATOM   743  C  CB    . SER A 1 93  ? 86.322  -8.391  24.424 1    31.79  ? 93  SER A CB    1 
ATOM   744  O  OG    . SER A 1 93  ? 86.504  -6.988  24.342 1    35.02  ? 93  SER A OG    1 
ATOM   745  N  N     . GLN A 1 94  ? 85.97   -10.886 26.33  1    28.18  ? 94  GLN A N     1 
ATOM   746  C  CA    . GLN A 1 94  ? 85.19   -11.667 27.279 1    28.05  ? 94  GLN A CA    1 
ATOM   747  C  C     . GLN A 1 94  ? 86.01   -12.076 28.502 1    28.36  ? 94  GLN A C     1 
ATOM   748  O  O     . GLN A 1 94  ? 85.494  -12.007 29.612 1    28.31  ? 94  GLN A O     1 
ATOM   749  C  CB    . GLN A 1 94  ? 84.562  -12.873 26.587 1    28.84  ? 94  GLN A CB    1 
ATOM   750  C  CG    . GLN A 1 94  ? 83.386  -12.502 25.69  1    29.84  ? 94  GLN A CG    1 
ATOM   751  C  CD    . GLN A 1 94  ? 82.958  -13.671 24.845 1    31.37  ? 94  GLN A CD    1 
ATOM   752  O  OE1   . GLN A 1 94  ? 83.785  -14.36  24.237 1    30.9   ? 94  GLN A OE1   1 
ATOM   753  N  NE2   . GLN A 1 94  ? 81.656  -13.915 24.788 1    31.98  ? 94  GLN A NE2   1 
ATOM   754  N  N     . LEU A 1 95  ? 87.299  -12.435 28.32  1    28.43  ? 95  LEU A N     1 
ATOM   755  C  CA    . LEU A 1 95  ? 88.156  -12.769 29.474 1    28.84  ? 95  LEU A CA    1 
ATOM   756  C  C     . LEU A 1 95  ? 88.459  -11.514 30.322 1    28.99  ? 95  LEU A C     1 
ATOM   757  O  O     . LEU A 1 95  ? 88.582  -11.612 31.53  1    30.36  ? 95  LEU A O     1 
ATOM   758  C  CB    . LEU A 1 95  ? 89.477  -13.413 29.033 1    29.25  ? 95  LEU A CB    1 
ATOM   759  C  CG    . LEU A 1 95  ? 89.374  -14.599 28.091 1    30.71  ? 95  LEU A CG    1 
ATOM   760  C  CD1   . LEU A 1 95  ? 90.637  -14.756 27.274 1    31.27  ? 95  LEU A CD1   1 
ATOM   761  C  CD2   . LEU A 1 95  ? 89.144  -15.851 28.832 1    31.42  ? 95  LEU A CD2   1 
ATOM   762  N  N     . ARG A 1 96  ? 88.56   -10.347 29.703 1    28.2   ? 96  ARG A N     1 
ATOM   763  C  CA    . ARG A 1 96  ? 88.796  -9.092  30.407 1    27.93  ? 96  ARG A CA    1 
ATOM   764  C  C     . ARG A 1 96  ? 87.535  -8.652  31.177 1    27.86  ? 96  ARG A C     1 
ATOM   765  O  O     . ARG A 1 96  ? 87.639  -8.09   32.266 1    27.26  ? 96  ARG A O     1 
ATOM   766  C  CB    . ARG A 1 96  ? 89.236  -7.994  29.411 1    29.14  ? 96  ARG A CB    1 
ATOM   767  C  CG    . ARG A 1 96  ? 90.622  -8.245  28.803 1    31.77  ? 96  ARG A CG    1 
ATOM   768  C  CD    . ARG A 1 96  ? 91.254  -7.009  28.182 1    34.99  ? 96  ARG A CD    1 
ATOM   769  N  NE    . ARG A 1 96  ? 90.415  -6.447  27.123 1    38.53  ? 96  ARG A NE    1 
ATOM   770  C  CZ    . ARG A 1 96  ? 90.477  -6.81   25.844 1    41.39  ? 96  ARG A CZ    1 
ATOM   771  N  NH1   . ARG A 1 96  ? 91.365  -7.715  25.444 1    41     ? 96  ARG A NH1   1 
ATOM   772  N  NH2   . ARG A 1 96  ? 89.659  -6.264  24.952 1    41.55  ? 96  ARG A NH2   1 
ATOM   773  N  N     . ALA A 1 97  ? 86.35   -8.903  30.603 1    28.4   ? 97  ALA A N     1 
ATOM   774  C  CA    . ALA A 1 97  ? 85.056  -8.557  31.197 1    29.32  ? 97  ALA A CA    1 
ATOM   775  C  C     . ALA A 1 97  ? 84.771  -9.301  32.508 1    30.4   ? 97  ALA A C     1 
ATOM   776  O  O     . ALA A 1 97  ? 83.931  -8.85   33.296 1    30.9   ? 97  ALA A O     1 
ATOM   777  C  CB    . ALA A 1 97  ? 83.946  -8.809  30.202 1    29.36  ? 97  ALA A CB    1 
ATOM   778  N  N     . THR A 1 98  ? 85.463  -10.432 32.755 1    30.67  ? 98  THR A N     1 
ATOM   779  C  CA    . THR A 1 98  ? 85.355  -11.143 34.036 1    31.48  ? 98  THR A CA    1 
ATOM   780  C  C     . THR A 1 98  ? 85.956  -10.294 35.176 1    32.77  ? 98  THR A C     1 
ATOM   781  O  O     . THR A 1 98  ? 85.501  -10.38  36.306 1    33.62  ? 98  THR A O     1 
ATOM   782  C  CB    . THR A 1 98  ? 86.108  -12.477 33.996 1    32.06  ? 98  THR A CB    1 
ATOM   783  O  OG1   . THR A 1 98  ? 87.515  -12.257 33.88  1    32.5   ? 98  THR A OG1   1 
ATOM   784  C  CG2   . THR A 1 98  ? 85.676  -13.329 32.869 1    32.51  ? 98  THR A CG2   1 
ATOM   785  N  N     . GLY A 1 99  ? 86.994  -9.523  34.869 1    33.23  ? 99  GLY A N     1 
ATOM   786  C  CA    . GLY A 1 99  ? 87.708  -8.703  35.835 1    34.44  ? 99  GLY A CA    1 
ATOM   787  C  C     . GLY A 1 99  ? 88.736  -9.478  36.638 1    35.99  ? 99  GLY A C     1 
ATOM   788  O  O     . GLY A 1 99  ? 89.404  -8.914  37.498 1    36.27  ? 99  GLY A O     1 
ATOM   789  N  N     . GLU A 1 100 ? 88.883  -10.769 36.369 1    37.13  ? 100 GLU A N     1 
ATOM   790  C  CA    . GLU A 1 100 ? 89.779  -11.646 37.09  1    39.03  ? 100 GLU A CA    1 
ATOM   791  C  C     . GLU A 1 100 ? 91.241  -11.481 36.752 1    40.2   ? 100 GLU A C     1 
ATOM   792  O  O     . GLU A 1 100 ? 91.59   -11.239 35.599 1    40.63  ? 100 GLU A O     1 
ATOM   793  C  CB    . GLU A 1 100 ? 89.35   -13.107 36.861 1    42.54  ? 100 GLU A CB    1 
ATOM   794  C  CG    . GLU A 1 100 ? 88.031  -13.482 37.527 1    48.13  ? 100 GLU A CG    1 
ATOM   795  C  CD    . GLU A 1 100 ? 88.018  -13.159 39.003 1    53.4   ? 100 GLU A CD    1 
ATOM   796  O  OE1   . GLU A 1 100 ? 88.692  -13.882 39.767 1    54.96  ? 100 GLU A OE1   1 
ATOM   797  O  OE2   . GLU A 1 100 ? 87.399  -12.142 39.385 1    55.69  ? 100 GLU A OE2   1 
ATOM   798  N  N     . ARG A 1 101 ? 92.109  -11.637 37.761 1    40.54  ? 101 ARG A N     1 
ATOM   799  C  CA    . ARG A 1 101 ? 93.555  -11.605 37.521 1    41.27  ? 101 ARG A CA    1 
ATOM   800  C  C     . ARG A 1 101 ? 94.022  -12.926 36.873 1    40.31  ? 101 ARG A C     1 
ATOM   801  O  O     . ARG A 1 101 ? 95.025  -12.939 36.163 1    40.13  ? 101 ARG A O     1 
ATOM   802  C  CB    . ARG A 1 101 ? 94.335  -11.325 38.819 1    44.19  ? 101 ARG A CB    1 
ATOM   803  C  CG    . ARG A 1 101 ? 94.545  -9.836  39.108 1    49.28  ? 101 ARG A CG    1 
ATOM   804  C  CD    . ARG A 1 101 ? 95.994  -9.537  39.454 1    53.81  ? 101 ARG A CD    1 
ATOM   805  N  NE    . ARG A 1 101 ? 96.418  -10.208 40.683 1    57.81  ? 101 ARG A NE    1 
ATOM   806  C  CZ    . ARG A 1 101 ? 97.682  -10.482 40.992 1    61     ? 101 ARG A CZ    1 
ATOM   807  N  NH1   . ARG A 1 101 ? 97.975  -11.09  42.134 1    61.37  ? 101 ARG A NH1   1 
ATOM   808  N  NH2   . ARG A 1 101 ? 98.663  -10.153 40.159 1    61     ? 101 ARG A NH2   1 
ATOM   809  N  N     . GLU A 1 102 ? 93.293  -14.032 37.126 1    39.54  ? 102 GLU A N     1 
ATOM   810  C  CA    . GLU A 1 102 ? 93.567  -15.341 36.564 1    39.19  ? 102 GLU A CA    1 
ATOM   811  C  C     . GLU A 1 102 ? 92.282  -16.04  36.135 1    38.71  ? 102 GLU A C     1 
ATOM   812  O  O     . GLU A 1 102 ? 91.24   -15.851 36.746 1    38.58  ? 102 GLU A O     1 
ATOM   813  C  CB    . GLU A 1 102 ? 94.394  -16.198 37.528 1    40.56  ? 102 GLU A CB    1 
ATOM   814  C  CG    . GLU A 1 102 ? 93.64   -16.756 38.705 1    43.15  ? 102 GLU A CG    1 
ATOM   815  C  CD    . GLU A 1 102 ? 94.418  -17.754 39.532 1    48.05  ? 102 GLU A CD    1 
ATOM   816  O  OE1   . GLU A 1 102 ? 93.806  -18.34  40.454 1    47.73  ? 102 GLU A OE1   1 
ATOM   817  O  OE2   . GLU A 1 102 ? 95.625  -17.959 39.263 1    50.04  ? 102 GLU A OE2   1 
ATOM   818  N  N     . VAL A 1 103 ? 92.345  -16.811 35.056 1    38.46  ? 103 VAL A N     1 
ATOM   819  C  CA    . VAL A 1 103 ? 91.182  -17.503 34.502 1    38.83  ? 103 VAL A CA    1 
ATOM   820  C  C     . VAL A 1 103 ? 91.519  -18.955 34.199 1    39.27  ? 103 VAL A C     1 
ATOM   821  O  O     . VAL A 1 103 ? 92.584  -19.247 33.643 1    39.88  ? 103 VAL A O     1 
ATOM   822  C  CB    . VAL A 1 103 ? 90.654  -16.806 33.208 1    38.99  ? 103 VAL A CB    1 
ATOM   823  C  CG1   . VAL A 1 103 ? 90.01   -15.469 33.516 1    39.6   ? 103 VAL A CG1   1 
ATOM   824  C  CG2   . VAL A 1 103 ? 91.763  -16.62  32.196 1    39.05  ? 103 VAL A CG2   1 
ATOM   825  N  N     . PRO A 1 104 ? 90.602  -19.88  34.502 1    38.78  ? 104 PRO A N     1 
ATOM   826  C  CA    . PRO A 1 104 ? 90.854  -21.287 34.165 1    39.29  ? 104 PRO A CA    1 
ATOM   827  C  C     . PRO A 1 104 ? 90.978  -21.492 32.655 1    40.08  ? 104 PRO A C     1 
ATOM   828  O  O     . PRO A 1 104 ? 90.264  -20.827 31.906 1    40.52  ? 104 PRO A O     1 
ATOM   829  C  CB    . PRO A 1 104 ? 89.617  -22.007 34.719 1    39.62  ? 104 PRO A CB    1 
ATOM   830  C  CG    . PRO A 1 104 ? 88.583  -20.974 34.821 1    39.46  ? 104 PRO A CG    1 
ATOM   831  C  CD    . PRO A 1 104 ? 89.287  -19.702 35.138 1    37.69  ? 104 PRO A CD    1 
ATOM   832  N  N     . SER A 1 105 ? 91.873  -22.393 32.191 1    40.08  ? 105 SER A N     1 
ATOM   833  C  CA    . SER A 1 105 ? 91.992  -22.642 30.743 1    40.36  ? 105 SER A CA    1 
ATOM   834  C  C     . SER A 1 105 ? 90.7    -23.259 30.159 1    40.34  ? 105 SER A C     1 
ATOM   835  O  O     . SER A 1 105 ? 90.439  -23.117 28.972 1    40.83  ? 105 SER A O     1 
ATOM   836  C  CB    . SER A 1 105 ? 93.207  -23.507 30.426 1    42     ? 105 SER A CB    1 
ATOM   837  O  OG    . SER A 1 105 ? 92.993  -24.857 30.798 1    45.04  ? 105 SER A OG    1 
ATOM   838  N  N     . LYS A 1 106 ? 89.883  -23.906 31     1    40.02  ? 106 LYS A N     1 
ATOM   839  C  CA    . LYS A 1 106 ? 88.585  -24.467 30.645 1    40.1   ? 106 LYS A CA    1 
ATOM   840  C  C     . LYS A 1 106 ? 87.657  -23.348 30.173 1    38.82  ? 106 LYS A C     1 
ATOM   841  O  O     . LYS A 1 106 ? 86.905  -23.549 29.228 1    38.98  ? 106 LYS A O     1 
ATOM   842  C  CB    . LYS A 1 106 ? 87.973  -25.177 31.869 1    44.04  ? 106 LYS A CB    1 
ATOM   843  C  CG    . LYS A 1 106 ? 86.604  -25.803 31.617 1    51.22  ? 106 LYS A CG    1 
ATOM   844  C  CD    . LYS A 1 106 ? 85.905  -26.185 32.935 1    58.91  ? 106 LYS A CD    1 
ATOM   845  C  CE    . LYS A 1 106 ? 84.639  -26.987 32.698 1    65.15  ? 106 LYS A CE    1 
ATOM   846  N  NZ    . LYS A 1 106 ? 83.507  -26.147 32.217 1    68.75  ? 106 LYS A NZ    1 
ATOM   847  N  N     . MET A 1 107 ? 87.742  -22.162 30.79  1    37.81  ? 107 MET A N     1 
ATOM   848  C  CA    . MET A 1 107 ? 86.949  -21     30.423 1    37.52  ? 107 MET A CA    1 
ATOM   849  C  C     . MET A 1 107 ? 87.34   -20.527 29.025 1    37.02  ? 107 MET A C     1 
ATOM   850  O  O     . MET A 1 107 ? 86.459  -20.253 28.219 1    37.28  ? 107 MET A O     1 
ATOM   851  C  CB    . MET A 1 107 ? 87.146  -19.885 31.444 1    38.28  ? 107 MET A CB    1 
ATOM   852  C  CG    . MET A 1 107 ? 86.212  -18.745 31.265 1    40.52  ? 107 MET A CG    1 
ATOM   853  S  SD    . MET A 1 107 ? 86.653  -17.42  32.397 1    45.14  ? 107 MET A SD    1 
ATOM   854  C  CE    . MET A 1 107 ? 87.209  -16.268 31.284 1    46.82  ? 107 MET A CE    1 
ATOM   855  N  N     . ILE A 1 108 ? 88.656  -20.501 28.71  1    36.07  ? 108 ILE A N     1 
ATOM   856  C  CA    . ILE A 1 108 ? 89.165  -20.14  27.38  1    35.45  ? 108 ILE A CA    1 
ATOM   857  C  C     . ILE A 1 108 ? 88.635  -21.133 26.328 1    35.74  ? 108 ILE A C     1 
ATOM   858  O  O     . ILE A 1 108 ? 88.24   -20.742 25.226 1    35.66  ? 108 ILE A O     1 
ATOM   859  C  CB    . ILE A 1 108 ? 90.716  -20.095 27.338 1    35.39  ? 108 ILE A CB    1 
ATOM   860  C  CG1   . ILE A 1 108 ? 91.296  -19.07  28.322 1    35.64  ? 108 ILE A CG1   1 
ATOM   861  C  CG2   . ILE A 1 108 ? 91.192  -19.81  25.908 1    36.43  ? 108 ILE A CG2   1 
ATOM   862  C  CD1   . ILE A 1 108 ? 92.776  -19.077 28.435 1    36.28  ? 108 ILE A CD1   1 
ATOM   863  N  N     . GLY A 1 109 ? 88.637  -22.41  26.685 1    35.58  ? 109 GLY A N     1 
ATOM   864  C  CA    . GLY A 1 109 ? 88.142  -23.47  25.825 1    35.63  ? 109 GLY A CA    1 
ATOM   865  C  C     . GLY A 1 109 ? 86.665  -23.332 25.536 1    35.65  ? 109 GLY A C     1 
ATOM   866  O  O     . GLY A 1 109 ? 86.278  -23.422 24.375 1    35.66  ? 109 GLY A O     1 
ATOM   867  N  N     . ASN A 1 110 ? 85.827  -23.051 26.565 1    35.73  ? 110 ASN A N     1 
ATOM   868  C  CA    . ASN A 1 110 ? 84.382  -22.906 26.334 1    36.15  ? 110 ASN A CA    1 
ATOM   869  C  C     . ASN A 1 110 ? 84.071  -21.704 25.449 1    35.99  ? 110 ASN A C     1 
ATOM   870  O  O     . ASN A 1 110 ? 83.171  -21.775 24.613 1    35.92  ? 110 ASN A O     1 
ATOM   871  C  CB    . ASN A 1 110 ? 83.588  -22.818 27.63  1    37.37  ? 110 ASN A CB    1 
ATOM   872  C  CG    . ASN A 1 110 ? 83.787  -23.96  28.586 1    41.69  ? 110 ASN A CG    1 
ATOM   873  O  OD1   . ASN A 1 110 ? 83.833  -23.762 29.806 1    45.04  ? 110 ASN A OD1   1 
ATOM   874  N  ND2   . ASN A 1 110 ? 83.888  -25.172 28.087 1    41.45  ? 110 ASN A ND2   1 
ATOM   875  N  N     . LEU A 1 111 ? 84.848  -20.622 25.598 1    35.55  ? 111 LEU A N     1 
ATOM   876  C  CA    . LEU A 1 111 ? 84.681  -19.43  24.791 1    35.35  ? 111 LEU A CA    1 
ATOM   877  C  C     . LEU A 1 111 ? 84.968  -19.73  23.337 1    35.61  ? 111 LEU A C     1 
ATOM   878  O  O     . LEU A 1 111 ? 84.207  -19.286 22.472 1    35.96  ? 111 LEU A O     1 
ATOM   879  C  CB    . LEU A 1 111 ? 85.554  -18.277 25.313 1    35.06  ? 111 LEU A CB    1 
ATOM   880  C  CG    . LEU A 1 111 ? 85.177  -17.702 26.68  1    35.47  ? 111 LEU A CG    1 
ATOM   881  C  CD1   . LEU A 1 111 ? 86.081  -16.541 27.056 1    35.5   ? 111 LEU A CD1   1 
ATOM   882  C  CD2   . LEU A 1 111 ? 83.706  -17.293 26.736 1    36.05  ? 111 LEU A CD2   1 
ATOM   883  N  N     . VAL A 1 112 ? 86.03   -20.523 23.058 1    35.42  ? 112 VAL A N     1 
ATOM   884  C  CA    . VAL A 1 112 ? 86.381  -20.944 21.687 1    35.35  ? 112 VAL A CA    1 
ATOM   885  C  C     . VAL A 1 112 ? 85.285  -21.831 21.093 1    36.31  ? 112 VAL A C     1 
ATOM   886  O  O     . VAL A 1 112 ? 84.903  -21.654 19.946 1    36.93  ? 112 VAL A O     1 
ATOM   887  C  CB    . VAL A 1 112 ? 87.757  -21.633 21.58  1    34.98  ? 112 VAL A CB    1 
ATOM   888  C  CG1   . VAL A 1 112 ? 88.025  -22.034 20.149 1    35.4   ? 112 VAL A CG1   1 
ATOM   889  C  CG2   . VAL A 1 112 ? 88.863  -20.727 22.072 1    34.87  ? 112 VAL A CG2   1 
ATOM   890  N  N     . MET A 1 113 ? 84.74   -22.739 21.886 1    36.94  ? 113 MET A N     1 
ATOM   891  C  CA    . MET A 1 113 ? 83.645  -23.61  21.493 1    38.23  ? 113 MET A CA    1 
ATOM   892  C  C     . MET A 1 113 ? 82.429  -22.792 21.057 1    39.53  ? 113 MET A C     1 
ATOM   893  O  O     . MET A 1 113 ? 81.811  -23.131 20.061 1    39.76  ? 113 MET A O     1 
ATOM   894  C  CB    . MET A 1 113 ? 83.258  -24.537 22.659 1    39.67  ? 113 MET A CB    1 
ATOM   895  C  CG    . MET A 1 113 ? 84.332  -25.52  23.029 1    43.19  ? 113 MET A CG    1 
ATOM   896  S  SD    . MET A 1 113 ? 84.285  -26.93  21.944 1    54.88  ? 113 MET A SD    1 
ATOM   897  C  CE    . MET A 1 113 ? 83.149  -27.942 22.805 1    52.89  ? 113 MET A CE    1 
ATOM   898  N  N     . GLU A 1 114 ? 82.108  -21.697 21.762 1    40.65  ? 114 GLU A N     1 
ATOM   899  C  CA    . GLU A 1 114 ? 80.966  -20.865 21.38  1    42.06  ? 114 GLU A CA    1 
ATOM   900  C  C     . GLU A 1 114 ? 81.22   -20.054 20.11  1    42.14  ? 114 GLU A C     1 
ATOM   901  O  O     . GLU A 1 114 ? 80.285  -19.821 19.339 1    42.15  ? 114 GLU A O     1 
ATOM   902  C  CB    . GLU A 1 114 ? 80.481  -19.991 22.53  1    45.77  ? 114 GLU A CB    1 
ATOM   903  C  CG    . GLU A 1 114 ? 79.569  -20.757 23.475 1    55.55  ? 114 GLU A CG    1 
ATOM   904  C  CD    . GLU A 1 114 ? 78.357  -21.425 22.842 1    68.36  ? 114 GLU A CD    1 
ATOM   905  O  OE1   . GLU A 1 114 ? 77.321  -20.741 22.659 1    71.36  ? 114 GLU A OE1   1 
ATOM   906  O  OE2   . GLU A 1 114 ? 78.442  -22.638 22.537 1    72.27  ? 114 GLU A OE2   1 
ATOM   907  N  N     . GLN A 1 115 ? 82.486  -19.654 19.869 1    41.66  ? 115 GLN A N     1 
ATOM   908  C  CA    . GLN A 1 115 ? 82.813  -18.926 18.648 1    41.33  ? 115 GLN A CA    1 
ATOM   909  C  C     . GLN A 1 115 ? 82.713  -19.89  17.495 1    41.45  ? 115 GLN A C     1 
ATOM   910  O  O     . GLN A 1 115 ? 82.058  -19.58  16.506 1    41.63  ? 115 GLN A O     1 
ATOM   911  C  CB    . GLN A 1 115 ? 84.219  -18.288 18.693 1    42.46  ? 115 GLN A CB    1 
ATOM   912  C  CG    . GLN A 1 115 ? 84.393  -17.105 19.637 1    46.18  ? 115 GLN A CG    1 
ATOM   913  C  CD    . GLN A 1 115 ? 83.335  -16.036 19.557 1    51.04  ? 115 GLN A CD    1 
ATOM   914  O  OE1   . GLN A 1 115 ? 83.335  -15.167 18.676 1    52.86  ? 115 GLN A OE1   1 
ATOM   915  N  NE2   . GLN A 1 115 ? 82.466  -16.025 20.556 1    51.49  ? 115 GLN A NE2   1 
ATOM   916  N  N     . LEU A 1 116 ? 83.298  -21.088 17.629 1    41.29  ? 116 LEU A N     1 
ATOM   917  C  CA    . LEU A 1 116 ? 83.251  -22.078 16.556 1    41.62  ? 116 LEU A CA    1 
ATOM   918  C  C     . LEU A 1 116 ? 81.846  -22.554 16.269 1    42.16  ? 116 LEU A C     1 
ATOM   919  O  O     . LEU A 1 116 ? 81.525  -22.779 15.121 1    42.16  ? 116 LEU A O     1 
ATOM   920  C  CB    . LEU A 1 116 ? 84.196  -23.242 16.829 1    41.43  ? 116 LEU A CB    1 
ATOM   921  C  CG    . LEU A 1 116 ? 85.662  -22.856 16.898 1    42.03  ? 116 LEU A CG    1 
ATOM   922  C  CD1   . LEU A 1 116 ? 86.5    -24.027 17.327 1    42.37  ? 116 LEU A CD1   1 
ATOM   923  C  CD2   . LEU A 1 116 ? 86.144  -22.279 15.582 1    42.02  ? 116 LEU A CD2   1 
ATOM   924  N  N     . LYS A 1 117 ? 80.972  -22.603 17.277 1    42.64  ? 117 LYS A N     1 
ATOM   925  C  CA    . LYS A 1 117 ? 79.572  -22.982 17.077 1    43.45  ? 117 LYS A CA    1 
ATOM   926  C  C     . LYS A 1 117 ? 78.887  -22.005 16.094 1    43.56  ? 117 LYS A C     1 
ATOM   927  O  O     . LYS A 1 117 ? 78.092  -22.426 15.257 1    43.87  ? 117 LYS A O     1 
ATOM   928  C  CB    . LYS A 1 117 ? 78.843  -22.988 18.424 1    45.96  ? 117 LYS A CB    1 
ATOM   929  C  CG    . LYS A 1 117 ? 77.589  -23.842 18.45  1    51.38  ? 117 LYS A CG    1 
ATOM   930  C  CD    . LYS A 1 117 ? 77.178  -24.15  19.883 1    58.05  ? 117 LYS A CD    1 
ATOM   931  C  CE    . LYS A 1 117 ? 75.734  -24.617 19.99  1    63.41  ? 117 LYS A CE    1 
ATOM   932  N  NZ    . LYS A 1 117 ? 74.746  -23.509 19.81  1    66.19  ? 117 LYS A NZ    1 
ATOM   933  N  N     . LYS A 1 118 ? 79.258  -20.715 16.16  1    43.11  ? 118 LYS A N     1 
ATOM   934  C  CA    . LYS A 1 118 ? 78.754  -19.659 15.285 1    43.12  ? 118 LYS A CA    1 
ATOM   935  C  C     . LYS A 1 118 ? 79.465  -19.666 13.928 1    42.34  ? 118 LYS A C     1 
ATOM   936  O  O     . LYS A 1 118 ? 78.815  -19.455 12.914 1    42.56  ? 118 LYS A O     1 
ATOM   937  C  CB    . LYS A 1 118 ? 78.949  -18.277 15.943 1    45.51  ? 118 LYS A CB    1 
ATOM   938  C  CG    . LYS A 1 118 ? 78.08   -18.035 17.175 1    50.42  ? 118 LYS A CG    1 
ATOM   939  C  CD    . LYS A 1 118 ? 78.375  -16.711 17.86  1    55.73  ? 118 LYS A CD    1 
ATOM   940  C  CE    . LYS A 1 118 ? 77.546  -16.56  19.12  1    60.6   ? 118 LYS A CE    1 
ATOM   941  N  NZ    . LYS A 1 118 ? 77.741  -17.701 20.06  1    63.59  ? 118 LYS A NZ    1 
ATOM   942  N  N     . LEU A 1 119 ? 80.796  -19.874 13.917 1    41.58  ? 119 LEU A N     1 
ATOM   943  C  CA    . LEU A 1 119 ? 81.646  -19.877 12.722 1    41.66  ? 119 LEU A CA    1 
ATOM   944  C  C     . LEU A 1 119 ? 81.445  -21.079 11.772 1    42.19  ? 119 LEU A C     1 
ATOM   945  O  O     . LEU A 1 119 ? 81.145  -20.892 10.592 1    41.79  ? 119 LEU A O     1 
ATOM   946  C  CB    . LEU A 1 119 ? 83.127  -19.775 13.12  1    41.48  ? 119 LEU A CB    1 
ATOM   947  C  CG    . LEU A 1 119 ? 83.617  -18.404 13.488 1    42.62  ? 119 LEU A CG    1 
ATOM   948  C  CD1   . LEU A 1 119 ? 85.002  -18.476 14.144 1    43     ? 119 LEU A CD1   1 
ATOM   949  C  CD2   . LEU A 1 119 ? 83.615  -17.494 12.274 1    42.71  ? 119 LEU A CD2   1 
ATOM   950  N  N     . ASP A 1 120 ? 81.632  -22.304 12.283 1    42.6   ? 120 ASP A N     1 
ATOM   951  C  CA    . ASP A 1 120 ? 81.545  -23.52  11.491 1    43.36  ? 120 ASP A CA    1 
ATOM   952  C  C     . ASP A 1 120 ? 81.266  -24.716 12.416 1    44.37  ? 120 ASP A C     1 
ATOM   953  O  O     . ASP A 1 120 ? 82.012  -24.953 13.368 1    43.95  ? 120 ASP A O     1 
ATOM   954  C  CB    . ASP A 1 120 ? 82.882  -23.721 10.776 1    44.77  ? 120 ASP A CB    1 
ATOM   955  C  CG    . ASP A 1 120 ? 82.869  -24.765 9.698  1    49.25  ? 120 ASP A CG    1 
ATOM   956  O  OD1   . ASP A 1 120 ? 82.655  -25.939 10.015 1    49.28  ? 120 ASP A OD1   1 
ATOM   957  O  OD2   . ASP A 1 120 ? 83.107  -24.406 8.542  1    52.65  ? 120 ASP A OD2   1 
ATOM   958  N  N     . LYS A 1 121 ? 80.193  -25.465 12.155 1    45.46  ? 121 LYS A N     1 
ATOM   959  C  CA    . LYS A 1 121 ? 79.854  -26.62  12.992 1    46.59  ? 121 LYS A CA    1 
ATOM   960  C  C     . LYS A 1 121 ? 80.846  -27.817 12.8   1    46.62  ? 121 LYS A C     1 
ATOM   961  O  O     . LYS A 1 121 ? 81.034  -28.565 13.753 1    47.05  ? 121 LYS A O     1 
ATOM   962  C  CB    . LYS A 1 121 ? 78.381  -27.041 12.815 1    49.44  ? 121 LYS A CB    1 
ATOM   963  C  CG    . LYS A 1 121 ? 77.383  -25.887 12.661 1    53.74  ? 121 LYS A CG    1 
ATOM   964  C  CD    . LYS A 1 121 ? 76.864  -25.354 13.991 1    57.83  ? 121 LYS A CD    1 
ATOM   965  C  CE    . LYS A 1 121 ? 75.713  -24.379 13.797 1    61.36  ? 121 LYS A CE    1 
ATOM   966  N  NZ    . LYS A 1 121 ? 75.193  -23.815 15.083 1    62.82  ? 121 LYS A NZ    1 
ATOM   967  N  N     . VAL A 1 122 ? 81.518  -27.969 11.622 1    45.82  ? 122 VAL A N     1 
ATOM   968  C  CA    . VAL A 1 122 ? 82.525  -29.037 11.459 1    45.91  ? 122 VAL A CA    1 
ATOM   969  C  C     . VAL A 1 122 ? 83.752  -28.713 12.324 1    46.17  ? 122 VAL A C     1 
ATOM   970  O  O     . VAL A 1 122 ? 84.254  -29.587 13.039 1    46.39  ? 122 VAL A O     1 
ATOM   971  C  CB    . VAL A 1 122 ? 82.895  -29.332 9.974  1    46.45  ? 122 VAL A CB    1 
ATOM   972  C  CG1   . VAL A 1 122 ? 84.169  -30.172 9.859  1    47.05  ? 122 VAL A CG1   1 
ATOM   973  C  CG2   . VAL A 1 122 ? 81.742  -30.012 9.257  1    46.47  ? 122 VAL A CG2   1 
ATOM   974  N  N     . ALA A 1 123 ? 84.179  -27.436 12.315 1    46.06  ? 123 ALA A N     1 
ATOM   975  C  CA    . ALA A 1 123 ? 85.284  -26.927 13.135 1    46.38  ? 123 ALA A CA    1 
ATOM   976  C  C     . ALA A 1 123 ? 84.986  -27.114 14.625 1    47.08  ? 123 ALA A C     1 
ATOM   977  O  O     . ALA A 1 123 ? 85.895  -27.379 15.408 1    47.27  ? 123 ALA A O     1 
ATOM   978  C  CB    . ALA A 1 123 ? 85.51   -25.458 12.84  1    46.18  ? 123 ALA A CB    1 
ATOM   979  N  N     . TYR A 1 124 ? 83.713  -26.97  15.011 1    47.32  ? 124 TYR A N     1 
ATOM   980  C  CA    . TYR A 1 124 ? 83.258  -27.154 16.379 1    48.28  ? 124 TYR A CA    1 
ATOM   981  C  C     . TYR A 1 124 ? 83.5    -28.612 16.816 1    48.24  ? 124 TYR A C     1 
ATOM   982  O  O     . TYR A 1 124 ? 84.08   -28.833 17.877 1    48.15  ? 124 TYR A O     1 
ATOM   983  C  CB    . TYR A 1 124 ? 81.767  -26.763 16.496 1    49.07  ? 124 TYR A CB    1 
ATOM   984  C  CG    . TYR A 1 124 ? 81.168  -27.027 17.858 1    50.69  ? 124 TYR A CG    1 
ATOM   985  C  CD1   . TYR A 1 124 ? 80.581  -28.25  18.158 1    52     ? 124 TYR A CD1   1 
ATOM   986  C  CD2   . TYR A 1 124 ? 81.202  -26.063 18.851 1    51.64  ? 124 TYR A CD2   1 
ATOM   987  C  CE1   . TYR A 1 124 ? 80.081  -28.518 19.427 1    52.99  ? 124 TYR A CE1   1 
ATOM   988  C  CE2   . TYR A 1 124 ? 80.678  -26.309 20.114 1    52.56  ? 124 TYR A CE2   1 
ATOM   989  C  CZ    . TYR A 1 124 ? 80.118  -27.539 20.398 1    53.74  ? 124 TYR A CZ    1 
ATOM   990  O  OH    . TYR A 1 124 ? 79.599  -27.79  21.645 1    55.76  ? 124 TYR A OH    1 
ATOM   991  N  N     . ILE A 1 125 ? 83.079  -29.598 15.99  1    48.17  ? 125 ILE A N     1 
ATOM   992  C  CA    . ILE A 1 125 ? 83.252  -31.037 16.261 1    48.44  ? 125 ILE A CA    1 
ATOM   993  C  C     . ILE A 1 125 ? 84.735  -31.398 16.354 1    48.82  ? 125 ILE A C     1 
ATOM   994  O  O     . ILE A 1 125 ? 85.124  -32.187 17.218 1    48.93  ? 125 ILE A O     1 
ATOM   995  C  CB    . ILE A 1 125 ? 82.551  -31.91  15.184 1    48.63  ? 125 ILE A CB    1 
ATOM   996  C  CG1   . ILE A 1 125 ? 81.087  -31.519 14.983 1    49.7   ? 125 ILE A CG1   1 
ATOM   997  C  CG2   . ILE A 1 125 ? 82.671  -33.385 15.503 1    48.83  ? 125 ILE A CG2   1 
ATOM   998  C  CD1   . ILE A 1 125 ? 80.239  -31.641 16.19  1    51.17  ? 125 ILE A CD1   1 
ATOM   999  N  N     . ARG A 1 126 ? 85.563  -30.817 15.462 1    48.74  ? 126 ARG A N     1 
ATOM   1000 C  CA    . ARG A 1 126 ? 87.004  -31.065 15.465 1    48.96  ? 126 ARG A CA    1 
ATOM   1001 C  C     . ARG A 1 126 ? 87.635  -30.599 16.782 1    48.85  ? 126 ARG A C     1 
ATOM   1002 O  O     . ARG A 1 126 ? 88.352  -31.371 17.421 1    48.82  ? 126 ARG A O     1 
ATOM   1003 C  CB    . ARG A 1 126 ? 87.693  -30.396 14.265 1    50.02  ? 126 ARG A CB    1 
ATOM   1004 C  CG    . ARG A 1 126 ? 87.334  -31.01  12.928 1    52.51  ? 126 ARG A CG    1 
ATOM   1005 C  CD    . ARG A 1 126 ? 88.434  -30.784 11.911 1    54.79  ? 126 ARG A CD    1 
ATOM   1006 N  NE    . ARG A 1 126 ? 87.95   -30.946 10.54  1    57     ? 126 ARG A NE    1 
ATOM   1007 C  CZ    . ARG A 1 126 ? 87.865  -29.962 9.651  1    58.1   ? 126 ARG A CZ    1 
ATOM   1008 N  NH1   . ARG A 1 126 ? 88.274  -28.743 9.961  1    57.35  ? 126 ARG A NH1   1 
ATOM   1009 N  NH2   . ARG A 1 126 ? 87.412  -30.202 8.432  1    57.89  ? 126 ARG A NH2   1 
ATOM   1010 N  N     . PHE A 1 127 ? 87.335  -29.361 17.205 1    48.64  ? 127 PHE A N     1 
ATOM   1011 C  CA    . PHE A 1 127 ? 87.861  -28.808 18.448 1    48.86  ? 127 PHE A CA    1 
ATOM   1012 C  C     . PHE A 1 127 ? 87.338  -29.583 19.65  1    49.72  ? 127 PHE A C     1 
ATOM   1013 O  O     . PHE A 1 127 ? 88.128  -29.915 20.526 1    50.1   ? 127 PHE A O     1 
ATOM   1014 C  CB    . PHE A 1 127 ? 87.504  -27.324 18.564 1    48.43  ? 127 PHE A CB    1 
ATOM   1015 C  CG    . PHE A 1 127 ? 88.262  -26.53  19.603 1    48.76  ? 127 PHE A CG    1 
ATOM   1016 C  CD1   . PHE A 1 127 ? 87.88   -26.553 20.933 1    49.29  ? 127 PHE A CD1   1 
ATOM   1017 C  CD2   . PHE A 1 127 ? 89.28   -25.668 19.233 1    49.43  ? 127 PHE A CD2   1 
ATOM   1018 C  CE1   . PHE A 1 127 ? 88.54   -25.783 21.88  1    49.81  ? 127 PHE A CE1   1 
ATOM   1019 C  CE2   . PHE A 1 127 ? 89.95   -24.909 20.189 1    50.07  ? 127 PHE A CE2   1 
ATOM   1020 C  CZ    . PHE A 1 127 ? 89.576  -24.976 21.506 1    49.68  ? 127 PHE A CZ    1 
ATOM   1021 N  N     . ALA A 1 128 ? 86.029  -29.905 19.684 1    49.7   ? 128 ALA A N     1 
ATOM   1022 C  CA    . ALA A 1 128 ? 85.437  -30.659 20.798 1    49.88  ? 128 ALA A CA    1 
ATOM   1023 C  C     . ALA A 1 128 ? 86.059  -32.044 20.964 1    49.72  ? 128 ALA A C     1 
ATOM   1024 O  O     . ALA A 1 128 ? 86.199  -32.512 22.084 1    49.73  ? 128 ALA A O     1 
ATOM   1025 C  CB    . ALA A 1 128 ? 83.929  -30.78  20.625 1    50.13  ? 128 ALA A CB    1 
ATOM   1026 N  N     . SER A 1 129 ? 86.463  -32.686 19.859 1    49.49  ? 129 SER A N     1 
ATOM   1027 C  CA    . SER A 1 129 ? 87.084  -34.008 19.903 1    49.8   ? 129 SER A CA    1 
ATOM   1028 C  C     . SER A 1 129 ? 88.41   -34.027 20.672 1    50.04  ? 129 SER A C     1 
ATOM   1029 O  O     . SER A 1 129 ? 88.76   -35.046 21.276 1    50.01  ? 129 SER A O     1 
ATOM   1030 C  CB    . SER A 1 129 ? 87.282  -34.554 18.498 1    50.89  ? 129 SER A CB    1 
ATOM   1031 O  OG    . SER A 1 129 ? 88.266  -33.807 17.801 1    53.07  ? 129 SER A OG    1 
ATOM   1032 N  N     . VAL A 1 130 ? 89.138  -32.905 20.659 1    49.98  ? 130 VAL A N     1 
ATOM   1033 C  CA    . VAL A 1 130 ? 90.392  -32.804 21.391 1    50.5   ? 130 VAL A CA    1 
ATOM   1034 C  C     . VAL A 1 130 ? 90.167  -32.105 22.729 1    51.32  ? 130 VAL A C     1 
ATOM   1035 O  O     . VAL A 1 130 ? 90.706  -32.532 23.743 1    51.38  ? 130 VAL A O     1 
ATOM   1036 C  CB    . VAL A 1 130 ? 91.507  -32.131 20.558 1    50.97  ? 130 VAL A CB    1 
ATOM   1037 C  CG1   . VAL A 1 130 ? 92.814  -32.07  21.341 1    51.4   ? 130 VAL A CG1   1 
ATOM   1038 C  CG2   . VAL A 1 130 ? 91.714  -32.867 19.246 1    51.39  ? 130 VAL A CG2   1 
ATOM   1039 N  N     . TYR A 1 131 ? 89.322  -31.079 22.754 1    51.8   ? 131 TYR A N     1 
ATOM   1040 C  CA    . TYR A 1 131 ? 89.031  -30.33  23.968 1    52.69  ? 131 TYR A CA    1 
ATOM   1041 C  C     . TYR A 1 131 ? 88.283  -31.178 25.015 1    54.5   ? 131 TYR A C     1 
ATOM   1042 O  O     . TYR A 1 131 ? 88.781  -31.345 26.134 1    54.97  ? 131 TYR A O     1 
ATOM   1043 C  CB    . TYR A 1 131 ? 88.307  -29.022 23.623 1    52.2   ? 131 TYR A CB    1 
ATOM   1044 C  CG    . TYR A 1 131 ? 87.912  -28.223 24.828 1    52.35  ? 131 TYR A CG    1 
ATOM   1045 C  CD1   . TYR A 1 131 ? 88.874  -27.664 25.659 1    53.07  ? 131 TYR A CD1   1 
ATOM   1046 C  CD2   . TYR A 1 131 ? 86.578  -28.015 25.137 1    52.99  ? 131 TYR A CD2   1 
ATOM   1047 C  CE1   . TYR A 1 131 ? 88.515  -26.949 26.786 1    53.82  ? 131 TYR A CE1   1 
ATOM   1048 C  CE2   . TYR A 1 131 ? 86.205  -27.305 26.263 1    53.62  ? 131 TYR A CE2   1 
ATOM   1049 C  CZ    . TYR A 1 131 ? 87.176  -26.766 27.08  1    54.47  ? 131 TYR A CZ    1 
ATOM   1050 O  OH    . TYR A 1 131 ? 86.795  -26.062 28.189 1    55.82  ? 131 TYR A OH    1 
ATOM   1051 N  N     . ARG A 1 132 ? 87.115  -31.731 24.664 1    55.25  ? 132 ARG A N     1 
ATOM   1052 C  CA    . ARG A 1 132 ? 86.387  -32.616 25.58  1    56.38  ? 132 ARG A CA    1 
ATOM   1053 C  C     . ARG A 1 132 ? 87.06   -34.018 25.691 1    57.13  ? 132 ARG A C     1 
ATOM   1054 O  O     . ARG A 1 132 ? 86.67   -34.81  26.549 1    57.54  ? 132 ARG A O     1 
ATOM   1055 C  CB    . ARG A 1 132 ? 84.909  -32.749 25.163 1    58.16  ? 132 ARG A CB    1 
ATOM   1056 C  CG    . ARG A 1 132 ? 84.146  -31.429 25.103 1    62.22  ? 132 ARG A CG    1 
ATOM   1057 C  CD    . ARG A 1 132 ? 82.679  -31.647 24.767 1    66.66  ? 132 ARG A CD    1 
ATOM   1058 N  NE    . ARG A 1 132 ? 81.958  -30.396 24.509 1    71.05  ? 132 ARG A NE    1 
ATOM   1059 C  CZ    . ARG A 1 132 ? 81.333  -29.68  25.444 1    74.55  ? 132 ARG A CZ    1 
ATOM   1060 N  NH1   . ARG A 1 132 ? 81.347  -30.074 26.713 1    74.64  ? 132 ARG A NH1   1 
ATOM   1061 N  NH2   . ARG A 1 132 ? 80.694  -28.563 25.117 1    74.94  ? 132 ARG A NH2   1 
ATOM   1062 N  N     . SER A 1 133 ? 88.075  -34.296 24.841 1    57.24  ? 133 SER A N     1 
ATOM   1063 C  CA    . SER A 1 133 ? 88.842  -35.528 24.739 1    58.44  ? 133 SER A CA    1 
ATOM   1064 C  C     . SER A 1 133 ? 87.979  -36.75  24.51  1    59.98  ? 133 SER A C     1 
ATOM   1065 O  O     . SER A 1 133 ? 87.676  -37.467 25.463 1    60.07  ? 133 SER A O     1 
ATOM   1066 C  CB    . SER A 1 133 ? 89.757  -35.726 25.938 1    59.61  ? 133 SER A CB    1 
ATOM   1067 O  OG    . SER A 1 133 ? 90.593  -36.851 25.73  1    61.71  ? 133 SER A OG    1 
ATOM   1068 N  N     . PHE A 1 134 ? 87.573  -36.99  23.241 1    60.95  ? 134 PHE A N     1 
ATOM   1069 C  CA    . PHE A 1 134 ? 86.753  -38.153 22.911 1    62.27  ? 134 PHE A CA    1 
ATOM   1070 C  C     . PHE A 1 134 ? 87.668  -39.365 23.037 1    64.33  ? 134 PHE A C     1 
ATOM   1071 O  O     . PHE A 1 134 ? 88.723  -39.382 22.411 1    64.57  ? 134 PHE A O     1 
ATOM   1072 C  CB    . PHE A 1 134 ? 86.187  -38.066 21.471 1    61.7   ? 134 PHE A CB    1 
ATOM   1073 C  CG    . PHE A 1 134 ? 85.232  -36.938 21.155 1    61.69  ? 134 PHE A CG    1 
ATOM   1074 C  CD1   . PHE A 1 134 ? 84.847  -36.036 22.131 1    62.11  ? 134 PHE A CD1   1 
ATOM   1075 C  CD2   . PHE A 1 134 ? 84.715  -36.782 19.88  1    62.02  ? 134 PHE A CD2   1 
ATOM   1076 C  CE1   . PHE A 1 134 ? 83.987  -34.988 21.831 1    62.72  ? 134 PHE A CE1   1 
ATOM   1077 C  CE2   . PHE A 1 134 ? 83.868  -35.721 19.581 1    62.56  ? 134 PHE A CE2   1 
ATOM   1078 C  CZ    . PHE A 1 134 ? 83.52   -34.825 20.557 1    62.47  ? 134 PHE A CZ    1 
ATOM   1079 N  N     . GLU A 1 135 ? 87.326  -40.323 23.901 1    65.75  ? 135 GLU A N     1 
ATOM   1080 C  CA    . GLU A 1 135 ? 88.18   -41.504 24.087 1    67.87  ? 135 GLU A CA    1 
ATOM   1081 C  C     . GLU A 1 135 ? 87.721  -42.72  23.268 1    69.8   ? 135 GLU A C     1 
ATOM   1082 O  O     . GLU A 1 135 ? 88.403  -43.739 23.259 1    70.03  ? 135 GLU A O     1 
ATOM   1083 C  CB    . GLU A 1 135 ? 88.299  -41.872 25.578 1    70.4   ? 135 GLU A CB    1 
ATOM   1084 C  CG    . GLU A 1 135 ? 88.659  -40.703 26.488 1    75.79  ? 135 GLU A CG    1 
ATOM   1085 C  CD    . GLU A 1 135 ? 90.124  -40.309 26.532 1    81.34  ? 135 GLU A CD    1 
ATOM   1086 O  OE1   . GLU A 1 135 ? 90.951  -41.013 25.906 1    81.29  ? 135 GLU A OE1   1 
ATOM   1087 O  OE2   . GLU A 1 135 ? 90.446  -39.303 27.211 1    83.51  ? 135 GLU A OE2   1 
ATOM   1088 N  N     . ASP A 1 136 ? 86.58   -42.594 22.566 1    70.93  ? 136 ASP A N     1 
ATOM   1089 C  CA    . ASP A 1 136 ? 85.912  -43.62  21.785 1    72.5   ? 136 ASP A CA    1 
ATOM   1090 C  C     . ASP A 1 136 ? 85.331  -43     20.515 1    73.81  ? 136 ASP A C     1 
ATOM   1091 O  O     . ASP A 1 136 ? 85.09   -41.794 20.451 1    73.84  ? 136 ASP A O     1 
ATOM   1092 C  CB    . ASP A 1 136 ? 84.756  -44.166 22.631 1    75.01  ? 136 ASP A CB    1 
ATOM   1093 C  CG    . ASP A 1 136 ? 84.226  -45.528 22.253 1    81.38  ? 136 ASP A CG    1 
ATOM   1094 O  OD1   . ASP A 1 136 ? 84.638  -46.059 21.192 1    82.54  ? 136 ASP A OD1   1 
ATOM   1095 O  OD2   . ASP A 1 136 ? 83.397  -46.07  23.018 1    84.45  ? 136 ASP A OD2   1 
ATOM   1096 N  N     . ILE A 1 137 ? 85.098  -43.832 19.499 1    74.72  ? 137 ILE A N     1 
ATOM   1097 C  CA    . ILE A 1 137 ? 84.492  -43.382 18.247 1    75.91  ? 137 ILE A CA    1 
ATOM   1098 C  C     . ILE A 1 137 ? 83.013  -43.023 18.505 1    76.92  ? 137 ILE A C     1 
ATOM   1099 O  O     . ILE A 1 137 ? 82.52   -42.049 17.942 1    76.98  ? 137 ILE A O     1 
ATOM   1100 C  CB    . ILE A 1 137 ? 84.671  -44.391 17.067 1    76.53  ? 137 ILE A CB    1 
ATOM   1101 C  CG1   . ILE A 1 137 ? 86.044  -45.098 17.09  1    77.84  ? 137 ILE A CG1   1 
ATOM   1102 C  CG2   . ILE A 1 137 ? 84.468  -43.694 15.731 1    76.87  ? 137 ILE A CG2   1 
ATOM   1103 C  CD1   . ILE A 1 137 ? 86.141  -46.376 17.999 1    79.54  ? 137 ILE A CD1   1 
ATOM   1104 N  N     . LYS A 1 138 ? 82.328  -43.766 19.416 1    77.44  ? 138 LYS A N     1 
ATOM   1105 C  CA    . LYS A 1 138 ? 80.933  -43.513 19.803 1    78.12  ? 138 LYS A CA    1 
ATOM   1106 C  C     . LYS A 1 138 ? 80.75   -42.063 20.259 1    78.04  ? 138 LYS A C     1 
ATOM   1107 O  O     . LYS A 1 138 ? 79.799  -41.409 19.837 1    78.04  ? 138 LYS A O     1 
ATOM   1108 C  CB    . LYS A 1 138 ? 80.493  -44.467 20.929 1    80.48  ? 138 LYS A CB    1 
ATOM   1109 C  CG    . LYS A 1 138 ? 80.688  -45.95  20.615 1    85.41  ? 138 LYS A CG    1 
ATOM   1110 C  CD    . LYS A 1 138 ? 80.157  -46.818 21.762 1    90.79  ? 138 LYS A CD    1 
ATOM   1111 C  CE    . LYS A 1 138 ? 80.467  -48.29  21.603 1    95.12  ? 138 LYS A CE    1 
ATOM   1112 N  NZ    . LYS A 1 138 ? 80.132  -49.05  22.841 1    97.59  ? 138 LYS A NZ    1 
ATOM   1113 N  N     . ASP A 1 139 ? 81.72   -41.555 21.057 1    77.8   ? 139 ASP A N     1 
ATOM   1114 C  CA    . ASP A 1 139 ? 81.785  -40.184 21.575 1    78.15  ? 139 ASP A CA    1 
ATOM   1115 C  C     . ASP A 1 139 ? 81.588  -39.139 20.474 1    78.03  ? 139 ASP A C     1 
ATOM   1116 O  O     . ASP A 1 139 ? 81.091  -38.051 20.757 1    78.21  ? 139 ASP A O     1 
ATOM   1117 C  CB    . ASP A 1 139 ? 83.147  -39.92  22.254 1    80.24  ? 139 ASP A CB    1 
ATOM   1118 C  CG    . ASP A 1 139 ? 83.246  -40.217 23.743 1    85.45  ? 139 ASP A CG    1 
ATOM   1119 O  OD1   . ASP A 1 139 ? 82.872  -41.339 24.153 1    86.73  ? 139 ASP A OD1   1 
ATOM   1120 O  OD2   . ASP A 1 139 ? 83.732  -39.337 24.493 1    87.41  ? 139 ASP A OD2   1 
ATOM   1121 N  N     . PHE A 1 140 ? 82.004  -39.454 19.231 1    77.52  ? 140 PHE A N     1 
ATOM   1122 C  CA    . PHE A 1 140 ? 81.876  -38.553 18.083 1    77.46  ? 140 PHE A CA    1 
ATOM   1123 C  C     . PHE A 1 140 ? 80.408  -38.359 17.685 1    79.42  ? 140 PHE A C     1 
ATOM   1124 O  O     . PHE A 1 140 ? 79.952  -37.225 17.583 1    79.26  ? 140 PHE A O     1 
ATOM   1125 C  CB    . PHE A 1 140 ? 82.685  -39.077 16.879 1    75.69  ? 140 PHE A CB    1 
ATOM   1126 C  CG    . PHE A 1 140 ? 84.076  -38.525 16.717 1    74.06  ? 140 PHE A CG    1 
ATOM   1127 C  CD1   . PHE A 1 140 ? 84.284  -37.309 16.102 1    73.75  ? 140 PHE A CD1   1 
ATOM   1128 C  CD2   . PHE A 1 140 ? 85.18   -39.25  17.129 1    73.75  ? 140 PHE A CD2   1 
ATOM   1129 C  CE1   . PHE A 1 140 ? 85.565  -36.807 15.937 1    73.87  ? 140 PHE A CE1   1 
ATOM   1130 C  CE2   . PHE A 1 140 ? 86.46   -38.75  16.956 1    73.83  ? 140 PHE A CE2   1 
ATOM   1131 C  CZ    . PHE A 1 140 ? 86.645  -37.532 16.361 1    73.48  ? 140 PHE A CZ    1 
ATOM   1132 N  N     . GLY A 1 141 ? 79.683  -39.463 17.496 1    81.16  ? 141 GLY A N     1 
ATOM   1133 C  CA    . GLY A 1 141 ? 78.277  -39.433 17.107 1    83.4   ? 141 GLY A CA    1 
ATOM   1134 C  C     . GLY A 1 141 ? 77.375  -38.828 18.164 1    85.77  ? 141 GLY A C     1 
ATOM   1135 O  O     . GLY A 1 141 ? 76.391  -38.152 17.846 1    86.02  ? 141 GLY A O     1 
ATOM   1136 N  N     . GLU A 1 142 ? 77.728  -39.051 19.435 1    87.24  ? 142 GLU A N     1 
ATOM   1137 C  CA    . GLU A 1 142 ? 76.987  -38.517 20.566 1    89.13  ? 142 GLU A CA    1 
ATOM   1138 C  C     . GLU A 1 142 ? 77.125  -36.992 20.656 1    90.8   ? 142 GLU A C     1 
ATOM   1139 O  O     . GLU A 1 142 ? 76.185  -36.332 21.081 1    91.15  ? 142 GLU A O     1 
ATOM   1140 C  CB    . GLU A 1 142 ? 77.413  -39.21  21.866 1    91.76  ? 142 GLU A CB    1 
ATOM   1141 C  CG    . GLU A 1 142 ? 77.172  -40.712 21.832 1    96.92  ? 142 GLU A CG    1 
ATOM   1142 C  CD    . GLU A 1 142 ? 77.45   -41.451 23.126 1    103.69 ? 142 GLU A CD    1 
ATOM   1143 O  OE1   . GLU A 1 142 ? 77.673  -40.778 24.159 1    105.28 ? 142 GLU A OE1   1 
ATOM   1144 O  OE2   . GLU A 1 142 ? 77.442  -42.704 23.107 1    105.32 ? 142 GLU A OE2   1 
ATOM   1145 N  N     . GLU A 1 143 ? 78.265  -36.424 20.216 1    91.71  ? 143 GLU A N     1 
ATOM   1146 C  CA    . GLU A 1 143 ? 78.458  -34.966 20.208 1    93.17  ? 143 GLU A CA    1 
ATOM   1147 C  C     . GLU A 1 143 ? 77.741  -34.297 19.009 1    94.65  ? 143 GLU A C     1 
ATOM   1148 O  O     . GLU A 1 143 ? 77.41   -33.113 19.066 1    94.62  ? 143 GLU A O     1 
ATOM   1149 C  CB    . GLU A 1 143 ? 79.956  -34.607 20.239 1    95.15  ? 143 GLU A CB    1 
ATOM   1150 C  CG    . GLU A 1 143 ? 80.266  -33.126 20.425 1    98.97  ? 143 GLU A CG    1 
ATOM   1151 C  CD    . GLU A 1 143 ? 80.21   -32.593 21.844 1    103.6  ? 143 GLU A CD    1 
ATOM   1152 O  OE1   . GLU A 1 143 ? 80.095  -31.357 22.008 1    104.24 ? 143 GLU A OE1   1 
ATOM   1153 O  OE2   . GLU A 1 143 ? 80.289  -33.407 22.792 1    105.23 ? 143 GLU A OE2   1 
ATOM   1154 N  N     . ILE A 1 144 ? 77.481  -35.062 17.937 1    95.86  ? 144 ILE A N     1 
ATOM   1155 C  CA    . ILE A 1 144 ? 76.764  -34.585 16.753 1    97.51  ? 144 ILE A CA    1 
ATOM   1156 C  C     . ILE A 1 144 ? 75.28   -34.451 17.126 1    99.26  ? 144 ILE A C     1 
ATOM   1157 O  O     . ILE A 1 144 ? 74.664  -33.413 16.868 1    99.33  ? 144 ILE A O     1 
ATOM   1158 C  CB    . ILE A 1 144 ? 76.967  -35.571 15.576 1    97.87  ? 144 ILE A CB    1 
ATOM   1159 C  CG1   . ILE A 1 144 ? 78.441  -35.639 15.15  1    98.69  ? 144 ILE A CG1   1 
ATOM   1160 C  CG2   . ILE A 1 144 ? 76.065  -35.218 14.403 1    98.34  ? 144 ILE A CG2   1 
ATOM   1161 C  CD1   . ILE A 1 144 ? 78.755  -36.831 14.386 1    99.87  ? 144 ILE A CD1   1 
ATOM   1162 N  N     . ALA A 1 145 ? 74.731  -35.487 17.794 1    100.44 ? 145 ALA A N     1 
ATOM   1163 C  CA    . ALA A 1 145 ? 73.354  -35.526 18.287 1    102.05 ? 145 ALA A CA    1 
ATOM   1164 C  C     . ALA A 1 145 ? 73.093  -34.392 19.287 1    103.54 ? 145 ALA A C     1 
ATOM   1165 O  O     . ALA A 1 145 ? 71.999  -33.831 19.308 1    103.62 ? 145 ALA A O     1 
ATOM   1166 C  CB    . ALA A 1 145 ? 73.084  -36.868 18.948 1    102.29 ? 145 ALA A CB    1 
ATOM   1167 N  N     . ARG A 1 146 ? 74.106  -34.055 20.105 1    104.59 ? 146 ARG A N     1 
ATOM   1168 C  CA    . ARG A 1 146 ? 74.082  -32.966 21.087 1    106.11 ? 146 ARG A CA    1 
ATOM   1169 C  C     . ARG A 1 146 ? 73.919  -31.611 20.375 1    107.56 ? 146 ARG A C     1 
ATOM   1170 O  O     . ARG A 1 146 ? 73.276  -30.71  20.909 1    107.77 ? 146 ARG A O     1 
ATOM   1171 C  CB    . ARG A 1 146 ? 75.403  -32.966 21.886 1    107.54 ? 146 ARG A CB    1 
ATOM   1172 C  CG    . ARG A 1 146 ? 75.262  -32.677 23.377 1    110.82 ? 146 ARG A CG    1 
ATOM   1173 C  CD    . ARG A 1 146 ? 75.326  -31.197 23.716 1    114.12 ? 146 ARG A CD    1 
ATOM   1174 N  NE    . ARG A 1 146 ? 76.623  -30.6   23.384 1    116.97 ? 146 ARG A NE    1 
ATOM   1175 C  CZ    . ARG A 1 146 ? 77.014  -29.389 23.775 1    119.09 ? 146 ARG A CZ    1 
ATOM   1176 N  NH1   . ARG A 1 146 ? 76.22   -28.637 24.53  1    118.68 ? 146 ARG A NH1   1 
ATOM   1177 N  NH2   . ARG A 1 146 ? 78.206  -28.925 23.423 1    119.04 ? 146 ARG A NH2   1 
ATOM   1178 N  N     . LEU A 1 147 ? 74.513  -31.465 19.177 1    108.39 ? 147 LEU A N     1 
ATOM   1179 C  CA    . LEU A 1 147 ? 74.457  -30.232 18.401 1    109.58 ? 147 LEU A CA    1 
ATOM   1180 C  C     . LEU A 1 147 ? 73.101  -30.009 17.723 1    110.72 ? 147 LEU A C     1 
ATOM   1181 O  O     . LEU A 1 147 ? 72.723  -28.858 17.51  1    111.05 ? 147 LEU A O     1 
ATOM   1182 C  CB    . LEU A 1 147 ? 75.606  -30.177 17.38  1    109.76 ? 147 LEU A CB    1 
ATOM   1183 C  CG    . LEU A 1 147 ? 76.123  -28.782 17.026 1    111.25 ? 147 LEU A CG    1 
ATOM   1184 C  CD1   . LEU A 1 147 ? 76.626  -28.045 18.258 1    111.79 ? 147 LEU A CD1   1 
ATOM   1185 C  CD2   . LEU A 1 147 ? 77.219  -28.858 15.982 1    111.95 ? 147 LEU A CD2   1 
ATOM   1186 N  N     . GLU A 1 148 ? 72.354  -31.09  17.413 1    111.11 ? 148 GLU A N     1 
ATOM   1187 C  CA    . GLU A 1 148 ? 71.03   -30.978 16.781 1    111.84 ? 148 GLU A CA    1 
ATOM   1188 C  C     . GLU A 1 148 ? 69.97   -30.359 17.71  1    112.72 ? 148 GLU A C     1 
ATOM   1189 O  O     . GLU A 1 148 ? 68.988  -29.792 17.23  1    112.9  ? 148 GLU A O     1 
ATOM   1190 C  CB    . GLU A 1 148 ? 70.547  -32.343 16.284 1    113.34 ? 148 GLU A CB    1 
ATOM   1191 C  CG    . GLU A 1 148 ? 71.516  -33.004 15.326 1    117.05 ? 148 GLU A CG    1 
ATOM   1192 C  CD    . GLU A 1 148 ? 71.262  -34.476 15.064 1    121.79 ? 148 GLU A CD    1 
ATOM   1193 O  OE1   . GLU A 1 148 ? 70.231  -35.002 15.545 1    122.55 ? 148 GLU A OE1   1 
ATOM   1194 O  OE2   . GLU A 1 148 ? 72.1    -35.105 14.378 1    123.15 ? 148 GLU A OE2   1 
ATOM   1195 N  N     . ASP A 1 149 ? 70.164  -30.471 19.032 1    113.02 ? 149 ASP A N     1 
ATOM   1196 C  CA    . ASP A 1 149 ? 69.226  -29.928 20.009 1    113.82 ? 149 ASP A CA    1 
ATOM   1197 C  C     . ASP A 1 149 ? 69.424  -28.419 20.165 1    114.04 ? 149 ASP A C     1 
ATOM   1198 O  O     . ASP A 1 149 ? 70.557  -27.94  20.163 1    114.05 ? 149 ASP A O     1 
ATOM   1199 C  CB    . ASP A 1 149 ? 69.389  -30.631 21.372 1    115.87 ? 149 ASP A CB    1 
ATOM   1200 C  CG    . ASP A 1 149 ? 69.375  -32.152 21.313 1    120.59 ? 149 ASP A CG    1 
ATOM   1201 O  OD1   . ASP A 1 149 ? 69.022  -32.706 20.245 1    121.14 ? 149 ASP A OD1   1 
ATOM   1202 O  OD2   . ASP A 1 149 ? 69.714  -32.788 22.338 1    122.85 ? 149 ASP A OD2   1 
ATOM   1203 N  N     . MET B 1 1   ? 79.519  4.589   7.376  1    31.25  ? 1   MET B N     1 
ATOM   1204 C  CA    . MET B 1 1   ? 80.253  4.679   8.631  1    32     ? 1   MET B CA    1 
ATOM   1205 C  C     . MET B 1 1   ? 81.629  5.277   8.512  1    32.46  ? 1   MET B C     1 
ATOM   1206 O  O     . MET B 1 1   ? 82.477  4.747   7.803  1    32.49  ? 1   MET B O     1 
ATOM   1207 C  CB    . MET B 1 1   ? 80.402  3.311   9.305  1    32.8   ? 1   MET B CB    1 
ATOM   1208 C  CG    . MET B 1 1   ? 79.206  2.876   10.076 1    34.43  ? 1   MET B CG    1 
ATOM   1209 S  SD    . MET B 1 1   ? 79.159  3.509   11.748 1    35.43  ? 1   MET B SD    1 
ATOM   1210 C  CE    . MET B 1 1   ? 80.522  2.687   12.42  1    36.23  ? 1   MET B CE    1 
ATOM   1211 N  N     . HIS B 1 2   ? 81.886  6.304   9.311  1    32.77  ? 2   HIS B N     1 
ATOM   1212 C  CA    . HIS B 1 2   ? 83.183  6.952   9.434  1    33.57  ? 2   HIS B CA    1 
ATOM   1213 C  C     . HIS B 1 2   ? 84.144  5.927   10.061 1    33.81  ? 2   HIS B C     1 
ATOM   1214 O  O     . HIS B 1 2   ? 83.728  5.16    10.944 1    34.02  ? 2   HIS B O     1 
ATOM   1215 C  CB    . HIS B 1 2   ? 83.025  8.138   10.39  1    34.88  ? 2   HIS B CB    1 
ATOM   1216 C  CG    . HIS B 1 2   ? 84.129  9.14    10.341 1    38.25  ? 2   HIS B CG    1 
ATOM   1217 N  ND1   . HIS B 1 2   ? 83.903  10.437  9.904  1    40.48  ? 2   HIS B ND1   1 
ATOM   1218 C  CD2   . HIS B 1 2   ? 85.426  9.021   10.708 1    39.7   ? 2   HIS B CD2   1 
ATOM   1219 C  CE1   . HIS B 1 2   ? 85.066  11.061  10.018 1    41.13  ? 2   HIS B CE1   1 
ATOM   1220 N  NE2   . HIS B 1 2   ? 86.014  10.247  10.494 1    41.02  ? 2   HIS B NE2   1 
ATOM   1221 N  N     . CYS B 1 3   ? 85.41   5.889   9.606  1    33.29  ? 3   CYS B N     1 
ATOM   1222 C  CA    . CYS B 1 3   ? 86.367  4.944   10.163 1    33.13  ? 3   CYS B CA    1 
ATOM   1223 C  C     . CYS B 1 3   ? 86.687  5.351   11.601 1    33.77  ? 3   CYS B C     1 
ATOM   1224 O  O     . CYS B 1 3   ? 87.11   6.488   11.86  1    34.07  ? 3   CYS B O     1 
ATOM   1225 C  CB    . CYS B 1 3   ? 87.626  4.87    9.31   1    32.14  ? 3   CYS B CB    1 
ATOM   1226 S  SG    . CYS B 1 3   ? 88.966  3.906   10.058 1    28.58  ? 3   CYS B SG    1 
ATOM   1227 N  N     . PRO B 1 4   ? 86.512  4.411   12.544 1    33.54  ? 4   PRO B N     1 
ATOM   1228 C  CA    . PRO B 1 4   ? 86.805  4.728   13.944 1    33.74  ? 4   PRO B CA    1 
ATOM   1229 C  C     . PRO B 1 4   ? 88.288  4.862   14.29  1    34.24  ? 4   PRO B C     1 
ATOM   1230 O  O     . PRO B 1 4   ? 88.609  5.185   15.423 1    34.41  ? 4   PRO B O     1 
ATOM   1231 C  CB    . PRO B 1 4   ? 86.163  3.564   14.706 1    34.17  ? 4   PRO B CB    1 
ATOM   1232 C  CG    . PRO B 1 4   ? 86.217  2.433   13.769 1    34.47  ? 4   PRO B CG    1 
ATOM   1233 C  CD    . PRO B 1 4   ? 86.039  3.022   12.388 1    32.97  ? 4   PRO B CD    1 
ATOM   1234 N  N     . PHE B 1 5   ? 89.184  4.629   13.331 1    34.48  ? 5   PHE B N     1 
ATOM   1235 C  CA    . PHE B 1 5   ? 90.615  4.691   13.581 1    35.42  ? 5   PHE B CA    1 
ATOM   1236 C  C     . PHE B 1 5   ? 91.314  5.851   12.871 1    37.21  ? 5   PHE B C     1 
ATOM   1237 O  O     . PHE B 1 5   ? 91.991  6.628   13.539 1    37.74  ? 5   PHE B O     1 
ATOM   1238 C  CB    . PHE B 1 5   ? 91.292  3.352   13.237 1    34.9   ? 5   PHE B CB    1 
ATOM   1239 C  CG    . PHE B 1 5   ? 90.544  2.124   13.706 1    35.32  ? 5   PHE B CG    1 
ATOM   1240 C  CD1   . PHE B 1 5   ? 90.276  1.926   15.051 1    35.85  ? 5   PHE B CD1   1 
ATOM   1241 C  CD2   . PHE B 1 5   ? 90.093  1.18    12.799 1    35.82  ? 5   PHE B CD2   1 
ATOM   1242 C  CE1   . PHE B 1 5   ? 89.568  0.809   15.477 1    36.4   ? 5   PHE B CE1   1 
ATOM   1243 C  CE2   . PHE B 1 5   ? 89.408  0.052   13.229 1    36.43  ? 5   PHE B CE2   1 
ATOM   1244 C  CZ    . PHE B 1 5   ? 89.142  -0.121  14.566 1    36.34  ? 5   PHE B CZ    1 
ATOM   1245 N  N     . CYS B 1 6   ? 91.152  5.989   11.542 1    38.21  ? 6   CYS B N     1 
ATOM   1246 C  CA    . CYS B 1 6   ? 91.865  7.028   10.814 1    39.99  ? 6   CYS B CA    1 
ATOM   1247 C  C     . CYS B 1 6   ? 91.099  8.342   10.628 1    41.76  ? 6   CYS B C     1 
ATOM   1248 O  O     . CYS B 1 6   ? 91.668  9.352   11.017 1    43.44  ? 6   CYS B O     1 
ATOM   1249 C  CB    . CYS B 1 6   ? 92.436  6.527   9.482  1    40.24  ? 6   CYS B CB    1 
ATOM   1250 S  SG    . CYS B 1 6   ? 91.224  6.364   8.14   1    41.17  ? 6   CYS B SG    1 
ATOM   1251 N  N     . PHE B 1 7   ? 89.955  8.406   9.952  1    41.24  ? 7   PHE B N     1 
ATOM   1252 C  CA    . PHE B 1 7   ? 89.331  9.699   9.58   1    41.27  ? 7   PHE B CA    1 
ATOM   1253 C  C     . PHE B 1 7   ? 88.452  9.59    8.333  1    39.78  ? 7   PHE B C     1 
ATOM   1254 O  O     . PHE B 1 7   ? 87.793  10.576  7.962  1    39.31  ? 7   PHE B O     1 
ATOM   1255 C  CB    . PHE B 1 7   ? 90.414  10.793  9.233  1    41.92  ? 7   PHE B CB    1 
ATOM   1256 C  CG    . PHE B 1 7   ? 91.151  10.703  7.899  1    43.77  ? 7   PHE B CG    1 
ATOM   1257 C  CD1   . PHE B 1 7   ? 92.35   10.015  7.791  1    45.03  ? 7   PHE B CD1   1 
ATOM   1258 C  CD2   . PHE B 1 7   ? 90.678  11.371  6.773  1    45.08  ? 7   PHE B CD2   1 
ATOM   1259 C  CE1   . PHE B 1 7   ? 93.026  9.942   6.57   1    45.95  ? 7   PHE B CE1   1 
ATOM   1260 C  CE2   . PHE B 1 7   ? 91.349  11.284  5.548  1    45.91  ? 7   PHE B CE2   1 
ATOM   1261 C  CZ    . PHE B 1 7   ? 92.52   10.578  5.456  1    45.77  ? 7   PHE B CZ    1 
ATOM   1262 N  N     . ALA B 1 8   ? 88.512  8.447   7.628  1    38.63  ? 8   ALA B N     1 
ATOM   1263 C  CA    . ALA B 1 8   ? 87.827  8.336   6.354  1    38.1   ? 8   ALA B CA    1 
ATOM   1264 C  C     . ALA B 1 8   ? 86.334  8.388   6.589  1    37.56  ? 8   ALA B C     1 
ATOM   1265 O  O     . ALA B 1 8   ? 85.854  7.734   7.504  1    37.91  ? 8   ALA B O     1 
ATOM   1266 C  CB    . ALA B 1 8   ? 88.24   7.073   5.647  1    38.13  ? 8   ALA B CB    1 
ATOM   1267 N  N     . VAL B 1 9   ? 85.632  9.276   5.881  1    36.32  ? 9   VAL B N     1 
ATOM   1268 C  CA    . VAL B 1 9   ? 84.209  9.542   6.104  1    35.39  ? 9   VAL B CA    1 
ATOM   1269 C  C     . VAL B 1 9   ? 83.266  8.378   5.801  1    34.06  ? 9   VAL B C     1 
ATOM   1270 O  O     . VAL B 1 9   ? 82.105  8.41    6.219  1    34.13  ? 9   VAL B O     1 
ATOM   1271 C  CB    . VAL B 1 9   ? 83.781  10.799  5.345  1    36.27  ? 9   VAL B CB    1 
ATOM   1272 C  CG1   . VAL B 1 9   ? 84.43   12.03   5.966  1    37.22  ? 9   VAL B CG1   1 
ATOM   1273 C  CG2   . VAL B 1 9   ? 84.128  10.684  3.862  1    36.42  ? 9   VAL B CG2   1 
ATOM   1274 N  N     . ASP B 1 10  ? 83.75   7.36    5.113  1    32.98  ? 10  ASP B N     1 
ATOM   1275 C  CA    . ASP B 1 10  ? 82.949  6.189   4.798  1    32.88  ? 10  ASP B CA    1 
ATOM   1276 C  C     . ASP B 1 10  ? 83.879  4.994   4.641  1    32.04  ? 10  ASP B C     1 
ATOM   1277 O  O     . ASP B 1 10  ? 85.042  5.129   4.25   1    32.61  ? 10  ASP B O     1 
ATOM   1278 C  CB    . ASP B 1 10  ? 82.094  6.405   3.521  1    35.17  ? 10  ASP B CB    1 
ATOM   1279 C  CG    . ASP B 1 10  ? 80.887  5.47    3.367  1    40.73  ? 10  ASP B CG    1 
ATOM   1280 O  OD1   . ASP B 1 10  ? 80.695  4.578   4.245  1    41.22  ? 10  ASP B OD1   1 
ATOM   1281 O  OD2   . ASP B 1 10  ? 80.127  5.634   2.376  1    43.43  ? 10  ASP B OD2   1 
ATOM   1282 N  N     . THR B 1 11  ? 83.357  3.821   4.955  1    30.45  ? 11  THR B N     1 
ATOM   1283 C  CA    . THR B 1 11  ? 84.078  2.548   4.876  1    29.18  ? 11  THR B CA    1 
ATOM   1284 C  C     . THR B 1 11  ? 83.266  1.537   4.034  1    28.35  ? 11  THR B C     1 
ATOM   1285 O  O     . THR B 1 11  ? 82.043  1.67    3.937  1    28.97  ? 11  THR B O     1 
ATOM   1286 C  CB    . THR B 1 11  ? 84.3    2.028   6.296  1    29.02  ? 11  THR B CB    1 
ATOM   1287 O  OG1   . THR B 1 11  ? 83.047  2.019   6.979  1    29.38  ? 11  THR B OG1   1 
ATOM   1288 C  CG2   . THR B 1 11  ? 85.308  2.867   7.072  1    29.16  ? 11  THR B CG2   1 
ATOM   1289 N  N     . LYS B 1 12  ? 83.926  0.522   3.453  1    26.61  ? 12  LYS B N     1 
ATOM   1290 C  CA    . LYS B 1 12  ? 83.218  -0.506  2.693  1    25.99  ? 12  LYS B CA    1 
ATOM   1291 C  C     . LYS B 1 12  ? 82.631  -1.591  3.6    1    25.37  ? 12  LYS B C     1 
ATOM   1292 O  O     . LYS B 1 12  ? 83.358  -2.12   4.42   1    24.98  ? 12  LYS B O     1 
ATOM   1293 C  CB    . LYS B 1 12  ? 84.2    -1.186  1.73   1    27.94  ? 12  LYS B CB    1 
ATOM   1294 C  CG    . LYS B 1 12  ? 83.634  -2.374  0.938  1    31.37  ? 12  LYS B CG    1 
ATOM   1295 C  CD    . LYS B 1 12  ? 82.513  -1.969  -0.01  1    34.58  ? 12  LYS B CD    1 
ATOM   1296 C  CE    . LYS B 1 12  ? 81.886  -3.176  -0.645 1    37.38  ? 12  LYS B CE    1 
ATOM   1297 N  NZ    . LYS B 1 12  ? 80.439  -2.973  -0.888 1    39.54  ? 12  LYS B NZ    1 
ATOM   1298 N  N     . VAL B 1 13  ? 81.362  -1.991  3.401  1    25.11  ? 13  VAL B N     1 
ATOM   1299 C  CA    . VAL B 1 13  ? 80.811  -3.141  4.116  1    25.36  ? 13  VAL B CA    1 
ATOM   1300 C  C     . VAL B 1 13  ? 81.314  -4.383  3.354  1    26.75  ? 13  VAL B C     1 
ATOM   1301 O  O     . VAL B 1 13  ? 80.928  -4.617  2.194  1    27.25  ? 13  VAL B O     1 
ATOM   1302 C  CB    . VAL B 1 13  ? 79.275  -3.15   4.189  1    25.35  ? 13  VAL B CB    1 
ATOM   1303 C  CG1   . VAL B 1 13  ? 78.769  -4.479  4.719  1    25.68  ? 13  VAL B CG1   1 
ATOM   1304 C  CG2   . VAL B 1 13  ? 78.761  -2.01   5.041  1    25.82  ? 13  VAL B CG2   1 
ATOM   1305 N  N     . ILE B 1 14  ? 82.231  -5.135  3.968  1    26.79  ? 14  ILE B N     1 
ATOM   1306 C  CA    . ILE B 1 14  ? 82.759  -6.341  3.334  1    26.78  ? 14  ILE B CA    1 
ATOM   1307 C  C     . ILE B 1 14  ? 82.029  -7.602  3.803  1    27.83  ? 14  ILE B C     1 
ATOM   1308 O  O     . ILE B 1 14  ? 82.474  -8.688  3.465  1    28.71  ? 14  ILE B O     1 
ATOM   1309 C  CB    . ILE B 1 14  ? 84.289  -6.456  3.474  1    26.13  ? 14  ILE B CB    1 
ATOM   1310 C  CG1   . ILE B 1 14  ? 84.672  -6.757  4.934  1    26.63  ? 14  ILE B CG1   1 
ATOM   1311 C  CG2   . ILE B 1 14  ? 84.982  -5.205  2.905  1    25.93  ? 14  ILE B CG2   1 
ATOM   1312 C  CD1   . ILE B 1 14  ? 86.102  -6.769  5.268  1    27.61  ? 14  ILE B CD1   1 
ATOM   1313 N  N     . ASP B 1 15  ? 80.892  -7.468  4.52   1    27.71  ? 15  ASP B N     1 
ATOM   1314 C  CA    . ASP B 1 15  ? 80.06   -8.582  4.968  1    28.55  ? 15  ASP B CA    1 
ATOM   1315 C  C     . ASP B 1 15  ? 78.956  -8.11   5.869  1    28.43  ? 15  ASP B C     1 
ATOM   1316 O  O     . ASP B 1 15  ? 79.164  -7.218  6.67   1    28.38  ? 15  ASP B O     1 
ATOM   1317 C  CB    . ASP B 1 15  ? 80.865  -9.651  5.705  1    31.58  ? 15  ASP B CB    1 
ATOM   1318 C  CG    . ASP B 1 15  ? 80.097  -10.942 5.891  1    38.78  ? 15  ASP B CG    1 
ATOM   1319 O  OD1   . ASP B 1 15  ? 79.363  -11.341 4.949  1    39.91  ? 15  ASP B OD1   1 
ATOM   1320 O  OD2   . ASP B 1 15  ? 80.228  -11.558 6.977  1    42.54  ? 15  ASP B OD2   1 
ATOM   1321 N  N     . SER B 1 16  ? 77.792  -8.712  5.755  1    28.6   ? 16  SER B N     1 
ATOM   1322 C  CA    . SER B 1 16  ? 76.667  -8.391  6.616  1    29.94  ? 16  SER B CA    1 
ATOM   1323 C  C     . SER B 1 16  ? 75.924  -9.674  6.988  1    31.67  ? 16  SER B C     1 
ATOM   1324 O  O     . SER B 1 16  ? 76.114  -10.698 6.328  1    32.92  ? 16  SER B O     1 
ATOM   1325 C  CB    . SER B 1 16  ? 75.742  -7.376  5.957  1    30.96  ? 16  SER B CB    1 
ATOM   1326 O  OG    . SER B 1 16  ? 74.85   -7.995  5.046  1    33.15  ? 16  SER B OG    1 
ATOM   1327 N  N     . ARG B 1 17  ? 75.064  -9.625  8.009  1    31.57  ? 17  ARG B N     1 
ATOM   1328 C  CA    . ARG B 1 17  ? 74.313  -10.799 8.434  1    32.18  ? 17  ARG B CA    1 
ATOM   1329 C  C     . ARG B 1 17  ? 73.261  -10.425 9.478  1    30.45  ? 17  ARG B C     1 
ATOM   1330 O  O     . ARG B 1 17  ? 73.508  -9.573  10.329 1    29.86  ? 17  ARG B O     1 
ATOM   1331 C  CB    . ARG B 1 17  ? 75.279  -11.844 9.013  1    36.4   ? 17  ARG B CB    1 
ATOM   1332 C  CG    . ARG B 1 17  ? 74.608  -13.103 9.542  1    43.93  ? 17  ARG B CG    1 
ATOM   1333 C  CD    . ARG B 1 17  ? 75.622  -14.12  10.014 1    50.47  ? 17  ARG B CD    1 
ATOM   1334 N  NE    . ARG B 1 17  ? 76.043  -13.884 11.395 1    56.81  ? 17  ARG B NE    1 
ATOM   1335 C  CZ    . ARG B 1 17  ? 77.182  -13.29  11.746 1    61.37  ? 17  ARG B CZ    1 
ATOM   1336 N  NH1   . ARG B 1 17  ? 77.498  -13.152 13.029 1    60.7   ? 17  ARG B NH1   1 
ATOM   1337 N  NH2   . ARG B 1 17  ? 78.021  -12.841 10.816 1    62.69  ? 17  ARG B NH2   1 
ATOM   1338 N  N     . LEU B 1 18  ? 72.086  -11.046 9.4    1    29.61  ? 18  LEU B N     1 
ATOM   1339 C  CA    . LEU B 1 18  ? 71.035  -10.818 10.371 1    29.53  ? 18  LEU B CA    1 
ATOM   1340 C  C     . LEU B 1 18  ? 71.332  -11.609 11.624 1    30.79  ? 18  LEU B C     1 
ATOM   1341 O  O     . LEU B 1 18  ? 71.484  -12.837 11.57  1    30.75  ? 18  LEU B O     1 
ATOM   1342 C  CB    . LEU B 1 18  ? 69.678  -11.243 9.831  1    28.85  ? 18  LEU B CB    1 
ATOM   1343 C  CG    . LEU B 1 18  ? 68.925  -10.169 9.123  1    29.43  ? 18  LEU B CG    1 
ATOM   1344 C  CD1   . LEU B 1 18  ? 67.731  -10.736 8.402  1    30.15  ? 18  LEU B CD1   1 
ATOM   1345 C  CD2   . LEU B 1 18  ? 68.498  -9.127  10.073 1    29.5   ? 18  LEU B CD2   1 
ATOM   1346 N  N     . VAL B 1 19  ? 71.427  -10.888 12.751 1    31.47  ? 19  VAL B N     1 
ATOM   1347 C  CA    . VAL B 1 19  ? 71.676  -11.437 14.08  1    32.79  ? 19  VAL B CA    1 
ATOM   1348 C  C     . VAL B 1 19  ? 70.43   -11.243 14.966 1    34.38  ? 19  VAL B C     1 
ATOM   1349 O  O     . VAL B 1 19  ? 69.533  -10.463 14.622 1    34.47  ? 19  VAL B O     1 
ATOM   1350 C  CB    . VAL B 1 19  ? 72.974  -10.865 14.738 1    32.96  ? 19  VAL B CB    1 
ATOM   1351 C  CG1   . VAL B 1 19  ? 74.196  -11.15  13.873 1    33.37  ? 19  VAL B CG1   1 
ATOM   1352 C  CG2   . VAL B 1 19  ? 72.852  -9.373  15.045 1    32.93  ? 19  VAL B CG2   1 
ATOM   1353 N  N     . GLY B 1 20  ? 70.373  -11.99  16.068 1    35.35  ? 20  GLY B N     1 
ATOM   1354 C  CA    . GLY B 1 20  ? 69.271  -11.926 17.018 1    36.78  ? 20  GLY B CA    1 
ATOM   1355 C  C     . GLY B 1 20  ? 67.925  -12.212 16.391 1    38.15  ? 20  GLY B C     1 
ATOM   1356 O  O     . GLY B 1 20  ? 66.964  -11.474 16.613 1    38.28  ? 20  GLY B O     1 
ATOM   1357 N  N     . GLU B 1 21  ? 67.865  -13.248 15.552 1    39.03  ? 21  GLU B N     1 
ATOM   1358 C  CA    . GLU B 1 21  ? 66.634  -13.647 14.874 1    40.34  ? 21  GLU B CA    1 
ATOM   1359 C  C     . GLU B 1 21  ? 65.97   -12.504 14.08  1    40.6   ? 21  GLU B C     1 
ATOM   1360 O  O     . GLU B 1 21  ? 64.745  -12.377 14.09  1    41.53  ? 21  GLU B O     1 
ATOM   1361 C  CB    . GLU B 1 21  ? 65.64   -14.271 15.875 1    43.51  ? 21  GLU B CB    1 
ATOM   1362 C  CG    . GLU B 1 21  ? 66.266  -15.288 16.819 1    50.22  ? 21  GLU B CG    1 
ATOM   1363 C  CD    . GLU B 1 21  ? 65.319  -15.8   17.884 1    58.96  ? 21  GLU B CD    1 
ATOM   1364 O  OE1   . GLU B 1 21  ? 65.601  -15.587 19.087 1    61.04  ? 21  GLU B OE1   1 
ATOM   1365 O  OE2   . GLU B 1 21  ? 64.287  -16.406 17.513 1    61.87  ? 21  GLU B OE2   1 
ATOM   1366 N  N     . GLY B 1 22  ? 66.777  -11.679 13.415 1    39.34  ? 22  GLY B N     1 
ATOM   1367 C  CA    . GLY B 1 22  ? 66.256  -10.555 12.646 1    38.38  ? 22  GLY B CA    1 
ATOM   1368 C  C     . GLY B 1 22  ? 66.195  -9.246  13.414 1    37.28  ? 22  GLY B C     1 
ATOM   1369 O  O     . GLY B 1 22  ? 66.012  -8.195  12.808 1    38.05  ? 22  GLY B O     1 
ATOM   1370 N  N     . SER B 1 23  ? 66.358  -9.274  14.748 1    35.06  ? 23  SER B N     1 
ATOM   1371 C  CA    . SER B 1 23  ? 66.298  -8.061  15.574 1    33.36  ? 23  SER B CA    1 
ATOM   1372 C  C     . SER B 1 23  ? 67.459  -7.064  15.35  1    31.54  ? 23  SER B C     1 
ATOM   1373 O  O     . SER B 1 23  ? 67.451  -5.975  15.946 1    31.54  ? 23  SER B O     1 
ATOM   1374 C  CB    . SER B 1 23  ? 66.227  -8.429  17.058 1    33.6   ? 23  SER B CB    1 
ATOM   1375 O  OG    . SER B 1 23  ? 67.488  -8.778  17.61  1    33.77  ? 23  SER B OG    1 
ATOM   1376 N  N     . SER B 1 24  ? 68.471  -7.448  14.546 1    29.49  ? 24  SER B N     1 
ATOM   1377 C  CA    . SER B 1 24  ? 69.618  -6.574  14.339 1    28.06  ? 24  SER B CA    1 
ATOM   1378 C  C     . SER B 1 24  ? 70.479  -6.965  13.148 1    25.33  ? 24  SER B C     1 
ATOM   1379 O  O     . SER B 1 24  ? 70.499  -8.126  12.741 1    24.91  ? 24  SER B O     1 
ATOM   1380 C  CB    . SER B 1 24  ? 70.463  -6.491  15.607 1    30.12  ? 24  SER B CB    1 
ATOM   1381 O  OG    . SER B 1 24  ? 71.296  -5.347  15.543 1    33.48  ? 24  SER B OG    1 
ATOM   1382 N  N     . VAL B 1 25  ? 71.201  -5.99   12.598 1    23.45  ? 25  VAL B N     1 
ATOM   1383 C  CA    . VAL B 1 25  ? 72.049  -6.217  11.434 1    21.9   ? 25  VAL B CA    1 
ATOM   1384 C  C     . VAL B 1 25  ? 73.506  -6.061  11.821 1    20.67  ? 25  VAL B C     1 
ATOM   1385 O  O     . VAL B 1 25  ? 73.919  -4.994  12.282 1    20.37  ? 25  VAL B O     1 
ATOM   1386 C  CB    . VAL B 1 25  ? 71.658  -5.28   10.259 1    22.09  ? 25  VAL B CB    1 
ATOM   1387 C  CG1   . VAL B 1 25  ? 72.723  -5.263  9.168  1    22.35  ? 25  VAL B CG1   1 
ATOM   1388 C  CG2   . VAL B 1 25  ? 70.313  -5.675  9.674  1    22.5   ? 25  VAL B CG2   1 
ATOM   1389 N  N     . ARG B 1 26  ? 74.29   -7.118  11.621 1    19.78  ? 26  ARG B N     1 
ATOM   1390 C  CA    . ARG B 1 26  ? 75.711  -7.069  11.923 1    19.78  ? 26  ARG B CA    1 
ATOM   1391 C  C     . ARG B 1 26  ? 76.468  -6.857  10.638 1    19.48  ? 26  ARG B C     1 
ATOM   1392 O  O     . ARG B 1 26  ? 76.202  -7.529  9.655  1    19.95  ? 26  ARG B O     1 
ATOM   1393 C  CB    . ARG B 1 26  ? 76.167  -8.365  12.597 1    21.38  ? 26  ARG B CB    1 
ATOM   1394 C  CG    . ARG B 1 26  ? 77.662  -8.445  12.845 1    25.03  ? 26  ARG B CG    1 
ATOM   1395 C  CD    . ARG B 1 26  ? 78.057  -9.881  13.032 1    30.37  ? 26  ARG B CD    1 
ATOM   1396 N  NE    . ARG B 1 26  ? 78.878  -10.054 14.228 1    37.47  ? 26  ARG B NE    1 
ATOM   1397 C  CZ    . ARG B 1 26  ? 80.202  -10.155 14.214 1    42.53  ? 26  ARG B CZ    1 
ATOM   1398 N  NH1   . ARG B 1 26  ? 80.868  -10.121 13.058 1    43.69  ? 26  ARG B NH1   1 
ATOM   1399 N  NH2   . ARG B 1 26  ? 80.876  -10.298 15.355 1    41.99  ? 26  ARG B NH2   1 
ATOM   1400 N  N     . ARG B 1 27  ? 77.402  -5.911  10.63  1    18.44  ? 27  ARG B N     1 
ATOM   1401 C  CA    . ARG B 1 27  ? 78.218  -5.636  9.453  1    17.2   ? 27  ARG B CA    1 
ATOM   1402 C  C     . ARG B 1 27  ? 79.696  -5.677  9.798  1    17.46  ? 27  ARG B C     1 
ATOM   1403 O  O     . ARG B 1 27  ? 80.087  -5.376  10.915 1    18.27  ? 27  ARG B O     1 
ATOM   1404 C  CB    . ARG B 1 27  ? 77.884  -4.264  8.886  1    16.66  ? 27  ARG B CB    1 
ATOM   1405 C  CG    . ARG B 1 27  ? 76.454  -4.137  8.397  1    17.19  ? 27  ARG B CG    1 
ATOM   1406 C  CD    . ARG B 1 27  ? 76.25   -2.817  7.698  1    17.32  ? 27  ARG B CD    1 
ATOM   1407 N  NE    . ARG B 1 27  ? 74.882  -2.699  7.234  1    17.31  ? 27  ARG B NE    1 
ATOM   1408 C  CZ    . ARG B 1 27  ? 73.914  -2.077  7.891  1    19.49  ? 27  ARG B CZ    1 
ATOM   1409 N  NH1   . ARG B 1 27  ? 74.143  -1.549  9.085  1    19.1   ? 27  ARG B NH1   1 
ATOM   1410 N  NH2   . ARG B 1 27  ? 72.687  -2.035  7.392  1    20.48  ? 27  ARG B NH2   1 
ATOM   1411 N  N     . ARG B 1 28  ? 80.513  -6.086  8.858  1    17.17  ? 28  ARG B N     1 
ATOM   1412 C  CA    . ARG B 1 28  ? 81.956  -6.13   9.014  1    17.49  ? 28  ARG B CA    1 
ATOM   1413 C  C     . ARG B 1 28  ? 82.499  -5.162  7.981  1    17.88  ? 28  ARG B C     1 
ATOM   1414 O  O     . ARG B 1 28  ? 82.436  -5.456  6.797  1    17.84  ? 28  ARG B O     1 
ATOM   1415 C  CB    . ARG B 1 28  ? 82.48   -7.546  8.712  1    18.42  ? 28  ARG B CB    1 
ATOM   1416 C  CG    . ARG B 1 28  ? 83.986  -7.722  8.916  1    19.59  ? 28  ARG B CG    1 
ATOM   1417 C  CD    . ARG B 1 28  ? 84.469  -7.183  10.25  1    19.18  ? 28  ARG B CD    1 
ATOM   1418 N  NE    . ARG B 1 28  ? 85.807  -7.655  10.589 1    19.85  ? 28  ARG B NE    1 
ATOM   1419 C  CZ    . ARG B 1 28  ? 86.418  -7.401  11.743 1    21.43  ? 28  ARG B CZ    1 
ATOM   1420 N  NH1   . ARG B 1 28  ? 87.63   -7.886  11.981 1    20.12  ? 28  ARG B NH1   1 
ATOM   1421 N  NH2   . ARG B 1 28  ? 85.809  -6.691  12.682 1    22.31  ? 28  ARG B NH2   1 
ATOM   1422 N  N     . ARG B 1 29  ? 82.972  -3.991  8.407  1    17.58  ? 29  ARG B N     1 
ATOM   1423 C  CA    . ARG B 1 29  ? 83.432  -2.968  7.468  1    17.21  ? 29  ARG B CA    1 
ATOM   1424 C  C     . ARG B 1 29  ? 84.961  -2.952  7.294  1    18.26  ? 29  ARG B C     1 
ATOM   1425 O  O     . ARG B 1 29  ? 85.672  -3.499  8.119  1    18.97  ? 29  ARG B O     1 
ATOM   1426 C  CB    . ARG B 1 29  ? 82.888  -1.587  7.9    1    16.84  ? 29  ARG B CB    1 
ATOM   1427 C  CG    . ARG B 1 29  ? 81.441  -1.638  8.391  1    18.02  ? 29  ARG B CG    1 
ATOM   1428 C  CD    . ARG B 1 29  ? 80.859  -0.279  8.629  1    21.03  ? 29  ARG B CD    1 
ATOM   1429 N  NE    . ARG B 1 29  ? 80.745  0.473   7.384  1    26.7   ? 29  ARG B NE    1 
ATOM   1430 C  CZ    . ARG B 1 29  ? 79.593  0.818   6.81   1    30.22  ? 29  ARG B CZ    1 
ATOM   1431 N  NH1   . ARG B 1 29  ? 78.438  0.498   7.378  1    30.47  ? 29  ARG B NH1   1 
ATOM   1432 N  NH2   . ARG B 1 29  ? 79.59   1.498   5.67   1    30.24  ? 29  ARG B NH2   1 
ATOM   1433 N  N     . GLN B 1 30  ? 85.468  -2.377  6.208  1    18.6   ? 30  GLN B N     1 
ATOM   1434 C  CA    . GLN B 1 30  ? 86.904  -2.23   5.984  1    19.47  ? 30  GLN B CA    1 
ATOM   1435 C  C     . GLN B 1 30  ? 87.183  -0.813  5.549  1    20.67  ? 30  GLN B C     1 
ATOM   1436 O  O     . GLN B 1 30  ? 86.471  -0.282  4.703  1    20.65  ? 30  GLN B O     1 
ATOM   1437 C  CB    . GLN B 1 30  ? 87.443  -3.214  4.937  1    20.24  ? 30  GLN B CB    1 
ATOM   1438 C  CG    . GLN B 1 30  ? 88.939  -3.041  4.685  1    22.47  ? 30  GLN B CG    1 
ATOM   1439 C  CD    . GLN B 1 30  ? 89.517  -4.167  3.875  1    28.11  ? 30  GLN B CD    1 
ATOM   1440 O  OE1   . GLN B 1 30  ? 89.044  -5.297  3.954  1    31.56  ? 30  GLN B OE1   1 
ATOM   1441 N  NE2   . GLN B 1 30  ? 90.561  -3.894  3.077  1    26.84  ? 30  GLN B NE2   1 
ATOM   1442 N  N     . CYS B 1 31  ? 88.196  -0.192  6.138  1    22.1   ? 31  CYS B N     1 
ATOM   1443 C  CA    . CYS B 1 31  ? 88.551  1.161   5.773  1    24.22  ? 31  CYS B CA    1 
ATOM   1444 C  C     . CYS B 1 31  ? 89.414  1.149   4.524  1    25.29  ? 31  CYS B C     1 
ATOM   1445 O  O     . CYS B 1 31  ? 90.29   0.302   4.378  1    25.27  ? 31  CYS B O     1 
ATOM   1446 C  CB    . CYS B 1 31  ? 89.228  1.897   6.922  1    25.99  ? 31  CYS B CB    1 
ATOM   1447 S  SG    . CYS B 1 31  ? 89.557  3.638   6.563  1    33.92  ? 31  CYS B SG    1 
ATOM   1448 N  N     . LEU B 1 32  ? 89.141  2.059   3.606  1    26.12  ? 32  LEU B N     1 
ATOM   1449 C  CA    . LEU B 1 32  ? 89.886  2.138   2.361  1    27.42  ? 32  LEU B CA    1 
ATOM   1450 C  C     . LEU B 1 32  ? 91.245  2.813   2.585  1    29.24  ? 32  LEU B C     1 
ATOM   1451 O  O     . LEU B 1 32  ? 92.248  2.386   2.016  1    29.58  ? 32  LEU B O     1 
ATOM   1452 C  CB    . LEU B 1 32  ? 89.052  2.862   1.288  1    27.61  ? 32  LEU B CB    1 
ATOM   1453 C  CG    . LEU B 1 32  ? 88.072  1.964   0.479  1    28.86  ? 32  LEU B CG    1 
ATOM   1454 C  CD1   . LEU B 1 32  ? 87.085  1.245   1.396  1    29.83  ? 32  LEU B CD1   1 
ATOM   1455 C  CD2   . LEU B 1 32  ? 87.341  2.736   -0.564 1    28.55  ? 32  LEU B CD2   1 
ATOM   1456 N  N     . VAL B 1 33  ? 91.285  3.831   3.46   1    30.41  ? 33  VAL B N     1 
ATOM   1457 C  CA    . VAL B 1 33  ? 92.497  4.588   3.776  1    31.51  ? 33  VAL B CA    1 
ATOM   1458 C  C     . VAL B 1 33  ? 93.5    3.82    4.657  1    32.5   ? 33  VAL B C     1 
ATOM   1459 O  O     . VAL B 1 33  ? 94.648  3.674   4.247  1    33.01  ? 33  VAL B O     1 
ATOM   1460 C  CB    . VAL B 1 33  ? 92.15   5.964   4.39   1    32.13  ? 33  VAL B CB    1 
ATOM   1461 C  CG1   . VAL B 1 33  ? 93.409  6.779   4.664  1    32.66  ? 33  VAL B CG1   1 
ATOM   1462 C  CG2   . VAL B 1 33  ? 91.185  6.734   3.496  1    32.17  ? 33  VAL B CG2   1 
ATOM   1463 N  N     . CYS B 1 34  ? 93.09   3.334   5.846  1    32.52  ? 34  CYS B N     1 
ATOM   1464 C  CA    . CYS B 1 34  ? 94.018  2.635   6.737  1    33.24  ? 34  CYS B CA    1 
ATOM   1465 C  C     . CYS B 1 34  ? 93.932  1.103   6.693  1    34.07  ? 34  CYS B C     1 
ATOM   1466 O  O     . CYS B 1 34  ? 94.625  0.45    7.464  1    33.97  ? 34  CYS B O     1 
ATOM   1467 C  CB    . CYS B 1 34  ? 93.874  3.144   8.163  1    33.91  ? 34  CYS B CB    1 
ATOM   1468 S  SG    . CYS B 1 34  ? 92.337  2.644   8.971  1    36.82  ? 34  CYS B SG    1 
ATOM   1469 N  N     . ASN B 1 35  ? 93.093  0.54    5.806  1    35.01  ? 35  ASN B N     1 
ATOM   1470 C  CA    . ASN B 1 35  ? 92.881  -0.903  5.589  1    36.25  ? 35  ASN B CA    1 
ATOM   1471 C  C     . ASN B 1 35  ? 92.476  -1.685  6.838  1    36.1   ? 35  ASN B C     1 
ATOM   1472 O  O     . ASN B 1 35  ? 92.699  -2.895  6.892  1    36.35  ? 35  ASN B O     1 
ATOM   1473 C  CB    . ASN B 1 35  ? 94.075  -1.581  4.91   1    39     ? 35  ASN B CB    1 
ATOM   1474 C  CG    . ASN B 1 35  ? 94.746  -0.761  3.836  1    45.1   ? 35  ASN B CG    1 
ATOM   1475 O  OD1   . ASN B 1 35  ? 95.805  -0.186  4.074  1    48.17  ? 35  ASN B OD1   1 
ATOM   1476 N  ND2   . ASN B 1 35  ? 94.17   -0.683  2.64   1    45.71  ? 35  ASN B ND2   1 
ATOM   1477 N  N     . GLU B 1 36  ? 91.873  -1.014  7.829  1    35.42  ? 36  GLU B N     1 
ATOM   1478 C  CA    . GLU B 1 36  ? 91.482  -1.682  9.065  1    35.1   ? 36  GLU B CA    1 
ATOM   1479 C  C     . GLU B 1 36  ? 90.068  -2.221  9.017  1    33.94  ? 36  GLU B C     1 
ATOM   1480 O  O     . GLU B 1 36  ? 89.222  -1.659  8.337  1    33.94  ? 36  GLU B O     1 
ATOM   1481 C  CB    . GLU B 1 36  ? 91.631  -0.736  10.259 1    38.37  ? 36  GLU B CB    1 
ATOM   1482 C  CG    . GLU B 1 36  ? 93.067  -0.48   10.68  1    45.64  ? 36  GLU B CG    1 
ATOM   1483 C  CD    . GLU B 1 36  ? 93.786  -1.667  11.288 1    54.76  ? 36  GLU B CD    1 
ATOM   1484 O  OE1   . GLU B 1 36  ? 94.993  -1.838  11.001 1    57.68  ? 36  GLU B OE1   1 
ATOM   1485 O  OE2   . GLU B 1 36  ? 93.144  -2.429  12.048 1    56.91  ? 36  GLU B OE2   1 
ATOM   1486 N  N     . ARG B 1 37  ? 89.793  -3.288  9.782  1    32.79  ? 37  ARG B N     1 
ATOM   1487 C  CA    . ARG B 1 37  ? 88.459  -3.879  9.834  1    31.63  ? 37  ARG B CA    1 
ATOM   1488 C  C     . ARG B 1 37  ? 87.795  -3.676  11.2   1    30.07  ? 37  ARG B C     1 
ATOM   1489 O  O     . ARG B 1 37  ? 88.476  -3.594  12.232 1    31.14  ? 37  ARG B O     1 
ATOM   1490 C  CB    . ARG B 1 37  ? 88.486  -5.36   9.422  1    33.01  ? 37  ARG B CB    1 
ATOM   1491 C  CG    . ARG B 1 37  ? 89.035  -5.573  8.012  1    36.56  ? 37  ARG B CG    1 
ATOM   1492 C  CD    . ARG B 1 37  ? 88.891  -7.014  7.555  1    41.92  ? 37  ARG B CD    1 
ATOM   1493 N  NE    . ARG B 1 37  ? 89.572  -7.279  6.282  1    47.27  ? 37  ARG B NE    1 
ATOM   1494 C  CZ    . ARG B 1 37  ? 89.338  -8.342  5.507  1    51.55  ? 37  ARG B CZ    1 
ATOM   1495 N  NH1   . ARG B 1 37  ? 90.018  -8.511  4.379  1    52.23  ? 37  ARG B NH1   1 
ATOM   1496 N  NH2   . ARG B 1 37  ? 88.361  -9.19   5.805  1    51.78  ? 37  ARG B NH2   1 
ATOM   1497 N  N     . PHE B 1 38  ? 86.468  -3.555  11.211 1    27.42  ? 38  PHE B N     1 
ATOM   1498 C  CA    . PHE B 1 38  ? 85.712  -3.357  12.448 1    25.24  ? 38  PHE B CA    1 
ATOM   1499 C  C     . PHE B 1 38  ? 84.299  -3.878  12.3   1    23.17  ? 38  PHE B C     1 
ATOM   1500 O  O     . PHE B 1 38  ? 83.774  -3.921  11.195 1    24.19  ? 38  PHE B O     1 
ATOM   1501 C  CB    . PHE B 1 38  ? 85.713  -1.89   12.897 1    25.22  ? 38  PHE B CB    1 
ATOM   1502 C  CG    . PHE B 1 38  ? 85.127  -0.903  11.919 1    26.49  ? 38  PHE B CG    1 
ATOM   1503 C  CD1   . PHE B 1 38  ? 85.873  -0.436  10.844 1    27.62  ? 38  PHE B CD1   1 
ATOM   1504 C  CD2   . PHE B 1 38  ? 83.866  -0.382  12.114 1    27.52  ? 38  PHE B CD2   1 
ATOM   1505 C  CE1   . PHE B 1 38  ? 85.343  0.491   9.955  1    28.47  ? 38  PHE B CE1   1 
ATOM   1506 C  CE2   . PHE B 1 38  ? 83.339  0.552   11.224 1    28.41  ? 38  PHE B CE2   1 
ATOM   1507 C  CZ    . PHE B 1 38  ? 84.084  0.987   10.156 1    28.39  ? 38  PHE B CZ    1 
ATOM   1508 N  N     . THR B 1 39  ? 83.688  -4.309  13.39  1    20.64  ? 39  THR B N     1 
ATOM   1509 C  CA    . THR B 1 39  ? 82.324  -4.841  13.388 1    18.63  ? 39  THR B CA    1 
ATOM   1510 C  C     . THR B 1 39  ? 81.334  -3.761  13.825 1    16.82  ? 39  THR B C     1 
ATOM   1511 O  O     . THR B 1 39  ? 81.665  -2.945  14.67  1    16.97  ? 39  THR B O     1 
ATOM   1512 C  CB    . THR B 1 39  ? 82.258  -6.059  14.327 1    19.32  ? 39  THR B CB    1 
ATOM   1513 O  OG1   . THR B 1 39  ? 82.994  -7.127  13.738 1    19.72  ? 39  THR B OG1   1 
ATOM   1514 C  CG2   . THR B 1 39  ? 80.824  -6.498  14.653 1    19.59  ? 39  THR B CG2   1 
ATOM   1515 N  N     . THR B 1 40  ? 80.152  -3.705  13.207 1    15     ? 40  THR B N     1 
ATOM   1516 C  CA    . THR B 1 40  ? 79.117  -2.763  13.608 1    13.65  ? 40  THR B CA    1 
ATOM   1517 C  C     . THR B 1 40  ? 77.785  -3.479  13.799 1    13.68  ? 40  THR B C     1 
ATOM   1518 O  O     . THR B 1 40  ? 77.521  -4.499  13.153 1    13.97  ? 40  THR B O     1 
ATOM   1519 C  CB    . THR B 1 40  ? 78.969  -1.561  12.655 1    12.67  ? 40  THR B CB    1 
ATOM   1520 O  OG1   . THR B 1 40  ? 78.243  -1.93   11.493 1    13.37  ? 40  THR B OG1   1 
ATOM   1521 C  CG2   . THR B 1 40  ? 80.259  -0.932  12.294 1    12.08  ? 40  THR B CG2   1 
ATOM   1522 N  N     . PHE B 1 41  ? 76.925  -2.911  14.642 1    12.99  ? 41  PHE B N     1 
ATOM   1523 C  CA    . PHE B 1 41  ? 75.597  -3.444  14.843 1    13.12  ? 41  PHE B CA    1 
ATOM   1524 C  C     . PHE B 1 41  ? 74.597  -2.331  14.607 1    13.15  ? 41  PHE B C     1 
ATOM   1525 O  O     . PHE B 1 41  ? 74.79   -1.207  15.073 1    12.89  ? 41  PHE B O     1 
ATOM   1526 C  CB    . PHE B 1 41  ? 75.442  -4.042  16.241 1    13.19  ? 41  PHE B CB    1 
ATOM   1527 C  CG    . PHE B 1 41  ? 76.238  -5.304  16.461 1    14.2   ? 41  PHE B CG    1 
ATOM   1528 C  CD1   . PHE B 1 41  ? 75.771  -6.524  16.01  1    15.12  ? 41  PHE B CD1   1 
ATOM   1529 C  CD2   . PHE B 1 41  ? 77.452  -5.271  17.127 1    15.06  ? 41  PHE B CD2   1 
ATOM   1530 C  CE1   . PHE B 1 41  ? 76.497  -7.681  16.226 1    15.83  ? 41  PHE B CE1   1 
ATOM   1531 C  CE2   . PHE B 1 41  ? 78.181  -6.428  17.331 1    15.68  ? 41  PHE B CE2   1 
ATOM   1532 C  CZ    . PHE B 1 41  ? 77.702  -7.625  16.874 1    15.59  ? 41  PHE B CZ    1 
ATOM   1533 N  N     . GLU B 1 42  ? 73.561  -2.628  13.819 1    13.24  ? 42  GLU B N     1 
ATOM   1534 C  CA    . GLU B 1 42  ? 72.502  -1.676  13.512 1    13.35  ? 42  GLU B CA    1 
ATOM   1535 C  C     . GLU B 1 42  ? 71.255  -2.135  14.264 1    13.55  ? 42  GLU B C     1 
ATOM   1536 O  O     . GLU B 1 42  ? 70.778  -3.253  14.056 1    13.16  ? 42  GLU B O     1 
ATOM   1537 C  CB    . GLU B 1 42  ? 72.238  -1.632  12.015 1    14.27  ? 42  GLU B CB    1 
ATOM   1538 C  CG    . GLU B 1 42  ? 71.141  -0.653  11.664 1    17.18  ? 42  GLU B CG    1 
ATOM   1539 C  CD    . GLU B 1 42  ? 70.66   -0.725  10.24  1    22.4   ? 42  GLU B CD    1 
ATOM   1540 O  OE1   . GLU B 1 42  ? 71.309  -1.406  9.416  1    23.83  ? 42  GLU B OE1   1 
ATOM   1541 O  OE2   . GLU B 1 42  ? 69.625  -0.09   9.945  1    24.78  ? 42  GLU B OE2   1 
ATOM   1542 N  N     . VAL B 1 43  ? 70.776  -1.295  15.192 1    13.77  ? 43  VAL B N     1 
ATOM   1543 C  CA    . VAL B 1 43  ? 69.666  -1.62   16.097 1    13.94  ? 43  VAL B CA    1 
ATOM   1544 C  C     . VAL B 1 43  ? 68.584  -0.547  16.02  1    14.65  ? 43  VAL B C     1 
ATOM   1545 O  O     . VAL B 1 43  ? 68.911  0.623   15.823 1    14.65  ? 43  VAL B O     1 
ATOM   1546 C  CB    . VAL B 1 43  ? 70.198  -1.713  17.546 1    13.82  ? 43  VAL B CB    1 
ATOM   1547 C  CG1   . VAL B 1 43  ? 69.116  -2.194  18.483 1    14.87  ? 43  VAL B CG1   1 
ATOM   1548 C  CG2   . VAL B 1 43  ? 71.42   -2.612  17.653 1    13.59  ? 43  VAL B CG2   1 
ATOM   1549 N  N     . ALA B 1 44  ? 67.311  -0.912  16.235 1    15.03  ? 44  ALA B N     1 
ATOM   1550 C  CA    . ALA B 1 44  ? 66.221  0.058   16.157 1    16.1   ? 44  ALA B CA    1 
ATOM   1551 C  C     . ALA B 1 44  ? 65.878  0.768   17.446 1    17.01  ? 44  ALA B C     1 
ATOM   1552 O  O     . ALA B 1 44  ? 65.975  0.2     18.522 1    17.8   ? 44  ALA B O     1 
ATOM   1553 C  CB    . ALA B 1 44  ? 64.983  -0.6    15.597 1    16.73  ? 44  ALA B CB    1 
ATOM   1554 N  N     . GLU B 1 45  ? 65.478  2.02    17.34  1    17.42  ? 45  GLU B N     1 
ATOM   1555 C  CA    . GLU B 1 45  ? 65.047  2.812   18.477 1    18.86  ? 45  GLU B CA    1 
ATOM   1556 C  C     . GLU B 1 45  ? 63.548  2.529   18.622 1    20.25  ? 45  GLU B C     1 
ATOM   1557 O  O     . GLU B 1 45  ? 62.739  2.986   17.814 1    20.11  ? 45  GLU B O     1 
ATOM   1558 C  CB    . GLU B 1 45  ? 65.306  4.305   18.233 1    21.15  ? 45  GLU B CB    1 
ATOM   1559 C  CG    . GLU B 1 45  ? 64.647  5.193   19.274 1    26.99  ? 45  GLU B CG    1 
ATOM   1560 C  CD    . GLU B 1 45  ? 64.883  6.677   19.104 1    33.76  ? 45  GLU B CD    1 
ATOM   1561 O  OE1   . GLU B 1 45  ? 65.759  7.055   18.293 1    33.53  ? 45  GLU B OE1   1 
ATOM   1562 O  OE2   . GLU B 1 45  ? 64.197  7.464   19.794 1    37.43  ? 45  GLU B OE2   1 
ATOM   1563 N  N     . LEU B 1 46  ? 63.183  1.731   19.632 1    21.28  ? 46  LEU B N     1 
ATOM   1564 C  CA    . LEU B 1 46  ? 61.79   1.317   19.804 1    22.13  ? 46  LEU B CA    1 
ATOM   1565 C  C     . LEU B 1 46  ? 61.153  1.786   21.091 1    22.98  ? 46  LEU B C     1 
ATOM   1566 O  O     . LEU B 1 46  ? 61.825  1.86    22.112 1    23.18  ? 46  LEU B O     1 
ATOM   1567 C  CB    . LEU B 1 46  ? 61.699  -0.219  19.75  1    21.77  ? 46  LEU B CB    1 
ATOM   1568 C  CG    . LEU B 1 46  ? 62.306  -0.89   18.547 1    21.67  ? 46  LEU B CG    1 
ATOM   1569 C  CD1   . LEU B 1 46  ? 62.353  -2.371  18.747 1    21.87  ? 46  LEU B CD1   1 
ATOM   1570 C  CD2   . LEU B 1 46  ? 61.578  -0.491  17.295 1    21.47  ? 46  LEU B CD2   1 
ATOM   1571 N  N     . VAL B 1 47  ? 59.841  2.061   21.032 1    23.53  ? 47  VAL B N     1 
ATOM   1572 C  CA    . VAL B 1 47  ? 58.981  2.418   22.162 1    24.58  ? 47  VAL B CA    1 
ATOM   1573 C  C     . VAL B 1 47  ? 58.771  1.125   22.958 1    25.51  ? 47  VAL B C     1 
ATOM   1574 O  O     . VAL B 1 47  ? 58.585  0.063   22.357 1    25.49  ? 47  VAL B O     1 
ATOM   1575 C  CB    . VAL B 1 47  ? 57.635  2.98    21.625 1    25.54  ? 47  VAL B CB    1 
ATOM   1576 C  CG1   . VAL B 1 47  ? 56.489  2.823   22.619 1    25.65  ? 47  VAL B CG1   1 
ATOM   1577 C  CG2   . VAL B 1 47  ? 57.781  4.43    21.179 1    26.48  ? 47  VAL B CG2   1 
ATOM   1578 N  N     . MET B 1 48  ? 58.82   1.2     24.291 1    26.08  ? 48  MET B N     1 
ATOM   1579 C  CA    . MET B 1 48  ? 58.641  0.01    25.102 1    27.66  ? 48  MET B CA    1 
ATOM   1580 C  C     . MET B 1 48  ? 57.349  0.008   25.942 1    29.58  ? 48  MET B C     1 
ATOM   1581 O  O     . MET B 1 48  ? 56.971  1.021   26.549 1    29.94  ? 48  MET B O     1 
ATOM   1582 C  CB    . MET B 1 48  ? 59.878  -0.24   25.967 1    28.41  ? 48  MET B CB    1 
ATOM   1583 C  CG    . MET B 1 48  ? 61.114  -0.559  25.155 1    30.77  ? 48  MET B CG    1 
ATOM   1584 S  SD    . MET B 1 48  ? 60.961  -2.028  24.099 1    35.64  ? 48  MET B SD    1 
ATOM   1585 C  CE    . MET B 1 48  ? 60.737  -3.228  25.289 1    31.3   ? 48  MET B CE    1 
ATOM   1586 N  N     . PRO B 1 49  ? 56.682  -1.165  26     1    30.48  ? 49  PRO B N     1 
ATOM   1587 C  CA    . PRO B 1 49  ? 55.441  -1.294  26.787 1    30.85  ? 49  PRO B CA    1 
ATOM   1588 C  C     . PRO B 1 49  ? 55.594  -0.974  28.263 1    31.87  ? 49  PRO B C     1 
ATOM   1589 O  O     . PRO B 1 49  ? 56.684  -0.999  28.815 1    32.43  ? 49  PRO B O     1 
ATOM   1590 C  CB    . PRO B 1 49  ? 55.065  -2.774  26.603 1    31     ? 49  PRO B CB    1 
ATOM   1591 C  CG    . PRO B 1 49  ? 56.326  -3.43   26.205 1    31.46  ? 49  PRO B CG    1 
ATOM   1592 C  CD    . PRO B 1 49  ? 57.016  -2.436  25.339 1    30.13  ? 49  PRO B CD    1 
ATOM   1593 N  N     . ARG B 1 50  ? 54.47   -0.685  28.9   1    31.95  ? 50  ARG B N     1 
ATOM   1594 C  CA    . ARG B 1 50  ? 54.377  -0.479  30.329 1    32.17  ? 50  ARG B CA    1 
ATOM   1595 C  C     . ARG B 1 50  ? 54.609  -1.858  30.987 1    31.95  ? 50  ARG B C     1 
ATOM   1596 O  O     . ARG B 1 50  ? 54.284  -2.883  30.392 1    31.61  ? 50  ARG B O     1 
ATOM   1597 C  CB    . ARG B 1 50  ? 52.969  0.031   30.64  1    34.09  ? 50  ARG B CB    1 
ATOM   1598 C  CG    . ARG B 1 50  ? 52.814  0.618   32.02  1    38.9   ? 50  ARG B CG    1 
ATOM   1599 C  CD    . ARG B 1 50  ? 51.68   1.62    32.035 1    42.94  ? 50  ARG B CD    1 
ATOM   1600 N  NE    . ARG B 1 50  ? 50.376  0.993   31.812 1    46.04  ? 50  ARG B NE    1 
ATOM   1601 C  CZ    . ARG B 1 50  ? 49.219  1.649   31.839 1    49.15  ? 50  ARG B CZ    1 
ATOM   1602 N  NH1   . ARG B 1 50  ? 49.192  2.958   32.067 1    48.71  ? 50  ARG B NH1   1 
ATOM   1603 N  NH2   . ARG B 1 50  ? 48.08   1.005   31.629 1    50.16  ? 50  ARG B NH2   1 
ATOM   1604 N  N     . VAL B 1 51  ? 55.198  -1.898  32.182 1    31.87  ? 51  VAL B N     1 
ATOM   1605 C  CA    . VAL B 1 51  ? 55.461  -3.166  32.862 1    32.45  ? 51  VAL B CA    1 
ATOM   1606 C  C     . VAL B 1 51  ? 54.44   -3.431  33.982 1    33.84  ? 51  VAL B C     1 
ATOM   1607 O  O     . VAL B 1 51  ? 54.192  -2.554  34.813 1    34.33  ? 51  VAL B O     1 
ATOM   1608 C  CB    . VAL B 1 51  ? 56.929  -3.242  33.36  1    32.33  ? 51  VAL B CB    1 
ATOM   1609 C  CG1   . VAL B 1 51  ? 57.201  -4.545  34.117 1    32.62  ? 51  VAL B CG1   1 
ATOM   1610 C  CG2   . VAL B 1 51  ? 57.9    -3.068  32.203 1    32.36  ? 51  VAL B CG2   1 
ATOM   1611 N  N     . VAL B 1 52  ? 53.835  -4.627  33.998 1    34.27  ? 52  VAL B N     1 
ATOM   1612 C  CA    . VAL B 1 52  ? 52.929  -4.997  35.079 1    35.28  ? 52  VAL B CA    1 
ATOM   1613 C  C     . VAL B 1 52  ? 53.77   -5.832  36.042 1    36.14  ? 52  VAL B C     1 
ATOM   1614 O  O     . VAL B 1 52  ? 54.21   -6.926  35.682 1    36.57  ? 52  VAL B O     1 
ATOM   1615 C  CB    . VAL B 1 52  ? 51.716  -5.801  34.592 1    36.05  ? 52  VAL B CB    1 
ATOM   1616 C  CG1   . VAL B 1 52  ? 50.733  -6.018  35.73  1    36.7   ? 52  VAL B CG1   1 
ATOM   1617 C  CG2   . VAL B 1 52  ? 51.046  -5.118  33.416 1    36.34  ? 52  VAL B CG2   1 
ATOM   1618 N  N     . LYS B 1 53  ? 54.049  -5.304  37.231 1    36.13  ? 53  LYS B N     1 
ATOM   1619 C  CA    . LYS B 1 53  ? 54.867  -6.011  38.213 1    36.92  ? 53  LYS B CA    1 
ATOM   1620 C  C     . LYS B 1 53  ? 54.115  -7.197  38.854 1    38.4   ? 53  LYS B C     1 
ATOM   1621 O  O     . LYS B 1 53  ? 52.896  -7.31   38.689 1    38.79  ? 53  LYS B O     1 
ATOM   1622 C  CB    . LYS B 1 53  ? 55.339  -5.025  39.287 1    37.61  ? 53  LYS B CB    1 
ATOM   1623 C  CG    . LYS B 1 53  ? 56.11   -3.851  38.719 1    38.26  ? 53  LYS B CG    1 
ATOM   1624 C  CD    . LYS B 1 53  ? 57.438  -3.724  39.397 1    39.27  ? 53  LYS B CD    1 
ATOM   1625 C  CE    . LYS B 1 53  ? 58.474  -4.433  38.598 1    40.53  ? 53  LYS B CE    1 
ATOM   1626 N  NZ    . LYS B 1 53  ? 59.819  -4.262  39.178 1    42.21  ? 53  LYS B NZ    1 
ATOM   1627 N  N     . SER B 1 54  ? 54.836  -8.07   39.594 1    39.02  ? 54  SER B N     1 
ATOM   1628 C  CA    . SER B 1 54  ? 54.27   -9.241  40.278 1    40.34  ? 54  SER B CA    1 
ATOM   1629 C  C     . SER B 1 54  ? 53.064  -8.885  41.131 1    41.83  ? 54  SER B C     1 
ATOM   1630 O  O     . SER B 1 54  ? 52.114  -9.66   41.209 1    42.07  ? 54  SER B O     1 
ATOM   1631 C  CB    . SER B 1 54  ? 55.315  -9.903  41.171 1    41.7   ? 54  SER B CB    1 
ATOM   1632 O  OG    . SER B 1 54  ? 56.428  -10.371 40.434 1    44.43  ? 54  SER B OG    1 
ATOM   1633 N  N     . ASN B 1 55  ? 53.104  -7.703  41.769 1    42.74  ? 55  ASN B N     1 
ATOM   1634 C  CA    . ASN B 1 55  ? 52.029  -7.214  42.623 1    43.82  ? 55  ASN B CA    1 
ATOM   1635 C  C     . ASN B 1 55  ? 51.016  -6.343  41.874 1    44.56  ? 55  ASN B C     1 
ATOM   1636 O  O     . ASN B 1 55  ? 50.39   -5.492  42.482 1    45.09  ? 55  ASN B O     1 
ATOM   1637 C  CB    . ASN B 1 55  ? 52.599  -6.471  43.835 1    45.32  ? 55  ASN B CB    1 
ATOM   1638 C  CG    . ASN B 1 55  ? 53.436  -5.255  43.504 1    49.22  ? 55  ASN B CG    1 
ATOM   1639 O  OD1   . ASN B 1 55  ? 53.848  -5.026  42.358 1    50.73  ? 55  ASN B OD1   1 
ATOM   1640 N  ND2   . ASN B 1 55  ? 53.701  -4.44   44.513 1    50.18  ? 55  ASN B ND2   1 
ATOM   1641 N  N     . ASP B 1 56  ? 50.885  -6.534  40.563 1    44.69  ? 56  ASP B N     1 
ATOM   1642 C  CA    . ASP B 1 56  ? 49.962  -5.846  39.666 1    45.44  ? 56  ASP B CA    1 
ATOM   1643 C  C     . ASP B 1 56  ? 50.147  -4.321  39.598 1    45.3   ? 56  ASP B C     1 
ATOM   1644 O  O     . ASP B 1 56  ? 49.305  -3.628  39.029 1    45.34  ? 56  ASP B O     1 
ATOM   1645 C  CB    . ASP B 1 56  ? 48.518  -6.23   39.983 1    47.79  ? 56  ASP B CB    1 
ATOM   1646 C  CG    . ASP B 1 56  ? 48.345  -7.732  39.876 1    54.13  ? 56  ASP B CG    1 
ATOM   1647 O  OD1   . ASP B 1 56  ? 48.549  -8.278  38.76  1    55.34  ? 56  ASP B OD1   1 
ATOM   1648 O  OD2   . ASP B 1 56  ? 48.072  -8.372  40.916 1    57.07  ? 56  ASP B OD2   1 
ATOM   1649 N  N     . VAL B 1 57  ? 51.275  -3.811  40.109 1    44.81  ? 57  VAL B N     1 
ATOM   1650 C  CA    . VAL B 1 57  ? 51.579  -2.388  40.024 1    44.64  ? 57  VAL B CA    1 
ATOM   1651 C  C     . VAL B 1 57  ? 52.11   -2.115  38.618 1    43.82  ? 57  VAL B C     1 
ATOM   1652 O  O     . VAL B 1 57  ? 53.008  -2.82   38.164 1    43.97  ? 57  VAL B O     1 
ATOM   1653 C  CB    . VAL B 1 57  ? 52.612  -1.973  41.096 1    45.36  ? 57  VAL B CB    1 
ATOM   1654 C  CG1   . VAL B 1 57  ? 53.197  -0.589  40.81  1    45.91  ? 57  VAL B CG1   1 
ATOM   1655 C  CG2   . VAL B 1 57  ? 52      -2.029  42.485 1    45.82  ? 57  VAL B CG2   1 
ATOM   1656 N  N     . ARG B 1 58  ? 51.557  -1.111  37.928 1    42.58  ? 58  ARG B N     1 
ATOM   1657 C  CA    . ARG B 1 58  ? 52.045  -0.762  36.598 1    41.71  ? 58  ARG B CA    1 
ATOM   1658 C  C     . ARG B 1 58  ? 53.165  0.269   36.75  1    40.67  ? 58  ARG B C     1 
ATOM   1659 O  O     . ARG B 1 58  ? 53.044  1.199   37.547 1    41.23  ? 58  ARG B O     1 
ATOM   1660 C  CB    . ARG B 1 58  ? 50.911  -0.226  35.704 1    42.87  ? 58  ARG B CB    1 
ATOM   1661 C  CG    . ARG B 1 58  ? 50.157  -1.301  34.928 1    45.8   ? 58  ARG B CG    1 
ATOM   1662 C  CD    . ARG B 1 58  ? 49.266  -2.151  35.816 1    49.03  ? 58  ARG B CD    1 
ATOM   1663 N  NE    . ARG B 1 58  ? 48.383  -3.007  35.029 1    52.49  ? 58  ARG B NE    1 
ATOM   1664 C  CZ    . ARG B 1 58  ? 47.687  -4.027  35.52  1    54.7   ? 58  ARG B CZ    1 
ATOM   1665 N  NH1   . ARG B 1 58  ? 47.776  -4.343  36.805 1    53.39  ? 58  ARG B NH1   1 
ATOM   1666 N  NH2   . ARG B 1 58  ? 46.911  -4.752  34.725 1    55.47  ? 58  ARG B NH2   1 
ATOM   1667 N  N     . GLU B 1 59  ? 54.276  0.074   36.043 1    39.16  ? 59  GLU B N     1 
ATOM   1668 C  CA    . GLU B 1 59  ? 55.395  1.014   36.091 1    38.3   ? 59  GLU B CA    1 
ATOM   1669 C  C     . GLU B 1 59  ? 56.062  1.108   34.716 1    37.11  ? 59  GLU B C     1 
ATOM   1670 O  O     . GLU B 1 59  ? 55.864  0.21    33.897 1    37.85  ? 59  GLU B O     1 
ATOM   1671 C  CB    . GLU B 1 59  ? 56.393  0.642   37.201 1    40.31  ? 59  GLU B CB    1 
ATOM   1672 C  CG    . GLU B 1 59  ? 57.147  -0.643  36.956 1    44.45  ? 59  GLU B CG    1 
ATOM   1673 C  CD    . GLU B 1 59  ? 58.364  -0.815  37.843 1    50.1   ? 59  GLU B CD    1 
ATOM   1674 O  OE1   . GLU B 1 59  ? 58.434  -0.167  38.911 1    50.5   ? 59  GLU B OE1   1 
ATOM   1675 O  OE2   . GLU B 1 59  ? 59.253  -1.613  37.473 1    53.16  ? 59  GLU B OE2   1 
ATOM   1676 N  N     . PRO B 1 60  ? 56.792  2.194   34.38  1    35.01  ? 60  PRO B N     1 
ATOM   1677 C  CA    . PRO B 1 60  ? 57.389  2.275   33.034 1    33.14  ? 60  PRO B CA    1 
ATOM   1678 C  C     . PRO B 1 60  ? 58.497  1.259   32.815 1    30.78  ? 60  PRO B C     1 
ATOM   1679 O  O     . PRO B 1 60  ? 59.088  0.768   33.78  1    31.03  ? 60  PRO B O     1 
ATOM   1680 C  CB    . PRO B 1 60  ? 57.944  3.696   32.985 1    34.37  ? 60  PRO B CB    1 
ATOM   1681 C  CG    . PRO B 1 60  ? 58.236  4.025   34.404 1    35.3   ? 60  PRO B CG    1 
ATOM   1682 C  CD    . PRO B 1 60  ? 57.118  3.389   35.179 1    34.16  ? 60  PRO B CD    1 
ATOM   1683 N  N     . PHE B 1 61  ? 58.795  0.949   31.54  1    28.67  ? 61  PHE B N     1 
ATOM   1684 C  CA    . PHE B 1 61  ? 59.862  0.005   31.235 1    26.58  ? 61  PHE B CA    1 
ATOM   1685 C  C     . PHE B 1 61  ? 61.181  0.661   31.593 1    26.22  ? 61  PHE B C     1 
ATOM   1686 O  O     . PHE B 1 61  ? 61.459  1.752   31.105 1    26.91  ? 61  PHE B O     1 
ATOM   1687 C  CB    . PHE B 1 61  ? 59.848  -0.388  29.769 1    24.83  ? 61  PHE B CB    1 
ATOM   1688 C  CG    . PHE B 1 61  ? 60.961  -1.329  29.375 1    23.7   ? 61  PHE B CG    1 
ATOM   1689 C  CD1   . PHE B 1 61  ? 60.856  -2.684  29.606 1    23.83  ? 61  PHE B CD1   1 
ATOM   1690 C  CD2   . PHE B 1 61  ? 62.093  -0.861  28.741 1    23.59  ? 61  PHE B CD2   1 
ATOM   1691 C  CE1   . PHE B 1 61  ? 61.878  -3.547  29.237 1    23.96  ? 61  PHE B CE1   1 
ATOM   1692 C  CE2   . PHE B 1 61  ? 63.111  -1.725  28.374 1    23.74  ? 61  PHE B CE2   1 
ATOM   1693 C  CZ    . PHE B 1 61  ? 62.999  -3.062  28.619 1    23.44  ? 61  PHE B CZ    1 
ATOM   1694 N  N     . ASN B 1 62  ? 61.941  0.056   32.514 1    24.85  ? 62  ASN B N     1 
ATOM   1695 C  CA    . ASN B 1 62  ? 63.223  0.601   32.918 1    24.26  ? 62  ASN B CA    1 
ATOM   1696 C  C     . ASN B 1 62  ? 64.326  -0.304  32.419 1    23.3   ? 62  ASN B C     1 
ATOM   1697 O  O     . ASN B 1 62  ? 64.563  -1.359  32.992 1    23.34  ? 62  ASN B O     1 
ATOM   1698 C  CB    . ASN B 1 62  ? 63.304  0.721   34.418 1    26.16  ? 62  ASN B CB    1 
ATOM   1699 C  CG    . ASN B 1 62  ? 64.464  1.558   34.898 1    29.8   ? 62  ASN B CG    1 
ATOM   1700 O  OD1   . ASN B 1 62  ? 65.55   1.563   34.309 1    31.68  ? 62  ASN B OD1   1 
ATOM   1701 N  ND2   . ASN B 1 62  ? 64.253  2.287   35.98  1    29.65  ? 62  ASN B ND2   1 
ATOM   1702 N  N     . GLU B 1 63  ? 65.043  0.136   31.379 1    22.21  ? 63  GLU B N     1 
ATOM   1703 C  CA    . GLU B 1 63  ? 66.136  -0.609  30.791 1    21.31  ? 63  GLU B CA    1 
ATOM   1704 C  C     . GLU B 1 63  ? 67.223  -0.927  31.823 1    20     ? 63  GLU B C     1 
ATOM   1705 O  O     . GLU B 1 63  ? 67.834  -1.989  31.745 1    20.46  ? 63  GLU B O     1 
ATOM   1706 C  CB    . GLU B 1 63  ? 66.713  0.208   29.643 1    23.71  ? 63  GLU B CB    1 
ATOM   1707 C  CG    . GLU B 1 63  ? 67.54   -0.594  28.659 1    29.08  ? 63  GLU B CG    1 
ATOM   1708 C  CD    . GLU B 1 63  ? 68.155  0.259   27.569 1    34.2   ? 63  GLU B CD    1 
ATOM   1709 O  OE1   . GLU B 1 63  ? 67.517  0.416   26.501 1    36.81  ? 63  GLU B OE1   1 
ATOM   1710 O  OE2   . GLU B 1 63  ? 69.267  0.789   27.794 1    34.25  ? 63  GLU B OE2   1 
ATOM   1711 N  N     . GLU B 1 64  ? 67.455  -0.031  32.797 1    17.92  ? 64  GLU B N     1 
ATOM   1712 C  CA    . GLU B 1 64  ? 68.502  -0.226  33.771 1    17.48  ? 64  GLU B CA    1 
ATOM   1713 C  C     . GLU B 1 64  ? 68.11   -1.263  34.844 1    18.61  ? 64  GLU B C     1 
ATOM   1714 O  O     . GLU B 1 64  ? 68.971  -1.994  35.337 1    18.96  ? 64  GLU B O     1 
ATOM   1715 C  CB    . GLU B 1 64  ? 68.929  1.123   34.35  1    18.14  ? 64  GLU B CB    1 
ATOM   1716 C  CG    . GLU B 1 64  ? 70.117  1.077   35.286 1    19.16  ? 64  GLU B CG    1 
ATOM   1717 C  CD    . GLU B 1 64  ? 71.383  0.491   34.696 1    23.77  ? 64  GLU B CD    1 
ATOM   1718 O  OE1   . GLU B 1 64  ? 71.526  0.488   33.45  1    24.78  ? 64  GLU B OE1   1 
ATOM   1719 O  OE2   . GLU B 1 64  ? 72.239  0.035   35.488 1    24.49  ? 64  GLU B OE2   1 
ATOM   1720 N  N     . LYS B 1 65  ? 66.798  -1.404  35.146 1    18.19  ? 65  LYS B N     1 
ATOM   1721 C  CA    . LYS B 1 65  ? 66.33   -2.47   36.024 1    17.89  ? 65  LYS B CA    1 
ATOM   1722 C  C     . LYS B 1 65  ? 66.624  -3.819  35.34  1    18.8   ? 65  LYS B C     1 
ATOM   1723 O  O     . LYS B 1 65  ? 67.128  -4.73   35.982 1    20.43  ? 65  LYS B O     1 
ATOM   1724 C  CB    . LYS B 1 65  ? 64.822  -2.363  36.27  1    18.42  ? 65  LYS B CB    1 
ATOM   1725 C  CG    . LYS B 1 65  ? 64.417  -1.344  37.296 1    19.59  ? 65  LYS B CG    1 
ATOM   1726 C  CD    . LYS B 1 65  ? 62.998  -1.585  37.747 1    21.1   ? 65  LYS B CD    1 
ATOM   1727 C  CE    . LYS B 1 65  ? 62.592  -0.54   38.757 1    24.29  ? 65  LYS B CE    1 
ATOM   1728 N  NZ    . LYS B 1 65  ? 61.479  -0.988  39.632 1    25.06  ? 65  LYS B NZ    1 
ATOM   1729 N  N     . LEU B 1 66  ? 66.358  -3.916  34.04  1    17.99  ? 66  LEU B N     1 
ATOM   1730 C  CA    . LEU B 1 66  ? 66.62   -5.09   33.225 1    18.25  ? 66  LEU B CA    1 
ATOM   1731 C  C     . LEU B 1 66  ? 68.129  -5.408  33.186 1    19.16  ? 66  LEU B C     1 
ATOM   1732 O  O     . LEU B 1 66  ? 68.522  -6.551  33.423 1    19.44  ? 66  LEU B O     1 
ATOM   1733 C  CB    . LEU B 1 66  ? 66.074  -4.845  31.797 1    17.36  ? 66  LEU B CB    1 
ATOM   1734 C  CG    . LEU B 1 66  ? 66.409  -5.884  30.761 1    17.76  ? 66  LEU B CG    1 
ATOM   1735 C  CD1   . LEU B 1 66  ? 65.778  -7.151  31.083 1    17.79  ? 66  LEU B CD1   1 
ATOM   1736 C  CD2   . LEU B 1 66  ? 65.924  -5.461  29.38  1    18.4   ? 66  LEU B CD2   1 
ATOM   1737 N  N     . ARG B 1 67  ? 68.958  -4.396  32.9   1    19.22  ? 67  ARG B N     1 
ATOM   1738 C  CA    . ARG B 1 67  ? 70.4    -4.522  32.783 1    19.79  ? 67  ARG B CA    1 
ATOM   1739 C  C     . ARG B 1 67  ? 71.067  -4.952  34.082 1    21.17  ? 67  ARG B C     1 
ATOM   1740 O  O     . ARG B 1 67  ? 71.869  -5.887  34.054 1    21.64  ? 67  ARG B O     1 
ATOM   1741 C  CB    . ARG B 1 67  ? 70.984  -3.206  32.271 1    20.42  ? 67  ARG B CB    1 
ATOM   1742 C  CG    . ARG B 1 67  ? 72.504  -3.166  32.174 1    22.91  ? 67  ARG B CG    1 
ATOM   1743 C  CD    . ARG B 1 67  ? 72.974  -2.251  31.059 1    26.58  ? 67  ARG B CD    1 
ATOM   1744 N  NE    . ARG B 1 67  ? 72.266  -0.967  31.064 1    29.13  ? 67  ARG B NE    1 
ATOM   1745 C  CZ    . ARG B 1 67  ? 71.638  -0.448  30.015 1    29.55  ? 67  ARG B CZ    1 
ATOM   1746 N  NH1   . ARG B 1 67  ? 71.663  -1.071  28.841 1    28.85  ? 67  ARG B NH1   1 
ATOM   1747 N  NH2   . ARG B 1 67  ? 70.999  0.712   30.124 1    28.74  ? 67  ARG B NH2   1 
ATOM   1748 N  N     . SER B 1 68  ? 70.735  -4.284  35.215 1    21.33  ? 68  SER B N     1 
ATOM   1749 C  CA    . SER B 1 68  ? 71.301  -4.568  36.536 1    22.08  ? 68  SER B CA    1 
ATOM   1750 C  C     . SER B 1 68  ? 71.1    -5.997  36.976 1    20.97  ? 68  SER B C     1 
ATOM   1751 O  O     . SER B 1 68  ? 71.999  -6.573  37.579 1    21.76  ? 68  SER B O     1 
ATOM   1752 C  CB    . SER B 1 68  ? 70.712  -3.652  37.604 1    25.39  ? 68  SER B CB    1 
ATOM   1753 O  OG    . SER B 1 68  ? 70.728  -2.304  37.17  1    30.2   ? 68  SER B OG    1 
ATOM   1754 N  N     . GLY B 1 69  ? 69.93   -6.553  36.702 1    19.23  ? 69  GLY B N     1 
ATOM   1755 C  CA    . GLY B 1 69  ? 69.633  -7.927  37.067 1    18.79  ? 69  GLY B CA    1 
ATOM   1756 C  C     . GLY B 1 69  ? 70.533  -8.91   36.357 1    18.51  ? 69  GLY B C     1 
ATOM   1757 O  O     . GLY B 1 69  ? 70.999  -9.886  36.954 1    18.71  ? 69  GLY B O     1 
ATOM   1758 N  N     . MET B 1 70  ? 70.818  -8.622  35.083 1    17.84  ? 70  MET B N     1 
ATOM   1759 C  CA    . MET B 1 70  ? 71.692  -9.432  34.266 1    17.3   ? 70  MET B CA    1 
ATOM   1760 C  C     . MET B 1 70  ? 73.112  -9.249  34.76  1    16.37  ? 70  MET B C     1 
ATOM   1761 O  O     . MET B 1 70  ? 73.782  -10.237 34.992 1    16.55  ? 70  MET B O     1 
ATOM   1762 C  CB    . MET B 1 70  ? 71.583  -9.04   32.773 1    18.11  ? 70  MET B CB    1 
ATOM   1763 C  CG    . MET B 1 70  ? 70.185  -9.191  32.196 1    20.13  ? 70  MET B CG    1 
ATOM   1764 S  SD    . MET B 1 70  ? 70.061  -8.804  30.427 1    22.67  ? 70  MET B SD    1 
ATOM   1765 C  CE    . MET B 1 70  ? 71.019  -10.094 29.742 1    22.26  ? 70  MET B CE    1 
ATOM   1766 N  N     . LEU B 1 71  ? 73.56   -8.005  34.982 1    15.48  ? 71  LEU B N     1 
ATOM   1767 C  CA    . LEU B 1 71  ? 74.929  -7.732  35.413 1    15.45  ? 71  LEU B CA    1 
ATOM   1768 C  C     . LEU B 1 71  ? 75.296  -8.362  36.75  1    16.67  ? 71  LEU B C     1 
ATOM   1769 O  O     . LEU B 1 71  ? 76.451  -8.743  36.951 1    16.29  ? 71  LEU B O     1 
ATOM   1770 C  CB    . LEU B 1 71  ? 75.223  -6.234  35.408 1    14.88  ? 71  LEU B CB    1 
ATOM   1771 C  CG    . LEU B 1 71  ? 75.346  -5.58   34.012 1    15.4   ? 71  LEU B CG    1 
ATOM   1772 C  CD1   . LEU B 1 71  ? 75.624  -4.123  34.138 1    16.17  ? 71  LEU B CD1   1 
ATOM   1773 C  CD2   . LEU B 1 71  ? 76.452  -6.183  33.215 1    15.22  ? 71  LEU B CD2   1 
ATOM   1774 N  N     . ARG B 1 72  ? 74.312  -8.49   37.653 1    17.85  ? 72  ARG B N     1 
ATOM   1775 C  CA    . ARG B 1 72  ? 74.471  -9.123  38.95  1    18.82  ? 72  ARG B CA    1 
ATOM   1776 C  C     . ARG B 1 72  ? 74.743  -10.601 38.75  1    19.81  ? 72  ARG B C     1 
ATOM   1777 O  O     . ARG B 1 72  ? 75.673  -11.128 39.339 1    20.21  ? 72  ARG B O     1 
ATOM   1778 C  CB    . ARG B 1 72  ? 73.192  -8.948  39.778 1    20.64  ? 72  ARG B CB    1 
ATOM   1779 C  CG    . ARG B 1 72  ? 73.335  -7.933  40.877 1    24.22  ? 72  ARG B CG    1 
ATOM   1780 C  CD    . ARG B 1 72  ? 72.134  -7.029  40.957 1    27.65  ? 72  ARG B CD    1 
ATOM   1781 N  NE    . ARG B 1 72  ? 71.156  -7.508  41.94  1    30.22  ? 72  ARG B NE    1 
ATOM   1782 C  CZ    . ARG B 1 72  ? 70.847  -6.879  43.065 1    30.54  ? 72  ARG B CZ    1 
ATOM   1783 N  NH1   . ARG B 1 72  ? 71.453  -5.745  43.387 1    30.86  ? 72  ARG B NH1   1 
ATOM   1784 N  NH2   . ARG B 1 72  ? 69.914  -7.367  43.865 1    29.05  ? 72  ARG B NH2   1 
ATOM   1785 N  N     . ALA B 1 73  ? 73.943  -11.263 37.908 1    20.4   ? 73  ALA B N     1 
ATOM   1786 C  CA    . ALA B 1 73  ? 74.088  -12.678 37.601 1    21.7   ? 73  ALA B CA    1 
ATOM   1787 C  C     . ALA B 1 73  ? 75.366  -12.956 36.811 1    23.17  ? 73  ALA B C     1 
ATOM   1788 O  O     . ALA B 1 73  ? 75.929  -14.026 36.952 1    23.46  ? 73  ALA B O     1 
ATOM   1789 C  CB    . ALA B 1 73  ? 72.875  -13.162 36.812 1    21.86  ? 73  ALA B CB    1 
ATOM   1790 N  N     . LEU B 1 74  ? 75.834  -11.99  35.995 1    24.16  ? 74  LEU B N     1 
ATOM   1791 C  CA    . LEU B 1 74  ? 77.038  -12.1   35.153 1    25.33  ? 74  LEU B CA    1 
ATOM   1792 C  C     . LEU B 1 74  ? 78.295  -11.538 35.853 1    26.51  ? 74  LEU B C     1 
ATOM   1793 O  O     . LEU B 1 74  ? 79.169  -10.975 35.184 1    27.21  ? 74  LEU B O     1 
ATOM   1794 C  CB    . LEU B 1 74  ? 76.826  -11.368 33.809 1    25.2   ? 74  LEU B CB    1 
ATOM   1795 C  CG    . LEU B 1 74  ? 75.748  -11.911 32.889 1    26.74  ? 74  LEU B CG    1 
ATOM   1796 C  CD1   . LEU B 1 74  ? 75.291  -10.86  31.925 1    27.21  ? 74  LEU B CD1   1 
ATOM   1797 C  CD2   . LEU B 1 74  ? 76.246  -13.074 32.102 1    27.75  ? 74  LEU B CD2   1 
ATOM   1798 N  N     . GLU B 1 75  ? 78.386  -11.679 37.184 1    26.27  ? 75  GLU B N     1 
ATOM   1799 C  CA    . GLU B 1 75  ? 79.558  -11.21  37.92  1    26.65  ? 75  GLU B CA    1 
ATOM   1800 C  C     . GLU B 1 75  ? 80.678  -12.226 37.746 1    27.29  ? 75  GLU B C     1 
ATOM   1801 O  O     . GLU B 1 75  ? 80.432  -13.419 37.917 1    27.16  ? 75  GLU B O     1 
ATOM   1802 C  CB    . GLU B 1 75  ? 79.225  -11.032 39.406 1    27.69  ? 75  GLU B CB    1 
ATOM   1803 C  CG    . GLU B 1 75  ? 78.665  -9.665  39.736 1    31.07  ? 75  GLU B CG    1 
ATOM   1804 C  CD    . GLU B 1 75  ? 79.708  -8.569  39.711 1    36.62  ? 75  GLU B CD    1 
ATOM   1805 O  OE1   . GLU B 1 75  ? 79.361  -7.427  39.334 1    37.36  ? 75  GLU B OE1   1 
ATOM   1806 O  OE2   . GLU B 1 75  ? 80.875  -8.851  40.069 1    39.23  ? 75  GLU B OE2   1 
ATOM   1807 N  N     . LYS B 1 76  ? 81.888  -11.754 37.352 1    27.65  ? 76  LYS B N     1 
ATOM   1808 C  CA    . LYS B 1 76  ? 83.094  -12.559 37.096 1    28.46  ? 76  LYS B CA    1 
ATOM   1809 C  C     . LYS B 1 76  ? 82.945  -13.583 35.927 1    29.27  ? 76  LYS B C     1 
ATOM   1810 O  O     . LYS B 1 76  ? 83.758  -14.506 35.799 1    29.82  ? 76  LYS B O     1 
ATOM   1811 C  CB    . LYS B 1 76  ? 83.591  -13.259 38.369 1    30.14  ? 76  LYS B CB    1 
ATOM   1812 C  CG    . LYS B 1 76  ? 84.068  -12.336 39.481 1    34.27  ? 76  LYS B CG    1 
ATOM   1813 C  CD    . LYS B 1 76  ? 84.569  -13.174 40.686 1    38.02  ? 76  LYS B CD    1 
ATOM   1814 C  CE    . LYS B 1 76  ? 85.087  -12.368 41.85  1    41.17  ? 76  LYS B CE    1 
ATOM   1815 N  NZ    . LYS B 1 76  ? 85.616  -13.258 42.919 1    42.41  ? 76  LYS B NZ    1 
ATOM   1816 N  N     . ARG B 1 77  ? 81.929  -13.388 35.057 1    28.69  ? 77  ARG B N     1 
ATOM   1817 C  CA    . ARG B 1 77  ? 81.627  -14.263 33.936 1    28.04  ? 77  ARG B CA    1 
ATOM   1818 C  C     . ARG B 1 77  ? 82.165  -13.69  32.615 1    27.86  ? 77  ARG B C     1 
ATOM   1819 O  O     . ARG B 1 77  ? 82.221  -12.463 32.44  1    28.22  ? 77  ARG B O     1 
ATOM   1820 C  CB    . ARG B 1 77  ? 80.111  -14.571 33.881 1    28.99  ? 77  ARG B CB    1 
ATOM   1821 C  CG    . ARG B 1 77  ? 79.554  -15.316 35.107 1    32.02  ? 77  ARG B CG    1 
ATOM   1822 C  CD    . ARG B 1 77  ? 80.411  -16.49  35.566 1    36.47  ? 77  ARG B CD    1 
ATOM   1823 N  NE    . ARG B 1 77  ? 80.507  -17.536 34.55  1    42.18  ? 77  ARG B NE    1 
ATOM   1824 C  CZ    . ARG B 1 77  ? 81.567  -18.32  34.363 1    46.03  ? 77  ARG B CZ    1 
ATOM   1825 N  NH1   . ARG B 1 77  ? 81.551  -19.254 33.421 1    45.4   ? 77  ARG B NH1   1 
ATOM   1826 N  NH2   . ARG B 1 77  ? 82.653  -18.17  35.113 1    47.13  ? 77  ARG B NH2   1 
ATOM   1827 N  N     . PRO B 1 78  ? 82.658  -14.569 31.71  1    26.43  ? 78  PRO B N     1 
ATOM   1828 C  CA    . PRO B 1 78  ? 83.266  -14.075 30.48  1    25.8   ? 78  PRO B CA    1 
ATOM   1829 C  C     . PRO B 1 78  ? 82.266  -13.672 29.402 1    25.51  ? 78  PRO B C     1 
ATOM   1830 O  O     . PRO B 1 78  ? 82.171  -14.298 28.342 1    25.48  ? 78  PRO B O     1 
ATOM   1831 C  CB    . PRO B 1 78  ? 84.165  -15.225 30.052 1    26.6   ? 78  PRO B CB    1 
ATOM   1832 C  CG    . PRO B 1 78  ? 83.508  -16.427 30.581 1    27.16  ? 78  PRO B CG    1 
ATOM   1833 C  CD    . PRO B 1 78  ? 82.721  -16.041 31.792 1    25.7   ? 78  PRO B CD    1 
ATOM   1834 N  N     . VAL B 1 79  ? 81.507  -12.616 29.697 1    24.56  ? 79  VAL B N     1 
ATOM   1835 C  CA    . VAL B 1 79  ? 80.495  -12.042 28.84  1    23.64  ? 79  VAL B CA    1 
ATOM   1836 C  C     . VAL B 1 79  ? 80.864  -10.567 28.733 1    24.13  ? 79  VAL B C     1 
ATOM   1837 O  O     . VAL B 1 79  ? 80.932  -9.886  29.743 1    24.11  ? 79  VAL B O     1 
ATOM   1838 C  CB    . VAL B 1 79  ? 79.113  -12.253 29.479 1    23.22  ? 79  VAL B CB    1 
ATOM   1839 C  CG1   . VAL B 1 79  ? 78.034  -11.519 28.717 1    23.38  ? 79  VAL B CG1   1 
ATOM   1840 C  CG2   . VAL B 1 79  ? 78.784  -13.731 29.592 1    23.37  ? 79  VAL B CG2   1 
ATOM   1841 N  N     . SER B 1 80  ? 81.195  -10.093 27.525 1    24.64  ? 80  SER B N     1 
ATOM   1842 C  CA    . SER B 1 80  ? 81.593  -8.702  27.332 1    24.85  ? 80  SER B CA    1 
ATOM   1843 C  C     . SER B 1 80  ? 80.403  -7.756  27.463 1    24.55  ? 80  SER B C     1 
ATOM   1844 O  O     . SER B 1 80  ? 79.253  -8.198  27.429 1    24.18  ? 80  SER B O     1 
ATOM   1845 C  CB    . SER B 1 80  ? 82.32   -8.523  25.999 1    26.1   ? 80  SER B CB    1 
ATOM   1846 O  OG    . SER B 1 80  ? 81.441  -8.543  24.884 1    29.25  ? 80  SER B OG    1 
ATOM   1847 N  N     . SER B 1 81  ? 80.674  -6.456  27.643 1    24.51  ? 81  SER B N     1 
ATOM   1848 C  CA    . SER B 1 81  ? 79.618  -5.447  27.717 1    24.78  ? 81  SER B CA    1 
ATOM   1849 C  C     . SER B 1 81  ? 78.779  -5.393  26.42  1    23.65  ? 81  SER B C     1 
ATOM   1850 O  O     . SER B 1 81  ? 77.61   -5.038  26.454 1    23.29  ? 81  SER B O     1 
ATOM   1851 C  CB    . SER B 1 81  ? 80.189  -4.073  28.067 1    27.45  ? 81  SER B CB    1 
ATOM   1852 O  OG    . SER B 1 81  ? 81.415  -3.758  27.423 1    31.37  ? 81  SER B OG    1 
ATOM   1853 N  N     . ASP B 1 82  ? 79.375  -5.772  25.292 1    23.06  ? 82  ASP B N     1 
ATOM   1854 C  CA    . ASP B 1 82  ? 78.718  -5.832  24.007 1    22.54  ? 82  ASP B CA    1 
ATOM   1855 C  C     . ASP B 1 82  ? 77.71   -6.979  23.981 1    20.87  ? 82  ASP B C     1 
ATOM   1856 O  O     . ASP B 1 82  ? 76.585  -6.781  23.528 1    20.76  ? 82  ASP B O     1 
ATOM   1857 C  CB    . ASP B 1 82  ? 79.773  -5.985  22.917 1    25.72  ? 82  ASP B CB    1 
ATOM   1858 C  CG    . ASP B 1 82  ? 80.628  -4.735  22.786 1    32.87  ? 82  ASP B CG    1 
ATOM   1859 O  OD1   . ASP B 1 82  ? 80.073  -3.669  22.404 1    34.03  ? 82  ASP B OD1   1 
ATOM   1860 O  OD2   . ASP B 1 82  ? 81.848  -4.816  23.073 1    35.99  ? 82  ASP B OD2   1 
ATOM   1861 N  N     . ASP B 1 83  ? 78.091  -8.156  24.503 1    19.58  ? 83  ASP B N     1 
ATOM   1862 C  CA    . ASP B 1 83  ? 77.217  -9.322  24.596 1    19.38  ? 83  ASP B CA    1 
ATOM   1863 C  C     . ASP B 1 83  ? 75.963  -9.004  25.398 1    19.12  ? 83  ASP B C     1 
ATOM   1864 O  O     . ASP B 1 83  ? 74.881  -9.476  25.055 1    19.06  ? 83  ASP B O     1 
ATOM   1865 C  CB    . ASP B 1 83  ? 77.946  -10.469 25.303 1    21.39  ? 83  ASP B CB    1 
ATOM   1866 C  CG    . ASP B 1 83  ? 79.096  -11.028 24.518 1    27.24  ? 83  ASP B CG    1 
ATOM   1867 O  OD1   . ASP B 1 83  ? 78.984  -11.1   23.271 1    29.02  ? 83  ASP B OD1   1 
ATOM   1868 O  OD2   . ASP B 1 83  ? 80.105  -11.414 25.143 1    28.56  ? 83  ASP B OD2   1 
ATOM   1869 N  N     . VAL B 1 84  ? 76.118  -8.225  26.488 1    18.67  ? 84  VAL B N     1 
ATOM   1870 C  CA    . VAL B 1 84  ? 75.02   -7.836  27.358 1    18.46  ? 84  VAL B CA    1 
ATOM   1871 C  C     . VAL B 1 84  ? 74.101  -6.908  26.587 1    18.29  ? 84  VAL B C     1 
ATOM   1872 O  O     . VAL B 1 84  ? 72.901  -7.163  26.552 1    18.92  ? 84  VAL B O     1 
ATOM   1873 C  CB    . VAL B 1 84  ? 75.519  -7.193  28.681 1    19.08  ? 84  VAL B CB    1 
ATOM   1874 C  CG1   . VAL B 1 84  ? 74.382  -6.552  29.456 1    19.71  ? 84  VAL B CG1   1 
ATOM   1875 C  CG2   . VAL B 1 84  ? 76.234  -8.209  29.555 1    19.51  ? 84  VAL B CG2   1 
ATOM   1876 N  N     . GLU B 1 85  ? 74.657  -5.868  25.914 1    16.95  ? 85  GLU B N     1 
ATOM   1877 C  CA    . GLU B 1 85  ? 73.838  -4.909  25.178 1    15.96  ? 85  GLU B CA    1 
ATOM   1878 C  C     . GLU B 1 85  ? 73.1    -5.51   24.036 1    15.23  ? 85  GLU B C     1 
ATOM   1879 O  O     . GLU B 1 85  ? 71.948  -5.149  23.821 1    15.04  ? 85  GLU B O     1 
ATOM   1880 C  CB    . GLU B 1 85  ? 74.645  -3.709  24.734 1    17.69  ? 85  GLU B CB    1 
ATOM   1881 C  CG    . GLU B 1 85  ? 75.271  -2.946  25.88  1    20.59  ? 85  GLU B CG    1 
ATOM   1882 C  CD    . GLU B 1 85  ? 74.346  -2.579  27.018 1    26.82  ? 85  GLU B CD    1 
ATOM   1883 O  OE1   . GLU B 1 85  ? 73.199  -2.162  26.742 1    28.33  ? 85  GLU B OE1   1 
ATOM   1884 O  OE2   . GLU B 1 85  ? 74.769  -2.712  28.189 1    30.02  ? 85  GLU B OE2   1 
ATOM   1885 N  N     . MET B 1 86  ? 73.722  -6.462  23.341 1    14.91  ? 86  MET B N     1 
ATOM   1886 C  CA    . MET B 1 86  ? 73.044  -7.186  22.293 1    15.4   ? 86  MET B CA    1 
ATOM   1887 C  C     . MET B 1 86  ? 71.909  -8.027  22.831 1    16.83  ? 86  MET B C     1 
ATOM   1888 O  O     . MET B 1 86  ? 70.832  -8.005  22.247 1    17.18  ? 86  MET B O     1 
ATOM   1889 C  CB    . MET B 1 86  ? 74.02   -7.99   21.443 1    16.03  ? 86  MET B CB    1 
ATOM   1890 C  CG    . MET B 1 86  ? 74.816  -7.102  20.495 1    18.89  ? 86  MET B CG    1 
ATOM   1891 S  SD    . MET B 1 86  ? 73.807  -5.91   19.522 1    23.08  ? 86  MET B SD    1 
ATOM   1892 C  CE    . MET B 1 86  ? 73.063  -7.049  18.326 1    18.73  ? 86  MET B CE    1 
ATOM   1893 N  N     . ALA B 1 87  ? 72.1    -8.689  24.001 1    17.64  ? 87  ALA B N     1 
ATOM   1894 C  CA    . ALA B 1 87  ? 71.031  -9.467  24.625 1    18.03  ? 87  ALA B CA    1 
ATOM   1895 C  C     . ALA B 1 87  ? 69.889  -8.569  25.046 1    18.32  ? 87  ALA B C     1 
ATOM   1896 O  O     . ALA B 1 87  ? 68.737  -8.951  24.877 1    18.97  ? 87  ALA B O     1 
ATOM   1897 C  CB    . ALA B 1 87  ? 71.552  -10.231 25.824 1    18.14  ? 87  ALA B CB    1 
ATOM   1898 N  N     . ILE B 1 88  ? 70.193  -7.378  25.572 1    17.88  ? 88  ILE B N     1 
ATOM   1899 C  CA    . ILE B 1 88  ? 69.158  -6.431  25.974 1    18.27  ? 88  ILE B CA    1 
ATOM   1900 C  C     . ILE B 1 88  ? 68.363  -5.967  24.745 1    20.35  ? 88  ILE B C     1 
ATOM   1901 O  O     . ILE B 1 88  ? 67.133  -6.012  24.784 1    21.09  ? 88  ILE B O     1 
ATOM   1902 C  CB    . ILE B 1 88  ? 69.742  -5.253  26.799 1    17.64  ? 88  ILE B CB    1 
ATOM   1903 C  CG1   . ILE B 1 88  ? 70.278  -5.736  28.161 1    17.6   ? 88  ILE B CG1   1 
ATOM   1904 C  CG2   . ILE B 1 88  ? 68.722  -4.128  26.975 1    17.84  ? 88  ILE B CG2   1 
ATOM   1905 C  CD1   . ILE B 1 88  ? 71.138  -4.782  28.852 1    18.67  ? 88  ILE B CD1   1 
ATOM   1906 N  N     . ASN B 1 89  ? 69.049  -5.613  23.63  1    21.04  ? 89  ASN B N     1 
ATOM   1907 C  CA    . ASN B 1 89  ? 68.367  -5.184  22.402 1    22.48  ? 89  ASN B CA    1 
ATOM   1908 C  C     . ASN B 1 89  ? 67.474  -6.265  21.827 1    22.2   ? 89  ASN B C     1 
ATOM   1909 O  O     . ASN B 1 89  ? 66.45   -5.938  21.248 1    22.44  ? 89  ASN B O     1 
ATOM   1910 C  CB    . ASN B 1 89  ? 69.343  -4.71   21.322 1    25.24  ? 89  ASN B CB    1 
ATOM   1911 C  CG    . ASN B 1 89  ? 70.139  -3.499  21.735 1    31.72  ? 89  ASN B CG    1 
ATOM   1912 O  OD1   . ASN B 1 89  ? 69.665  -2.625  22.489 1    34.15  ? 89  ASN B OD1   1 
ATOM   1913 N  ND2   . ASN B 1 89  ? 71.385  -3.429  21.262 1    32.95  ? 89  ASN B ND2   1 
ATOM   1914 N  N     . HIS B 1 90  ? 67.856  -7.534  21.959 1    21.71  ? 90  HIS B N     1 
ATOM   1915 C  CA    . HIS B 1 90  ? 67.041  -8.628  21.45  1    21.94  ? 90  HIS B CA    1 
ATOM   1916 C  C     . HIS B 1 90  ? 65.776  -8.791  22.281 1    22.3   ? 90  HIS B C     1 
ATOM   1917 O  O     . HIS B 1 90  ? 64.702  -9.037  21.721 1    23.15  ? 90  HIS B O     1 
ATOM   1918 C  CB    . HIS B 1 90  ? 67.83   -9.935  21.391 1    22.8   ? 90  HIS B CB    1 
ATOM   1919 C  CG    . HIS B 1 90  ? 67.11   -11.038 20.664 1    25.75  ? 90  HIS B CG    1 
ATOM   1920 N  ND1   . HIS B 1 90  ? 67.406  -12.37  20.894 1    27.52  ? 90  HIS B ND1   1 
ATOM   1921 C  CD2   . HIS B 1 90  ? 66.166  -10.968 19.692 1    27.61  ? 90  HIS B CD2   1 
ATOM   1922 C  CE1   . HIS B 1 90  ? 66.617  -13.067 20.091 1    28.18  ? 90  HIS B CE1   1 
ATOM   1923 N  NE2   . HIS B 1 90  ? 65.859  -12.269 19.337 1    28.65  ? 90  HIS B NE2   1 
ATOM   1924 N  N     . ILE B 1 91  ? 65.883  -8.624  23.599 1    21.3   ? 91  ILE B N     1 
ATOM   1925 C  CA    . ILE B 1 91  ? 64.724  -8.72   24.474 1    20.59  ? 91  ILE B CA    1 
ATOM   1926 C  C     . ILE B 1 91  ? 63.756  -7.576  24.168 1    20.43  ? 91  ILE B C     1 
ATOM   1927 O  O     . ILE B 1 91  ? 62.561  -7.819  23.99  1    20.47  ? 91  ILE B O     1 
ATOM   1928 C  CB    . ILE B 1 91  ? 65.162  -8.764  25.944 1    20.09  ? 91  ILE B CB    1 
ATOM   1929 C  CG1   . ILE B 1 91  ? 65.994  -10.023 26.223 1    20.3   ? 91  ILE B CG1   1 
ATOM   1930 C  CG2   . ILE B 1 91  ? 63.953  -8.742  26.828 1    20.76  ? 91  ILE B CG2   1 
ATOM   1931 C  CD1   . ILE B 1 91  ? 66.738  -9.997  27.552 1    21.34  ? 91  ILE B CD1   1 
ATOM   1932 N  N     . LYS B 1 92  ? 64.29   -6.358  23.983 1    19.99  ? 92  LYS B N     1 
ATOM   1933 C  CA    . LYS B 1 92  ? 63.485  -5.188  23.647 1    20.07  ? 92  LYS B CA    1 
ATOM   1934 C  C     . LYS B 1 92  ? 62.743  -5.387  22.335 1    20.87  ? 92  LYS B C     1 
ATOM   1935 O  O     . LYS B 1 92  ? 61.572  -5.043  22.227 1    21     ? 92  LYS B O     1 
ATOM   1936 C  CB    . LYS B 1 92  ? 64.355  -3.931  23.597 1    20.68  ? 92  LYS B CB    1 
ATOM   1937 C  CG    . LYS B 1 92  ? 64.873  -3.495  24.959 1    23.17  ? 92  LYS B CG    1 
ATOM   1938 C  CD    . LYS B 1 92  ? 65.856  -2.361  24.814 1    26.51  ? 92  LYS B CD    1 
ATOM   1939 C  CE    . LYS B 1 92  ? 65.172  -1.106  24.356 1    30.42  ? 92  LYS B CE    1 
ATOM   1940 N  NZ    . LYS B 1 92  ? 66.145  -0.018  24.08  1    33.9   ? 92  LYS B NZ    1 
ATOM   1941 N  N     . SER B 1 93  ? 63.415  -5.983  21.353 1    21.38  ? 93  SER B N     1 
ATOM   1942 C  CA    . SER B 1 93  ? 62.856  -6.3    20.044 1    21.91  ? 93  SER B CA    1 
ATOM   1943 C  C     . SER B 1 93  ? 61.711  -7.303  20.164 1    22.14  ? 93  SER B C     1 
ATOM   1944 O  O     . SER B 1 93  ? 60.698  -7.155  19.495 1    21.95  ? 93  SER B O     1 
ATOM   1945 C  CB    . SER B 1 93  ? 63.941  -6.87   19.142 1    23.94  ? 93  SER B CB    1 
ATOM   1946 O  OG    . SER B 1 93  ? 64.142  -6.046  18.002 1    28.86  ? 93  SER B OG    1 
ATOM   1947 N  N     . GLN B 1 94  ? 61.868  -8.308  21.033 1    22.55  ? 94  GLN B N     1 
ATOM   1948 C  CA    . GLN B 1 94  ? 60.871  -9.337  21.276 1    23.38  ? 94  GLN B CA    1 
ATOM   1949 C  C     . GLN B 1 94  ? 59.638  -8.784  21.979 1    24.11  ? 94  GLN B C     1 
ATOM   1950 O  O     . GLN B 1 94  ? 58.524  -9.149  21.613 1    24.33  ? 94  GLN B O     1 
ATOM   1951 C  CB    . GLN B 1 94  ? 61.477  -10.469 22.105 1    25.18  ? 94  GLN B CB    1 
ATOM   1952 C  CG    . GLN B 1 94  ? 62.429  -11.353 21.321 1    29.51  ? 94  GLN B CG    1 
ATOM   1953 C  CD    . GLN B 1 94  ? 63.199  -12.305 22.211 1    34.86  ? 94  GLN B CD    1 
ATOM   1954 O  OE1   . GLN B 1 94  ? 63.797  -11.91  23.234 1    36.17  ? 94  GLN B OE1   1 
ATOM   1955 N  NE2   . GLN B 1 94  ? 63.215  -13.588 21.832 1    35.56  ? 94  GLN B NE2   1 
ATOM   1956 N  N     . LEU B 1 95  ? 59.822  -7.923  22.997 1    24.26  ? 95  LEU B N     1 
ATOM   1957 C  CA    . LEU B 1 95  ? 58.7    -7.311  23.714 1    24.5   ? 95  LEU B CA    1 
ATOM   1958 C  C     . LEU B 1 95  ? 57.908  -6.386  22.762 1    26.35  ? 95  LEU B C     1 
ATOM   1959 O  O     . LEU B 1 95  ? 56.673  -6.368  22.794 1    27.19  ? 95  LEU B O     1 
ATOM   1960 C  CB    . LEU B 1 95  ? 59.222  -6.489  24.898 1    23.57  ? 95  LEU B CB    1 
ATOM   1961 C  CG    . LEU B 1 95  ? 59.986  -7.272  25.969 1    23.75  ? 95  LEU B CG    1 
ATOM   1962 C  CD1   . LEU B 1 95  ? 60.872  -6.369  26.792 1    23.42  ? 95  LEU B CD1   1 
ATOM   1963 C  CD2   . LEU B 1 95  ? 59.049  -8.038  26.865 1    23.92  ? 95  LEU B CD2   1 
ATOM   1964 N  N     . ARG B 1 96  ? 58.622  -5.615  21.916 1    26.21  ? 96  ARG B N     1 
ATOM   1965 C  CA    . ARG B 1 96  ? 57.969  -4.685  21.014 1    26.72  ? 96  ARG B CA    1 
ATOM   1966 C  C     . ARG B 1 96  ? 57.192  -5.422  19.925 1    29.81  ? 96  ARG B C     1 
ATOM   1967 O  O     . ARG B 1 96  ? 56.116  -4.969  19.529 1    30.14  ? 96  ARG B O     1 
ATOM   1968 C  CB    . ARG B 1 96  ? 58.984  -3.681  20.453 1    25.56  ? 96  ARG B CB    1 
ATOM   1969 C  CG    . ARG B 1 96  ? 58.415  -2.699  19.442 1    25.43  ? 96  ARG B CG    1 
ATOM   1970 C  CD    . ARG B 1 96  ? 57.321  -1.845  20.028 1    26.1   ? 96  ARG B CD    1 
ATOM   1971 N  NE    . ARG B 1 96  ? 56.695  -0.942  19.061 1    26.41  ? 96  ARG B NE    1 
ATOM   1972 C  CZ    . ARG B 1 96  ? 55.584  -1.22   18.384 1    26.88  ? 96  ARG B CZ    1 
ATOM   1973 N  NH1   . ARG B 1 96  ? 55.068  -0.327  17.552 1    25.83  ? 96  ARG B NH1   1 
ATOM   1974 N  NH2   . ARG B 1 96  ? 54.98   -2.393  18.533 1    26.24  ? 96  ARG B NH2   1 
ATOM   1975 N  N     . ALA B 1 97  ? 57.698  -6.604  19.495 1    31.57  ? 97  ALA B N     1 
ATOM   1976 C  CA    . ALA B 1 97  ? 57.052  -7.447  18.501 1    33.19  ? 97  ALA B CA    1 
ATOM   1977 C  C     . ALA B 1 97  ? 55.691  -7.969  18.975 1    35.37  ? 97  ALA B C     1 
ATOM   1978 O  O     . ALA B 1 97  ? 54.87   -8.31   18.128 1    35.62  ? 97  ALA B O     1 
ATOM   1979 C  CB    . ALA B 1 97  ? 57.96   -8.603  18.124 1    33.27  ? 97  ALA B CB    1 
ATOM   1980 N  N     . THR B 1 98  ? 55.448  -8.033  20.312 1    36.68  ? 98  THR B N     1 
ATOM   1981 C  CA    . THR B 1 98  ? 54.154  -8.443  20.869 1    38.47  ? 98  THR B CA    1 
ATOM   1982 C  C     . THR B 1 98  ? 53.062  -7.452  20.482 1    40.9   ? 98  THR B C     1 
ATOM   1983 O  O     . THR B 1 98  ? 51.916  -7.853  20.309 1    41.51  ? 98  THR B O     1 
ATOM   1984 C  CB    . THR B 1 98  ? 54.204  -8.526  22.404 1    39.18  ? 98  THR B CB    1 
ATOM   1985 O  OG1   . THR B 1 98  ? 54.362  -7.222  22.977 1    40.13  ? 98  THR B OG1   1 
ATOM   1986 C  CG2   . THR B 1 98  ? 55.289  -9.431  22.895 1    39.31  ? 98  THR B CG2   1 
ATOM   1987 N  N     . GLY B 1 99  ? 53.416  -6.168  20.4   1    42.19  ? 99  GLY B N     1 
ATOM   1988 C  CA    . GLY B 1 99  ? 52.477  -5.096  20.089 1    43.92  ? 99  GLY B CA    1 
ATOM   1989 C  C     . GLY B 1 99  ? 51.627  -4.661  21.271 1    45.49  ? 99  GLY B C     1 
ATOM   1990 O  O     . GLY B 1 99  ? 50.744  -3.813  21.123 1    46.02  ? 99  GLY B O     1 
ATOM   1991 N  N     . GLU B 1 100 ? 51.889  -5.23   22.454 1    46.03  ? 100 GLU B N     1 
ATOM   1992 C  CA    . GLU B 1 100 ? 51.148  -4.935  23.666 1    47.13  ? 100 GLU B CA    1 
ATOM   1993 C  C     . GLU B 1 100 ? 51.492  -3.589  24.272 1    47.48  ? 100 GLU B C     1 
ATOM   1994 O  O     . GLU B 1 100 ? 52.658  -3.179  24.249 1    47.99  ? 100 GLU B O     1 
ATOM   1995 C  CB    . GLU B 1 100 ? 51.388  -6.046  24.694 1    49.87  ? 100 GLU B CB    1 
ATOM   1996 C  CG    . GLU B 1 100 ? 50.739  -7.363  24.33  1    56.09  ? 100 GLU B CG    1 
ATOM   1997 C  CD    . GLU B 1 100 ? 49.266  -7.253  23.994 1    65.85  ? 100 GLU B CD    1 
ATOM   1998 O  OE1   . GLU B 1 100 ? 48.931  -7.364  22.792 1    68.12  ? 100 GLU B OE1   1 
ATOM   1999 O  OE2   . GLU B 1 100 ? 48.454  -7.017  24.917 1    69.8   ? 100 GLU B OE2   1 
ATOM   2000 N  N     . ARG B 1 101 ? 50.477  -2.895  24.823 1    46.85  ? 101 ARG B N     1 
ATOM   2001 C  CA    . ARG B 1 101 ? 50.744  -1.622  25.501 1    46.7   ? 101 ARG B CA    1 
ATOM   2002 C  C     . ARG B 1 101 ? 51.356  -1.832  26.876 1    44.83  ? 101 ARG B C     1 
ATOM   2003 O  O     . ARG B 1 101 ? 52.015  -0.927  27.375 1    44.48  ? 101 ARG B O     1 
ATOM   2004 C  CB    . ARG B 1 101 ? 49.539  -0.67   25.565 1    49.76  ? 101 ARG B CB    1 
ATOM   2005 C  CG    . ARG B 1 101 ? 48.168  -1.29   25.325 1    56.09  ? 101 ARG B CG    1 
ATOM   2006 C  CD    . ARG B 1 101 ? 47.678  -1.178  23.881 1    62.33  ? 101 ARG B CD    1 
ATOM   2007 N  NE    . ARG B 1 101 ? 47.958  0.112   23.235 1    68.17  ? 101 ARG B NE    1 
ATOM   2008 C  CZ    . ARG B 1 101 ? 47.268  1.231   23.449 1    71.91  ? 101 ARG B CZ    1 
ATOM   2009 N  NH1   . ARG B 1 101 ? 47.581  2.347   22.797 1    72.21  ? 101 ARG B NH1   1 
ATOM   2010 N  NH2   . ARG B 1 101 ? 46.265  1.245   24.322 1    71.66  ? 101 ARG B NH2   1 
ATOM   2011 N  N     . GLU B 1 102 ? 51.142  -3.028  27.481 1    43.65  ? 102 GLU B N     1 
ATOM   2012 C  CA    . GLU B 1 102 ? 51.691  -3.45   28.763 1    42.68  ? 102 GLU B CA    1 
ATOM   2013 C  C     . GLU B 1 102 ? 52.06   -4.94   28.734 1    41.11  ? 102 GLU B C     1 
ATOM   2014 O  O     . GLU B 1 102 ? 51.411  -5.736  28.054 1    40.99  ? 102 GLU B O     1 
ATOM   2015 C  CB    . GLU B 1 102 ? 50.764  -3.103  29.932 1    45.29  ? 102 GLU B CB    1 
ATOM   2016 C  CG    . GLU B 1 102 ? 49.529  -3.971  30.015 1    51.73  ? 102 GLU B CG    1 
ATOM   2017 C  CD    . GLU B 1 102 ? 48.716  -3.756  31.273 1    61.02  ? 102 GLU B CD    1 
ATOM   2018 O  OE1   . GLU B 1 102 ? 48.754  -2.635  31.83  1    63.04  ? 102 GLU B OE1   1 
ATOM   2019 O  OE2   . GLU B 1 102 ? 48.061  -4.723  31.719 1    64.4   ? 102 GLU B OE2   1 
ATOM   2020 N  N     . VAL B 1 103 ? 53.134  -5.303  29.432 1    39.95  ? 103 VAL B N     1 
ATOM   2021 C  CA    . VAL B 1 103 ? 53.647  -6.669  29.455 1    39.73  ? 103 VAL B CA    1 
ATOM   2022 C  C     . VAL B 1 103 ? 53.932  -7.119  30.877 1    39.7   ? 103 VAL B C     1 
ATOM   2023 O  O     . VAL B 1 103 ? 54.486  -6.357  31.674 1    40.33  ? 103 VAL B O     1 
ATOM   2024 C  CB    . VAL B 1 103 ? 54.942  -6.789  28.607 1    40.32  ? 103 VAL B CB    1 
ATOM   2025 C  CG1   . VAL B 1 103 ? 54.643  -6.705  27.113 1    40.77  ? 103 VAL B CG1   1 
ATOM   2026 C  CG2   . VAL B 1 103 ? 55.983  -5.753  29.031 1    40.79  ? 103 VAL B CG2   1 
ATOM   2027 N  N     . PRO B 1 104 ? 53.618  -8.379  31.21  1    38.62  ? 104 PRO B N     1 
ATOM   2028 C  CA    . PRO B 1 104 ? 53.94   -8.875  32.556 1    37.92  ? 104 PRO B CA    1 
ATOM   2029 C  C     . PRO B 1 104 ? 55.452  -8.901  32.799 1    37.53  ? 104 PRO B C     1 
ATOM   2030 O  O     . PRO B 1 104 ? 56.192  -9.212  31.878 1    37.79  ? 104 PRO B O     1 
ATOM   2031 C  CB    . PRO B 1 104 ? 53.371  -10.294 32.543 1    38.59  ? 104 PRO B CB    1 
ATOM   2032 C  CG    . PRO B 1 104 ? 53.293  -10.674 31.109 1    39.03  ? 104 PRO B CG    1 
ATOM   2033 C  CD    . PRO B 1 104 ? 52.979  -9.415  30.379 1    37.77  ? 104 PRO B CD    1 
ATOM   2034 N  N     . SER B 1 105 ? 55.923  -8.581  34.022 1    36.99  ? 105 SER B N     1 
ATOM   2035 C  CA    . SER B 1 105 ? 57.367  -8.632  34.312 1    36.52  ? 105 SER B CA    1 
ATOM   2036 C  C     . SER B 1 105 ? 57.937  -10.072 34.204 1    35.67  ? 105 SER B C     1 
ATOM   2037 O  O     . SER B 1 105 ? 59.13   -10.25  33.964 1    34.95  ? 105 SER B O     1 
ATOM   2038 C  CB    . SER B 1 105 ? 57.677  -8.012  35.67  1    37.39  ? 105 SER B CB    1 
ATOM   2039 O  OG    . SER B 1 105 ? 57.288  -8.87   36.729 1    40.04  ? 105 SER B OG    1 
ATOM   2040 N  N     . LYS B 1 106 ? 57.064  -11.085 34.348 1    35.52  ? 106 LYS B N     1 
ATOM   2041 C  CA    . LYS B 1 106 ? 57.39   -12.496 34.193 1    35.81  ? 106 LYS B CA    1 
ATOM   2042 C  C     . LYS B 1 106 ? 57.875  -12.751 32.77  1    34.54  ? 106 LYS B C     1 
ATOM   2043 O  O     . LYS B 1 106 ? 58.825  -13.506 32.586 1    35.14  ? 106 LYS B O     1 
ATOM   2044 C  CB    . LYS B 1 106 ? 56.154  -13.364 34.479 1    39.32  ? 106 LYS B CB    1 
ATOM   2045 C  CG    . LYS B 1 106 ? 56.403  -14.863 34.345 1    45.87  ? 106 LYS B CG    1 
ATOM   2046 C  CD    . LYS B 1 106 ? 55.113  -15.667 34.438 1    52.78  ? 106 LYS B CD    1 
ATOM   2047 C  CE    . LYS B 1 106 ? 55.332  -17.171 34.447 1    58.06  ? 106 LYS B CE    1 
ATOM   2048 N  NZ    . LYS B 1 106 ? 55.755  -17.708 33.109 1    60.57  ? 106 LYS B NZ    1 
ATOM   2049 N  N     . MET B 1 107 ? 57.259  -12.09  31.768 1    32.69  ? 107 MET B N     1 
ATOM   2050 C  CA    . MET B 1 107 ? 57.642  -12.187 30.362 1    31.09  ? 107 MET B CA    1 
ATOM   2051 C  C     . MET B 1 107 ? 59.064  -11.668 30.159 1    29.22  ? 107 MET B C     1 
ATOM   2052 O  O     . MET B 1 107 ? 59.858  -12.331 29.494 1    30.04  ? 107 MET B O     1 
ATOM   2053 C  CB    . MET B 1 107 ? 56.655  -11.404 29.494 1    31.84  ? 107 MET B CB    1 
ATOM   2054 C  CG    . MET B 1 107 ? 56.859  -11.612 28.022 1    34.58  ? 107 MET B CG    1 
ATOM   2055 S  SD    . MET B 1 107 ? 56.161  -10.252 27.034 1    39.39  ? 107 MET B SD    1 
ATOM   2056 C  CE    . MET B 1 107 ? 54.728  -10.976 26.433 1    36.72  ? 107 MET B CE    1 
ATOM   2057 N  N     . ILE B 1 108 ? 59.388  -10.501 30.725 1    26.79  ? 108 ILE B N     1 
ATOM   2058 C  CA    . ILE B 1 108 ? 60.73   -9.922  30.671 1    25.04  ? 108 ILE B CA    1 
ATOM   2059 C  C     . ILE B 1 108 ? 61.747  -10.871 31.314 1    23.9   ? 108 ILE B C     1 
ATOM   2060 O  O     . ILE B 1 108 ? 62.842  -11.067 30.784 1    23.1   ? 108 ILE B O     1 
ATOM   2061 C  CB    . ILE B 1 108 ? 60.738  -8.544  31.361 1    24.79  ? 108 ILE B CB    1 
ATOM   2062 C  CG1   . ILE B 1 108 ? 59.706  -7.609  30.716 1    25.38  ? 108 ILE B CG1   1 
ATOM   2063 C  CG2   . ILE B 1 108 ? 62.137  -7.952  31.35  1    25.25  ? 108 ILE B CG2   1 
ATOM   2064 C  CD1   . ILE B 1 108 ? 59.684  -6.202  31.239 1    26.68  ? 108 ILE B CD1   1 
ATOM   2065 N  N     . GLY B 1 109 ? 61.352  -11.458 32.442 1    23.88  ? 109 GLY B N     1 
ATOM   2066 C  CA    . GLY B 1 109 ? 62.148  -12.412 33.196 1    23.97  ? 109 GLY B CA    1 
ATOM   2067 C  C     . GLY B 1 109 ? 62.469  -13.667 32.412 1    23.87  ? 109 GLY B C     1 
ATOM   2068 O  O     . GLY B 1 109 ? 63.606  -14.135 32.462 1    23.95  ? 109 GLY B O     1 
ATOM   2069 N  N     . ASN B 1 110 ? 61.486  -14.221 31.675 1    23.49  ? 110 ASN B N     1 
ATOM   2070 C  CA    . ASN B 1 110 ? 61.728  -15.431 30.888 1    24.21  ? 110 ASN B CA    1 
ATOM   2071 C  C     . ASN B 1 110 ? 62.652  -15.157 29.724 1    24.75  ? 110 ASN B C     1 
ATOM   2072 O  O     . ASN B 1 110 ? 63.494  -15.995 29.409 1    25.75  ? 110 ASN B O     1 
ATOM   2073 C  CB    . ASN B 1 110 ? 60.447  -16.051 30.381 1    25.93  ? 110 ASN B CB    1 
ATOM   2074 C  CG    . ASN B 1 110 ? 59.456  -16.436 31.444 1    31.08  ? 110 ASN B CG    1 
ATOM   2075 O  OD1   . ASN B 1 110 ? 58.245  -16.274 31.252 1    33.32  ? 110 ASN B OD1   1 
ATOM   2076 N  ND2   . ASN B 1 110 ? 59.929  -16.96  32.586 1    31.72  ? 110 ASN B ND2   1 
ATOM   2077 N  N     . LEU B 1 111 ? 62.522  -13.981 29.088 1    23.88  ? 111 LEU B N     1 
ATOM   2078 C  CA    . LEU B 1 111 ? 63.413  -13.612 28.003 1    23.39  ? 111 LEU B CA    1 
ATOM   2079 C  C     . LEU B 1 111 ? 64.847  -13.489 28.523 1    23.9   ? 111 LEU B C     1 
ATOM   2080 O  O     . LEU B 1 111 ? 65.725  -14.084 27.912 1    24.34  ? 111 LEU B O     1 
ATOM   2081 C  CB    . LEU B 1 111 ? 62.943  -12.338 27.28  1    22.96  ? 111 LEU B CB    1 
ATOM   2082 C  CG    . LEU B 1 111 ? 61.505  -12.357 26.725 1    23.45  ? 111 LEU B CG    1 
ATOM   2083 C  CD1   . LEU B 1 111 ? 61.207  -11.111 25.928 1    23.53  ? 111 LEU B CD1   1 
ATOM   2084 C  CD2   . LEU B 1 111 ? 61.241  -13.574 25.862 1    23.69  ? 111 LEU B CD2   1 
ATOM   2085 N  N     . VAL B 1 112 ? 65.068  -12.879 29.722 1    23.97  ? 112 VAL B N     1 
ATOM   2086 C  CA    . VAL B 1 112 ? 66.418  -12.799 30.31  1    24.51  ? 112 VAL B CA    1 
ATOM   2087 C  C     . VAL B 1 112 ? 66.989  -14.19  30.562 1    26.15  ? 112 VAL B C     1 
ATOM   2088 O  O     . VAL B 1 112 ? 68.154  -14.444 30.266 1    26.59  ? 112 VAL B O     1 
ATOM   2089 C  CB    . VAL B 1 112 ? 66.511  -11.94  31.587 1    23.99  ? 112 VAL B CB    1 
ATOM   2090 C  CG1   . VAL B 1 112 ? 67.941  -11.892 32.089 1    24.24  ? 112 VAL B CG1   1 
ATOM   2091 C  CG2   . VAL B 1 112 ? 66.02   -10.545 31.325 1    24.08  ? 112 VAL B CG2   1 
ATOM   2092 N  N     . MET B 1 113 ? 66.159  -15.105 31.052 1    26.99  ? 113 MET B N     1 
ATOM   2093 C  CA    . MET B 1 113 ? 66.554  -16.489 31.288 1    28.73  ? 113 MET B CA    1 
ATOM   2094 C  C     . MET B 1 113 ? 67.036  -17.162 30.017 1    30.27  ? 113 MET B C     1 
ATOM   2095 O  O     . MET B 1 113 ? 68.037  -17.874 30.033 1    30.41  ? 113 MET B O     1 
ATOM   2096 C  CB    . MET B 1 113 ? 65.376  -17.272 31.876 1    29.6   ? 113 MET B CB    1 
ATOM   2097 C  CG    . MET B 1 113 ? 65.006  -16.812 33.263 1    30.51  ? 113 MET B CG    1 
ATOM   2098 S  SD    . MET B 1 113 ? 66.116  -17.518 34.492 1    32.59  ? 113 MET B SD    1 
ATOM   2099 C  CE    . MET B 1 113 ? 65.249  -19.015 34.839 1    31.87  ? 113 MET B CE    1 
ATOM   2100 N  N     . GLU B 1 114 ? 66.35   -16.887 28.904 1    31.29  ? 114 GLU B N     1 
ATOM   2101 C  CA    . GLU B 1 114 ? 66.694  -17.426 27.604 1    32.52  ? 114 GLU B CA    1 
ATOM   2102 C  C     . GLU B 1 114 ? 67.99   -16.852 27.059 1    31.75  ? 114 GLU B C     1 
ATOM   2103 O  O     . GLU B 1 114 ? 68.724  -17.565 26.384 1    31.76  ? 114 GLU B O     1 
ATOM   2104 C  CB    . GLU B 1 114 ? 65.537  -17.222 26.63  1    37.62  ? 114 GLU B CB    1 
ATOM   2105 C  CG    . GLU B 1 114 ? 64.269  -17.89  27.134 1    47.61  ? 114 GLU B CG    1 
ATOM   2106 C  CD    . GLU B 1 114 ? 63.308  -18.383 26.068 1    60.15  ? 114 GLU B CD    1 
ATOM   2107 O  OE1   . GLU B 1 114 ? 63.44   -17.951 24.895 1    62.46  ? 114 GLU B OE1   1 
ATOM   2108 O  OE2   . GLU B 1 114 ? 62.421  -19.202 26.41  1    63.94  ? 114 GLU B OE2   1 
ATOM   2109 N  N     . GLN B 1 115 ? 68.284  -15.592 27.362 1    31.11  ? 115 GLN B N     1 
ATOM   2110 C  CA    . GLN B 1 115 ? 69.518  -14.972 26.925 1    31.52  ? 115 GLN B CA    1 
ATOM   2111 C  C     . GLN B 1 115 ? 70.667  -15.516 27.75  1    31.67  ? 115 GLN B C     1 
ATOM   2112 O  O     . GLN B 1 115 ? 71.673  -15.922 27.184 1    32.45  ? 115 GLN B O     1 
ATOM   2113 C  CB    . GLN B 1 115 ? 69.45   -13.441 27.011 1    33.09  ? 115 GLN B CB    1 
ATOM   2114 C  CG    . GLN B 1 115 ? 68.504  -12.777 26     1    35.54  ? 115 GLN B CG    1 
ATOM   2115 C  CD    . GLN B 1 115 ? 68.722  -13.215 24.562 1    39.77  ? 115 GLN B CD    1 
ATOM   2116 O  OE1   . GLN B 1 115 ? 67.952  -14.002 23.993 1    40.26  ? 115 GLN B OE1   1 
ATOM   2117 N  NE2   . GLN B 1 115 ? 69.805  -12.756 23.944 1    40.52  ? 115 GLN B NE2   1 
ATOM   2118 N  N     . LEU B 1 116 ? 70.507  -15.582 29.057 1    31.26  ? 116 LEU B N     1 
ATOM   2119 C  CA    . LEU B 1 116 ? 71.559  -16.094 29.923 1    31.45  ? 116 LEU B CA    1 
ATOM   2120 C  C     . LEU B 1 116 ? 71.868  -17.551 29.654 1    32.25  ? 116 LEU B C     1 
ATOM   2121 O  O     . LEU B 1 116 ? 73.025  -17.934 29.724 1    32.23  ? 116 LEU B O     1 
ATOM   2122 C  CB    . LEU B 1 116 ? 71.245  -15.838 31.392 1    30.9   ? 116 LEU B CB    1 
ATOM   2123 C  CG    . LEU B 1 116 ? 71.175  -14.38  31.764 1    31.44  ? 116 LEU B CG    1 
ATOM   2124 C  CD1   . LEU B 1 116 ? 70.737  -14.228 33.165 1    31.41  ? 116 LEU B CD1   1 
ATOM   2125 C  CD2   . LEU B 1 116 ? 72.515  -13.674 31.539 1    31.91  ? 116 LEU B CD2   1 
ATOM   2126 N  N     . LYS B 1 117 ? 70.872  -18.343 29.245 1    32.86  ? 117 LYS B N     1 
ATOM   2127 C  CA    . LYS B 1 117 ? 71.08   -19.747 28.899 1    34.32  ? 117 LYS B CA    1 
ATOM   2128 C  C     . LYS B 1 117 ? 72.096  -19.868 27.744 1    35.58  ? 117 LYS B C     1 
ATOM   2129 O  O     . LYS B 1 117 ? 72.94   -20.765 27.755 1    35.78  ? 117 LYS B O     1 
ATOM   2130 C  CB    . LYS B 1 117 ? 69.738  -20.371 28.502 1    36.89  ? 117 LYS B CB    1 
ATOM   2131 C  CG    . LYS B 1 117 ? 69.676  -21.877 28.638 1    42.47  ? 117 LYS B CG    1 
ATOM   2132 C  CD    . LYS B 1 117 ? 68.215  -22.34  28.681 1    48.24  ? 117 LYS B CD    1 
ATOM   2133 C  CE    . LYS B 1 117 ? 68.017  -23.793 28.319 1    53.01  ? 117 LYS B CE    1 
ATOM   2134 N  NZ    . LYS B 1 117 ? 68.213  -24.061 26.854 1    54.47  ? 117 LYS B NZ    1 
ATOM   2135 N  N     . LYS B 1 118 ? 72.046  -18.914 26.784 1    36     ? 118 LYS B N     1 
ATOM   2136 C  CA    . LYS B 1 118 ? 72.954  -18.836 25.642 1    36.59  ? 118 LYS B CA    1 
ATOM   2137 C  C     . LYS B 1 118 ? 74.31   -18.229 26.044 1    36.69  ? 118 LYS B C     1 
ATOM   2138 O  O     . LYS B 1 118 ? 75.352  -18.709 25.592 1    37     ? 118 LYS B O     1 
ATOM   2139 C  CB    . LYS B 1 118 ? 72.341  -17.968 24.525 1    38.76  ? 118 LYS B CB    1 
ATOM   2140 C  CG    . LYS B 1 118 ? 71.112  -18.545 23.835 1    43.23  ? 118 LYS B CG    1 
ATOM   2141 C  CD    . LYS B 1 118 ? 70.608  -17.543 22.759 1    47.3   ? 118 LYS B CD    1 
ATOM   2142 C  CE    . LYS B 1 118 ? 69.247  -17.874 22.177 1    50.68  ? 118 LYS B CE    1 
ATOM   2143 N  NZ    . LYS B 1 118 ? 68.702  -16.774 21.327 1    52.16  ? 118 LYS B NZ    1 
ATOM   2144 N  N     . LEU B 1 119 ? 74.287  -17.153 26.869 1    36.21  ? 119 LEU B N     1 
ATOM   2145 C  CA    . LEU B 1 119 ? 75.46   -16.39  27.315 1    35.74  ? 119 LEU B CA    1 
ATOM   2146 C  C     . LEU B 1 119 ? 76.382  -17.119 28.284 1    36.35  ? 119 LEU B C     1 
ATOM   2147 O  O     . LEU B 1 119 ? 77.575  -17.26  28.002 1    36.23  ? 119 LEU B O     1 
ATOM   2148 C  CB    . LEU B 1 119 ? 75.025  -15.051 27.921 1    35     ? 119 LEU B CB    1 
ATOM   2149 C  CG    . LEU B 1 119 ? 74.649  -13.972 26.941 1    35.55  ? 119 LEU B CG    1 
ATOM   2150 C  CD1   . LEU B 1 119 ? 73.982  -12.809 27.654 1    35.6   ? 119 LEU B CD1   1 
ATOM   2151 C  CD2   . LEU B 1 119 ? 75.854  -13.541 26.121 1    35.88  ? 119 LEU B CD2   1 
ATOM   2152 N  N     . ASP B 1 120 ? 75.845  -17.555 29.435 1    36.9   ? 120 ASP B N     1 
ATOM   2153 C  CA    . ASP B 1 120 ? 76.628  -18.214 30.465 1    37.93  ? 120 ASP B CA    1 
ATOM   2154 C  C     . ASP B 1 120 ? 75.735  -19.072 31.355 1    38.09  ? 120 ASP B C     1 
ATOM   2155 O  O     . ASP B 1 120 ? 74.735  -18.6   31.895 1    37.53  ? 120 ASP B O     1 
ATOM   2156 C  CB    . ASP B 1 120 ? 77.362  -17.163 31.301 1    40.56  ? 120 ASP B CB    1 
ATOM   2157 C  CG    . ASP B 1 120 ? 78.378  -17.758 32.236 1    46.09  ? 120 ASP B CG    1 
ATOM   2158 O  OD1   . ASP B 1 120 ? 79.468  -18.139 31.763 1    46.68  ? 120 ASP B OD1   1 
ATOM   2159 O  OD2   . ASP B 1 120 ? 78.063  -17.899 33.43  1    49.37  ? 120 ASP B OD2   1 
ATOM   2160 N  N     . LYS B 1 121 ? 76.14   -20.326 31.528 1    38.59  ? 121 LYS B N     1 
ATOM   2161 C  CA    . LYS B 1 121 ? 75.423  -21.316 32.311 1    39.34  ? 121 LYS B CA    1 
ATOM   2162 C  C     . LYS B 1 121 ? 75.418  -20.996 33.808 1    38.27  ? 121 LYS B C     1 
ATOM   2163 O  O     . LYS B 1 121 ? 74.411  -21.239 34.473 1    39.02  ? 121 LYS B O     1 
ATOM   2164 C  CB    . LYS B 1 121 ? 76.009  -22.713 32.026 1    43.69  ? 121 LYS B CB    1 
ATOM   2165 C  CG    . LYS B 1 121 ? 77.494  -22.824 32.404 1    51.28  ? 121 LYS B CG    1 
ATOM   2166 C  CD    . LYS B 1 121 ? 78.22   -24.046 31.822 1    57.83  ? 121 LYS B CD    1 
ATOM   2167 C  CE    . LYS B 1 121 ? 79.689  -24.022 32.198 1    62.36  ? 121 LYS B CE    1 
ATOM   2168 N  NZ    . LYS B 1 121 ? 80.313  -22.69  31.913 1    64.62  ? 121 LYS B NZ    1 
ATOM   2169 N  N     . VAL B 1 122 ? 76.515  -20.431 34.345 1    36.33  ? 122 VAL B N     1 
ATOM   2170 C  CA    . VAL B 1 122 ? 76.604  -20.081 35.771 1    34.7   ? 122 VAL B CA    1 
ATOM   2171 C  C     . VAL B 1 122 ? 75.715  -18.87  36.062 1    33.88  ? 122 VAL B C     1 
ATOM   2172 O  O     . VAL B 1 122 ? 74.979  -18.874 37.063 1    34.4   ? 122 VAL B O     1 
ATOM   2173 C  CB    . VAL B 1 122 ? 78.071  -19.901 36.254 1    34.08  ? 122 VAL B CB    1 
ATOM   2174 C  CG1   . VAL B 1 122 ? 78.148  -19.209 37.608 1    33.56  ? 122 VAL B CG1   1 
ATOM   2175 C  CG2   . VAL B 1 122 ? 78.795  -21.234 36.296 1    34.26  ? 122 VAL B CG2   1 
ATOM   2176 N  N     . ALA B 1 123 ? 75.745  -17.867 35.162 1    32.3   ? 123 ALA B N     1 
ATOM   2177 C  CA    . ALA B 1 123 ? 74.914  -16.668 35.234 1    32.09  ? 123 ALA B CA    1 
ATOM   2178 C  C     . ALA B 1 123 ? 73.43   -17.022 35.206 1    32.33  ? 123 ALA B C     1 
ATOM   2179 O  O     . ALA B 1 123 ? 72.633  -16.357 35.858 1    32.47  ? 123 ALA B O     1 
ATOM   2180 C  CB    . ALA B 1 123 ? 75.229  -15.753 34.071 1    32.14  ? 123 ALA B CB    1 
ATOM   2181 N  N     . TYR B 1 124 ? 73.062  -18.065 34.455 1    32.5   ? 124 TYR B N     1 
ATOM   2182 C  CA    . TYR B 1 124 ? 71.695  -18.557 34.355 1    33.37  ? 124 TYR B CA    1 
ATOM   2183 C  C     . TYR B 1 124 ? 71.228  -19.057 35.732 1    33.68  ? 124 TYR B C     1 
ATOM   2184 O  O     . TYR B 1 124 ? 70.16   -18.653 36.184 1    33.5   ? 124 TYR B O     1 
ATOM   2185 C  CB    . TYR B 1 124 ? 71.596  -19.668 33.271 1    33.78  ? 124 TYR B CB    1 
ATOM   2186 C  CG    . TYR B 1 124 ? 70.229  -20.315 33.182 1    35.28  ? 124 TYR B CG    1 
ATOM   2187 C  CD1   . TYR B 1 124 ? 69.908  -21.417 33.96  1    37.16  ? 124 TYR B CD1   1 
ATOM   2188 C  CD2   . TYR B 1 124 ? 69.245  -19.798 32.353 1    36.32  ? 124 TYR B CD2   1 
ATOM   2189 C  CE1   . TYR B 1 124 ? 68.637  -21.976 33.931 1    38.57  ? 124 TYR B CE1   1 
ATOM   2190 C  CE2   . TYR B 1 124 ? 67.982  -20.369 32.287 1    37.69  ? 124 TYR B CE2   1 
ATOM   2191 C  CZ    . TYR B 1 124 ? 67.68   -21.461 33.076 1    39.65  ? 124 TYR B CZ    1 
ATOM   2192 O  OH    . TYR B 1 124 ? 66.429  -22.033 33.033 1    42.35  ? 124 TYR B OH    1 
ATOM   2193 N  N     . ILE B 1 125 ? 72.042  -19.906 36.404 1    33.93  ? 125 ILE B N     1 
ATOM   2194 C  CA    . ILE B 1 125 ? 71.738  -20.46  37.733 1    34.33  ? 125 ILE B CA    1 
ATOM   2195 C  C     . ILE B 1 125 ? 71.613  -19.345 38.777 1    32.83  ? 125 ILE B C     1 
ATOM   2196 O  O     . ILE B 1 125 ? 70.729  -19.395 39.65  1    32.84  ? 125 ILE B O     1 
ATOM   2197 C  CB    . ILE B 1 125 ? 72.801  -21.5   38.169 1    36.09  ? 125 ILE B CB    1 
ATOM   2198 C  CG1   . ILE B 1 125 ? 73.026  -22.586 37.11  1    38.14  ? 125 ILE B CG1   1 
ATOM   2199 C  CG2   . ILE B 1 125 ? 72.456  -22.106 39.538 1    37.43  ? 125 ILE B CG2   1 
ATOM   2200 C  CD1   . ILE B 1 125 ? 71.833  -23.384 36.79  1    40.03  ? 125 ILE B CD1   1 
ATOM   2201 N  N     . ARG B 1 126 ? 72.507  -18.337 38.693 1    30.94  ? 126 ARG B N     1 
ATOM   2202 C  CA    . ARG B 1 126 ? 72.48   -17.211 39.627 1    29.15  ? 126 ARG B CA    1 
ATOM   2203 C  C     . ARG B 1 126 ? 71.169  -16.432 39.496 1    29.06  ? 126 ARG B C     1 
ATOM   2204 O  O     . ARG B 1 126 ? 70.503  -16.193 40.505 1    28.98  ? 126 ARG B O     1 
ATOM   2205 C  CB    . ARG B 1 126 ? 73.685  -16.282 39.416 1    27.91  ? 126 ARG B CB    1 
ATOM   2206 C  CG    . ARG B 1 126 ? 75.01   -16.898 39.802 1    27.66  ? 126 ARG B CG    1 
ATOM   2207 C  CD    . ARG B 1 126 ? 76.007  -15.836 40.201 1    28.05  ? 126 ARG B CD    1 
ATOM   2208 N  NE    . ARG B 1 126 ? 77.381  -16.329 40.162 1    28.87  ? 126 ARG B NE    1 
ATOM   2209 C  CZ    . ARG B 1 126 ? 78.297  -15.934 39.28  1    29.58  ? 126 ARG B CZ    1 
ATOM   2210 N  NH1   . ARG B 1 126 ? 78.014  -14.983 38.396 1    27.42  ? 126 ARG B NH1   1 
ATOM   2211 N  NH2   . ARG B 1 126 ? 79.523  -16.442 39.316 1    29.6   ? 126 ARG B NH2   1 
ATOM   2212 N  N     . PHE B 1 127 ? 70.779  -16.074 38.25  1    28.78  ? 127 PHE B N     1 
ATOM   2213 C  CA    . PHE B 1 127 ? 69.541  -15.348 37.989 1    28.49  ? 127 PHE B CA    1 
ATOM   2214 C  C     . PHE B 1 127 ? 68.328  -16.188 38.373 1    30.38  ? 127 PHE B C     1 
ATOM   2215 O  O     . PHE B 1 127 ? 67.434  -15.66  39.02  1    30.43  ? 127 PHE B O     1 
ATOM   2216 C  CB    . PHE B 1 127 ? 69.464  -14.932 36.531 1    26.68  ? 127 PHE B CB    1 
ATOM   2217 C  CG    . PHE B 1 127 ? 68.432  -13.886 36.174 1    25.31  ? 127 PHE B CG    1 
ATOM   2218 C  CD1   . PHE B 1 127 ? 67.11   -14.237 35.952 1    25.45  ? 127 PHE B CD1   1 
ATOM   2219 C  CD2   . PHE B 1 127 ? 68.808  -12.585 35.913 1    24.76  ? 127 PHE B CD2   1 
ATOM   2220 C  CE1   . PHE B 1 127 ? 66.176  -13.284 35.577 1    25     ? 127 PHE B CE1   1 
ATOM   2221 C  CE2   . PHE B 1 127 ? 67.868  -11.638 35.541 1    24.64  ? 127 PHE B CE2   1 
ATOM   2222 C  CZ    . PHE B 1 127 ? 66.56   -11.993 35.379 1    24.19  ? 127 PHE B CZ    1 
ATOM   2223 N  N     . ALA B 1 128 ? 68.304  -17.491 38.02  1    31.43  ? 128 ALA B N     1 
ATOM   2224 C  CA    . ALA B 1 128 ? 67.186  -18.375 38.362 1    32.64  ? 128 ALA B CA    1 
ATOM   2225 C  C     . ALA B 1 128 ? 66.972  -18.513 39.862 1    33.27  ? 128 ALA B C     1 
ATOM   2226 O  O     . ALA B 1 128 ? 65.825  -18.614 40.298 1    33.82  ? 128 ALA B O     1 
ATOM   2227 C  CB    . ALA B 1 128 ? 67.379  -19.743 37.747 1    33.57  ? 128 ALA B CB    1 
ATOM   2228 N  N     . SER B 1 129 ? 68.052  -18.503 40.668 1    32.83  ? 129 SER B N     1 
ATOM   2229 C  CA    . SER B 1 129 ? 67.898  -18.612 42.121 1    32.11  ? 129 SER B CA    1 
ATOM   2230 C  C     . SER B 1 129 ? 67.123  -17.443 42.728 1    31.75  ? 129 SER B C     1 
ATOM   2231 O  O     . SER B 1 129 ? 66.417  -17.63  43.725 1    32.36  ? 129 SER B O     1 
ATOM   2232 C  CB    . SER B 1 129 ? 69.238  -18.822 42.813 1    32.54  ? 129 SER B CB    1 
ATOM   2233 O  OG    . SER B 1 129 ? 70.174  -17.819 42.476 1    34.57  ? 129 SER B OG    1 
ATOM   2234 N  N     . VAL B 1 130 ? 67.218  -16.255 42.122 1    30.78  ? 130 VAL B N     1 
ATOM   2235 C  CA    . VAL B 1 130 ? 66.485  -15.1   42.612 1    30.72  ? 130 VAL B CA    1 
ATOM   2236 C  C     . VAL B 1 130 ? 65.167  -14.934 41.848 1    32.44  ? 130 VAL B C     1 
ATOM   2237 O  O     . VAL B 1 130 ? 64.137  -14.653 42.447 1    32.77  ? 130 VAL B O     1 
ATOM   2238 C  CB    . VAL B 1 130 ? 67.351  -13.831 42.627 1    29.91  ? 130 VAL B CB    1 
ATOM   2239 C  CG1   . VAL B 1 130 ? 66.58   -12.653 43.193 1    29.95  ? 130 VAL B CG1   1 
ATOM   2240 C  CG2   . VAL B 1 130 ? 68.615  -14.064 43.438 1    29.84  ? 130 VAL B CG2   1 
ATOM   2241 N  N     . TYR B 1 131 ? 65.172  -15.19  40.55  1    33.7   ? 131 TYR B N     1 
ATOM   2242 C  CA    . TYR B 1 131 ? 63.976  -15.067 39.715 1    35.12  ? 131 TYR B CA    1 
ATOM   2243 C  C     . TYR B 1 131 ? 62.919  -16.133 40.062 1    38.47  ? 131 TYR B C     1 
ATOM   2244 O  O     . TYR B 1 131 ? 61.794  -15.783 40.42  1    38.52  ? 131 TYR B O     1 
ATOM   2245 C  CB    . TYR B 1 131 ? 64.352  -15.049 38.225 1    33.35  ? 131 TYR B CB    1 
ATOM   2246 C  CG    . TYR B 1 131 ? 63.159  -14.992 37.301 1    32.31  ? 131 TYR B CG    1 
ATOM   2247 C  CD1   . TYR B 1 131 ? 62.332  -13.88  37.265 1    32.31  ? 131 TYR B CD1   1 
ATOM   2248 C  CD2   . TYR B 1 131 ? 62.865  -16.043 36.447 1    32.6   ? 131 TYR B CD2   1 
ATOM   2249 C  CE1   . TYR B 1 131 ? 61.21   -13.837 36.437 1    32.77  ? 131 TYR B CE1   1 
ATOM   2250 C  CE2   . TYR B 1 131 ? 61.757  -16.005 35.603 1    32.98  ? 131 TYR B CE2   1 
ATOM   2251 C  CZ    . TYR B 1 131 ? 60.926  -14.903 35.605 1    33.57  ? 131 TYR B CZ    1 
ATOM   2252 O  OH    . TYR B 1 131 ? 59.833  -14.871 34.774 1    34.98  ? 131 TYR B OH    1 
ATOM   2253 N  N     . ARG B 1 132 ? 63.297  -17.419 40.021 1    40.84  ? 132 ARG B N     1 
ATOM   2254 C  CA    . ARG B 1 132 ? 62.402  -18.515 40.404 1    43.54  ? 132 ARG B CA    1 
ATOM   2255 C  C     . ARG B 1 132 ? 62.338  -18.718 41.932 1    45.68  ? 132 ARG B C     1 
ATOM   2256 O  O     . ARG B 1 132 ? 61.689  -19.663 42.396 1    45.91  ? 132 ARG B O     1 
ATOM   2257 C  CB    . ARG B 1 132 ? 62.826  -19.828 39.728 1    46.06  ? 132 ARG B CB    1 
ATOM   2258 C  CG    . ARG B 1 132 ? 62.507  -19.902 38.25  1    51.25  ? 132 ARG B CG    1 
ATOM   2259 C  CD    . ARG B 1 132 ? 62.295  -21.343 37.808 1    57     ? 132 ARG B CD    1 
ATOM   2260 N  NE    . ARG B 1 132 ? 63.526  -22.143 37.839 1    61.92  ? 132 ARG B NE    1 
ATOM   2261 C  CZ    . ARG B 1 132 ? 64.307  -22.363 36.779 1    64.57  ? 132 ARG B CZ    1 
ATOM   2262 N  NH1   . ARG B 1 132 ? 63.986  -21.86  35.593 1    63.56  ? 132 ARG B NH1   1 
ATOM   2263 N  NH2   . ARG B 1 132 ? 65.396  -23.117 36.893 1    64.72  ? 132 ARG B NH2   1 
ATOM   2264 N  N     . SER B 1 133 ? 63.029  -17.837 42.699 1    46.85  ? 133 SER B N     1 
ATOM   2265 C  CA    . SER B 1 133 ? 63.129  -17.775 44.146 1    47.99  ? 133 SER B CA    1 
ATOM   2266 C  C     . SER B 1 133 ? 63.313  -19.13  44.78  1    49.8   ? 133 SER B C     1 
ATOM   2267 O  O     . SER B 1 133 ? 62.335  -19.729 45.216 1    50.06  ? 133 SER B O     1 
ATOM   2268 C  CB    . SER B 1 133 ? 61.927  -17.052 44.735 1    48.73  ? 133 SER B CB    1 
ATOM   2269 O  OG    . SER B 1 133 ? 62.119  -16.877 46.127 1    50.1   ? 133 SER B OG    1 
ATOM   2270 N  N     . PHE B 1 134 ? 64.553  -19.635 44.822 1    51.08  ? 134 PHE B N     1 
ATOM   2271 C  CA    . PHE B 1 134 ? 64.823  -20.939 45.434 1    53.14  ? 134 PHE B CA    1 
ATOM   2272 C  C     . PHE B 1 134 ? 64.662  -20.754 46.936 1    55.27  ? 134 PHE B C     1 
ATOM   2273 O  O     . PHE B 1 134 ? 65.301  -19.863 47.496 1    55.22  ? 134 PHE B O     1 
ATOM   2274 C  CB    . PHE B 1 134 ? 66.254  -21.408 45.131 1    53.09  ? 134 PHE B CB    1 
ATOM   2275 C  CG    . PHE B 1 134 ? 66.633  -21.669 43.689 1    53.66  ? 134 PHE B CG    1 
ATOM   2276 C  CD1   . PHE B 1 134 ? 65.696  -21.563 42.676 1    54.24  ? 134 PHE B CD1   1 
ATOM   2277 C  CD2   . PHE B 1 134 ? 67.925  -22.036 43.353 1    54.52  ? 134 PHE B CD2   1 
ATOM   2278 C  CE1   . PHE B 1 134 ? 66.058  -21.777 41.355 1    54.76  ? 134 PHE B CE1   1 
ATOM   2279 C  CE2   . PHE B 1 134 ? 68.283  -22.253 42.031 1    55.02  ? 134 PHE B CE2   1 
ATOM   2280 C  CZ    . PHE B 1 134 ? 67.353  -22.105 41.042 1    54.56  ? 134 PHE B CZ    1 
ATOM   2281 N  N     . GLU B 1 135 ? 63.77   -21.528 47.579 1    57.13  ? 135 GLU B N     1 
ATOM   2282 C  CA    . GLU B 1 135 ? 63.5    -21.335 49.007 1    59.47  ? 135 GLU B CA    1 
ATOM   2283 C  C     . GLU B 1 135 ? 64.313  -22.246 49.946 1    62.02  ? 135 GLU B C     1 
ATOM   2284 O  O     . GLU B 1 135 ? 64.365  -21.984 51.148 1    61.89  ? 135 GLU B O     1 
ATOM   2285 C  CB    . GLU B 1 135 ? 61.998  -21.428 49.297 1    61.27  ? 135 GLU B CB    1 
ATOM   2286 C  CG    . GLU B 1 135 ? 61.157  -20.473 48.454 1    65.62  ? 135 GLU B CG    1 
ATOM   2287 C  CD    . GLU B 1 135 ? 61.129  -18.998 48.835 1    71.98  ? 135 GLU B CD    1 
ATOM   2288 O  OE1   . GLU B 1 135 ? 61.735  -18.621 49.866 1    73.59  ? 135 GLU B OE1   1 
ATOM   2289 O  OE2   . GLU B 1 135 ? 60.487  -18.214 48.099 1    73.74  ? 135 GLU B OE2   1 
ATOM   2290 N  N     . ASP B 1 136 ? 64.96   -23.275 49.413 1    64.34  ? 136 ASP B N     1 
ATOM   2291 C  CA    . ASP B 1 136 ? 65.831  -24.128 50.221 1    67.26  ? 136 ASP B CA    1 
ATOM   2292 C  C     . ASP B 1 136 ? 67.073  -24.547 49.385 1    69.6   ? 136 ASP B C     1 
ATOM   2293 O  O     . ASP B 1 136 ? 67.139  -24.246 48.193 1    69.77  ? 136 ASP B O     1 
ATOM   2294 C  CB    . ASP B 1 136 ? 65.065  -25.285 50.913 1    69.87  ? 136 ASP B CB    1 
ATOM   2295 C  CG    . ASP B 1 136 ? 65.101  -26.663 50.266 1    76.37  ? 136 ASP B CG    1 
ATOM   2296 O  OD1   . ASP B 1 136 ? 65.026  -26.741 49.011 1    76.93  ? 136 ASP B OD1   1 
ATOM   2297 O  OD2   . ASP B 1 136 ? 65.177  -27.669 51.015 1    79.58  ? 136 ASP B OD2   1 
ATOM   2298 N  N     . ILE B 1 137 ? 68.087  -25.144 50.019 1    71.38  ? 137 ILE B N     1 
ATOM   2299 C  CA    . ILE B 1 137 ? 69.344  -25.473 49.353 1    73.62  ? 137 ILE B CA    1 
ATOM   2300 C  C     . ILE B 1 137 ? 69.213  -26.662 48.341 1    76.26  ? 137 ILE B C     1 
ATOM   2301 O  O     . ILE B 1 137 ? 69.994  -26.737 47.386 1    76.53  ? 137 ILE B O     1 
ATOM   2302 C  CB    . ILE B 1 137 ? 70.456  -25.656 50.425 1    74.11  ? 137 ILE B CB    1 
ATOM   2303 C  CG1   . ILE B 1 137 ? 71.815  -26.003 49.795 1    75     ? 137 ILE B CG1   1 
ATOM   2304 C  CG2   . ILE B 1 137 ? 70.055  -26.642 51.524 1    74.6   ? 137 ILE B CG2   1 
ATOM   2305 C  CD1   . ILE B 1 137 ? 72.974  -25.988 50.751 1    76.24  ? 137 ILE B CD1   1 
ATOM   2306 N  N     . LYS B 1 138 ? 68.174  -27.509 48.475 1    77.99  ? 138 LYS B N     1 
ATOM   2307 C  CA    . LYS B 1 138 ? 67.927  -28.614 47.535 1    79.98  ? 138 LYS B CA    1 
ATOM   2308 C  C     . LYS B 1 138 ? 67.52   -28.078 46.168 1    81.71  ? 138 LYS B C     1 
ATOM   2309 O  O     . LYS B 1 138 ? 67.981  -28.583 45.141 1    81.82  ? 138 LYS B O     1 
ATOM   2310 C  CB    . LYS B 1 138 ? 66.835  -29.56  48.067 1    82.12  ? 138 LYS B CB    1 
ATOM   2311 C  CG    . LYS B 1 138 ? 67.107  -30.099 49.472 1    85.92  ? 138 LYS B CG    1 
ATOM   2312 C  CD    . LYS B 1 138 ? 66.185  -31.271 49.804 1    89.95  ? 138 LYS B CD    1 
ATOM   2313 C  CE    . LYS B 1 138 ? 66.498  -31.909 51.139 1    93.15  ? 138 LYS B CE    1 
ATOM   2314 N  NZ    . LYS B 1 138 ? 65.767  -33.192 51.327 1    94.66  ? 138 LYS B NZ    1 
ATOM   2315 N  N     . ASP B 1 139 ? 66.698  -27.012 46.15  1    82.98  ? 139 ASP B N     1 
ATOM   2316 C  CA    . ASP B 1 139 ? 66.227  -26.356 44.923 1    84.66  ? 139 ASP B CA    1 
ATOM   2317 C  C     . ASP B 1 139 ? 67.381  -26.02  43.979 1    86.25  ? 139 ASP B C     1 
ATOM   2318 O  O     . ASP B 1 139 ? 67.223  -26.118 42.766 1    86.51  ? 139 ASP B O     1 
ATOM   2319 C  CB    . ASP B 1 139 ? 65.447  -25.069 45.249 1    86.46  ? 139 ASP B CB    1 
ATOM   2320 C  CG    . ASP B 1 139 ? 64.06   -25.267 45.834 1    91.22  ? 139 ASP B CG    1 
ATOM   2321 O  OD1   . ASP B 1 139 ? 63.874  -26.232 46.622 1    91.67  ? 139 ASP B OD1   1 
ATOM   2322 O  OD2   . ASP B 1 139 ? 63.166  -24.446 45.525 1    93.45  ? 139 ASP B OD2   1 
ATOM   2323 N  N     . PHE B 1 140 ? 68.546  -25.663 44.538 1    87.16  ? 140 PHE B N     1 
ATOM   2324 C  CA    . PHE B 1 140 ? 69.721  -25.335 43.739 1    88.5   ? 140 PHE B CA    1 
ATOM   2325 C  C     . PHE B 1 140 ? 70.169  -26.519 42.868 1    90.67  ? 140 PHE B C     1 
ATOM   2326 O  O     . PHE B 1 140 ? 70.319  -26.366 41.653 1    90.77  ? 140 PHE B O     1 
ATOM   2327 C  CB    . PHE B 1 140 ? 70.871  -24.865 44.642 1    87.79  ? 140 PHE B CB    1 
ATOM   2328 C  CG    . PHE B 1 140 ? 71.027  -23.374 44.78  1    87.5   ? 140 PHE B CG    1 
ATOM   2329 C  CD1   . PHE B 1 140 ? 71.684  -22.635 43.81  1    87.82  ? 140 PHE B CD1   1 
ATOM   2330 C  CD2   . PHE B 1 140 ? 70.567  -22.718 45.902 1    87.7   ? 140 PHE B CD2   1 
ATOM   2331 C  CE1   . PHE B 1 140 ? 71.85   -21.271 43.955 1    88.24  ? 140 PHE B CE1   1 
ATOM   2332 C  CE2   . PHE B 1 140 ? 70.739  -21.357 46.042 1    88.15  ? 140 PHE B CE2   1 
ATOM   2333 C  CZ    . PHE B 1 140 ? 71.38   -20.642 45.071 1    87.93  ? 140 PHE B CZ    1 
ATOM   2334 N  N     . GLY B 1 141 ? 70.337  -27.687 43.487 1    92.08  ? 141 GLY B N     1 
ATOM   2335 C  CA    . GLY B 1 141 ? 70.769  -28.888 42.784 1    93.79  ? 141 GLY B CA    1 
ATOM   2336 C  C     . GLY B 1 141 ? 69.763  -29.376 41.764 1    95.18  ? 141 GLY B C     1 
ATOM   2337 O  O     . GLY B 1 141 ? 70.144  -29.897 40.712 1    95.13  ? 141 GLY B O     1 
ATOM   2338 N  N     . GLU B 1 142 ? 68.469  -29.188 42.068 1    96.04  ? 142 GLU B N     1 
ATOM   2339 C  CA    . GLU B 1 142 ? 67.377  -29.589 41.192 1    97.01  ? 142 GLU B CA    1 
ATOM   2340 C  C     . GLU B 1 142 ? 67.36   -28.772 39.914 1    98.14  ? 142 GLU B C     1 
ATOM   2341 O  O     . GLU B 1 142 ? 67.005  -29.311 38.864 1    98.48  ? 142 GLU B O     1 
ATOM   2342 C  CB    . GLU B 1 142 ? 66.031  -29.496 41.927 1    98.73  ? 142 GLU B CB    1 
ATOM   2343 C  CG    . GLU B 1 142 ? 65.959  -30.399 43.146 1    102    ? 142 GLU B CG    1 
ATOM   2344 C  CD    . GLU B 1 142 ? 64.619  -30.43  43.858 1    106.52 ? 142 GLU B CD    1 
ATOM   2345 O  OE1   . GLU B 1 142 ? 63.643  -29.86  43.316 1    106.67 ? 142 GLU B OE1   1 
ATOM   2346 O  OE2   . GLU B 1 142 ? 64.542  -31.03  44.956 1    108.41 ? 142 GLU B OE2   1 
ATOM   2347 N  N     . GLU B 1 143 ? 67.743  -27.484 39.982 1    98.66  ? 143 GLU B N     1 
ATOM   2348 C  CA    . GLU B 1 143 ? 67.769  -26.652 38.773 1    99.83  ? 143 GLU B CA    1 
ATOM   2349 C  C     . GLU B 1 143 ? 69.085  -26.781 37.971 1    100.84 ? 143 GLU B C     1 
ATOM   2350 O  O     . GLU B 1 143 ? 69.163  -26.279 36.85  1    100.96 ? 143 GLU B O     1 
ATOM   2351 C  CB    . GLU B 1 143 ? 67.421  -25.194 39.068 1    102.09 ? 143 GLU B CB    1 
ATOM   2352 C  CG    . GLU B 1 143 ? 66.195  -25.044 39.951 1    107.09 ? 143 GLU B CG    1 
ATOM   2353 C  CD    . GLU B 1 143 ? 64.92   -25.735 39.516 1    113.5  ? 143 GLU B CD    1 
ATOM   2354 O  OE1   . GLU B 1 143 ? 64.232  -25.191 38.623 1    114.71 ? 143 GLU B OE1   1 
ATOM   2355 O  OE2   . GLU B 1 143 ? 64.585  -26.793 40.099 1    115.34 ? 143 GLU B OE2   1 
ATOM   2356 N  N     . ILE B 1 144 ? 70.099  -27.47  38.528 1    101.48 ? 144 ILE B N     1 
ATOM   2357 C  CA    . ILE B 1 144 ? 71.341  -27.801 37.833 1    102.64 ? 144 ILE B CA    1 
ATOM   2358 C  C     . ILE B 1 144 ? 71.048  -29.062 36.98  1    104.07 ? 144 ILE B C     1 
ATOM   2359 O  O     . ILE B 1 144 ? 71.36   -29.097 35.784 1    104.19 ? 144 ILE B O     1 
ATOM   2360 C  CB    . ILE B 1 144 ? 72.479  -28.068 38.85  1    102.93 ? 144 ILE B CB    1 
ATOM   2361 C  CG1   . ILE B 1 144 ? 72.829  -26.817 39.647 1    103.53 ? 144 ILE B CG1   1 
ATOM   2362 C  CG2   . ILE B 1 144 ? 73.711  -28.64  38.162 1    103.41 ? 144 ILE B CG2   1 
ATOM   2363 C  CD1   . ILE B 1 144 ? 73.558  -27.135 40.874 1    104.42 ? 144 ILE B CD1   1 
ATOM   2364 N  N     . ALA B 1 145 ? 70.408  -30.081 37.609 1    104.86 ? 145 ALA B N     1 
ATOM   2365 C  CA    . ALA B 1 145 ? 70.002  -31.337 36.985 1    105.97 ? 145 ALA B CA    1 
ATOM   2366 C  C     . ALA B 1 145 ? 69.051  -31.087 35.828 1    107.38 ? 145 ALA B C     1 
ATOM   2367 O  O     . ALA B 1 145 ? 69.122  -31.795 34.828 1    107.6  ? 145 ALA B O     1 
ATOM   2368 C  CB    . ALA B 1 145 ? 69.33   -32.228 38.014 1    106.03 ? 145 ALA B CB    1 
ATOM   2369 N  N     . ARG B 1 146 ? 68.168  -30.08  35.963 1    108.24 ? 146 ARG B N     1 
ATOM   2370 C  CA    . ARG B 1 146 ? 67.203  -29.691 34.939 1    109.73 ? 146 ARG B CA    1 
ATOM   2371 C  C     . ARG B 1 146 ? 67.873  -29.42  33.589 1    111.11 ? 146 ARG B C     1 
ATOM   2372 O  O     . ARG B 1 146 ? 67.375  -29.89  32.561 1    111.5  ? 146 ARG B O     1 
ATOM   2373 C  CB    . ARG B 1 146 ? 66.382  -28.481 35.398 1    111.05 ? 146 ARG B CB    1 
ATOM   2374 C  CG    . ARG B 1 146 ? 64.998  -28.851 35.934 1    113.9  ? 146 ARG B CG    1 
ATOM   2375 C  CD    . ARG B 1 146 ? 64.153  -27.632 36.288 1    116.79 ? 146 ARG B CD    1 
ATOM   2376 N  NE    . ARG B 1 146 ? 64.136  -26.624 35.221 1    119.15 ? 146 ARG B NE    1 
ATOM   2377 C  CZ    . ARG B 1 146 ? 63.35   -25.553 35.211 1    120.66 ? 146 ARG B CZ    1 
ATOM   2378 N  NH1   . ARG B 1 146 ? 62.492  -25.341 36.202 1    120.11 ? 146 ARG B NH1   1 
ATOM   2379 N  NH2   . ARG B 1 146 ? 63.406  -24.692 34.202 1    120.26 ? 146 ARG B NH2   1 
ATOM   2380 N  N     . LEU B 1 147 ? 69.017  -28.716 33.583 1    111.68 ? 147 LEU B N     1 
ATOM   2381 C  CA    . LEU B 1 147 ? 69.738  -28.469 32.335 1    112.74 ? 147 LEU B CA    1 
ATOM   2382 C  C     . LEU B 1 147 ? 70.526  -29.726 31.929 1    113.77 ? 147 LEU B C     1 
ATOM   2383 O  O     . LEU B 1 147 ? 71.703  -29.862 32.263 1    114.04 ? 147 LEU B O     1 
ATOM   2384 C  CB    . LEU B 1 147 ? 70.653  -27.249 32.47  1    112.9  ? 147 LEU B CB    1 
ATOM   2385 C  CG    . LEU B 1 147 ? 69.921  -25.927 32.648 1    114.25 ? 147 LEU B CG    1 
ATOM   2386 C  CD1   . LEU B 1 147 ? 70.442  -25.183 33.845 1    114.82 ? 147 LEU B CD1   1 
ATOM   2387 C  CD2   . LEU B 1 147 ? 70.003  -25.075 31.388 1    114.8  ? 147 LEU B CD2   1 
ATOM   2388 N  N     . GLU B 1 148 ? 69.854  -30.663 31.242 1    114.16 ? 148 GLU B N     1 
ATOM   2389 C  CA    . GLU B 1 148 ? 70.465  -31.92  30.833 1    115.11 ? 148 GLU B CA    1 
ATOM   2390 C  C     . GLU B 1 148 ? 71.437  -31.737 29.682 1    116.16 ? 148 GLU B C     1 
ATOM   2391 O  O     . GLU B 1 148 ? 71.071  -31.166 28.656 1    116.34 ? 148 GLU B O     1 
ATOM   2392 C  CB    . GLU B 1 148 ? 69.387  -32.939 30.458 1    117.15 ? 148 GLU B CB    1 
ATOM   2393 C  CG    . GLU B 1 148 ? 69.542  -34.25  31.199 1    121.82 ? 148 GLU B CG    1 
ATOM   2394 C  CD    . GLU B 1 148 ? 69.372  -34.104 32.697 1    127.99 ? 148 GLU B CD    1 
ATOM   2395 O  OE1   . GLU B 1 148 ? 68.303  -33.614 33.126 1    128.98 ? 148 GLU B OE1   1 
ATOM   2396 O  OE2   . GLU B 1 148 ? 70.311  -34.461 33.445 1    130.17 ? 148 GLU B OE2   1 
ATOM   2397 N  N     . ASP B 1 149 ? 72.674  -32.235 29.841 1    116.68 ? 149 ASP B N     1 
ATOM   2398 C  CA    . ASP B 1 149 ? 73.7    -32.126 28.799 1    117.52 ? 149 ASP B CA    1 
ATOM   2399 C  C     . ASP B 1 149 ? 74.213  -33.508 28.372 1    117.73 ? 149 ASP B C     1 
ATOM   2400 O  O     . ASP B 1 149 ? 74.6    -33.696 27.218 1    117.77 ? 149 ASP B O     1 
ATOM   2401 C  CB    . ASP B 1 149 ? 74.864  -31.232 29.274 1    119.53 ? 149 ASP B CB    1 
ATOM   2402 C  CG    . ASP B 1 149 ? 75.82   -30.818 28.171 1    124.31 ? 149 ASP B CG    1 
ATOM   2403 O  OD1   . ASP B 1 149 ? 75.619  -29.725 27.588 1    125.03 ? 149 ASP B OD1   1 
ATOM   2404 O  OD2   . ASP B 1 149 ? 76.774  -31.581 27.893 1    126.53 ? 149 ASP B OD2   1 
HETATM 2405 P  PG    . DTP C 2 .   ? 99.522  -26.35  25.656 1    46.41  ? 200 DTP A PG    1 
HETATM 2406 O  O1G   . DTP C 2 .   ? 100.577 -26.974 24.771 1    46.35  ? 200 DTP A O1G   1 
HETATM 2407 O  O2G   . DTP C 2 .   ? 98.49   -27.343 26.151 1    46.34  ? 200 DTP A O2G   1 
HETATM 2408 O  O3G   . DTP C 2 .   ? 100.106 -25.511 26.773 1    46.94  ? 200 DTP A O3G   1 
HETATM 2409 P  PB    . DTP C 2 .   ? 97.167  -25.196 24.265 1    45.95  ? 200 DTP A PB    1 
HETATM 2410 O  O1B   . DTP C 2 .   ? 97.005  -23.895 23.584 1    45.91  ? 200 DTP A O1B   1 
HETATM 2411 O  O2B   . DTP C 2 .   ? 96.247  -25.538 25.373 1    45.95  ? 200 DTP A O2B   1 
HETATM 2412 O  O3B   . DTP C 2 .   ? 98.682  -25.32  24.755 1    45.97  ? 200 DTP A O3B   1 
HETATM 2413 P  PA    . DTP C 2 .   ? 96.487  -27.858 23.098 1    46.73  ? 200 DTP A PA    1 
HETATM 2414 O  O1A   . DTP C 2 .   ? 97.401  -28.754 22.356 1    46.66  ? 200 DTP A O1A   1 
HETATM 2415 O  O2A   . DTP C 2 .   ? 95.98   -28.295 24.426 1    47.09  ? 200 DTP A O2A   1 
HETATM 2416 O  O3A   . DTP C 2 .   ? 97.142  -26.396 23.202 1    46.53  ? 200 DTP A O3A   1 
HETATM 2417 O  "O5'" . DTP C 2 .   ? 95.237  -27.552 22.15  1    45.9   ? 200 DTP A "O5'" 1 
HETATM 2418 C  "C5'" . DTP C 2 .   ? 94.283  -26.532 22.518 1    45.4   ? 200 DTP A "C5'" 1 
HETATM 2419 C  "C4'" . DTP C 2 .   ? 92.941  -26.876 21.927 1    45.12  ? 200 DTP A "C4'" 1 
HETATM 2420 O  "O4'" . DTP C 2 .   ? 93.013  -26.775 20.489 1    45.09  ? 200 DTP A "O4'" 1 
HETATM 2421 C  "C3'" . DTP C 2 .   ? 92.475  -28.303 22.187 1    45.02  ? 200 DTP A "C3'" 1 
HETATM 2422 O  "O3'" . DTP C 2 .   ? 91.846  -28.437 23.463 1    44.99  ? 200 DTP A "O3'" 1 
HETATM 2423 C  "C2'" . DTP C 2 .   ? 91.52   -28.538 21.024 1    44.79  ? 200 DTP A "C2'" 1 
HETATM 2424 C  "C1'" . DTP C 2 .   ? 92.156  -27.738 19.888 1    44.54  ? 200 DTP A "C1'" 1 
HETATM 2425 N  N9    . DTP C 2 .   ? 92.929  -28.52  18.931 1    43.73  ? 200 DTP A N9    1 
HETATM 2426 C  C8    . DTP C 2 .   ? 94.227  -28.946 19.04  1    43.39  ? 200 DTP A C8    1 
HETATM 2427 N  N7    . DTP C 2 .   ? 94.602  -29.768 18.089 1    43.37  ? 200 DTP A N7    1 
HETATM 2428 C  C5    . DTP C 2 .   ? 93.471  -29.89  17.294 1    43.51  ? 200 DTP A C5    1 
HETATM 2429 C  C6    . DTP C 2 .   ? 93.191  -30.659 16.147 1    43.39  ? 200 DTP A C6    1 
HETATM 2430 N  N6    . DTP C 2 .   ? 94.085  -31.441 15.535 1    43.39  ? 200 DTP A N6    1 
HETATM 2431 N  N1    . DTP C 2 .   ? 91.946  -30.583 15.627 1    43.33  ? 200 DTP A N1    1 
HETATM 2432 C  C2    . DTP C 2 .   ? 91.05   -29.787 16.216 1    43.29  ? 200 DTP A C2    1 
HETATM 2433 N  N3    . DTP C 2 .   ? 91.197  -29.018 17.297 1    43.57  ? 200 DTP A N3    1 
HETATM 2434 C  C4    . DTP C 2 .   ? 92.433  -29.12  17.799 1    43.72  ? 200 DTP A C4    1 
HETATM 2435 P  PB    . ADP D 3 .   ? 95.348  -26.897 29.07  1    48.14  ? 201 ADP A PB    1 
HETATM 2436 O  O1B   . ADP D 3 .   ? 95.519  -28.402 29.076 1    48.32  ? 201 ADP A O1B   1 
HETATM 2437 O  O2B   . ADP D 3 .   ? 95.185  -26.309 30.455 1    47.92  ? 201 ADP A O2B   1 
HETATM 2438 O  O3B   . ADP D 3 .   ? 96.417  -26.192 28.259 1    48.41  ? 201 ADP A O3B   1 
HETATM 2439 P  PA    . ADP D 3 .   ? 93.063  -27.002 27.099 1    45.04  ? 201 ADP A PA    1 
HETATM 2440 O  O1A   . ADP D 3 .   ? 91.707  -27.463 27.464 1    45.08  ? 201 ADP A O1A   1 
HETATM 2441 O  O2A   . ADP D 3 .   ? 93.915  -27.854 26.237 1    45.14  ? 201 ADP A O2A   1 
HETATM 2442 O  O3A   . ADP D 3 .   ? 93.882  -26.645 28.424 1    46.84  ? 201 ADP A O3A   1 
HETATM 2443 O  "O5'" . ADP D 3 .   ? 92.914  -25.546 26.479 1    43.82  ? 201 ADP A "O5'" 1 
HETATM 2444 C  "C5'" . ADP D 3 .   ? 91.598  -24.993 26.302 1    43.24  ? 201 ADP A "C5'" 1 
HETATM 2445 C  "C4'" . ADP D 3 .   ? 91.716  -23.702 25.53  1    42.88  ? 201 ADP A "C4'" 1 
HETATM 2446 O  "O4'" . ADP D 3 .   ? 92.647  -22.818 26.199 1    42.72  ? 201 ADP A "O4'" 1 
HETATM 2447 C  "C3'" . ADP D 3 .   ? 92.224  -23.828 24.095 1    42.49  ? 201 ADP A "C3'" 1 
HETATM 2448 O  "O3'" . ADP D 3 .   ? 91.546  -22.844 23.317 1    42.73  ? 201 ADP A "O3'" 1 
HETATM 2449 C  "C2'" . ADP D 3 .   ? 93.714  -23.511 24.249 1    42.23  ? 201 ADP A "C2'" 1 
HETATM 2450 O  "O2'" . ADP D 3 .   ? 94.318  -23.107 23.026 1    42.5   ? 201 ADP A "O2'" 1 
HETATM 2451 C  "C1'" . ADP D 3 .   ? 93.623  -22.386 25.271 1    42     ? 201 ADP A "C1'" 1 
HETATM 2452 N  N9    . ADP D 3 .   ? 94.845  -22.056 25.999 1    41.01  ? 201 ADP A N9    1 
HETATM 2453 C  C8    . ADP D 3 .   ? 95.62   -22.878 26.777 1    40.46  ? 201 ADP A C8    1 
HETATM 2454 N  N7    . ADP D 3 .   ? 96.62   -22.268 27.367 1    40.11  ? 201 ADP A N7    1 
HETATM 2455 C  C5    . ADP D 3 .   ? 96.495  -20.951 26.951 1    40.03  ? 201 ADP A C5    1 
HETATM 2456 C  C6    . ADP D 3 .   ? 97.235  -19.787 27.243 1    39.55  ? 201 ADP A C6    1 
HETATM 2457 N  N6    . ADP D 3 .   ? 98.313  -19.763 28.035 1    38.55  ? 201 ADP A N6    1 
HETATM 2458 N  N1    . ADP D 3 .   ? 96.825  -18.627 26.682 1    40.11  ? 201 ADP A N1    1 
HETATM 2459 C  C2    . ADP D 3 .   ? 95.749  -18.64  25.886 1    40.3   ? 201 ADP A C2    1 
HETATM 2460 N  N3    . ADP D 3 .   ? 94.977  -19.672 25.536 1    40.4   ? 201 ADP A N3    1 
HETATM 2461 C  C4    . ADP D 3 .   ? 95.405  -20.806 26.106 1    40.5   ? 201 ADP A C4    1 
HETATM 2462 ZN ZN    . ZN  E 4 .   ? 108.661 16.728  49.282 1    89.6   2 202 ZN  A ZN    1 
HETATM 2463 MG MG    . MG  F 5 .   ? 96.419  -27.342 26.041 0.49 34.09  2 203 MG  A MG    1 
HETATM 2464 P  PG    . DTP G 2 .   ? 62.196  -4.126  41.296 1    30.19  ? 200 DTP B PG    1 
HETATM 2465 O  O1G   . DTP G 2 .   ? 61.081  -3.2    40.865 1    30.7   ? 200 DTP B O1G   1 
HETATM 2466 O  O2G   . DTP G 2 .   ? 63.075  -3.54   42.38  1    30.3   ? 200 DTP B O2G   1 
HETATM 2467 O  O3G   . DTP G 2 .   ? 61.727  -5.536  41.595 1    29.88  ? 200 DTP B O3G   1 
HETATM 2468 P  PB    . DTP G 2 .   ? 63.917  -5.525  39.387 1    29.28  ? 200 DTP B PB    1 
HETATM 2469 O  O1B   . DTP G 2 .   ? 64.784  -5.036  38.292 1    28.89  ? 200 DTP B O1B   1 
HETATM 2470 O  O2B   . DTP G 2 .   ? 62.881  -6.553  39.133 1    29.75  ? 200 DTP B O2B   1 
HETATM 2471 O  O3B   . DTP G 2 .   ? 63.192  -4.276  40.067 1    29.72  ? 200 DTP B O3B   1 
HETATM 2472 P  PA    . DTP G 2 .   ? 64.916  -7.483  41.358 1    27.51  ? 200 DTP B PA    1 
HETATM 2473 O  O1A   . DTP G 2 .   ? 65.618  -7.233  42.634 1    27.01  ? 200 DTP B O1A   1 
HETATM 2474 O  O2A   . DTP G 2 .   ? 63.6    -8.168  41.366 1    27.05  ? 200 DTP B O2A   1 
HETATM 2475 O  O3A   . DTP G 2 .   ? 64.805  -6.081  40.594 1    28.61  ? 200 DTP B O3A   1 
HETATM 2476 O  "O5'" . DTP G 2 .   ? 65.946  -8.252  40.4   1    27.29  ? 200 DTP B "O5'" 1 
HETATM 2477 C  "C5'" . DTP G 2 .   ? 65.55   -8.65   39.066 1    26.9   ? 200 DTP B "C5'" 1 
HETATM 2478 C  "C4'" . DTP G 2 .   ? 66.223  -9.934  38.646 1    26.36  ? 200 DTP B "C4'" 1 
HETATM 2479 O  "O4'" . DTP G 2 .   ? 67.656  -9.776  38.678 1    25.92  ? 200 DTP B "O4'" 1 
HETATM 2480 C  "C3'" . DTP G 2 .   ? 65.948  -11.139 39.535 1    26.53  ? 200 DTP B "C3'" 1 
HETATM 2481 O  "O3'" . DTP G 2 .   ? 64.746  -11.773 39.107 1    27.17  ? 200 DTP B "O3'" 1 
HETATM 2482 C  "C2'" . DTP G 2 .   ? 67.153  -12.021 39.248 1    26.01  ? 200 DTP B "C2'" 1 
HETATM 2483 C  "C1'" . DTP G 2 .   ? 68.273  -11.01  39.023 1    25.85  ? 200 DTP B "C1'" 1 
HETATM 2484 N  N9    . DTP G 2 .   ? 69.142  -10.803 40.176 1    25.9   ? 200 DTP B N9    1 
HETATM 2485 C  C8    . DTP G 2 .   ? 68.953  -9.952  41.234 1    25.35  ? 200 DTP B C8    1 
HETATM 2486 N  N7    . DTP G 2 .   ? 69.793  -10.132 42.222 1    25.12  ? 200 DTP B N7    1 
HETATM 2487 C  C5    . DTP G 2 .   ? 70.596  -11.175 41.786 1    25.58  ? 200 DTP B C5    1 
HETATM 2488 C  C6    . DTP G 2 .   ? 71.641  -11.893 42.403 1    25.84  ? 200 DTP B C6    1 
HETATM 2489 N  N6    . DTP G 2 .   ? 72.029  -11.701 43.673 1    25.84  ? 200 DTP B N6    1 
HETATM 2490 N  N1    . DTP G 2 .   ? 72.204  -12.906 41.707 1    25.73  ? 200 DTP B N1    1 
HETATM 2491 C  C2    . DTP G 2 .   ? 71.737  -13.186 40.488 1    26.04  ? 200 DTP B C2    1 
HETATM 2492 N  N3    . DTP G 2 .   ? 70.754  -12.589 39.809 1    26.22  ? 200 DTP B N3    1 
HETATM 2493 C  C4    . DTP G 2 .   ? 70.212  -11.593 40.522 1    26.04  ? 200 DTP B C4    1 
HETATM 2494 P  PB    . ADP H 3 .   ? 59.022  -7.849  39.682 1    25.6   ? 201 ADP B PB    1 
HETATM 2495 O  O1B   . ADP H 3 .   ? 60.162  -7.035  40.258 1    25.11  ? 201 ADP B O1B   1 
HETATM 2496 O  O2B   . ADP H 3 .   ? 58.156  -8.512  40.734 1    26.28  ? 201 ADP B O2B   1 
HETATM 2497 O  O3B   . ADP H 3 .   ? 58.213  -7.093  38.65  1    25.58  ? 201 ADP B O3B   1 
HETATM 2498 P  PA    . ADP H 3 .   ? 60.916  -9.953  38.719 1    25.71  ? 201 ADP B PA    1 
HETATM 2499 O  O1A   . ADP H 3 .   ? 60.516  -11.341 38.4   1    25.93  ? 201 ADP B O1A   1 
HETATM 2500 O  O2A   . ADP H 3 .   ? 61.784  -9.674  39.895 1    26.13  ? 201 ADP B O2A   1 
HETATM 2501 O  O3A   . ADP H 3 .   ? 59.604  -9.05   38.802 1    25.6   ? 201 ADP B O3A   1 
HETATM 2502 O  "O5'" . ADP H 3 .   ? 61.555  -9.35   37.405 1    24.88  ? 201 ADP B "O5'" 1 
HETATM 2503 C  "C5'" . ADP H 3 .   ? 61.751  -10.211 36.262 1    24.19  ? 201 ADP B "C5'" 1 
HETATM 2504 C  "C4'" . ADP H 3 .   ? 62.561  -9.474  35.225 1    22.77  ? 201 ADP B "C4'" 1 
HETATM 2505 O  "O4'" . ADP H 3 .   ? 61.917  -8.222  34.905 1    22.12  ? 201 ADP B "O4'" 1 
HETATM 2506 C  "C3'" . ADP H 3 .   ? 63.985  -9.113  35.648 1    22.1   ? 201 ADP B "C3'" 1 
HETATM 2507 O  "O3'" . ADP H 3 .   ? 64.794  -9.233  34.484 1    22.39  ? 201 ADP B "O3'" 1 
HETATM 2508 C  "C2'" . ADP H 3 .   ? 63.838  -7.662  36.115 1    20.92  ? 201 ADP B "C2'" 1 
HETATM 2509 O  "O2'" . ADP H 3 .   ? 65.064  -6.945  36.1   1    19.94  ? 201 ADP B "O2'" 1 
HETATM 2510 C  "C1'" . ADP H 3 .   ? 62.847  -7.172  35.075 1    21.66  ? 201 ADP B "C1'" 1 
HETATM 2511 N  N9    . ADP H 3 .   ? 62.128  -5.944  35.389 1    21.82  ? 201 ADP B N9    1 
HETATM 2512 C  C8    . ADP H 3 .   ? 61.352  -5.661  36.483 1    21.52  ? 201 ADP B C8    1 
HETATM 2513 N  N7    . ADP H 3 .   ? 60.777  -4.483  36.441 1    21.53  ? 201 ADP B N7    1 
HETATM 2514 C  C5    . ADP H 3 .   ? 61.204  -3.951  35.232 1    21.69  ? 201 ADP B C5    1 
HETATM 2515 C  C6    . ADP H 3 .   ? 60.928  -2.735  34.574 1    21.56  ? 201 ADP B C6    1 
HETATM 2516 N  N6    . ADP H 3 .   ? 60.148  -1.773  35.072 1    21.08  ? 201 ADP B N6    1 
HETATM 2517 N  N1    . ADP H 3 .   ? 61.493  -2.537  33.363 1    22.03  ? 201 ADP B N1    1 
HETATM 2518 C  C2    . ADP H 3 .   ? 62.276  -3.491  32.853 1    21.94  ? 201 ADP B C2    1 
HETATM 2519 N  N3    . ADP H 3 .   ? 62.612  -4.667  33.381 1    21.65  ? 201 ADP B N3    1 
HETATM 2520 C  C4    . ADP H 3 .   ? 62.039  -4.841  34.574 1    21.72  ? 201 ADP B C4    1 
HETATM 2521 ZN ZN    . ZN  I 4 .   ? 90.542  4.248   8.599  1    32.22  2 202 ZN  B ZN    1 
HETATM 2522 MG MG    . MG  J 5 .   ? 62.026  -7.24   40.722 0.49 19.88  2 203 MG  B MG    1 
HETATM 2523 O  O     . HOH K 6 .   ? 97.099  -28.752 27.193 1    5.05   ? 301 HOH A O     1 
HETATM 2524 O  O     . HOH K 6 .   ? 113.999 9.091   41.971 1    30.13  ? 302 HOH A O     1 
HETATM 2525 O  O     . HOH K 6 .   ? 84.275  -14.57  5.624  1    40.86  ? 303 HOH A O     1 
HETATM 2526 O  O     . HOH K 6 .   ? 86.364  -37.643 27.874 1    42.52  ? 304 HOH A O     1 
HETATM 2527 O  O     . HOH K 6 .   ? 102.131 -7.085  32.387 1    48.5   ? 305 HOH A O     1 
HETATM 2528 O  O     . HOH K 6 .   ? 100.086 -30.028 39.441 1    41.88  ? 306 HOH A O     1 
HETATM 2529 O  O     . HOH K 6 .   ? 78.947  -14.393 25.345 1    21.37  ? 307 HOH A O     1 
HETATM 2530 O  O     . HOH K 6 .   ? 99.626  -28.274 20.676 1    35.88  ? 308 HOH A O     1 
HETATM 2531 O  O     . HOH K 6 .   ? 89.222  -6.802  14.728 1    6.93   ? 309 HOH A O     1 
HETATM 2532 O  O     . HOH K 6 .   ? 79.006  -25.348 23.232 1    30.93  ? 310 HOH A O     1 
HETATM 2533 O  O     . HOH K 6 .   ? 98.895  -12.946 31.329 1    18.61  ? 311 HOH A O     1 
HETATM 2534 O  O     . HOH K 6 .   ? 109.832 1.287   58.107 1    32.65  ? 312 HOH A O     1 
HETATM 2535 O  O     . HOH K 6 .   ? 96.659  -7.329  36.958 1    34.63  ? 313 HOH A O     1 
HETATM 2536 O  O     . HOH K 6 .   ? 81.972  -16.729 23.399 1    5.07   ? 314 HOH A O     1 
HETATM 2537 O  O     . HOH K 6 .   ? 90.817  -8.387  10.459 1    19.5   ? 315 HOH A O     1 
HETATM 2538 O  O     . HOH K 6 .   ? 103.982 8.117   56.408 1    29.24  ? 316 HOH A O     1 
HETATM 2539 O  O     . HOH K 6 .   ? 91.166  -23.176 5.453  1    32.01  ? 317 HOH A O     1 
HETATM 2540 O  O     . HOH K 6 .   ? 96.939  -17.034 43.394 1    25.43  ? 318 HOH A O     1 
HETATM 2541 O  O     . HOH K 6 .   ? 94.183  -17.427 43.476 1    21.51  ? 319 HOH A O     1 
HETATM 2542 O  O     . HOH K 6 .   ? 105.73  11.731  57.546 1    46.04  ? 320 HOH A O     1 
HETATM 2543 O  O     . HOH K 6 .   ? 102.851 21.988  47.234 1    24.42  ? 321 HOH A O     1 
HETATM 2544 O  O     . HOH K 6 .   ? 101.199 -28.615 13.783 1    23.52  ? 322 HOH A O     1 
HETATM 2545 O  O     . HOH K 6 .   ? 117.369 -0.142  52.708 1    39.2   ? 323 HOH A O     1 
HETATM 2546 O  O     . HOH K 6 .   ? 84.222  -5.633  33.834 1    22.02  ? 324 HOH A O     1 
HETATM 2547 O  O     . HOH K 6 .   ? 80.733  -8.321  33.8   1    5.83   ? 325 HOH A O     1 
HETATM 2548 O  O     . HOH K 6 .   ? 87.837  -34.447 29.655 1    33.3   ? 326 HOH A O     1 
HETATM 2549 O  O     . HOH K 6 .   ? 79.409  -25.233 8.908  1    22.73  ? 327 HOH A O     1 
HETATM 2550 O  O     . HOH K 6 .   ? 84.603  -6.146  28.186 1    11.58  ? 328 HOH A O     1 
HETATM 2551 O  O     . HOH K 6 .   ? 115.771 -3.131  51.858 1    27.01  ? 329 HOH A O     1 
HETATM 2552 O  O     . HOH K 6 .   ? 86.324  -3.77   25.628 1    27.55  ? 330 HOH A O     1 
HETATM 2553 O  O     . HOH K 6 .   ? 100.65  -9.908  30.742 1    9.9    ? 331 HOH A O     1 
HETATM 2554 O  O     . HOH K 6 .   ? 95.821  -9.141  17.431 1    28.44  ? 332 HOH A O     1 
HETATM 2555 O  O     . HOH K 6 .   ? 101.906 -21.211 19.172 1    42.64  ? 333 HOH A O     1 
HETATM 2556 O  O     . HOH K 6 .   ? 93.791  -7.794  34.784 1    16.8   ? 334 HOH A O     1 
HETATM 2557 O  O     . HOH K 6 .   ? 91.028  -8.314  33.396 1    16.29  ? 335 HOH A O     1 
HETATM 2558 O  O     . HOH K 6 .   ? 106.513 -12.991 52.377 1    34.19  ? 336 HOH A O     1 
HETATM 2559 O  O     . HOH K 6 .   ? 113.591 -6.681  47.161 1    32.28  ? 337 HOH A O     1 
HETATM 2560 O  O     . HOH K 6 .   ? 77.861  -16.83  23.543 1    20.24  ? 338 HOH A O     1 
HETATM 2561 O  O     . HOH K 6 .   ? 113.432 -7.586  49.489 1    51.47  ? 339 HOH A O     1 
HETATM 2562 O  O     . HOH K 6 .   ? 91.804  -21.087 7.396  1    27.69  ? 340 HOH A O     1 
HETATM 2563 O  O     . HOH K 6 .   ? 102.896 13.235  43.222 1    27.48  ? 341 HOH A O     1 
HETATM 2564 O  O     . HOH K 6 .   ? 114.788 23.288  51.323 1    35.63  ? 342 HOH A O     1 
HETATM 2565 O  O     . HOH K 6 .   ? 94.215  -14.658 42.527 1    40.54  ? 343 HOH A O     1 
HETATM 2566 O  O     . HOH K 6 .   ? 86.583  -24.131 1.409  1    40.72  ? 344 HOH A O     1 
HETATM 2567 O  O     . HOH K 6 .   ? 86.434  -7.828  16.209 1    25.63  ? 345 HOH A O     1 
HETATM 2568 O  O     . HOH K 6 .   ? 79.728  -18.009 8.717  1    28.19  ? 346 HOH A O     1 
HETATM 2569 O  O     . HOH K 6 .   ? 90.409  -10.595 41.06  1    5.51   ? 347 HOH A O     1 
HETATM 2570 O  O     . HOH K 6 .   ? 89.598  -28.818 30.326 1    23.68  ? 348 HOH A O     1 
HETATM 2571 O  O     . HOH K 6 .   ? 99.305  -28.553 29.893 1    30.37  ? 349 HOH A O     1 
HETATM 2572 O  O     . HOH K 6 .   ? 96.616  -20.271 45.113 1    23.34  ? 350 HOH A O     1 
HETATM 2573 O  O     . HOH K 6 .   ? 93.45   -6.589  36.988 1    36.97  ? 351 HOH A O     1 
HETATM 2574 O  O     . HOH K 6 .   ? 99.797  -31.389 30.659 1    44.52  ? 352 HOH A O     1 
HETATM 2575 O  O     . HOH K 6 .   ? 89.677  -17.199 3.119  1    29.28  ? 353 HOH A O     1 
HETATM 2576 O  O     . HOH K 6 .   ? 111.205 24.347  50.913 1    29.84  ? 354 HOH A O     1 
HETATM 2577 O  O     . HOH L 6 .   ? 58.726  -9.375  42.758 1    29.88  ? 301 HOH B O     1 
HETATM 2578 O  O     . HOH L 6 .   ? 61.143  -7.91   42.297 1    14.9   ? 302 HOH B O     1 
HETATM 2579 O  O     . HOH L 6 .   ? 87.291  4.182   4.393  1    11.27  ? 303 HOH B O     1 
HETATM 2580 O  O     . HOH L 6 .   ? 67.276  -8.065  34.921 1    3      ? 304 HOH B O     1 
HETATM 2581 O  O     . HOH L 6 .   ? 61.905  7.658   20.692 1    3      ? 305 HOH B O     1 
HETATM 2582 O  O     . HOH L 6 .   ? 87.808  13.067  8.559  1    40.26  ? 306 HOH B O     1 
HETATM 2583 O  O     . HOH L 6 .   ? 67.293  -6.615  11.243 1    34.17  ? 307 HOH B O     1 
HETATM 2584 O  O     . HOH L 6 .   ? 79.439  -5.156  40.564 1    16.85  ? 308 HOH B O     1 
HETATM 2585 O  O     . HOH L 6 .   ? 65.395  -0.591  20.917 1    26.46  ? 309 HOH B O     1 
HETATM 2586 O  O     . HOH L 6 .   ? 80.333  -15.743 27.228 1    3      ? 310 HOH B O     1 
HETATM 2587 O  O     . HOH L 6 .   ? 91.224  -1.342  2.583  1    21.65  ? 311 HOH B O     1 
HETATM 2588 O  O     . HOH L 6 .   ? 67.385  -4.954  38.596 1    31.34  ? 312 HOH B O     1 
HETATM 2589 O  O     . HOH L 6 .   ? 79.572  -0.888  -2.262 1    8.77   ? 313 HOH B O     1 
HETATM 2590 O  O     . HOH L 6 .   ? 65.085  -13.809 24.586 1    26.61  ? 314 HOH B O     1 
HETATM 2591 O  O     . HOH L 6 .   ? 69.818  -8.164  18.761 1    15.91  ? 315 HOH B O     1 
HETATM 2592 O  O     . HOH L 6 .   ? 64.859  -17.214 47.398 1    10.96  ? 316 HOH B O     1 
HETATM 2593 O  O     . HOH L 6 .   ? 83.282  -2.568  25.869 1    33.59  ? 317 HOH B O     1 
HETATM 2594 O  O     . HOH L 6 .   ? 62.51   -23.093 43.262 1    33.28  ? 318 HOH B O     1 
HETATM 2595 O  O     . HOH L 6 .   ? 66.283  -3.78   17.069 1    17.24  ? 319 HOH B O     1 
HETATM 2596 O  O     . HOH L 6 .   ? 75.659  -2.748  11.083 1    3.4    ? 320 HOH B O     1 
HETATM 2597 O  O     . HOH L 6 .   ? 96.513  3.598   2.172  1    35.66  ? 321 HOH B O     1 
HETATM 2598 O  O     . HOH L 6 .   ? 67.163  9.381   19.204 1    19.57  ? 322 HOH B O     1 
HETATM 2599 O  O     . HOH L 6 .   ? 61.171  -6.184  16.835 1    22.81  ? 323 HOH B O     1 
HETATM 2600 O  O     . HOH L 6 .   ? 74.199  -4.953  38.527 1    8.43   ? 324 HOH B O     1 
HETATM 2601 O  O     . HOH L 6 .   ? 61.003  -28.916 44.03  1    38.6   ? 325 HOH B O     1 
HETATM 2602 O  O     . HOH L 6 .   ? 79.057  7.06    5.936  1    20.19  ? 326 HOH B O     1 
HETATM 2603 O  O     . HOH L 6 .   ? 96.396  -3.47   9.061  1    51.1   ? 327 HOH B O     1 
HETATM 2604 O  O     . HOH L 6 .   ? 83.082  -9.052  16.802 1    28.36  ? 328 HOH B O     1 
HETATM 2605 O  O     . HOH L 6 .   ? 77.847  -3.496  0.350  1    3.07   ? 329 HOH B O     1 
HETATM 2606 O  O     . HOH L 6 .   ? 61.757  4.835   15.751 1    3      ? 330 HOH B O     1 
HETATM 2607 O  O     . HOH L 6 .   ? 57.465  -11.675 37.704 1    19.49  ? 331 HOH B O     1 
HETATM 2608 O  O     . HOH L 6 .   ? 71.285  -13.197 7.492  1    12.68  ? 332 HOH B O     1 
HETATM 2609 O  O     . HOH L 6 .   ? 72.176  -3.675  41.310 1    18.93  ? 333 HOH B O     1 
HETATM 2610 O  O     . HOH L 6 .   ? 59.539  -19.206 27.327 1    51.66  ? 334 HOH B O     1 
HETATM 2611 O  O     . HOH L 6 .   ? 76.974  -5.754  38.51  1    15.01  ? 335 HOH B O     1 
HETATM 2612 O  O     . HOH L 6 .   ? 79.233  7.759   0.396  1    36.94  ? 336 HOH B O     1 
HETATM 2613 O  O     . HOH L 6 .   ? 86.911  -11.46  4.388  1    24.97  ? 337 HOH B O     1 
HETATM 2614 O  O     . HOH L 6 .   ? 66.284  -3.307  19.681 1    4.86   ? 338 HOH B O     1 
HETATM 2615 O  O     . HOH L 6 .   ? 78.415  -21.24  29.676 1    21.21  ? 339 HOH B O     1 
HETATM 2616 O  O     . HOH L 6 .   ? 49.496  0.547   39.495 1    33.16  ? 340 HOH B O     1 
HETATM 2617 O  O     . HOH L 6 .   ? 78.953  -7.427  35.742 1    18.26  ? 341 HOH B O     1 
HETATM 2618 O  O     . HOH L 6 .   ? 92.079  -5.167  11.122 1    22.28  ? 342 HOH B O     1 
HETATM 2619 O  O     . HOH L 6 .   ? 69.632  -15.348 18.742 1    43.9   ? 343 HOH B O     1 
HETATM 2620 O  O     . HOH L 6 .   ? 82.635  -20.986 30.696 1    27.25  ? 344 HOH B O     1 
HETATM 2621 O  O     . HOH L 6 .   ? 54.511  -10.471 36.091 1    19.97  ? 345 HOH B O     1 
HETATM 2622 O  O     . HOH L 6 .   ? 51.06   -0.813  20.228 1    21.31  ? 346 HOH B O     1 
HETATM 2623 O  O     . HOH L 6 .   ? 56.323  -15.589 28.851 1    52.23  ? 347 HOH B O     1 
HETATM 2624 O  O     . HOH L 6 .   ? 64.981  -20.757 30.482 1    26.57  ? 348 HOH B O     1 
HETATM 2625 O  O     . HOH L 6 .   ? 93.764  5.577   15.992 1    8      ? 349 HOH B O     1 
HETATM 2626 O  O     . HOH L 6 .   ? 71.598  -10.054 19.905 1    23.01  ? 350 HOH B O     1 
HETATM 2627 O  O     . HOH L 6 .   ? 74.258  -2.011  21.503 1    7.06   ? 351 HOH B O     1 
HETATM 2628 O  O     . HOH L 6 .   ? 77.95   -2.328  20.388 1    11.05  ? 352 HOH B O     1 
HETATM 2629 O  O     . HOH L 6 .   ? 93.249  -5.706  8.367  1    43.87  ? 353 HOH B O     1 
HETATM 2630 O  O     . HOH L 6 .   ? 76.884  1.81    3.919  1    23.16  ? 354 HOH B O     1 
HETATM 2631 O  O     . HOH L 6 .   ? 72.288  -14.638 15.93  1    28.73  ? 355 HOH B O     1 
HETATM 2632 O  O     . HOH L 6 .   ? 78.769  -1.093  1.240  1    8.22   ? 356 HOH B O     1 
HETATM 2633 O  O     . HOH L 6 .   ? 79.354  -7.498  31.388 1    13.16  ? 357 HOH B O     1 
HETATM 2634 O  O     . HOH L 6 .   ? 95.896  1.476   0.829  1    35.67  ? 358 HOH B O     1 
HETATM 2635 O  O     . HOH L 6 .   ? 68.913  -5.376  40.734 1    17.93  ? 359 HOH B O     1 
HETATM 2636 O  O     . HOH L 6 .   ? 65.675  -16.528 22.847 1    28.64  ? 360 HOH B O     1 
HETATM 2637 O  O     . HOH L 6 .   ? 93.384  -6.021  5.845  1    34.61  ? 361 HOH B O     1 
HETATM 2638 O  O     . HOH L 6 .   ? 81.486  -18.812 29.132 1    17.97  ? 362 HOH B O     1 
HETATM 2639 O  O     . HOH L 6 .   ? 52.291  -2.785  16.482 1    27.02  ? 363 HOH B O     1 
HETATM 2640 O  O     . HOH L 6 .   ? 65.468  4.477   38.290 1    28.15  ? 364 HOH B O     1 
HETATM 2641 O  O     . HOH L 6 .   ? 74.889  -3.866  4.024  1    14.18  ? 365 HOH B O     1 
HETATM 2642 O  O     . HOH L 6 .   ? 87.798  10.791  3.692  1    17.68  ? 366 HOH B O     1 
HETATM 2643 O  O     . HOH L 6 .   ? 97.146  0.994   9.744  1    34.03  ? 367 HOH B O     1 
HETATM 2644 O  O     . HOH L 6 .   ? 73.025  -11.899 22.873 1    30.77  ? 368 HOH B O     1 
HETATM 2645 O  O     . HOH L 6 .   ? 78.069  -9.747  20.161 1    3      ? 369 HOH B O     1 
HETATM 2646 O  O     . HOH L 6 .   ? 57.612  2.137   17.62  1    5.24   ? 370 HOH B O     1 
HETATM 2647 O  O     . HOH L 6 .   ? 53.65   2.225   26.465 1    32.89  ? 371 HOH B O     1 
HETATM 2648 O  O     . HOH L 6 .   ? 72.418  -2.34   43.425 1    29.02  ? 372 HOH B O     1 
HETATM 2649 O  O     . HOH L 6 .   ? 86.930  8.819   14.584 1    35.22  ? 373 HOH B O     1 
HETATM 2650 O  O     . HOH L 6 .   ? 62.326  -9.983  15.328 1    18.61  ? 374 HOH B O     1 
HETATM 2651 O  O     . HOH L 6 .   ? 66.68   -3.627  42.766 1    25.62  ? 375 HOH B O     1 
HETATM 2652 O  O     . HOH L 6 .   ? 90.141  9.863   14.307 1    23.15  ? 376 HOH B O     1 
HETATM 2653 O  O     . HOH L 6 .   ? 77.738  -6.400  1.866  1    24.47  ? 377 HOH B O     1 
HETATM 2654 O  O     . HOH L 6 .   ? 76.558  -21.613 27.565 1    27.07  ? 378 HOH B O     1 
HETATM 2655 O  O     . HOH L 6 .   ? 58.188  -5.335  42.991 1    4.69   ? 379 HOH B O     1 
HETATM 2656 O  O     . HOH L 6 .   ? 91.482  -7.005  1.068  1    26.55  ? 380 HOH B O     1 
HETATM 2657 O  O     . HOH L 6 .   ? 69.303  -15.227 9.525  1    47.65  ? 381 HOH B O     1 
HETATM 2658 O  O     . HOH L 6 .   ? 62.872  -10.794 17.422 1    13.47  ? 382 HOH B O     1 
HETATM 2659 O  O     . HOH L 6 .   ? 60.776  5.705   19.767 1    19.26  ? 383 HOH B O     1 
HETATM 2660 O  O     . HOH L 6 .   ? 86.467  8.075   2.215  1    25.37  ? 384 HOH B O     1 
HETATM 2661 O  O     . HOH L 6 .   ? 62.662  -19.636 31.98  1    46.54  ? 385 HOH B O     1 
HETATM 2662 O  O     . HOH L 6 .   ? 80.293  -17.976 25.221 1    22.1   ? 386 HOH B O     1 
HETATM 2663 O  O     . HOH L 6 .   ? 96.547  -3.722  6.308  1    72.31  ? 387 HOH B O     1 
HETATM 2664 O  O     . HOH L 6 .   ? 53.149  1.905   20.249 1    29.74  ? 388 HOH B O     1 
HETATM 2665 O  O     . HOH L 6 .   ? 91.526  -7.653  12.921 1    28.02  ? 389 HOH B O     1 
HETATM 2666 O  O     . HOH L 6 .   ? 67.957  3.897   36.694 1    4.35   ? 390 HOH B O     1 
HETATM 2667 O  O     . HOH L 6 .   ? 81.828  -9.365  -0.534 1    32.25  ? 391 HOH B O     1 
HETATM 2668 O  O     . HOH L 6 .   ? 84.25   7.213   0.785  1    6.04   ? 392 HOH B O     1 
HETATM 2669 O  O     . HOH L 6 .   ? 53.456  0.203   22.033 1    7.72   ? 393 HOH B O     1 
HETATM 2670 O  O     . HOH L 6 .   ? 65.959  5.236   32.443 1    6.97   ? 394 HOH B O     1 
HETATM 2671 O  O     . HOH L 6 .   ? 67.799  -1.913  40.108 1    44.68  ? 395 HOH B O     1 
HETATM 2672 O  O     . HOH L 6 .   ? 93.871  -5.330  0.988  1    26.89  ? 396 HOH B O     1 
HETATM 2673 O  O     . HOH L 6 .   ? 98.477  -1.138  7.616  1    42.08  ? 397 HOH B O     1 
HETATM 2674 O  O     . HOH L 6 .   ? 69.458  -2.130  42.222 1    73.44  ? 398 HOH B O     1 
HETATM 2675 O  O     . HOH L 6 .   ? 96.942  -3.398  0.769  1    44.96  ? 399 HOH B O     1 
HETATM 2676 O  O     . HOH L 6 .   ? 70.537  -8.425  5.294  1    11.25  ? 400 HOH B O     1 
HETATM 2677 O  O     . HOH L 6 .   ? 94.543  3.117   11.55  1    23.13  ? 401 HOH B O     1 
HETATM 2678 O  O     . HOH L 6 .   ? 71.125  -0.294  41.219 1    55.99  ? 402 HOH B O     1 
HETATM 2679 O  O     . HOH L 6 .   ? 61.293  -30.176 51.826 1    28.88  ? 403 HOH B O     1 
HETATM 2680 O  O     . HOH L 6 .   ? 57.299  -17.194 41.441 1    36.11  ? 404 HOH B O     1 
HETATM 2681 O  O     . HOH L 6 .   ? 66.637  -15.797 10.868 1    35.43  ? 405 HOH B O     1 
HETATM 2682 O  O     . HOH L 6 .   ? 74.536  -11.178 18.777 1    24.9   ? 406 HOH B O     1 
HETATM 2683 O  O     . HOH L 6 .   ? 86.511  13.861  2.781  1    47.04  ? 407 HOH B 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     . MET A 1   ? 0.8732 1.1416 0.6773 -0.3093 0.13    -0.2897 1   MET A N     
2    C  CA    . MET A 1   ? 0.9453 1.0878 0.6735 -0.2969 0.1272  -0.2512 1   MET A CA    
3    C  C     . MET A 1   ? 0.9927 1.0595 0.6772 -0.3221 0.1218  -0.2543 1   MET A C     
4    O  O     . MET A 1   ? 0.9672 1.0832 0.684  -0.3377 0.1137  -0.2833 1   MET A O     
5    C  CB    . MET A 1   ? 0.951  1.0837 0.6785 -0.2294 0.1033  -0.2257 1   MET A CB    
6    C  CG    . MET A 1   ? 0.9495 1.1146 0.6998 -0.1945 0.0744  -0.236  1   MET A CG    
7    S  SD    . MET A 1   ? 0.9874 1.0922 0.7034 -0.1348 0.055   -0.2037 1   MET A SD    
8    C  CE    . MET A 1   ? 0.9168 1.0868 0.6687 -0.0983 0.0524  -0.1969 1   MET A CE    
9    N  N     . HIS A 2   ? 1.0616 1.0072 0.6714 -0.3244 0.1241  -0.2267 2   HIS A N     
10   C  CA    . HIS A 2   ? 1.12   0.9739 0.6764 -0.3431 0.117   -0.2271 2   HIS A CA    
11   C  C     . HIS A 2   ? 1.1055 0.9829 0.6858 -0.3032 0.0886  -0.2349 2   HIS A C     
12   O  O     . HIS A 2   ? 1.0971 0.994  0.6931 -0.25   0.0724  -0.2212 2   HIS A O     
13   C  CB    . HIS A 2   ? 1.2128 0.9352 0.6873 -0.331  0.1145  -0.1956 2   HIS A CB    
14   C  CG    . HIS A 2   ? 1.3225 0.9463 0.7228 -0.3892 0.1353  -0.1922 2   HIS A CG    
15   N  ND1   . HIS A 2   ? 1.3522 0.9851 0.7406 -0.4309 0.1656  -0.1904 2   HIS A ND1   
16   C  CD2   . HIS A 2   ? 1.4079 0.9138 0.7342 -0.4106 0.1295  -0.1898 2   HIS A CD2   
17   C  CE1   . HIS A 2   ? 1.4295 0.9454 0.7312 -0.4799 0.1788  -0.1852 2   HIS A CE1   
18   N  NE2   . HIS A 2   ? 1.4726 0.9055 0.733  -0.4684 0.1563  -0.1842 2   HIS A NE2   
19   N  N     . CYS A 3   ? 1.1043 0.9729 0.6808 -0.3316 0.0841  -0.2573 3   CYS A N     
20   C  CA    . CYS A 3   ? 1.097  0.9726 0.6827 -0.2995 0.0583  -0.2663 3   CYS A CA    
21   C  C     . CYS A 3   ? 1.138  0.9115 0.6676 -0.2644 0.0459  -0.2424 3   CYS A C     
22   O  O     . CYS A 3   ? 1.1914 0.863  0.6604 -0.2848 0.0514  -0.2329 3   CYS A O     
23   C  CB    . CYS A 3   ? 1.112  0.9928 0.7005 -0.3433 0.058   -0.2972 3   CYS A CB    
24   S  SG    . CYS A 3   ? 1.1961 1.0576 0.7756 -0.3104 0.028   -0.3081 3   CYS A SG    
25   N  N     . PRO A 4   ? 1.114  0.9116 0.6599 -0.2118 0.0286  -0.2354 4   PRO A N     
26   C  CA    . PRO A 4   ? 1.1524 0.8694 0.6563 -0.1771 0.0176  -0.2208 4   PRO A CA    
27   C  C     . PRO A 4   ? 1.1925 0.8432 0.6608 -0.1833 0.0054  -0.2356 4   PRO A C     
28   O  O     . PRO A 4   ? 1.2271 0.8126 0.6632 -0.1539 -0.0053 -0.2301 4   PRO A O     
29   C  CB    . PRO A 4   ? 1.1265 0.903  0.663  -0.1289 0.0082  -0.2151 4   PRO A CB    
30   C  CG    . PRO A 4   ? 1.0871 0.9539 0.6678 -0.1358 0.0038  -0.2325 4   PRO A CG    
31   C  CD    . PRO A 4   ? 1.0542 0.9498 0.6526 -0.1823 0.018   -0.243  4   PRO A CD    
32   N  N     . PHE A 5   ? 1.1841 0.8538 0.6606 -0.2199 0.0058  -0.2581 5   PHE A N     
33   C  CA    . PHE A 5   ? 1.221  0.83   0.6644 -0.227  -0.0063 -0.2748 5   PHE A CA    
34   C  C     . PHE A 5   ? 1.2844 0.811  0.6796 -0.2808 0.0034  -0.2808 5   PHE A C     
35   O  O     . PHE A 5   ? 1.3409 0.7584 0.6758 -0.2757 -0.0048 -0.2759 5   PHE A O     
36   C  CB    . PHE A 5   ? 1.1724 0.8576 0.654  -0.2214 -0.0182 -0.2989 5   PHE A CB    
37   C  CG    . PHE A 5   ? 1.1306 0.8935 0.6493 -0.1776 -0.0257 -0.293  5   PHE A CG    
38   C  CD1   . PHE A 5   ? 1.1452 0.8823 0.6494 -0.1339 -0.0305 -0.2797 5   PHE A CD1   
39   C  CD2   . PHE A 5   ? 1.0886 0.9474 0.6537 -0.1805 -0.0285 -0.3033 5   PHE A CD2   
40   C  CE1   . PHE A 5   ? 1.1215 0.919  0.6489 -0.1004 -0.0341 -0.2739 5   PHE A CE1   
41   C  CE2   . PHE A 5   ? 1.0682 0.9805 0.6521 -0.1403 -0.0376 -0.2962 5   PHE A CE2   
42   C  CZ    . PHE A 5   ? 1.0816 0.9588 0.6429 -0.1037 -0.0382 -0.2798 5   PHE A CZ    
43   N  N     . CYS A 6   ? 1.2757 0.8508 0.6941 -0.3328 0.0205  -0.2941 6   CYS A N     
44   C  CA    . CYS A 6   ? 1.3395 0.8349 0.7071 -0.3941 0.0343  -0.3032 6   CYS A CA    
45   C  C     . CYS A 6   ? 1.3926 0.8223 0.7129 -0.4209 0.0551  -0.2806 6   CYS A C     
46   O  O     . CYS A 6   ? 1.4634 0.7645 0.7019 -0.4442 0.0568  -0.2722 6   CYS A O     
47   C  CB    . CYS A 6   ? 1.3095 0.8849 0.7218 -0.444  0.0433  -0.3375 6   CYS A CB    
48   S  SG    . CYS A 6   ? 1.2872 0.9917 0.7703 -0.4785 0.0693  -0.3488 6   CYS A SG    
49   N  N     . PHE A 7   ? 1.3602 0.8745 0.7275 -0.4127 0.0683  -0.2708 7   PHE A N     
50   C  CA    . PHE A 7   ? 1.3974 0.8852 0.7388 -0.4263 0.0884  -0.2487 7   PHE A CA    
51   C  C     . PHE A 7   ? 1.3934 0.934  0.7535 -0.4958 0.1225  -0.2654 7   PHE A C     
52   O  O     . PHE A 7   ? 1.4336 0.9131 0.7418 -0.5272 0.1443  -0.2498 7   PHE A O     
53   C  CB    . PHE A 7   ? 1.4818 0.8148 0.7252 -0.4169 0.0813  -0.2228 7   PHE A CB    
54   C  CG    . PHE A 7   ? 1.4931 0.8099 0.7396 -0.3415 0.0535  -0.207  7   PHE A CG    
55   C  CD1   . PHE A 7   ? 1.4762 0.8412 0.7525 -0.3036 0.0543  -0.1886 7   PHE A CD1   
56   C  CD2   . PHE A 7   ? 1.5286 0.7883 0.752  -0.3106 0.0281  -0.2149 7   PHE A CD2   
57   C  CE1   . PHE A 7   ? 1.4846 0.8418 0.7678 -0.2402 0.032   -0.1792 7   PHE A CE1   
58   C  CE2   . PHE A 7   ? 1.5335 0.791  0.767  -0.2454 0.0063  -0.2075 7   PHE A CE2   
59   C  CZ    . PHE A 7   ? 1.5044 0.8113 0.768  -0.2126 0.0092  -0.1901 7   PHE A CZ    
60   N  N     . ALA A 8   ? 1.3372 1.0019 0.7761 -0.5154 0.1264  -0.2993 8   ALA A N     
61   C  CA    . ALA A 8   ? 1.3039 1.067  0.7943 -0.5683 0.1554  -0.3259 8   ALA A CA    
62   C  C     . ALA A 8   ? 1.2914 1.1073 0.81   -0.5377 0.1634  -0.307  8   ALA A C     
63   O  O     . ALA A 8   ? 1.2718 1.1217 0.8199 -0.4716 0.1401  -0.2911 8   ALA A O     
64   C  CB    . ALA A 8   ? 1.2322 1.129  0.8125 -0.5635 0.1419  -0.3655 8   ALA A CB    
65   N  N     . VAL A 9   ? 1.3088 1.119  0.8086 -0.5872 0.1974  -0.3074 9   VAL A N     
66   C  CA    . VAL A 9   ? 1.306  1.1543 0.8229 -0.563  0.2076  -0.2896 9   VAL A CA    
67   C  C     . VAL A 9   ? 1.2271 1.2395 0.853  -0.5304 0.2004  -0.3132 9   VAL A C     
68   O  O     . VAL A 9   ? 1.209  1.2546 0.8533 -0.4975 0.2021  -0.2977 9   VAL A O     
69   C  CB    . VAL A 9   ? 1.3537 1.1456 0.8115 -0.6311 0.2488  -0.2864 9   VAL A CB    
70   C  CG1   . VAL A 9   ? 1.464  1.0711 0.7964 -0.6428 0.2465  -0.2526 9   VAL A CG1   
71   C  CG2   . VAL A 9   ? 1.3242 1.1877 0.8176 -0.7101 0.2806  -0.3322 9   VAL A CG2   
72   N  N     . ASP A 10  ? 1.1783 1.2869 0.8717 -0.5356 0.1886  -0.3515 10  ASP A N     
73   C  CA    . ASP A 10  ? 1.1048 1.3653 0.8973 -0.5051 0.176   -0.3812 10  ASP A CA    
74   C  C     . ASP A 10  ? 1.0761 1.3826 0.9067 -0.4611 0.1368  -0.3958 10  ASP A C     
75   O  O     . ASP A 10  ? 1.0919 1.3752 0.9104 -0.4894 0.132   -0.4134 10  ASP A O     
76   C  CB    . ASP A 10  ? 1.0864 1.4443 0.9317 -0.5725 0.2087  -0.4291 10  ASP A CB    
77   C  CG    . ASP A 10  ? 1.0644 1.5876 1.0186 -0.5545 0.1923  -0.4793 10  ASP A CG    
78   O  OD1   . ASP A 10  ? 1.0434 1.63   1.0406 -0.4915 0.1694  -0.4742 10  ASP A OD1   
79   O  OD2   . ASP A 10  ? 1.0573 1.6446 1.0518 -0.6036 0.2012  -0.526  10  ASP A OD2   
80   N  N     . THR A 11  ? 1.0354 1.4038 0.9068 -0.3944 0.1091  -0.39   11  THR A N     
81   C  CA    . THR A 11  ? 1.0096 1.4241 0.911  -0.3514 0.0713  -0.4049 11  THR A CA    
82   C  C     . THR A 11  ? 0.9386 1.4864 0.9198 -0.3193 0.0539  -0.4355 11  THR A C     
83   O  O     . THR A 11  ? 0.9218 1.5017 0.9222 -0.3026 0.063   -0.4274 11  THR A O     
84   C  CB    . THR A 11  ? 1.0683 1.3968 0.9166 -0.2982 0.0489  -0.3655 11  THR A CB    
85   O  OG1   . THR A 11  ? 1.0871 1.4038 0.9275 -0.2605 0.0513  -0.3351 11  THR A OG1   
86   C  CG2   . THR A 11  ? 1.1362 1.3425 0.9132 -0.3224 0.0575  -0.3456 11  THR A CG2   
87   N  N     . LYS A 12  ? 0.8965 1.5204 0.9226 -0.3089 0.0266  -0.4734 12  LYS A N     
88   C  CA    . LYS A 12  ? 0.8354 1.5834 0.9349 -0.2727 0.0023  -0.5084 12  LYS A CA    
89   C  C     . LYS A 12  ? 0.8506 1.578  0.9279 -0.1951 -0.0345 -0.4809 12  LYS A C     
90   O  O     . LYS A 12  ? 0.8953 1.5439 0.9174 -0.1732 -0.0497 -0.4539 12  LYS A O     
91   C  CB    . LYS A 12  ? 0.8079 1.6488 0.9645 -0.2931 -0.0155 -0.5661 12  LYS A CB    
92   C  CG    . LYS A 12  ? 0.7807 1.7664 1.0262 -0.267  -0.0367 -0.6167 12  LYS A CG    
93   C  CD    . LYS A 12  ? 0.7882 1.864  1.0883 -0.2783 -0.0625 -0.6755 12  LYS A CD    
94   C  CE    . LYS A 12  ? 0.7569 1.9792 1.1471 -0.2421 -0.0928 -0.7316 12  LYS A CE    
95   N  NZ    . LYS A 12  ? 0.7436 2.0467 1.1801 -0.2398 -0.1287 -0.7874 12  LYS A NZ    
96   N  N     . VAL A 13  ? 0.8127 1.6077 0.9292 -0.1552 -0.0477 -0.4896 13  VAL A N     
97   C  CA    . VAL A 13  ? 0.8333 1.6023 0.9211 -0.0848 -0.0819 -0.4648 13  VAL A CA    
98   C  C     . VAL A 13  ? 0.8078 1.6326 0.9152 -0.0454 -0.1304 -0.498  13  VAL A C     
99   O  O     . VAL A 13  ? 0.7495 1.6831 0.9266 -0.0447 -0.1457 -0.5485 13  VAL A O     
100  C  CB    . VAL A 13  ? 0.8297 1.6212 0.9342 -0.0575 -0.0746 -0.4527 13  VAL A CB    
101  C  CG1   . VAL A 13  ? 0.8516 1.6288 0.9314 0.0142  -0.1146 -0.4382 13  VAL A CG1   
102  C  CG2   . VAL A 13  ? 0.8757 1.5836 0.9368 -0.0841 -0.0348 -0.4095 13  VAL A CG2   
103  N  N     . ILE A 14  ? 0.8507 1.6008 0.8945 -0.0132 -0.1546 -0.4722 14  ILE A N     
104  C  CA    . ILE A 14  ? 0.8475 1.6212 0.8835 0.0256  -0.2024 -0.4954 14  ILE A CA    
105  C  C     . ILE A 14  ? 0.8632 1.6329 0.8753 0.0948  -0.2398 -0.4857 14  ILE A C     
106  O  O     . ILE A 14  ? 0.8387 1.6704 0.8746 0.1307  -0.2831 -0.5222 14  ILE A O     
107  C  CB    . ILE A 14  ? 0.8971 1.586  0.8682 0.0147  -0.2044 -0.4758 14  ILE A CB    
108  C  CG1   . ILE A 14  ? 0.9039 1.5811 0.8888 -0.0516 -0.1697 -0.484  14  ILE A CG1   
109  C  CG2   . ILE A 14  ? 0.9018 1.6095 0.8562 0.0507  -0.2531 -0.5004 14  ILE A CG2   
110  C  CD1   . ILE A 14  ? 0.8607 1.6398 0.9188 -0.0873 -0.1722 -0.5399 14  ILE A CD1   
111  N  N     . ASP A 15  ? 0.9034 1.5971 0.8653 0.1143  -0.2256 -0.439  15  ASP A N     
112  C  CA    . ASP A 15  ? 0.9275 1.5994 0.8536 0.1756  -0.2585 -0.4267 15  ASP A CA    
113  C  C     . ASP A 15  ? 0.9524 1.586  0.8651 0.1839  -0.233  -0.3913 15  ASP A C     
114  O  O     . ASP A 15  ? 0.9663 1.5681 0.8789 0.1457  -0.1911 -0.3674 15  ASP A O     
115  C  CB    . ASP A 15  ? 0.9992 1.586  0.8368 0.2035  -0.2852 -0.4058 15  ASP A CB    
116  C  CG    . ASP A 15  ? 1.0574 1.643  0.862  0.266   -0.3374 -0.4164 15  ASP A CG    
117  O  OD1   . ASP A 15  ? 1.0311 1.686  0.8698 0.2851  -0.3768 -0.4604 15  ASP A OD1   
118  O  OD2   . ASP A 15  ? 1.1259 1.6389 0.8682 0.296   -0.3406 -0.3828 15  ASP A OD2   
119  N  N     . SER A 16  ? 0.9582 1.59   0.8554 0.2357  -0.2609 -0.389  16  SER A N     
120  C  CA    . SER A 16  ? 0.9789 1.5757 0.8627 0.247   -0.2406 -0.3585 16  SER A CA    
121  C  C     . SER A 16  ? 1.0273 1.5598 0.8411 0.3043  -0.2751 -0.34   16  SER A C     
122  O  O     . SER A 16  ? 1.012  1.5868 0.8413 0.3484  -0.3156 -0.3679 16  SER A O     
123  C  CB    . SER A 16  ? 0.9331 1.6268 0.9024 0.2379  -0.2274 -0.3882 16  SER A CB    
124  O  OG    . SER A 16  ? 0.9727 1.639  0.9307 0.2549  -0.2135 -0.3638 16  SER A OG    
125  N  N     . ARG A 17  ? 1.0854 1.5144 0.8203 0.3035  -0.2599 -0.2959 17  ARG A N     
126  C  CA    . ARG A 17  ? 1.1431 1.4943 0.7969 0.3486  -0.2864 -0.2751 17  ARG A CA    
127  C  C     . ARG A 17  ? 1.1713 1.4626 0.7962 0.344   -0.2547 -0.2376 17  ARG A C     
128  O  O     . ARG A 17  ? 1.1691 1.4542 0.8136 0.305   -0.2129 -0.2203 17  ARG A O     
129  C  CB    . ARG A 17  ? 1.2193 1.4938 0.7865 0.3532  -0.3034 -0.2629 17  ARG A CB    
130  C  CG    . ARG A 17  ? 1.2536 1.5734 0.8295 0.3746  -0.3493 -0.3005 17  ARG A CG    
131  C  CD    . ARG A 17  ? 1.3641 1.5977 0.8406 0.3812  -0.3668 -0.2866 17  ARG A CD    
132  N  NE    . ARG A 17  ? 1.3857 1.6579 0.8886 0.3534  -0.367  -0.3085 17  ARG A NE    
133  C  CZ    . ARG A 17  ? 1.4212 1.6846 0.9376 0.3055  -0.3256 -0.2965 17  ARG A CZ    
134  N  NH1   . ARG A 17  ? 1.4347 1.6593 0.9464 0.2814  -0.2819 -0.265  17  ARG A NH1   
135  N  NH2   . ARG A 17  ? 1.4086 1.7029 0.9449 0.2833  -0.33   -0.3191 17  ARG A NH2   
136  N  N     . LEU A 18  ? 1.199  1.4411 0.773  0.3846  -0.2767 -0.2264 18  LEU A N     
137  C  CA    . LEU A 18  ? 1.2299 1.4128 0.7728 0.3808  -0.2487 -0.1933 18  LEU A CA    
138  C  C     . LEU A 18  ? 1.3015 1.3755 0.7443 0.3722  -0.239  -0.1613 18  LEU A C     
139  O  O     . LEU A 18  ? 1.356  1.3552 0.7173 0.4019  -0.2623 -0.1498 18  LEU A O     
140  C  CB    . LEU A 18  ? 1.2319 1.4153 0.7709 0.4266  -0.2757 -0.2001 18  LEU A CB    
141  C  CG    . LEU A 18  ? 1.1901 1.4601 0.8204 0.4234  -0.2599 -0.2174 18  LEU A CG    
142  C  CD1   . LEU A 18  ? 1.1964 1.454  0.8444 0.3805  -0.2077 -0.1909 18  LEU A CD1   
143  C  CD2   . LEU A 18  ? 1.1291 1.5152 0.8498 0.4169  -0.2704 -0.2614 18  LEU A CD2   
144  N  N     . VAL A 19  ? 1.3011 1.3634 0.7461 0.3309  -0.2046 -0.1496 19  VAL A N     
145  C  CA    . VAL A 19  ? 1.3598 1.3343 0.7196 0.3172  -0.1912 -0.1277 19  VAL A CA    
146  C  C     . VAL A 19  ? 1.3921 1.3059 0.715  0.3065  -0.1599 -0.1004 19  VAL A C     
147  O  O     . VAL A 19  ? 1.4521 1.2841 0.687  0.3061  -0.1578 -0.0854 19  VAL A O     
148  C  CB    . VAL A 19  ? 1.3575 1.3464 0.7329 0.2824  -0.1725 -0.1337 19  VAL A CB    
149  C  CG1   . VAL A 19  ? 1.3382 1.3797 0.7401 0.2911  -0.2048 -0.1623 19  VAL A CG1   
150  C  CG2   . VAL A 19  ? 1.3274 1.3537 0.7709 0.2497  -0.1342 -0.1298 19  VAL A CG2   
151  N  N     . GLY A 20  ? 1.353  1.3036 0.7369 0.2955  -0.1353 -0.0957 20  GLY A N     
152  C  CA    . GLY A 20  ? 1.3794 1.2809 0.7361 0.2853  -0.1069 -0.0741 20  GLY A CA    
153  C  C     . GLY A 20  ? 1.4105 1.2659 0.7193 0.3161  -0.1252 -0.0652 20  GLY A C     
154  O  O     . GLY A 20  ? 1.4171 1.255  0.7283 0.3122  -0.1054 -0.0527 20  GLY A O     
155  N  N     . GLU A 21  ? 1.4303 1.2616 0.6916 0.3493  -0.1663 -0.0733 21  GLU A N     
156  C  CA    . GLU A 21  ? 1.4658 1.2455 0.6726 0.3878  -0.1956 -0.0691 21  GLU A CA    
157  C  C     . GLU A 21  ? 1.41   1.253  0.6939 0.4041  -0.1954 -0.0778 21  GLU A C     
158  O  O     . GLU A 21  ? 1.4354 1.2358 0.6931 0.4129  -0.1888 -0.0648 21  GLU A O     
159  C  CB    . GLU A 21  ? 1.5747 1.2383 0.6725 0.3771  -0.181  -0.0438 21  GLU A CB    
160  C  CG    . GLU A 21  ? 1.7131 1.2922 0.7008 0.3871  -0.2071 -0.0403 21  GLU A CG    
161  C  CD    . GLU A 21  ? 1.7982 1.4053 0.7933 0.3677  -0.2054 -0.0506 21  GLU A CD    
162  O  OE1   . GLU A 21  ? 1.7795 1.4341 0.8329 0.3305  -0.1677 -0.0516 21  GLU A OE1   
163  O  OE2   . GLU A 21  ? 1.8602 1.4362 0.7974 0.3916  -0.2442 -0.0587 21  GLU A OE2   
164  N  N     . GLY A 22  ? 1.3309 1.2756 0.7083 0.403   -0.1993 -0.1013 22  GLY A N     
165  C  CA    . GLY A 22  ? 1.2683 1.2891 0.7275 0.4118  -0.195  -0.1156 22  GLY A CA    
166  C  C     . GLY A 22  ? 1.2235 1.2784 0.7384 0.3711  -0.149  -0.1055 22  GLY A C     
167  O  O     . GLY A 22  ? 1.1749 1.3095 0.7669 0.3625  -0.1395 -0.122  22  GLY A O     
168  N  N     . SER A 23  ? 1.239  1.2326 0.7119 0.3455  -0.1206 -0.081  23  SER A N     
169  C  CA    . SER A 23  ? 1.2054 1.2177 0.7193 0.3124  -0.082  -0.0713 23  SER A CA    
170  C  C     . SER A 23  ? 1.1478 1.2172 0.7175 0.284   -0.0693 -0.0827 23  SER A C     
171  O  O     . SER A 23  ? 1.1238 1.2215 0.7367 0.2635  -0.0456 -0.0808 23  SER A O     
172  C  CB    . SER A 23  ? 1.2651 1.2037 0.7221 0.2949  -0.059  -0.0501 23  SER A CB    
173  O  OG    . SER A 23  ? 1.2794 1.2265 0.7677 0.2771  -0.0297 -0.0418 23  SER A OG    
174  N  N     . SER A 24  ? 1.1276 1.2075 0.6903 0.2825  -0.0862 -0.095  24  SER A N     
175  C  CA    . SER A 24  ? 1.0852 1.2089 0.6925 0.2534  -0.0749 -0.1066 24  SER A CA    
176  C  C     . SER A 24  ? 1.0444 1.2191 0.6752 0.2611  -0.1025 -0.1332 24  SER A C     
177  O  O     . SER A 24  ? 1.0674 1.2219 0.6581 0.288   -0.1327 -0.1388 24  SER A O     
178  C  CB    . SER A 24  ? 1.1272 1.2019 0.701  0.2294  -0.0554 -0.0937 24  SER A CB    
179  O  OG    . SER A 24  ? 1.1346 1.2387 0.7418 0.2035  -0.0477 -0.1049 24  SER A OG    
180  N  N     . VAL A 25  ? 0.9856 1.2217 0.676  0.2355  -0.0923 -0.1507 25  VAL A N     
181  C  CA    . VAL A 25  ? 0.9432 1.2398 0.6681 0.2344  -0.1136 -0.1816 25  VAL A CA    
182  C  C     . VAL A 25  ? 0.9399 1.2197 0.655  0.2034  -0.1043 -0.1824 25  VAL A C     
183  O  O     . VAL A 25  ? 0.9363 1.2074 0.6658 0.1702  -0.0761 -0.1745 25  VAL A O     
184  C  CB    . VAL A 25  ? 0.896  1.2814 0.6969 0.2239  -0.1075 -0.2083 25  VAL A CB    
185  C  CG1   . VAL A 25  ? 0.8668 1.3208 0.7123 0.2075  -0.1198 -0.244  25  VAL A CG1   
186  C  CG2   . VAL A 25  ? 0.8878 1.3005 0.7016 0.2637  -0.1267 -0.2177 25  VAL A CG2   
187  N  N     . ARG A 26  ? 0.9427 1.2126 0.6281 0.2162  -0.1305 -0.1929 26  ARG A N     
188  C  CA    . ARG A 26  ? 0.9487 1.2032 0.6229 0.1897  -0.1248 -0.1971 26  ARG A CA    
189  C  C     . ARG A 26  ? 0.8999 1.2296 0.6289 0.1757  -0.1379 -0.2321 26  ARG A C     
190  O  O     . ARG A 26  ? 0.8764 1.2557 0.625  0.2019  -0.1689 -0.2564 26  ARG A O     
191  C  CB    . ARG A 26  ? 1.0131 1.2057 0.6135 0.2079  -0.1423 -0.1879 26  ARG A CB    
192  C  CG    . ARG A 26  ? 1.0626 1.2412 0.6486 0.1846  -0.1397 -0.1961 26  ARG A CG    
193  C  CD    . ARG A 26  ? 1.1418 1.2777 0.6583 0.2067  -0.166  -0.1969 26  ARG A CD    
194  N  NE    . ARG A 26  ? 1.2152 1.2923 0.6831 0.1881  -0.1462 -0.1848 26  ARG A NE    
195  C  CZ    . ARG A 26  ? 1.2432 1.3206 0.7049 0.1716  -0.1492 -0.1995 26  ARG A CZ    
196  N  NH1   . ARG A 26  ? 1.199  1.3309 0.6986 0.1692  -0.1717 -0.2261 26  ARG A NH1   
197  N  NH2   . ARG A 26  ? 1.277  1.3042 0.6969 0.1569  -0.1296 -0.1916 26  ARG A NH2   
198  N  N     . ARG A 27  ? 0.8851 1.2224 0.6381 0.1349  -0.1158 -0.2377 27  ARG A N     
199  C  CA    . ARG A 27  ? 0.8495 1.2552 0.6533 0.1115  -0.1224 -0.273  27  ARG A CA    
200  C  C     . ARG A 27  ? 0.8778 1.2518 0.659  0.0863  -0.1204 -0.2771 27  ARG A C     
201  O  O     . ARG A 27  ? 0.9129 1.218  0.6537 0.0759  -0.1028 -0.2534 27  ARG A O     
202  C  CB    . ARG A 27  ? 0.8246 1.2751 0.6827 0.0759  -0.0932 -0.2819 27  ARG A CB    
203  C  CG    . ARG A 27  ? 0.8229 1.3166 0.7122 0.097   -0.0927 -0.2843 27  ARG A CG    
204  C  CD    . ARG A 27  ? 0.813  1.3493 0.7489 0.0549  -0.0601 -0.2958 27  ARG A CD    
205  N  NE    . ARG A 27  ? 0.8158 1.3573 0.76   0.0696  -0.0474 -0.2824 27  ARG A NE    
206  C  CZ    . ARG A 27  ? 0.7913 1.4047 0.7788 0.0952  -0.0609 -0.3061 27  ARG A CZ    
207  N  NH1   . ARG A 27  ? 0.7503 1.442  0.7811 0.1095  -0.0889 -0.3472 27  ARG A NH1   
208  N  NH2   . ARG A 27  ? 0.7828 1.3939 0.7733 0.1074  -0.048  -0.293  27  ARG A NH2   
209  N  N     . ARG A 28  ? 0.8568 1.2856 0.6678 0.0776  -0.1395 -0.3115 28  ARG A N     
210  C  CA    . ARG A 28  ? 0.8814 1.29   0.6798 0.049   -0.1375 -0.322  28  ARG A CA    
211  C  C     . ARG A 28  ? 0.8539 1.3143 0.7094 0.0005  -0.1166 -0.3466 28  ARG A C     
212  O  O     . ARG A 28  ? 0.8085 1.3493 0.7204 -0.002  -0.1193 -0.3722 28  ARG A O     
213  C  CB    . ARG A 28  ? 0.9022 1.332  0.6861 0.0733  -0.1766 -0.3455 28  ARG A CB    
214  C  CG    . ARG A 28  ? 0.9867 1.3587 0.7234 0.0598  -0.1761 -0.3412 28  ARG A CG    
215  C  CD    . ARG A 28  ? 1.0858 1.3717 0.7533 0.0784  -0.1663 -0.3049 28  ARG A CD    
216  N  NE    . ARG A 28  ? 1.1584 1.4041 0.7733 0.0828  -0.1801 -0.3094 28  ARG A NE    
217  C  CZ    . ARG A 28  ? 1.2049 1.4148 0.8062 0.0559  -0.1642 -0.3111 28  ARG A CZ    
218  N  NH1   . ARG A 28  ? 1.1929 1.3923 0.8223 0.0242  -0.1364 -0.3065 28  ARG A NH1   
219  N  NH2   . ARG A 28  ? 1.2336 1.4117 0.7867 0.0617  -0.1773 -0.3181 28  ARG A NH2   
220  N  N     . ARG A 29  ? 0.8806 1.2915 0.7183 -0.0389 -0.0938 -0.34   29  ARG A N     
221  C  CA    . ARG A 29  ? 0.8677 1.3076 0.7423 -0.0925 -0.0703 -0.3608 29  ARG A CA    
222  C  C     . ARG A 29  ? 0.8916 1.3064 0.7516 -0.1247 -0.0721 -0.378  29  ARG A C     
223  O  O     . ARG A 29  ? 0.9316 1.2765 0.742  -0.1126 -0.0778 -0.3607 29  ARG A O     
224  C  CB    . ARG A 29  ? 0.9008 1.29   0.7598 -0.1152 -0.0354 -0.3329 29  ARG A CB    
225  C  CG    . ARG A 29  ? 0.894  1.3405 0.7921 -0.1085 -0.0252 -0.3345 29  ARG A CG    
226  C  CD    . ARG A 29  ? 0.9514 1.3336 0.8192 -0.1221 0.0046  -0.3015 29  ARG A CD    
227  N  NE    . ARG A 29  ? 0.937  1.3755 0.842  -0.124  0.0188  -0.3069 29  ARG A NE    
228  C  CZ    . ARG A 29  ? 0.9394 1.4081 0.8677 -0.1726 0.0466  -0.3243 29  ARG A CZ    
229  N  NH1   . ARG A 29  ? 0.9457 1.3868 0.8595 -0.2252 0.0629  -0.3363 29  ARG A NH1   
230  N  NH2   . ARG A 29  ? 0.911  1.4338 0.8725 -0.1713 0.0599  -0.3309 29  ARG A NH2   
231  N  N     . GLN A 30  ? 0.8638 1.339  0.7684 -0.1667 -0.0666 -0.4155 30  GLN A N     
232  C  CA    . GLN A 30  ? 0.8883 1.3411 0.7808 -0.2023 -0.0676 -0.4357 30  GLN A CA    
233  C  C     . GLN A 30  ? 0.9029 1.3293 0.7955 -0.2671 -0.0314 -0.4411 30  GLN A C     
234  O  O     . GLN A 30  ? 0.8754 1.362  0.8109 -0.2943 -0.0123 -0.4574 30  GLN A O     
235  C  CB    . GLN A 30  ? 0.8703 1.4162 0.8098 -0.197  -0.098  -0.4825 30  GLN A CB    
236  C  CG    . GLN A 30  ? 0.9428 1.4701 0.8729 -0.2372 -0.0988 -0.5072 30  GLN A CG    
237  C  CD    . GLN A 30  ? 0.9895 1.5992 0.9558 -0.2203 -0.1363 -0.5505 30  GLN A CD    
238  O  OE1   . GLN A 30  ? 1.0078 1.6487 0.9741 -0.1647 -0.1699 -0.5502 30  GLN A OE1   
239  N  NE2   . GLN A 30  ? 0.9887 1.6291 0.9805 -0.2678 -0.1333 -0.5896 30  GLN A NE2   
240  N  N     . CYS A 31  ? 0.9464 1.2785 0.7859 -0.2924 -0.0216 -0.4286 31  CYS A N     
241  C  CA    . CYS A 31  ? 0.9704 1.2531 0.79   -0.3556 0.0107  -0.4313 31  CYS A CA    
242  C  C     . CYS A 31  ? 0.936  1.2802 0.7945 -0.4075 0.0135  -0.4797 31  CYS A C     
243  O  O     . CYS A 31  ? 0.9228 1.2954 0.7939 -0.396  -0.012  -0.503  31  CYS A O     
244  C  CB    . CYS A 31  ? 1.0468 1.1943 0.7882 -0.3577 0.0166  -0.3999 31  CYS A CB    
245  S  SG    . CYS A 31  ? 1.1201 1.1749 0.8107 -0.4316 0.0535  -0.3959 31  CYS A SG    
246  N  N     . LEU A 32  ? 0.9188 1.2874 0.7963 -0.4663 0.0455  -0.4975 32  LEU A N     
247  C  CA    . LEU A 32  ? 0.8867 1.3226 0.807  -0.5257 0.055   -0.549  32  LEU A CA    
248  C  C     . LEU A 32  ? 0.9446 1.2718 0.8006 -0.5721 0.0641  -0.548  32  LEU A C     
249  O  O     . LEU A 32  ? 0.9288 1.2928 0.8081 -0.5946 0.0522  -0.5855 32  LEU A O     
250  C  CB    . LEU A 32  ? 0.856  1.3589 0.8177 -0.5776 0.0921  -0.5712 32  LEU A CB    
251  C  CG    . LEU A 32  ? 0.7957 1.4514 0.851  -0.5477 0.0815  -0.6028 32  LEU A CG    
252  C  CD1   . LEU A 32  ? 0.8002 1.4611 0.8558 -0.46   0.0476  -0.5706 32  LEU A CD1   
253  C  CD2   . LEU A 32  ? 0.788  1.4795 0.8636 -0.5959 0.125   -0.6122 32  LEU A CD2   
254  N  N     . VAL A 33  ? 1.0125 1.2018 0.7847 -0.5805 0.0804  -0.506  33  VAL A N     
255  C  CA    . VAL A 33  ? 1.0799 1.1446 0.7777 -0.6187 0.0866  -0.5011 33  VAL A CA    
256  C  C     . VAL A 33  ? 1.0982 1.1224 0.7737 -0.5725 0.0514  -0.4967 33  VAL A C     
257  O  O     . VAL A 33  ? 1.1038 1.1238 0.7778 -0.6028 0.0449  -0.5265 33  VAL A O     
258  C  CB    . VAL A 33  ? 1.1681 1.0933 0.7777 -0.6381 0.1107  -0.4605 33  VAL A CB    
259  C  CG1   . VAL A 33  ? 1.2507 1.0375 0.776  -0.6771 0.1136  -0.4587 33  VAL A CG1   
260  C  CG2   . VAL A 33  ? 1.1577 1.1184 0.7804 -0.6889 0.1489  -0.4657 33  VAL A CG2   
261  N  N     . CYS A 34  ? 1.1051 1.1011 0.763  -0.5029 0.031   -0.4629 34  CYS A N     
262  C  CA    . CYS A 34  ? 1.126  1.0809 0.7577 -0.4617 0.0026  -0.4598 34  CYS A CA    
263  C  C     . CYS A 34  ? 1.0661 1.1244 0.7502 -0.4134 -0.0268 -0.4754 34  CYS A C     
264  O  O     . CYS A 34  ? 1.0835 1.1113 0.7426 -0.3788 -0.0481 -0.4727 34  CYS A O     
265  C  CB    . CYS A 34  ? 1.1973 1.0405 0.765  -0.423  0.0002  -0.4193 34  CYS A CB    
266  S  SG    . CYS A 34  ? 1.2266 1.111  0.8162 -0.3597 -0.0033 -0.3848 34  CYS A SG    
267  N  N     . ASN A 35  ? 0.9979 1.1725 0.7485 -0.4097 -0.029  -0.493  35  ASN A N     
268  C  CA    . ASN A 35  ? 0.95   1.221  0.7453 -0.3626 -0.0608 -0.5097 35  ASN A CA    
269  C  C     . ASN A 35  ? 0.9602 1.1964 0.7218 -0.296  -0.079  -0.4754 35  ASN A C     
270  O  O     . ASN A 35  ? 0.9485 1.2249 0.7161 -0.259  -0.1079 -0.4863 35  ASN A O     
271  C  CB    . ASN A 35  ? 0.9534 1.268  0.7683 -0.3784 -0.0825 -0.5528 35  ASN A CB    
272  C  CG    . ASN A 35  ? 0.9977 1.3291 0.835  -0.4525 -0.0617 -0.5893 35  ASN A CG    
273  O  OD1   . ASN A 35  ? 0.9814 1.3788 0.8661 -0.4898 -0.0407 -0.6084 35  ASN A OD1   
274  N  ND2   . ASN A 35  ? 1.0404 1.3121 0.8423 -0.4783 -0.0654 -0.6026 35  ASN A ND2   
275  N  N     . GLU A 36  ? 0.9805 1.1422 0.7041 -0.2821 -0.0621 -0.4363 36  GLU A N     
276  C  CA    . GLU A 36  ? 0.9896 1.1188 0.6825 -0.2262 -0.0737 -0.407  36  GLU A CA    
277  C  C     . GLU A 36  ? 0.9431 1.1299 0.664  -0.1914 -0.0771 -0.3923 36  GLU A C     
278  O  O     . GLU A 36  ? 0.9189 1.1446 0.6736 -0.2096 -0.0622 -0.3931 36  GLU A O     
279  C  CB    . GLU A 36  ? 1.0692 1.091  0.7089 -0.2241 -0.0581 -0.3782 36  GLU A CB    
280  C  CG    . GLU A 36  ? 1.1589 1.1094 0.7584 -0.2386 -0.0628 -0.3902 36  GLU A CG    
281  C  CD    . GLU A 36  ? 1.2202 1.1769 0.8043 -0.2051 -0.0845 -0.4    36  GLU A CD    
282  O  OE1   . GLU A 36  ? 1.2229 1.2171 0.8119 -0.1656 -0.0941 -0.3893 36  GLU A OE1   
283  O  OE2   . GLU A 36  ? 1.2504 1.1673 0.8108 -0.2201 -0.0909 -0.4187 36  GLU A OE2   
284  N  N     . ARG A 37  ? 0.9327 1.1182 0.6333 -0.1431 -0.0949 -0.3788 37  ARG A N     
285  C  CA    . ARG A 37  ? 0.9044 1.1298 0.6201 -0.1071 -0.1005 -0.3633 37  ARG A CA    
286  C  C     . ARG A 37  ? 0.9156 1.077  0.5935 -0.0811 -0.0871 -0.326  37  ARG A C     
287  O  O     . ARG A 37  ? 0.9536 1.0512 0.5913 -0.0761 -0.0831 -0.3169 37  ARG A O     
288  C  CB    . ARG A 37  ? 0.9108 1.1897 0.6305 -0.0733 -0.1343 -0.3806 37  ARG A CB    
289  C  CG    . ARG A 37  ? 0.9189 1.2788 0.6885 -0.0945 -0.1514 -0.4238 37  ARG A CG    
290  C  CD    . ARG A 37  ? 0.9574 1.3653 0.7252 -0.0532 -0.1918 -0.4418 37  ARG A CD    
291  N  NE    . ARG A 37  ? 0.9612 1.4606 0.7878 -0.0693 -0.2113 -0.4892 37  ARG A NE    
292  C  CZ    . ARG A 37  ? 0.9932 1.5301 0.8175 -0.0467 -0.2501 -0.5181 37  ARG A CZ    
293  N  NH1   . ARG A 37  ? 1.0338 1.5149 0.7894 -0.0095 -0.2719 -0.5013 37  ARG A NH1   
294  N  NH2   . ARG A 37  ? 0.9462 1.5767 0.8345 -0.063  -0.267  -0.5667 37  ARG A NH2   
295  N  N     . PHE A 38  ? 0.8775 1.0604 0.5722 -0.0651 -0.0798 -0.3085 38  PHE A N     
296  C  CA    . PHE A 38  ? 0.8845 1.0166 0.5504 -0.042  -0.0669 -0.2765 38  PHE A CA    
297  C  C     . PHE A 38  ? 0.8446 1.0156 0.5264 -0.0137 -0.0711 -0.2643 38  PHE A C     
298  O  O     . PHE A 38  ? 0.8109 1.046  0.5344 -0.0182 -0.0768 -0.2789 38  PHE A O     
299  C  CB    . PHE A 38  ? 0.9021 0.9785 0.5588 -0.066  -0.0429 -0.2625 38  PHE A CB    
300  C  CG    . PHE A 38  ? 0.8888 0.9927 0.5771 -0.0974 -0.0277 -0.2658 38  PHE A CG    
301  C  CD1   . PHE A 38  ? 0.8835 1.0078 0.59   -0.1396 -0.0239 -0.2907 38  PHE A CD1   
302  C  CD2   . PHE A 38  ? 0.8942 0.9997 0.5899 -0.0889 -0.0141 -0.2457 38  PHE A CD2   
303  C  CE1   . PHE A 38  ? 0.8739 1.0228 0.6047 -0.1755 -0.0043 -0.2965 38  PHE A CE1   
304  C  CE2   . PHE A 38  ? 0.8849 1.0135 0.6037 -0.1213 0.0034  -0.2502 38  PHE A CE2   
305  C  CZ    . PHE A 38  ? 0.8692 1.0187 0.604  -0.1661 0.0098  -0.2758 38  PHE A CZ    
306  N  N     . THR A 39  ? 0.8469 0.9807 0.4962 0.0146  -0.0681 -0.2412 39  THR A N     
307  C  CA    . THR A 39  ? 0.826  0.9807 0.4786 0.0432  -0.0724 -0.2274 39  THR A CA    
308  C  C     . THR A 39  ? 0.8096 0.9495 0.4753 0.0384  -0.0493 -0.2071 39  THR A C     
309  O  O     . THR A 39  ? 0.8331 0.924  0.4834 0.0268  -0.0328 -0.1964 39  THR A O     
310  C  CB    . THR A 39  ? 0.8696 0.9864 0.4696 0.0716  -0.0814 -0.2163 39  THR A CB    
311  O  OG1   . THR A 39  ? 0.8821 1.0158 0.4657 0.0794  -0.1073 -0.2354 39  THR A OG1   
312  C  CG2   . THR A 39  ? 0.8773 0.9898 0.4645 0.0988  -0.0814 -0.1969 39  THR A CG2   
313  N  N     . THR A 40  ? 0.7671 0.949  0.4605 0.0491  -0.0505 -0.2047 40  THR A N     
314  C  CA    . THR A 40  ? 0.7567 0.9252 0.4582 0.0473  -0.0302 -0.1857 40  THR A CA    
315  C  C     . THR A 40  ? 0.7418 0.9203 0.4378 0.0815  -0.0374 -0.1731 40  THR A C     
316  O  O     . THR A 40  ? 0.7323 0.9428 0.43   0.1036  -0.0597 -0.1837 40  THR A O     
317  C  CB    . THR A 40  ? 0.7463 0.9488 0.4862 0.0149  -0.0155 -0.1961 40  THR A CB    
318  O  OG1   . THR A 40  ? 0.7149 0.9925 0.496  0.0238  -0.0258 -0.2138 40  THR A OG1   
319  C  CG2   . THR A 40  ? 0.7584 0.949  0.4988 -0.0236 -0.0099 -0.2121 40  THR A CG2   
320  N  N     . PHE A 41  ? 0.7405 0.8885 0.4273 0.087   -0.0207 -0.1521 41  PHE A N     
321  C  CA    . PHE A 41  ? 0.7323 0.8825 0.4117 0.1154  -0.0244 -0.1396 41  PHE A CA    
322  C  C     . PHE A 41  ? 0.7021 0.8704 0.4106 0.1081  -0.0082 -0.1331 41  PHE A C     
323  O  O     . PHE A 41  ? 0.7116 0.853  0.419  0.088   0.0098  -0.125  41  PHE A O     
324  C  CB    . PHE A 41  ? 0.7656 0.8586 0.3988 0.1297  -0.019  -0.1223 41  PHE A CB    
325  C  CG    . PHE A 41  ? 0.7921 0.865  0.3859 0.138   -0.0338 -0.1286 41  PHE A CG    
326  C  CD1   . PHE A 41  ? 0.81   0.8855 0.3776 0.1623  -0.0556 -0.1301 41  PHE A CD1   
327  C  CD2   . PHE A 41  ? 0.8144 0.8597 0.3908 0.123   -0.0274 -0.134  41  PHE A CD2   
328  C  CE1   . PHE A 41  ? 0.8416 0.8886 0.3601 0.1687  -0.0696 -0.1348 41  PHE A CE1   
329  C  CE2   . PHE A 41  ? 0.8405 0.8664 0.3757 0.1286  -0.039  -0.1409 41  PHE A CE2   
330  C  CZ    . PHE A 41  ? 0.8483 0.8732 0.3517 0.15    -0.0595 -0.1402 41  PHE A CZ    
331  N  N     . GLU A 42  ? 0.6662 0.8785 0.3977 0.1254  -0.0169 -0.1391 42  GLU A N     
332  C  CA    . GLU A 42  ? 0.641  0.8772 0.3999 0.1205  -0.0018 -0.1362 42  GLU A CA    
333  C  C     . GLU A 42  ? 0.6508 0.8593 0.3873 0.15    -0.0031 -0.1179 42  GLU A C     
334  O  O     . GLU A 42  ? 0.6542 0.866  0.377  0.179   -0.0234 -0.1204 42  GLU A O     
335  C  CB    . GLU A 42  ? 0.6176 0.9341 0.4262 0.1181  -0.0097 -0.1641 42  GLU A CB    
336  C  CG    . GLU A 42  ? 0.6455 0.9918 0.4819 0.1104  0.0088  -0.1649 42  GLU A CG    
337  C  CD    . GLU A 42  ? 0.6627 1.099  0.5537 0.1158  0.0004  -0.1981 42  GLU A CD    
338  O  OE1   . GLU A 42  ? 0.6464 1.1282 0.5604 0.1194  -0.0198 -0.2243 42  GLU A OE1   
339  O  OE2   . GLU A 42  ? 0.6709 1.1363 0.5839 0.1183  0.0125  -0.2014 42  GLU A OE2   
340  N  N     . VAL A 43  ? 0.6606 0.8333 0.386  0.1431  0.0164  -0.0998 43  VAL A N     
341  C  CA    . VAL A 43  ? 0.6764 0.8185 0.3797 0.1656  0.0186  -0.0833 43  VAL A CA    
342  C  C     . VAL A 43  ? 0.6576 0.8127 0.3804 0.1629  0.0333  -0.0779 43  VAL A C     
343  O  O     . VAL A 43  ? 0.658  0.8186 0.394  0.1382  0.0475  -0.0794 43  VAL A O     
344  C  CB    . VAL A 43  ? 0.7196 0.8044 0.3876 0.163   0.0266  -0.0706 43  VAL A CB    
345  C  CG1   . VAL A 43  ? 0.7471 0.8033 0.3918 0.1815  0.0302  -0.0579 43  VAL A CG1   
346  C  CG2   . VAL A 43  ? 0.738  0.8094 0.3838 0.1611  0.0157  -0.0779 43  VAL A CG2   
347  N  N     . ALA A 44  ? 0.6452 0.7965 0.3617 0.1865  0.0303  -0.0712 44  ALA A N     
348  C  CA    . ALA A 44  ? 0.6252 0.7883 0.3573 0.1861  0.0436  -0.0671 44  ALA A CA    
349  C  C     . ALA A 44  ? 0.6307 0.7461 0.3421 0.1794  0.059   -0.05   44  ALA A C     
350  O  O     . ALA A 44  ? 0.6482 0.7261 0.3344 0.1902  0.0576  -0.0412 44  ALA A O     
351  C  CB    . ALA A 44  ? 0.6219 0.8018 0.3571 0.2164  0.0313  -0.0708 44  ALA A CB    
352  N  N     . GLU A 45  ? 0.6174 0.734  0.3368 0.1608  0.0733  -0.048  45  GLU A N     
353  C  CA    . GLU A 45  ? 0.6335 0.7066 0.3332 0.1585  0.0827  -0.0353 45  GLU A CA    
354  C  C     . GLU A 45  ? 0.6206 0.7035 0.3253 0.1669  0.0901  -0.0315 45  GLU A C     
355  O  O     . GLU A 45  ? 0.6084 0.7153 0.3237 0.1527  0.0996  -0.0362 45  GLU A O     
356  C  CB    . GLU A 45  ? 0.6736 0.7188 0.36   0.1339  0.0892  -0.034  45  GLU A CB    
357  C  CG    . GLU A 45  ? 0.7595 0.771  0.4309 0.1326  0.0819  -0.035  45  GLU A CG    
358  C  CD    . GLU A 45  ? 0.8659 0.8527 0.5276 0.1521  0.0786  -0.0321 45  GLU A CD    
359  O  OE1   . GLU A 45  ? 0.8937 0.8757 0.5512 0.1554  0.0737  -0.0378 45  GLU A OE1   
360  O  OE2   . GLU A 45  ? 0.8836 0.8582 0.5418 0.162   0.0822  -0.0269 45  GLU A OE2   
361  N  N     . LEU A 46  ? 0.6243 0.6882 0.3193 0.1867  0.0879  -0.025  46  LEU A N     
362  C  CA    . LEU A 46  ? 0.6201 0.6888 0.3173 0.1971  0.0936  -0.0219 46  LEU A CA    
363  C  C     . LEU A 46  ? 0.6365 0.6733 0.3182 0.1891  0.1013  -0.0149 46  LEU A C     
364  O  O     . LEU A 46  ? 0.6551 0.6588 0.3237 0.1896  0.0979  -0.0126 46  LEU A O     
365  C  CB    . LEU A 46  ? 0.6253 0.6803 0.313  0.2193  0.0876  -0.0194 46  LEU A CB    
366  C  CG    . LEU A 46  ? 0.6314 0.7005 0.3186 0.2344  0.0743  -0.0249 46  LEU A CG    
367  C  CD1   . LEU A 46  ? 0.6574 0.6906 0.3172 0.251   0.0704  -0.0195 46  LEU A CD1   
368  C  CD2   . LEU A 46  ? 0.6122 0.7317 0.3268 0.2416  0.0701  -0.0371 46  LEU A CD2   
369  N  N     . VAL A 47  ? 0.6264 0.6739 0.3079 0.1834  0.1102  -0.0144 47  VAL A N     
370  C  CA    . VAL A 47  ? 0.6429 0.6546 0.2994 0.1778  0.1148  -0.0075 47  VAL A CA    
371  C  C     . VAL A 47  ? 0.6458 0.6371 0.2979 0.1988  0.1091  -0.0053 47  VAL A C     
372  O  O     . VAL A 47  ? 0.6677 0.6241 0.3017 0.2015  0.104   -0.0036 47  VAL A O     
373  C  CB    . VAL A 47  ? 0.6465 0.673  0.2964 0.1638  0.1285  -0.0087 47  VAL A CB    
374  C  CG1   . VAL A 47  ? 0.6885 0.6612 0.2944 0.1483  0.1309  -0.0003 47  VAL A CG1   
375  C  CG2   . VAL A 47  ? 0.6267 0.7049 0.3013 0.1464  0.1378  -0.0207 47  VAL A CG2   
376  N  N     . MET A 48  ? 0.6215 0.6337 0.2885 0.214   0.1088  -0.0079 48  MET A N     
377  C  CA    . MET A 48  ? 0.6196 0.6174 0.2842 0.2293  0.1066  -0.0087 48  MET A CA    
378  C  C     . MET A 48  ? 0.6159 0.6188 0.284  0.2375  0.1031  -0.0106 48  MET A C     
379  O  O     . MET A 48  ? 0.6028 0.6284 0.2784 0.2396  0.0995  -0.0122 48  MET A O     
380  C  CB    . MET A 48  ? 0.6147 0.6199 0.278  0.2374  0.1114  -0.0088 48  MET A CB    
381  C  CG    . MET A 48  ? 0.6308 0.6159 0.2765 0.232   0.1128  -0.0062 48  MET A CG    
382  S  SD    . MET A 48  ? 0.6282 0.5811 0.2673 0.2415  0.1027  -0.0114 48  MET A SD    
383  C  CE    . MET A 48  ? 0.5771 0.539  0.2261 0.2547  0.1062  -0.017  48  MET A CE    
384  N  N     . PRO A 49  ? 0.6244 0.605  0.2834 0.2414  0.1036  -0.0128 49  PRO A N     
385  C  CA    . PRO A 49  ? 0.6333 0.6026 0.278  0.2459  0.101   -0.0125 49  PRO A CA    
386  C  C     . PRO A 49  ? 0.6432 0.6183 0.2831 0.2623  0.0952  -0.0111 49  PRO A C     
387  O  O     . PRO A 49  ? 0.6462 0.6322 0.2949 0.2695  0.0977  -0.0123 49  PRO A O     
388  C  CB    . PRO A 49  ? 0.6528 0.5955 0.2852 0.2401  0.1087  -0.0179 49  PRO A CB    
389  C  CG    . PRO A 49  ? 0.6534 0.6017 0.3001 0.2414  0.1117  -0.0227 49  PRO A CG    
390  C  CD    . PRO A 49  ? 0.6245 0.5887 0.283  0.2403  0.1067  -0.0189 49  PRO A CD    
391  N  N     . ARG A 50  ? 0.6533 0.6206 0.2774 0.2709  0.085   -0.0108 50  ARG A N     
392  C  CA    . ARG A 50  ? 0.6643 0.6302 0.2793 0.2934  0.0736  -0.0132 50  ARG A CA    
393  C  C     . ARG A 50  ? 0.6945 0.6103 0.2756 0.2965  0.0779  -0.0098 50  ARG A C     
394  O  O     . ARG A 50  ? 0.718  0.6024 0.279  0.2795  0.0882  -0.0076 50  ARG A O     
395  C  CB    . ARG A 50  ? 0.6907 0.658  0.2934 0.3067  0.055   -0.0164 50  ARG A CB    
396  C  CG    . ARG A 50  ? 0.7565 0.6686 0.31   0.302   0.0512  -0.0098 50  ARG A CG    
397  C  CD    . ARG A 50  ? 0.8012 0.7055 0.3318 0.322   0.0267  -0.0134 50  ARG A CD    
398  N  NE    . ARG A 50  ? 0.8702 0.7153 0.3434 0.3127  0.0252  -0.0059 50  ARG A NE    
399  C  CZ    . ARG A 50  ? 0.8906 0.7436 0.3625 0.2991  0.0253  -0.0066 50  ARG A CZ    
400  N  NH1   . ARG A 50  ? 0.8511 0.7647 0.3754 0.2927  0.0258  -0.0138 50  ARG A NH1   
401  N  NH2   . ARG A 50  ? 0.923  0.719  0.3361 0.289   0.0265  -0.001  50  ARG A NH2   
402  N  N     . VAL A 51  ? 0.6921 0.6032 0.2688 0.3156  0.0718  -0.0128 51  VAL A N     
403  C  CA    . VAL A 51  ? 0.7282 0.5888 0.2711 0.317   0.0761  -0.0109 51  VAL A CA    
404  C  C     . VAL A 51  ? 0.781  0.5821 0.2682 0.3325  0.0604  -0.0078 51  VAL A C     
405  O  O     . VAL A 51  ? 0.7797 0.5902 0.2659 0.3602  0.0392  -0.0126 51  VAL A O     
406  C  CB    . VAL A 51  ? 0.7231 0.606  0.2883 0.3292  0.0783  -0.0169 51  VAL A CB    
407  C  CG1   . VAL A 51  ? 0.7588 0.5882 0.2895 0.329   0.0828  -0.0169 51  VAL A CG1   
408  C  CG2   . VAL A 51  ? 0.7007 0.6296 0.3061 0.3145  0.0911  -0.0185 51  VAL A CG2   
409  N  N     . VAL A 52  ? 0.8265 0.564  0.2635 0.3145  0.07    -0.0025 52  VAL A N     
410  C  CA    . VAL A 52  ? 0.8916 0.55   0.2556 0.3257  0.0561  0.0028  52  VAL A CA    
411  C  C     . VAL A 52  ? 0.9245 0.5463 0.2687 0.3347  0.0569  0.0003  52  VAL A C     
412  O  O     . VAL A 52  ? 0.931  0.5415 0.276  0.3093  0.0789  -0.0019 52  VAL A O     
413  C  CB    . VAL A 52  ? 0.9439 0.5428 0.2511 0.2944  0.0706  0.0089  52  VAL A CB    
414  C  CG1   . VAL A 52  ? 1.0167 0.5186 0.2308 0.3069  0.0528  0.0169  52  VAL A CG1   
415  C  CG2   . VAL A 52  ? 0.9241 0.5666 0.2595 0.281   0.0749  0.0085  52  VAL A CG2   
416  N  N     . LYS A 53  ? 0.938  0.5487 0.2711 0.372   0.0321  -0.0035 53  LYS A N     
417  C  CA    . LYS A 53  ? 0.9671 0.5406 0.2799 0.3852  0.0297  -0.0078 53  LYS A CA    
418  C  C     . LYS A 53  ? 1.0511 0.5083 0.2689 0.3721  0.0312  0.0006  53  LYS A C     
419  O  O     . LYS A 53  ? 1.0841 0.4878 0.2458 0.3586  0.03    0.0097  53  LYS A O     
420  C  CB    . LYS A 53  ? 0.9692 0.5712 0.3022 0.4326  0.0008  -0.0198 53  LYS A CB    
421  C  CG    . LYS A 53  ? 0.9498 0.6633 0.37   0.438   0.0047  -0.0308 53  LYS A CG    
422  C  CD    . LYS A 53  ? 0.9657 0.7175 0.4221 0.4561  0.0057  -0.0448 53  LYS A CD    
423  C  CE    . LYS A 53  ? 0.9826 0.7567 0.4659 0.4254  0.0344  -0.0411 53  LYS A CE    
424  N  NZ    . LYS A 53  ? 0.9798 0.7938 0.4955 0.4421  0.0361  -0.0554 53  LYS A NZ    
425  N  N     . SER A 54  ? 1.0853 0.4984 0.2788 0.3733  0.0351  -0.0031 54  SER A N     
426  C  CA    . SER A 54  ? 1.1762 0.47   0.273  0.3563  0.0393  0.0033  54  SER A CA    
427  C  C     . SER A 54  ? 1.2531 0.4544 0.2597 0.3813  0.0088  0.0127  54  SER A C     
428  O  O     . SER A 54  ? 1.3187 0.4206 0.2345 0.3536  0.0176  0.023   54  SER A O     
429  C  CB    . SER A 54  ? 1.2122 0.478  0.3017 0.3665  0.0388  -0.005  54  SER A CB    
430  O  OG    . SER A 54  ? 1.2051 0.543  0.3649 0.3421  0.0653  -0.0144 54  SER A OG    
431  N  N     . ASN A 55  ? 1.2434 0.4778 0.2727 0.4329  -0.0272 0.0064  55  ASN A N     
432  C  CA    . ASN A 55  ? 1.3115 0.4667 0.2614 0.4682  -0.0657 0.0107  55  ASN A CA    
433  C  C     . ASN A 55  ? 1.3088 0.5014 0.2705 0.4655  -0.0726 0.0152  55  ASN A C     
434  O  O     . ASN A 55  ? 1.3285 0.5045 0.264  0.5074  -0.1117 0.0109  55  ASN A O     
435  C  CB    . ASN A 55  ? 1.3217 0.4892 0.287  0.5311  -0.1062 -0.0062 55  ASN A CB    
436  C  CG    . ASN A 55  ? 1.277  0.592  0.3639 0.5539  -0.1099 -0.0255 55  ASN A CG    
437  O  OD1   . ASN A 55  ? 1.2486 0.6545 0.4109 0.5214  -0.0798 -0.0242 55  ASN A OD1   
438  N  ND2   . ASN A 55  ? 1.264  0.6029 0.3692 0.61    -0.147  -0.0464 55  ASN A ND2   
439  N  N     . ASP A 56  ? 1.2781 0.5231 0.281  0.4189  -0.037  0.0206  56  ASP A N     
440  C  CA    . ASP A 56  ? 1.2574 0.54   0.2751 0.4065  -0.0355 0.0244  56  ASP A CA    
441  C  C     . ASP A 56  ? 1.1768 0.5611 0.2743 0.4433  -0.0607 0.0115  56  ASP A C     
442  O  O     . ASP A 56  ? 1.1659 0.5749 0.2696 0.4396  -0.0665 0.0127  56  ASP A O     
443  C  CB    . ASP A 56  ? 1.3797 0.5428 0.2777 0.3982  -0.0461 0.0379  56  ASP A CB    
444  C  CG    . ASP A 56  ? 1.527  0.6    0.3517 0.3485  -0.0113 0.047   56  ASP A CG    
445  O  OD1   . ASP A 56  ? 1.5242 0.6491 0.3965 0.3029  0.0284  0.044   56  ASP A OD1   
446  O  OD2   . ASP A 56  ? 1.6251 0.5761 0.3457 0.3556  -0.0245 0.0542  56  ASP A OD2   
447  N  N     . VAL A 57  ? 1.1176 0.5667 0.2796 0.4735  -0.0713 -0.0035 57  VAL A N     
448  C  CA    . VAL A 57  ? 1.0425 0.5983 0.2871 0.5002  -0.088  -0.0212 57  VAL A CA    
449  C  C     . VAL A 57  ? 0.9782 0.625  0.3025 0.4616  -0.0536 -0.0199 57  VAL A C     
450  O  O     . VAL A 57  ? 0.9699 0.6307 0.3189 0.4372  -0.0258 -0.0163 57  VAL A O     
451  C  CB    . VAL A 57  ? 1.0168 0.6109 0.2998 0.5424  -0.1073 -0.0422 57  VAL A CB    
452  C  CG1   . VAL A 57  ? 0.9456 0.6691 0.3288 0.5547  -0.1101 -0.0648 57  VAL A CG1   
453  C  CG2   . VAL A 57  ? 1.074  0.5797 0.2794 0.5909  -0.1509 -0.0481 57  VAL A CG2   
454  N  N     . ARG A 58  ? 0.934  0.6368 0.2936 0.4573  -0.0578 -0.0238 58  ARG A N     
455  C  CA    . ARG A 58  ? 0.8803 0.6596 0.3077 0.4239  -0.0294 -0.0232 58  ARG A CA    
456  C  C     . ARG A 58  ? 0.8173 0.6914 0.3233 0.4383  -0.0303 -0.0421 58  ARG A C     
457  O  O     . ARG A 58  ? 0.8033 0.7116 0.3277 0.4714  -0.0561 -0.0607 58  ARG A O     
458  C  CB    . ARG A 58  ? 0.886  0.6744 0.3097 0.407   -0.03   -0.019  58  ARG A CB    
459  C  CG    . ARG A 58  ? 0.9411 0.6671 0.3142 0.3723  -0.0088 -0.0029 58  ARG A CG    
460  C  CD    . ARG A 58  ? 1.0343 0.6533 0.3101 0.3795  -0.0207 0.0066  58  ARG A CD    
461  N  NE    . ARG A 58  ? 1.0823 0.6501 0.3092 0.3416  0.002   0.017   58  ARG A NE    
462  C  CZ    . ARG A 58  ? 1.1488 0.6166 0.2845 0.3291  0.0064  0.0263  58  ARG A CZ    
463  N  NH1   . ARG A 58  ? 1.1846 0.5819 0.2617 0.3544  -0.0137 0.0294  58  ARG A NH1   
464  N  NH2   . ARG A 58  ? 1.1549 0.5899 0.2542 0.2895  0.0321  0.0306  58  ARG A NH2   
465  N  N     . GLU A 59  ? 0.7767 0.6909 0.3251 0.4143  -0.003  -0.0402 59  GLU A N     
466  C  CA    . GLU A 59  ? 0.7249 0.7221 0.3375 0.4187  0.0029  -0.0571 59  GLU A CA    
467  C  C     . GLU A 59  ? 0.7031 0.7347 0.3481 0.3813  0.0313  -0.0495 59  GLU A C     
468  O  O     . GLU A 59  ? 0.7315 0.7223 0.3532 0.3597  0.0445  -0.0341 59  GLU A O     
469  C  CB    . GLU A 59  ? 0.7448 0.7384 0.3582 0.4426  -0.0007 -0.0672 59  GLU A CB    
470  C  CG    . GLU A 59  ? 0.8006 0.7528 0.3938 0.4242  0.02    -0.0536 59  GLU A CG    
471  C  CD    . GLU A 59  ? 0.8467 0.8145 0.4543 0.442   0.0215  -0.0662 59  GLU A CD    
472  O  OE1   . GLU A 59  ? 0.8564 0.83   0.4742 0.4222  0.0426  -0.0613 59  GLU A OE1   
473  O  OE2   . GLU A 59  ? 0.8555 0.8305 0.4639 0.4779  -0.0003 -0.0835 59  GLU A OE2   
474  N  N     . PRO A 60  ? 0.6527 0.7554 0.347  0.3717  0.0405  -0.062  60  PRO A N     
475  C  CA    . PRO A 60  ? 0.6407 0.7569 0.3492 0.3373  0.0637  -0.0528 60  PRO A CA    
476  C  C     . PRO A 60  ? 0.655  0.7474 0.3528 0.3293  0.079   -0.0445 60  PRO A C     
477  O  O     . PRO A 60  ? 0.6652 0.7508 0.358  0.3476  0.0763  -0.05   60  PRO A O     
478  C  CB    . PRO A 60  ? 0.6089 0.798  0.3613 0.3279  0.0701  -0.0708 60  PRO A CB    
479  C  CG    . PRO A 60  ? 0.5972 0.8218 0.369  0.3587  0.057   -0.0927 60  PRO A CG    
480  C  CD    . PRO A 60  ? 0.6075 0.7795 0.3435 0.3899  0.0308  -0.0881 60  PRO A CD    
481  N  N     . PHE A 61  ? 0.654  0.7333 0.3477 0.3045  0.0925  -0.0335 61  PHE A N     
482  C  CA    . PHE A 61  ? 0.6624 0.7213 0.3463 0.2988  0.103   -0.0284 61  PHE A CA    
483  C  C     . PHE A 61  ? 0.6528 0.7487 0.3523 0.2981  0.1123  -0.0375 61  PHE A C     
484  O  O     . PHE A 61  ? 0.6472 0.7768 0.3611 0.282   0.1204  -0.042  61  PHE A O     
485  C  CB    . PHE A 61  ? 0.6669 0.7049 0.3429 0.2783  0.1091  -0.0194 61  PHE A CB    
486  C  CG    . PHE A 61  ? 0.6808 0.6999 0.3469 0.2761  0.1148  -0.0179 61  PHE A CG    
487  C  CD1   . PHE A 61  ? 0.7017 0.6926 0.3574 0.2825  0.1132  -0.0191 61  PHE A CD1   
488  C  CD2   . PHE A 61  ? 0.6881 0.7144 0.3504 0.2658  0.1213  -0.0169 61  PHE A CD2   
489  C  CE1   . PHE A 61  ? 0.7135 0.6929 0.3642 0.282   0.1155  -0.0219 61  PHE A CE1   
490  C  CE2   . PHE A 61  ? 0.7062 0.7115 0.3539 0.2676  0.1218  -0.0166 61  PHE A CE2   
491  C  CZ    . PHE A 61  ? 0.7099 0.6965 0.3564 0.2774  0.1175  -0.0204 61  PHE A CZ    
492  N  N     . ASN A 62  ? 0.6479 0.7359 0.3414 0.3125  0.1131  -0.0417 62  ASN A N     
493  C  CA    . ASN A 62  ? 0.6214 0.7438 0.3261 0.3132  0.1234  -0.053  62  ASN A CA    
494  C  C     . ASN A 62  ? 0.6277 0.722  0.311  0.305   0.1317  -0.046  62  ASN A C     
495  O  O     . ASN A 62  ? 0.6451 0.7123 0.3169 0.3185  0.1269  -0.0461 62  ASN A O     
496  C  CB    . ASN A 62  ? 0.6249 0.7615 0.3393 0.3426  0.1135  -0.0681 62  ASN A CB    
497  C  CG    . ASN A 62  ? 0.6366 0.8307 0.3759 0.3447  0.1239  -0.0886 62  ASN A CG    
498  O  OD1   . ASN A 62  ? 0.6428 0.8411 0.3739 0.3318  0.1397  -0.0893 62  ASN A OD1   
499  N  ND2   . ASN A 62  ? 0.6238 0.8652 0.3931 0.3612  0.1146  -0.1088 62  ASN A ND2   
500  N  N     . GLU A 63  ? 0.6144 0.7105 0.2871 0.283   0.1428  -0.0414 63  GLU A N     
501  C  CA    . GLU A 63  ? 0.6242 0.6884 0.2689 0.2777  0.1458  -0.0355 63  GLU A CA    
502  C  C     . GLU A 63  ? 0.622  0.696  0.2633 0.2902  0.1509  -0.0459 63  GLU A C     
503  O  O     . GLU A 63  ? 0.643  0.6876 0.2674 0.2973  0.146   -0.0441 63  GLU A O     
504  C  CB    . GLU A 63  ? 0.6516 0.7061 0.2724 0.2523  0.1549  -0.0288 63  GLU A CB    
505  C  CG    . GLU A 63  ? 0.7482 0.7538 0.3312 0.2508  0.1483  -0.0205 63  GLU A CG    
506  C  CD    . GLU A 63  ? 0.8618 0.8393 0.4035 0.2268  0.1547  -0.0125 63  GLU A CD    
507  O  OE1   . GLU A 63  ? 0.898  0.8502 0.4309 0.2193  0.1465  -0.0047 63  GLU A OE1   
508  O  OE2   . GLU A 63  ? 0.8758 0.8513 0.3882 0.2143  0.1684  -0.0145 63  GLU A OE2   
509  N  N     . GLU A 64  ? 0.5888 0.7092 0.2497 0.2934  0.1601  -0.0607 64  GLU A N     
510  C  CA    . GLU A 64  ? 0.5728 0.7111 0.2353 0.3071  0.1658  -0.0755 64  GLU A CA    
511  C  C     . GLU A 64  ? 0.561  0.675  0.2264 0.3352  0.1503  -0.078  64  GLU A C     
512  O  O     . GLU A 64  ? 0.5716 0.667  0.2216 0.3428  0.1507  -0.0812 64  GLU A O     
513  C  CB    . GLU A 64  ? 0.5846 0.7887 0.2775 0.3062  0.178   -0.0978 64  GLU A CB    
514  C  CG    . GLU A 64  ? 0.6836 0.9104 0.3664 0.27    0.2005  -0.0994 64  GLU A CG    
515  C  CD    . GLU A 64  ? 0.7739 1.0767 0.4993 0.2627  0.2125  -0.1253 64  GLU A CD    
516  O  OE1   . GLU A 64  ? 0.7942 1.1171 0.5498 0.271   0.1997  -0.1284 64  GLU A OE1   
517  O  OE2   . GLU A 64  ? 0.7785 1.1235 0.5071 0.2475  0.2353  -0.1456 64  GLU A OE2   
518  N  N     . LYS A 65  ? 0.5479 0.6537 0.2251 0.3483  0.1366  -0.0761 65  LYS A N     
519  C  CA    . LYS A 65  ? 0.5599 0.6262 0.2255 0.3699  0.1228  -0.0766 65  LYS A CA    
520  C  C     . LYS A 65  ? 0.5851 0.6056 0.2279 0.3592  0.1236  -0.0663 65  LYS A C     
521  O  O     . LYS A 65  ? 0.5964 0.5931 0.2267 0.369   0.1214  -0.0722 65  LYS A O     
522  C  CB    . LYS A 65  ? 0.5713 0.6223 0.2373 0.3795  0.1085  -0.0725 65  LYS A CB    
523  C  CG    . LYS A 65  ? 0.5792 0.6672 0.2659 0.4035  0.0978  -0.0896 65  LYS A CG    
524  C  CD    . LYS A 65  ? 0.6161 0.6655 0.2844 0.4198  0.0772  -0.0847 65  LYS A CD    
525  C  CE    . LYS A 65  ? 0.6253 0.7168 0.3171 0.4486  0.0604  -0.1058 65  LYS A CE    
526  N  NZ    . LYS A 65  ? 0.6816 0.7162 0.338  0.4772  0.0333  -0.1045 65  LYS A NZ    
527  N  N     . LEU A 66  ? 0.5914 0.6039 0.2315 0.3397  0.1259  -0.0549 66  LEU A N     
528  C  CA    . LEU A 66  ? 0.6146 0.5968 0.2423 0.3305  0.1243  -0.0514 66  LEU A CA    
529  C  C     . LEU A 66  ? 0.6395 0.6222 0.2551 0.3317  0.1274  -0.0573 66  LEU A C     
530  O  O     . LEU A 66  ? 0.6568 0.6186 0.2654 0.3359  0.1238  -0.0641 66  LEU A O     
531  C  CB    . LEU A 66  ? 0.6069 0.588  0.2371 0.3144  0.1232  -0.0422 66  LEU A CB    
532  C  CG    . LEU A 66  ? 0.6193 0.5802 0.2432 0.3085  0.1181  -0.0445 66  LEU A CG    
533  C  CD1   . LEU A 66  ? 0.6319 0.5741 0.2601 0.3085  0.1168  -0.0524 66  LEU A CD1   
534  C  CD2   . LEU A 66  ? 0.6216 0.581  0.246  0.2979  0.1145  -0.0381 66  LEU A CD2   
535  N  N     . ARG A 67  ? 0.6374 0.6418 0.2465 0.3252  0.1353  -0.0563 67  ARG A N     
536  C  CA    . ARG A 67  ? 0.6495 0.6491 0.2352 0.3238  0.1392  -0.0604 67  ARG A CA    
537  C  C     . ARG A 67  ? 0.6493 0.6547 0.236  0.3397  0.1414  -0.074  67  ARG A C     
538  O  O     . ARG A 67  ? 0.6673 0.6524 0.2381 0.3439  0.1365  -0.0791 67  ARG A O     
539  C  CB    . ARG A 67  ? 0.6688 0.6847 0.2384 0.3066  0.1521  -0.0563 67  ARG A CB    
540  C  CG    . ARG A 67  ? 0.7339 0.7382 0.2652 0.3014  0.159   -0.0597 67  ARG A CG    
541  C  CD    . ARG A 67  ? 0.7987 0.7847 0.2901 0.2772  0.167   -0.0493 67  ARG A CD    
542  N  NE    . ARG A 67  ? 0.8325 0.8513 0.3439 0.2598  0.1813  -0.0487 67  ARG A NE    
543  C  CZ    . ARG A 67  ? 0.8892 0.8899 0.3913 0.2438  0.1789  -0.0367 67  ARG A CZ    
544  N  NH1   . ARG A 67  ? 0.9153 0.8637 0.3863 0.2455  0.1617  -0.0248 67  ARG A NH1   
545  N  NH2   . ARG A 67  ? 0.8809 0.9176 0.4059 0.2274  0.1921  -0.0399 67  ARG A NH2   
546  N  N     . SER A 68  ? 0.6283 0.6618 0.2342 0.3509  0.146   -0.0829 68  SER A N     
547  C  CA    . SER A 68  ? 0.6277 0.6674 0.2355 0.3703  0.1463  -0.0991 68  SER A CA    
548  C  C     . SER A 68  ? 0.645  0.6417 0.2433 0.3807  0.1351  -0.1008 68  SER A C     
549  O  O     . SER A 68  ? 0.6592 0.6469 0.2461 0.3892  0.1353  -0.1119 68  SER A O     
550  C  CB    . SER A 68  ? 0.6248 0.6999 0.2586 0.3869  0.1459  -0.1115 68  SER A CB    
551  O  OG    . SER A 68  ? 0.6358 0.7576 0.2859 0.3725  0.1577  -0.1136 68  SER A OG    
552  N  N     . GLY A 69  ? 0.644  0.6141 0.2448 0.377   0.1273  -0.0921 69  GLY A N     
553  C  CA    . GLY A 69  ? 0.6653 0.5919 0.2538 0.3784  0.1212  -0.0956 69  GLY A CA    
554  C  C     . GLY A 69  ? 0.6755 0.5932 0.2573 0.3676  0.1211  -0.1003 69  GLY A C     
555  O  O     . GLY A 69  ? 0.6931 0.589  0.2652 0.3714  0.1191  -0.1119 69  GLY A O     
556  N  N     . MET A 70  ? 0.6666 0.5993 0.2508 0.3563  0.1209  -0.0935 70  MET A N     
557  C  CA    . MET A 70  ? 0.675  0.601  0.2512 0.3517  0.1145  -0.1004 70  MET A CA    
558  C  C     . MET A 70  ? 0.6838 0.6146 0.2404 0.3605  0.1161  -0.1078 70  MET A C     
559  O  O     . MET A 70  ? 0.698  0.6165 0.248  0.3644  0.1103  -0.1211 70  MET A O     
560  C  CB    . MET A 70  ? 0.6821 0.613  0.2572 0.3428  0.109   -0.0914 70  MET A CB    
561  C  CG    . MET A 70  ? 0.7076 0.6373 0.3024 0.3336  0.1084  -0.0863 70  MET A CG    
562  S  SD    . MET A 70  ? 0.7402 0.6707 0.3329 0.3272  0.0986  -0.0795 70  MET A SD    
563  C  CE    . MET A 70  ? 0.7179 0.6405 0.3071 0.3352  0.0813  -0.1    70  MET A CE    
564  N  N     . LEU A 71  ? 0.6753 0.6264 0.2226 0.3614  0.1258  -0.1025 71  LEU A N     
565  C  CA    . LEU A 71  ? 0.6796 0.6372 0.2033 0.366   0.1317  -0.111  71  LEU A CA    
566  C  C     . LEU A 71  ? 0.6823 0.6365 0.2101 0.3814  0.132   -0.1275 71  LEU A C     
567  O  O     . LEU A 71  ? 0.7023 0.6507 0.2091 0.3856  0.1313  -0.1378 71  LEU A O     
568  C  CB    . LEU A 71  ? 0.6734 0.6599 0.19   0.3576  0.148   -0.1068 71  LEU A CB    
569  C  CG    . LEU A 71  ? 0.699  0.6751 0.1897 0.3386  0.1498  -0.0919 71  LEU A CG    
570  C  CD1   . LEU A 71  ? 0.6904 0.6973 0.1741 0.3232  0.1717  -0.0924 71  LEU A CD1   
571  C  CD2   . LEU A 71  ? 0.7372 0.6776 0.1825 0.3378  0.1392  -0.0913 71  LEU A CD2   
572  N  N     . ARG A 72  ? 0.674  0.6247 0.2219 0.3907  0.131   -0.1301 72  ARG A N     
573  C  CA    . ARG A 72  ? 0.6836 0.6169 0.2295 0.4066  0.1277  -0.1447 72  ARG A CA    
574  C  C     . ARG A 72  ? 0.7075 0.6074 0.2433 0.4006  0.1202  -0.1523 72  ARG A C     
575  O  O     . ARG A 72  ? 0.7211 0.6122 0.2442 0.4082  0.1189  -0.1669 72  ARG A O     
576  C  CB    . ARG A 72  ? 0.6874 0.608  0.2439 0.4183  0.1239  -0.1433 72  ARG A CB    
577  C  CG    . ARG A 72  ? 0.6928 0.6441 0.2592 0.44    0.1266  -0.1556 72  ARG A CG    
578  C  CD    . ARG A 72  ? 0.677  0.6451 0.2616 0.4462  0.123   -0.1495 72  ARG A CD    
579  N  NE    . ARG A 72  ? 0.7106 0.6391 0.2854 0.4695  0.108   -0.1555 72  ARG A NE    
580  C  CZ    . ARG A 72  ? 0.7262 0.6742 0.3122 0.4989  0.0994  -0.1719 72  ARG A CZ    
581  N  NH1   . ARG A 72  ? 0.6987 0.7181 0.3153 0.5041  0.1092  -0.1869 72  ARG A NH1   
582  N  NH2   . ARG A 72  ? 0.7491 0.6434 0.3127 0.5233  0.0806  -0.1763 72  ARG A NH2   
583  N  N     . ALA A 73  ? 0.7178 0.6043 0.2622 0.3857  0.1157  -0.1458 73  ALA A N     
584  C  CA    . ALA A 73  ? 0.7405 0.6069 0.2852 0.3753  0.1099  -0.1586 73  ALA A CA    
585  C  C     . ALA A 73  ? 0.7618 0.6428 0.2987 0.3762  0.1018  -0.1674 73  ALA A C     
586  O  O     . ALA A 73  ? 0.7751 0.6463 0.31   0.375   0.0957  -0.1857 73  ALA A O     
587  C  CB    . ALA A 73  ? 0.7378 0.5975 0.2985 0.3577  0.11    -0.1538 73  ALA A CB    
588  N  N     . LEU A 74  ? 0.7679 0.6667 0.2941 0.378   0.1009  -0.1555 74  LEU A N     
589  C  CA    . LEU A 74  ? 0.7866 0.6853 0.2883 0.3811  0.0897  -0.1603 74  LEU A CA    
590  C  C     . LEU A 74  ? 0.8187 0.7189 0.2882 0.3895  0.0967  -0.1638 74  LEU A C     
591  O  O     . LEU A 74  ? 0.8433 0.7388 0.2771 0.3886  0.0942  -0.1582 74  LEU A O     
592  C  CB    . LEU A 74  ? 0.7858 0.6862 0.278  0.3756  0.0843  -0.1444 74  LEU A CB    
593  C  CG    . LEU A 74  ? 0.7863 0.6889 0.3074 0.3691  0.0753  -0.1448 74  LEU A CG    
594  C  CD1   . LEU A 74  ? 0.7948 0.6966 0.3068 0.3639  0.0757  -0.1255 74  LEU A CD1   
595  C  CD2   . LEU A 74  ? 0.7875 0.6882 0.3128 0.3748  0.054   -0.1661 74  LEU A CD2   
596  N  N     . GLU A 75  ? 0.822  0.7234 0.298  0.3972  0.1055  -0.1742 75  GLU A N     
597  C  CA    . GLU A 75  ? 0.8358 0.7443 0.286  0.4058  0.1139  -0.1832 75  GLU A CA    
598  C  C     . GLU A 75  ? 0.8568 0.7485 0.2832 0.41    0.1006  -0.1991 75  GLU A C     
599  O  O     . GLU A 75  ? 0.8568 0.7361 0.3006 0.4104  0.0902  -0.2124 75  GLU A O     
600  C  CB    . GLU A 75  ? 0.8562 0.7709 0.3233 0.4184  0.1236  -0.1932 75  GLU A CB    
601  C  CG    . GLU A 75  ? 0.9076 0.8531 0.3892 0.4201  0.1373  -0.1852 75  GLU A CG    
602  C  CD    . GLU A 75  ? 0.9885 0.9643 0.4487 0.4153  0.1534  -0.1886 75  GLU A CD    
603  O  OE1   . GLU A 75  ? 1.0062 1.0081 0.473  0.4042  0.1651  -0.1789 75  GLU A OE1   
604  O  OE2   . GLU A 75  ? 1.023  0.9956 0.457  0.4197  0.1562  -0.2028 75  GLU A OE2   
605  N  N     . LYS A 76  ? 0.8744 0.7635 0.2568 0.4104  0.101   -0.1988 76  LYS A N     
606  C  CA    . LYS A 76  ? 0.898  0.7689 0.246  0.417   0.0857  -0.214  76  LYS A CA    
607  C  C     . LYS A 76  ? 0.907  0.7649 0.2621 0.4185  0.0585  -0.2197 76  LYS A C     
608  O  O     . LYS A 76  ? 0.9229 0.7714 0.2642 0.4266  0.0409  -0.2392 76  LYS A O     
609  C  CB    . LYS A 76  ? 0.9105 0.7824 0.2642 0.427   0.0899  -0.2364 76  LYS A CB    
610  C  CG    . LYS A 76  ? 0.9475 0.8367 0.2848 0.4306  0.1129  -0.239  76  LYS A CG    
611  C  CD    . LYS A 76  ? 0.9918 0.8801 0.3358 0.4447  0.1161  -0.2632 76  LYS A CD    
612  C  CE    . LYS A 76  ? 1.013  0.9278 0.3442 0.4509  0.1384  -0.2732 76  LYS A CE    
613  N  NZ    . LYS A 76  ? 1.0062 0.9303 0.3722 0.4686  0.1436  -0.2886 76  LYS A NZ    
614  N  N     . ARG A 77  ? 0.8947 0.7562 0.2719 0.4119  0.0541  -0.2061 77  ARG A N     
615  C  CA    . ARG A 77  ? 0.8906 0.7499 0.284  0.4149  0.029   -0.2157 77  ARG A CA    
616  C  C     . ARG A 77  ? 0.9274 0.7624 0.2714 0.4213  0.0107  -0.2045 77  ARG A C     
617  O  O     . ARG A 77  ? 0.9488 0.77   0.258  0.4136  0.0242  -0.1815 77  ARG A O     
618  C  CB    . ARG A 77  ? 0.8624 0.7386 0.3096 0.404   0.0357  -0.2114 77  ARG A CB    
619  C  CG    . ARG A 77  ? 0.855  0.7372 0.3359 0.3961  0.0525  -0.2196 77  ARG A CG    
620  C  CD    . ARG A 77  ? 0.8669 0.7462 0.3549 0.3973  0.045   -0.2484 77  ARG A CD    
621  N  NE    . ARG A 77  ? 0.8745 0.7659 0.3768 0.3992  0.0214  -0.2713 77  ARG A NE    
622  C  CZ    . ARG A 77  ? 0.9012 0.794  0.3955 0.4068  0.0052  -0.2976 77  ARG A CZ    
623  N  NH1   . ARG A 77  ? 0.8788 0.7904 0.3925 0.4118  -0.0197 -0.3229 77  ARG A NH1   
624  N  NH2   . ARG A 77  ? 0.92   0.7985 0.3889 0.4115  0.0122  -0.3023 77  ARG A NH2   
625  N  N     . PRO A 78  ? 0.9342 0.7612 0.2725 0.4353  -0.0216 -0.2228 78  PRO A N     
626  C  CA    . PRO A 78  ? 0.971  0.7591 0.2487 0.4468  -0.046  -0.2128 78  PRO A CA    
627  C  C     . PRO A 78  ? 0.9724 0.7579 0.2672 0.445   -0.053  -0.1999 78  PRO A C     
628  O  O     . PRO A 78  ? 0.9767 0.76   0.2813 0.4616  -0.0849 -0.2158 78  PRO A O     
629  C  CB    . PRO A 78  ? 0.98   0.7627 0.2466 0.469   -0.0829 -0.2434 78  PRO A CB    
630  C  CG    . PRO A 78  ? 0.9401 0.7724 0.2876 0.464   -0.0792 -0.2718 78  PRO A CG    
631  C  CD    . PRO A 78  ? 0.9038 0.7541 0.2854 0.4419  -0.039  -0.257  78  PRO A CD    
632  N  N     . VAL A 79  ? 0.9647 0.7542 0.2659 0.4264  -0.0241 -0.1747 79  VAL A N     
633  C  CA    . VAL A 79  ? 0.9657 0.7522 0.2808 0.4205  -0.0243 -0.1594 79  VAL A CA    
634  C  C     . VAL A 79  ? 1.0045 0.7559 0.2558 0.4059  -0.0062 -0.1308 79  VAL A C     
635  O  O     . VAL A 79  ? 1.006  0.7741 0.2573 0.3909  0.0242  -0.1229 79  VAL A O     
636  C  CB    . VAL A 79  ? 0.9331 0.7652 0.3244 0.407   -0.0021 -0.1608 79  VAL A CB    
637  C  CG1   . VAL A 79  ? 0.9395 0.7702 0.3427 0.3979  0.0031  -0.1426 79  VAL A CG1   
638  C  CG2   . VAL A 79  ? 0.9074 0.7702 0.3546 0.4128  -0.0143 -0.1916 79  VAL A CG2   
639  N  N     . SER A 80  ? 1.0363 0.7365 0.2284 0.41    -0.0254 -0.1188 80  SER A N     
640  C  CA    . SER A 80  ? 1.073  0.7314 0.1941 0.3888  -0.0058 -0.0931 80  SER A CA    
641  C  C     . SER A 80  ? 1.0416 0.7301 0.2047 0.3659  0.0233  -0.0773 80  SER A C     
642  O  O     . SER A 80  ? 1.0031 0.7299 0.237  0.3702  0.0213  -0.0829 80  SER A O     
643  C  CB    . SER A 80  ? 1.1461 0.723  0.1755 0.3992  -0.0373 -0.0845 80  SER A CB    
644  O  OG    . SER A 80  ? 1.1762 0.74   0.2233 0.4081  -0.0579 -0.0815 80  SER A OG    
645  N  N     . SER A 81  ? 1.0564 0.7299 0.1751 0.3395  0.0515  -0.0604 81  SER A N     
646  C  CA    . SER A 81  ? 1.0355 0.738  0.189  0.3169  0.0775  -0.0482 81  SER A CA    
647  C  C     . SER A 81  ? 1.0258 0.6997 0.1804 0.3201  0.0572  -0.0386 81  SER A C     
648  O  O     . SER A 81  ? 0.9979 0.7072 0.2064 0.3113  0.069   -0.0345 81  SER A O     
649  C  CB    . SER A 81  ? 1.0888 0.779  0.1869 0.2846  0.1108  -0.038  81  SER A CB    
650  O  OG    . SER A 81  ? 1.1296 0.8305 0.2415 0.2604  0.1293  -0.0264 81  SER A OG    
651  N  N     . ASP A 82  ? 1.0531 0.6603 0.1446 0.3353  0.0245  -0.0367 82  ASP A N     
652  C  CA    . ASP A 82  ? 1.0582 0.6305 0.1432 0.3456  -0.0016 -0.0324 82  ASP A CA    
653  C  C     . ASP A 82  ? 0.9988 0.6285 0.1774 0.3679  -0.0174 -0.0524 82  ASP A C     
654  O  O     . ASP A 82  ? 0.9832 0.629  0.2007 0.3635  -0.0155 -0.0494 82  ASP A O     
655  C  CB    . ASP A 82  ? 1.1383 0.6201 0.1251 0.3635  -0.038  -0.0302 82  ASP A CB    
656  C  CG    . ASP A 82  ? 1.1934 0.6447 0.1839 0.3904  -0.0781 -0.0375 82  ASP A CG    
657  O  OD1   . ASP A 82  ? 1.1906 0.6229 0.1766 0.3765  -0.072  -0.0242 82  ASP A OD1   
658  O  OD2   . ASP A 82  ? 1.2303 0.6818 0.2324 0.4262  -0.1163 -0.0603 82  ASP A OD2   
659  N  N     . ASP A 83  ? 0.9679 0.6282 0.1805 0.3876  -0.0303 -0.0744 83  ASP A N     
660  C  CA    . ASP A 83  ? 0.9187 0.635  0.2169 0.4012  -0.0394 -0.0976 83  ASP A CA    
661  C  C     . ASP A 83  ? 0.8779 0.6458 0.2403 0.3806  -0.0068 -0.0908 83  ASP A C     
662  O  O     . ASP A 83  ? 0.8539 0.6494 0.2692 0.3822  -0.01   -0.0999 83  ASP A O     
663  C  CB    . ASP A 83  ? 0.9265 0.6675 0.2446 0.4154  -0.0485 -0.1216 83  ASP A CB    
664  C  CG    . ASP A 83  ? 1.0233 0.7216 0.2883 0.4425  -0.0882 -0.136  83  ASP A CG    
665  O  OD1   . ASP A 83  ? 1.0457 0.7128 0.2914 0.4607  -0.1192 -0.141  83  ASP A OD1   
666  O  OD2   . ASP A 83  ? 1.0683 0.7623 0.3089 0.4483  -0.091  -0.1446 83  ASP A OD2   
667  N  N     . VAL A 84  ? 0.869  0.6499 0.225  0.3627  0.0232  -0.0777 84  VAL A N     
668  C  CA    . VAL A 84  ? 0.8371 0.6611 0.245  0.3479  0.0497  -0.072  84  VAL A CA    
669  C  C     . VAL A 84  ? 0.8385 0.6546 0.2461 0.3353  0.0542  -0.0567 84  VAL A C     
670  O  O     . VAL A 84  ? 0.8166 0.6584 0.2724 0.3338  0.0563  -0.0594 84  VAL A O     
671  C  CB    . VAL A 84  ? 0.8395 0.6825 0.2407 0.3378  0.0759  -0.068  84  VAL A CB    
672  C  CG1   . VAL A 84  ? 0.82   0.7015 0.2665 0.3271  0.0973  -0.0625 84  VAL A CG1   
673  C  CG2   . VAL A 84  ? 0.8339 0.6866 0.2424 0.351   0.0719  -0.0853 84  VAL A CG2   
674  N  N     . GLU A 85  ? 0.8679 0.6424 0.2151 0.324   0.0554  -0.0415 85  GLU A N     
675  C  CA    . GLU A 85  ? 0.8756 0.6369 0.2167 0.3087  0.0603  -0.0276 85  GLU A CA    
676  C  C     . GLU A 85  ? 0.8639 0.6108 0.2216 0.324   0.0343  -0.034  85  GLU A C     
677  O  O     . GLU A 85  ? 0.8535 0.6187 0.2446 0.3157  0.0408  -0.0302 85  GLU A O     
678  C  CB    . GLU A 85  ? 0.9577 0.6681 0.2207 0.2877  0.0698  -0.0116 85  GLU A CB    
679  C  CG    . GLU A 85  ? 1.0338 0.7724 0.2891 0.2677  0.1018  -0.0106 85  GLU A CG    
680  C  CD    . GLU A 85  ? 1.0786 0.8903 0.4072 0.2607  0.1251  -0.0162 85  GLU A CD    
681  O  OE1   . GLU A 85  ? 1.0454 0.8739 0.407  0.2536  0.1275  -0.0117 85  GLU A OE1   
682  O  OE2   . GLU A 85  ? 1.1063 0.955  0.4557 0.2648  0.1384  -0.0265 85  GLU A OE2   
683  N  N     . MET A 86  ? 0.8623 0.5838 0.2026 0.3483  0.004   -0.0482 86  MET A N     
684  C  CA    . MET A 86  ? 0.8502 0.5667 0.2118 0.3707  -0.0263 -0.0655 86  MET A CA    
685  C  C     . MET A 86  ? 0.79   0.5727 0.2372 0.3697  -0.0159 -0.0824 86  MET A C     
686  O  O     . MET A 86  ? 0.7847 0.578  0.2619 0.3726  -0.0231 -0.0903 86  MET A O     
687  C  CB    . MET A 86  ? 0.8857 0.5756 0.2163 0.3985  -0.0591 -0.0836 86  MET A CB    
688  C  CG    . MET A 86  ? 0.9313 0.6179 0.2808 0.4277  -0.0964 -0.1091 86  MET A CG    
689  S  SD    . MET A 86  ? 1.1275 0.7344 0.3863 0.4618  -0.1445 -0.1166 86  MET A SD    
690  C  CE    . MET A 86  ? 1.075  0.7193 0.3509 0.4677  -0.1417 -0.1338 86  MET A CE    
691  N  N     . ALA A 87  ? 0.7496 0.5707 0.2295 0.3636  0.0023  -0.088  87  ALA A N     
692  C  CA    . ALA A 87  ? 0.703  0.572  0.2472 0.357   0.0158  -0.1014 87  ALA A CA    
693  C  C     . ALA A 87  ? 0.6857 0.5669 0.2447 0.3381  0.0388  -0.083  87  ALA A C     
694  O  O     . ALA A 87  ? 0.6721 0.5745 0.2682 0.3327  0.0432  -0.0906 87  ALA A O     
695  C  CB    . ALA A 87  ? 0.6916 0.5808 0.2506 0.3567  0.0255  -0.1117 87  ALA A CB    
696  N  N     . ILE A 88  ? 0.6853 0.5567 0.2161 0.3271  0.054   -0.0621 88  ILE A N     
697  C  CA    . ILE A 88  ? 0.6691 0.5572 0.2156 0.3115  0.0726  -0.0483 88  ILE A CA    
698  C  C     . ILE A 88  ? 0.6753 0.5496 0.2199 0.307   0.0647  -0.0435 88  ILE A C     
699  O  O     . ILE A 88  ? 0.6655 0.56   0.2423 0.3013  0.0709  -0.0447 88  ILE A O     
700  C  CB    . ILE A 88  ? 0.6744 0.5671 0.1988 0.3006  0.0906  -0.0356 88  ILE A CB    
701  C  CG1   . ILE A 88  ? 0.6658 0.5783 0.2018 0.3078  0.0992  -0.0438 88  ILE A CG1   
702  C  CG2   . ILE A 88  ? 0.669  0.5817 0.2098 0.2859  0.1047  -0.0256 88  ILE A CG2   
703  C  CD1   . ILE A 88  ? 0.6823 0.6025 0.1962 0.3008  0.1143  -0.0394 88  ILE A CD1   
704  N  N     . ASN A 89  ? 0.6944 0.5274 0.1958 0.3109  0.0488  -0.0393 89  ASN A N     
705  C  CA    . ASN A 89  ? 0.6982 0.5094 0.1924 0.3089  0.0383  -0.0362 89  ASN A CA    
706  C  C     . ASN A 89  ? 0.6524 0.4856 0.1917 0.3218  0.0256  -0.057  89  ASN A C     
707  O  O     . ASN A 89  ? 0.6444 0.4814 0.1989 0.3161  0.0265  -0.0567 89  ASN A O     
708  C  CB    . ASN A 89  ? 0.7714 0.5177 0.1974 0.3139  0.0191  -0.0291 89  ASN A CB    
709  C  CG    . ASN A 89  ? 0.8563 0.5763 0.2293 0.2919  0.0373  -0.0098 89  ASN A CG    
710  O  OD1   . ASN A 89  ? 0.8579 0.6101 0.2494 0.27    0.0635  -0.0014 89  ASN A OD1   
711  N  ND2   . ASN A 89  ? 0.9235 0.5858 0.2277 0.2968  0.0238  -0.0054 89  ASN A ND2   
712  N  N     . HIS A 90  ? 0.6236 0.4742 0.1848 0.337   0.0151  -0.0784 90  HIS A N     
713  C  CA    . HIS A 90  ? 0.59   0.4714 0.1988 0.3449  0.0072  -0.1055 90  HIS A CA    
714  C  C     . HIS A 90  ? 0.5571 0.4751 0.2051 0.3254  0.0334  -0.1051 90  HIS A C     
715  O  O     . HIS A 90  ? 0.543  0.4778 0.2181 0.3207  0.0357  -0.1168 90  HIS A O     
716  C  CB    . HIS A 90  ? 0.5866 0.4815 0.2098 0.3637  -0.0108 -0.1338 90  HIS A CB    
717  C  CG    . HIS A 90  ? 0.5705 0.5016 0.2435 0.3725  -0.0217 -0.17   90  HIS A CG    
718  N  ND1   . HIS A 90  ? 0.5689 0.5369 0.2785 0.3787  -0.0267 -0.2031 90  HIS A ND1   
719  C  CD2   . HIS A 90  ? 0.5697 0.5089 0.2622 0.3749  -0.0274 -0.1813 90  HIS A CD2   
720  C  CE1   . HIS A 90  ? 0.55   0.5527 0.3035 0.3833  -0.0337 -0.2357 90  HIS A CE1   
721  N  NE2   . HIS A 90  ? 0.5541 0.5402 0.2984 0.3824  -0.0345 -0.2235 90  HIS A NE2   
722  N  N     . ILE A 91  ? 0.5434 0.4683 0.1884 0.315   0.0523  -0.0921 91  ILE A N     
723  C  CA    . ILE A 91  ? 0.5235 0.4665 0.1893 0.2992  0.0734  -0.0884 91  ILE A CA    
724  C  C     . ILE A 91  ? 0.5214 0.4604 0.182  0.2898  0.0795  -0.0714 91  ILE A C     
725  O  O     . ILE A 91  ? 0.5242 0.4732 0.2014 0.2803  0.0874  -0.0762 91  ILE A O     
726  C  CB    . ILE A 91  ? 0.5263 0.4693 0.184  0.2971  0.0858  -0.0806 91  ILE A CB    
727  C  CG1   . ILE A 91  ? 0.5292 0.4775 0.1958 0.3029  0.0814  -0.1013 91  ILE A CG1   
728  C  CG2   . ILE A 91  ? 0.5265 0.4716 0.1895 0.2854  0.1018  -0.073  91  ILE A CG2   
729  C  CD1   . ILE A 91  ? 0.5473 0.4893 0.1999 0.3052  0.0892  -0.0952 91  ILE A CD1   
730  N  N     . LYS A 92  ? 0.5227 0.4457 0.1574 0.2897  0.0763  -0.0543 92  LYS A N     
731  C  CA    . LYS A 92  ? 0.5225 0.4434 0.1528 0.2788  0.0811  -0.0411 92  LYS A CA    
732  C  C     . LYS A 92  ? 0.5225 0.4377 0.1624 0.2801  0.0708  -0.0514 92  LYS A C     
733  O  O     . LYS A 92  ? 0.5178 0.4432 0.1705 0.2707  0.0779  -0.0499 92  LYS A O     
734  C  CB    . LYS A 92  ? 0.5582 0.4612 0.1555 0.2728  0.082   -0.0257 92  LYS A CB    
735  C  CG    . LYS A 92  ? 0.5998 0.5206 0.1948 0.2694  0.0961  -0.0193 92  LYS A CG    
736  C  CD    . LYS A 92  ? 0.6864 0.592  0.2463 0.2577  0.1016  -0.0094 92  LYS A CD    
737  C  CE    . LYS A 92  ? 0.7513 0.6575 0.3077 0.2394  0.1078  -0.0018 92  LYS A CE    
738  N  NZ    . LYS A 92  ? 0.8174 0.7013 0.3313 0.2202  0.1169  0.0059  92  LYS A NZ    
739  N  N     . SER A 93  ? 0.5266 0.4259 0.16   0.2946  0.0519  -0.0652 93  SER A N     
740  C  CA    . SER A 93  ? 0.5272 0.4232 0.1726 0.3026  0.0375  -0.0823 93  SER A CA    
741  C  C     . SER A 93  ? 0.4928 0.4272 0.1815 0.2969  0.0482  -0.1039 93  SER A C     
742  O  O     . SER A 93  ? 0.4921 0.4336 0.1938 0.2921  0.0496  -0.1116 93  SER A O     
743  C  CB    . SER A 93  ? 0.5691 0.4409 0.1977 0.3262  0.0099  -0.0974 93  SER A CB    
744  O  OG    . SER A 93  ? 0.638  0.4635 0.229  0.3323  -0.0074 -0.0896 93  SER A OG    
745  N  N     . GLN A 94  ? 0.4674 0.425  0.1783 0.2883  0.0511  -0.1062 94  GLN A N     
746  C  CA    . GLN A 94  ? 0.4432 0.4318 0.191  0.2682  0.0585  -0.1179 94  GLN A CA    
747  C  C     . GLN A 94  ? 0.4525 0.4348 0.1901 0.2517  0.0819  -0.1047 94  GLN A C     
748  O  O     . GLN A 94  ? 0.4419 0.4371 0.1967 0.2364  0.0879  -0.1143 94  GLN A O     
749  C  CB    . GLN A 94  ? 0.444  0.4469 0.205  0.2657  0.0619  -0.1315 94  GLN A CB    
750  C  CG    . GLN A 94  ? 0.4436 0.4655 0.2245 0.2831  0.0386  -0.1597 94  GLN A CG    
751  C  CD    . GLN A 94  ? 0.4579 0.4894 0.2445 0.2854  0.0453  -0.176  94  GLN A CD    
752  O  OE1   . GLN A 94  ? 0.4682 0.4777 0.2284 0.2853  0.0521  -0.1544 94  GLN A OE1   
753  N  NE2   . GLN A 94  ? 0.4385 0.5099 0.2669 0.2809  0.0364  -0.2099 94  GLN A NE2   
754  N  N     . LEU A 95  ? 0.4687 0.4331 0.1784 0.2544  0.0916  -0.083  95  LEU A N     
755  C  CA    . LEU A 95  ? 0.4811 0.4389 0.1757 0.2446  0.1075  -0.0722 95  LEU A CA    
756  C  C     . LEU A 95  ? 0.4841 0.4418 0.1757 0.2433  0.1059  -0.0716 95  LEU A C     
757  O  O     . LEU A 95  ? 0.5031 0.46   0.1905 0.2321  0.1146  -0.0714 95  LEU A O     
758  C  CB    . LEU A 95  ? 0.4961 0.4456 0.1695 0.2508  0.1121  -0.054  95  LEU A CB    
759  C  CG    . LEU A 95  ? 0.5173 0.463  0.1867 0.2566  0.1149  -0.056  95  LEU A CG    
760  C  CD1   . LEU A 95  ? 0.5273 0.4747 0.1862 0.2659  0.1123  -0.0409 95  LEU A CD1   
761  C  CD2   . LEU A 95  ? 0.5348 0.4657 0.1933 0.2474  0.1263  -0.0596 95  LEU A CD2   
762  N  N     . ARG A 96  ? 0.4766 0.4278 0.1672 0.2516  0.0905  -0.0679 96  ARG A N     
763  C  CA    . ARG A 96  ? 0.4769 0.4211 0.1634 0.2492  0.0853  -0.0671 96  ARG A CA    
764  C  C     . ARG A 96  ? 0.4626 0.4196 0.1762 0.246   0.0774  -0.0868 96  ARG A C     
765  O  O     . ARG A 96  ? 0.4528 0.4117 0.1713 0.2359  0.0771  -0.0855 96  ARG A O     
766  C  CB    . ARG A 96  ? 0.5078 0.4269 0.1724 0.2567  0.0714  -0.0577 96  ARG A CB    
767  C  CG    . ARG A 96  ? 0.5487 0.464  0.1946 0.2488  0.0785  -0.0359 96  ARG A CG    
768  C  CD    . ARG A 96  ? 0.6098 0.4945 0.2251 0.2433  0.0714  -0.0253 96  ARG A CD    
769  N  NE    . ARG A 96  ? 0.674  0.5241 0.2658 0.2575  0.0544  -0.0312 96  ARG A NE    
770  C  CZ    . ARG A 96  ? 0.7224 0.5583 0.2918 0.2625  0.0524  -0.0261 96  ARG A CZ    
771  N  NH1   . ARG A 96  ? 0.7093 0.5671 0.2814 0.2534  0.0687  -0.0164 96  ARG A NH1   
772  N  NH2   . ARG A 96  ? 0.7462 0.5446 0.288  0.2791  0.0318  -0.033  96  ARG A NH2   
773  N  N     . ALA A 97  ? 0.4579 0.4292 0.1918 0.2538  0.0697  -0.1077 97  ALA A N     
774  C  CA    . ALA A 97  ? 0.4505 0.4479 0.2157 0.2539  0.0659  -0.1394 97  ALA A CA    
775  C  C     . ALA A 97  ? 0.4546 0.4708 0.2297 0.2309  0.0922  -0.1512 97  ALA A C     
776  O  O     . ALA A 97  ? 0.4449 0.4845 0.2449 0.2238  0.0924  -0.1745 97  ALA A O     
777  C  CB    . ALA A 97  ? 0.4356 0.4537 0.2261 0.2642  0.0484  -0.1593 97  ALA A CB    
778  N  N     . THR A 98  ? 0.4708 0.4733 0.2214 0.2187  0.1129  -0.1357 98  THR A N     
779  C  CA    . THR A 98  ? 0.4862 0.4865 0.2235 0.1952  0.1372  -0.1408 98  THR A CA    
780  C  C     . THR A 98  ? 0.5123 0.5034 0.2296 0.1935  0.1417  -0.1366 98  THR A C     
781  O  O     . THR A 98  ? 0.5236 0.5186 0.2352 0.1753  0.1575  -0.1503 98  THR A O     
782  C  CB    . THR A 98  ? 0.5157 0.4882 0.2142 0.1894  0.1525  -0.1232 98  THR A CB    
783  O  OG1   . THR A 98  ? 0.5341 0.4884 0.2123 0.201   0.1409  -0.0931 98  THR A OG1   
784  C  CG2   . THR A 98  ? 0.5168 0.4935 0.225  0.1937  0.1528  -0.1299 98  THR A CG2   
785  N  N     . GLY A 99  ? 0.5255 0.5034 0.2337 0.2066  0.1254  -0.1146 99  GLY A N     
786  C  CA    . GLY A 99  ? 0.5481 0.5174 0.2432 0.2024  0.1224  -0.1051 99  GLY A CA    
787  C  C     . GLY A 99  ? 0.5839 0.536  0.2474 0.1924  0.1297  -0.0843 99  GLY A C     
788  O  O     . GLY A 99  ? 0.5935 0.5401 0.2446 0.189   0.126   -0.0771 99  GLY A O     
789  N  N     . GLU A 100 ? 0.6077 0.5479 0.2551 0.19    0.1371  -0.0763 100 GLU A N     
790  C  CA    . GLU A 100 ? 0.6527 0.5675 0.2627 0.1864  0.139   -0.0594 100 GLU A CA    
791  C  C     . GLU A 100 ? 0.6669 0.5848 0.2755 0.2013  0.1232  -0.0402 100 GLU A C     
792  O  O     . GLU A 100 ? 0.6605 0.5937 0.2897 0.2115  0.1166  -0.0358 100 GLU A O     
793  C  CB    . GLU A 100 ? 0.7122 0.604  0.3    0.1801  0.1505  -0.0599 100 GLU A CB    
794  C  CG    . GLU A 100 ? 0.7883 0.6736 0.3668 0.1553  0.1724  -0.0814 100 GLU A CG    
795  C  CD    . GLU A 100 ? 0.8705 0.7399 0.4186 0.1393  0.1805  -0.084  100 GLU A CD    
796  O  OE1   . GLU A 100 ? 0.923  0.7481 0.417  0.1357  0.1796  -0.0679 100 GLU A OE1   
797  O  OE2   . GLU A 100 ? 0.8807 0.779  0.456  0.1338  0.1843  -0.1025 100 GLU A OE2   
798  N  N     . ARG A 101 ? 0.6844 0.5891 0.2669 0.2017  0.1174  -0.0316 101 ARG A N     
799  C  CA    . ARG A 101 ? 0.6877 0.6056 0.2747 0.216   0.1022  -0.0204 101 ARG A CA    
800  C  C     . ARG A 101 ? 0.6832 0.5901 0.2582 0.2304  0.0985  -0.0139 101 ARG A C     
801  O  O     . ARG A 101 ? 0.6666 0.598  0.2603 0.2432  0.0896  -0.0109 101 ARG A O     
802  C  CB    . ARG A 101 ? 0.7335 0.6457 0.2996 0.2161  0.0921  -0.0184 101 ARG A CB    
803  C  CG    . ARG A 101 ? 0.7825 0.7183 0.3717 0.2076  0.0891  -0.0236 101 ARG A CG    
804  C  CD    . ARG A 101 ? 0.8307 0.788  0.4257 0.2148  0.0734  -0.0218 101 ARG A CD    
805  N  NE    . ARG A 101 ? 0.9019 0.8363 0.4584 0.2223  0.0623  -0.0206 101 ARG A NE    
806  C  CZ    . ARG A 101 ? 0.9374 0.8873 0.493  0.2381  0.0431  -0.0221 101 ARG A CZ    
807  N  NH1   . ARG A 101 ? 0.968  0.8859 0.4779 0.2484  0.0287  -0.0211 101 ARG A NH1   
808  N  NH2   . ARG A 101 ? 0.9077 0.9047 0.5054 0.2434  0.0376  -0.0272 101 ARG A NH2   
809  N  N     . GLU A 102 ? 0.6969 0.5662 0.2393 0.226   0.1069  -0.0142 102 GLU A N     
810  C  CA    . GLU A 102 ? 0.7062 0.5529 0.2297 0.2389  0.1035  -0.0095 102 GLU A CA    
811  C  C     . GLU A 102 ? 0.7103 0.5353 0.2252 0.2246  0.1209  -0.0161 102 GLU A C     
812  O  O     . GLU A 102 ? 0.7149 0.5298 0.2211 0.203   0.136   -0.0253 102 GLU A O     
813  C  CB    . GLU A 102 ? 0.7543 0.5596 0.2272 0.2522  0.0885  -0.0025 102 GLU A CB    
814  C  CG    . GLU A 102 ? 0.8281 0.5722 0.2392 0.2342  0.0979  -0.001  102 GLU A CG    
815  C  CD    . GLU A 102 ? 0.9329 0.6163 0.2765 0.251   0.0786  0.0077  102 GLU A CD    
816  O  OE1   . GLU A 102 ? 0.9735 0.5906 0.2494 0.2331  0.0878  0.0108  102 GLU A OE1   
817  O  OE2   . GLU A 102 ? 0.949  0.6487 0.3036 0.2819  0.054   0.0089  102 GLU A OE2   
818  N  N     . VAL A 103 ? 0.7051 0.5294 0.2269 0.2352  0.1198  -0.0155 103 VAL A N     
819  C  CA    . VAL A 103 ? 0.7155 0.5251 0.2347 0.2219  0.135   -0.0249 103 VAL A CA    
820  C  C     . VAL A 103 ? 0.7483 0.5137 0.23   0.2319  0.1312  -0.0196 103 VAL A C     
821  O  O     . VAL A 103 ? 0.7516 0.5251 0.2386 0.257   0.1157  -0.0132 103 VAL A O     
822  C  CB    . VAL A 103 ? 0.685  0.5407 0.2556 0.2244  0.1368  -0.0341 103 VAL A CB    
823  C  CG1   . VAL A 103 ? 0.6737 0.5584 0.2725 0.2141  0.1401  -0.0443 103 VAL A CG1   
824  C  CG2   . VAL A 103 ? 0.6709 0.5517 0.261  0.246   0.1236  -0.0253 103 VAL A CG2   
825  N  N     . PRO A 104 ? 0.77   0.4892 0.2141 0.2111  0.1465  -0.0254 104 PRO A N     
826  C  CA    . PRO A 104 ? 0.8087 0.4742 0.2099 0.2195  0.1424  -0.021  104 PRO A CA    
827  C  C     . PRO A 104 ? 0.7934 0.4937 0.2358 0.2365  0.1378  -0.0257 104 PRO A C     
828  O  O     . PRO A 104 ? 0.7676 0.5149 0.2571 0.228   0.1463  -0.0366 104 PRO A O     
829  C  CB    . PRO A 104 ? 0.8437 0.4594 0.2022 0.1824  0.1668  -0.0307 104 PRO A CB    
830  C  CG    . PRO A 104 ? 0.8071 0.4781 0.214  0.1593  0.1841  -0.0476 104 PRO A CG    
831  C  CD    . PRO A 104 ? 0.7595 0.474  0.1985 0.1766  0.1698  -0.0401 104 PRO A CD    
832  N  N     . SER A 105 ? 0.8077 0.4844 0.2306 0.2625  0.1225  -0.0198 105 SER A N     
833  C  CA    . SER A 105 ? 0.7893 0.4975 0.2467 0.2771  0.1201  -0.026  105 SER A CA    
834  C  C     . SER A 105 ? 0.7953 0.4872 0.2503 0.2546  0.1373  -0.0385 105 SER A C     
835  O  O     . SER A 105 ? 0.7767 0.5061 0.2687 0.2596  0.1384  -0.0468 105 SER A O     
836  C  CB    . SER A 105 ? 0.8228 0.5118 0.2613 0.3106  0.1006  -0.0226 105 SER A CB    
837  O  OG    . SER A 105 ? 0.9096 0.5171 0.2845 0.3101  0.0985  -0.0215 105 SER A OG    
838  N  N     . LYS A 106 ? 0.8248 0.4615 0.2344 0.227   0.1516  -0.042  106 LYS A N     
839  C  CA    . LYS A 106 ? 0.8303 0.455  0.2385 0.1971  0.172   -0.0595 106 LYS A CA    
840  C  C     . LYS A 106 ? 0.7667 0.4666 0.2417 0.1854  0.1808  -0.0768 106 LYS A C     
841  O  O     . LYS A 106 ? 0.7512 0.4751 0.2547 0.1796  0.1859  -0.0941 106 LYS A O     
842  C  CB    . LYS A 106 ? 0.927  0.4783 0.2678 0.1622  0.19    -0.0606 106 LYS A CB    
843  C  CG    . LYS A 106 ? 1.0229 0.5625 0.3606 0.1228  0.2161  -0.0839 106 LYS A CG    
844  C  CD    . LYS A 106 ? 1.1598 0.6416 0.437  0.077   0.2421  -0.0894 106 LYS A CD    
845  C  CE    . LYS A 106 ? 1.2486 0.7116 0.5151 0.0325  0.271   -0.1156 106 LYS A CE    
846  N  NZ    . LYS A 106 ? 1.231  0.7941 0.5869 0.0172  0.2845  -0.1491 106 LYS A NZ    
847  N  N     . MET A 107 ? 0.7342 0.4696 0.2329 0.1856  0.1788  -0.0738 107 MET A N     
848  C  CA    . MET A 107 ? 0.6903 0.4892 0.2463 0.1813  0.181   -0.0905 107 MET A CA    
849  C  C     . MET A 107 ? 0.6589 0.4963 0.2514 0.2086  0.1644  -0.0882 107 MET A C     
850  O  O     . MET A 107 ? 0.6403 0.5099 0.2662 0.2073  0.1641  -0.1071 107 MET A O     
851  C  CB    . MET A 107 ? 0.6919 0.5077 0.2549 0.179   0.1797  -0.0851 107 MET A CB    
852  C  CG    . MET A 107 ? 0.6855 0.5552 0.299  0.1747  0.1809  -0.1059 107 MET A CG    
853  S  SD    . MET A 107 ? 0.7387 0.6211 0.3553 0.1757  0.1766  -0.0976 107 MET A SD    
854  C  CE    . MET A 107 ? 0.7356 0.6543 0.3889 0.204   0.1546  -0.0909 107 MET A CE    
855  N  N     . ILE A 108 ? 0.6516 0.4844 0.2344 0.2327  0.1507  -0.0682 108 ILE A N     
856  C  CA    . ILE A 108 ? 0.6262 0.4888 0.232  0.2539  0.1392  -0.0653 108 ILE A CA    
857  C  C     . ILE A 108 ? 0.6334 0.4871 0.2375 0.2554  0.1413  -0.0772 108 ILE A C     
858  O  O     . ILE A 108 ? 0.6158 0.4966 0.2427 0.2623  0.1359  -0.0862 108 ILE A O     
859  C  CB    . ILE A 108 ? 0.628  0.4923 0.2246 0.2743  0.1292  -0.048  108 ILE A CB    
860  C  CG1   . ILE A 108 ? 0.6251 0.5027 0.2265 0.2723  0.1257  -0.0386 108 ILE A CG1   
861  C  CG2   . ILE A 108 ? 0.6257 0.5188 0.2398 0.2895  0.1235  -0.0482 108 ILE A CG2   
862  C  CD1   . ILE A 108 ? 0.6311 0.5182 0.2293 0.2898  0.1161  -0.0288 108 ILE A CD1   
863  N  N     . GLY A 109 ? 0.6576 0.4664 0.2279 0.2495  0.1474  -0.0772 109 GLY A N     
864  C  CA    . GLY A 109 ? 0.6664 0.4581 0.2292 0.2477  0.1505  -0.0895 109 GLY A CA    
865  C  C     . GLY A 109 ? 0.6499 0.4651 0.2398 0.2264  0.1598  -0.1145 109 GLY A C     
866  O  O     . GLY A 109 ? 0.6351 0.4737 0.246  0.2348  0.1538  -0.1269 109 GLY A O     
867  N  N     . ASN A 110 ? 0.6501 0.4653 0.2423 0.1998  0.1736  -0.1257 110 ASN A N     
868  C  CA    . ASN A 110 ? 0.6314 0.4825 0.2596 0.1791  0.1828  -0.1582 110 ASN A CA    
869  C  C     . ASN A 110 ? 0.5942 0.503  0.2704 0.2005  0.1649  -0.1683 110 ASN A C     
870  O  O     . ASN A 110 ? 0.5734 0.5123 0.2791 0.2007  0.1603  -0.1949 110 ASN A O     
871  C  CB    . ASN A 110 ? 0.6505 0.4965 0.2728 0.1454  0.2037  -0.1711 110 ASN A CB    
872  C  CG    . ASN A 110 ? 0.7489 0.5246 0.3106 0.1171  0.2233  -0.1658 110 ASN A CG    
873  O  OD1   . ASN A 110 ? 0.816  0.5559 0.3394 0.1021  0.2332  -0.1538 110 ASN A OD1   
874  N  ND2   . ASN A 110 ? 0.7616 0.5079 0.3052 0.1082  0.2285  -0.1746 110 ASN A ND2   
875  N  N     . LEU A 111 ? 0.5845 0.5032 0.263  0.2191  0.1528  -0.1481 111 LEU A N     
876  C  CA    . LEU A 111 ? 0.5611 0.5147 0.2671 0.2395  0.1338  -0.1532 111 LEU A CA    
877  C  C     . LEU A 111 ? 0.5666 0.5194 0.2671 0.259   0.1209  -0.1508 111 LEU A C     
878  O  O     . LEU A 111 ? 0.5569 0.5325 0.277  0.2697  0.1066  -0.1701 111 LEU A O     
879  C  CB    . LEU A 111 ? 0.5595 0.5131 0.2596 0.2493  0.1267  -0.1309 111 LEU A CB    
880  C  CG    . LEU A 111 ? 0.5588 0.5203 0.2686 0.2336  0.1354  -0.1375 111 LEU A CG    
881  C  CD1   . LEU A 111 ? 0.5616 0.522  0.2652 0.2441  0.1261  -0.1166 111 LEU A CD1   
882  C  CD2   . LEU A 111 ? 0.5412 0.539  0.2893 0.2267  0.1348  -0.1746 111 LEU A CD2   
883  N  N     . VAL A 112 ? 0.5824 0.5086 0.2549 0.2652  0.1244  -0.131  112 VAL A N     
884  C  CA    . VAL A 112 ? 0.5854 0.5095 0.2483 0.2816  0.1159  -0.1299 112 VAL A CA    
885  C  C     . VAL A 112 ? 0.593  0.5203 0.2665 0.2743  0.1171  -0.157  112 VAL A C     
886  O  O     . VAL A 112 ? 0.5941 0.5356 0.2737 0.2874  0.1037  -0.1685 112 VAL A O     
887  C  CB    . VAL A 112 ? 0.5968 0.4991 0.2334 0.2913  0.1199  -0.1093 112 VAL A CB    
888  C  CG1   . VAL A 112 ? 0.6041 0.5088 0.2321 0.3063  0.1137  -0.1128 112 VAL A CG1   
889  C  CG2   . VAL A 112 ? 0.5942 0.5039 0.227  0.2975  0.1183  -0.0885 112 VAL A CG2   
890  N  N     . MET A 113 ? 0.6067 0.5185 0.2785 0.251   0.1331  -0.1688 113 MET A N     
891  C  CA    . MET A 113 ? 0.6174 0.5338 0.3015 0.2351  0.139   -0.199  113 MET A CA    
892  C  C     . MET A 113 ? 0.602  0.5697 0.3303 0.2378  0.1268  -0.2305 113 MET A C     
893  O  O     . MET A 113 ? 0.5949 0.5789 0.3369 0.2432  0.1175  -0.2534 113 MET A O     
894  C  CB    . MET A 113 ? 0.6521 0.5364 0.3187 0.2008  0.1631  -0.2058 113 MET A CB    
895  C  CG    . MET A 113 ? 0.7348 0.5569 0.3495 0.2025  0.1691  -0.1799 113 MET A CG    
896  S  SD    . MET A 113 ? 0.9002 0.6908 0.4942 0.205   0.1683  -0.1907 113 MET A SD    
897  C  CE    . MET A 113 ? 0.8939 0.6473 0.4682 0.1561  0.1947  -0.2146 113 MET A CE    
898  N  N     . GLU A 114 ? 0.6004 0.5935 0.3506 0.2381  0.1233  -0.2341 114 GLU A N     
899  C  CA    . GLU A 114 ? 0.5878 0.6295 0.3808 0.2478  0.1061  -0.2682 114 GLU A CA    
900  C  C     . GLU A 114 ? 0.5916 0.6343 0.3753 0.2839  0.0752  -0.2607 114 GLU A C     
901  O  O     . GLU A 114 ? 0.5741 0.6457 0.3818 0.2982  0.0547  -0.292  114 GLU A O     
902  C  CB    . GLU A 114 ? 0.6175 0.685  0.4366 0.2378  0.1116  -0.2802 114 GLU A CB    
903  C  CG    . GLU A 114 ? 0.7289 0.8133 0.5686 0.1981  0.1403  -0.3104 114 GLU A CG    
904  C  CD    . GLU A 114 ? 0.8662 0.9888 0.7424 0.1858  0.1417  -0.3571 114 GLU A CD    
905  O  OE1   . GLU A 114 ? 0.867  1.049  0.7952 0.1953  0.1271  -0.3986 114 GLU A OE1   
906  O  OE2   . GLU A 114 ? 0.9329 1.0265 0.7864 0.1679  0.1557  -0.3551 114 GLU A OE2   
907  N  N     . GLN A 115 ? 0.6092 0.6191 0.3545 0.2975  0.0717  -0.222  115 GLN A N     
908  C  CA    . GLN A 115 ? 0.617  0.6153 0.3379 0.3248  0.0474  -0.2123 115 GLN A CA    
909  C  C     . GLN A 115 ? 0.6241 0.6171 0.3335 0.3302  0.0439  -0.2215 115 GLN A C     
910  O  O     . GLN A 115 ? 0.6241 0.6249 0.3328 0.3487  0.0202  -0.2404 115 GLN A O     
911  C  CB    . GLN A 115 ? 0.6534 0.6226 0.3371 0.3298  0.0508  -0.1731 115 GLN A CB    
912  C  CG    . GLN A 115 ? 0.6987 0.6685 0.3875 0.3278  0.0492  -0.1632 115 GLN A CG    
913  C  CD    . GLN A 115 ? 0.7508 0.733  0.4556 0.3431  0.0247  -0.1864 115 GLN A CD    
914  O  OE1   . GLN A 115 ? 0.7911 0.7507 0.4664 0.3638  0.0008  -0.1824 115 GLN A OE1   
915  N  NE2   . GLN A 115 ? 0.7317 0.7459 0.4789 0.333   0.0302  -0.2119 115 GLN A NE2   
916  N  N     . LEU A 116 ? 0.6311 0.6082 0.3294 0.3161  0.0647  -0.2114 116 LEU A N     
917  C  CA    . LEU A 116 ? 0.6421 0.6113 0.3281 0.3206  0.0627  -0.2211 116 LEU A CA    
918  C  C     . LEU A 116 ? 0.6284 0.6257 0.3479 0.314   0.0558  -0.2627 116 LEU A C     
919  O  O     . LEU A 116 ? 0.6294 0.63   0.3423 0.328   0.04    -0.2773 116 LEU A O     
920  C  CB    . LEU A 116 ? 0.6563 0.5968 0.3209 0.3104  0.0836  -0.2035 116 LEU A CB    
921  C  CG    . LEU A 116 ? 0.6784 0.6025 0.3159 0.3207  0.088   -0.17   116 LEU A CG    
922  C  CD1   . LEU A 116 ? 0.6967 0.595  0.3182 0.316   0.1033  -0.1595 116 LEU A CD1   
923  C  CD2   . LEU A 116 ? 0.6867 0.6104 0.2993 0.3397  0.0751  -0.1625 116 LEU A CD2   
924  N  N     . LYS A 117 ? 0.6137 0.6362 0.3703 0.2926  0.0667  -0.2856 117 LYS A N     
925  C  CA    . LYS A 117 ? 0.5961 0.6594 0.3953 0.2821  0.0624  -0.3337 117 LYS A CA    
926  C  C     . LYS A 117 ? 0.5822 0.6757 0.3972 0.3154  0.0249  -0.3566 117 LYS A C     
927  O  O     . LYS A 117 ? 0.5723 0.6894 0.4052 0.3215  0.0103  -0.3903 117 LYS A O     
928  C  CB    . LYS A 117 ? 0.6071 0.6968 0.4423 0.2507  0.0842  -0.3551 117 LYS A CB    
929  C  CG    . LYS A 117 ? 0.65   0.7768 0.5252 0.2223  0.096   -0.4052 117 LYS A CG    
930  C  CD    . LYS A 117 ? 0.728  0.8608 0.617  0.1787  0.1305  -0.4175 117 LYS A CD    
931  C  CE    . LYS A 117 ? 0.7588 0.9489 0.7015 0.1472  0.143   -0.4786 117 LYS A CE    
932  N  NZ    . LYS A 117 ? 0.7458 1.0153 0.7537 0.169   0.1182  -0.5225 117 LYS A NZ    
933  N  N     . LYS A 118 ? 0.5845 0.6689 0.3847 0.3384  0.007   -0.3372 118 LYS A N     
934  C  CA    . LYS A 118 ? 0.5838 0.6751 0.3792 0.3745  -0.0331 -0.3521 118 LYS A CA    
935  C  C     . LYS A 118 ? 0.6083 0.656  0.3444 0.396   -0.0495 -0.3286 118 LYS A C     
936  O  O     . LYS A 118 ? 0.6121 0.664  0.3411 0.4209  -0.0813 -0.3519 118 LYS A O     
937  C  CB    . LYS A 118 ? 0.619  0.7016 0.4087 0.3875  -0.0442 -0.3376 118 LYS A CB    
938  C  CG    . LYS A 118 ? 0.6457 0.7761 0.4939 0.3714  -0.0329 -0.367  118 LYS A CG    
939  C  CD    . LYS A 118 ? 0.7198 0.838  0.5599 0.3863  -0.0454 -0.3535 118 LYS A CD    
940  C  CE    . LYS A 118 ? 0.7435 0.915  0.644  0.3689  -0.0317 -0.388  118 LYS A CE    
941  N  NZ    . LYS A 118 ? 0.7744 0.9541 0.6876 0.3241  0.0131  -0.3827 118 LYS A NZ    
942  N  N     . LEU A 119 ? 0.6263 0.6343 0.3192 0.3873  -0.0288 -0.2856 119 LEU A N     
943  C  CA    . LEU A 119 ? 0.6603 0.6286 0.294  0.4011  -0.0357 -0.2618 119 LEU A CA    
944  C  C     . LEU A 119 ? 0.6676 0.6386 0.2967 0.4009  -0.0348 -0.2783 119 LEU A C     
945  O  O     . LEU A 119 ? 0.677  0.6353 0.2756 0.422   -0.0602 -0.2883 119 LEU A O     
946  C  CB    . LEU A 119 ? 0.6777 0.6181 0.28   0.389   -0.0104 -0.2193 119 LEU A CB    
947  C  CG    . LEU A 119 ? 0.7072 0.6268 0.2855 0.3942  -0.0171 -0.1965 119 LEU A CG    
948  C  CD1   . LEU A 119 ? 0.7185 0.6289 0.2864 0.3768  0.0117  -0.1637 119 LEU A CD1   
949  C  CD2   . LEU A 119 ? 0.7411 0.6217 0.2599 0.4158  -0.0444 -0.191  119 LEU A CD2   
950  N  N     . ASP A 120 ? 0.6626 0.642  0.3139 0.3777  -0.0071 -0.2806 120 ASP A N     
951  C  CA    . ASP A 120 ? 0.6757 0.6513 0.3204 0.3747  -0.003  -0.2949 120 ASP A CA    
952  C  C     . ASP A 120 ? 0.6748 0.6587 0.3526 0.3448  0.0236  -0.3079 120 ASP A C     
953  O  O     . ASP A 120 ? 0.6774 0.643  0.3496 0.3303  0.0463  -0.2841 120 ASP A O     
954  C  CB    . ASP A 120 ? 0.7226 0.6633 0.3153 0.3823  0.0062  -0.2634 120 ASP A CB    
955  C  CG    . ASP A 120 ? 0.788  0.7202 0.3631 0.3867  0.0048  -0.2775 120 ASP A CG    
956  O  OD1   . ASP A 120 ? 0.7812 0.7148 0.3765 0.3709  0.0201  -0.2909 120 ASP A OD1   
957  O  OD2   . ASP A 120 ? 0.8497 0.7672 0.3837 0.4046  -0.0109 -0.2745 120 ASP A OD2   
958  N  N     . LYS A 121 ? 0.6709 0.6781 0.3784 0.3343  0.0202  -0.347  121 LYS A N     
959  C  CA    . LYS A 121 ? 0.6795 0.6836 0.4073 0.2994  0.0476  -0.3615 121 LYS A CA    
960  C  C     . LYS A 121 ? 0.7104 0.6637 0.3971 0.2937  0.0656  -0.3398 121 LYS A C     
961  O  O     . LYS A 121 ? 0.7273 0.6528 0.4076 0.269   0.0892  -0.3326 121 LYS A O     
962  C  CB    . LYS A 121 ? 0.6852 0.7333 0.4598 0.2836  0.042   -0.415  121 LYS A CB    
963  C  CG    . LYS A 121 ? 0.7069 0.8112 0.5239 0.3018  0.0139  -0.4459 121 LYS A CG    
964  C  CD    . LYS A 121 ? 0.7349 0.8702 0.5922 0.2815  0.0284  -0.4564 121 LYS A CD    
965  C  CE    . LYS A 121 ? 0.7409 0.9403 0.65   0.301   -0.0016 -0.5007 121 LYS A CE    
966  N  NZ    . LYS A 121 ? 0.7326 0.9692 0.6852 0.2821  0.0132  -0.5165 121 LYS A NZ    
967  N  N     . VAL A 122 ? 0.7169 0.6537 0.3704 0.3175  0.0541  -0.3294 122 VAL A N     
968  C  CA    . VAL A 122 ? 0.7442 0.6377 0.3623 0.3178  0.0688  -0.3124 122 VAL A CA    
969  C  C     . VAL A 122 ? 0.7606 0.6329 0.3607 0.322   0.0816  -0.275  122 VAL A C     
970  O  O     . VAL A 122 ? 0.7805 0.6167 0.3654 0.3118  0.0972  -0.2657 122 VAL A O     
971  C  CB    . VAL A 122 ? 0.7624 0.65   0.3523 0.3407  0.0556  -0.3166 122 VAL A CB    
972  C  CG1   . VAL A 122 ? 0.7938 0.6443 0.3496 0.3487  0.0693  -0.2971 122 VAL A CG1   
973  C  CG2   . VAL A 122 ? 0.7528 0.6539 0.3588 0.3331  0.0452  -0.3566 122 VAL A CG2   
974  N  N     . ALA A 123 ? 0.7531 0.6443 0.3526 0.3363  0.0731  -0.2559 123 ALA A N     
975  C  CA    . ALA A 123 ? 0.7634 0.6458 0.3532 0.3391  0.0833  -0.2245 123 ALA A CA    
976  C  C     . ALA A 123 ? 0.77   0.6429 0.3761 0.317   0.0968  -0.2222 123 ALA A C     
977  O  O     . ALA A 123 ? 0.7851 0.6347 0.3764 0.3167  0.1073  -0.202  123 ALA A O     
978  C  CB    . ALA A 123 ? 0.7558 0.6576 0.3413 0.3518  0.0714  -0.2105 123 ALA A CB    
979  N  N     . TYR A 124 ? 0.7565 0.6493 0.3922 0.2989  0.096   -0.2459 124 TYR A N     
980  C  CA    . TYR A 124 ? 0.767  0.6522 0.4151 0.2715  0.1125  -0.2493 124 TYR A CA    
981  C  C     . TYR A 124 ? 0.7946 0.6263 0.4122 0.2538  0.1296  -0.2486 124 TYR A C     
982  O  O     . TYR A 124 ? 0.8128 0.6092 0.4074 0.2455  0.1411  -0.2293 124 TYR A O     
983  C  CB    . TYR A 124 ? 0.748  0.6768 0.4397 0.2551  0.1091  -0.2855 124 TYR A CB    
984  C  CG    . TYR A 124 ? 0.7659 0.6906 0.4695 0.2193  0.1317  -0.2961 124 TYR A CG    
985  C  CD1   . TYR A 124 ? 0.7937 0.6931 0.4888 0.1857  0.1515  -0.3169 124 TYR A CD1   
986  C  CD2   . TYR A 124 ? 0.7686 0.7087 0.4849 0.2159  0.1352  -0.2856 124 TYR A CD2   
987  C  CE1   . TYR A 124 ? 0.8117 0.6973 0.5044 0.1469  0.1767  -0.3254 124 TYR A CE1   
988  C  CE2   . TYR A 124 ? 0.781  0.7146 0.5012 0.1806  0.1586  -0.2956 124 TYR A CE2   
989  C  CZ    . TYR A 124 ? 0.8102 0.7155 0.5162 0.1447  0.1804  -0.3153 124 TYR A CZ    
990  O  OH    . TYR A 124 ? 0.8427 0.7343 0.5417 0.1039  0.2073  -0.3255 124 TYR A OH    
991  N  N     . ILE A 125 ? 0.8    0.6192 0.411  0.2498  0.1288  -0.2697 125 ILE A N     
992  C  CA    . ILE A 125 ? 0.837  0.5934 0.4102 0.234   0.1422  -0.2716 125 ILE A CA    
993  C  C     . ILE A 125 ? 0.8693 0.5828 0.4027 0.2605  0.1388  -0.2412 125 ILE A C     
994  O  O     . ILE A 125 ? 0.9039 0.5565 0.3987 0.2512  0.1477  -0.2307 125 ILE A O     
995  C  CB    . ILE A 125 ? 0.8385 0.5947 0.4147 0.2282  0.1388  -0.3022 125 ILE A CB    
996  C  CG1   . ILE A 125 ? 0.8172 0.6292 0.4421 0.2061  0.138   -0.3404 125 ILE A CG1   
997  C  CG2   . ILE A 125 ? 0.8817 0.5621 0.4116 0.21    0.1522  -0.3048 125 ILE A CG2   
998  C  CD1   . ILE A 125 ? 0.833  0.6419 0.4693 0.1632  0.1605  -0.3556 125 ILE A CD1   
999  N  N     . ARG A 126 ? 0.8561 0.6001 0.3957 0.2932  0.1255  -0.2299 126 ARG A N     
1000 C  CA    . ARG A 126 ? 0.8746 0.597  0.3888 0.3201  0.1223  -0.209  126 ARG A CA    
1001 C  C     . ARG A 126 ? 0.8791 0.5899 0.3871 0.3191  0.1261  -0.1861 126 ARG A C     
1002 O  O     . ARG A 126 ? 0.9063 0.5672 0.3815 0.3267  0.1261  -0.177  126 ARG A O     
1003 C  CB    . ARG A 126 ? 0.8701 0.6362 0.3941 0.3467  0.1129  -0.2053 126 ARG A CB    
1004 C  CG    . ARG A 126 ? 0.903  0.6712 0.4209 0.3534  0.1074  -0.2262 126 ARG A CG    
1005 C  CD    . ARG A 126 ? 0.9284 0.7174 0.4359 0.3801  0.1039  -0.2208 126 ARG A CD    
1006 N  NE    . ARG A 126 ? 0.9544 0.7555 0.4557 0.3853  0.0969  -0.2393 126 ARG A NE    
1007 C  CZ    . ARG A 126 ? 0.9583 0.7913 0.4578 0.3913  0.0898  -0.238  126 ARG A CZ    
1008 N  NH1   . ARG A 126 ? 0.9403 0.7948 0.444  0.3916  0.0906  -0.2186 126 ARG A NH1   
1009 N  NH2   . ARG A 126 ? 0.9592 0.7954 0.445  0.3972  0.0811  -0.2558 126 ARG A NH2   
1010 N  N     . PHE A 127 ? 0.8537 0.6053 0.3893 0.3113  0.1267  -0.1789 127 PHE A N     
1011 C  CA    . PHE A 127 ? 0.8594 0.6053 0.3918 0.3089  0.1298  -0.159  127 PHE A CA    
1012 C  C     . PHE A 127 ? 0.8979 0.5886 0.4025 0.2828  0.1409  -0.1607 127 PHE A C     
1013 O  O     . PHE A 127 ? 0.9269 0.5767 0.4    0.2897  0.1397  -0.1448 127 PHE A O     
1014 C  CB    . PHE A 127 ? 0.8256 0.6231 0.3916 0.3046  0.1276  -0.1549 127 PHE A CB    
1015 C  CG    . PHE A 127 ? 0.8274 0.6309 0.3944 0.3076  0.1282  -0.1338 127 PHE A CG    
1016 C  CD1   . PHE A 127 ? 0.8443 0.6249 0.4034 0.2876  0.1365  -0.1302 127 PHE A CD1   
1017 C  CD2   . PHE A 127 ? 0.8227 0.6574 0.3981 0.3262  0.1222  -0.1201 127 PHE A CD2   
1018 C  CE1   . PHE A 127 ? 0.8485 0.636  0.4082 0.2907  0.1354  -0.1126 127 PHE A CE1   
1019 C  CE2   . PHE A 127 ? 0.8265 0.6702 0.4058 0.3267  0.1225  -0.104  127 PHE A CE2   
1020 C  CZ    . PHE A 127 ? 0.8318 0.652  0.404  0.311   0.1275  -0.1001 127 PHE A CZ    
1021 N  N     . ALA A 128 ? 0.8965 0.5835 0.4085 0.2519  0.1517  -0.1824 128 ALA A N     
1022 C  CA    . ALA A 128 ? 0.9292 0.559  0.4069 0.2172  0.1684  -0.1871 128 ALA A CA    
1023 C  C     . ALA A 128 ? 0.9774 0.52   0.3918 0.2227  0.1672  -0.1798 128 ALA A C     
1024 O  O     . ALA A 128 ? 1.0162 0.4926 0.3805 0.2078  0.1741  -0.1687 128 ALA A O     
1025 C  CB    . ALA A 128 ? 0.9154 0.5694 0.4201 0.1807  0.1824  -0.2198 128 ALA A CB    
1026 N  N     . SER A 129 ? 0.9778 0.5144 0.388  0.2463  0.1564  -0.1861 129 SER A N     
1027 C  CA    . SER A 129 ? 1.03   0.4821 0.3802 0.2586  0.1505  -0.1826 129 SER A CA    
1028 C  C     . SER A 129 ? 1.0557 0.4727 0.3729 0.2902  0.1361  -0.1587 129 SER A C     
1029 O  O     . SER A 129 ? 1.1078 0.4332 0.3591 0.2936  0.1308  -0.1531 129 SER A O     
1030 C  CB    . SER A 129 ? 1.0352 0.5019 0.3964 0.2817  0.1408  -0.1972 129 SER A CB    
1031 O  OG    . SER A 129 ? 1.0308 0.5599 0.4258 0.3198  0.1277  -0.1885 129 SER A OG    
1032 N  N     . VAL A 130 ? 1.0182 0.5037 0.3771 0.3132  0.1282  -0.1466 130 VAL A N     
1033 C  CA    . VAL A 130 ? 1.0366 0.5059 0.3763 0.3433  0.1134  -0.1293 130 VAL A CA    
1034 C  C     . VAL A 130 ? 1.052  0.5143 0.3834 0.3222  0.12    -0.1145 130 VAL A C     
1035 O  O     . VAL A 130 ? 1.0906 0.4902 0.3716 0.3308  0.1109  -0.1026 130 VAL A O     
1036 C  CB    . VAL A 130 ? 1.0017 0.5473 0.3876 0.3804  0.1019  -0.1292 130 VAL A CB    
1037 C  CG1   . VAL A 130 ? 1.0137 0.5518 0.3874 0.4117  0.0853  -0.1187 130 VAL A CG1   
1038 C  CG2   . VAL A 130 ? 1.0044 0.5546 0.3934 0.3997  0.0974  -0.1461 130 VAL A CG2   
1039 N  N     . TYR A 131 ? 1.0243 0.5446 0.3995 0.2958  0.1341  -0.1174 131 TYR A N     
1040 C  CA    . TYR A 131 ? 1.0355 0.5578 0.4087 0.2745  0.1424  -0.1071 131 TYR A CA    
1041 C  C     . TYR A 131 ? 1.108  0.5445 0.4183 0.2382  0.157   -0.1085 131 TYR A C     
1042 O  O     . TYR A 131 ? 1.1497 0.5296 0.4092 0.2403  0.1522  -0.0929 131 TYR A O     
1043 C  CB    . TYR A 131 ? 0.9799 0.5864 0.4169 0.2607  0.1506  -0.1143 131 TYR A CB    
1044 C  CG    . TYR A 131 ? 0.9786 0.5921 0.4182 0.2382  0.1602  -0.1084 131 TYR A CG    
1045 C  CD1   . TYR A 131 ? 0.9914 0.6036 0.4212 0.2544  0.1508  -0.089  131 TYR A CD1   
1046 C  CD2   . TYR A 131 ? 0.9768 0.6043 0.4322 0.2009  0.1786  -0.1264 131 TYR A CD2   
1047 C  CE1   . TYR A 131 ? 1.0001 0.616  0.4287 0.2337  0.1596  -0.0845 131 TYR A CE1   
1048 C  CE2   . TYR A 131 ? 0.981  0.6174 0.4389 0.18    0.1892  -0.1245 131 TYR A CE2   
1049 C  CZ    . TYR A 131 ? 1.0001 0.6276 0.442  0.1966  0.1796  -0.1019 131 TYR A CZ    
1050 O  OH    . TYR A 131 ? 1.0147 0.6494 0.4566 0.1755  0.1902  -0.1012 131 TYR A OH    
1051 N  N     . ARG A 132 ? 1.1226 0.5458 0.4308 0.2036  0.175   -0.1286 132 ARG A N     
1052 C  CA    . ARG A 132 ? 1.1884 0.5242 0.4294 0.1607  0.1944  -0.1329 132 ARG A CA    
1053 C  C     . ARG A 132 ? 1.2652 0.4862 0.4191 0.1754  0.182   -0.1233 132 ARG A C     
1054 O  O     . ARG A 132 ? 1.3295 0.4528 0.4041 0.1426  0.195   -0.1208 132 ARG A O     
1055 C  CB    . ARG A 132 ? 1.1906 0.5567 0.4627 0.1147  0.2196  -0.164  132 ARG A CB    
1056 C  CG    . ARG A 132 ? 1.1794 0.6517 0.5329 0.1035  0.2277  -0.1792 132 ARG A CG    
1057 C  CD    . ARG A 132 ? 1.2132 0.7194 0.6001 0.0602  0.2499  -0.2175 132 ARG A CD    
1058 N  NE    . ARG A 132 ? 1.2059 0.8178 0.6757 0.0606  0.2494  -0.2376 132 ARG A NE    
1059 C  CZ    . ARG A 132 ? 1.2333 0.8768 0.7226 0.0344  0.2655  -0.248  132 ARG A CZ    
1060 N  NH1   . ARG A 132 ? 1.2767 0.8541 0.7053 0.002   0.2863  -0.2381 132 ARG A NH1   
1061 N  NH2   . ARG A 132 ? 1.1822 0.9187 0.7465 0.0421  0.2595  -0.2694 132 ARG A NH2   
1062 N  N     . SER A 133 ? 1.2603 0.4899 0.4245 0.2245  0.157   -0.1194 133 SER A N     
1063 C  CA    . SER A 133 ? 1.33   0.4655 0.4251 0.2525  0.1377  -0.1151 133 SER A CA    
1064 C  C     . SER A 133 ? 1.396  0.4471 0.4357 0.2177  0.1524  -0.1297 133 SER A C     
1065 O  O     . SER A 133 ? 1.4628 0.4048 0.4147 0.1883  0.1612  -0.1233 133 SER A O     
1066 C  CB    . SER A 133 ? 1.3935 0.4522 0.4193 0.2745  0.1187  -0.0939 133 SER A CB    
1067 O  OG    . SER A 133 ? 1.4677 0.4432 0.4337 0.3135  0.0924  -0.0935 133 SER A OG    
1068 N  N     . PHE A 134 ? 1.3784 0.4747 0.4629 0.2186  0.1556  -0.1502 134 PHE A N     
1069 C  CA    . PHE A 134 ? 1.4349 0.4579 0.4732 0.1847  0.1695  -0.1683 134 PHE A CA    
1070 C  C     . PHE A 134 ? 1.5303 0.4336 0.4802 0.2182  0.1457  -0.1587 134 PHE A C     
1071 O  O     . PHE A 134 ? 1.5166 0.4479 0.4889 0.274   0.1191  -0.1566 134 PHE A O     
1072 C  CB    . PHE A 134 ? 1.3757 0.4823 0.4865 0.1846  0.1733  -0.1939 134 PHE A CB    
1073 C  CG    . PHE A 134 ? 1.308  0.5303 0.5055 0.1597  0.1894  -0.2094 134 PHE A CG    
1074 C  CD1   . PHE A 134 ? 1.2965 0.5513 0.512  0.1359  0.2028  -0.2026 134 PHE A CD1   
1075 C  CD2   . PHE A 134 ? 1.2679 0.5632 0.5255 0.1632  0.188   -0.2328 134 PHE A CD2   
1076 C  CE1   . PHE A 134 ? 1.243  0.6021 0.5379 0.1197  0.2126  -0.2202 134 PHE A CE1   
1077 C  CE2   . PHE A 134 ? 1.2161 0.6123 0.5486 0.1483  0.1955  -0.2488 134 PHE A CE2   
1078 C  CZ    . PHE A 134 ? 1.1979 0.6257 0.55   0.1285  0.2068  -0.2429 134 PHE A CZ    
1079 N  N     . GLU A 135 ? 1.628  0.3965 0.4738 0.1859  0.154   -0.1535 135 GLU A N     
1080 C  CA    . GLU A 135 ? 1.7319 0.3679 0.4791 0.2215  0.126   -0.1447 135 GLU A CA    
1081 C  C     . GLU A 135 ? 1.7934 0.3581 0.5008 0.2072  0.13    -0.1647 135 GLU A C     
1082 O  O     . GLU A 135 ? 1.8584 0.3144 0.4879 0.2416  0.1039  -0.1616 135 GLU A O     
1083 C  CB    . GLU A 135 ? 1.8464 0.3501 0.4786 0.2044  0.1241  -0.1226 135 GLU A CB    
1084 C  CG    . GLU A 135 ? 1.8829 0.4494 0.5474 0.2123  0.1221  -0.1043 135 GLU A CG    
1085 C  CD    . GLU A 135 ? 1.9327 0.5361 0.6217 0.2874  0.0808  -0.0925 135 GLU A CD    
1086 O  OE1   . GLU A 135 ? 1.9461 0.5206 0.6219 0.339   0.0507  -0.0994 135 GLU A OE1   
1087 O  OE2   . GLU A 135 ? 1.9291 0.5922 0.6516 0.294   0.0788  -0.0798 135 GLU A OE2   
1088 N  N     . ASP A 136 ? 1.7676 0.3965 0.5309 0.1599  0.1596  -0.188  136 ASP A N     
1089 C  CA    . ASP A 136 ? 1.8124 0.3913 0.5509 0.1332  0.1702  -0.2121 136 ASP A CA    
1090 C  C     . ASP A 136 ? 1.7415 0.4659 0.597  0.1309  0.1792  -0.2377 136 ASP A C     
1091 O  O     . ASP A 136 ? 1.6721 0.5191 0.6144 0.1298  0.1864  -0.2379 136 ASP A O     
1092 C  CB    . ASP A 136 ? 1.8995 0.3861 0.5643 0.0522  0.2068  -0.2191 136 ASP A CB    
1093 C  CG    . ASP A 136 ? 2.0446 0.4151 0.6323 0.0183  0.2165  -0.2377 136 ASP A CG    
1094 O  OD1   . ASP A 136 ? 2.053  0.4267 0.6563 0.0577  0.195   -0.2493 136 ASP A OD1   
1095 O  OD2   . ASP A 136 ? 2.1419 0.4163 0.6506 -0.0506 0.2474  -0.2423 136 ASP A OD2   
1096 N  N     . ILE A 137 ? 1.7612 0.4651 0.6128 0.1318  0.1765  -0.2599 137 ILE A N     
1097 C  CA    . ILE A 137 ? 1.7032 0.5297 0.6515 0.1291  0.1822  -0.2867 137 ILE A CA    
1098 C  C     . ILE A 137 ? 1.6874 0.5623 0.6729 0.0584  0.2169  -0.3098 137 ILE A C     
1099 O  O     . ILE A 137 ? 1.6139 0.6172 0.6936 0.0587  0.22    -0.324  137 ILE A O     
1100 C  CB    . ILE A 137 ? 1.7273 0.5202 0.6605 0.1512  0.1683  -0.3068 137 ILE A CB    
1101 C  CG1   . ILE A 137 ? 1.7937 0.5005 0.6634 0.2128  0.1364  -0.2902 137 ILE A CG1   
1102 C  CG2   . ILE A 137 ? 1.6523 0.5826 0.6858 0.1708  0.1635  -0.3264 137 ILE A CG2   
1103 C  CD1   . ILE A 137 ? 1.9206 0.4433 0.6582 0.1966  0.1334  -0.281  137 ILE A CD1   
1104 N  N     . LYS A 138 ? 1.7545 0.5253 0.6625 -0.0022 0.2429  -0.3146 138 LYS A N     
1105 C  CA    . LYS A 138 ? 1.7384 0.5522 0.6775 -0.0759 0.2806  -0.3423 138 LYS A CA    
1106 C  C     . LYS A 138 ? 1.6701 0.6044 0.6905 -0.0723 0.2856  -0.3364 138 LYS A C     
1107 O  O     . LYS A 138 ? 1.6026 0.6512 0.7113 -0.0942 0.2977  -0.367  138 LYS A O     
1108 C  CB    . LYS A 138 ? 1.8558 0.5228 0.6794 -0.1403 0.3093  -0.3403 138 LYS A CB    
1109 C  CG    . LYS A 138 ? 2.0005 0.5215 0.7234 -0.1467 0.3038  -0.3437 138 LYS A CG    
1110 C  CD    . LYS A 138 ? 2.1617 0.5286 0.7591 -0.2195 0.3361  -0.3413 138 LYS A CD    
1111 C  CE    . LYS A 138 ? 2.3158 0.5085 0.7897 -0.2233 0.327   -0.3389 138 LYS A CE    
1112 N  NZ    . LYS A 138 ? 2.4518 0.4741 0.7821 -0.2904 0.3555  -0.3284 138 LYS A NZ    
1113 N  N     . ASP A 139 ? 1.6847 0.5947 0.6767 -0.0375 0.2711  -0.2989 139 ASP A N     
1114 C  CA    . ASP A 139 ? 1.6353 0.6426 0.6913 -0.0261 0.2711  -0.2869 139 ASP A CA    
1115 C  C     . ASP A 139 ? 1.5454 0.7017 0.7176 0.0031  0.2584  -0.3037 139 ASP A C     
1116 O  O     . ASP A 139 ? 1.4962 0.7431 0.7325 -0.0078 0.2667  -0.3112 139 ASP A O     
1117 C  CB    . ASP A 139 ? 1.6904 0.654  0.7045 0.0261  0.2455  -0.2454 139 ASP A CB    
1118 C  CG    . ASP A 139 ? 1.8258 0.6778 0.7429 -0.0002 0.2565  -0.2233 139 ASP A CG    
1119 O  OD1   . ASP A 139 ? 1.9177 0.641  0.7368 -0.0358 0.269   -0.2257 139 ASP A OD1   
1120 O  OD2   . ASP A 139 ? 1.8348 0.7202 0.7662 0.0156  0.2512  -0.2029 139 ASP A OD2   
1121 N  N     . PHE A 140 ? 1.526  0.7012 0.7183 0.0424  0.2367  -0.3093 140 PHE A N     
1122 C  CA    . PHE A 140 ? 1.4542 0.7516 0.7374 0.0725  0.2215  -0.3233 140 PHE A CA    
1123 C  C     . PHE A 140 ? 1.4347 0.8048 0.778  0.0294  0.238   -0.3665 140 PHE A C     
1124 O  O     . PHE A 140 ? 1.3763 0.8451 0.7901 0.0336  0.2352  -0.3764 140 PHE A O     
1125 C  CB    . PHE A 140 ? 1.438  0.7244 0.7134 0.1198  0.1976  -0.321  140 PHE A CB    
1126 C  CG    . PHE A 140 ? 1.4104 0.7146 0.6891 0.1786  0.1744  -0.2907 140 PHE A CG    
1127 C  CD1   . PHE A 140 ? 1.3505 0.7568 0.695  0.2063  0.1634  -0.2868 140 PHE A CD1   
1128 C  CD2   . PHE A 140 ? 1.4572 0.6742 0.6708 0.2066  0.1625  -0.2699 140 PHE A CD2   
1129 C  CE1   . PHE A 140 ? 1.3442 0.7702 0.6923 0.2532  0.1468  -0.263  140 PHE A CE1   
1130 C  CE2   . PHE A 140 ? 1.4441 0.691  0.6703 0.2594  0.1423  -0.2499 140 PHE A CE2   
1131 C  CZ    . PHE A 140 ? 1.3811 0.7347 0.6759 0.2788  0.1373  -0.247  140 PHE A CZ    
1132 N  N     . GLY A 141 ? 1.4834 0.8029 0.7975 -0.0115 0.2539  -0.3945 141 GLY A N     
1133 C  CA    . GLY A 141 ? 1.4686 0.8586 0.8415 -0.0554 0.2698  -0.4437 141 GLY A CA    
1134 C  C     . GLY A 141 ? 1.4742 0.9074 0.8772 -0.1034 0.297   -0.4605 141 GLY A C     
1135 O  O     . GLY A 141 ? 1.414  0.9546 0.8995 -0.1161 0.299   -0.4986 141 GLY A O     
1136 N  N     . GLU A 142 ? 1.5437 0.8932 0.8778 -0.1272 0.3158  -0.4339 142 GLU A N     
1137 C  CA    . GLU A 142 ? 1.5532 0.9313 0.9022 -0.1747 0.3451  -0.4465 142 GLU A CA    
1138 C  C     . GLU A 142 ? 1.5124 0.999  0.9384 -0.1362 0.328   -0.4377 142 GLU A C     
1139 O  O     . GLU A 142 ? 1.4712 1.0368 0.9553 -0.1663 0.3448  -0.469  142 GLU A O     
1140 C  CB    . GLU A 142 ? 1.669  0.9115 0.906  -0.208  0.3672  -0.417  142 GLU A CB    
1141 C  CG    . GLU A 142 ? 1.8042 0.9247 0.9534 -0.2502 0.3843  -0.427  142 GLU A CG    
1142 C  CD    . GLU A 142 ? 1.9828 0.9521 1.0048 -0.2911 0.4073  -0.402  142 GLU A CD    
1143 O  OE1   . GLU A 142 ? 2.0084 0.9766 1.0151 -0.2958 0.4155  -0.3817 142 GLU A OE1   
1144 O  OE2   . GLU A 142 ? 2.075  0.9203 1.0062 -0.3184 0.4159  -0.403  142 GLU A OE2   
1145 N  N     . GLU A 143 ? 1.5206 1.0147 0.9494 -0.0708 0.2949  -0.3999 143 GLU A N     
1146 C  CA    . GLU A 143 ? 1.4863 1.0734 0.9804 -0.0341 0.2772  -0.3903 143 GLU A CA    
1147 C  C     . GLU A 143 ? 1.4393 1.1365 1.0206 -0.0138 0.258   -0.4253 143 GLU A C     
1148 O  O     . GLU A 143 ? 1.3918 1.1709 1.0325 0.0009  0.2483  -0.434  143 GLU A O     
1149 C  CB    . GLU A 143 ? 1.5334 1.0867 0.995  0.0212  0.2527  -0.3402 143 GLU A CB    
1150 C  CG    . GLU A 143 ? 1.54   1.1687 1.052  0.0519  0.2384  -0.3252 143 GLU A CG    
1151 C  CD    . GLU A 143 ? 1.6063 1.2249 1.105  0.028   0.256   -0.3138 143 GLU A CD    
1152 O  OE1   . GLU A 143 ? 1.5734 1.2636 1.1235 0.0423  0.2485  -0.314  143 GLU A OE1   
1153 O  OE2   . GLU A 143 ? 1.6787 1.2109 1.1088 -0.0047 0.2763  -0.3043 143 GLU A OE2   
1154 N  N     . ILE A 144 ? 1.455  1.1483 1.0387 -0.012  0.2503  -0.447  144 ILE A N     
1155 C  CA    . ILE A 144 ? 1.4214 1.2073 1.0762 0.0071  0.2291  -0.4833 144 ILE A CA    
1156 C  C     . ILE A 144 ? 1.4001 1.2565 1.1148 -0.0411 0.2488  -0.5388 144 ILE A C     
1157 O  O     . ILE A 144 ? 1.346  1.2969 1.131  -0.0232 0.2322  -0.5636 144 ILE A O     
1158 C  CB    . ILE A 144 ? 1.4452 1.1971 1.0764 0.0195  0.2171  -0.4912 144 ILE A CB    
1159 C  CG1   . ILE A 144 ? 1.4909 1.1873 1.0718 0.0694  0.198   -0.4434 144 ILE A CG1   
1160 C  CG2   . ILE A 144 ? 1.3988 1.2408 1.0971 0.0331  0.1955  -0.535  144 ILE A CG2   
1161 C  CD1   . ILE A 144 ? 1.5392 1.1767 1.0788 0.0732  0.1947  -0.4478 144 ILE A CD1   
1162 N  N     . ALA A 145 ? 1.4424 1.2489 1.1249 -0.1033 0.2849  -0.5594 145 ALA A N     
1163 C  CA    . ALA A 145 ? 1.4251 1.2938 1.1587 -0.1619 0.3137  -0.6167 145 ALA A CA    
1164 C  C     . ALA A 145 ? 1.4116 1.3384 1.1839 -0.1657 0.3223  -0.6181 145 ALA A C     
1165 O  O     . ALA A 145 ? 1.3517 1.3812 1.2043 -0.1817 0.3259  -0.6709 145 ALA A O     
1166 C  CB    . ALA A 145 ? 1.4823 1.2574 1.1468 -0.2318 0.3558  -0.6258 145 ALA A CB    
1167 N  N     . ARG A 146 ? 1.4642 1.3284 1.1814 -0.1485 0.3233  -0.5636 146 ARG A N     
1168 C  CA    . ARG A 146 ? 1.462  1.3664 1.2034 -0.1464 0.329   -0.5557 146 ARG A CA    
1169 C  C     . ARG A 146 ? 1.4183 1.4274 1.2412 -0.0908 0.2907  -0.5673 146 ARG A C     
1170 O  O     . ARG A 146 ? 1.3779 1.4608 1.2562 -0.0963 0.2943  -0.5935 146 ARG A O     
1171 C  CB    . ARG A 146 ? 1.5399 1.3472 1.1988 -0.1288 0.3289  -0.4908 146 ARG A CB    
1172 C  CG    . ARG A 146 ? 1.5968 1.3838 1.2299 -0.1678 0.3598  -0.4851 146 ARG A CG    
1173 C  CD    . ARG A 146 ? 1.5935 1.4592 1.2836 -0.1348 0.3437  -0.4802 146 ARG A CD    
1174 N  NE    . ARG A 146 ? 1.6439 1.4861 1.3145 -0.0723 0.3092  -0.4281 146 ARG A NE    
1175 C  CZ    . ARG A 146 ? 1.6503 1.5296 1.3452 -0.0419 0.2945  -0.4096 146 ARG A CZ    
1176 N  NH1   . ARG A 146 ? 1.6102 1.5499 1.349  -0.0636 0.3089  -0.4377 146 ARG A NH1   
1177 N  NH2   . ARG A 146 ? 1.6634 1.5207 1.3389 0.0084  0.2668  -0.3657 146 ARG A NH2   
1178 N  N     . LEU A 147 ? 1.4285 1.4379 1.2519 -0.0372 0.254   -0.5484 147 LEU A N     
1179 C  CA    . LEU A 147 ? 1.4    1.4849 1.2786 0.017   0.2147  -0.5538 147 LEU A CA    
1180 C  C     . LEU A 147 ? 1.3547 1.5381 1.314  0.0142  0.2012  -0.621  147 LEU A C     
1181 O  O     . LEU A 147 ? 1.3182 1.5715 1.3296 0.0478  0.1743  -0.6385 147 LEU A O     
1182 C  CB    . LEU A 147 ? 1.4295 1.4724 1.2684 0.0701  0.1841  -0.5094 147 LEU A CB    
1183 C  CG    . LEU A 147 ? 1.4332 1.5071 1.2867 0.1226  0.1517  -0.4851 147 LEU A CG    
1184 C  CD1   . LEU A 147 ? 1.4474 1.5093 1.2907 0.1172  0.165   -0.4568 147 LEU A CD1   
1185 C  CD2   . LEU A 147 ? 1.4711 1.5022 1.2802 0.1639  0.1299  -0.4461 147 LEU A CD2   
1186 N  N     . GLU A 148 ? 1.3548 1.543  1.3239 -0.0252 0.2183  -0.6619 148 GLU A N     
1187 C  CA    . GLU A 148 ? 1.3029 1.5922 1.3545 -0.0307 0.2056  -0.7342 148 GLU A CA    
1188 C  C     . GLU A 148 ? 1.2613 1.6382 1.3835 -0.061  0.224   -0.7852 148 GLU A C     
1189 O  O     . GLU A 148 ? 1.2027 1.6813 1.4058 -0.0431 0.1997  -0.8429 148 GLU A O     
1190 C  CB    . GLU A 148 ? 1.3315 1.6012 1.3738 -0.0729 0.2241  -0.7666 148 GLU A CB    
1191 C  CG    . GLU A 148 ? 1.4263 1.6167 1.4045 -0.0424 0.2056  -0.7249 148 GLU A CG    
1192 C  CD    . GLU A 148 ? 1.5129 1.6541 1.4603 -0.0886 0.2296  -0.7454 148 GLU A CD    
1193 O  OE1   . GLU A 148 ? 1.5008 1.6752 1.4804 -0.1492 0.2613  -0.7975 148 GLU A OE1   
1194 O  OE2   . GLU A 148 ? 1.5735 1.6424 1.4633 -0.0659 0.2178  -0.7114 148 GLU A OE2   
1195 N  N     . ASP A 149 ? 1.2887 1.6266 1.3788 -0.1047 0.265   -0.7669 149 ASP A N     
1196 C  CA    . ASP A 149 ? 1.2526 1.6692 1.4029 -0.1389 0.2891  -0.8145 149 ASP A CA    
1197 C  C     . ASP A 149 ? 1.2278 1.692  1.4131 -0.083  0.2562  -0.8019 149 ASP A C     
1198 O  O     . ASP A 149 ? 1.2664 1.6676 1.3992 -0.0406 0.2356  -0.7379 149 ASP A O     
1199 C  CB    . ASP A 149 ? 1.3231 1.6679 1.4113 -0.2093 0.3467  -0.7976 149 ASP A CB    
1200 C  CG    . ASP A 149 ? 1.4309 1.6941 1.4569 -0.265  0.3795  -0.7974 149 ASP A CG    
1201 O  OD1   . ASP A 149 ? 1.4225 1.7074 1.4728 -0.2587 0.3634  -0.8253 149 ASP A OD1   
1202 O  OD2   . ASP A 149 ? 1.5165 1.6877 1.4634 -0.3146 0.4197  -0.7697 149 ASP A OD2   
1203 N  N     . MET B 1   ? 0.5695 0.3761 0.2418 -0.0296 0.0296  0.097   1   MET B N     
1204 C  CA    . MET B 1   ? 0.5797 0.372  0.264  -0.0429 0.0309  0.0874  1   MET B CA    
1205 C  C     . MET B 1   ? 0.5858 0.3802 0.2673 -0.0652 0.0401  0.0904  1   MET B C     
1206 O  O     . MET B 1   ? 0.5715 0.4031 0.2599 -0.0706 0.0426  0.087   1   MET B O     
1207 C  CB    . MET B 1   ? 0.5742 0.3917 0.2803 -0.0394 0.0227  0.0682  1   MET B CB    
1208 C  CG    . MET B 1   ? 0.5973 0.4027 0.3082 -0.0262 0.015   0.0624  1   MET B CG    
1209 S  SD    . MET B 1   ? 0.622  0.3888 0.3354 -0.0315 0.0152  0.0595  1   MET B SD    
1210 C  CE    . MET B 1   ? 0.6191 0.4082 0.3493 -0.0435 0.0128  0.0447  1   MET B CE    
1211 N  N     . HIS B 2   ? 0.6056 0.3621 0.2774 -0.0795 0.0453  0.0944  2   HIS B N     
1212 C  CA    . HIS B 2   ? 0.6165 0.3736 0.2854 -0.1077 0.0536  0.0954  2   HIS B CA    
1213 C  C     . HIS B 2   ? 0.5936 0.3987 0.2924 -0.1142 0.0473  0.0786  2   HIS B C     
1214 O  O     . HIS B 2   ? 0.5906 0.3986 0.3035 -0.1016 0.0379  0.0671  2   HIS B O     
1215 C  CB    . HIS B 2   ? 0.6596 0.3575 0.3081 -0.1209 0.0588  0.0992  2   HIS B CB    
1216 C  CG    . HIS B 2   ? 0.7127 0.3953 0.3452 -0.1546 0.07    0.1042  2   HIS B CG    
1217 N  ND1   . HIS B 2   ? 0.7729 0.3978 0.3674 -0.163  0.0828  0.1206  2   HIS B ND1   
1218 C  CD2   . HIS B 2   ? 0.7141 0.4322 0.3622 -0.1823 0.0704  0.0952  2   HIS B CD2   
1219 C  CE1   . HIS B 2   ? 0.7845 0.4074 0.3708 -0.1997 0.0912  0.1198  2   HIS B CE1   
1220 N  NE2   . HIS B 2   ? 0.7515 0.4354 0.3718 -0.2129 0.0835  0.1046  2   HIS B NE2   
1221 N  N     . CYS B 3   ? 0.5706 0.4157 0.2785 -0.1319 0.0529  0.0781  3   CYS B N     
1222 C  CA    . CYS B 3   ? 0.5421 0.4383 0.2783 -0.1335 0.0476  0.0645  3   CYS B CA    
1223 C  C     . CYS B 3   ? 0.5537 0.435  0.2945 -0.15   0.0429  0.0576  3   CYS B C     
1224 O  O     . CYS B 3   ? 0.5702 0.4279 0.2964 -0.1778 0.0491  0.0627  3   CYS B O     
1225 C  CB    . CYS B 3   ? 0.5084 0.4582 0.2546 -0.1468 0.0561  0.067   3   CYS B CB    
1226 S  SG    . CYS B 3   ? 0.428  0.4484 0.2096 -0.1474 0.051   0.0535  3   CYS B SG    
1227 N  N     . PRO B 4   ? 0.5416 0.4342 0.2986 -0.1346 0.0323  0.0456  4   PRO B N     
1228 C  CA    . PRO B 4   ? 0.5469 0.4284 0.3065 -0.1493 0.0266  0.0385  4   PRO B CA    
1229 C  C     . PRO B 4   ? 0.5309 0.4637 0.3065 -0.1744 0.0267  0.0352  4   PRO B C     
1230 O  O     . PRO B 4   ? 0.5347 0.4628 0.3101 -0.1912 0.0215  0.0293  4   PRO B O     
1231 C  CB    . PRO B 4   ? 0.5486 0.4305 0.3191 -0.123  0.016   0.0285  4   PRO B CB    
1232 C  CG    . PRO B 4   ? 0.5371 0.4538 0.3189 -0.1009 0.0163  0.027   4   PRO B CG    
1233 C  CD    . PRO B 4   ? 0.5241 0.4357 0.2931 -0.105  0.0258  0.038   4   PRO B CD    
1234 N  N     . PHE B 5   ? 0.5118 0.4975 0.3007 -0.1778 0.0328  0.0389  5   PHE B N     
1235 C  CA    . PHE B 5   ? 0.4957 0.5453 0.3047 -0.2    0.0332  0.0366  5   PHE B CA    
1236 C  C     . PHE B 5   ? 0.5202 0.5754 0.3182 -0.2366 0.0458  0.0458  5   PHE B C     
1237 O  O     . PHE B 5   ? 0.5256 0.5873 0.321  -0.2717 0.0459  0.044   5   PHE B O     
1238 C  CB    . PHE B 5   ? 0.4562 0.5762 0.2938 -0.1732 0.031   0.0323  5   PHE B CB    
1239 C  CG    . PHE B 5   ? 0.4653 0.5702 0.3064 -0.136  0.0218  0.0245  5   PHE B CG    
1240 C  CD1   . PHE B 5   ? 0.4777 0.565  0.3196 -0.1332 0.0107  0.0176  5   PHE B CD1   
1241 C  CD2   . PHE B 5   ? 0.4724 0.5772 0.3115 -0.1064 0.0252  0.0236  5   PHE B CD2   
1242 C  CE1   . PHE B 5   ? 0.491  0.5597 0.3322 -0.1017 0.0039  0.0113  5   PHE B CE1   
1243 C  CE2   . PHE B 5   ? 0.4871 0.5725 0.3245 -0.0769 0.0183  0.0159  5   PHE B CE2   
1244 C  CZ    . PHE B 5   ? 0.4917 0.5585 0.3303 -0.0749 0.008   0.0104  5   PHE B CZ    
1245 N  N     . CYS B 6   ? 0.5376 0.5886 0.3256 -0.2314 0.0566  0.0554  6   CYS B N     
1246 C  CA    . CYS B 6   ? 0.5622 0.6198 0.3376 -0.2665 0.0702  0.0653  6   CYS B CA    
1247 C  C     . CYS B 6   ? 0.6275 0.5984 0.3607 -0.2848 0.0788  0.0757  6   CYS B C     
1248 O  O     . CYS B 6   ? 0.659  0.6143 0.3773 -0.3244 0.0848  0.0772  6   CYS B O     
1249 C  CB    . CYS B 6   ? 0.5427 0.6559 0.3303 -0.2567 0.0797  0.071   6   CYS B CB    
1250 S  SG    . CYS B 6   ? 0.5791 0.6447 0.3405 -0.227  0.0854  0.0807  6   CYS B SG    
1251 N  N     . PHE B 7   ? 0.6455 0.5647 0.3569 -0.26   0.0812  0.084   7   PHE B N     
1252 C  CA    . PHE B 7   ? 0.6863 0.527  0.3547 -0.2733 0.0922  0.0978  7   PHE B CA    
1253 C  C     . PHE B 7   ? 0.6793 0.5005 0.3316 -0.2451 0.0965  0.1107  7   PHE B C     
1254 O  O     . PHE B 7   ? 0.7077 0.4632 0.3228 -0.2464 0.1049  0.1246  7   PHE B O     
1255 C  CB    . PHE B 7   ? 0.7003 0.5417 0.3509 -0.3205 0.1071  0.1055  7   PHE B CB    
1256 C  CG    . PHE B 7   ? 0.7057 0.5963 0.361  -0.328  0.1183  0.1151  7   PHE B CG    
1257 C  CD1   . PHE B 7   ? 0.6784 0.6615 0.3711 -0.3374 0.1176  0.1078  7   PHE B CD1   
1258 C  CD2   . PHE B 7   ? 0.7493 0.5944 0.3692 -0.3255 0.1307  0.1326  7   PHE B CD2   
1259 C  CE1   . PHE B 7   ? 0.6734 0.7032 0.3694 -0.3434 0.1298  0.1164  7   PHE B CE1   
1260 C  CE2   . PHE B 7   ? 0.7443 0.6344 0.3658 -0.3325 0.1418  0.1416  7   PHE B CE2   
1261 C  CZ    . PHE B 7   ? 0.6993 0.681  0.3588 -0.3423 0.1419  0.1328  7   PHE B CZ    
1262 N  N     . ALA B 8   ? 0.6379 0.5158 0.3139 -0.2211 0.0921  0.1069  8   ALA B N     
1263 C  CA    . ALA B 8   ? 0.6396 0.509  0.299  -0.1999 0.0961  0.1183  8   ALA B CA    
1264 C  C     . ALA B 8   ? 0.6553 0.4721 0.2995 -0.1726 0.0883  0.1215  8   ALA B C     
1265 O  O     . ALA B 8   ? 0.6537 0.4714 0.3152 -0.1577 0.0769  0.1092  8   ALA B O     
1266 C  CB    . ALA B 8   ? 0.6092 0.5464 0.2932 -0.1823 0.0937  0.1105  8   ALA B CB    
1267 N  N     . VAL B 9   ? 0.6671 0.4358 0.277  -0.1678 0.0956  0.1392  9   VAL B N     
1268 C  CA    . VAL B 9   ? 0.677  0.3971 0.2704 -0.1416 0.0901  0.1457  9   VAL B CA    
1269 C  C     . VAL B 9   ? 0.6435 0.3963 0.2545 -0.1094 0.0772  0.1392  9   VAL B C     
1270 O  O     . VAL B 9   ? 0.6542 0.3811 0.2613 -0.0886 0.0706  0.1407  9   VAL B O     
1271 C  CB    . VAL B 9   ? 0.7213 0.3855 0.2713 -0.1416 0.1023  0.169   9   VAL B CB    
1272 C  CG1   . VAL B 9   ? 0.7604 0.3691 0.2848 -0.1737 0.1151  0.1734  9   VAL B CG1   
1273 C  CG2   . VAL B 9   ? 0.7157 0.4121 0.2559 -0.1417 0.1084  0.1804  9   VAL B CG2   
1274 N  N     . ASP B 10  ? 0.6054 0.414  0.2338 -0.1062 0.0747  0.1312  10  ASP B N     
1275 C  CA    . ASP B 10  ? 0.5906 0.4276 0.231  -0.0814 0.0636  0.1224  10  ASP B CA    
1276 C  C     . ASP B 10  ? 0.5545 0.4449 0.218  -0.0835 0.0626  0.1063  10  ASP B C     
1277 O  O     . ASP B 10  ? 0.5518 0.4685 0.2188 -0.0995 0.0719  0.1072  10  ASP B O     
1278 C  CB    . ASP B 10  ? 0.6284 0.4632 0.2445 -0.0661 0.064   0.1375  10  ASP B CB    
1279 C  CG    . ASP B 10  ? 0.6911 0.5431 0.3131 -0.0428 0.0509  0.1305  10  ASP B CG    
1280 O  OD1   . ASP B 10  ? 0.6869 0.5485 0.3309 -0.0384 0.0425  0.1133  10  ASP B OD1   
1281 O  OD2   . ASP B 10  ? 0.7301 0.587  0.3332 -0.0305 0.0489  0.1427  10  ASP B OD2   
1282 N  N     . THR B 11  ? 0.5247 0.4301 0.2022 -0.0666 0.0524  0.0918  11  THR B N     
1283 C  CA    . THR B 11  ? 0.4894 0.4357 0.1836 -0.0613 0.0517  0.0756  11  THR B CA    
1284 C  C     . THR B 11  ? 0.4788 0.4359 0.1624 -0.0439 0.0467  0.069   11  THR B C     
1285 O  O     . THR B 11  ? 0.4966 0.4347 0.1693 -0.0359 0.0395  0.0738  11  THR B O     
1286 C  CB    . THR B 11  ? 0.4808 0.425  0.1969 -0.0601 0.045   0.0623  11  THR B CB    
1287 O  OG1   . THR B 11  ? 0.4974 0.4085 0.2104 -0.0506 0.0357  0.061   11  THR B OG1   
1288 C  CG2   . THR B 11  ? 0.4788 0.424  0.2053 -0.0811 0.0495  0.0656  11  THR B CG2   
1289 N  N     . LYS B 12  ? 0.4457 0.4341 0.1311 -0.0381 0.0508  0.0576  12  LYS B N     
1290 C  CA    . LYS B 12  ? 0.4412 0.4349 0.1112 -0.0255 0.047   0.0481  12  LYS B CA    
1291 C  C     . LYS B 12  ? 0.4356 0.4153 0.113  -0.0158 0.038   0.0316  12  LYS B C     
1292 O  O     . LYS B 12  ? 0.4242 0.4078 0.1171 -0.0123 0.0395  0.0222  12  LYS B O     
1293 C  CB    . LYS B 12  ? 0.4577 0.4831 0.1206 -0.0222 0.058   0.0412  12  LYS B CB    
1294 C  CG    . LYS B 12  ? 0.5081 0.5347 0.1491 -0.0112 0.0564  0.0273  12  LYS B CG    
1295 C  CD    . LYS B 12  ? 0.5585 0.5799 0.1754 -0.0142 0.0504  0.0362  12  LYS B CD    
1296 C  CE    . LYS B 12  ? 0.6019 0.6228 0.1957 -0.0088 0.0468  0.0197  12  LYS B CE    
1297 N  NZ    . LYS B 12  ? 0.6351 0.6515 0.2158 -0.012  0.034   0.0254  12  LYS B NZ    
1298 N  N     . VAL B 13  ? 0.4407 0.4082 0.1053 -0.0117 0.0292  0.028   13  VAL B N     
1299 C  CA    . VAL B 13  ? 0.4482 0.4015 0.1139 -0.006  0.0227  0.0114  13  VAL B CA    
1300 C  C     . VAL B 13  ? 0.4688 0.4307 0.1169 0.0001  0.0294  -0.0041 13  VAL B C     
1301 O  O     . VAL B 13  ? 0.4799 0.4505 0.1049 -0.0017 0.0302  -0.0059 13  VAL B O     
1302 C  CB    . VAL B 13  ? 0.4536 0.397  0.1126 -0.0075 0.0118  0.0125  13  VAL B CB    
1303 C  CG1   . VAL B 13  ? 0.4644 0.3936 0.1179 -0.0064 0.0075  -0.0063 13  VAL B CG1   
1304 C  CG2   . VAL B 13  ? 0.4589 0.3891 0.1331 -0.0085 0.0074  0.0264  13  VAL B CG2   
1305 N  N     . ILE B 14  ? 0.4673 0.4273 0.1234 0.0088  0.0351  -0.0146 14  ILE B N     
1306 C  CA    . ILE B 14  ? 0.4737 0.4344 0.1095 0.0195  0.0441  -0.0296 14  ILE B CA    
1307 C  C     . ILE B 14  ? 0.5045 0.4304 0.1224 0.0234  0.0402  -0.0466 14  ILE B C     
1308 O  O     . ILE B 14  ? 0.5269 0.4408 0.1233 0.0342  0.0491  -0.0605 14  ILE B O     
1309 C  CB    . ILE B 14  ? 0.4527 0.4374 0.1027 0.0312  0.0557  -0.0295 14  ILE B CB    
1310 C  CG1   . ILE B 14  ? 0.455  0.4304 0.1263 0.0394  0.052   -0.0325 14  ILE B CG1   
1311 C  CG2   . ILE B 14  ? 0.434  0.4536 0.0977 0.0212  0.0611  -0.0131 14  ILE B CG2   
1312 C  CD1   . ILE B 14  ? 0.4498 0.4584 0.1409 0.0507  0.0602  -0.0304 14  ILE B CD1   
1313 N  N     . ASP B 15  ? 0.5074 0.4152 0.1303 0.0143  0.0287  -0.0457 15  ASP B N     
1314 C  CA    . ASP B 15  ? 0.5352 0.41   0.1398 0.0118  0.0251  -0.0608 15  ASP B CA    
1315 C  C     . ASP B 15  ? 0.5307 0.3985 0.1509 0.0018  0.0135  -0.055  15  ASP B C     
1316 O  O     . ASP B 15  ? 0.5192 0.3936 0.1656 0.0036  0.0105  -0.0432 15  ASP B O     
1317 C  CB    . ASP B 15  ? 0.5843 0.4332 0.1826 0.0274  0.0329  -0.0723 15  ASP B CB    
1318 C  CG    . ASP B 15  ? 0.7006 0.506  0.2667 0.0235  0.0334  -0.0895 15  ASP B CG    
1319 O  OD1   . ASP B 15  ? 0.7261 0.526  0.2642 0.0105  0.033   -0.0984 15  ASP B OD1   
1320 O  OD2   . ASP B 15  ? 0.7581 0.5343 0.3241 0.0315  0.0343  -0.0941 15  ASP B OD2   
1321 N  N     . SER B 16  ? 0.5428 0.3981 0.1456 -0.0098 0.0079  -0.0639 16  SER B N     
1322 C  CA    . SER B 16  ? 0.5557 0.4089 0.173  -0.0187 -0.0017 -0.0596 16  SER B CA    
1323 C  C     . SER B 16  ? 0.595  0.4187 0.1897 -0.0294 -0.0024 -0.0766 16  SER B C     
1324 O  O     . SER B 16  ? 0.6277 0.4328 0.1905 -0.0327 0.0036  -0.0913 16  SER B O     
1325 C  CB    . SER B 16  ? 0.5546 0.4415 0.1802 -0.0256 -0.0098 -0.0458 16  SER B CB    
1326 O  OG    . SER B 16  ? 0.5862 0.4849 0.1884 -0.0391 -0.0142 -0.0545 16  SER B OG    
1327 N  N     . ARG B 17  ? 0.5917 0.4086 0.1991 -0.0363 -0.0082 -0.0751 17  ARG B N     
1328 C  CA    . ARG B 17  ? 0.6165 0.4043 0.2018 -0.0506 -0.0079 -0.0902 17  ARG B CA    
1329 C  C     . ARG B 17  ? 0.5851 0.3807 0.1912 -0.0588 -0.0148 -0.0842 17  ARG B C     
1330 O  O     . ARG B 17  ? 0.5672 0.3673 0.2    -0.0473 -0.0162 -0.0723 17  ARG B O     
1331 C  CB    . ARG B 17  ? 0.6927 0.432  0.2584 -0.0389 0.0022  -0.1012 17  ARG B CB    
1332 C  CG    . ARG B 17  ? 0.8127 0.5078 0.3484 -0.0534 0.0054  -0.1163 17  ARG B CG    
1333 C  CD    . ARG B 17  ? 0.9216 0.5644 0.4318 -0.0362 0.0169  -0.125  17  ARG B CD    
1334 N  NE    . ARG B 17  ? 0.9985 0.6302 0.5297 -0.0215 0.0162  -0.1163 17  ARG B NE    
1335 C  CZ    . ARG B 17  ? 1.0427 0.6911 0.5978 0.0013  0.0168  -0.106  17  ARG B CZ    
1336 N  NH1   . ARG B 17  ? 1.0328 0.6711 0.6024 0.0116  0.0151  -0.0996 17  ARG B NH1   
1337 N  NH2   . ARG B 17  ? 1.047  0.7247 0.6102 0.012   0.0194  -0.1022 17  ARG B NH2   
1338 N  N     . LEU B 18  ? 0.5779 0.3769 0.1704 -0.0803 -0.0183 -0.093  18  LEU B N     
1339 C  CA    . LEU B 18  ? 0.567  0.3773 0.1778 -0.0892 -0.023  -0.0886 18  LEU B CA    
1340 C  C     . LEU B 18  ? 0.6029 0.3634 0.2037 -0.0884 -0.0164 -0.0963 18  LEU B C     
1341 O  O     . LEU B 18  ? 0.6276 0.3468 0.194  -0.0984 -0.01   -0.1114 18  LEU B O     
1342 C  CB    . LEU B 18  ? 0.552  0.3919 0.1523 -0.1156 -0.0289 -0.0956 18  LEU B CB    
1343 C  CG    . LEU B 18  ? 0.5306 0.434  0.1536 -0.1139 -0.0385 -0.0813 18  LEU B CG    
1344 C  CD1   . LEU B 18  ? 0.5322 0.472  0.1411 -0.142  -0.0452 -0.0901 18  LEU B CD1   
1345 C  CD2   . LEU B 18  ? 0.5131 0.4365 0.1711 -0.0996 -0.0408 -0.065  18  LEU B CD2   
1346 N  N     . VAL B 19  ? 0.6029 0.3633 0.2296 -0.076  -0.0172 -0.0855 19  VAL B N     
1347 C  CA    . VAL B 19  ? 0.6356 0.3543 0.2559 -0.0731 -0.0123 -0.0892 19  VAL B CA    
1348 C  C     . VAL B 19  ? 0.6466 0.3792 0.2804 -0.0861 -0.0147 -0.0862 19  VAL B C     
1349 O  O     . VAL B 19  ? 0.6253 0.4046 0.2799 -0.0908 -0.0203 -0.0784 19  VAL B O     
1350 C  CB    . VAL B 19  ? 0.6372 0.3431 0.2719 -0.0489 -0.0106 -0.0809 19  VAL B CB    
1351 C  CG1   . VAL B 19  ? 0.6488 0.3479 0.2713 -0.036  -0.0066 -0.0841 19  VAL B CG1   
1352 C  CG2   . VAL B 19  ? 0.6148 0.3534 0.283  -0.0408 -0.0156 -0.0658 19  VAL B CG2   
1353 N  N     . GLY B 20  ? 0.6767 0.37   0.2963 -0.0907 -0.0096 -0.0918 20  GLY B N     
1354 C  CA    . GLY B 20  ? 0.6885 0.3912 0.3177 -0.1036 -0.0093 -0.0899 20  GLY B CA    
1355 C  C     . GLY B 20  ? 0.6942 0.4336 0.3218 -0.1302 -0.012  -0.0949 20  GLY B C     
1356 O  O     . GLY B 20  ? 0.6714 0.4574 0.3256 -0.1328 -0.0155 -0.0866 20  GLY B O     
1357 N  N     . GLU B 21  ? 0.7218 0.4437 0.3174 -0.1492 -0.0101 -0.1086 21  GLU B N     
1358 C  CA    . GLU B 21  ? 0.7283 0.487  0.3173 -0.1806 -0.0134 -0.116  21  GLU B CA    
1359 C  C     . GLU B 21  ? 0.6942 0.531  0.3174 -0.1757 -0.0239 -0.1041 21  GLU B C     
1360 O  O     . GLU B 21  ? 0.6841 0.5726 0.3212 -0.1939 -0.028  -0.1026 21  GLU B O     
1361 C  CB    . GLU B 21  ? 0.7728 0.5247 0.3557 -0.2055 -0.0085 -0.1207 21  GLU B CB    
1362 C  CG    . GLU B 21  ? 0.8963 0.5675 0.4445 -0.2061 0.0024  -0.1284 21  GLU B CG    
1363 C  CD    . GLU B 21  ? 1.0118 0.6745 0.5539 -0.2295 0.0086  -0.1306 21  GLU B CD    
1364 O  OE1   . GLU B 21  ? 1.0435 0.6828 0.5931 -0.2135 0.0127  -0.1231 21  GLU B OE1   
1365 O  OE2   . GLU B 21  ? 1.0465 0.7288 0.5753 -0.2661 0.0094  -0.1401 21  GLU B OE2   
1366 N  N     . GLY B 22  ? 0.6706 0.5176 0.3063 -0.1507 -0.0274 -0.0948 22  GLY B N     
1367 C  CA    . GLY B 22  ? 0.6278 0.5399 0.2907 -0.1411 -0.0361 -0.0809 22  GLY B CA    
1368 C  C     . GLY B 22  ? 0.5965 0.5261 0.2937 -0.115  -0.0364 -0.0627 22  GLY B C     
1369 O  O     . GLY B 22  ? 0.588  0.5549 0.3029 -0.0987 -0.0412 -0.0486 22  GLY B O     
1370 N  N     . SER B 23  ? 0.5772 0.4752 0.2797 -0.1102 -0.0303 -0.0626 23  SER B N     
1371 C  CA    . SER B 23  ? 0.5444 0.4502 0.2731 -0.0872 -0.0287 -0.0478 23  SER B CA    
1372 C  C     . SER B 23  ? 0.5254 0.413  0.2599 -0.0627 -0.0285 -0.0377 23  SER B C     
1373 O  O     . SER B 23  ? 0.5197 0.4081 0.2705 -0.0451 -0.0264 -0.0259 23  SER B O     
1374 C  CB    . SER B 23  ? 0.5594 0.4312 0.286  -0.0904 -0.0218 -0.0521 23  SER B CB    
1375 O  OG    . SER B 23  ? 0.5859 0.4007 0.2965 -0.0832 -0.0181 -0.0572 23  SER B OG    
1376 N  N     . SER B 24  ? 0.5112 0.3797 0.2297 -0.0629 -0.0292 -0.0432 24  SER B N     
1377 C  CA    . SER B 24  ? 0.4959 0.3508 0.2195 -0.0445 -0.0282 -0.0344 24  SER B CA    
1378 C  C     . SER B 24  ? 0.4674 0.3198 0.1754 -0.0458 -0.0288 -0.0392 24  SER B C     
1379 O  O     . SER B 24  ? 0.4727 0.3142 0.1596 -0.0592 -0.0281 -0.0528 24  SER B O     
1380 C  CB    . SER B 24  ? 0.5349 0.3494 0.26   -0.0364 -0.0236 -0.0355 24  SER B CB    
1381 O  OG    . SER B 24  ? 0.5758 0.3864 0.3097 -0.0223 -0.0227 -0.025  24  SER B OG    
1382 N  N     . VAL B 25  ? 0.439  0.2979 0.1539 -0.0327 -0.0286 -0.0281 25  VAL B N     
1383 C  CA    . VAL B 25  ? 0.423  0.2845 0.1246 -0.0323 -0.0277 -0.0307 25  VAL B CA    
1384 C  C     . VAL B 25  ? 0.4156 0.2513 0.1185 -0.0225 -0.0223 -0.0306 25  VAL B C     
1385 O  O     . VAL B 25  ? 0.4079 0.2409 0.125  -0.0144 -0.0211 -0.0195 25  VAL B O     
1386 C  CB    . VAL B 25  ? 0.412  0.3103 0.1171 -0.0277 -0.0315 -0.017  25  VAL B CB    
1387 C  CG1   . VAL B 25  ? 0.4193 0.3179 0.1121 -0.025  -0.0284 -0.0167 25  VAL B CG1   
1388 C  CG2   . VAL B 25  ? 0.4063 0.3412 0.1075 -0.0392 -0.0383 -0.0192 25  VAL B CG2   
1389 N  N     . ARG B 26  ? 0.4158 0.2334 0.1022 -0.0235 -0.0185 -0.043  26  ARG B N     
1390 C  CA    . ARG B 26  ? 0.4192 0.2237 0.1086 -0.0127 -0.0136 -0.0427 26  ARG B CA    
1391 C  C     . ARG B 26  ? 0.4109 0.2345 0.0949 -0.0093 -0.0104 -0.04   26  ARG B C     
1392 O  O     . ARG B 26  ? 0.4217 0.25   0.0866 -0.0141 -0.0094 -0.0476 26  ARG B O     
1393 C  CB    . ARG B 26  ? 0.4553 0.2279 0.129  -0.0097 -0.0098 -0.0559 26  ARG B CB    
1394 C  CG    . ARG B 26  ? 0.5015 0.2706 0.1789 0.0048  -0.0052 -0.0553 26  ARG B CG    
1395 C  CD    . ARG B 26  ? 0.5878 0.3257 0.2404 0.0125  0.0005  -0.068  26  ARG B CD    
1396 N  NE    . ARG B 26  ? 0.6796 0.4052 0.3389 0.0256  0.001   -0.066  26  ARG B NE    
1397 C  CZ    . ARG B 26  ? 0.7379 0.476  0.402  0.0422  0.0049  -0.0641 26  ARG B CZ    
1398 N  NH1   . ARG B 26  ? 0.7458 0.5059 0.4082 0.0478  0.0103  -0.0645 26  ARG B NH1   
1399 N  NH2   . ARG B 26  ? 0.7305 0.4638 0.4012 0.0537  0.0034  -0.0614 26  ARG B NH2   
1400 N  N     . ARG B 27  ? 0.3893 0.2239 0.0876 -0.0035 -0.008  -0.0297 27  ARG B N     
1401 C  CA    . ARG B 27  ? 0.3682 0.2232 0.0621 -0.0012 -0.0031 -0.0258 27  ARG B CA    
1402 C  C     . ARG B 27  ? 0.3673 0.2263 0.0699 0.0064  0.0028  -0.0263 27  ARG B C     
1403 O  O     . ARG B 27  ? 0.3751 0.2272 0.0919 0.0078  0.0012  -0.0242 27  ARG B O     
1404 C  CB    . ARG B 27  ? 0.3535 0.2252 0.0545 -0.0046 -0.0046 -0.0093 27  ARG B CB    
1405 C  CG    . ARG B 27  ? 0.3593 0.2401 0.0537 -0.0084 -0.011  -0.0057 27  ARG B CG    
1406 C  CD    . ARG B 27  ? 0.3556 0.2511 0.0514 -0.0064 -0.0109 0.0127  27  ARG B CD    
1407 N  NE    . ARG B 27  ? 0.3511 0.2643 0.0423 -0.0062 -0.0179 0.0179  27  ARG B NE    
1408 C  CZ    . ARG B 27  ? 0.3755 0.2878 0.0772 -0.0014 -0.0217 0.0266  27  ARG B CZ    
1409 N  NH1   . ARG B 27  ? 0.3749 0.2621 0.0889 0.0019  -0.0187 0.0291  27  ARG B NH1   
1410 N  NH2   . ARG B 27  ? 0.3796 0.3195 0.0792 0.0002  -0.0284 0.0318  27  ARG B NH2   
1411 N  N     . ARG B 28  ? 0.3616 0.2356 0.0551 0.0117  0.0098  -0.0297 28  ARG B N     
1412 C  CA    . ARG B 28  ? 0.3565 0.2476 0.0604 0.0204  0.0164  -0.0292 28  ARG B CA    
1413 C  C     . ARG B 28  ? 0.35   0.2708 0.0585 0.0141  0.0215  -0.0182 28  ARG B C     
1414 O  O     . ARG B 28  ? 0.3522 0.2818 0.0439 0.0153  0.0262  -0.0205 28  ARG B O     
1415 C  CB    . ARG B 28  ? 0.3771 0.2603 0.0624 0.0356  0.0236  -0.0429 28  ARG B CB    
1416 C  CG    . ARG B 28  ? 0.3792 0.288  0.0771 0.0504  0.0309  -0.042  28  ARG B CG    
1417 C  CD    . ARG B 28  ? 0.3629 0.28   0.0858 0.0495  0.0249  -0.0357 28  ARG B CD    
1418 N  NE    . ARG B 28  ? 0.3583 0.3037 0.092  0.0668  0.0302  -0.0363 28  ARG B NE    
1419 C  CZ    . ARG B 28  ? 0.3665 0.3275 0.1201 0.0684  0.0249  -0.0321 28  ARG B CZ    
1420 N  NH1   . ARG B 28  ? 0.3348 0.3306 0.0989 0.0868  0.0293  -0.0317 28  ARG B NH1   
1421 N  NH2   . ARG B 28  ? 0.3808 0.3245 0.1424 0.0531  0.0153  -0.0283 28  ARG B NH2   
1422 N  N     . ARG B 29  ? 0.3364 0.2685 0.063  0.0051  0.021   -0.0064 29  ARG B N     
1423 C  CA    . ARG B 29  ? 0.3246 0.2779 0.0515 -0.0045 0.027   0.0059  29  ARG B CA    
1424 C  C     . ARG B 29  ? 0.3215 0.3115 0.0609 -0.0042 0.0359  0.0067  29  ARG B C     
1425 O  O     . ARG B 29  ? 0.3224 0.3233 0.0751 0.0034  0.0354  0.0004  29  ARG B O     
1426 C  CB    . ARG B 29  ? 0.3244 0.2599 0.0554 -0.0176 0.0232  0.0193  29  ARG B CB    
1427 C  CG    . ARG B 29  ? 0.3508 0.2574 0.0764 -0.0143 0.0145  0.0183  29  ARG B CG    
1428 C  CD    . ARG B 29  ? 0.3959 0.283  0.1201 -0.0212 0.0135  0.0326  29  ARG B CD    
1429 N  NE    . ARG B 29  ? 0.4699 0.3642 0.1802 -0.0238 0.0182  0.046   29  ARG B NE    
1430 C  CZ    . ARG B 29  ? 0.5207 0.4089 0.2186 -0.0178 0.0147  0.0548  29  ARG B CZ    
1431 N  NH1   . ARG B 29  ? 0.5261 0.4049 0.2267 -0.0106 0.0069  0.051   29  ARG B NH1   
1432 N  NH2   . ARG B 29  ? 0.5238 0.4187 0.2063 -0.0188 0.0192  0.0686  29  ARG B NH2   
1433 N  N     . GLN B 30  ? 0.3197 0.3328 0.0543 -0.0113 0.0444  0.0149  30  GLN B N     
1434 C  CA    . GLN B 30  ? 0.3115 0.368  0.0602 -0.0143 0.0542  0.0174  30  GLN B CA    
1435 C  C     . GLN B 30  ? 0.3245 0.3878 0.0731 -0.037  0.0592  0.033   30  GLN B C     
1436 O  O     . GLN B 30  ? 0.3367 0.3819 0.0659 -0.0416 0.0605  0.0415  30  GLN B O     
1437 C  CB    . GLN B 30  ? 0.3163 0.3981 0.0545 0.0019  0.0644  0.0097  30  GLN B CB    
1438 C  CG    . GLN B 30  ? 0.3206 0.457  0.0763 0.0003  0.076   0.0134  30  GLN B CG    
1439 C  CD    . GLN B 30  ? 0.3875 0.5471 0.1333 0.0232  0.0873  0.0036  30  GLN B CD    
1440 O  OE1   . GLN B 30  ? 0.4457 0.5779 0.1757 0.0431  0.0855  -0.0091 30  GLN B OE1   
1441 N  NE2   . GLN B 30  ? 0.3534 0.5614 0.1052 0.0206  0.1009  0.0089  30  GLN B NE2   
1442 N  N     . CYS B 31  ? 0.3281 0.4161 0.0956 -0.0523 0.0621  0.0374  31  CYS B N     
1443 C  CA    . CYS B 31  ? 0.3562 0.4449 0.119  -0.0784 0.069   0.0517  31  CYS B CA    
1444 C  C     . CYS B 31  ? 0.3565 0.4879 0.1164 -0.0816 0.0828  0.0563  31  CYS B C     
1445 O  O     . CYS B 31  ? 0.3359 0.514  0.1105 -0.0693 0.088   0.0485  31  CYS B O     
1446 C  CB    . CYS B 31  ? 0.371  0.4658 0.1506 -0.1001 0.0665  0.0533  31  CYS B CB    
1447 S  SG    . CYS B 31  ? 0.4824 0.5598 0.2465 -0.1377 0.0765  0.0702  31  CYS B SG    
1448 N  N     . LEU B 32  ? 0.3798 0.4944 0.1182 -0.0953 0.0896  0.0698  32  LEU B N     
1449 C  CA    . LEU B 32  ? 0.3863 0.538  0.1173 -0.1003 0.1039  0.0758  32  LEU B CA    
1450 C  C     . LEU B 32  ? 0.3886 0.5839 0.1383 -0.1268 0.1139  0.0812  32  LEU B C     
1451 O  O     . LEU B 32  ? 0.3698 0.6224 0.1315 -0.1245 0.1248  0.079   32  LEU B O     
1452 C  CB    . LEU B 32  ? 0.4117 0.5283 0.1089 -0.1046 0.1073  0.0899  32  LEU B CB    
1453 C  CG    . LEU B 32  ? 0.4378 0.5434 0.1155 -0.0798 0.1022  0.0836  32  LEU B CG    
1454 C  CD1   . LEU B 32  ? 0.4573 0.5345 0.1415 -0.0633 0.0868  0.0716  32  LEU B CD1   
1455 C  CD2   . LEU B 32  ? 0.4529 0.5334 0.0983 -0.0838 0.1044  0.0998  32  LEU B CD2   
1456 N  N     . VAL B 33  ? 0.4111 0.5813 0.163  -0.1521 0.1105  0.0871  33  VAL B N     
1457 C  CA    . VAL B 33  ? 0.4077 0.6153 0.1742 -0.1853 0.1187  0.0917  33  VAL B CA    
1458 C  C     . VAL B 33  ? 0.3858 0.6584 0.1907 -0.1802 0.1142  0.0794  33  VAL B C     
1459 O  O     . VAL B 33  ? 0.3632 0.7047 0.1864 -0.1875 0.1245  0.0802  33  VAL B O     
1460 C  CB    . VAL B 33  ? 0.4416 0.5904 0.1888 -0.2166 0.1177  0.101   33  VAL B CB    
1461 C  CG1   . VAL B 33  ? 0.4326 0.6185 0.1899 -0.2583 0.127   0.1048  33  VAL B CG1   
1462 C  CG2   . VAL B 33  ? 0.4764 0.5624 0.1837 -0.2161 0.1232  0.116   33  VAL B CG2   
1463 N  N     . CYS B 34  ? 0.388  0.643  0.2046 -0.1665 0.0995  0.0694  34  CYS B N     
1464 C  CA    . CYS B 34  ? 0.3655 0.6814 0.2159 -0.1593 0.094   0.0599  34  CYS B CA    
1465 C  C     . CYS B 34  ? 0.3661 0.7021 0.2265 -0.115  0.0907  0.049   34  CYS B C     
1466 O  O     . CYS B 34  ? 0.3414 0.7228 0.2265 -0.1024 0.0858  0.0426  34  CYS B O     
1467 C  CB    . CYS B 34  ? 0.3805 0.6718 0.236  -0.1771 0.0815  0.0566  34  CYS B CB    
1468 S  SG    . CYS B 34  ? 0.449  0.6614 0.2886 -0.1508 0.0665  0.0493  34  CYS B SG    
1469 N  N     . ASN B 35  ? 0.3971 0.6981 0.2352 -0.0923 0.0936  0.0471  35  ASN B N     
1470 C  CA    . ASN B 35  ? 0.4127 0.7162 0.2483 -0.053  0.0932  0.0358  35  ASN B CA    
1471 C  C     . ASN B 35  ? 0.4163 0.6967 0.2588 -0.0336 0.0795  0.026   35  ASN B C     
1472 O  O     . ASN B 35  ? 0.4145 0.7078 0.2589 -0.0023 0.0809  0.0171  35  ASN B O     
1473 C  CB    . ASN B 35  ? 0.4193 0.7934 0.2691 -0.0365 0.1069  0.0337  35  ASN B CB    
1474 C  CG    . ASN B 35  ? 0.4841 0.8965 0.333  -0.0597 0.1219  0.0442  35  ASN B CG    
1475 O  OD1   . ASN B 35  ? 0.4958 0.9659 0.3687 -0.0813 0.1267  0.05    35  ASN B OD1   
1476 N  ND2   . ASN B 35  ? 0.5105 0.8953 0.3309 -0.058  0.1298  0.0471  35  ASN B ND2   
1477 N  N     . GLU B 36  ? 0.4207 0.6625 0.2628 -0.0508 0.0679  0.0278  36  GLU B N     
1478 C  CA    . GLU B 36  ? 0.4224 0.6419 0.2694 -0.0353 0.0554  0.0196  36  GLU B CA    
1479 C  C     . GLU B 36  ? 0.4371 0.592  0.2604 -0.0204 0.0497  0.0139  36  GLU B C     
1480 O  O     . GLU B 36  ? 0.4544 0.5753 0.2598 -0.0304 0.0509  0.0188  36  GLU B O     
1481 C  CB    . GLU B 36  ? 0.4615 0.677  0.3195 -0.0619 0.0465  0.0229  36  GLU B CB    
1482 C  CG    . GLU B 36  ? 0.5201 0.8088 0.4055 -0.0755 0.048   0.0251  36  GLU B CG    
1483 C  CD    . GLU B 36  ? 0.6135 0.9491 0.5182 -0.0448 0.0441  0.0189  36  GLU B CD    
1484 O  OE1   . GLU B 36  ? 0.6179 1.0289 0.5447 -0.0413 0.0508  0.0214  36  GLU B OE1   
1485 O  OE2   . GLU B 36  ? 0.6559 0.9538 0.5526 -0.0232 0.0351  0.0125  36  GLU B OE2   
1486 N  N     . ARG B 37  ? 0.4282 0.5671 0.2505 0.0026  0.0432  0.0046  37  ARG B N     
1487 C  CA    . ARG B 37  ? 0.44   0.5214 0.2404 0.0133  0.0378  -0.0019 37  ARG B CA    
1488 C  C     . ARG B 37  ? 0.4309 0.478  0.2338 0.0076  0.0259  -0.0033 37  ARG B C     
1489 O  O     . ARG B 37  ? 0.4322 0.4997 0.2511 0.0056  0.021   -0.0031 37  ARG B O     
1490 C  CB    . ARG B 37  ? 0.4641 0.5401 0.25   0.0427  0.0431  -0.0126 37  ARG B CB    
1491 C  CG    . ARG B 37  ? 0.5025 0.6065 0.2803 0.0491  0.0564  -0.0127 37  ARG B CG    
1492 C  CD    . ARG B 37  ? 0.585  0.669  0.3388 0.077   0.0632  -0.0251 37  ARG B CD    
1493 N  NE    . ARG B 37  ? 0.6455 0.76   0.3907 0.0866  0.0778  -0.0264 37  ARG B NE    
1494 C  CZ    . ARG B 37  ? 0.7179 0.8084 0.4325 0.1054  0.0867  -0.0378 37  ARG B CZ    
1495 N  NH1   . ARG B 37  ? 0.7193 0.8397 0.4256 0.1141  0.1013  -0.0388 37  ARG B NH1   
1496 N  NH2   . ARG B 37  ? 0.7484 0.7819 0.4369 0.1116  0.0819  -0.0485 37  ARG B NH2   
1497 N  N     . PHE B 38  ? 0.4184 0.418  0.2053 0.0041  0.0212  -0.0043 38  PHE B N     
1498 C  CA    . PHE B 38  ? 0.4023 0.3677 0.1892 -0.0006 0.0118  -0.0056 38  PHE B CA    
1499 C  C     . PHE B 38  ? 0.3957 0.3201 0.1647 0.0056  0.0088  -0.0104 38  PHE B C     
1500 O  O     . PHE B 38  ? 0.4135 0.3348 0.1706 0.0053  0.0122  -0.0092 38  PHE B O     
1501 C  CB    . PHE B 38  ? 0.402  0.3613 0.1948 -0.0245 0.0099  0.0033  38  PHE B CB    
1502 C  CG    . PHE B 38  ? 0.4269 0.3713 0.2084 -0.0364 0.0147  0.0128  38  PHE B CG    
1503 C  CD1   . PHE B 38  ? 0.4315 0.4044 0.2134 -0.0447 0.0233  0.0196  38  PHE B CD1   
1504 C  CD2   . PHE B 38  ? 0.4574 0.3612 0.2271 -0.0385 0.0114  0.0164  38  PHE B CD2   
1505 C  CE1   . PHE B 38  ? 0.4528 0.4086 0.2202 -0.0542 0.028   0.0305  38  PHE B CE1   
1506 C  CE2   . PHE B 38  ? 0.4772 0.3678 0.2344 -0.0452 0.0159  0.0276  38  PHE B CE2   
1507 C  CZ    . PHE B 38  ? 0.4701 0.384  0.2246 -0.0531 0.024   0.0349  38  PHE B CZ    
1508 N  N     . THR B 39  ? 0.3736 0.2707 0.1398 0.01    0.0025  -0.0157 39  THR B N     
1509 C  CA    . THR B 39  ? 0.3645 0.2278 0.1156 0.0125  -0.0004 -0.0207 39  THR B CA    
1510 C  C     . THR B 39  ? 0.347  0.1915 0.1004 0.0002  -0.0045 -0.0136 39  THR B C     
1511 O  O     . THR B 39  ? 0.3469 0.1886 0.1092 -0.0075 -0.0064 -0.0092 39  THR B O     
1512 C  CB    . THR B 39  ? 0.3827 0.2255 0.126  0.0249  -0.0027 -0.0302 39  THR B CB    
1513 O  OG1   . THR B 39  ? 0.3879 0.2395 0.1216 0.0407  0.0035  -0.0366 39  THR B OG1   
1514 C  CG2   . THR B 39  ? 0.4021 0.2104 0.1319 0.0213  -0.006  -0.0351 39  THR B CG2   
1515 N  N     . THR B 40  ? 0.3305 0.1646 0.0747 -0.0012 -0.0053 -0.0122 40  THR B N     
1516 C  CA    . THR B 40  ? 0.3184 0.1365 0.064  -0.0067 -0.0079 -0.0047 40  THR B CA    
1517 C  C     . THR B 40  ? 0.3249 0.1312 0.0637 -0.0041 -0.0116 -0.0105 40  THR B C     
1518 O  O     . THR B 40  ? 0.3304 0.1414 0.059  -0.0026 -0.0117 -0.0185 40  THR B O     
1519 C  CB    . THR B 40  ? 0.304  0.1292 0.0481 -0.0111 -0.0047 0.0085  40  THR B CB    
1520 O  OG1   . THR B 40  ? 0.3115 0.1496 0.047  -0.0076 -0.0054 0.0093  40  THR B OG1   
1521 C  CG2   . THR B 40  ? 0.2872 0.1263 0.0455 -0.0182 0.0003  0.0123  40  THR B CG2   
1522 N  N     . PHE B 41  ? 0.3198 0.1112 0.0624 -0.0052 -0.0135 -0.0068 41  PHE B N     
1523 C  CA    . PHE B 41  ? 0.3236 0.1121 0.0629 -0.0051 -0.0161 -0.0105 41  PHE B CA    
1524 C  C     . PHE B 41  ? 0.3205 0.1155 0.0637 -0.0022 -0.016  0.0018  41  PHE B C     
1525 O  O     . PHE B 41  ? 0.3212 0.1018 0.0669 0.0002  -0.013  0.0104  41  PHE B O     
1526 C  CB    . PHE B 41  ? 0.3299 0.0979 0.0735 -0.0055 -0.0167 -0.0162 41  PHE B CB    
1527 C  CG    . PHE B 41  ? 0.3499 0.108  0.0817 -0.004  -0.0167 -0.0284 41  PHE B CG    
1528 C  CD1   . PHE B 41  ? 0.3682 0.1215 0.0849 -0.0064 -0.0162 -0.0383 41  PHE B CD1   
1529 C  CD2   . PHE B 41  ? 0.3619 0.1147 0.0956 0.0002  -0.0167 -0.03   41  PHE B CD2   
1530 C  CE1   . PHE B 41  ? 0.3866 0.1233 0.0916 -0.001  -0.0136 -0.0455 41  PHE B CE1   
1531 C  CE2   . PHE B 41  ? 0.3753 0.1207 0.0996 0.0076  -0.0157 -0.0379 41  PHE B CE2   
1532 C  CZ    . PHE B 41  ? 0.3826 0.1169 0.0928 0.0087  -0.0133 -0.0438 41  PHE B CZ    
1533 N  N     . GLU B 42  ? 0.3151 0.132  0.0561 -0.002  -0.0188 0.0029  42  GLU B N     
1534 C  CA    . GLU B 42  ? 0.3103 0.1419 0.0552 0.0056  -0.0192 0.0162  42  GLU B CA    
1535 C  C     . GLU B 42  ? 0.3078 0.1479 0.059  0.0047  -0.0212 0.0118  42  GLU B C     
1536 O  O     . GLU B 42  ? 0.2983 0.1529 0.0489 -0.0055 -0.0245 0.0012  42  GLU B O     
1537 C  CB    . GLU B 42  ? 0.3137 0.1759 0.0525 0.0065  -0.0222 0.0226  42  GLU B CB    
1538 C  CG    . GLU B 42  ? 0.3429 0.2249 0.085  0.019   -0.0231 0.0389  42  GLU B CG    
1539 C  CD    . GLU B 42  ? 0.3984 0.319  0.1337 0.0201  -0.0283 0.0454  42  GLU B CD    
1540 O  OE1   . GLU B 42  ? 0.4179 0.3445 0.143  0.0101  -0.0298 0.0373  42  GLU B OE1   
1541 O  OE2   . GLU B 42  ? 0.4189 0.365  0.1577 0.0326  -0.0307 0.0592  42  GLU B OE2   
1542 N  N     . VAL B 43  ? 0.3129 0.14   0.0702 0.0137  -0.0175 0.0188  43  VAL B N     
1543 C  CA    . VAL B 43  ? 0.3101 0.1447 0.0747 0.0138  -0.0169 0.0153  43  VAL B CA    
1544 C  C     . VAL B 43  ? 0.3104 0.1641 0.0822 0.0311  -0.014  0.0305  43  VAL B C     
1545 O  O     . VAL B 43  ? 0.3183 0.1538 0.0845 0.0442  -0.0096 0.0428  43  VAL B O     
1546 C  CB    . VAL B 43  ? 0.3223 0.1185 0.0844 0.0109  -0.0129 0.0076  43  VAL B CB    
1547 C  CG1   . VAL B 43  ? 0.3316 0.1346 0.0987 0.0087  -0.0111 0.0029  43  VAL B CG1   
1548 C  CG2   . VAL B 43  ? 0.3281 0.1059 0.0824 0.0004  -0.0152 -0.0041 43  VAL B CG2   
1549 N  N     . ALA B 44  ? 0.3001 0.1887 0.0824 0.0317  -0.0153 0.0303  44  ALA B N     
1550 C  CA    . ALA B 44  ? 0.3017 0.2173 0.0927 0.0529  -0.012  0.046   44  ALA B CA    
1551 C  C     . ALA B 44  ? 0.3216 0.2108 0.1139 0.0667  -0.0021 0.0489  44  ALA B C     
1552 O  O     . ALA B 44  ? 0.3382 0.2079 0.1303 0.0556  0.0004  0.037   44  ALA B O     
1553 C  CB    . ALA B 44  ? 0.2836 0.2645 0.0878 0.0476  -0.0186 0.0462  44  ALA B CB    
1554 N  N     . GLU B 45  ? 0.3292 0.2138 0.1187 0.0923  0.0045  0.0652  45  GLU B N     
1555 C  CA    . GLU B 45  ? 0.3576 0.2152 0.1437 0.1097  0.0163  0.069   45  GLU B CA    
1556 C  C     . GLU B 45  ? 0.3479 0.2672 0.1544 0.1202  0.017   0.0733  45  GLU B C     
1557 O  O     . GLU B 45  ? 0.3282 0.2928 0.143  0.1399  0.0155  0.0885  45  GLU B O     
1558 C  CB    . GLU B 45  ? 0.4065 0.2233 0.1738 0.134   0.0255  0.0851  45  GLU B CB    
1559 C  CG    . GLU B 45  ? 0.4921 0.2819 0.2515 0.1575  0.0398  0.0904  45  GLU B CG    
1560 C  CD    . GLU B 45  ? 0.6041 0.3417 0.3368 0.1823  0.0516  0.106   45  GLU B CD    
1561 O  OE1   . GLU B 45  ? 0.6147 0.3267 0.3327 0.1755  0.0491  0.1111  45  GLU B OE1   
1562 O  OE2   . GLU B 45  ? 0.66   0.3788 0.3834 0.2085  0.065   0.1131  45  GLU B OE2   
1563 N  N     . LEU B 46  ? 0.3562 0.2819 0.1706 0.1061  0.0189  0.0605  46  LEU B N     
1564 C  CA    . LEU B 46  ? 0.3378 0.3293 0.1736 0.109   0.0198  0.0625  46  LEU B CA    
1565 C  C     . LEU B 46  ? 0.3517 0.3326 0.189  0.1251  0.0338  0.0636  46  LEU B C     
1566 O  O     . LEU B 46  ? 0.3793 0.301  0.2006 0.1194  0.0402  0.0543  46  LEU B O     
1567 C  CB    . LEU B 46  ? 0.3217 0.3409 0.1647 0.0732  0.0109  0.0463  46  LEU B CB    
1568 C  CG    . LEU B 46  ? 0.3194 0.347  0.1571 0.0542  -0.0015 0.0415  46  LEU B CG    
1569 C  CD1   . LEU B 46  ? 0.3223 0.3522 0.1566 0.0199  -0.0061 0.0234  46  LEU B CD1   
1570 C  CD2   . LEU B 46  ? 0.2921 0.3825 0.1412 0.0669  -0.0083 0.0556  46  LEU B CD2   
1571 N  N     . VAL B 47  ? 0.331  0.3753 0.1878 0.1448  0.0382  0.0746  47  VAL B N     
1572 C  CA    . VAL B 47  ? 0.3393 0.3927 0.2021 0.1623  0.0528  0.0765  47  VAL B CA    
1573 C  C     . VAL B 47  ? 0.3436 0.4116 0.2139 0.1277  0.0515  0.0593  47  VAL B C     
1574 O  O     . VAL B 47  ? 0.3254 0.4361 0.207  0.0993  0.0402  0.0525  47  VAL B O     
1575 C  CB    . VAL B 47  ? 0.3167 0.4512 0.2026 0.1941  0.056   0.0952  47  VAL B CB    
1576 C  CG1   . VAL B 47  ? 0.2973 0.4767 0.2007 0.2022  0.0683  0.0947  47  VAL B CG1   
1577 C  CG2   . VAL B 47  ? 0.3446 0.447  0.2145 0.2364  0.063   0.1144  47  VAL B CG2   
1578 N  N     . MET B 48  ? 0.3679 0.3958 0.2273 0.1284  0.0637  0.052   48  MET B N     
1579 C  CA    . MET B 48  ? 0.3851 0.4195 0.2463 0.0967  0.0641  0.0373  48  MET B CA    
1580 C  C     . MET B 48  ? 0.3871 0.4721 0.2647 0.1051  0.0776  0.04    48  MET B C     
1581 O  O     . MET B 48  ? 0.3962 0.4708 0.2705 0.1376  0.0919  0.048   48  MET B O     
1582 C  CB    . MET B 48  ? 0.432  0.3822 0.2651 0.0816  0.0646  0.0243  48  MET B CB    
1583 C  CG    . MET B 48  ? 0.4775 0.3927 0.299  0.0669  0.051   0.0197  48  MET B CG    
1584 S  SD    . MET B 48  ? 0.5199 0.4816 0.3524 0.0336  0.0366  0.0124  48  MET B SD    
1585 C  CE    . MET B 48  ? 0.4722 0.4211 0.2959 0.0059  0.0418  -0.0013 48  MET B CE    
1586 N  N     . PRO B 49  ? 0.3763 0.5135 0.2684 0.0739  0.0745  0.0326  49  PRO B N     
1587 C  CA    . PRO B 49  ? 0.3559 0.5504 0.2657 0.0759  0.0877  0.0346  49  PRO B CA    
1588 C  C     . PRO B 49  ? 0.3938 0.5331 0.2842 0.0854  0.1042  0.0296  49  PRO B C     
1589 O  O     . PRO B 49  ? 0.4378 0.495  0.2995 0.0791  0.1032  0.0209  49  PRO B O     
1590 C  CB    . PRO B 49  ? 0.342  0.5769 0.2591 0.0287  0.0803  0.0235  49  PRO B CB    
1591 C  CG    . PRO B 49  ? 0.3783 0.5464 0.2708 0.0053  0.0675  0.0126  49  PRO B CG    
1592 C  CD    . PRO B 49  ? 0.3701 0.5148 0.26   0.034   0.0604  0.0218  49  PRO B CD    
1593 N  N     . ARG B 50  ? 0.3722 0.5632 0.2787 0.1006  0.1194  0.0351  50  ARG B N     
1594 C  CA    . ARG B 50  ? 0.3938 0.5458 0.2828 0.1076  0.137   0.0299  50  ARG B CA    
1595 C  C     . ARG B 50  ? 0.4022 0.5338 0.2781 0.0611  0.1345  0.0151  50  ARG B C     
1596 O  O     . ARG B 50  ? 0.3788 0.5544 0.2679 0.0283  0.1249  0.0115  50  ARG B O     
1597 C  CB    . ARG B 50  ? 0.3828 0.6146 0.2979 0.1346  0.154   0.0407  50  ARG B CB    
1598 C  CG    . ARG B 50  ? 0.4642 0.6546 0.3592 0.1563  0.1757  0.0384  50  ARG B CG    
1599 C  CD    . ARG B 50  ? 0.4872 0.7409 0.4034 0.2032  0.1928  0.0535  50  ARG B CD    
1600 N  NE    . ARG B 50  ? 0.4729 0.846  0.4306 0.1916  0.1952  0.0591  50  ARG B NE    
1601 C  CZ    . ARG B 50  ? 0.4763 0.9303 0.4609 0.2293  0.21    0.073   50  ARG B CZ    
1602 N  NH1   . ARG B 50  ? 0.4871 0.9065 0.4574 0.2841  0.2251  0.083   50  ARG B NH1   
1603 N  NH2   . ARG B 50  ? 0.4371 1.0074 0.4614 0.2127  0.2106  0.0772  50  ARG B NH2   
1604 N  N     . VAL B 51  ? 0.4348 0.4959 0.2804 0.0574  0.1429  0.0066  51  VAL B N     
1605 C  CA    . VAL B 51  ? 0.4574 0.4909 0.2845 0.0178  0.1416  -0.0051 51  VAL B CA    
1606 C  C     . VAL B 51  ? 0.4634 0.5297 0.2927 0.0114  0.1607  -0.006  51  VAL B C     
1607 O  O     . VAL B 51  ? 0.4769 0.529  0.2983 0.0393  0.1762  -0.0035 51  VAL B O     
1608 C  CB    . VAL B 51  ? 0.5011 0.4367 0.2907 0.0125  0.1343  -0.0137 51  VAL B CB    
1609 C  CG1   . VAL B 51  ? 0.5233 0.4268 0.2895 -0.0232 0.134   -0.0233 51  VAL B CG1   
1610 C  CG2   . VAL B 51  ? 0.5088 0.4218 0.2991 0.0154  0.1166  -0.0127 51  VAL B CG2   
1611 N  N     . VAL B 52  ? 0.4523 0.5604 0.2894 -0.0264 0.161   -0.01   52  VAL B N     
1612 C  CA    . VAL B 52  ? 0.4558 0.5927 0.292  -0.0386 0.1797  -0.0112 52  VAL B CA    
1613 C  C     . VAL B 52  ? 0.5095 0.561  0.3025 -0.0642 0.18    -0.0213 52  VAL B C     
1614 O  O     . VAL B 52  ? 0.5282 0.5545 0.307  -0.0978 0.169   -0.0273 52  VAL B O     
1615 C  CB    . VAL B 52  ? 0.423  0.6568 0.2899 -0.069  0.1818  -0.0094 52  VAL B CB    
1616 C  CG1   . VAL B 52  ? 0.4187 0.6886 0.2869 -0.0788 0.2039  -0.0092 52  VAL B CG1   
1617 C  CG2   . VAL B 52  ? 0.3834 0.705  0.2925 -0.0454 0.1757  0.0015  52  VAL B CG2   
1618 N  N     . LYS B 53  ? 0.534  0.5367 0.3022 -0.0465 0.1921  -0.0229 53  LYS B N     
1619 C  CA    . LYS B 53  ? 0.5848 0.5085 0.3096 -0.0662 0.192   -0.0306 53  LYS B CA    
1620 C  C     . LYS B 53  ? 0.6001 0.5436 0.3154 -0.1038 0.2037  -0.0328 53  LYS B C     
1621 O  O     . LYS B 53  ? 0.5684 0.5925 0.3129 -0.1127 0.2146  -0.029  53  LYS B O     
1622 C  CB    . LYS B 53  ? 0.6198 0.4903 0.319  -0.0369 0.2014  -0.0321 53  LYS B CB    
1623 C  CG    . LYS B 53  ? 0.637  0.4783 0.3385 -0.0048 0.1917  -0.0306 53  LYS B CG    
1624 C  CD    . LYS B 53  ? 0.6921 0.4466 0.3533 -0.0047 0.1838  -0.0374 53  LYS B CD    
1625 C  CE    . LYS B 53  ? 0.7181 0.4457 0.3761 -0.022  0.1623  -0.0395 53  LYS B CE    
1626 N  NZ    . LYS B 53  ? 0.775  0.43   0.3986 -0.0198 0.153   -0.0448 53  LYS B NZ    
1627 N  N     . SER B 54  ? 0.6458 0.5178 0.3191 -0.1255 0.202   -0.038  54  SER B N     
1628 C  CA    . SER B 54  ? 0.6696 0.5408 0.3223 -0.1629 0.2139  -0.0396 54  SER B CA    
1629 C  C     . SER B 54  ? 0.6656 0.5932 0.3308 -0.1597 0.2374  -0.0363 54  SER B C     
1630 O  O     . SER B 54  ? 0.6499 0.6255 0.323  -0.1919 0.2485  -0.0356 54  SER B O     
1631 C  CB    . SER B 54  ? 0.7358 0.513  0.3358 -0.172  0.2109  -0.0428 54  SER B CB    
1632 O  OG    . SER B 54  ? 0.7915 0.5186 0.3781 -0.1749 0.191   -0.0453 54  SER B OG    
1633 N  N     . ASN B 55  ? 0.6791 0.6004 0.3442 -0.1217 0.2462  -0.0348 55  ASN B N     
1634 C  CA    . ASN B 55  ? 0.6733 0.6439 0.3477 -0.11   0.2707  -0.0319 55  ASN B CA    
1635 C  C     . ASN B 55  ? 0.6335 0.6996 0.3599 -0.0839 0.2769  -0.0252 55  ASN B C     
1636 O  O     . ASN B 55  ? 0.6283 0.723  0.3621 -0.0543 0.2955  -0.0222 55  ASN B O     
1637 C  CB    . ASN B 55  ? 0.727  0.6312 0.3637 -0.0841 0.2797  -0.0351 55  ASN B CB    
1638 C  CG    . ASN B 55  ? 0.7898 0.6552 0.4251 -0.0454 0.2692  -0.0366 55  ASN B CG    
1639 O  OD1   . ASN B 55  ? 0.7995 0.6716 0.4566 -0.0381 0.2519  -0.0349 55  ASN B OD1   
1640 N  ND2   . ASN B 55  ? 0.8262 0.648  0.4323 -0.0218 0.2806  -0.0402 55  ASN B ND2   
1641 N  N     . ASP B 56  ? 0.6084 0.7219 0.3678 -0.0922 0.2616  -0.0225 56  ASP B N     
1642 C  CA    . ASP B 56  ? 0.5684 0.7796 0.3783 -0.0698 0.263   -0.0142 56  ASP B CA    
1643 C  C     . ASP B 56  ? 0.5678 0.7686 0.3847 -0.0128 0.2665  -0.009  56  ASP B C     
1644 O  O     . ASP B 56  ? 0.5289 0.8096 0.384  0.0147  0.2718  0.0003  56  ASP B O     
1645 C  CB    . ASP B 56  ? 0.5553 0.8671 0.3933 -0.0874 0.2823  -0.01   56  ASP B CB    
1646 C  CG    . ASP B 56  ? 0.6367 0.9551 0.4651 -0.1485 0.2781  -0.0155 56  ASP B CG    
1647 O  OD1   . ASP B 56  ? 0.6441 0.9749 0.4836 -0.1712 0.2594  -0.0173 56  ASP B OD1   
1648 O  OD2   . ASP B 56  ? 0.6878 0.9892 0.4913 -0.1743 0.2941  -0.0184 56  ASP B OD2   
1649 N  N     . VAL B 57  ? 0.6072 0.7097 0.3856 0.0042  0.2625  -0.0144 57  VAL B N     
1650 C  CA    . VAL B 57  ? 0.615  0.6904 0.3905 0.0529  0.2657  -0.011  57  VAL B CA    
1651 C  C     . VAL B 57  ? 0.597  0.6759 0.3918 0.0609  0.244   -0.0067 57  VAL B C     
1652 O  O     . VAL B 57  ? 0.6166 0.6545 0.3997 0.034   0.2247  -0.0119 57  VAL B O     
1653 C  CB    . VAL B 57  ? 0.6763 0.6467 0.4005 0.0611  0.2686  -0.0199 57  VAL B CB    
1654 C  CG1   . VAL B 57  ? 0.7018 0.6268 0.4157 0.1024  0.2675  -0.0185 57  VAL B CG1   
1655 C  CG2   . VAL B 57  ? 0.6895 0.6588 0.3926 0.0605  0.2927  -0.0233 57  VAL B CG2   
1656 N  N     . ARG B 58  ? 0.556  0.6835 0.3782 0.0993  0.248   0.0038  58  ARG B N     
1657 C  CA    . ARG B 58  ? 0.5394 0.6687 0.3766 0.1097  0.2288  0.0094  58  ARG B CA    
1658 C  C     . ARG B 58  ? 0.5702 0.6026 0.3727 0.1357  0.2264  0.0066  58  ARG B C     
1659 O  O     . ARG B 58  ? 0.5956 0.5939 0.3771 0.1658  0.2443  0.0064  58  ARG B O     
1660 C  CB    . ARG B 58  ? 0.5055 0.7362 0.3871 0.1384  0.2328  0.0241  58  ARG B CB    
1661 C  CG    . ARG B 58  ? 0.498  0.825  0.4171 0.1031  0.2223  0.0264  58  ARG B CG    
1662 C  CD    . ARG B 58  ? 0.52   0.8967 0.4462 0.0731  0.237   0.022   58  ARG B CD    
1663 N  NE    . ARG B 58  ? 0.5167 0.9971 0.4805 0.0407  0.2293  0.025   58  ARG B NE    
1664 C  CZ    . ARG B 58  ? 0.5271 1.0539 0.4972 -0.0013 0.2371  0.02    58  ARG B CZ    
1665 N  NH1   . ARG B 58  ? 0.5365 1.0144 0.4776 -0.014  0.2531  0.0128  58  ARG B NH1   
1666 N  NH2   . ARG B 58  ? 0.4949 1.1158 0.4971 -0.0339 0.229   0.0218  58  ARG B NH2   
1667 N  N     . GLU B 59  ? 0.5698 0.5554 0.3626 0.1212  0.2055  0.0033  59  GLU B N     
1668 C  CA    . GLU B 59  ? 0.5983 0.4975 0.3594 0.1391  0.2016  0.0005  59  GLU B CA    
1669 C  C     . GLU B 59  ? 0.5798 0.4771 0.353  0.1376  0.1814  0.0052  59  GLU B C     
1670 O  O     . GLU B 59  ? 0.5644 0.5115 0.3622 0.1144  0.1681  0.0065  59  GLU B O     
1671 C  CB    . GLU B 59  ? 0.6638 0.4835 0.3842 0.1166  0.1999  -0.013  59  GLU B CB    
1672 C  CG    . GLU B 59  ? 0.7215 0.5282 0.4393 0.0771  0.1805  -0.0193 59  GLU B CG    
1673 C  CD    . GLU B 59  ? 0.8335 0.5595 0.5105 0.0628  0.1749  -0.0297 59  GLU B CD    
1674 O  OE1   . GLU B 59  ? 0.861  0.5476 0.51   0.0748  0.1881  -0.0342 59  GLU B OE1   
1675 O  OE2   . GLU B 59  ? 0.8813 0.5853 0.5531 0.0403  0.1574  -0.0333 59  GLU B OE2   
1676 N  N     . PRO B 60  ? 0.5773 0.4203 0.3326 0.1611  0.1798  0.0081  60  PRO B N     
1677 C  CA    . PRO B 60  ? 0.549  0.3946 0.3158 0.1592  0.1619  0.0137  60  PRO B CA    
1678 C  C     . PRO B 60  ? 0.5315 0.3476 0.2906 0.1215  0.1425  0.0038  60  PRO B C     
1679 O  O     . PRO B 60  ? 0.5574 0.3287 0.2929 0.1021  0.1424  -0.0071 60  PRO B O     
1680 C  CB    . PRO B 60  ? 0.5951 0.3757 0.335  0.1896  0.1688  0.0177  60  PRO B CB    
1681 C  CG    . PRO B 60  ? 0.6398 0.3579 0.3436 0.1899  0.1827  0.0068  60  PRO B CG    
1682 C  CD    . PRO B 60  ? 0.6015 0.3753 0.3212 0.1877  0.1952  0.0058  60  PRO B CD    
1683 N  N     . PHE B 61  ? 0.4906 0.3315 0.2673 0.1131  0.1264  0.008   61  PHE B N     
1684 C  CA    . PHE B 61  ? 0.4761 0.2892 0.2446 0.0821  0.1095  -0.0007 61  PHE B CA    
1685 C  C     . PHE B 61  ? 0.5073 0.2431 0.2458 0.0852  0.1065  -0.0056 61  PHE B C     
1686 O  O     . PHE B 61  ? 0.5248 0.2399 0.2578 0.1061  0.1084  0.0009  61  PHE B O     
1687 C  CB    . PHE B 61  ? 0.432  0.2884 0.2229 0.075   0.0951  0.0046  61  PHE B CB    
1688 C  CG    . PHE B 61  ? 0.4312 0.2575 0.2119 0.0476  0.0796  -0.0042 61  PHE B CG    
1689 C  CD1   . PHE B 61  ? 0.4303 0.2659 0.2092 0.0181  0.0758  -0.0126 61  PHE B CD1   
1690 C  CD2   . PHE B 61  ? 0.4455 0.2345 0.2165 0.052   0.0704  -0.0033 61  PHE B CD2   
1691 C  CE1   . PHE B 61  ? 0.4467 0.251  0.2128 -0.0017 0.0636  -0.0199 61  PHE B CE1   
1692 C  CE2   . PHE B 61  ? 0.4574 0.2243 0.2202 0.0308  0.0578  -0.0107 61  PHE B CE2   
1693 C  CZ    . PHE B 61  ? 0.4523 0.2259 0.2123 0.0063  0.0546  -0.0188 61  PHE B CZ    
1694 N  N     . ASN B 62  ? 0.5115 0.2049 0.2278 0.0651  0.1033  -0.0164 62  ASN B N     
1695 C  CA    . ASN B 62  ? 0.5347 0.1639 0.2234 0.0635  0.0989  -0.022  62  ASN B CA    
1696 C  C     . ASN B 62  ? 0.5258 0.1455 0.2141 0.0415  0.0813  -0.0266 62  ASN B C     
1697 O  O     . ASN B 62  ? 0.5315 0.1442 0.2112 0.0238  0.0773  -0.0329 62  ASN B O     
1698 C  CB    . ASN B 62  ? 0.5811 0.1713 0.2415 0.0613  0.1088  -0.03   62  ASN B CB    
1699 C  CG    . ASN B 62  ? 0.6582 0.1863 0.2877 0.0617  0.107   -0.0356 62  ASN B CG    
1700 O  OD1   . ASN B 62  ? 0.688  0.1999 0.3157 0.0522  0.0937  -0.0366 62  ASN B OD1   
1701 N  ND2   . ASN B 62  ? 0.6764 0.1705 0.2796 0.0711  0.1212  -0.0401 62  ASN B ND2   
1702 N  N     . GLU B 63  ? 0.5111 0.1272 0.2055 0.0445  0.0722  -0.0227 63  GLU B N     
1703 C  CA    . GLU B 63  ? 0.5015 0.1118 0.1965 0.0282  0.0571  -0.0262 63  GLU B CA    
1704 C  C     . GLU B 63  ? 0.5068 0.0756 0.1775 0.0161  0.0523  -0.0348 63  GLU B C     
1705 O  O     . GLU B 63  ? 0.5129 0.0824 0.1822 0.0031  0.0428  -0.0385 63  GLU B O     
1706 C  CB    . GLU B 63  ? 0.5302 0.1392 0.2316 0.036   0.0519  -0.0199 63  GLU B CB    
1707 C  CG    . GLU B 63  ? 0.5908 0.2129 0.3011 0.0232  0.0381  -0.0212 63  GLU B CG    
1708 C  CD    . GLU B 63  ? 0.6551 0.275  0.3693 0.0296  0.0343  -0.0146 63  GLU B CD    
1709 O  OE1   . GLU B 63  ? 0.6719 0.3247 0.4019 0.0381  0.0342  -0.0065 63  GLU B OE1   
1710 O  OE2   . GLU B 63  ? 0.6712 0.2587 0.3714 0.0249  0.0317  -0.017  63  GLU B OE2   
1711 N  N     . GLU B 64  ? 0.4867 0.055  0.1393 0.018   0.0582  -0.0261 64  GLU B N     
1712 C  CA    . GLU B 64  ? 0.4897 0.0525 0.122  0.0057  0.052   -0.0239 64  GLU B CA    
1713 C  C     . GLU B 64  ? 0.514  0.0585 0.1345 -0.0005 0.0548  -0.0318 64  GLU B C     
1714 O  O     . GLU B 64  ? 0.5257 0.0611 0.1338 -0.0096 0.0459  -0.0333 64  GLU B O     
1715 C  CB    . GLU B 64  ? 0.5158 0.0487 0.125  0.0084  0.0577  -0.0246 64  GLU B CB    
1716 C  CG    . GLU B 64  ? 0.545  0.0523 0.1307 -0.0044 0.0499  -0.0302 64  GLU B CG    
1717 C  CD    . GLU B 64  ? 0.6216 0.0731 0.2085 -0.0138 0.0337  -0.0548 64  GLU B CD    
1718 O  OE1   . GLU B 64  ? 0.6222 0.0891 0.2301 -0.0111 0.0297  -0.0511 64  GLU B OE1   
1719 O  OE2   . GLU B 64  ? 0.6393 0.0805 0.2109 -0.0239 0.0247  -0.0608 64  GLU B OE2   
1720 N  N     . LYS B 65  ? 0.5034 0.0581 0.1297 0.0043  0.0672  -0.0314 65  LYS B N     
1721 C  CA    . LYS B 65  ? 0.5018 0.0582 0.1196 -0.0054 0.0711  -0.0318 65  LYS B CA    
1722 C  C     . LYS B 65  ? 0.513  0.0659 0.1355 -0.0166 0.0613  -0.0396 65  LYS B C     
1723 O  O     . LYS B 65  ? 0.5524 0.0716 0.1523 -0.0254 0.0571  -0.0481 65  LYS B O     
1724 C  CB    . LYS B 65  ? 0.5055 0.065  0.1294 0.002   0.0878  -0.0398 65  LYS B CB    
1725 C  CG    . LYS B 65  ? 0.5354 0.0692 0.1398 0.0151  0.1025  -0.0442 65  LYS B CG    
1726 C  CD    . LYS B 65  ? 0.5448 0.1022 0.1546 0.0203  0.12    -0.0477 65  LYS B CD    
1727 C  CE    . LYS B 65  ? 0.6002 0.1338 0.1888 0.0369  0.1369  -0.0505 65  LYS B CE    
1728 N  NZ    . LYS B 65  ? 0.6028 0.1598 0.1895 0.0357  0.1535  -0.0505 65  LYS B NZ    
1729 N  N     . LEU B 66  ? 0.4853 0.0661 0.1322 -0.0157 0.0575  -0.0375 66  LEU B N     
1730 C  CA    . LEU B 66  ? 0.4859 0.0705 0.1369 -0.0268 0.0491  -0.0408 66  LEU B CA    
1731 C  C     . LEU B 66  ? 0.5089 0.0719 0.1472 -0.0271 0.0365  -0.0408 66  LEU B C     
1732 O  O     . LEU B 66  ? 0.5207 0.0731 0.1447 -0.0341 0.0331  -0.0402 66  LEU B O     
1733 C  CB    . LEU B 66  ? 0.4552 0.0719 0.1324 -0.024  0.0473  -0.0407 66  LEU B CB    
1734 C  CG    . LEU B 66  ? 0.4574 0.0797 0.1375 -0.0355 0.0384  -0.044  66  LEU B CG    
1735 C  CD1   . LEU B 66  ? 0.4621 0.0831 0.1307 -0.0534 0.0429  -0.0478 66  LEU B CD1   
1736 C  CD2   . LEU B 66  ? 0.4434 0.1072 0.1486 -0.0315 0.0357  -0.0396 66  LEU B CD2   
1737 N  N     . ARG B 67  ? 0.5088 0.0701 0.1516 -0.0189 0.0309  -0.0392 67  ARG B N     
1738 C  CA    . ARG B 67  ? 0.5222 0.0716 0.1582 -0.019  0.0191  -0.0402 67  ARG B CA    
1739 C  C     . ARG B 67  ? 0.56   0.0752 0.1689 -0.0217 0.0159  -0.0458 67  ARG B C     
1740 O  O     . ARG B 67  ? 0.5726 0.0773 0.1724 -0.022  0.0079  -0.0475 67  ARG B O     
1741 C  CB    . ARG B 67  ? 0.5307 0.0712 0.1738 -0.0144 0.0164  -0.0432 67  ARG B CB    
1742 C  CG    . ARG B 67  ? 0.5692 0.0944 0.2068 -0.0175 0.0047  -0.0484 67  ARG B CG    
1743 C  CD    . ARG B 67  ? 0.6065 0.1439 0.2593 -0.0164 0.0023  -0.0452 67  ARG B CD    
1744 N  NE    . ARG B 67  ? 0.6429 0.1693 0.2947 -0.0121 0.0121  -0.043  67  ARG B NE    
1745 C  CZ    . ARG B 67  ? 0.6386 0.1789 0.3052 -0.0046 0.0167  -0.0369 67  ARG B CZ    
1746 N  NH1   . ARG B 67  ? 0.6147 0.1825 0.2988 -0.0041 0.0116  -0.0336 67  ARG B NH1   
1747 N  NH2   . ARG B 67  ? 0.6353 0.1604 0.2963 0.0039  0.0271  -0.0337 67  ARG B NH2   
1748 N  N     . SER B 68  ? 0.5708 0.0744 0.1651 -0.0217 0.0225  -0.0459 68  SER B N     
1749 C  CA    . SER B 68  ? 0.5984 0.076  0.1645 -0.0246 0.0195  -0.0491 68  SER B CA    
1750 C  C     . SER B 68  ? 0.5869 0.0694 0.1405 -0.0266 0.0203  -0.0405 68  SER B C     
1751 O  O     . SER B 68  ? 0.6114 0.0714 0.144  -0.0253 0.0119  -0.0431 68  SER B O     
1752 C  CB    . SER B 68  ? 0.6583 0.1018 0.2045 -0.0252 0.0297  -0.0602 68  SER B CB    
1753 O  OG    . SER B 68  ? 0.7165 0.1594 0.2715 -0.0217 0.0331  -0.0617 68  SER B OG    
1754 N  N     . GLY B 69  ? 0.5526 0.0619 0.1162 -0.0304 0.0308  -0.031  69  GLY B N     
1755 C  CA    . GLY B 69  ? 0.5558 0.057  0.1012 -0.0362 0.0344  -0.0259 69  GLY B CA    
1756 C  C     . GLY B 69  ? 0.5529 0.0555 0.095  -0.0326 0.025   -0.0215 69  GLY B C     
1757 O  O     . GLY B 69  ? 0.5725 0.0515 0.0868 -0.0307 0.0229  -0.0183 69  GLY B O     
1758 N  N     . MET B 70  ? 0.5262 0.0573 0.0945 -0.0294 0.0198  -0.0198 70  MET B N     
1759 C  CA    . MET B 70  ? 0.5176 0.0544 0.0855 -0.0239 0.0121  -0.0158 70  MET B CA    
1760 C  C     . MET B 70  ? 0.5051 0.05   0.0668 -0.0126 0.0005  -0.0083 70  MET B C     
1761 O  O     . MET B 70  ? 0.5214 0.046  0.0615 -0.0055 -0.0036 -0.0071 70  MET B O     
1762 C  CB    . MET B 70  ? 0.5152 0.0633 0.1097 -0.025  0.01    -0.0237 70  MET B CB    
1763 C  CG    . MET B 70  ? 0.5443 0.0755 0.1452 -0.0383 0.0187  -0.0383 70  MET B CG    
1764 S  SD    . MET B 70  ? 0.5676 0.1014 0.1923 -0.0404 0.0139  -0.053  70  MET B SD    
1765 C  CE    . MET B 70  ? 0.5715 0.094  0.1805 -0.038  0.0096  -0.0509 70  MET B CE    
1766 N  N     . LEU B 71  ? 0.4794 0.0517 0.0572 -0.0111 -0.0043 -0.0029 71  LEU B N     
1767 C  CA    . LEU B 71  ? 0.481  0.0508 0.0552 -0.0048 -0.0163 -0.0021 71  LEU B CA    
1768 C  C     . LEU B 71  ? 0.5227 0.0483 0.0623 -0.0014 -0.0199 -0.0083 71  LEU B C     
1769 O  O     . LEU B 71  ? 0.5201 0.0451 0.0537 0.0084  -0.0307 -0.0056 71  LEU B O     
1770 C  CB    . LEU B 71  ? 0.4612 0.0512 0.053  -0.0095 -0.0181 -0.0003 71  LEU B CB    
1771 C  CG    . LEU B 71  ? 0.4562 0.0572 0.0719 -0.0106 -0.019  -0.008  71  LEU B CG    
1772 C  CD1   . LEU B 71  ? 0.4684 0.0597 0.0865 -0.0179 -0.0193 -0.016  71  LEU B CD1   
1773 C  CD2   . LEU B 71  ? 0.4478 0.0578 0.0727 -0.0038 -0.0281 -0.0083 71  LEU B CD2   
1774 N  N     . ARG B 72  ? 0.555  0.0503 0.0729 -0.0081 -0.0103 -0.0135 72  ARG B N     
1775 C  CA    . ARG B 72  ? 0.5924 0.0493 0.0735 -0.0055 -0.0113 -0.0156 72  ARG B CA    
1776 C  C     . ARG B 72  ? 0.6233 0.0486 0.0809 0.0042  -0.0119 -0.0169 72  ARG B C     
1777 O  O     . ARG B 72  ? 0.6428 0.0478 0.0774 0.0171  -0.0206 -0.0166 72  ARG B O     
1778 C  CB    . ARG B 72  ? 0.6333 0.0549 0.0959 -0.0166 0.0025  -0.0264 72  ARG B CB    
1779 C  CG    . ARG B 72  ? 0.6981 0.083  0.1392 -0.0215 0.0006  -0.0477 72  ARG B CG    
1780 C  CD    . ARG B 72  ? 0.7384 0.1234 0.1886 -0.0298 0.0148  -0.0535 72  ARG B CD    
1781 N  NE    . ARG B 72  ? 0.7862 0.1504 0.2116 -0.0346 0.0279  -0.0526 72  ARG B NE    
1782 C  CZ    . ARG B 72  ? 0.8017 0.1535 0.2053 -0.0378 0.0343  -0.0565 72  ARG B CZ    
1783 N  NH1   . ARG B 72  ? 0.8065 0.1596 0.2064 -0.0381 0.0283  -0.0626 72  ARG B NH1   
1784 N  NH2   . ARG B 72  ? 0.795  0.1313 0.1777 -0.0426 0.0479  -0.055  72  ARG B NH2   
1785 N  N     . ALA B 73  ? 0.6322 0.0496 0.0934 -0.0011 -0.0022 -0.0189 73  ALA B N     
1786 C  CA    . ALA B 73  ? 0.6713 0.0471 0.1063 0.006   0.0009  -0.0205 73  ALA B CA    
1787 C  C     . ALA B 73  ? 0.6936 0.0522 0.1345 0.0255  -0.0094 -0.0275 73  ALA B C     
1788 O  O     . ALA B 73  ? 0.7152 0.0479 0.1285 0.0414  -0.0096 -0.021  73  ALA B O     
1789 C  CB    . ALA B 73  ? 0.6717 0.0473 0.1117 -0.0101 0.0139  -0.022  73  ALA B CB    
1790 N  N     . LEU B 74  ? 0.6813 0.0787 0.1582 0.0254  -0.0167 -0.0323 74  LEU B N     
1791 C  CA    . LEU B 74  ? 0.6829 0.1049 0.1745 0.0417  -0.0254 -0.0301 74  LEU B CA    
1792 C  C     . LEU B 74  ? 0.6861 0.1396 0.1816 0.0524  -0.0393 -0.0257 74  LEU B C     
1793 O  O     . LEU B 74  ? 0.673  0.1665 0.1944 0.0564  -0.0472 -0.0262 74  LEU B O     
1794 C  CB    . LEU B 74  ? 0.6595 0.1113 0.1867 0.0325  -0.0246 -0.0361 74  LEU B CB    
1795 C  CG    . LEU B 74  ? 0.6847 0.1192 0.2122 0.0217  -0.0139 -0.0407 74  LEU B CG    
1796 C  CD1   . LEU B 74  ? 0.6683 0.1359 0.2297 0.0105  -0.0138 -0.045  74  LEU B CD1   
1797 C  CD2   . LEU B 74  ? 0.7087 0.1243 0.2212 0.0346  -0.0114 -0.0401 74  LEU B CD2   
1798 N  N     . GLU B 75  ? 0.6966 0.1357 0.1658 0.0549  -0.0423 -0.0214 75  GLU B N     
1799 C  CA    . GLU B 75  ? 0.69   0.1632 0.1596 0.0628  -0.0568 -0.0174 75  GLU B CA    
1800 C  C     . GLU B 75  ? 0.698  0.1806 0.1581 0.0917  -0.0632 -0.0075 75  GLU B C     
1801 O  O     . GLU B 75  ? 0.721  0.1605 0.1505 0.1068  -0.0557 -0.0014 75  GLU B O     
1802 C  CB    . GLU B 75  ? 0.7189 0.1737 0.1597 0.0557  -0.0579 -0.0162 75  GLU B CB    
1803 C  CG    . GLU B 75  ? 0.7547 0.2183 0.2074 0.0316  -0.0564 -0.026  75  GLU B CG    
1804 C  CD    . GLU B 75  ? 0.8032 0.3126 0.2757 0.0243  -0.0697 -0.0296 75  GLU B CD    
1805 O  OE1   . GLU B 75  ? 0.8048 0.3201 0.2948 0.0064  -0.0661 -0.0381 75  GLU B OE1   
1806 O  OE2   . GLU B 75  ? 0.8273 0.3673 0.296  0.0361  -0.0831 -0.0235 75  GLU B OE2   
1807 N  N     . LYS B 76  ? 0.6755 0.214  0.1612 0.0996  -0.0752 -0.0058 76  LYS B N     
1808 C  CA    . LYS B 76  ? 0.6773 0.2418 0.1622 0.1307  -0.0817 0.0041  76  LYS B CA    
1809 C  C     . LYS B 76  ? 0.6982 0.234  0.1799 0.1482  -0.0697 0.0049  76  LYS B C     
1810 O  O     . LYS B 76  ? 0.7085 0.247  0.1777 0.18    -0.0704 0.014   76  LYS B O     
1811 C  CB    . LYS B 76  ? 0.713  0.2694 0.163  0.1521  -0.0887 0.016   76  LYS B CB    
1812 C  CG    . LYS B 76  ? 0.7507 0.349  0.2024 0.1393  -0.104  0.0161  76  LYS B CG    
1813 C  CD    . LYS B 76  ? 0.8131 0.4048 0.2266 0.1655  -0.1115 0.0305  76  LYS B CD    
1814 C  CE    . LYS B 76  ? 0.8387 0.4761 0.2494 0.153   -0.1284 0.0307  76  LYS B CE    
1815 N  NZ    . LYS B 76  ? 0.8699 0.5005 0.241  0.1804  -0.1357 0.0463  76  LYS B NZ    
1816 N  N     . ARG B 77  ? 0.6963 0.2063 0.1876 0.1285  -0.0585 -0.0047 77  ARG B N     
1817 C  CA    . ARG B 77  ? 0.7007 0.1798 0.1851 0.1374  -0.0467 -0.007  77  ARG B CA    
1818 C  C     . ARG B 77  ? 0.6706 0.1955 0.1924 0.1361  -0.0484 -0.0117 77  ARG B C     
1819 O  O     . ARG B 77  ? 0.6511 0.2165 0.2045 0.1164  -0.0545 -0.0161 77  ARG B O     
1820 C  CB    . ARG B 77  ? 0.7373 0.161  0.2033 0.1154  -0.0336 -0.0139 77  ARG B CB    
1821 C  CG    . ARG B 77  ? 0.8074 0.1788 0.2304 0.1168  -0.0284 -0.0084 77  ARG B CG    
1822 C  CD    . ARG B 77  ? 0.8847 0.2297 0.2712 0.151   -0.0286 0.0034  77  ARG B CD    
1823 N  NE    . ARG B 77  ? 0.9758 0.2833 0.3437 0.1659  -0.0173 0.0023  77  ARG B NE    
1824 C  CZ    . ARG B 77  ? 1.0317 0.3343 0.3827 0.2025  -0.0172 0.0109  77  ARG B CZ    
1825 N  NH1   . ARG B 77  ? 1.0459 0.3049 0.3743 0.2141  -0.0043 0.0079  77  ARG B NH1   
1826 N  NH2   . ARG B 77  ? 1.0306 0.3741 0.386  0.2282  -0.0298 0.0225  77  ARG B NH2   
1827 N  N     . PRO B 78  ? 0.6574 0.1747 0.1723 0.1587  -0.0422 -0.0102 78  PRO B N     
1828 C  CA    . PRO B 78  ? 0.6229 0.1865 0.171  0.1595  -0.0431 -0.0136 78  PRO B CA    
1829 C  C     . PRO B 78  ? 0.6191 0.1702 0.18   0.1348  -0.0353 -0.0239 78  PRO B C     
1830 O  O     . PRO B 78  ? 0.6265 0.1612 0.1804 0.1416  -0.0266 -0.0279 78  PRO B O     
1831 C  CB    . PRO B 78  ? 0.641  0.1983 0.1713 0.1968  -0.038  -0.0077 78  PRO B CB    
1832 C  CG    . PRO B 78  ? 0.6899 0.1707 0.1714 0.2068  -0.0282 -0.0057 78  PRO B CG    
1833 C  CD    . PRO B 78  ? 0.6807 0.1429 0.1527 0.1855  -0.0327 -0.005  78  PRO B CD    
1834 N  N     . VAL B 79  ? 0.5991 0.1579 0.1761 0.1072  -0.0384 -0.0279 79  VAL B N     
1835 C  CA    . VAL B 79  ? 0.5838 0.139  0.1752 0.0843  -0.033  -0.0353 79  VAL B CA    
1836 C  C     . VAL B 79  ? 0.5632 0.1658 0.1879 0.0702  -0.0407 -0.0352 79  VAL B C     
1837 O  O     . VAL B 79  ? 0.5598 0.17   0.1862 0.0621  -0.0468 -0.0336 79  VAL B O     
1838 C  CB    . VAL B 79  ? 0.5993 0.1116 0.1715 0.0678  -0.027  -0.0386 79  VAL B CB    
1839 C  CG1   . VAL B 79  ? 0.5924 0.1127 0.1834 0.0457  -0.023  -0.0443 79  VAL B CG1   
1840 C  CG2   . VAL B 79  ? 0.6319 0.0908 0.1653 0.0775  -0.018  -0.0388 79  VAL B CG2   
1841 N  N     . SER B 80  ? 0.5525 0.1844 0.1994 0.0672  -0.0397 -0.0367 80  SER B N     
1842 C  CA    . SER B 80  ? 0.5334 0.2039 0.207  0.0522  -0.045  -0.0359 80  SER B CA    
1843 C  C     . SER B 80  ? 0.5343 0.1871 0.2113 0.0314  -0.042  -0.0388 80  SER B C     
1844 O  O     . SER B 80  ? 0.5436 0.166  0.2091 0.0282  -0.0358 -0.0416 80  SER B O     
1845 C  CB    . SER B 80  ? 0.5311 0.2366 0.2239 0.0559  -0.0434 -0.0352 80  SER B CB    
1846 O  OG    . SER B 80  ? 0.5758 0.2664 0.2691 0.0496  -0.036  -0.0388 80  SER B OG    
1847 N  N     . SER B 81  ? 0.523  0.1945 0.2136 0.0171  -0.0455 -0.0381 81  SER B N     
1848 C  CA    . SER B 81  ? 0.5321 0.1856 0.224  0.0021  -0.0409 -0.0396 81  SER B CA    
1849 C  C     . SER B 81  ? 0.5151 0.1675 0.2159 0.001   -0.0342 -0.0394 81  SER B C     
1850 O  O     . SER B 81  ? 0.5167 0.1528 0.2156 -0.0042 -0.029  -0.0398 81  SER B O     
1851 C  CB    . SER B 81  ? 0.5598 0.2254 0.2577 -0.0128 -0.0442 -0.0392 81  SER B CB    
1852 O  OG    . SER B 81  ? 0.5922 0.2947 0.305  -0.0159 -0.0483 -0.0369 81  SER B OG    
1853 N  N     . ASP B 82  ? 0.4976 0.1712 0.2074 0.0071  -0.0341 -0.0383 82  ASP B N     
1854 C  CA    . ASP B 82  ? 0.4881 0.165  0.2033 0.0063  -0.0292 -0.0383 82  ASP B CA    
1855 C  C     . ASP B 82  ? 0.4798 0.1331 0.1802 0.0093  -0.0252 -0.0428 82  ASP B C     
1856 O  O     . ASP B 82  ? 0.4786 0.1291 0.1811 0.0023  -0.0217 -0.0431 82  ASP B O     
1857 C  CB    . ASP B 82  ? 0.5158 0.2212 0.2403 0.0121  -0.0295 -0.0369 82  ASP B CB    
1858 C  CG    . ASP B 82  ? 0.593  0.3239 0.3321 0.0026  -0.0318 -0.0322 82  ASP B CG    
1859 O  OD1   . ASP B 82  ? 0.6079 0.3341 0.3511 -0.0081 -0.029  -0.0289 82  ASP B OD1   
1860 O  OD2   . ASP B 82  ? 0.6221 0.3781 0.3671 0.0057  -0.0359 -0.0314 82  ASP B OD2   
1861 N  N     . ASP B 83  ? 0.4746 0.111  0.1582 0.0192  -0.0254 -0.0455 83  ASP B N     
1862 C  CA    . ASP B 83  ? 0.4897 0.0946 0.152  0.0185  -0.0202 -0.0503 83  ASP B CA    
1863 C  C     . ASP B 83  ? 0.4907 0.0843 0.1513 0.0061  -0.0178 -0.0492 83  ASP B C     
1864 O  O     . ASP B 83  ? 0.4921 0.0836 0.1483 -0.0031 -0.0129 -0.049  83  ASP B O     
1865 C  CB    . ASP B 83  ? 0.5307 0.1117 0.1701 0.0335  -0.0201 -0.0507 83  ASP B CB    
1866 C  CG    . ASP B 83  ? 0.6015 0.1943 0.2391 0.0509  -0.0196 -0.0504 83  ASP B CG    
1867 O  OD1   . ASP B 83  ? 0.6199 0.2214 0.2611 0.0486  -0.016  -0.0538 83  ASP B OD1   
1868 O  OD2   . ASP B 83  ? 0.6193 0.2151 0.2509 0.0681  -0.0227 -0.0465 83  ASP B OD2   
1869 N  N     . VAL B 84  ? 0.481  0.0816 0.1469 0.0053  -0.0207 -0.0428 84  VAL B N     
1870 C  CA    . VAL B 84  ? 0.4783 0.0796 0.1435 -0.003  -0.0167 -0.0373 84  VAL B CA    
1871 C  C     . VAL B 84  ? 0.4648 0.0828 0.1475 -0.0095 -0.0135 -0.037  84  VAL B C     
1872 O  O     . VAL B 84  ? 0.4774 0.0846 0.157  -0.0164 -0.0084 -0.043  84  VAL B O     
1873 C  CB    . VAL B 84  ? 0.4929 0.0806 0.1516 -0.0022 -0.0203 -0.0392 84  VAL B CB    
1874 C  CG1   . VAL B 84  ? 0.5061 0.081  0.1618 -0.0096 -0.0143 -0.041  84  VAL B CG1   
1875 C  CG2   . VAL B 84  ? 0.5122 0.0796 0.1494 0.0062  -0.0239 -0.0401 84  VAL B CG2   
1876 N  N     . GLU B 85  ? 0.4315 0.0807 0.1319 -0.0072 -0.0159 -0.028  85  GLU B N     
1877 C  CA    . GLU B 85  ? 0.4063 0.0788 0.1211 -0.0088 -0.0125 -0.0213 85  GLU B CA    
1878 C  C     . GLU B 85  ? 0.3887 0.0795 0.1104 -0.0108 -0.0109 -0.019  85  GLU B C     
1879 O  O     . GLU B 85  ? 0.3828 0.0787 0.11   -0.013  -0.0076 -0.0199 85  GLU B O     
1880 C  CB    . GLU B 85  ? 0.4373 0.0807 0.1542 -0.0095 -0.0149 -0.0323 85  GLU B CB    
1881 C  CG    . GLU B 85  ? 0.483  0.1073 0.1921 -0.0127 -0.016  -0.0339 85  GLU B CG    
1882 C  CD    . GLU B 85  ? 0.5722 0.1753 0.2716 -0.013  -0.0106 -0.0352 85  GLU B CD    
1883 O  OE1   . GLU B 85  ? 0.5891 0.1942 0.2931 -0.0093 -0.004  -0.0319 85  GLU B OE1   
1884 O  OE2   . GLU B 85  ? 0.6222 0.2098 0.3088 -0.0158 -0.0127 -0.0391 85  GLU B OE2   
1885 N  N     . MET B 86  ? 0.3834 0.08   0.1033 -0.0098 -0.0129 -0.0175 86  MET B N     
1886 C  CA    . MET B 86  ? 0.3926 0.0842 0.1085 -0.016  -0.0117 -0.0267 86  MET B CA    
1887 C  C     . MET B 86  ? 0.4237 0.0919 0.1238 -0.0271 -0.0081 -0.0394 86  MET B C     
1888 O  O     . MET B 86  ? 0.424  0.1027 0.1261 -0.0367 -0.0074 -0.0467 86  MET B O     
1889 C  CB    . MET B 86  ? 0.408  0.0881 0.1129 -0.0127 -0.0133 -0.0352 86  MET B CB    
1890 C  CG    . MET B 86  ? 0.4422 0.1249 0.1505 -0.0084 -0.0167 -0.0451 86  MET B CG    
1891 S  SD    . MET B 86  ? 0.4799 0.1927 0.2043 -0.0124 -0.0169 -0.0367 86  MET B SD    
1892 C  CE    . MET B 86  ? 0.4247 0.1494 0.1375 -0.0213 -0.0169 -0.0442 86  MET B CE    
1893 N  N     . ALA B 87  ? 0.4483 0.0901 0.132  -0.027  -0.0059 -0.0409 87  ALA B N     
1894 C  CA    . ALA B 87  ? 0.4615 0.091  0.1325 -0.0392 -0.0001 -0.044  87  ALA B CA    
1895 C  C     . ALA B 87  ? 0.4583 0.0967 0.141  -0.0445 0.002   -0.0491 87  ALA B C     
1896 O  O     . ALA B 87  ? 0.4644 0.111  0.1453 -0.0588 0.0052  -0.0564 87  ALA B O     
1897 C  CB    . ALA B 87  ? 0.4784 0.0824 0.1284 -0.0351 0.0023  -0.039  87  ALA B CB    
1898 N  N     . ILE B 88  ? 0.4472 0.0904 0.1417 -0.0333 0.001   -0.0432 88  ILE B N     
1899 C  CA    . ILE B 88  ? 0.4453 0.0982 0.1507 -0.0319 0.0056  -0.0433 88  ILE B CA    
1900 C  C     . ILE B 88  ? 0.4515 0.1459 0.176  -0.0313 0.0048  -0.0386 88  ILE B C     
1901 O  O     . ILE B 88  ? 0.4489 0.1704 0.1819 -0.0364 0.0091  -0.0373 88  ILE B O     
1902 C  CB    . ILE B 88  ? 0.4409 0.082  0.1475 -0.0203 0.0064  -0.0374 88  ILE B CB    
1903 C  CG1   . ILE B 88  ? 0.4506 0.0777 0.1406 -0.0214 0.0072  -0.0336 88  ILE B CG1   
1904 C  CG2   . ILE B 88  ? 0.4359 0.0887 0.1533 -0.0126 0.0134  -0.0334 88  ILE B CG2   
1905 C  CD1   . ILE B 88  ? 0.4734 0.079  0.1572 -0.0157 0.0049  -0.0354 88  ILE B CD1   
1906 N  N     . ASN B 89  ? 0.455  0.1589 0.1854 -0.026  -0.0007 -0.0358 89  ASN B N     
1907 C  CA    . ASN B 89  ? 0.4551 0.1989 0.2002 -0.0241 -0.0026 -0.0299 89  ASN B CA    
1908 C  C     . ASN B 89  ? 0.4439 0.2125 0.1871 -0.0409 -0.0036 -0.036  89  ASN B C     
1909 O  O     . ASN B 89  ? 0.4278 0.2395 0.1851 -0.0415 -0.0041 -0.0309 89  ASN B O     
1910 C  CB    . ASN B 89  ? 0.4887 0.2346 0.2358 -0.0175 -0.0075 -0.026  89  ASN B CB    
1911 C  CG    . ASN B 89  ? 0.5774 0.3026 0.3254 -0.0059 -0.006  -0.0197 89  ASN B CG    
1912 O  OD1   . ASN B 89  ? 0.6102 0.3271 0.3601 0.0018  -0.0007 -0.0149 89  ASN B OD1   
1913 N  ND2   . ASN B 89  ? 0.5973 0.313  0.3417 -0.0058 -0.0095 -0.0202 89  ASN B ND2   
1914 N  N     . HIS B 90  ? 0.4532 0.1951 0.1767 -0.0546 -0.0037 -0.0464 90  HIS B N     
1915 C  CA    . HIS B 90  ? 0.4546 0.2104 0.1686 -0.0761 -0.0034 -0.0545 90  HIS B CA    
1916 C  C     . HIS B 90  ? 0.4514 0.2254 0.1706 -0.0879 0.0024  -0.0546 90  HIS B C     
1917 O  O     . HIS B 90  ? 0.445  0.2623 0.1723 -0.1031 0.0018  -0.0556 90  HIS B O     
1918 C  CB    . HIS B 90  ? 0.4908 0.2009 0.1746 -0.0855 -0.0024 -0.0655 90  HIS B CB    
1919 C  CG    . HIS B 90  ? 0.532  0.2479 0.1985 -0.1107 -0.0014 -0.0756 90  HIS B CG    
1920 N  ND1   . HIS B 90  ? 0.583  0.2485 0.2142 -0.1239 0.0038  -0.0864 90  HIS B ND1   
1921 C  CD2   . HIS B 90  ? 0.5359 0.3006 0.2124 -0.1251 -0.005  -0.0763 90  HIS B CD2   
1922 C  CE1   . HIS B 90  ? 0.5906 0.2708 0.2093 -0.1494 0.0041  -0.0951 90  HIS B CE1   
1923 N  NE2   . HIS B 90  ? 0.5659 0.3102 0.2126 -0.1519 -0.0022 -0.0896 90  HIS B NE2   
1924 N  N     . ILE B 91  ? 0.449  0.196  0.1643 -0.0819 0.008   -0.0533 91  ILE B N     
1925 C  CA    . ILE B 91  ? 0.4325 0.1972 0.1526 -0.0917 0.0156  -0.0528 91  ILE B CA    
1926 C  C     . ILE B 91  ? 0.4009 0.2238 0.1514 -0.0792 0.0163  -0.0426 91  ILE B C     
1927 O  O     . ILE B 91  ? 0.3815 0.2523 0.1439 -0.0924 0.0187  -0.0423 91  ILE B O     
1928 C  CB    . ILE B 91  ? 0.4464 0.1658 0.1512 -0.0862 0.0215  -0.0534 91  ILE B CB    
1929 C  CG1   . ILE B 91  ? 0.4779 0.1432 0.1501 -0.0963 0.0213  -0.0615 91  ILE B CG1   
1930 C  CG2   . ILE B 91  ? 0.4456 0.1868 0.1562 -0.0948 0.031   -0.0522 91  ILE B CG2   
1931 C  CD1   . ILE B 91  ? 0.5115 0.1326 0.1666 -0.0864 0.0241  -0.0604 91  ILE B CD1   
1932 N  N     . LYS B 92  ? 0.3924 0.2134 0.1538 -0.0543 0.0141  -0.0339 92  LYS B N     
1933 C  CA    . LYS B 92  ? 0.3706 0.2369 0.1552 -0.0356 0.016   -0.0221 92  LYS B CA    
1934 C  C     . LYS B 92  ? 0.3563 0.2814 0.1551 -0.043  0.0095  -0.0192 92  LYS B C     
1935 O  O     . LYS B 92  ? 0.3328 0.314  0.1511 -0.0384 0.012   -0.0121 92  LYS B O     
1936 C  CB    . LYS B 92  ? 0.3878 0.2262 0.1718 -0.0111 0.0157  -0.0142 92  LYS B CB    
1937 C  CG    . LYS B 92  ? 0.4395 0.23   0.2107 -0.0034 0.0226  -0.0161 92  LYS B CG    
1938 C  CD    . LYS B 92  ? 0.4941 0.2536 0.2597 0.0127  0.0215  -0.0106 92  LYS B CD    
1939 C  CE    . LYS B 92  ? 0.5327 0.314  0.3092 0.0349  0.0267  0.0022  92  LYS B CE    
1940 N  NZ    . LYS B 92  ? 0.5923 0.3375 0.3581 0.0464  0.0269  0.0077  92  LYS B NZ    
1941 N  N     . SER B 93  ? 0.3696 0.2851 0.1576 -0.0545 0.0013  -0.0249 93  SER B N     
1942 C  CA    . SER B 93  ? 0.3573 0.3232 0.1518 -0.0659 -0.0063 -0.0248 93  SER B CA    
1943 C  C     . SER B 93  ? 0.3475 0.351  0.1429 -0.095  -0.0049 -0.0328 93  SER B C     
1944 O  O     . SER B 93  ? 0.3165 0.3879 0.1294 -0.0996 -0.0089 -0.0278 93  SER B O     
1945 C  CB    . SER B 93  ? 0.3999 0.3347 0.1751 -0.0737 -0.0127 -0.0323 93  SER B CB    
1946 O  OG    . SER B 93  ? 0.4509 0.4108 0.2349 -0.0578 -0.0187 -0.0222 93  SER B OG    
1947 N  N     . GLN B 94  ? 0.3735 0.3344 0.1488 -0.1152 0.0009  -0.0443 94  GLN B N     
1948 C  CA    . GLN B 94  ? 0.3781 0.3625 0.1476 -0.1483 0.0046  -0.0531 94  GLN B CA    
1949 C  C     . GLN B 94  ? 0.3594 0.4008 0.1558 -0.1438 0.0112  -0.0446 94  GLN B C     
1950 O  O     . GLN B 94  ? 0.3369 0.4421 0.1455 -0.1655 0.0103  -0.046  94  GLN B O     
1951 C  CB    . GLN B 94  ? 0.4369 0.3479 0.172  -0.1664 0.0112  -0.0651 94  GLN B CB    
1952 C  CG    . GLN B 94  ? 0.5181 0.3807 0.2225 -0.1767 0.0069  -0.0757 94  GLN B CG    
1953 C  CD    . GLN B 94  ? 0.624  0.4074 0.2931 -0.1824 0.0141  -0.0836 94  GLN B CD    
1954 O  OE1   . GLN B 94  ? 0.6515 0.4019 0.3208 -0.1621 0.0175  -0.0783 94  GLN B OE1   
1955 N  NE2   . GLN B 94  ? 0.6562 0.4048 0.2902 -0.2098 0.0169  -0.0964 94  GLN B NE2   
1956 N  N     . LEU B 95  ? 0.3654 0.3864 0.1698 -0.1167 0.0186  -0.0367 95  LEU B N     
1957 C  CA    . LEU B 95  ? 0.3436 0.4153 0.172  -0.1061 0.0275  -0.0281 95  LEU B CA    
1958 C  C     . LEU B 95  ? 0.33   0.4816 0.1894 -0.0861 0.0222  -0.0148 95  LEU B C     
1959 O  O     . LEU B 95  ? 0.3082 0.5345 0.1903 -0.0914 0.0254  -0.0102 95  LEU B O     
1960 C  CB    . LEU B 95  ? 0.3499 0.3723 0.1733 -0.0787 0.0365  -0.0235 95  LEU B CB    
1961 C  CG    . LEU B 95  ? 0.3868 0.3358 0.1799 -0.0929 0.0414  -0.0337 95  LEU B CG    
1962 C  CD1   . LEU B 95  ? 0.4031 0.2992 0.1874 -0.0659 0.0447  -0.0301 95  LEU B CD1   
1963 C  CD2   . LEU B 95  ? 0.3847 0.3498 0.1743 -0.1165 0.0519  -0.0383 95  LEU B CD2   
1964 N  N     . ARG B 96  ? 0.3326 0.471  0.1924 -0.0624 0.0146  -0.0074 96  ARG B N     
1965 C  CA    . ARG B 96  ? 0.3088 0.5139 0.1925 -0.0386 0.0099  0.0078  96  ARG B CA    
1966 C  C     . ARG B 96  ? 0.3203 0.5987 0.2135 -0.0655 -0.0007 0.0047  96  ARG B C     
1967 O  O     . ARG B 96  ? 0.2879 0.6501 0.2072 -0.0544 -0.0027 0.0163  96  ARG B O     
1968 C  CB    . ARG B 96  ? 0.311  0.4736 0.1865 -0.0091 0.0062  0.0168  96  ARG B CB    
1969 C  CG    . ARG B 96  ? 0.2839 0.5051 0.1771 0.0186  0.0015  0.0347  96  ARG B CG    
1970 C  CD    . ARG B 96  ? 0.2694 0.5381 0.1842 0.0477  0.0116  0.0486  96  ARG B CD    
1971 N  NE    . ARG B 96  ? 0.2479 0.5771 0.1785 0.0784  0.0074  0.0681  96  ARG B NE    
1972 C  CZ    . ARG B 96  ? 0.2135 0.6403 0.1675 0.0731  0       0.0743  96  ARG B CZ    
1973 N  NH1   . ARG B 96  ? 0.1786 0.6582 0.1447 0.1066  -0.0037 0.0945  96  ARG B NH1   
1974 N  NH2   . ARG B 96  ? 0.1874 0.6595 0.1503 0.0332  -0.0036 0.0607  96  ARG B NH2   
1975 N  N     . ALA B 97  ? 0.3605 0.6085 0.2304 -0.1015 -0.0068 -0.0114 97  ALA B N     
1976 C  CA    . ALA B 97  ? 0.3622 0.6672 0.2317 -0.1351 -0.0163 -0.0187 97  ALA B CA    
1977 C  C     . ALA B 97  ? 0.3603 0.7365 0.2472 -0.161  -0.0119 -0.0212 97  ALA B C     
1978 O  O     . ALA B 97  ? 0.3342 0.7874 0.2318 -0.1824 -0.0206 -0.022  97  ALA B O     
1979 C  CB    . ALA B 97  ? 0.3976 0.6362 0.2303 -0.1659 -0.0195 -0.0369 97  ALA B CB    
1980 N  N     . THR B 98  ? 0.3833 0.7382 0.2723 -0.1611 0.0016  -0.0225 98  THR B N     
1981 C  CA    . THR B 98  ? 0.3764 0.8016 0.2839 -0.1843 0.0085  -0.0234 98  THR B CA    
1982 C  C     . THR B 98  ? 0.3569 0.8908 0.3065 -0.1564 0.0061  -0.0053 98  THR B C     
1983 O  O     . THR B 98  ? 0.3275 0.9521 0.2975 -0.181  0.0049  -0.0056 98  THR B O     
1984 C  CB    . THR B 98  ? 0.404  0.7804 0.3041 -0.182  0.0248  -0.0259 98  THR B CB    
1985 O  OG1   . THR B 98  ? 0.4138 0.7813 0.3298 -0.1323 0.0316  -0.0114 98  THR B OG1   
1986 C  CG2   . THR B 98  ? 0.4551 0.7253 0.3133 -0.2023 0.0277  -0.0404 98  THR B CG2   
1987 N  N     . GLY B 99  ? 0.373  0.8963 0.3337 -0.1053 0.0067  0.0107  99  GLY B N     
1988 C  CA    . GLY B 99  ? 0.3531 0.9666 0.3489 -0.0675 0.0067  0.031   99  GLY B CA    
1989 C  C     . GLY B 99  ? 0.3545 1.0023 0.3718 -0.0488 0.0234  0.0383  99  GLY B C     
1990 O  O     . GLY B 99  ? 0.3246 1.0521 0.3718 -0.0142 0.0261  0.0558  99  GLY B O     
1991 N  N     . GLU B 100 ? 0.3866 0.9752 0.3872 -0.0688 0.0355  0.0259  100 GLU B N     
1992 C  CA    . GLU B 100 ? 0.3874 1.0005 0.4029 -0.0555 0.0532  0.0303  100 GLU B CA    
1993 C  C     . GLU B 100 ? 0.4071 0.9758 0.4212 0.0007  0.0646  0.043   100 GLU B C     
1994 O  O     . GLU B 100 ? 0.4526 0.9299 0.4411 0.0159  0.062   0.0413  100 GLU B O     
1995 C  CB    . GLU B 100 ? 0.4492 1.0052 0.4403 -0.0975 0.0621  0.0129  100 GLU B CB    
1996 C  CG    . GLU B 100 ? 0.5109 1.1181 0.5022 -0.1557 0.057   0.0008  100 GLU B CG    
1997 C  CD    . GLU B 100 ? 0.5744 1.32   0.6076 -0.1608 0.0572  0.0099  100 GLU B CD    
1998 O  OE1   . GLU B 100 ? 0.5765 1.3889 0.6229 -0.1722 0.0417  0.0121  100 GLU B OE1   
1999 O  OE2   . GLU B 100 ? 0.6024 1.3943 0.6556 -0.1518 0.0727  0.0156  100 GLU B OE2   
2000 N  N     . ARG B 101 ? 0.3692 1.0022 0.4089 0.0311  0.0784  0.0554  101 ARG B N     
2001 C  CA    . ARG B 101 ? 0.3869 0.9691 0.4183 0.084   0.0927  0.0659  101 ARG B CA    
2002 C  C     . ARG B 101 ? 0.4035 0.8938 0.406  0.0745  0.1062  0.0531  101 ARG B C     
2003 O  O     . ARG B 101 ? 0.431  0.8465 0.4125 0.1071  0.1144  0.056   101 ARG B O     
2004 C  CB    . ARG B 101 ? 0.3849 1.0576 0.4481 0.1298  0.1048  0.085   101 ARG B CB    
2005 C  CG    . ARG B 101 ? 0.4063 1.2154 0.5096 0.1088  0.1032  0.0885  101 ARG B CG    
2006 C  CD    . ARG B 101 ? 0.4458 1.348  0.5744 0.1149  0.0851  0.1012  101 ARG B CD    
2007 N  NE    . ARG B 101 ? 0.5279 1.4102 0.6522 0.1731  0.0834  0.1203  101 ARG B NE    
2008 C  CZ    . ARG B 101 ? 0.5566 1.4795 0.6963 0.2318  0.0973  0.1403  101 ARG B CZ    
2009 N  NH1   . ARG B 101 ? 0.5739 1.4674 0.7022 0.2818  0.0958  0.1578  101 ARG B NH1   
2010 N  NH2   . ARG B 101 ? 0.5229 1.5134 0.6866 0.2418  0.1143  0.1434  101 ARG B NH2   
2011 N  N     . GLU B 102 ? 0.3889 0.883  0.3867 0.0281  0.1086  0.0391  102 GLU B N     
2012 C  CA    . GLU B 102 ? 0.4137 0.8261 0.3817 0.0124  0.1196  0.0269  102 GLU B CA    
2013 C  C     . GLU B 102 ? 0.4093 0.7942 0.3585 -0.0442 0.1112  0.011   102 GLU B C     
2014 O  O     . GLU B 102 ? 0.3804 0.8319 0.345  -0.0773 0.1039  0.0082  102 GLU B O     
2015 C  CB    . GLU B 102 ? 0.4319 0.8786 0.4102 0.0286  0.1416  0.0309  102 GLU B CB    
2016 C  CG    . GLU B 102 ? 0.4713 1.0178 0.4764 -0.0049 0.1466  0.0296  102 GLU B CG    
2017 C  CD    . GLU B 102 ? 0.5774 1.1521 0.5891 0.0065  0.1702  0.0319  102 GLU B CD    
2018 O  OE1   . GLU B 102 ? 0.6134 1.1616 0.6203 0.0545  0.1834  0.0393  102 GLU B OE1   
2019 O  OE2   . GLU B 102 ? 0.6035 1.222  0.6213 -0.0343 0.1767  0.0255  102 GLU B OE2   
2020 N  N     . VAL B 103 ? 0.4402 0.7247 0.353  -0.0546 0.1121  0.0008  103 VAL B N     
2021 C  CA    . VAL B 103 ? 0.4614 0.7004 0.3477 -0.1008 0.1058  -0.0131 103 VAL B CA    
2022 C  C     . VAL B 103 ? 0.492  0.6674 0.3488 -0.1124 0.1188  -0.0201 103 VAL B C     
2023 O  O     . VAL B 103 ? 0.5222 0.6449 0.3652 -0.0838 0.1253  -0.0181 103 VAL B O     
2024 C  CB    . VAL B 103 ? 0.497  0.6715 0.3634 -0.1007 0.0893  -0.0176 103 VAL B CB    
2025 C  CG1   . VAL B 103 ? 0.4748 0.7113 0.3629 -0.1035 0.0752  -0.0136 103 VAL B CG1   
2026 C  CG2   . VAL B 103 ? 0.5302 0.6366 0.3832 -0.0627 0.0899  -0.0136 103 VAL B CG2   
2027 N  N     . PRO B 104 ? 0.4843 0.6572 0.3257 -0.1563 0.1228  -0.0287 104 PRO B N     
2028 C  CA    . PRO B 104 ? 0.5087 0.6155 0.3165 -0.1678 0.1348  -0.0341 104 PRO B CA    
2029 C  C     . PRO B 104 ? 0.5499 0.5539 0.3223 -0.1562 0.1263  -0.0385 104 PRO B C     
2030 O  O     . PRO B 104 ? 0.5639 0.5428 0.3292 -0.1619 0.112   -0.042  104 PRO B O     
2031 C  CB    . PRO B 104 ? 0.5175 0.6373 0.3116 -0.2207 0.1383  -0.042  104 PRO B CB    
2032 C  CG    . PRO B 104 ? 0.5063 0.6634 0.3135 -0.2385 0.1232  -0.045  104 PRO B CG    
2033 C  CD    . PRO B 104 ? 0.454  0.6786 0.3023 -0.1994 0.1168  -0.0342 104 PRO B CD    
2034 N  N     . SER B 105 ? 0.5689 0.5179 0.3187 -0.1404 0.1349  -0.0385 105 SER B N     
2035 C  CA    . SER B 105 ? 0.6032 0.4639 0.3204 -0.131  0.126   -0.0422 105 SER B CA    
2036 C  C     . SER B 105 ? 0.6207 0.4298 0.3048 -0.1637 0.1203  -0.0495 105 SER B C     
2037 O  O     . SER B 105 ? 0.6369 0.3898 0.3015 -0.1566 0.1091  -0.0519 105 SER B O     
2038 C  CB    . SER B 105 ? 0.6348 0.4538 0.3322 -0.1112 0.136   -0.0413 105 SER B CB    
2039 O  OG    . SER B 105 ? 0.6827 0.4836 0.3552 -0.1346 0.1483  -0.0439 105 SER B OG    
2040 N  N     . LYS B 106 ? 0.6144 0.4439 0.2912 -0.1992 0.1292  -0.0525 106 LYS B N     
2041 C  CA    . LYS B 106 ? 0.6467 0.4263 0.2877 -0.233  0.1275  -0.0594 106 LYS B CA    
2042 C  C     . LYS B 106 ? 0.6281 0.4094 0.275  -0.2369 0.1123  -0.0635 106 LYS B C     
2043 O  O     . LYS B 106 ? 0.669  0.3835 0.2828 -0.2421 0.1064  -0.0681 106 LYS B O     
2044 C  CB    . LYS B 106 ? 0.6812 0.4954 0.3175 -0.2744 0.1415  -0.0618 106 LYS B CB    
2045 C  CG    . LYS B 106 ? 0.8001 0.5521 0.3906 -0.3129 0.1429  -0.0694 106 LYS B CG    
2046 C  CD    . LYS B 106 ? 0.875  0.6681 0.4623 -0.3607 0.1566  -0.0728 106 LYS B CD    
2047 C  CE    . LYS B 106 ? 0.9859 0.7025 0.5175 -0.4012 0.1615  -0.0805 106 LYS B CE    
2048 N  NZ    . LYS B 106 ? 1.025  0.7274 0.5491 -0.4131 0.1486  -0.0889 106 LYS B NZ    
2049 N  N     . MET B 107 ? 0.5656 0.4232 0.2531 -0.231  0.1063  -0.061  107 MET B N     
2050 C  CA    . MET B 107 ? 0.5389 0.4077 0.2345 -0.2327 0.0919  -0.0642 107 MET B CA    
2051 C  C     . MET B 107 ? 0.5369 0.35   0.2235 -0.2007 0.0812  -0.0627 107 MET B C     
2052 O  O     . MET B 107 ? 0.5681 0.3398 0.2335 -0.2079 0.0733  -0.0685 107 MET B O     
2053 C  CB    . MET B 107 ? 0.5006 0.4673 0.242  -0.2263 0.0881  -0.0586 107 MET B CB    
2054 C  CG    . MET B 107 ? 0.5268 0.5134 0.2737 -0.2353 0.074   -0.0624 107 MET B CG    
2055 S  SD    . MET B 107 ? 0.5372 0.6234 0.3362 -0.2054 0.0659  -0.0502 107 MET B SD    
2056 C  CE    . MET B 107 ? 0.466  0.6461 0.2831 -0.2467 0.0669  -0.0535 107 MET B CE    
2057 N  N     . ILE B 108 ? 0.5018 0.3137 0.2023 -0.1666 0.082   -0.0555 108 ILE B N     
2058 C  CA    . ILE B 108 ? 0.4985 0.262  0.1908 -0.1394 0.0729  -0.054  108 ILE B CA    
2059 C  C     . ILE B 108 ? 0.5234 0.21   0.1747 -0.147  0.0722  -0.0591 108 ILE B C     
2060 O  O     . ILE B 108 ? 0.5287 0.1805 0.1685 -0.1391 0.0625  -0.0611 108 ILE B O     
2061 C  CB    . ILE B 108 ? 0.488  0.259  0.195  -0.1083 0.0772  -0.047  108 ILE B CB    
2062 C  CG1   . ILE B 108 ? 0.4584 0.3031 0.2029 -0.0947 0.0795  -0.0398 108 ILE B CG1   
2063 C  CG2   . ILE B 108 ? 0.5136 0.236  0.2099 -0.0867 0.068   -0.0465 108 ILE B CG2   
2064 C  CD1   . ILE B 108 ? 0.4712 0.317  0.2255 -0.0615 0.0858  -0.0328 108 ILE B CD1   
2065 N  N     . GLY B 109 ? 0.5381 0.2018 0.1672 -0.161  0.0834  -0.06   109 GLY B N     
2066 C  CA    . GLY B 109 ? 0.5777 0.1692 0.1638 -0.1669 0.0848  -0.0623 109 GLY B CA    
2067 C  C     . GLY B 109 ? 0.5961 0.1542 0.1565 -0.1875 0.0819  -0.0685 109 GLY B C     
2068 O  O     . GLY B 109 ? 0.625  0.1269 0.1582 -0.1767 0.0766  -0.0691 109 GLY B O     
2069 N  N     . ASN B 110 ? 0.5771 0.1708 0.1446 -0.2168 0.0855  -0.0734 110 ASN B N     
2070 C  CA    . ASN B 110 ? 0.6093 0.1648 0.1456 -0.2401 0.0846  -0.0814 110 ASN B CA    
2071 C  C     . ASN B 110 ? 0.6145 0.1666 0.1595 -0.2209 0.0713  -0.0833 110 ASN B C     
2072 O  O     . ASN B 110 ? 0.6581 0.1514 0.169  -0.2202 0.0699  -0.0876 110 ASN B O     
2073 C  CB    . ASN B 110 ? 0.6151 0.2141 0.1559 -0.2806 0.0907  -0.0877 110 ASN B CB    
2074 C  CG    . ASN B 110 ? 0.6779 0.2909 0.2121 -0.3063 0.1055  -0.0864 110 ASN B CG    
2075 O  OD1   . ASN B 110 ? 0.672  0.3595 0.2347 -0.3277 0.1091  -0.0871 110 ASN B OD1   
2076 N  ND2   . ASN B 110 ? 0.7204 0.2678 0.217  -0.3052 0.1148  -0.0836 110 ASN B ND2   
2077 N  N     . LEU B 111 ? 0.5688 0.1817 0.1569 -0.2032 0.0628  -0.0793 111 LEU B N     
2078 C  CA    . LEU B 111 ? 0.559  0.1729 0.1569 -0.1847 0.0511  -0.0798 111 LEU B CA    
2079 C  C     . LEU B 111 ? 0.5888 0.1488 0.1706 -0.1571 0.047   -0.0766 111 LEU B C     
2080 O  O     . LEU B 111 ? 0.6121 0.1379 0.1747 -0.1525 0.0428  -0.0805 111 LEU B O     
2081 C  CB    . LEU B 111 ? 0.5144 0.2004 0.1577 -0.1705 0.0444  -0.0738 111 LEU B CB    
2082 C  CG    . LEU B 111 ? 0.4897 0.2462 0.1552 -0.1936 0.0465  -0.0747 111 LEU B CG    
2083 C  CD1   . LEU B 111 ? 0.4559 0.2769 0.1613 -0.1722 0.039   -0.0664 111 LEU B CD1   
2084 C  CD2   . LEU B 111 ? 0.5031 0.2518 0.1451 -0.2276 0.0456  -0.0857 111 LEU B CD2   
2085 N  N     . VAL B 112 ? 0.5919 0.1424 0.1765 -0.1409 0.0493  -0.0704 112 VAL B N     
2086 C  CA    . VAL B 112 ? 0.6188 0.1251 0.1872 -0.1177 0.0442  -0.0674 112 VAL B CA    
2087 C  C     . VAL B 112 ? 0.6753 0.1189 0.1993 -0.1234 0.0476  -0.0705 112 VAL B C     
2088 O  O     . VAL B 112 ? 0.6937 0.1107 0.206  -0.106  0.0414  -0.0701 112 VAL B O     
2089 C  CB    . VAL B 112 ? 0.611  0.1164 0.1842 -0.1033 0.0459  -0.0618 112 VAL B CB    
2090 C  CG1   . VAL B 112 ? 0.6313 0.1009 0.1887 -0.0827 0.0383  -0.0591 112 VAL B CG1   
2091 C  CG2   . VAL B 112 ? 0.5829 0.1387 0.1932 -0.0933 0.0446  -0.0585 112 VAL B CG2   
2092 N  N     . MET B 113 ? 0.7024 0.1228 0.2001 -0.1476 0.0586  -0.0731 113 MET B N     
2093 C  CA    . MET B 113 ? 0.7645 0.1153 0.2118 -0.1548 0.0649  -0.0754 113 MET B CA    
2094 C  C     . MET B 113 ? 0.7948 0.1267 0.2288 -0.1565 0.0621  -0.0824 113 MET B C     
2095 O  O     . MET B 113 ? 0.8257 0.1032 0.2267 -0.1406 0.0624  -0.0818 113 MET B O     
2096 C  CB    . MET B 113 ? 0.7894 0.1235 0.2118 -0.1881 0.079   -0.0778 113 MET B CB    
2097 C  CG    . MET B 113 ? 0.7985 0.138  0.2228 -0.1848 0.0845  -0.0708 113 MET B CG    
2098 S  SD    . MET B 113 ? 0.8684 0.1282 0.2417 -0.1642 0.0864  -0.0631 113 MET B SD    
2099 C  CE    . MET B 113 ? 0.8964 0.0985 0.2161 -0.2013 0.1046  -0.0658 113 MET B CE    
2100 N  N     . GLU B 114 ? 0.7832 0.1629 0.2427 -0.173  0.0593  -0.0885 114 GLU B N     
2101 C  CA    . GLU B 114 ? 0.8065 0.175  0.2542 -0.1772 0.0568  -0.0966 114 GLU B CA    
2102 C  C     . GLU B 114 ? 0.7893 0.164  0.253  -0.143  0.0465  -0.0931 114 GLU B C     
2103 O  O     . GLU B 114 ? 0.8105 0.1479 0.2483 -0.1354 0.0474  -0.0978 114 GLU B O     
2104 C  CB    . GLU B 114 ? 0.8438 0.2705 0.3149 -0.2058 0.0555  -0.1031 114 GLU B CB    
2105 C  CG    . GLU B 114 ? 0.9755 0.4026 0.4308 -0.244  0.0663  -0.1072 114 GLU B CG    
2106 C  CD    . GLU B 114 ? 1.1257 0.5821 0.5775 -0.282  0.0674  -0.1182 114 GLU B CD    
2107 O  OE1   . GLU B 114 ? 1.1349 0.6304 0.6079 -0.2767 0.0578  -0.121  114 GLU B OE1   
2108 O  OE2   . GLU B 114 ? 1.1871 0.6289 0.6134 -0.3193 0.078   -0.1239 114 GLU B OE2   
2109 N  N     . GLN B 115 ? 0.7534 0.1722 0.2564 -0.1233 0.0383  -0.0852 115 GLN B N     
2110 C  CA    . GLN B 115 ? 0.7497 0.1788 0.2691 -0.0949 0.0292  -0.0814 115 GLN B CA    
2111 C  C     . GLN B 115 ? 0.777  0.1574 0.2689 -0.0731 0.0297  -0.0771 115 GLN B C     
2112 O  O     . GLN B 115 ? 0.7965 0.1594 0.2769 -0.056  0.0276  -0.0779 115 GLN B O     
2113 C  CB    . GLN B 115 ? 0.7367 0.2205 0.3001 -0.0842 0.0219  -0.0746 115 GLN B CB    
2114 C  CG    . GLN B 115 ? 0.7398 0.2779 0.3327 -0.097  0.0199  -0.0758 115 GLN B CG    
2115 C  CD    . GLN B 115 ? 0.7926 0.3372 0.3814 -0.1018 0.0169  -0.0818 115 GLN B CD    
2116 O  OE1   . GLN B 115 ? 0.8029 0.3488 0.378  -0.1253 0.0205  -0.0894 115 GLN B OE1   
2117 N  NE2   . GLN B 115 ? 0.7978 0.3465 0.3955 -0.0819 0.0109  -0.0793 115 GLN B NE2   
2118 N  N     . LEU B 116 ? 0.7828 0.1429 0.2619 -0.0726 0.033   -0.0722 116 LEU B N     
2119 C  CA    . LEU B 116 ? 0.8085 0.1266 0.2597 -0.0505 0.0324  -0.0662 116 LEU B CA    
2120 C  C     . LEU B 116 ? 0.8557 0.1109 0.2589 -0.0486 0.0408  -0.0693 116 LEU B C     
2121 O  O     . LEU B 116 ? 0.8684 0.1007 0.2554 -0.0213 0.0384  -0.0647 116 LEU B O     
2122 C  CB    . LEU B 116 ? 0.8065 0.1166 0.2509 -0.052  0.0343  -0.0602 116 LEU B CB    
2123 C  CG    . LEU B 116 ? 0.7835 0.1441 0.2671 -0.048  0.0271  -0.0572 116 LEU B CG    
2124 C  CD1   . LEU B 116 ? 0.7915 0.1398 0.2622 -0.0521 0.0315  -0.0533 116 LEU B CD1   
2125 C  CD2   . LEU B 116 ? 0.7757 0.1586 0.2782 -0.0242 0.0152  -0.0537 116 LEU B CD2   
2126 N  N     . LYS B 117 ? 0.8799 0.1091 0.2596 -0.0771 0.051   -0.0773 117 LYS B N     
2127 C  CA    . LYS B 117 ? 0.9398 0.0982 0.2659 -0.0792 0.0616  -0.0822 117 LYS B CA    
2128 C  C     . LYS B 117 ? 0.9548 0.1144 0.2825 -0.0568 0.0579  -0.0857 117 LYS B C     
2129 O  O     . LYS B 117 ? 0.9889 0.0934 0.2772 -0.0346 0.0637  -0.084  117 LYS B O     
2130 C  CB    . LYS B 117 ? 0.984  0.1271 0.2905 -0.1221 0.072   -0.0927 117 LYS B CB    
2131 C  CG    . LYS B 117 ? 1.108  0.1599 0.3458 -0.1331 0.0872  -0.0969 117 LYS B CG    
2132 C  CD    . LYS B 117 ? 1.1891 0.2335 0.4102 -0.1828 0.0976  -0.1052 117 LYS B CD    
2133 C  CE    . LYS B 117 ? 1.3025 0.2579 0.4539 -0.2049 0.1135  -0.1147 117 LYS B CE    
2134 N  NZ    . LYS B 117 ? 1.3238 0.2775 0.4682 -0.2107 0.1126  -0.128  117 LYS B NZ    
2135 N  N     . LYS B 118 ? 0.9236 0.1474 0.2967 -0.0594 0.0488  -0.0891 118 LYS B N     
2136 C  CA    . LYS B 118 ? 0.9237 0.1613 0.3051 -0.0404 0.0451  -0.0921 118 LYS B CA    
2137 C  C     . LYS B 118 ? 0.9097 0.1716 0.313  -0.0035 0.0364  -0.0815 118 LYS B C     
2138 O  O     . LYS B 118 ? 0.9238 0.1694 0.3126 0.0219  0.0381  -0.081  118 LYS B O     
2139 C  CB    . LYS B 118 ? 0.9175 0.2171 0.3381 -0.0584 0.0387  -0.0977 118 LYS B CB    
2140 C  CG    . LYS B 118 ? 0.9821 0.2744 0.3858 -0.0959 0.0449  -0.1091 118 LYS B CG    
2141 C  CD    . LYS B 118 ? 0.9967 0.359  0.4414 -0.1068 0.0363  -0.1117 118 LYS B CD    
2142 C  CE    . LYS B 118 ? 1.0316 0.4169 0.477  -0.1457 0.0382  -0.1191 118 LYS B CE    
2143 N  NZ    . LYS B 118 ? 1.0143 0.4701 0.4974 -0.1521 0.029   -0.1192 118 LYS B NZ    
2144 N  N     . LEU B 119 ? 0.8781 0.182  0.3159 -0.0017 0.0275  -0.0738 119 LEU B N     
2145 C  CA    . LEU B 119 ? 0.8526 0.1901 0.3152 0.0247  0.0174  -0.0648 119 LEU B CA    
2146 C  C     . LEU B 119 ? 0.8821 0.1842 0.3149 0.0511  0.0182  -0.0567 119 LEU B C     
2147 O  O     . LEU B 119 ? 0.8764 0.1893 0.3109 0.0786  0.015   -0.0526 119 LEU B O     
2148 C  CB    . LEU B 119 ? 0.8156 0.1989 0.3155 0.0137  0.0097  -0.0611 119 LEU B CB    
2149 C  CG    . LEU B 119 ? 0.7929 0.2265 0.3313 0.0025  0.0052  -0.0639 119 LEU B CG    
2150 C  CD1   . LEU B 119 ? 0.7759 0.2376 0.3392 -0.0084 0.002   -0.0607 119 LEU B CD1   
2151 C  CD2   . LEU B 119 ? 0.7806 0.2447 0.3381 0.0206  -0.0009 -0.0618 119 LEU B CD2   
2152 N  N     . ASP B 120 ? 0.9104 0.1751 0.3164 0.0443  0.0224  -0.0531 120 ASP B N     
2153 C  CA    . ASP B 120 ? 0.9451 0.1763 0.3198 0.07    0.0225  -0.0432 120 ASP B CA    
2154 C  C     . ASP B 120 ? 0.9826 0.1517 0.313  0.0551  0.0333  -0.0421 120 ASP B C     
2155 O  O     . ASP B 120 ? 0.9688 0.1481 0.3092 0.0296  0.0343  -0.0439 120 ASP B O     
2156 C  CB    . ASP B 120 ? 0.9508 0.2338 0.3566 0.0822  0.0086  -0.0351 120 ASP B CB    
2157 C  CG    . ASP B 120 ? 1.0357 0.3008 0.4146 0.1134  0.0053  -0.0234 120 ASP B CG    
2158 O  OD1   . ASP B 120 ? 1.0398 0.3156 0.418  0.1423  0.0031  -0.0193 120 ASP B OD1   
2159 O  OD2   . ASP B 120 ? 1.093  0.3336 0.4494 0.1103  0.0059  -0.0177 120 ASP B OD2   
2160 N  N     . LYS B 121 ? 1.0279 0.1315 0.307  0.0732  0.0427  -0.038  121 LYS B N     
2161 C  CA    . LYS B 121 ? 1.0792 0.1104 0.3053 0.0606  0.0556  -0.0358 121 LYS B CA    
2162 C  C     . LYS B 121 ? 1.0658 0.101  0.2874 0.0648  0.0506  -0.0246 121 LYS B C     
2163 O  O     . LYS B 121 ? 1.0919 0.0979 0.2928 0.0388  0.0591  -0.0253 121 LYS B O     
2164 C  CB    . LYS B 121 ? 1.1798 0.1333 0.3471 0.0851  0.0678  -0.0331 121 LYS B CB    
2165 C  CG    . LYS B 121 ? 1.2729 0.2379 0.4376 0.1356  0.06    -0.0194 121 LYS B CG    
2166 C  CD    . LYS B 121 ? 1.3951 0.2935 0.5087 0.1683  0.0727  -0.0171 121 LYS B CD    
2167 C  CE    . LYS B 121 ? 1.4405 0.3688 0.5601 0.2209  0.0636  -0.0019 121 LYS B CE    
2168 N  NZ    . LYS B 121 ? 1.4097 0.4443 0.6011 0.2244  0.0452  -0.0027 121 LYS B NZ    
2169 N  N     . VAL B 122 ? 1.0213 0.0968 0.2622 0.0949  0.0371  -0.0148 122 VAL B N     
2170 C  CA    . VAL B 122 ? 1      0.0835 0.2349 0.0996  0.0306  -0.0048 122 VAL B CA    
2171 C  C     . VAL B 122 ? 0.9603 0.092  0.2351 0.0685  0.0261  -0.0117 122 VAL B C     
2172 O  O     . VAL B 122 ? 0.9791 0.092  0.236  0.053   0.0311  -0.0093 122 VAL B O     
2173 C  CB    . VAL B 122 ? 0.9793 0.0956 0.22   0.1393  0.0166  0.0074  122 VAL B CB    
2174 C  CG1   . VAL B 122 ? 0.962  0.1059 0.2073 0.1377  0.0061  0.0145  122 VAL B CG1   
2175 C  CG2   . VAL B 122 ? 1.0184 0.0756 0.2077 0.1748  0.0241  0.0181  122 VAL B CG2   
2176 N  N     . ALA B 123 ? 0.9042 0.0939 0.2293 0.0604  0.0188  -0.0199 123 ALA B N     
2177 C  CA    . ALA B 123 ? 0.8742 0.1079 0.2372 0.0354  0.0162  -0.0264 123 ALA B CA    
2178 C  C     . ALA B 123 ? 0.8896 0.0982 0.2407 0.0044  0.03    -0.0326 123 ALA B C     
2179 O  O     . ALA B 123 ? 0.8814 0.1078 0.2443 -0.0121 0.0321  -0.0338 123 ALA B O     
2180 C  CB    . ALA B 123 ? 0.8415 0.1289 0.251  0.035   0.0086  -0.0326 123 ALA B CB    
2181 N  N     . TYR B 124 ? 0.9134 0.082  0.2397 -0.0045 0.0403  -0.037  124 TYR B N     
2182 C  CA    . TYR B 124 ? 0.9369 0.0827 0.2482 -0.0381 0.0538  -0.0435 124 TYR B CA    
2183 C  C     . TYR B 124 ? 0.9675 0.0717 0.2404 -0.0458 0.0626  -0.0366 124 TYR B C     
2184 O  O     . TYR B 124 ? 0.9552 0.0784 0.2391 -0.0702 0.0685  -0.0391 124 TYR B O     
2185 C  CB    . TYR B 124 ? 0.9661 0.0686 0.2488 -0.0461 0.0627  -0.0504 124 TYR B CB    
2186 C  CG    . TYR B 124 ? 1.0013 0.0773 0.2617 -0.0859 0.0769  -0.0577 124 TYR B CG    
2187 C  CD1   . TYR B 124 ? 1.0679 0.0723 0.2716 -0.0963 0.0905  -0.054  124 TYR B CD1   
2188 C  CD2   . TYR B 124 ? 0.9859 0.1123 0.2815 -0.114  0.0768  -0.0673 124 TYR B CD2   
2189 C  CE1   . TYR B 124 ? 1.0989 0.0839 0.2826 -0.1381 0.1042  -0.0609 124 TYR B CE1   
2190 C  CE2   . TYR B 124 ? 1.0131 0.1273 0.2917 -0.1534 0.089   -0.0739 124 TYR B CE2   
2191 C  CZ    . TYR B 124 ? 1.08   0.1236 0.3028 -0.1676 0.103   -0.0714 124 TYR B CZ    
2192 O  OH    . TYR B 124 ? 1.1234 0.1573 0.3283 -0.2116 0.1159  -0.0783 124 TYR B OH    
2193 N  N     . ILE B 125 ? 1.0037 0.0542 0.2315 -0.0226 0.0639  -0.0268 125 ILE B N     
2194 C  CA    . ILE B 125 ? 1.0388 0.043  0.2226 -0.026  0.0723  -0.0179 125 ILE B CA    
2195 C  C     . ILE B 125 ? 0.9956 0.0465 0.2052 -0.0261 0.0647  -0.0146 125 ILE B C     
2196 O  O     . ILE B 125 ? 1.0055 0.0436 0.1987 -0.0462 0.0746  -0.0133 125 ILE B O     
2197 C  CB    . ILE B 125 ? 1.099  0.0415 0.2306 0.0074  0.0729  -0.0056 125 ILE B CB    
2198 C  CG1   . ILE B 125 ? 1.1538 0.0415 0.2537 0.0117  0.0824  -0.0096 125 ILE B CG1   
2199 C  CG2   . ILE B 125 ? 1.1501 0.0409 0.2312 0.0042  0.082   0.0054  125 ILE B CG2   
2200 C  CD1   . ILE B 125 ? 1.2053 0.0427 0.273  -0.0276 0.1005  -0.018  125 ILE B CD1   
2201 N  N     . ARG B 126 ? 0.9416 0.0452 0.1889 -0.0051 0.0484  -0.0139 126 ARG B N     
2202 C  CA    . ARG B 126 ? 0.8987 0.0422 0.1665 -0.0056 0.0412  -0.0128 126 ARG B CA    
2203 C  C     . ARG B 126 ? 0.877  0.0526 0.1746 -0.0343 0.0492  -0.0219 126 ARG B C     
2204 O  O     . ARG B 126 ? 0.8809 0.0533 0.167  -0.0456 0.0562  -0.0205 126 ARG B O     
2205 C  CB    . ARG B 126 ? 0.8557 0.0482 0.1565 0.0164  0.0232  -0.0123 126 ARG B CB    
2206 C  CG    . ARG B 126 ? 0.8663 0.0433 0.1414 0.0479  0.0138  -0.0012 126 ARG B CG    
2207 C  CD    . ARG B 126 ? 0.8449 0.0755 0.1455 0.0607  -0.0036 0.0003  126 ARG B CD    
2208 N  NE    . ARG B 126 ? 0.8558 0.0939 0.147  0.0926  -0.0147 0.0099  126 ARG B NE    
2209 C  CZ    . ARG B 126 ? 0.8389 0.1214 0.1637 0.1052  -0.0246 0.0081  126 ARG B CZ    
2210 N  NH1   . ARG B 126 ? 0.785  0.1042 0.1526 0.0877  -0.0256 -0.0028 126 ARG B NH1   
2211 N  NH2   . ARG B 126 ? 0.8383 0.1325 0.154  0.1365  -0.0333 0.0181  126 ARG B NH2   
2212 N  N     . PHE B 127 ? 0.8506 0.0583 0.1847 -0.0446 0.0491  -0.0303 127 PHE B N     
2213 C  CA    . PHE B 127 ? 0.8237 0.0695 0.1891 -0.0672 0.0561  -0.0373 127 PHE B CA    
2214 C  C     . PHE B 127 ? 0.8655 0.0842 0.2045 -0.0938 0.073   -0.038  127 PHE B C     
2215 O  O     . PHE B 127 ? 0.8558 0.0965 0.204  -0.1066 0.0807  -0.0388 127 PHE B O     
2216 C  CB    . PHE B 127 ? 0.7754 0.059  0.1794 -0.0698 0.0513  -0.044  127 PHE B CB    
2217 C  CG    . PHE B 127 ? 0.7263 0.0646 0.1708 -0.0824 0.0544  -0.0481 127 PHE B CG    
2218 C  CD1   . PHE B 127 ? 0.7238 0.072  0.1712 -0.1077 0.0662  -0.0523 127 PHE B CD1   
2219 C  CD2   . PHE B 127 ? 0.6955 0.0709 0.1743 -0.0695 0.0455  -0.0495 127 PHE B CD2   
2220 C  CE1   . PHE B 127 ? 0.6868 0.0902 0.1728 -0.1143 0.0688  -0.0549 127 PHE B CE1   
2221 C  CE2   . PHE B 127 ? 0.6684 0.0875 0.1804 -0.0762 0.0494  -0.0521 127 PHE B CE2   
2222 C  CZ    . PHE B 127 ? 0.6556 0.0913 0.1723 -0.0961 0.0607  -0.0541 127 PHE B CZ    
2223 N  N     . ALA B 128 ? 0.9076 0.0762 0.2102 -0.1027 0.0801  -0.0376 128 ALA B N     
2224 C  CA    . ALA B 128 ? 0.9438 0.0811 0.2154 -0.1336 0.0973  -0.0386 128 ALA B CA    
2225 C  C     . ALA B 128 ? 0.9715 0.082  0.2108 -0.1349 0.1053  -0.0306 128 ALA B C     
2226 O  O     . ALA B 128 ? 0.9772 0.0952 0.2124 -0.162  0.1191  -0.0321 128 ALA B O     
2227 C  CB    . ALA B 128 ? 0.9908 0.0653 0.2195 -0.1413 0.1039  -0.0399 128 ALA B CB    
2228 N  N     . SER B 129 ? 0.9819 0.0669 0.1987 -0.1063 0.0967  -0.0217 129 SER B N     
2229 C  CA    . SER B 129 ? 0.9924 0.0524 0.1751 -0.1063 0.1033  -0.0135 129 SER B CA    
2230 C  C     . SER B 129 ? 0.9594 0.0728 0.1741 -0.1158 0.1063  -0.0176 129 SER B C     
2231 O  O     . SER B 129 ? 0.9802 0.0793 0.1701 -0.1301 0.1193  -0.0142 129 SER B O     
2232 C  CB    . SER B 129 ? 1.0181 0.0477 0.1706 -0.0729 0.0915  -0.0026 129 SER B CB    
2233 O  OG    . SER B 129 ? 1.0145 0.0925 0.2063 -0.05   0.0731  -0.005  129 SER B OG    
2234 N  N     . VAL B 130 ? 0.9107 0.082  0.1768 -0.1077 0.0964  -0.0245 130 VAL B N     
2235 C  CA    . VAL B 130 ? 0.8853 0.1024 0.1794 -0.1127 0.101   -0.0287 130 VAL B CA    
2236 C  C     . VAL B 130 ? 0.882  0.141  0.2095 -0.1359 0.1123  -0.0353 130 VAL B C     
2237 O  O     . VAL B 130 ? 0.8776 0.1583 0.2092 -0.1493 0.1259  -0.0361 130 VAL B O     
2238 C  CB    . VAL B 130 ? 0.856  0.1036 0.1769 -0.0897 0.0858  -0.0311 130 VAL B CB    
2239 C  CG1   . VAL B 130 ? 0.8381 0.1208 0.179  -0.0927 0.0935  -0.0358 130 VAL B CG1   
2240 C  CG2   . VAL B 130 ? 0.8768 0.0927 0.1644 -0.0701 0.0739  -0.0242 130 VAL B CG2   
2241 N  N     . TYR B 131 ? 0.8865 0.1588 0.235  -0.1412 0.1076  -0.0394 131 TYR B N     
2242 C  CA    . TYR B 131 ? 0.8779 0.1976 0.259  -0.1634 0.1155  -0.0452 131 TYR B CA    
2243 C  C     . TYR B 131 ? 0.9356 0.2374 0.2888 -0.1971 0.1331  -0.045  131 TYR B C     
2244 O  O     . TYR B 131 ? 0.9169 0.2601 0.2867 -0.2126 0.1453  -0.0459 131 TYR B O     
2245 C  CB    . TYR B 131 ? 0.8404 0.1789 0.2477 -0.16   0.1042  -0.0499 131 TYR B CB    
2246 C  CG    . TYR B 131 ? 0.7994 0.1905 0.2378 -0.1834 0.1101  -0.0553 131 TYR B CG    
2247 C  CD1   . TYR B 131 ? 0.7637 0.2201 0.2437 -0.1801 0.1131  -0.0555 131 TYR B CD1   
2248 C  CD2   . TYR B 131 ? 0.8128 0.189  0.2369 -0.208  0.1128  -0.06   131 TYR B CD2   
2249 C  CE1   . TYR B 131 ? 0.74   0.2548 0.2502 -0.1997 0.1176  -0.0587 131 TYR B CE1   
2250 C  CE2   . TYR B 131 ? 0.7895 0.2217 0.2418 -0.2326 0.1167  -0.0652 131 TYR B CE2   
2251 C  CZ    . TYR B 131 ? 0.7572 0.2635 0.2548 -0.2275 0.1183  -0.0637 131 TYR B CZ    
2252 O  OH    . TYR B 131 ? 0.7436 0.3145 0.2708 -0.2495 0.1209  -0.0672 131 TYR B OH    
2253 N  N     . ARG B 132 ? 1.0022 0.24   0.3097 -0.2075 0.1358  -0.0432 132 ARG B N     
2254 C  CA    . ARG B 132 ? 1.0591 0.2655 0.3296 -0.2429 0.1537  -0.0426 132 ARG B CA    
2255 C  C     . ARG B 132 ? 1.1114 0.2815 0.3428 -0.2421 0.1646  -0.0342 132 ARG B C     
2256 O  O     . ARG B 132 ? 1.1389 0.2736 0.3317 -0.2714 0.1809  -0.0319 132 ARG B O     
2257 C  CB    . ARG B 132 ? 1.1273 0.2671 0.3557 -0.2546 0.1548  -0.0443 132 ARG B CB    
2258 C  CG    . ARG B 132 ? 1.1725 0.3456 0.4292 -0.2704 0.1501  -0.0546 132 ARG B CG    
2259 C  CD    . ARG B 132 ? 1.2841 0.3922 0.4895 -0.3023 0.1613  -0.059  132 ARG B CD    
2260 N  NE    . ARG B 132 ? 1.3923 0.4132 0.5472 -0.278  0.1583  -0.0543 132 ARG B NE    
2261 C  CZ    . ARG B 132 ? 1.4319 0.4352 0.5861 -0.2622 0.149   -0.0591 132 ARG B CZ    
2262 N  NH1   . ARG B 132 ? 1.3841 0.4477 0.583  -0.2709 0.141   -0.069  132 ARG B NH1   
2263 N  NH2   . ARG B 132 ? 1.4755 0.4014 0.5822 -0.2366 0.1485  -0.0535 132 ARG B NH2   
2264 N  N     . SER B 133 ? 1.1217 0.2989 0.3596 -0.2109 0.1557  -0.0298 133 SER B N     
2265 C  CA    . SER B 133 ? 1.1559 0.3069 0.3604 -0.2037 0.1621  -0.0223 133 SER B CA    
2266 C  C     . SER B 133 ? 1.2276 0.299  0.3658 -0.2144 0.1717  -0.0136 133 SER B C     
2267 O  O     . SER B 133 ? 1.2427 0.3015 0.3577 -0.2454 0.1904  -0.0123 133 SER B O     
2268 C  CB    . SER B 133 ? 1.1398 0.344  0.3676 -0.2182 0.1766  -0.0249 133 SER B CB    
2269 O  OG    . SER B 133 ? 1.1763 0.3559 0.3713 -0.2081 0.1816  -0.0187 133 SER B OG    
2270 N  N     . PHE B 134 ? 1.2723 0.2902 0.3783 -0.1887 0.1599  -0.0068 134 PHE B N     
2271 C  CA    . PHE B 134 ? 1.3499 0.2831 0.386  -0.192  0.1692  0.004   134 PHE B CA    
2272 C  C     . PHE B 134 ? 1.3906 0.3127 0.3967 -0.1895 0.1765  0.0128  134 PHE B C     
2273 O  O     . PHE B 134 ? 1.376  0.3255 0.3967 -0.1633 0.1635  0.0144  134 PHE B O     
2274 C  CB    . PHE B 134 ? 1.3719 0.2604 0.3848 -0.1566 0.1541  0.0108  134 PHE B CB    
2275 C  CG    . PHE B 134 ? 1.3719 0.2616 0.4055 -0.1529 0.1468  0.0032  134 PHE B CG    
2276 C  CD1   . PHE B 134 ? 1.3558 0.2816 0.4236 -0.1834 0.1528  -0.0094 134 PHE B CD1   
2277 C  CD2   . PHE B 134 ? 1.3988 0.2566 0.416  -0.1181 0.1344  0.009   134 PHE B CD2   
2278 C  CE1   . PHE B 134 ? 1.3566 0.2838 0.4404 -0.1802 0.146   -0.0168 134 PHE B CE1   
2279 C  CE2   . PHE B 134 ? 1.3988 0.2583 0.4335 -0.1137 0.1292  0.0015  134 PHE B CE2   
2280 C  CZ    . PHE B 134 ? 1.3712 0.2637 0.4381 -0.1452 0.1347  -0.0118 134 PHE B CZ    
2281 N  N     . GLU B 135 ? 1.4398 0.3261 0.4049 -0.2197 0.1977  0.0174  135 GLU B N     
2282 C  CA    . GLU B 135 ? 1.4815 0.3607 0.4174 -0.2203 0.207   0.0253  135 GLU B CA    
2283 C  C     . GLU B 135 ? 1.5662 0.3621 0.428  -0.2024 0.2073  0.0421  135 GLU B C     
2284 O  O     . GLU B 135 ? 1.5744 0.3661 0.4109 -0.1941 0.2095  0.0496  135 GLU B O     
2285 C  CB    . GLU B 135 ? 1.4947 0.3989 0.4346 -0.2627 0.2311  0.0212  135 GLU B CB    
2286 C  CG    . GLU B 135 ? 1.4948 0.49   0.5085 -0.2753 0.2308  0.007   135 GLU B CG    
2287 C  CD    . GLU B 135 ? 1.5373 0.6007 0.597  -0.253  0.2238  0.0018  135 GLU B CD    
2288 O  OE1   . GLU B 135 ? 1.572  0.617  0.607  -0.2307 0.219   0.0074  135 GLU B OE1   
2289 O  OE2   . GLU B 135 ? 1.5168 0.6506 0.6342 -0.258  0.2236  -0.0079 135 GLU B OE2   
2290 N  N     . ASP B 136 ? 1.6298 0.3601 0.4548 -0.1935 0.2052  0.0484  136 ASP B N     
2291 C  CA    . ASP B 136 ? 1.7165 0.3681 0.471  -0.1683 0.2041  0.0666  136 ASP B CA    
2292 C  C     . ASP B 136 ? 1.7573 0.3799 0.5074 -0.1326 0.1878  0.0701  136 ASP B C     
2293 O  O     . ASP B 136 ? 1.7319 0.3898 0.5292 -0.1342 0.1802  0.0575  136 ASP B O     
2294 C  CB    . ASP B 136 ? 1.7995 0.3731 0.4823 -0.1989 0.2302  0.0769  136 ASP B CB    
2295 C  CG    . ASP B 136 ? 1.93   0.4127 0.559  -0.2103 0.2428  0.0813  136 ASP B CG    
2296 O  OD1   . ASP B 136 ? 1.9224 0.4179 0.5828 -0.2206 0.2402  0.0684  136 ASP B OD1   
2297 O  OD2   . ASP B 136 ? 2.026  0.4206 0.5771 -0.21   0.2565  0.0974  136 ASP B OD2   
2298 N  N     . ILE B 137 ? 1.8159 0.3835 0.5128 -0.0971 0.1813  0.0875  137 ILE B N     
2299 C  CA    . ILE B 137 ? 1.8512 0.4009 0.5452 -0.0564 0.1658  0.0928  137 ILE B CA    
2300 C  C     . ILE B 137 ? 1.9208 0.3959 0.5809 -0.0663 0.1801  0.091   137 ILE B C     
2301 O  O     . ILE B 137 ? 1.9166 0.396  0.595  -0.0414 0.1694  0.0876  137 ILE B O     
2302 C  CB    . ILE B 137 ? 1.8796 0.4063 0.5301 -0.0124 0.1536  0.1134  137 ILE B CB    
2303 C  CG1   . ILE B 137 ? 1.894  0.4123 0.5436 0.0349  0.1374  0.1208  137 ILE B CG1   
2304 C  CG2   . ILE B 137 ? 1.9422 0.3829 0.5092 -0.0204 0.1729  0.1309  137 ILE B CG2   
2305 C  CD1   . ILE B 137 ? 1.9168 0.4405 0.5394 0.0803  0.1205  0.14    137 ILE B CD1   
2306 N  N     . LYS B 138 ? 1.9787 0.3913 0.5931 -0.1069 0.205   0.0907  138 LYS B N     
2307 C  CA    . LYS B 138 ? 2.0416 0.3788 0.6184 -0.1251 0.2208  0.086   138 LYS B CA    
2308 C  C     . LYS B 138 ? 2.0196 0.4209 0.6642 -0.1471 0.2152  0.0639  138 LYS B C     
2309 O  O     . LYS B 138 ? 2.0336 0.4036 0.6715 -0.1359 0.2138  0.0587  138 LYS B O     
2310 C  CB    . LYS B 138 ? 2.116  0.3766 0.6278 -0.1716 0.2494  0.0898  138 LYS B CB    
2311 C  CG    . LYS B 138 ? 2.2105 0.4044 0.6498 -0.1539 0.2574  0.1129  138 LYS B CG    
2312 C  CD    . LYS B 138 ? 2.3207 0.4153 0.6817 -0.1985 0.2884  0.1179  138 LYS B CD    
2313 C  CE    . LYS B 138 ? 2.4149 0.4302 0.6941 -0.1785 0.2979  0.1433  138 LYS B CE    
2314 N  NZ    . LYS B 138 ? 2.5028 0.4004 0.6935 -0.2182 0.3294  0.1497  138 LYS B NZ    
2315 N  N     . ASP B 139 ? 1.9831 0.4766 0.6931 -0.1743 0.2116  0.0516  139 ASP B N     
2316 C  CA    . ASP B 139 ? 1.9574 0.5235 0.736  -0.1943 0.2052  0.0323  139 ASP B CA    
2317 C  C     . ASP B 139 ? 1.9588 0.5481 0.7702 -0.1544 0.1851  0.029   139 ASP B C     
2318 O  O     . ASP B 139 ? 1.9511 0.5514 0.7846 -0.1672 0.1846  0.0162  139 ASP B O     
2319 C  CB    . ASP B 139 ? 1.9247 0.5912 0.7691 -0.211  0.2008  0.0244  139 ASP B CB    
2320 C  CG    . ASP B 139 ? 1.989  0.6578 0.8191 -0.258  0.2223  0.023   139 ASP B CG    
2321 O  OD1   . ASP B 139 ? 2.0446 0.6337 0.8049 -0.2708 0.2391  0.0339  139 ASP B OD1   
2322 O  OD2   . ASP B 139 ? 1.9706 0.722  0.8583 -0.2807 0.2231  0.012   139 ASP B OD2   
2323 N  N     . PHE B 140 ? 1.9676 0.5649 0.7789 -0.1074 0.169   0.0408  140 PHE B N     
2324 C  CA    . PHE B 140 ? 1.9655 0.59   0.8072 -0.0682 0.1503  0.0396  140 PHE B CA    
2325 C  C     . PHE B 140 ? 2.0342 0.5804 0.8304 -0.0576 0.1589  0.04    140 PHE B C     
2326 O  O     . PHE B 140 ? 2.0163 0.5872 0.8452 -0.0588 0.1541  0.0277  140 PHE B O     
2327 C  CB    . PHE B 140 ? 1.949  0.5955 0.791  -0.0235 0.1328  0.0538  140 PHE B CB    
2328 C  CG    . PHE B 140 ? 1.8896 0.6346 0.8004 -0.0194 0.1146  0.0468  140 PHE B CG    
2329 C  CD1   . PHE B 140 ? 1.855  0.6599 0.8218 -0.0041 0.0986  0.0381  140 PHE B CD1   
2330 C  CD2   . PHE B 140 ? 1.882  0.6542 0.796  -0.0299 0.1147  0.0493  140 PHE B CD2   
2331 C  CE1   . PHE B 140 ? 1.815  0.7001 0.8375 -0.0019 0.0836  0.032   140 PHE B CE1   
2332 C  CE2   . PHE B 140 ? 1.8428 0.6945 0.8119 -0.0259 0.0997  0.0421  140 PHE B CE2   
2333 C  CZ    . PHE B 140 ? 1.8046 0.7098 0.8264 -0.0126 0.0844  0.0337  140 PHE B CZ    
2334 N  N     . GLY B 141 ? 2.1109 0.5595 0.828  -0.048  0.173   0.0541  141 GLY B N     
2335 C  CA    . GLY B 141 ? 2.1818 0.5395 0.8423 -0.0345 0.1846  0.0559  141 GLY B CA    
2336 C  C     . GLY B 141 ? 2.2113 0.5406 0.8647 -0.0839 0.2007  0.0374  141 GLY B C     
2337 O  O     . GLY B 141 ? 2.227  0.5211 0.8666 -0.0751 0.2037  0.0299  141 GLY B O     
2338 N  N     . GLU B 142 ? 2.2119 0.562  0.8753 -0.1368 0.211   0.0297  142 GLU B N     
2339 C  CA    . GLU B 142 ? 2.2291 0.5673 0.8895 -0.1917 0.2254  0.012   142 GLU B CA    
2340 C  C     . GLU B 142 ? 2.1898 0.6147 0.9242 -0.1956 0.2105  -0.0054 142 GLU B C     
2341 O  O     . GLU B 142 ? 2.208  0.6054 0.9285 -0.2213 0.2184  -0.0192 142 GLU B O     
2342 C  CB    . GLU B 142 ? 2.2449 0.6015 0.9048 -0.2441 0.239   0.0102  142 GLU B CB    
2343 C  CG    . GLU B 142 ? 2.3439 0.608  0.9237 -0.2449 0.2563  0.0277  142 GLU B CG    
2344 C  CD    . GLU B 142 ? 2.4002 0.6753 0.9717 -0.2999 0.2735  0.0263  142 GLU B CD    
2345 O  OE1   . GLU B 142 ? 2.3577 0.7112 0.9839 -0.3412 0.2737  0.0105  142 GLU B OE1   
2346 O  OE2   . GLU B 142 ? 2.4672 0.6751 0.9767 -0.3008 0.2872  0.0419  142 GLU B OE2   
2347 N  N     . GLU B 143 ? 2.1385 0.6635 0.9467 -0.1716 0.1896  -0.0049 143 GLU B N     
2348 C  CA    . GLU B 143 ? 2.1036 0.7093 0.9802 -0.1726 0.1756  -0.0193 143 GLU B CA    
2349 C  C     . GLU B 143 ? 2.121  0.7125 0.9979 -0.1272 0.1647  -0.0184 143 GLU B C     
2350 O  O     . GLU B 143 ? 2.0898 0.7337 1.0123 -0.1284 0.1554  -0.0302 143 GLU B O     
2351 C  CB    . GLU B 143 ? 2.0703 0.7854 1.0232 -0.1741 0.1614  -0.0213 143 GLU B CB    
2352 C  CG    . GLU B 143 ? 2.1279 0.8607 1.0803 -0.2118 0.1734  -0.0206 143 GLU B CG    
2353 C  CD    . GLU B 143 ? 2.2213 0.9367 1.1545 -0.2675 0.1914  -0.0312 143 GLU B CD    
2354 O  OE1   . GLU B 143 ? 2.196  0.9823 1.1801 -0.2913 0.1873  -0.044  143 GLU B OE1   
2355 O  OE2   . GLU B 143 ? 2.2939 0.928  1.1605 -0.2888 0.2097  -0.0261 143 GLU B OE2   
2356 N  N     . ILE B 144 ? 2.1694 0.692  0.9942 -0.0865 0.1667  -0.0036 144 ILE B N     
2357 C  CA    . ILE B 144 ? 2.1952 0.695  1.0097 -0.0412 0.1607  -0.0009 144 ILE B CA    
2358 C  C     . ILE B 144 ? 2.2659 0.6704 1.0178 -0.0606 0.1807  -0.0105 144 ILE B C     
2359 O  O     . ILE B 144 ? 2.2594 0.6735 1.0259 -0.0555 0.1783  -0.0223 144 ILE B O     
2360 C  CB    . ILE B 144 ? 2.2206 0.6885 1.0017 0.0117  0.1557  0.0207  144 ILE B CB    
2361 C  CG1   . ILE B 144 ? 2.1784 0.7386 1.0166 0.0274  0.1354  0.028   144 ILE B CG1   
2362 C  CG2   . ILE B 144 ? 2.2446 0.6796 1.0049 0.0602  0.1541  0.025   144 ILE B CG2   
2363 C  CD1   . ILE B 144 ? 2.2141 0.7419 1.0116 0.064   0.1327  0.0488  144 ILE B CD1   
2364 N  N     . ALA B 145 ? 2.3315 0.6421 1.0106 -0.0862 0.2015  -0.0063 145 ALA B N     
2365 C  CA    . ALA B 145 ? 2.4053 0.6098 1.0113 -0.1129 0.2239  -0.0156 145 ALA B CA    
2366 C  C     . ALA B 145 ? 2.3966 0.6458 1.0375 -0.1653 0.2247  -0.0391 145 ALA B C     
2367 O  O     . ALA B 145 ? 2.4301 0.6234 1.0349 -0.1735 0.2344  -0.0515 145 ALA B O     
2368 C  CB    . ALA B 145 ? 2.4615 0.5742 0.9929 -0.1402 0.2449  -0.0063 145 ALA B CB    
2369 N  N     . ARG B 146 ? 2.3515 0.7013 1.0599 -0.1989 0.2149  -0.045  146 ARG B N     
2370 C  CA    . ARG B 146 ? 2.3352 0.748  1.0861 -0.2468 0.2128  -0.0649 146 ARG B CA    
2371 C  C     . ARG B 146 ? 2.3327 0.7757 1.1132 -0.2254 0.2016  -0.076  146 ARG B C     
2372 O  O     . ARG B 146 ? 2.3506 0.7731 1.1129 -0.2595 0.209   -0.0927 146 ARG B O     
2373 C  CB    . ARG B 146 ? 2.2887 0.8158 1.1151 -0.2671 0.2014  -0.0647 146 ARG B CB    
2374 C  CG    . ARG B 146 ? 2.3341 0.8534 1.1401 -0.3256 0.2176  -0.068  146 ARG B CG    
2375 C  CD    . ARG B 146 ? 2.3056 0.9434 1.1884 -0.3417 0.2079  -0.0684 146 ARG B CD    
2376 N  NE    . ARG B 146 ? 2.2786 1.0138 1.2348 -0.3362 0.1904  -0.0785 146 ARG B NE    
2377 C  CZ    . ARG B 146 ? 2.2402 1.0803 1.2641 -0.3502 0.1825  -0.0811 146 ARG B CZ    
2378 N  NH1   . ARG B 146 ? 2.2223 1.0886 1.2526 -0.3717 0.1911  -0.0758 146 ARG B NH1   
2379 N  NH2   . ARG B 146 ? 2.1895 1.1075 1.2723 -0.3416 0.1674  -0.0885 146 ARG B NH2   
2380 N  N     . LEU B 147 ? 2.3109 0.7999 1.1324 -0.171  0.1847  -0.067  147 LEU B N     
2381 C  CA    . LEU B 147 ? 2.3061 0.8236 1.1539 -0.1479 0.1753  -0.0758 147 LEU B CA    
2382 C  C     . LEU B 147 ? 2.3821 0.7879 1.1529 -0.1221 0.1901  -0.0759 147 LEU B C     
2383 O  O     . LEU B 147 ? 2.397  0.7807 1.1553 -0.0672 0.1869  -0.0623 147 LEU B O     
2384 C  CB    . LEU B 147 ? 2.2544 0.863  1.1724 -0.1037 0.1534  -0.0663 147 LEU B CB    
2385 C  CG    . LEU B 147 ? 2.2108 0.9265 1.2039 -0.1255 0.1398  -0.0682 147 LEU B CG    
2386 C  CD1   . LEU B 147 ? 2.1976 0.949  1.2161 -0.0953 0.1289  -0.0525 147 LEU B CD1   
2387 C  CD2   . LEU B 147 ? 2.1714 0.9664 1.224  -0.1265 0.1268  -0.0791 147 LEU B CD2   
2388 N  N     . GLU B 148 ? 2.4292 0.7634 1.145  -0.1622 0.2073  -0.0913 148 GLU B N     
2389 C  CA    . GLU B 148 ? 2.5094 0.7231 1.1412 -0.1425 0.2256  -0.0936 148 GLU B CA    
2390 C  C     . GLU B 148 ? 2.5081 0.745  1.1603 -0.104  0.2183  -0.1002 148 GLU B C     
2391 O  O     . GLU B 148 ? 2.4715 0.7782 1.1705 -0.1277 0.209   -0.1154 148 GLU B O     
2392 C  CB    . GLU B 148 ? 2.5866 0.7147 1.1497 -0.2046 0.247   -0.1104 148 GLU B CB    
2393 C  CG    . GLU B 148 ? 2.7284 0.7113 1.1888 -0.198  0.2713  -0.101  148 GLU B CG    
2394 C  CD    . GLU B 148 ? 2.806  0.7908 1.2664 -0.1925 0.2708  -0.0804 148 GLU B CD    
2395 O  OE1   . GLU B 148 ? 2.7838 0.8334 1.2834 -0.2397 0.2665  -0.0833 148 GLU B OE1   
2396 O  OE2   . GLU B 148 ? 2.8655 0.7924 1.2879 -0.1391 0.2746  -0.0607 148 GLU B OE2   
2397 N  N     . ASP B 149 ? 2.5455 0.7264 1.1614 -0.0434 0.2233  -0.0878 149 ASP B N     
2398 C  CA    . ASP B 149 ? 2.5441 0.7453 1.1757 -0.0013 0.2189  -0.0923 149 ASP B CA    
2399 C  C     . ASP B 149 ? 2.624  0.6904 1.1589 0.0223  0.2436  -0.0959 149 ASP B C     
2400 O  O     . ASP B 149 ? 2.6306 0.6873 1.1567 0.0314  0.2482  -0.1096 149 ASP B O     
2401 C  CB    . ASP B 149 ? 2.52   0.8075 1.2141 0.0573  0.1993  -0.0736 149 ASP B CB    
2402 C  CG    . ASP B 149 ? 2.5492 0.8921 1.2817 0.0925  0.1912  -0.0787 149 ASP B CG    
2403 O  OD1   . ASP B 149 ? 2.4987 0.9458 1.306  0.0748  0.1742  -0.0862 149 ASP B OD1   
2404 O  OD2   . ASP B 149 ? 2.6133 0.8949 1.2995 0.1393  0.203   -0.0744 149 ASP B OD2   
2405 P  PG    . DTP C .   ? 0.7819 0.6465 0.3349 0.5014  0.0263  -0.0982 200 DTP A PG    
2406 O  O1G   . DTP C .   ? 0.7591 0.6646 0.3375 0.5359  0.0168  -0.1248 200 DTP A O1G   
2407 O  O2G   . DTP C .   ? 0.8371 0.5995 0.3242 0.4946  0.0226  -0.0846 200 DTP A O2G   
2408 O  O3G   . DTP C .   ? 0.7749 0.667  0.3415 0.5012  0.017   -0.0948 200 DTP A O3G   
2409 P  PB    . DTP C .   ? 0.7681 0.6418 0.3359 0.4307  0.0742  -0.0769 200 DTP A PB    
2410 O  O1B   . DTP C .   ? 0.7372 0.6674 0.3398 0.4084  0.0904  -0.0737 200 DTP A O1B   
2411 O  O2B   . DTP C .   ? 0.8051 0.6097 0.331  0.4163  0.0722  -0.064  200 DTP A O2B   
2412 O  O3B   . DTP C .   ? 0.753  0.6581 0.3356 0.4628  0.0557  -0.0894 200 DTP A O3B   
2413 P  PA    . DTP C .   ? 0.8302 0.6062 0.3393 0.4555  0.0666  -0.0938 200 DTP A PA    
2414 O  O1A   . DTP C .   ? 0.8254 0.6101 0.3374 0.4903  0.055   -0.1131 200 DTP A O1A   
2415 O  O2A   . DTP C .   ? 0.8765 0.5765 0.3362 0.4472  0.0594  -0.0812 200 DTP A O2A   
2416 O  O3A   . DTP C .   ? 0.7857 0.6403 0.3417 0.4479  0.0726  -0.0905 200 DTP A O3A   
2417 O  "O5'" . DTP C .   ? 0.8139 0.5975 0.3326 0.4258  0.0859  -0.0924 200 DTP A "O5'" 
2418 C  "C5'" . DTP C .   ? 0.8001 0.5949 0.3301 0.3945  0.0976  -0.0814 200 DTP A "C5'" 
2419 C  "C4'" . DTP C .   ? 0.8064 0.5792 0.3289 0.3738  0.1074  -0.0871 200 DTP A "C4'" 
2420 O  "O4'" . DTP C .   ? 0.7872 0.5969 0.3292 0.381   0.1101  -0.097  200 DTP A "O4'" 
2421 C  "C3'" . DTP C .   ? 0.8439 0.5439 0.3228 0.3723  0.1055  -0.0927 200 DTP A "C3'" 
2422 O  "O3'" . DTP C .   ? 0.8704 0.5208 0.3184 0.35    0.1101  -0.085  200 DTP A "O3'" 
2423 C  "C2'" . DTP C .   ? 0.834  0.5437 0.3243 0.3601  0.1137  -0.1063 200 DTP A "C2'" 
2424 C  "C1'" . DTP C .   ? 0.7971 0.573  0.3223 0.3754  0.1123  -0.1087 200 DTP A "C1'" 
2425 N  N9    . DTP C .   ? 0.7875 0.5663 0.3076 0.4003  0.1073  -0.1198 200 DTP A N9    
2426 C  C8    . DTP C .   ? 0.7823 0.5663 0.3    0.429   0.0982  -0.1232 200 DTP A C8    
2427 N  N7    . DTP C .   ? 0.7842 0.567  0.2967 0.4482  0.0953  -0.1387 200 DTP A N7    
2428 C  C5    . DTP C .   ? 0.7905 0.5638 0.2989 0.4294  0.1029  -0.1438 200 DTP A C5    
2429 C  C6    . DTP C .   ? 0.7947 0.5594 0.2943 0.4355  0.1035  -0.16   200 DTP A C6    
2430 N  N6    . DTP C .   ? 0.7962 0.5623 0.2901 0.4634  0.0981  -0.1745 200 DTP A N6    
2431 N  N1    . DTP C .   ? 0.7959 0.555  0.2954 0.4132  0.1087  -0.1648 200 DTP A N1    
2432 C  C2    . DTP C .   ? 0.7895 0.5548 0.3005 0.3884  0.1129  -0.1562 200 DTP A C2    
2433 N  N3    . DTP C .   ? 0.7878 0.5604 0.3073 0.3804  0.1142  -0.1409 200 DTP A N3    
2434 C  C4    . DTP C .   ? 0.7906 0.5643 0.3061 0.4009  0.1093  -0.1338 200 DTP A C4    
2435 P  PB    . ADP D .   ? 0.9559 0.5503 0.3231 0.3998  0.0526  -0.0362 201 ADP A PB    
2436 O  O1B   . ADP D .   ? 1.0077 0.5163 0.3118 0.4203  0.0375  -0.0394 201 ADP A O1B   
2437 O  O2B   . ADP D .   ? 0.9695 0.5411 0.3103 0.3834  0.0527  -0.0244 201 ADP A O2B   
2438 O  O3B   . ADP D .   ? 0.9065 0.5927 0.3399 0.4233  0.0459  -0.046  201 ADP A O3B   
2439 P  PA    . ADP D .   ? 0.8941 0.5149 0.3022 0.349   0.0951  -0.0492 201 ADP A PA    
2440 O  O1A   . ADP D .   ? 0.922  0.4925 0.2982 0.3124  0.1132  -0.0519 201 ADP A O1A   
2441 O  O2A   . ADP D .   ? 0.8974 0.5145 0.3031 0.3826  0.0807  -0.0575 201 ADP A O2A   
2442 O  O3A   . ADP D .   ? 0.929  0.5353 0.3155 0.3603  0.0811  -0.038  201 ADP A O3A   
2443 O  "O5'" . ADP D .   ? 0.8275 0.5362 0.3014 0.3402  0.1041  -0.0505 201 ADP A "O5'" 
2444 C  "C5'" . ADP D .   ? 0.8086 0.5331 0.3014 0.3098  0.1205  -0.0555 201 ADP A "C5'" 
2445 C  "C4'" . ADP D .   ? 0.7642 0.5582 0.3068 0.3125  0.121   -0.0561 201 ADP A "C4'" 
2446 O  "O4'" . ADP D .   ? 0.7501 0.5694 0.3037 0.3202  0.1145  -0.046  201 ADP A "O4'" 
2447 C  "C3'" . ADP D .   ? 0.7431 0.5675 0.3038 0.3303  0.1173  -0.0621 201 ADP A "C3'" 
2448 O  "O3'" . ADP D .   ? 0.7251 0.5858 0.3126 0.3201  0.1215  -0.0659 201 ADP A "O3'" 
2449 C  "C2'" . ADP D .   ? 0.7276 0.5794 0.2974 0.3513  0.1086  -0.0565 201 ADP A "C2'" 
2450 O  "O2'" . ADP D .   ? 0.7082 0.6054 0.3011 0.3603  0.1104  -0.0617 201 ADP A "O2'" 
2451 C  "C1'" . ADP D .   ? 0.7173 0.5821 0.2964 0.3371  0.1099  -0.047  201 ADP A "C1'" 
2452 N  N9    . ADP D .   ? 0.6975 0.5797 0.2811 0.3501  0.1009  -0.0425 201 ADP A N9    
2453 C  C8    . ADP D .   ? 0.7074 0.5622 0.2676 0.3697  0.0874  -0.0429 201 ADP A C8    
2454 N  N7    . ADP D .   ? 0.6875 0.5736 0.263  0.3787  0.0787  -0.0424 201 ADP A N7    
2455 C  C5    . ADP D .   ? 0.6598 0.5929 0.2681 0.3599  0.0904  -0.0399 201 ADP A C5    
2456 C  C6    . ADP D .   ? 0.63   0.6082 0.2644 0.3537  0.0907  -0.0392 201 ADP A C6    
2457 N  N6    . ADP D .   ? 0.6088 0.6057 0.2502 0.3679  0.078   -0.0444 201 ADP A N6    
2458 N  N1    . ADP D .   ? 0.6244 0.6248 0.2746 0.3328  0.1026  -0.0351 201 ADP A N1    
2459 C  C2    . ADP D .   ? 0.6349 0.618  0.2782 0.3235  0.1101  -0.0334 201 ADP A C2    
2460 N  N3    . ADP D .   ? 0.6519 0.6037 0.2793 0.3284  0.1104  -0.0367 201 ADP A N3    
2461 C  C4    . ADP D .   ? 0.6674 0.5941 0.2772 0.3445  0.1022  -0.039  201 ADP A C4    
2462 ZN ZN    . ZN  E .   ? 1.3089 1.1939 0.9015 -0.3891 0.0353  -0.3568 202 ZN  A ZN    
2463 MG MG    . MG  F .   ? 0.7121 0.4156 0.1675 0.4416  0.0516  -0.0664 203 MG  A MG    
2464 P  PG    . DTP G .   ? 0.6957 0.2165 0.2347 -0.0228 0.1414  -0.0565 200 DTP B PG    
2465 O  O1G   . DTP G .   ? 0.6791 0.2421 0.2455 -0.0043 0.1559  -0.0534 200 DTP B O1G   
2466 O  O2G   . DTP G .   ? 0.727  0.1964 0.228  -0.0181 0.1397  -0.0625 200 DTP B O2G   
2467 O  O3G   . DTP G .   ? 0.691  0.2209 0.2235 -0.0455 0.1445  -0.0544 200 DTP B O3G   
2468 P  PB    . DTP G .   ? 0.6814 0.1937 0.2376 -0.04   0.105   -0.054  200 DTP B PB    
2469 O  O1B   . DTP G .   ? 0.6703 0.1842 0.2434 -0.0318 0.0908  -0.0535 200 DTP B O1B   
2470 O  O2B   . DTP G .   ? 0.674  0.2159 0.2405 -0.0566 0.1125  -0.0516 200 DTP B O2B   
2471 O  O3B   . DTP G .   ? 0.6853 0.2036 0.2404 -0.0241 0.1211  -0.0553 200 DTP B O3B   
2472 P  PA    . DTP G .   ? 0.7079 0.1456 0.1917 -0.0618 0.1009  -0.0544 200 DTP B PA    
2473 O  O1A   . DTP G .   ? 0.7256 0.1271 0.1735 -0.0573 0.0987  -0.0561 200 DTP B O1A   
2474 O  O2A   . DTP G .   ? 0.6921 0.1536 0.1822 -0.0765 0.1161  -0.0524 200 DTP B O2A   
2475 O  O3A   . DTP G .   ? 0.7026 0.1669 0.2177 -0.0463 0.1003  -0.0563 200 DTP B O3A   
2476 O  "O5'" . DTP G .   ? 0.7073 0.1349 0.1948 -0.0637 0.0838  -0.0525 200 DTP B "O5'" 
2477 C  "C5'" . DTP G .   ? 0.6838 0.1391 0.1992 -0.0699 0.0821  -0.0519 200 DTP B "C5'" 
2478 C  "C4'" . DTP G .   ? 0.6911 0.1205 0.1899 -0.0773 0.0738  -0.0504 200 DTP B "C4'" 
2479 O  "O4'" . DTP G .   ? 0.6956 0.1042 0.1849 -0.0632 0.0591  -0.0496 200 DTP B "O4'" 
2480 C  "C3'" . DTP G .   ? 0.7176 0.1117 0.1786 -0.0909 0.0822  -0.0479 200 DTP B "C3'" 
2481 O  "O3'" . DTP G .   ? 0.7171 0.1297 0.1855 -0.1121 0.094   -0.0489 200 DTP B "O3'" 
2482 C  "C2'" . DTP G .   ? 0.7304 0.088  0.1698 -0.0843 0.0704  -0.0454 200 DTP B "C2'" 
2483 C  "C1'" . DTP G .   ? 0.7182 0.0889 0.1748 -0.0646 0.0558  -0.0461 200 DTP B "C1'" 
2484 N  N9    . DTP G .   ? 0.735  0.0835 0.1657 -0.0539 0.0496  -0.0436 200 DTP B N9    
2485 C  C8    . DTP G .   ? 0.7305 0.0799 0.1527 -0.0525 0.0534  -0.0453 200 DTP B C8    
2486 N  N7    . DTP G .   ? 0.7457 0.0718 0.1371 -0.0458 0.0463  -0.0422 200 DTP B N7    
2487 C  C5    . DTP G .   ? 0.7606 0.0704 0.1411 -0.0389 0.0377  -0.0367 200 DTP B C5    
2488 C  C6    . DTP G .   ? 0.7825 0.0679 0.1312 -0.0265 0.0281  -0.0294 200 DTP B C6    
2489 N  N6    . DTP G .   ? 0.7956 0.0704 0.1159 -0.0222 0.0243  -0.0266 200 DTP B N6    
2490 N  N1    . DTP G .   ? 0.7883 0.0585 0.1307 -0.0174 0.0239  -0.0245 200 DTP B N1    
2491 C  C2    . DTP G .   ? 0.7828 0.0596 0.1471 -0.0244 0.0288  -0.0283 200 DTP B C2    
2492 N  N3    . DTP G .   ? 0.7659 0.0691 0.1613 -0.0388 0.0362  -0.0352 200 DTP B N3    
2493 C  C4    . DTP G .   ? 0.7555 0.0752 0.1585 -0.044  0.0405  -0.0383 200 DTP B C4    
2494 P  PB    . ADP H .   ? 0.5719 0.2323 0.1684 -0.0968 0.1571  -0.0467 201 ADP B PB    
2495 O  O1B   . ADP H .   ? 0.5905 0.1983 0.1652 -0.0748 0.1501  -0.0488 201 ADP B O1B   
2496 O  O2B   . ADP H .   ? 0.5847 0.2505 0.1633 -0.116  0.1749  -0.0463 201 ADP B O2B   
2497 O  O3B   . ADP H .   ? 0.534  0.2629 0.1751 -0.0841 0.1585  -0.0431 201 ADP B O3B   
2498 P  PA    . ADP H .   ? 0.6147 0.1902 0.1718 -0.1259 0.1287  -0.0502 201 ADP B PA    
2499 O  O1A   . ADP H .   ? 0.6245 0.1932 0.1673 -0.1569 0.1317  -0.0514 201 ADP B O1A   
2500 O  O2A   . ADP H .   ? 0.6477 0.1725 0.1727 -0.1123 0.1276  -0.05   201 ADP B O2A   
2501 O  O3A   . ADP H .   ? 0.5808 0.2215 0.1705 -0.119  0.1428  -0.0482 201 ADP B O3A   
2502 O  "O5'" . ADP H .   ? 0.5901 0.181  0.1744 -0.1107 0.113   -0.0506 201 ADP B "O5'" 
2503 C  "C5'" . ADP H .   ? 0.579  0.1727 0.1675 -0.1258 0.1041  -0.0525 201 ADP B "C5'" 
2504 C  "C4'" . ADP H .   ? 0.5516 0.1528 0.1608 -0.1068 0.0899  -0.0521 201 ADP B "C4'" 
2505 O  "O4'" . ADP H .   ? 0.5163 0.1659 0.1583 -0.0899 0.0932  -0.0487 201 ADP B "O4'" 
2506 C  "C3'" . ADP H .   ? 0.5649 0.1188 0.1558 -0.0889 0.0798  -0.0521 201 ADP B "C3'" 
2507 O  "O3'" . ADP H .   ? 0.5657 0.1189 0.166  -0.085  0.0669  -0.0529 201 ADP B "O3'" 
2508 C  "C2'" . ADP H .   ? 0.541  0.1088 0.145  -0.0688 0.084   -0.0504 201 ADP B "C2'" 
2509 O  "O2'" . ADP H .   ? 0.539  0.0811 0.1378 -0.0533 0.0733  -0.0508 201 ADP B "O2'" 
2510 C  "C1'" . ADP H .   ? 0.5192 0.1444 0.1592 -0.0664 0.0871  -0.0477 201 ADP B "C1'" 
2511 N  N9    . ADP H .   ? 0.5074 0.1588 0.163  -0.0479 0.0973  -0.0444 201 ADP B N9    
2512 C  C8    . ADP H .   ? 0.5044 0.1606 0.1526 -0.0446 0.1127  -0.0442 201 ADP B C8    
2513 N  N7    . ADP H .   ? 0.4908 0.1718 0.1553 -0.0225 0.1213  -0.0405 201 ADP B N7    
2514 C  C5    . ADP H .   ? 0.4829 0.175  0.1662 -0.0117 0.1101  -0.0372 201 ADP B C5    
2515 C  C6    . ADP H .   ? 0.4679 0.1815 0.1699 0.0133  0.1125  -0.0309 201 ADP B C6    
2516 N  N6    . ADP H .   ? 0.4567 0.1828 0.1615 0.0357  0.128   -0.0271 201 ADP B N6    
2517 N  N1    . ADP H .   ? 0.4677 0.1866 0.1826 0.0166  0.0996  -0.0278 201 ADP B N1    
2518 C  C2    . ADP H .   ? 0.4725 0.1783 0.1829 -0.0029 0.0859  -0.0319 201 ADP B C2    
2519 N  N3    . ADP H .   ? 0.4823 0.1654 0.1748 -0.0244 0.083   -0.0381 201 ADP B N3    
2520 C  C4    . ADP H .   ? 0.4899 0.1663 0.169  -0.0282 0.0953  -0.04   201 ADP B C4    
2521 ZN ZN    . ZN  I .   ? 0.4482 0.539  0.237  -0.1693 0.0686  0.063   202 ZN  B ZN    
2522 MG MG    . MG  J .   ? 0.5631 0.0934 0.0989 -0.0713 0.1313  -0.0519 203 MG  B MG    
# 
