data_8Y1Q
# 
_entry.id   8Y1Q 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8Y1Q         pdb_00008y1q 10.2210/pdb8y1q/pdb 
WWPDB D_1300044691 ?            ?                   
# 
_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       2024-11-06 
# 
_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                        8Y1Q 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              takato.yano@ompu.ac.jp 
_pdbx_contact_author.name_first         Takato 
_pdbx_contact_author.name_last          Yano 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9720-8339 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fukui, K.'    1 0000-0003-2463-7578 
'Murakawa, T.' 2 0000-0001-5905-532X 
'Yano, T.'     3 0000-0002-9720-8339 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Protein Sci.' 
_citation.journal_id_ASTM           PRCIEI 
_citation.journal_id_CSD            0795 
_citation.journal_id_ISSN           1469-896X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                e5185 
_citation.page_last                 e5185 
_citation.title                     
;dUTP pyrophosphatases from hyperthermophilic eubacterium and archaeon: Structural and functional examinations on the suitability for PCR application.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/pro.5185 
_citation.pdbx_database_id_PubMed   39440877 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fukui, K.'    1 0000-0003-2463-7578 
primary 'Kondo, N.'    2 0000-0002-6624-5989 
primary 'Murakawa, T.' 3 ?                   
primary 'Baba, S.'     4 ?                   
primary 'Kumasaka, T.' 5 ?                   
primary 'Yano, T.'     6 ?                   
# 
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 
;Deoxyuridine 5'-triphosphate nucleotidohydrolase
;
16402.982 3 3.6.1.23 ? ? ? 
2 non-polymer syn "2'-DEOXYURIDINE-5'-MONOPHOSPHATE"                 308.182   3 ?        ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                    24.305    2 ?        ? ? ? 
4 water       nat water                                              18.015    9 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'dUTPase,dUTP pyrophosphatase' 
# 
_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       
;MSKVILKIKRLPHAQDLPLPSYATPHSSGLDLRAAIEKPLKIKPFERVLIPTGLILEIPEGYEGQVRPRSGLAWKKGLTV
LNAPGTIDADYRGEVKVILVNLGNEEVVIERGERIAQLVIAPVQRVEVVEVEEVSQTQRGEGGFGSTGTK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKVILKIKRLPHAQDLPLPSYATPHSSGLDLRAAIEKPLKIKPFERVLIPTGLILEIPEGYEGQVRPRSGLAWKKGLTV
LNAPGTIDADYRGEVKVILVNLGNEEVVIERGERIAQLVIAPVQRVEVVEVEEVSQTQRGEGGFGSTGTK
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "2'-DEOXYURIDINE-5'-MONOPHOSPHATE" DU  
3 'MAGNESIUM ION'                    MG  
4 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   SER n 
1 3   LYS n 
1 4   VAL n 
1 5   ILE n 
1 6   LEU n 
1 7   LYS n 
1 8   ILE n 
1 9   LYS n 
1 10  ARG n 
1 11  LEU n 
1 12  PRO n 
1 13  HIS n 
1 14  ALA n 
1 15  GLN n 
1 16  ASP n 
1 17  LEU n 
1 18  PRO n 
1 19  LEU n 
1 20  PRO n 
1 21  SER n 
1 22  TYR n 
1 23  ALA n 
1 24  THR n 
1 25  PRO n 
1 26  HIS n 
1 27  SER n 
1 28  SER n 
1 29  GLY n 
1 30  LEU n 
1 31  ASP n 
1 32  LEU n 
1 33  ARG n 
1 34  ALA n 
1 35  ALA n 
1 36  ILE n 
1 37  GLU n 
1 38  LYS n 
1 39  PRO n 
1 40  LEU n 
1 41  LYS n 
1 42  ILE n 
1 43  LYS n 
1 44  PRO n 
1 45  PHE n 
1 46  GLU n 
1 47  ARG n 
1 48  VAL n 
1 49  LEU n 
1 50  ILE n 
1 51  PRO n 
1 52  THR n 
1 53  GLY n 
1 54  LEU n 
1 55  ILE n 
1 56  LEU n 
1 57  GLU n 
1 58  ILE n 
1 59  PRO n 
1 60  GLU n 
1 61  GLY n 
1 62  TYR n 
1 63  GLU n 
1 64  GLY n 
1 65  GLN n 
1 66  VAL n 
1 67  ARG n 
1 68  PRO n 
1 69  ARG n 
1 70  SER n 
1 71  GLY n 
1 72  LEU n 
1 73  ALA n 
1 74  TRP n 
1 75  LYS n 
1 76  LYS n 
1 77  GLY n 
1 78  LEU n 
1 79  THR n 
1 80  VAL n 
1 81  LEU n 
1 82  ASN n 
1 83  ALA n 
1 84  PRO n 
1 85  GLY n 
1 86  THR n 
1 87  ILE n 
1 88  ASP n 
1 89  ALA n 
1 90  ASP n 
1 91  TYR n 
1 92  ARG n 
1 93  GLY n 
1 94  GLU n 
1 95  VAL n 
1 96  LYS n 
1 97  VAL n 
1 98  ILE n 
1 99  LEU n 
1 100 VAL n 
1 101 ASN n 
1 102 LEU n 
1 103 GLY n 
1 104 ASN n 
1 105 GLU n 
1 106 GLU n 
1 107 VAL n 
1 108 VAL n 
1 109 ILE n 
1 110 GLU n 
1 111 ARG n 
1 112 GLY n 
1 113 GLU n 
1 114 ARG n 
1 115 ILE n 
1 116 ALA n 
1 117 GLN n 
1 118 LEU n 
1 119 VAL n 
1 120 ILE n 
1 121 ALA n 
1 122 PRO n 
1 123 VAL n 
1 124 GLN n 
1 125 ARG n 
1 126 VAL n 
1 127 GLU n 
1 128 VAL n 
1 129 VAL n 
1 130 GLU n 
1 131 VAL n 
1 132 GLU n 
1 133 GLU n 
1 134 VAL n 
1 135 SER n 
1 136 GLN n 
1 137 THR n 
1 138 GLN n 
1 139 ARG n 
1 140 GLY n 
1 141 GLU n 
1 142 GLY n 
1 143 GLY n 
1 144 PHE n 
1 145 GLY n 
1 146 SER n 
1 147 THR n 
1 148 GLY n 
1 149 THR n 
1 150 LYS 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                   150 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'dut, aq_220' 
_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      'Aquifex aeolicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     63363 
_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               'Rosetta2(DE3) pLysS' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET11a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                            ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                           ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                         ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                    ? 'C4 H7 N O4'     133.103 
DU  'DNA linking'       y "2'-DEOXYURIDINE-5'-MONOPHOSPHATE" ? 'C9 H13 N2 O8 P' 308.182 
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 
TRP 'L-peptide linking' y TRYPTOPHAN                         ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                           ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                             ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  HIS 13  13  13  HIS HIS A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  HIS 26  26  26  HIS HIS A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  PRO 51  51  51  PRO PRO A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  TRP 74  74  74  TRP TRP A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLN 117 117 117 GLN GLN A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 ILE 120 120 120 ILE ILE A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 GLN 124 124 124 GLN GLN A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 GLY 143 143 ?   ?   ?   A . n 
A 1 144 PHE 144 144 ?   ?   ?   A . n 
A 1 145 GLY 145 145 ?   ?   ?   A . n 
A 1 146 SER 146 146 ?   ?   ?   A . n 
A 1 147 THR 147 147 ?   ?   ?   A . n 
A 1 148 GLY 148 148 ?   ?   ?   A . n 
A 1 149 THR 149 149 ?   ?   ?   A . n 
A 1 150 LYS 150 150 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   VAL 4   4   4   VAL VAL B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   LYS 7   7   7   LYS LYS B . n 
B 1 8   ILE 8   8   8   ILE ILE B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  HIS 13  13  13  HIS HIS B . n 
B 1 14  ALA 14  14  14  ALA ALA B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  PRO 18  18  18  PRO PRO B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  TYR 22  22  22  TYR TYR B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  HIS 26  26  26  HIS HIS B . n 
B 1 27  SER 27  27  27  SER SER B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ARG 33  33  33  ARG ARG B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  LYS 38  38  38  LYS LYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  LEU 40  40  40  LEU LEU B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  ILE 42  42  42  ILE ILE B . n 
B 1 43  LYS 43  43  43  LYS LYS B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  PRO 51  51  51  PRO PRO B . n 
B 1 52  THR 52  52  52  THR THR B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  GLU 57  57  57  GLU GLU B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  PRO 59  59  59  PRO PRO B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  TYR 62  62  62  TYR TYR B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  GLY 64  64  64  GLY GLY B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  ARG 67  67  67  ARG ARG B . n 
B 1 68  PRO 68  68  68  PRO PRO B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  SER 70  70  70  SER SER B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  TRP 74  74  74  TRP TRP B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  THR 79  79  79  THR THR B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  ASN 82  82  82  ASN ASN B . n 
B 1 83  ALA 83  83  83  ALA ALA B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  ILE 87  87  87  ILE ILE B . n 
B 1 88  ASP 88  88  88  ASP ASP B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  ARG 92  92  92  ARG ARG B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  GLU 94  94  94  GLU GLU B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  LYS 96  96  96  LYS LYS B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  ILE 98  98  98  ILE ILE B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 ASN 104 104 104 ASN ASN B . n 
B 1 105 GLU 105 105 105 GLU GLU B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 VAL 108 108 108 VAL VAL B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 GLU 110 110 110 GLU GLU B . n 
B 1 111 ARG 111 111 111 ARG ARG B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 GLU 113 113 113 GLU GLU B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 ILE 115 115 115 ILE ILE B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 GLN 117 117 117 GLN GLN B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 ILE 120 120 120 ILE ILE B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 GLN 124 124 124 GLN GLN B . n 
B 1 125 ARG 125 125 125 ARG ARG B . n 
B 1 126 VAL 126 126 126 VAL VAL B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 VAL 129 129 129 VAL VAL B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 VAL 131 131 131 VAL VAL B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 ?   ?   ?   B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 SER 135 135 135 SER SER B . n 
B 1 136 GLN 136 136 136 GLN GLN B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 ARG 139 139 139 ARG ARG B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 GLU 141 141 141 GLU GLU B . n 
B 1 142 GLY 142 142 ?   ?   ?   B . n 
B 1 143 GLY 143 143 ?   ?   ?   B . n 
B 1 144 PHE 144 144 ?   ?   ?   B . n 
B 1 145 GLY 145 145 ?   ?   ?   B . n 
B 1 146 SER 146 146 ?   ?   ?   B . n 
B 1 147 THR 147 147 ?   ?   ?   B . n 
B 1 148 GLY 148 148 ?   ?   ?   B . n 
B 1 149 THR 149 149 ?   ?   ?   B . n 
B 1 150 LYS 150 150 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   VAL 4   4   4   VAL VAL C . n 
C 1 5   ILE 5   5   5   ILE ILE C . n 
C 1 6   LEU 6   6   6   LEU LEU C . n 
C 1 7   LYS 7   7   7   LYS LYS C . n 
C 1 8   ILE 8   8   8   ILE ILE C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  ARG 10  10  10  ARG ARG C . n 
C 1 11  LEU 11  11  11  LEU LEU C . n 
C 1 12  PRO 12  12  12  PRO PRO C . n 
C 1 13  HIS 13  13  13  HIS HIS C . n 
C 1 14  ALA 14  14  14  ALA ALA C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  ASP 16  16  16  ASP ASP C . n 
C 1 17  LEU 17  17  17  LEU LEU C . n 
C 1 18  PRO 18  18  18  PRO PRO C . n 
C 1 19  LEU 19  19  19  LEU LEU C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  TYR 22  22  22  TYR TYR C . n 
C 1 23  ALA 23  23  23  ALA ALA C . n 
C 1 24  THR 24  24  24  THR THR C . n 
C 1 25  PRO 25  25  25  PRO PRO C . n 
C 1 26  HIS 26  26  26  HIS HIS C . n 
C 1 27  SER 27  27  27  SER SER C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  GLY 29  29  29  GLY GLY C . n 
C 1 30  LEU 30  30  30  LEU LEU C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  ARG 33  33  33  ARG ARG C . n 
C 1 34  ALA 34  34  34  ALA ALA C . n 
C 1 35  ALA 35  35  35  ALA ALA C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  GLU 37  37  37  GLU GLU C . n 
C 1 38  LYS 38  38  38  LYS LYS C . n 
C 1 39  PRO 39  39  39  PRO PRO C . n 
C 1 40  LEU 40  40  40  LEU LEU C . n 
C 1 41  LYS 41  41  41  LYS LYS C . n 
C 1 42  ILE 42  42  42  ILE ILE C . n 
C 1 43  LYS 43  43  43  LYS LYS C . n 
C 1 44  PRO 44  44  44  PRO PRO C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  GLU 46  46  46  GLU GLU C . n 
C 1 47  ARG 47  47  47  ARG ARG C . n 
C 1 48  VAL 48  48  48  VAL VAL C . n 
C 1 49  LEU 49  49  49  LEU LEU C . n 
C 1 50  ILE 50  50  50  ILE ILE C . n 
C 1 51  PRO 51  51  51  PRO PRO C . n 
C 1 52  THR 52  52  52  THR THR C . n 
C 1 53  GLY 53  53  53  GLY GLY C . n 
C 1 54  LEU 54  54  54  LEU LEU C . n 
C 1 55  ILE 55  55  55  ILE ILE C . n 
C 1 56  LEU 56  56  56  LEU LEU C . n 
C 1 57  GLU 57  57  57  GLU GLU C . n 
C 1 58  ILE 58  58  58  ILE ILE C . n 
C 1 59  PRO 59  59  59  PRO PRO C . n 
C 1 60  GLU 60  60  60  GLU GLU C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  TYR 62  62  62  TYR TYR C . n 
C 1 63  GLU 63  63  63  GLU GLU C . n 
C 1 64  GLY 64  64  64  GLY GLY C . n 
C 1 65  GLN 65  65  65  GLN GLN C . n 
C 1 66  VAL 66  66  66  VAL VAL C . n 
C 1 67  ARG 67  67  67  ARG ARG C . n 
C 1 68  PRO 68  68  68  PRO PRO C . n 
C 1 69  ARG 69  69  69  ARG ARG C . n 
C 1 70  SER 70  70  70  SER SER C . n 
C 1 71  GLY 71  71  71  GLY GLY C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  ALA 73  73  73  ALA ALA C . n 
C 1 74  TRP 74  74  74  TRP TRP C . n 
C 1 75  LYS 75  75  75  LYS LYS C . n 
C 1 76  LYS 76  76  76  LYS LYS C . n 
C 1 77  GLY 77  77  77  GLY GLY C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  THR 79  79  79  THR THR C . n 
C 1 80  VAL 80  80  80  VAL VAL C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  ASN 82  82  82  ASN ASN C . n 
C 1 83  ALA 83  83  83  ALA ALA C . n 
C 1 84  PRO 84  84  84  PRO PRO C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  THR 86  86  86  THR THR C . n 
C 1 87  ILE 87  87  87  ILE ILE C . n 
C 1 88  ASP 88  88  88  ASP ASP C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  TYR 91  91  91  TYR TYR C . n 
C 1 92  ARG 92  92  92  ARG ARG C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  GLU 94  94  94  GLU GLU C . n 
C 1 95  VAL 95  95  95  VAL VAL C . n 
C 1 96  LYS 96  96  96  LYS LYS C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  ILE 98  98  98  ILE ILE C . n 
C 1 99  LEU 99  99  99  LEU LEU C . n 
C 1 100 VAL 100 100 100 VAL VAL C . n 
C 1 101 ASN 101 101 101 ASN ASN C . n 
C 1 102 LEU 102 102 102 LEU LEU C . n 
C 1 103 GLY 103 103 103 GLY GLY C . n 
C 1 104 ASN 104 104 104 ASN ASN C . n 
C 1 105 GLU 105 105 105 GLU GLU C . n 
C 1 106 GLU 106 106 106 GLU GLU C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 VAL 108 108 108 VAL VAL C . n 
C 1 109 ILE 109 109 109 ILE ILE C . n 
C 1 110 GLU 110 110 110 GLU GLU C . n 
C 1 111 ARG 111 111 111 ARG ARG C . n 
C 1 112 GLY 112 112 112 GLY GLY C . n 
C 1 113 GLU 113 113 113 GLU GLU C . n 
C 1 114 ARG 114 114 114 ARG ARG C . n 
C 1 115 ILE 115 115 115 ILE ILE C . n 
C 1 116 ALA 116 116 116 ALA ALA C . n 
C 1 117 GLN 117 117 117 GLN GLN C . n 
C 1 118 LEU 118 118 118 LEU LEU C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 ILE 120 120 120 ILE ILE C . n 
C 1 121 ALA 121 121 121 ALA ALA C . n 
C 1 122 PRO 122 122 122 PRO PRO C . n 
C 1 123 VAL 123 123 123 VAL VAL C . n 
C 1 124 GLN 124 124 124 GLN GLN C . n 
C 1 125 ARG 125 125 125 ARG ARG C . n 
C 1 126 VAL 126 126 126 VAL VAL C . n 
C 1 127 GLU 127 127 127 GLU GLU C . n 
C 1 128 VAL 128 128 128 VAL VAL C . n 
C 1 129 VAL 129 129 129 VAL VAL C . n 
C 1 130 GLU 130 130 130 GLU GLU C . n 
C 1 131 VAL 131 131 131 VAL VAL C . n 
C 1 132 GLU 132 132 132 GLU GLU C . n 
C 1 133 GLU 133 133 133 GLU GLU C . n 
C 1 134 VAL 134 134 134 VAL VAL C . n 
C 1 135 SER 135 135 135 SER SER C . n 
C 1 136 GLN 136 136 136 GLN GLN C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 GLN 138 138 138 GLN GLN C . n 
C 1 139 ARG 139 139 139 ARG ARG C . n 
C 1 140 GLY 140 140 140 GLY GLY C . n 
C 1 141 GLU 141 141 141 GLU GLU C . n 
C 1 142 GLY 142 142 ?   ?   ?   C . n 
C 1 143 GLY 143 143 ?   ?   ?   C . n 
C 1 144 PHE 144 144 ?   ?   ?   C . n 
C 1 145 GLY 145 145 ?   ?   ?   C . n 
C 1 146 SER 146 146 ?   ?   ?   C . n 
C 1 147 THR 147 147 ?   ?   ?   C . n 
C 1 148 GLY 148 148 ?   ?   ?   C . n 
C 1 149 THR 149 149 ?   ?   ?   C . n 
C 1 150 LYS 150 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        DU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   DU 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 DU  1 201 201 DU  DU  A . 
E 3 MG  1 202 1   MG  MG  A . 
F 2 DU  1 201 201 DU  DU  B . 
G 2 DU  1 201 201 DU  DU  C . 
H 3 MG  1 202 2   MG  MG  C . 
I 4 HOH 1 301 4   HOH HOH A . 
I 4 HOH 2 302 7   HOH HOH A . 
I 4 HOH 3 303 5   HOH HOH A . 
I 4 HOH 4 304 2   HOH HOH A . 
J 4 HOH 1 301 1   HOH HOH B . 
J 4 HOH 2 302 8   HOH HOH B . 
J 4 HOH 3 303 6   HOH HOH B . 
J 4 HOH 4 304 9   HOH HOH B . 
K 4 HOH 1 301 3   HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 9   ? CG  ? A LYS 9   CG  
2   1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
3   1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
4   1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
5   1 Y 1 A GLU 37  ? CG  ? A GLU 37  CG  
6   1 Y 1 A GLU 37  ? CD  ? A GLU 37  CD  
7   1 Y 1 A GLU 37  ? OE1 ? A GLU 37  OE1 
8   1 Y 1 A GLU 37  ? OE2 ? A GLU 37  OE2 
9   1 Y 1 A LYS 38  ? CG  ? A LYS 38  CG  
10  1 Y 1 A LYS 38  ? CD  ? A LYS 38  CD  
11  1 Y 1 A LYS 38  ? CE  ? A LYS 38  CE  
12  1 Y 1 A LYS 38  ? NZ  ? A LYS 38  NZ  
13  1 Y 1 A LEU 40  ? CG  ? A LEU 40  CG  
14  1 Y 1 A LEU 40  ? CD1 ? A LEU 40  CD1 
15  1 Y 1 A LEU 40  ? CD2 ? A LEU 40  CD2 
16  1 Y 1 A LYS 41  ? CG  ? A LYS 41  CG  
17  1 Y 1 A LYS 41  ? CD  ? A LYS 41  CD  
18  1 Y 1 A LYS 41  ? CE  ? A LYS 41  CE  
19  1 Y 1 A LYS 41  ? NZ  ? A LYS 41  NZ  
20  1 Y 1 A LYS 43  ? CG  ? A LYS 43  CG  
21  1 Y 1 A LYS 43  ? CD  ? A LYS 43  CD  
22  1 Y 1 A LYS 43  ? CE  ? A LYS 43  CE  
23  1 Y 1 A LYS 43  ? NZ  ? A LYS 43  NZ  
24  1 Y 1 A LYS 75  ? CG  ? A LYS 75  CG  
25  1 Y 1 A LYS 75  ? CD  ? A LYS 75  CD  
26  1 Y 1 A LYS 75  ? CE  ? A LYS 75  CE  
27  1 Y 1 A LYS 75  ? NZ  ? A LYS 75  NZ  
28  1 Y 1 A GLU 106 ? CG  ? A GLU 106 CG  
29  1 Y 1 A GLU 106 ? CD  ? A GLU 106 CD  
30  1 Y 1 A GLU 106 ? OE1 ? A GLU 106 OE1 
31  1 Y 1 A GLU 106 ? OE2 ? A GLU 106 OE2 
32  1 Y 1 A ARG 111 ? CG  ? A ARG 111 CG  
33  1 Y 1 A ARG 111 ? CD  ? A ARG 111 CD  
34  1 Y 1 A ARG 111 ? NE  ? A ARG 111 NE  
35  1 Y 1 A ARG 111 ? CZ  ? A ARG 111 CZ  
36  1 Y 1 A ARG 111 ? NH1 ? A ARG 111 NH1 
37  1 Y 1 A ARG 111 ? NH2 ? A ARG 111 NH2 
38  1 Y 1 A ARG 114 ? CG  ? A ARG 114 CG  
39  1 Y 1 A ARG 114 ? CD  ? A ARG 114 CD  
40  1 Y 1 A ARG 114 ? NE  ? A ARG 114 NE  
41  1 Y 1 A ARG 114 ? CZ  ? A ARG 114 CZ  
42  1 Y 1 A ARG 114 ? NH1 ? A ARG 114 NH1 
43  1 Y 1 A ARG 114 ? NH2 ? A ARG 114 NH2 
44  1 Y 1 A GLU 127 ? CG  ? A GLU 127 CG  
45  1 Y 1 A GLU 127 ? CD  ? A GLU 127 CD  
46  1 Y 1 A GLU 127 ? OE1 ? A GLU 127 OE1 
47  1 Y 1 A GLU 127 ? OE2 ? A GLU 127 OE2 
48  1 Y 1 A GLU 132 ? CG  ? A GLU 132 CG  
49  1 Y 1 A GLU 132 ? CD  ? A GLU 132 CD  
50  1 Y 1 A GLU 132 ? OE1 ? A GLU 132 OE1 
51  1 Y 1 A GLU 132 ? OE2 ? A GLU 132 OE2 
52  1 Y 1 A GLU 133 ? CG  ? A GLU 133 CG  
53  1 Y 1 A GLU 133 ? CD  ? A GLU 133 CD  
54  1 Y 1 A GLU 133 ? OE1 ? A GLU 133 OE1 
55  1 Y 1 A GLU 133 ? OE2 ? A GLU 133 OE2 
56  1 Y 1 B LYS 3   ? CG  ? B LYS 3   CG  
57  1 Y 1 B LYS 3   ? CD  ? B LYS 3   CD  
58  1 Y 1 B LYS 3   ? CE  ? B LYS 3   CE  
59  1 Y 1 B LYS 3   ? NZ  ? B LYS 3   NZ  
60  1 Y 1 B VAL 4   ? CG1 ? B VAL 4   CG1 
61  1 Y 1 B VAL 4   ? CG2 ? B VAL 4   CG2 
62  1 Y 1 B LYS 7   ? CG  ? B LYS 7   CG  
63  1 Y 1 B LYS 7   ? CD  ? B LYS 7   CD  
64  1 Y 1 B LYS 7   ? CE  ? B LYS 7   CE  
65  1 Y 1 B LYS 7   ? NZ  ? B LYS 7   NZ  
66  1 Y 1 B ILE 8   ? CG1 ? B ILE 8   CG1 
67  1 Y 1 B ILE 8   ? CG2 ? B ILE 8   CG2 
68  1 Y 1 B ILE 8   ? CD1 ? B ILE 8   CD1 
69  1 Y 1 B LYS 9   ? CG  ? B LYS 9   CG  
70  1 Y 1 B LYS 9   ? CD  ? B LYS 9   CD  
71  1 Y 1 B LYS 9   ? CE  ? B LYS 9   CE  
72  1 Y 1 B LYS 9   ? NZ  ? B LYS 9   NZ  
73  1 Y 1 B LYS 38  ? CG  ? B LYS 38  CG  
74  1 Y 1 B LYS 38  ? CD  ? B LYS 38  CD  
75  1 Y 1 B LYS 38  ? CE  ? B LYS 38  CE  
76  1 Y 1 B LYS 38  ? NZ  ? B LYS 38  NZ  
77  1 Y 1 B LYS 41  ? CG  ? B LYS 41  CG  
78  1 Y 1 B LYS 41  ? CD  ? B LYS 41  CD  
79  1 Y 1 B LYS 41  ? CE  ? B LYS 41  CE  
80  1 Y 1 B LYS 41  ? NZ  ? B LYS 41  NZ  
81  1 Y 1 B LYS 43  ? CG  ? B LYS 43  CG  
82  1 Y 1 B LYS 43  ? CD  ? B LYS 43  CD  
83  1 Y 1 B LYS 43  ? CE  ? B LYS 43  CE  
84  1 Y 1 B LYS 43  ? NZ  ? B LYS 43  NZ  
85  1 Y 1 B ILE 55  ? CG1 ? B ILE 55  CG1 
86  1 Y 1 B ILE 55  ? CG2 ? B ILE 55  CG2 
87  1 Y 1 B ILE 55  ? CD1 ? B ILE 55  CD1 
88  1 Y 1 B LYS 75  ? CG  ? B LYS 75  CG  
89  1 Y 1 B LYS 75  ? CD  ? B LYS 75  CD  
90  1 Y 1 B LYS 75  ? CE  ? B LYS 75  CE  
91  1 Y 1 B LYS 75  ? NZ  ? B LYS 75  NZ  
92  1 Y 1 B LYS 96  ? CG  ? B LYS 96  CG  
93  1 Y 1 B LYS 96  ? CD  ? B LYS 96  CD  
94  1 Y 1 B LYS 96  ? CE  ? B LYS 96  CE  
95  1 Y 1 B LYS 96  ? NZ  ? B LYS 96  NZ  
96  1 Y 1 B GLU 106 ? CG  ? B GLU 106 CG  
97  1 Y 1 B GLU 106 ? CD  ? B GLU 106 CD  
98  1 Y 1 B GLU 106 ? OE1 ? B GLU 106 OE1 
99  1 Y 1 B GLU 106 ? OE2 ? B GLU 106 OE2 
100 1 Y 1 B ARG 111 ? CG  ? B ARG 111 CG  
101 1 Y 1 B ARG 111 ? CD  ? B ARG 111 CD  
102 1 Y 1 B ARG 111 ? NE  ? B ARG 111 NE  
103 1 Y 1 B ARG 111 ? CZ  ? B ARG 111 CZ  
104 1 Y 1 B ARG 111 ? NH1 ? B ARG 111 NH1 
105 1 Y 1 B ARG 111 ? NH2 ? B ARG 111 NH2 
106 1 Y 1 B GLU 127 ? CG  ? B GLU 127 CG  
107 1 Y 1 B GLU 127 ? CD  ? B GLU 127 CD  
108 1 Y 1 B GLU 127 ? OE1 ? B GLU 127 OE1 
109 1 Y 1 B GLU 127 ? OE2 ? B GLU 127 OE2 
110 1 Y 1 B VAL 129 ? CG1 ? B VAL 129 CG1 
111 1 Y 1 B VAL 129 ? CG2 ? B VAL 129 CG2 
112 1 Y 1 B VAL 134 ? CG1 ? B VAL 134 CG1 
113 1 Y 1 B VAL 134 ? CG2 ? B VAL 134 CG2 
114 1 Y 1 B GLN 138 ? CG  ? B GLN 138 CG  
115 1 Y 1 B GLN 138 ? CD  ? B GLN 138 CD  
116 1 Y 1 B GLN 138 ? OE1 ? B GLN 138 OE1 
117 1 Y 1 B GLN 138 ? NE2 ? B GLN 138 NE2 
118 1 Y 1 B ARG 139 ? CG  ? B ARG 139 CG  
119 1 Y 1 B ARG 139 ? CD  ? B ARG 139 CD  
120 1 Y 1 B ARG 139 ? NE  ? B ARG 139 NE  
121 1 Y 1 B ARG 139 ? CZ  ? B ARG 139 CZ  
122 1 Y 1 B ARG 139 ? NH1 ? B ARG 139 NH1 
123 1 Y 1 B ARG 139 ? NH2 ? B ARG 139 NH2 
124 1 Y 1 B GLU 141 ? CG  ? B GLU 141 CG  
125 1 Y 1 B GLU 141 ? CD  ? B GLU 141 CD  
126 1 Y 1 B GLU 141 ? OE1 ? B GLU 141 OE1 
127 1 Y 1 B GLU 141 ? OE2 ? B GLU 141 OE2 
128 1 Y 1 C LYS 3   ? CG  ? C LYS 3   CG  
129 1 Y 1 C LYS 3   ? CD  ? C LYS 3   CD  
130 1 Y 1 C LYS 3   ? CE  ? C LYS 3   CE  
131 1 Y 1 C LYS 3   ? NZ  ? C LYS 3   NZ  
132 1 Y 1 C LYS 7   ? CG  ? C LYS 7   CG  
133 1 Y 1 C LYS 7   ? CD  ? C LYS 7   CD  
134 1 Y 1 C LYS 7   ? CE  ? C LYS 7   CE  
135 1 Y 1 C LYS 7   ? NZ  ? C LYS 7   NZ  
136 1 Y 1 C LYS 9   ? CG  ? C LYS 9   CG  
137 1 Y 1 C LYS 9   ? CD  ? C LYS 9   CD  
138 1 Y 1 C LYS 9   ? CE  ? C LYS 9   CE  
139 1 Y 1 C LYS 9   ? NZ  ? C LYS 9   NZ  
140 1 Y 1 C GLU 37  ? CG  ? C GLU 37  CG  
141 1 Y 1 C GLU 37  ? CD  ? C GLU 37  CD  
142 1 Y 1 C GLU 37  ? OE1 ? C GLU 37  OE1 
143 1 Y 1 C GLU 37  ? OE2 ? C GLU 37  OE2 
144 1 Y 1 C LYS 38  ? CG  ? C LYS 38  CG  
145 1 Y 1 C LYS 38  ? CD  ? C LYS 38  CD  
146 1 Y 1 C LYS 38  ? CE  ? C LYS 38  CE  
147 1 Y 1 C LYS 38  ? NZ  ? C LYS 38  NZ  
148 1 Y 1 C ARG 111 ? CG  ? C ARG 111 CG  
149 1 Y 1 C ARG 111 ? CD  ? C ARG 111 CD  
150 1 Y 1 C ARG 111 ? NE  ? C ARG 111 NE  
151 1 Y 1 C ARG 111 ? CZ  ? C ARG 111 CZ  
152 1 Y 1 C ARG 111 ? NH1 ? C ARG 111 NH1 
153 1 Y 1 C ARG 111 ? NH2 ? C ARG 111 NH2 
154 1 Y 1 C ARG 114 ? CG  ? C ARG 114 CG  
155 1 Y 1 C ARG 114 ? CD  ? C ARG 114 CD  
156 1 Y 1 C ARG 114 ? NE  ? C ARG 114 NE  
157 1 Y 1 C ARG 114 ? CZ  ? C ARG 114 CZ  
158 1 Y 1 C ARG 114 ? NH1 ? C ARG 114 NH1 
159 1 Y 1 C ARG 114 ? NH2 ? C ARG 114 NH2 
160 1 Y 1 C GLU 127 ? CG  ? C GLU 127 CG  
161 1 Y 1 C GLU 127 ? CD  ? C GLU 127 CD  
162 1 Y 1 C GLU 127 ? OE1 ? C GLU 127 OE1 
163 1 Y 1 C GLU 127 ? OE2 ? C GLU 127 OE2 
164 1 Y 1 C GLU 132 ? CG  ? C GLU 132 CG  
165 1 Y 1 C GLU 132 ? CD  ? C GLU 132 CD  
166 1 Y 1 C GLU 132 ? OE1 ? C GLU 132 OE1 
167 1 Y 1 C GLU 132 ? OE2 ? C GLU 132 OE2 
168 1 Y 1 C GLU 133 ? CG  ? C GLU 133 CG  
169 1 Y 1 C GLU 133 ? CD  ? C GLU 133 CD  
170 1 Y 1 C GLU 133 ? OE1 ? C GLU 133 OE1 
171 1 Y 1 C GLU 133 ? OE2 ? C GLU 133 OE2 
172 1 Y 1 C GLN 136 ? CG  ? C GLN 136 CG  
173 1 Y 1 C GLN 136 ? CD  ? C GLN 136 CD  
174 1 Y 1 C GLN 136 ? OE1 ? C GLN 136 OE1 
175 1 Y 1 C GLN 136 ? NE2 ? C GLN 136 NE2 
176 1 Y 1 C GLN 138 ? CG  ? C GLN 138 CG  
177 1 Y 1 C GLN 138 ? CD  ? C GLN 138 CD  
178 1 Y 1 C GLN 138 ? OE1 ? C GLN 138 OE1 
179 1 Y 1 C GLN 138 ? NE2 ? C GLN 138 NE2 
180 1 Y 1 C GLU 141 ? CG  ? C GLU 141 CG  
181 1 Y 1 C GLU 141 ? CD  ? C GLU 141 CD  
182 1 Y 1 C GLU 141 ? OE1 ? C GLU 141 OE1 
183 1 Y 1 C GLU 141 ? OE2 ? C GLU 141 OE2 
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21-5207 2 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.9.8.92  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21-5207 4 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y1Q 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.260 
_cell.length_a_esd                 ? 
_cell.length_b                     61.260 
_cell.length_b_esd                 ? 
_cell.length_c                     112.660 
_cell.length_c_esd                 ? 
_cell.volume                       422789.051 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         8Y1Q 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                76 
_symmetry.space_group_name_Hall            'P 4w' 
_symmetry.space_group_name_H-M             'P 41' 
_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                   8Y1Q 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.09 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.1 
_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              8.5 
_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    '200 mM magnesium chloride, 100 mM Tris-HCl (pH 8.5), and 25% (w/v) polyethylene glycol 3,350.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER 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         2023-07-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_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                        'SPRING-8 BEAMLINE BL41XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL41XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          78.81 
_reflns.entry_id                                       8Y1Q 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.42 
_reflns.d_resolution_low                               43.32 
_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                                     15876 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                15.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.42 
_reflns_shell.d_res_low                                     2.51 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1570 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               10.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.758 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               96.12 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Y1Q 
_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                            2.42 
_refine.ls_d_res_low                             43.32 
_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                     15858 
_refine.ls_number_reflns_R_free                  1572 
_refine.ls_number_reflns_R_work                  14286 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.86 
_refine.ls_percent_reflns_R_free                 9.91 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2371 
_refine.ls_R_factor_R_free                       0.2731 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2331 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 38.2555 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.4960 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.42 
_refine_hist.d_res_low                        43.32 
_refine_hist.number_atoms_solvent             9 
_refine_hist.number_atoms_total               3135 
_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        3064 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         62 
_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' ? 0.0020  ? 3180 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5033  ? 4360 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0483  ? 533  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0058  ? 561  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.7210 ? 1167 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.42 2.50  . . 140 1294 100.00 . . . . 0.4096 . . . . . . . . . . . 0.4720 
'X-RAY DIFFRACTION' 2.50 2.59  . . 139 1300 99.79  . . . . 0.3857 . . . . . . . . . . . 0.4518 
'X-RAY DIFFRACTION' 2.59 2.69  . . 141 1309 100.00 . . . . 0.3359 . . . . . . . . . . . 0.3577 
'X-RAY DIFFRACTION' 2.69 2.81  . . 146 1280 99.93  . . . . 0.3368 . . . . . . . . . . . 0.3535 
'X-RAY DIFFRACTION' 2.81 2.96  . . 142 1288 99.58  . . . . 0.3430 . . . . . . . . . . . 0.3745 
'X-RAY DIFFRACTION' 2.96 3.15  . . 143 1284 99.93  . . . . 0.3371 . . . . . . . . . . . 0.4044 
'X-RAY DIFFRACTION' 3.15 3.39  . . 152 1298 99.79  . . . . 0.3052 . . . . . . . . . . . 0.3807 
'X-RAY DIFFRACTION' 3.39 3.73  . . 147 1287 99.86  . . . . 0.2868 . . . . . . . . . . . 0.3031 
'X-RAY DIFFRACTION' 3.73 4.27  . . 137 1308 99.93  . . . . 0.2215 . . . . . . . . . . . 0.2435 
'X-RAY DIFFRACTION' 4.27 5.38  . . 145 1317 100.00 . . . . 0.1763 . . . . . . . . . . . 0.2258 
'X-RAY DIFFRACTION' 5.38 43.32 . . 140 1321 99.86  . . . . 0.1842 . . . . . . . . . . . 0.2216 
# 
_struct.entry_id                     8Y1Q 
_struct.title                        'Crystal structure of Aquifex aeolicus dUTPase complexed with dUMP.' 
_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        8Y1Q 
_struct_keywords.text            'dUTPase, dUTP, dUMP, hyperthermophile, Aquifex aeolicus, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DUT_AQUAE 
_struct_ref.pdbx_db_accession          O66592 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSKVILKIKRLPHAQDLPLPSYATPHSSGLDLRAAIEKPLKIKPFERVLIPTGLILEIPEGYEGQVRPRSGLAWKKGLTV
LNAPGTIDADYRGEVKVILVNLGNEEVVIERGERIAQLVIAPVQRVEVVEVEEVSQTQRGEGGFGSTGTK
;
_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 8Y1Q A 1 ? 150 ? O66592 1 ? 150 ? 1 150 
2 1 8Y1Q B 1 ? 150 ? O66592 1 ? 150 ? 1 150 
3 1 8Y1Q C 1 ? 150 ? O66592 1 ? 150 ? 1 150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
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)' 11840 ? 
1 MORE         -69   ? 
1 'SSA (A^2)'  16460 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   homology 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 PRO A 12 ? GLN A 15 ? PRO A 12 GLN A 15 5 ? 4 
HELX_P HELX_P2 AA2 ARG A 69 ? LYS A 76 ? ARG A 69 LYS A 76 1 ? 8 
HELX_P HELX_P3 AA3 PRO B 12 ? GLN B 15 ? PRO B 12 GLN B 15 5 ? 4 
HELX_P HELX_P4 AA4 ARG B 69 ? GLY B 77 ? ARG B 69 GLY B 77 1 ? 9 
HELX_P HELX_P5 AA5 PRO C 12 ? GLN C 15 ? PRO C 12 GLN C 15 5 ? 4 
HELX_P HELX_P6 AA6 ARG C 69 ? GLY C 77 ? ARG C 69 GLY C 77 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            metalc1 
_struct_conn.conn_type_id                  metalc 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           I 
_struct_conn.ptnr1_label_comp_id           HOH 
_struct_conn.ptnr1_label_seq_id            . 
_struct_conn.ptnr1_label_atom_id           O 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           H 
_struct_conn.ptnr2_label_comp_id           MG 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           MG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            HOH 
_struct_conn.ptnr1_auth_seq_id             302 
_struct_conn.ptnr2_auth_asym_id            C 
_struct_conn.ptnr2_auth_comp_id            MG 
_struct_conn.ptnr2_auth_seq_id             202 
_struct_conn.ptnr2_symmetry                1_555 
_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               2.304 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 83 A . ? ALA 83 A PRO 84 A ? PRO 84 A 1 -2.45 
2 ALA 83 B . ? ALA 83 B PRO 84 B ? PRO 84 B 1 -0.90 
3 ALA 83 C . ? ALA 83 C PRO 84 C ? PRO 84 C 1 -4.22 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
AA7 ? 4 ? 
AA8 ? 2 ? 
AA9 ? 3 ? 
AB1 ? 4 ? 
AB2 ? 2 ? 
# 
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 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 54  ? GLU A 57  ? LEU A 54  GLU A 57  
AA1 2 ILE A 5   ? ARG A 10  ? ILE A 5   ARG A 10  
AA1 3 GLU B 127 ? VAL B 131 ? GLU B 127 VAL B 131 
AA2 1 LEU A 30  ? ARG A 33  ? LEU A 30  ARG A 33  
AA2 2 ARG A 114 ? PRO A 122 ? ARG A 114 PRO A 122 
AA2 3 TYR A 62  ? PRO A 68  ? TYR A 62  PRO A 68  
AA2 4 GLY A 85  ? ILE A 87  ? GLY A 85  ILE A 87  
AA3 1 LEU A 40  ? ILE A 42  ? LEU A 40  ILE A 42  
AA3 2 VAL A 107 ? ILE A 109 ? VAL A 107 ILE A 109 
AA4 1 ARG A 47  ? PRO A 51  ? ARG A 47  PRO A 51  
AA4 2 LYS A 96  ? ASN A 101 ? LYS A 96  ASN A 101 
AA4 3 LEU A 78  ? VAL A 80  ? LEU A 78  VAL A 80  
AA5 1 GLU A 127 ? GLU A 130 ? GLU A 127 GLU A 130 
AA5 2 ILE C 5   ? ARG C 10  ? ILE C 5   ARG C 10  
AA5 3 ARG C 47  ? GLU C 57  ? ARG C 47  GLU C 57  
AA5 4 GLU C 94  ? ASN C 101 ? GLU C 94  ASN C 101 
AA5 5 LEU C 78  ? VAL C 80  ? LEU C 78  VAL C 80  
AA6 1 LEU B 54  ? GLU B 57  ? LEU B 54  GLU B 57  
AA6 2 VAL B 4   ? ARG B 10  ? VAL B 4   ARG B 10  
AA6 3 VAL C 126 ? GLU C 130 ? VAL C 126 GLU C 130 
AA7 1 LEU B 30  ? ARG B 33  ? LEU B 30  ARG B 33  
AA7 2 ARG B 114 ? PRO B 122 ? ARG B 114 PRO B 122 
AA7 3 TYR B 62  ? PRO B 68  ? TYR B 62  PRO B 68  
AA7 4 GLY B 85  ? ILE B 87  ? GLY B 85  ILE B 87  
AA8 1 LEU B 40  ? ILE B 42  ? LEU B 40  ILE B 42  
AA8 2 VAL B 107 ? ILE B 109 ? VAL B 107 ILE B 109 
AA9 1 ARG B 47  ? PRO B 51  ? ARG B 47  PRO B 51  
AA9 2 LYS B 96  ? ASN B 101 ? LYS B 96  ASN B 101 
AA9 3 LEU B 78  ? VAL B 80  ? LEU B 78  VAL B 80  
AB1 1 GLY C 29  ? ARG C 33  ? GLY C 29  ARG C 33  
AB1 2 ARG C 114 ? PRO C 122 ? ARG C 114 PRO C 122 
AB1 3 TYR C 62  ? ARG C 67  ? TYR C 62  ARG C 67  
AB1 4 GLY C 85  ? ILE C 87  ? GLY C 85  ILE C 87  
AB2 1 LEU C 40  ? ILE C 42  ? LEU C 40  ILE C 42  
AB2 2 VAL C 107 ? ILE C 109 ? VAL C 107 ILE C 109 
# 
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 O ILE A 55  ? O ILE A 55  N LYS A 9   ? N LYS A 9   
AA1 2 3 N ILE A 8   ? N ILE A 8   O VAL B 131 ? O VAL B 131 
AA2 1 2 N LEU A 30  ? N LEU A 30  O LEU A 118 ? O LEU A 118 
AA2 2 3 O GLN A 117 ? O GLN A 117 N ARG A 67  ? N ARG A 67  
AA2 3 4 N GLY A 64  ? N GLY A 64  O ILE A 87  ? O ILE A 87  
AA3 1 2 N ILE A 42  ? N ILE A 42  O VAL A 107 ? O VAL A 107 
AA4 1 2 N ILE A 50  ? N ILE A 50  O VAL A 97  ? O VAL A 97  
AA4 2 3 O VAL A 100 ? O VAL A 100 N THR A 79  ? N THR A 79  
AA5 1 2 N GLU A 127 ? N GLU A 127 O LEU C 6   ? O LEU C 6   
AA5 2 3 N LYS C 9   ? N LYS C 9   O ILE C 55  ? O ILE C 55  
AA5 3 4 N ILE C 50  ? N ILE C 50  O VAL C 97  ? O VAL C 97  
AA5 4 5 O VAL C 100 ? O VAL C 100 N THR C 79  ? N THR C 79  
AA6 1 2 O GLU B 57  ? O GLU B 57  N LYS B 7   ? N LYS B 7   
AA6 2 3 N ILE B 8   ? N ILE B 8   O VAL C 129 ? O VAL C 129 
AA7 1 2 N LEU B 30  ? N LEU B 30  O LEU B 118 ? O LEU B 118 
AA7 2 3 O GLN B 117 ? O GLN B 117 N ARG B 67  ? N ARG B 67  
AA7 3 4 N GLY B 64  ? N GLY B 64  O ILE B 87  ? O ILE B 87  
AA8 1 2 N LEU B 40  ? N LEU B 40  O ILE B 109 ? O ILE B 109 
AA9 1 2 N ILE B 50  ? N ILE B 50  O VAL B 97  ? O VAL B 97  
AA9 2 3 O VAL B 100 ? O VAL B 100 N THR B 79  ? N THR B 79  
AB1 1 2 N LEU C 30  ? N LEU C 30  O LEU C 118 ? O LEU C 118 
AB1 2 3 O ALA C 121 ? O ALA C 121 N GLU C 63  ? N GLU C 63  
AB1 3 4 N GLY C 64  ? N GLY C 64  O ILE C 87  ? O ILE C 87  
AB2 1 2 N LEU C 40  ? N LEU C 40  O ILE C 109 ? O ILE C 109 
# 
_pdbx_entry_details.entry_id                   8Y1Q 
_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 
# 
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 GLU A 37  ? ? -109.16 -68.24 
2 1 ASN A 82  ? ? -95.41  31.65  
3 1 PRO B 25  ? ? -63.52  0.13   
4 1 GLU B 37  ? ? -78.97  -71.74 
5 1 ASN B 82  ? ? -88.97  30.25  
6 1 GLU C 57  ? ? -115.97 79.84  
7 1 ASN C 82  ? ? -97.10  31.10  
8 1 GLN C 138 ? ? -28.80  -75.64 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -y,x,z+1/4  
3 y,-x,z+3/4  
4 -x,-y,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         2.02038653401 
_pdbx_refine_tls.origin_y         30.4396863486 
_pdbx_refine_tls.origin_z         -0.536320535887 
_pdbx_refine_tls.T[1][1]          0.446715815842 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0864224640796 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.00485151828578 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.500386130027 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0159800843402 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.475705725247 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.33340246645 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.376366896226 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -1.43597131996 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          3.97454999858 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0148530197394 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          5.48302102543 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0262588017161 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0311002231724 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.160889670285 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0768665375442 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.31501193379 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.150721573894 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.34570989178 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.444787267788 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.285454035028 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     3 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   I 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    M 
_pdbx_refine_tls_group.end_auth_seq_id     2 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A GLY 143 ? A GLY 143 
4  1 Y 1 A PHE 144 ? A PHE 144 
5  1 Y 1 A GLY 145 ? A GLY 145 
6  1 Y 1 A SER 146 ? A SER 146 
7  1 Y 1 A THR 147 ? A THR 147 
8  1 Y 1 A GLY 148 ? A GLY 148 
9  1 Y 1 A THR 149 ? A THR 149 
10 1 Y 1 A LYS 150 ? A LYS 150 
11 1 Y 1 B MET 1   ? B MET 1   
12 1 Y 1 B SER 2   ? B SER 2   
13 1 Y 1 B GLU 133 ? B GLU 133 
14 1 Y 1 B GLY 142 ? B GLY 142 
15 1 Y 1 B GLY 143 ? B GLY 143 
16 1 Y 1 B PHE 144 ? B PHE 144 
17 1 Y 1 B GLY 145 ? B GLY 145 
18 1 Y 1 B SER 146 ? B SER 146 
19 1 Y 1 B THR 147 ? B THR 147 
20 1 Y 1 B GLY 148 ? B GLY 148 
21 1 Y 1 B THR 149 ? B THR 149 
22 1 Y 1 B LYS 150 ? B LYS 150 
23 1 Y 1 C MET 1   ? C MET 1   
24 1 Y 1 C SER 2   ? C SER 2   
25 1 Y 1 C GLY 142 ? C GLY 142 
26 1 Y 1 C GLY 143 ? C GLY 143 
27 1 Y 1 C PHE 144 ? C PHE 144 
28 1 Y 1 C GLY 145 ? C GLY 145 
29 1 Y 1 C SER 146 ? C SER 146 
30 1 Y 1 C THR 147 ? C THR 147 
31 1 Y 1 C GLY 148 ? C GLY 148 
32 1 Y 1 C THR 149 ? C THR 149 
33 1 Y 1 C LYS 150 ? C LYS 150 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
DU  OP3    O  N N 74  
DU  P      P  N N 75  
DU  OP1    O  N N 76  
DU  OP2    O  N N 77  
DU  "O5'"  O  N N 78  
DU  "C5'"  C  N N 79  
DU  "C4'"  C  N R 80  
DU  "O4'"  O  N N 81  
DU  "C3'"  C  N S 82  
DU  "O3'"  O  N N 83  
DU  "C2'"  C  N N 84  
DU  "C1'"  C  N R 85  
DU  N1     N  N N 86  
DU  C2     C  N N 87  
DU  O2     O  N N 88  
DU  N3     N  N N 89  
DU  C4     C  N N 90  
DU  O4     O  N N 91  
DU  C5     C  N N 92  
DU  C6     C  N N 93  
DU  HOP3   H  N N 94  
DU  HOP2   H  N N 95  
DU  "H5'"  H  N N 96  
DU  "H5''" H  N N 97  
DU  "H4'"  H  N N 98  
DU  "H3'"  H  N N 99  
DU  "HO3'" H  N N 100 
DU  "H2'"  H  N N 101 
DU  "H2''" H  N N 102 
DU  "H1'"  H  N N 103 
DU  H3     H  N N 104 
DU  H5     H  N N 105 
DU  H6     H  N N 106 
GLN N      N  N N 107 
GLN CA     C  N S 108 
GLN C      C  N N 109 
GLN O      O  N N 110 
GLN CB     C  N N 111 
GLN CG     C  N N 112 
GLN CD     C  N N 113 
GLN OE1    O  N N 114 
GLN NE2    N  N N 115 
GLN OXT    O  N N 116 
GLN H      H  N N 117 
GLN H2     H  N N 118 
GLN HA     H  N N 119 
GLN HB2    H  N N 120 
GLN HB3    H  N N 121 
GLN HG2    H  N N 122 
GLN HG3    H  N N 123 
GLN HE21   H  N N 124 
GLN HE22   H  N N 125 
GLN HXT    H  N N 126 
GLU N      N  N N 127 
GLU CA     C  N S 128 
GLU C      C  N N 129 
GLU O      O  N N 130 
GLU CB     C  N N 131 
GLU CG     C  N N 132 
GLU CD     C  N N 133 
GLU OE1    O  N N 134 
GLU OE2    O  N N 135 
GLU OXT    O  N N 136 
GLU H      H  N N 137 
GLU H2     H  N N 138 
GLU HA     H  N N 139 
GLU HB2    H  N N 140 
GLU HB3    H  N N 141 
GLU HG2    H  N N 142 
GLU HG3    H  N N 143 
GLU HE2    H  N N 144 
GLU HXT    H  N N 145 
GLY N      N  N N 146 
GLY CA     C  N N 147 
GLY C      C  N N 148 
GLY O      O  N N 149 
GLY OXT    O  N N 150 
GLY H      H  N N 151 
GLY H2     H  N N 152 
GLY HA2    H  N N 153 
GLY HA3    H  N N 154 
GLY HXT    H  N N 155 
HIS N      N  N N 156 
HIS CA     C  N S 157 
HIS C      C  N N 158 
HIS O      O  N N 159 
HIS CB     C  N N 160 
HIS CG     C  Y N 161 
HIS ND1    N  Y N 162 
HIS CD2    C  Y N 163 
HIS CE1    C  Y N 164 
HIS NE2    N  Y N 165 
HIS OXT    O  N N 166 
HIS H      H  N N 167 
HIS H2     H  N N 168 
HIS HA     H  N N 169 
HIS HB2    H  N N 170 
HIS HB3    H  N N 171 
HIS HD1    H  N N 172 
HIS HD2    H  N N 173 
HIS HE1    H  N N 174 
HIS HE2    H  N N 175 
HIS HXT    H  N N 176 
HOH O      O  N N 177 
HOH H1     H  N N 178 
HOH H2     H  N N 179 
ILE N      N  N N 180 
ILE CA     C  N S 181 
ILE C      C  N N 182 
ILE O      O  N N 183 
ILE CB     C  N S 184 
ILE CG1    C  N N 185 
ILE CG2    C  N N 186 
ILE CD1    C  N N 187 
ILE OXT    O  N N 188 
ILE H      H  N N 189 
ILE H2     H  N N 190 
ILE HA     H  N N 191 
ILE HB     H  N N 192 
ILE HG12   H  N N 193 
ILE HG13   H  N N 194 
ILE HG21   H  N N 195 
ILE HG22   H  N N 196 
ILE HG23   H  N N 197 
ILE HD11   H  N N 198 
ILE HD12   H  N N 199 
ILE HD13   H  N N 200 
ILE HXT    H  N N 201 
LEU N      N  N N 202 
LEU CA     C  N S 203 
LEU C      C  N N 204 
LEU O      O  N N 205 
LEU CB     C  N N 206 
LEU CG     C  N N 207 
LEU CD1    C  N N 208 
LEU CD2    C  N N 209 
LEU OXT    O  N N 210 
LEU H      H  N N 211 
LEU H2     H  N N 212 
LEU HA     H  N N 213 
LEU HB2    H  N N 214 
LEU HB3    H  N N 215 
LEU HG     H  N N 216 
LEU HD11   H  N N 217 
LEU HD12   H  N N 218 
LEU HD13   H  N N 219 
LEU HD21   H  N N 220 
LEU HD22   H  N N 221 
LEU HD23   H  N N 222 
LEU HXT    H  N N 223 
LYS N      N  N N 224 
LYS CA     C  N S 225 
LYS C      C  N N 226 
LYS O      O  N N 227 
LYS CB     C  N N 228 
LYS CG     C  N N 229 
LYS CD     C  N N 230 
LYS CE     C  N N 231 
LYS NZ     N  N N 232 
LYS OXT    O  N N 233 
LYS H      H  N N 234 
LYS H2     H  N N 235 
LYS HA     H  N N 236 
LYS HB2    H  N N 237 
LYS HB3    H  N N 238 
LYS HG2    H  N N 239 
LYS HG3    H  N N 240 
LYS HD2    H  N N 241 
LYS HD3    H  N N 242 
LYS HE2    H  N N 243 
LYS HE3    H  N N 244 
LYS HZ1    H  N N 245 
LYS HZ2    H  N N 246 
LYS HZ3    H  N N 247 
LYS HXT    H  N N 248 
MET N      N  N N 249 
MET CA     C  N S 250 
MET C      C  N N 251 
MET O      O  N N 252 
MET CB     C  N N 253 
MET CG     C  N N 254 
MET SD     S  N N 255 
MET CE     C  N N 256 
MET OXT    O  N N 257 
MET H      H  N N 258 
MET H2     H  N N 259 
MET HA     H  N N 260 
MET HB2    H  N N 261 
MET HB3    H  N N 262 
MET HG2    H  N N 263 
MET HG3    H  N N 264 
MET HE1    H  N N 265 
MET HE2    H  N N 266 
MET HE3    H  N N 267 
MET HXT    H  N N 268 
MG  MG     MG N N 269 
PHE N      N  N N 270 
PHE CA     C  N S 271 
PHE C      C  N N 272 
PHE O      O  N N 273 
PHE CB     C  N N 274 
PHE CG     C  Y N 275 
PHE CD1    C  Y N 276 
PHE CD2    C  Y N 277 
PHE CE1    C  Y N 278 
PHE CE2    C  Y N 279 
PHE CZ     C  Y N 280 
PHE OXT    O  N N 281 
PHE H      H  N N 282 
PHE H2     H  N N 283 
PHE HA     H  N N 284 
PHE HB2    H  N N 285 
PHE HB3    H  N N 286 
PHE HD1    H  N N 287 
PHE HD2    H  N N 288 
PHE HE1    H  N N 289 
PHE HE2    H  N N 290 
PHE HZ     H  N N 291 
PHE HXT    H  N N 292 
PRO N      N  N N 293 
PRO CA     C  N S 294 
PRO C      C  N N 295 
PRO O      O  N N 296 
PRO CB     C  N N 297 
PRO CG     C  N N 298 
PRO CD     C  N N 299 
PRO OXT    O  N N 300 
PRO H      H  N N 301 
PRO HA     H  N N 302 
PRO HB2    H  N N 303 
PRO HB3    H  N N 304 
PRO HG2    H  N N 305 
PRO HG3    H  N N 306 
PRO HD2    H  N N 307 
PRO HD3    H  N N 308 
PRO HXT    H  N N 309 
SER N      N  N N 310 
SER CA     C  N S 311 
SER C      C  N N 312 
SER O      O  N N 313 
SER CB     C  N N 314 
SER OG     O  N N 315 
SER OXT    O  N N 316 
SER H      H  N N 317 
SER H2     H  N N 318 
SER HA     H  N N 319 
SER HB2    H  N N 320 
SER HB3    H  N N 321 
SER HG     H  N N 322 
SER HXT    H  N N 323 
THR N      N  N N 324 
THR CA     C  N S 325 
THR C      C  N N 326 
THR O      O  N N 327 
THR CB     C  N R 328 
THR OG1    O  N N 329 
THR CG2    C  N N 330 
THR OXT    O  N N 331 
THR H      H  N N 332 
THR H2     H  N N 333 
THR HA     H  N N 334 
THR HB     H  N N 335 
THR HG1    H  N N 336 
THR HG21   H  N N 337 
THR HG22   H  N N 338 
THR HG23   H  N N 339 
THR HXT    H  N N 340 
TRP N      N  N N 341 
TRP CA     C  N S 342 
TRP C      C  N N 343 
TRP O      O  N N 344 
TRP CB     C  N N 345 
TRP CG     C  Y N 346 
TRP CD1    C  Y N 347 
TRP CD2    C  Y N 348 
TRP NE1    N  Y N 349 
TRP CE2    C  Y N 350 
TRP CE3    C  Y N 351 
TRP CZ2    C  Y N 352 
TRP CZ3    C  Y N 353 
TRP CH2    C  Y N 354 
TRP OXT    O  N N 355 
TRP H      H  N N 356 
TRP H2     H  N N 357 
TRP HA     H  N N 358 
TRP HB2    H  N N 359 
TRP HB3    H  N N 360 
TRP HD1    H  N N 361 
TRP HE1    H  N N 362 
TRP HE3    H  N N 363 
TRP HZ2    H  N N 364 
TRP HZ3    H  N N 365 
TRP HH2    H  N N 366 
TRP HXT    H  N N 367 
TYR N      N  N N 368 
TYR CA     C  N S 369 
TYR C      C  N N 370 
TYR O      O  N N 371 
TYR CB     C  N N 372 
TYR CG     C  Y N 373 
TYR CD1    C  Y N 374 
TYR CD2    C  Y N 375 
TYR CE1    C  Y N 376 
TYR CE2    C  Y N 377 
TYR CZ     C  Y N 378 
TYR OH     O  N N 379 
TYR OXT    O  N N 380 
TYR H      H  N N 381 
TYR H2     H  N N 382 
TYR HA     H  N N 383 
TYR HB2    H  N N 384 
TYR HB3    H  N N 385 
TYR HD1    H  N N 386 
TYR HD2    H  N N 387 
TYR HE1    H  N N 388 
TYR HE2    H  N N 389 
TYR HH     H  N N 390 
TYR HXT    H  N N 391 
VAL N      N  N N 392 
VAL CA     C  N S 393 
VAL C      C  N N 394 
VAL O      O  N N 395 
VAL CB     C  N N 396 
VAL CG1    C  N N 397 
VAL CG2    C  N N 398 
VAL OXT    O  N N 399 
VAL H      H  N N 400 
VAL H2     H  N N 401 
VAL HA     H  N N 402 
VAL HB     H  N N 403 
VAL HG11   H  N N 404 
VAL HG12   H  N N 405 
VAL HG13   H  N N 406 
VAL HG21   H  N N 407 
VAL HG22   H  N N 408 
VAL HG23   H  N N 409 
VAL HXT    H  N N 410 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
DU  OP3   P      sing N N 70  
DU  OP3   HOP3   sing N N 71  
DU  P     OP1    doub N N 72  
DU  P     OP2    sing N N 73  
DU  P     "O5'"  sing N N 74  
DU  OP2   HOP2   sing N N 75  
DU  "O5'" "C5'"  sing N N 76  
DU  "C5'" "C4'"  sing N N 77  
DU  "C5'" "H5'"  sing N N 78  
DU  "C5'" "H5''" sing N N 79  
DU  "C4'" "O4'"  sing N N 80  
DU  "C4'" "C3'"  sing N N 81  
DU  "C4'" "H4'"  sing N N 82  
DU  "O4'" "C1'"  sing N N 83  
DU  "C3'" "O3'"  sing N N 84  
DU  "C3'" "C2'"  sing N N 85  
DU  "C3'" "H3'"  sing N N 86  
DU  "O3'" "HO3'" sing N N 87  
DU  "C2'" "C1'"  sing N N 88  
DU  "C2'" "H2'"  sing N N 89  
DU  "C2'" "H2''" sing N N 90  
DU  "C1'" N1     sing N N 91  
DU  "C1'" "H1'"  sing N N 92  
DU  N1    C2     sing N N 93  
DU  N1    C6     sing N N 94  
DU  C2    O2     doub N N 95  
DU  C2    N3     sing N N 96  
DU  N3    C4     sing N N 97  
DU  N3    H3     sing N N 98  
DU  C4    O4     doub N N 99  
DU  C4    C5     sing N N 100 
DU  C5    C6     doub N N 101 
DU  C5    H5     sing N N 102 
DU  C6    H6     sing N N 103 
GLN N     CA     sing N N 104 
GLN N     H      sing N N 105 
GLN N     H2     sing N N 106 
GLN CA    C      sing N N 107 
GLN CA    CB     sing N N 108 
GLN CA    HA     sing N N 109 
GLN C     O      doub N N 110 
GLN C     OXT    sing N N 111 
GLN CB    CG     sing N N 112 
GLN CB    HB2    sing N N 113 
GLN CB    HB3    sing N N 114 
GLN CG    CD     sing N N 115 
GLN CG    HG2    sing N N 116 
GLN CG    HG3    sing N N 117 
GLN CD    OE1    doub N N 118 
GLN CD    NE2    sing N N 119 
GLN NE2   HE21   sing N N 120 
GLN NE2   HE22   sing N N 121 
GLN OXT   HXT    sing N N 122 
GLU N     CA     sing N N 123 
GLU N     H      sing N N 124 
GLU N     H2     sing N N 125 
GLU CA    C      sing N N 126 
GLU CA    CB     sing N N 127 
GLU CA    HA     sing N N 128 
GLU C     O      doub N N 129 
GLU C     OXT    sing N N 130 
GLU CB    CG     sing N N 131 
GLU CB    HB2    sing N N 132 
GLU CB    HB3    sing N N 133 
GLU CG    CD     sing N N 134 
GLU CG    HG2    sing N N 135 
GLU CG    HG3    sing N N 136 
GLU CD    OE1    doub N N 137 
GLU CD    OE2    sing N N 138 
GLU OE2   HE2    sing N N 139 
GLU OXT   HXT    sing N N 140 
GLY N     CA     sing N N 141 
GLY N     H      sing N N 142 
GLY N     H2     sing N N 143 
GLY CA    C      sing N N 144 
GLY CA    HA2    sing N N 145 
GLY CA    HA3    sing N N 146 
GLY C     O      doub N N 147 
GLY C     OXT    sing N N 148 
GLY OXT   HXT    sing N N 149 
HIS N     CA     sing N N 150 
HIS N     H      sing N N 151 
HIS N     H2     sing N N 152 
HIS CA    C      sing N N 153 
HIS CA    CB     sing N N 154 
HIS CA    HA     sing N N 155 
HIS C     O      doub N N 156 
HIS C     OXT    sing N N 157 
HIS CB    CG     sing N N 158 
HIS CB    HB2    sing N N 159 
HIS CB    HB3    sing N N 160 
HIS CG    ND1    sing Y N 161 
HIS CG    CD2    doub Y N 162 
HIS ND1   CE1    doub Y N 163 
HIS ND1   HD1    sing N N 164 
HIS CD2   NE2    sing Y N 165 
HIS CD2   HD2    sing N N 166 
HIS CE1   NE2    sing Y N 167 
HIS CE1   HE1    sing N N 168 
HIS NE2   HE2    sing N N 169 
HIS OXT   HXT    sing N N 170 
HOH O     H1     sing N N 171 
HOH O     H2     sing N N 172 
ILE N     CA     sing N N 173 
ILE N     H      sing N N 174 
ILE N     H2     sing N N 175 
ILE CA    C      sing N N 176 
ILE CA    CB     sing N N 177 
ILE CA    HA     sing N N 178 
ILE C     O      doub N N 179 
ILE C     OXT    sing N N 180 
ILE CB    CG1    sing N N 181 
ILE CB    CG2    sing N N 182 
ILE CB    HB     sing N N 183 
ILE CG1   CD1    sing N N 184 
ILE CG1   HG12   sing N N 185 
ILE CG1   HG13   sing N N 186 
ILE CG2   HG21   sing N N 187 
ILE CG2   HG22   sing N N 188 
ILE CG2   HG23   sing N N 189 
ILE CD1   HD11   sing N N 190 
ILE CD1   HD12   sing N N 191 
ILE CD1   HD13   sing N N 192 
ILE OXT   HXT    sing N N 193 
LEU N     CA     sing N N 194 
LEU N     H      sing N N 195 
LEU N     H2     sing N N 196 
LEU CA    C      sing N N 197 
LEU CA    CB     sing N N 198 
LEU CA    HA     sing N N 199 
LEU C     O      doub N N 200 
LEU C     OXT    sing N N 201 
LEU CB    CG     sing N N 202 
LEU CB    HB2    sing N N 203 
LEU CB    HB3    sing N N 204 
LEU CG    CD1    sing N N 205 
LEU CG    CD2    sing N N 206 
LEU CG    HG     sing N N 207 
LEU CD1   HD11   sing N N 208 
LEU CD1   HD12   sing N N 209 
LEU CD1   HD13   sing N N 210 
LEU CD2   HD21   sing N N 211 
LEU CD2   HD22   sing N N 212 
LEU CD2   HD23   sing N N 213 
LEU OXT   HXT    sing N N 214 
LYS N     CA     sing N N 215 
LYS N     H      sing N N 216 
LYS N     H2     sing N N 217 
LYS CA    C      sing N N 218 
LYS CA    CB     sing N N 219 
LYS CA    HA     sing N N 220 
LYS C     O      doub N N 221 
LYS C     OXT    sing N N 222 
LYS CB    CG     sing N N 223 
LYS CB    HB2    sing N N 224 
LYS CB    HB3    sing N N 225 
LYS CG    CD     sing N N 226 
LYS CG    HG2    sing N N 227 
LYS CG    HG3    sing N N 228 
LYS CD    CE     sing N N 229 
LYS CD    HD2    sing N N 230 
LYS CD    HD3    sing N N 231 
LYS CE    NZ     sing N N 232 
LYS CE    HE2    sing N N 233 
LYS CE    HE3    sing N N 234 
LYS NZ    HZ1    sing N N 235 
LYS NZ    HZ2    sing N N 236 
LYS NZ    HZ3    sing N N 237 
LYS OXT   HXT    sing N N 238 
MET N     CA     sing N N 239 
MET N     H      sing N N 240 
MET N     H2     sing N N 241 
MET CA    C      sing N N 242 
MET CA    CB     sing N N 243 
MET CA    HA     sing N N 244 
MET C     O      doub N N 245 
MET C     OXT    sing N N 246 
MET CB    CG     sing N N 247 
MET CB    HB2    sing N N 248 
MET CB    HB3    sing N N 249 
MET CG    SD     sing N N 250 
MET CG    HG2    sing N N 251 
MET CG    HG3    sing N N 252 
MET SD    CE     sing N N 253 
MET CE    HE1    sing N N 254 
MET CE    HE2    sing N N 255 
MET CE    HE3    sing N N 256 
MET OXT   HXT    sing N N 257 
PHE N     CA     sing N N 258 
PHE N     H      sing N N 259 
PHE N     H2     sing N N 260 
PHE CA    C      sing N N 261 
PHE CA    CB     sing N N 262 
PHE CA    HA     sing N N 263 
PHE C     O      doub N N 264 
PHE C     OXT    sing N N 265 
PHE CB    CG     sing N N 266 
PHE CB    HB2    sing N N 267 
PHE CB    HB3    sing N N 268 
PHE CG    CD1    doub Y N 269 
PHE CG    CD2    sing Y N 270 
PHE CD1   CE1    sing Y N 271 
PHE CD1   HD1    sing N N 272 
PHE CD2   CE2    doub Y N 273 
PHE CD2   HD2    sing N N 274 
PHE CE1   CZ     doub Y N 275 
PHE CE1   HE1    sing N N 276 
PHE CE2   CZ     sing Y N 277 
PHE CE2   HE2    sing N N 278 
PHE CZ    HZ     sing N N 279 
PHE OXT   HXT    sing N N 280 
PRO N     CA     sing N N 281 
PRO N     CD     sing N N 282 
PRO N     H      sing N N 283 
PRO CA    C      sing N N 284 
PRO CA    CB     sing N N 285 
PRO CA    HA     sing N N 286 
PRO C     O      doub N N 287 
PRO C     OXT    sing N N 288 
PRO CB    CG     sing N N 289 
PRO CB    HB2    sing N N 290 
PRO CB    HB3    sing N N 291 
PRO CG    CD     sing N N 292 
PRO CG    HG2    sing N N 293 
PRO CG    HG3    sing N N 294 
PRO CD    HD2    sing N N 295 
PRO CD    HD3    sing N N 296 
PRO OXT   HXT    sing N N 297 
SER N     CA     sing N N 298 
SER N     H      sing N N 299 
SER N     H2     sing N N 300 
SER CA    C      sing N N 301 
SER CA    CB     sing N N 302 
SER CA    HA     sing N N 303 
SER C     O      doub N N 304 
SER C     OXT    sing N N 305 
SER CB    OG     sing N N 306 
SER CB    HB2    sing N N 307 
SER CB    HB3    sing N N 308 
SER OG    HG     sing N N 309 
SER OXT   HXT    sing N N 310 
THR N     CA     sing N N 311 
THR N     H      sing N N 312 
THR N     H2     sing N N 313 
THR CA    C      sing N N 314 
THR CA    CB     sing N N 315 
THR CA    HA     sing N N 316 
THR C     O      doub N N 317 
THR C     OXT    sing N N 318 
THR CB    OG1    sing N N 319 
THR CB    CG2    sing N N 320 
THR CB    HB     sing N N 321 
THR OG1   HG1    sing N N 322 
THR CG2   HG21   sing N N 323 
THR CG2   HG22   sing N N 324 
THR CG2   HG23   sing N N 325 
THR OXT   HXT    sing N N 326 
TRP N     CA     sing N N 327 
TRP N     H      sing N N 328 
TRP N     H2     sing N N 329 
TRP CA    C      sing N N 330 
TRP CA    CB     sing N N 331 
TRP CA    HA     sing N N 332 
TRP C     O      doub N N 333 
TRP C     OXT    sing N N 334 
TRP CB    CG     sing N N 335 
TRP CB    HB2    sing N N 336 
TRP CB    HB3    sing N N 337 
TRP CG    CD1    doub Y N 338 
TRP CG    CD2    sing Y N 339 
TRP CD1   NE1    sing Y N 340 
TRP CD1   HD1    sing N N 341 
TRP CD2   CE2    doub Y N 342 
TRP CD2   CE3    sing Y N 343 
TRP NE1   CE2    sing Y N 344 
TRP NE1   HE1    sing N N 345 
TRP CE2   CZ2    sing Y N 346 
TRP CE3   CZ3    doub Y N 347 
TRP CE3   HE3    sing N N 348 
TRP CZ2   CH2    doub Y N 349 
TRP CZ2   HZ2    sing N N 350 
TRP CZ3   CH2    sing Y N 351 
TRP CZ3   HZ3    sing N N 352 
TRP CH2   HH2    sing N N 353 
TRP OXT   HXT    sing N N 354 
TYR N     CA     sing N N 355 
TYR N     H      sing N N 356 
TYR N     H2     sing N N 357 
TYR CA    C      sing N N 358 
TYR CA    CB     sing N N 359 
TYR CA    HA     sing N N 360 
TYR C     O      doub N N 361 
TYR C     OXT    sing N N 362 
TYR CB    CG     sing N N 363 
TYR CB    HB2    sing N N 364 
TYR CB    HB3    sing N N 365 
TYR CG    CD1    doub Y N 366 
TYR CG    CD2    sing Y N 367 
TYR CD1   CE1    sing Y N 368 
TYR CD1   HD1    sing N N 369 
TYR CD2   CE2    doub Y N 370 
TYR CD2   HD2    sing N N 371 
TYR CE1   CZ     doub Y N 372 
TYR CE1   HE1    sing N N 373 
TYR CE2   CZ     sing Y N 374 
TYR CE2   HE2    sing N N 375 
TYR CZ    OH     sing N N 376 
TYR OH    HH     sing N N 377 
TYR OXT   HXT    sing N N 378 
VAL N     CA     sing N N 379 
VAL N     H      sing N N 380 
VAL N     H2     sing N N 381 
VAL CA    C      sing N N 382 
VAL CA    CB     sing N N 383 
VAL CA    HA     sing N N 384 
VAL C     O      doub N N 385 
VAL C     OXT    sing N N 386 
VAL CB    CG1    sing N N 387 
VAL CB    CG2    sing N N 388 
VAL CB    HB     sing N N 389 
VAL CG1   HG11   sing N N 390 
VAL CG1   HG12   sing N N 391 
VAL CG1   HG13   sing N N 392 
VAL CG2   HG21   sing N N 393 
VAL CG2   HG22   sing N N 394 
VAL CG2   HG23   sing N N 395 
VAL OXT   HXT    sing N N 396 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 41' 
_space_group.name_Hall        'P 4w' 
_space_group.IT_number        76 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Y1Q 
_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]   0.016324 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016324 
_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]   0.008876 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . LYS A 1 3   ? 7.61971   52.91824 12.81819  1.000 158.78053 ? 3   LYS A N     1 
ATOM   2    C  CA    . LYS A 1 3   ? 6.27045   52.88313 12.26674  1.000 157.81404 ? 3   LYS A CA    1 
ATOM   3    C  C     . LYS A 1 3   ? 6.28589   52.48949 10.79417  1.000 155.37806 ? 3   LYS A C     1 
ATOM   4    O  O     . LYS A 1 3   ? 7.03822   53.05211 9.99903   1.000 161.65390 ? 3   LYS A O     1 
ATOM   5    C  CB    . LYS A 1 3   ? 5.58433   54.24127 12.43587  1.000 157.59550 ? 3   LYS A CB    1 
ATOM   6    C  CG    . LYS A 1 3   ? 4.19124   54.31742 11.82544  1.000 157.83086 ? 3   LYS A CG    1 
ATOM   7    C  CD    . LYS A 1 3   ? 3.21184   53.41763 12.56166  1.000 154.15004 ? 3   LYS A CD    1 
ATOM   8    C  CE    . LYS A 1 3   ? 3.08260   53.83058 14.01812  1.000 154.86073 ? 3   LYS A CE    1 
ATOM   9    N  NZ    . LYS A 1 3   ? 2.69182   55.26190 14.14597  1.000 149.89525 ? 3   LYS A NZ    1 
ATOM   10   N  N     . VAL A 1 4   ? 5.45410   51.51625 10.43828  1.000 148.48625 ? 4   VAL A N     1 
ATOM   11   C  CA    . VAL A 1 4   ? 5.27442   51.09783 9.05327   1.000 145.20515 ? 4   VAL A CA    1 
ATOM   12   C  C     . VAL A 1 4   ? 3.97963   51.70892 8.53776   1.000 145.11785 ? 4   VAL A C     1 
ATOM   13   O  O     . VAL A 1 4   ? 3.00803   51.86130 9.29002   1.000 148.92287 ? 4   VAL A O     1 
ATOM   14   C  CB    . VAL A 1 4   ? 5.26518   49.56092 8.93095   1.000 133.16186 ? 4   VAL A CB    1 
ATOM   15   C  CG1   . VAL A 1 4   ? 4.05033   48.97118 9.63170   1.000 128.13900 ? 4   VAL A CG1   1 
ATOM   16   C  CG2   . VAL A 1 4   ? 5.31756   49.13689 7.47026   1.000 123.97548 ? 4   VAL A CG2   1 
ATOM   17   N  N     . ILE A 1 5   ? 3.96573   52.08307 7.26090   1.000 128.67326 ? 5   ILE A N     1 
ATOM   18   C  CA    . ILE A 1 5   ? 2.82575   52.77612 6.67145   1.000 117.84636 ? 5   ILE A CA    1 
ATOM   19   C  C     . ILE A 1 5   ? 2.56824   52.21504 5.27956   1.000 116.55331 ? 5   ILE A C     1 
ATOM   20   O  O     . ILE A 1 5   ? 3.48618   52.12466 4.45813   1.000 115.11299 ? 5   ILE A O     1 
ATOM   21   C  CB    . ILE A 1 5   ? 3.05246   54.30199 6.61712   1.000 120.72094 ? 5   ILE A CB    1 
ATOM   22   C  CG1   . ILE A 1 5   ? 1.88958   54.99802 5.90490   1.000 118.72689 ? 5   ILE A CG1   1 
ATOM   23   C  CG2   . ILE A 1 5   ? 4.39054   54.63819 5.96014   1.000 118.57218 ? 5   ILE A CG2   1 
ATOM   24   C  CD1   . ILE A 1 5   ? 0.57894   54.92427 6.65583   1.000 115.62196 ? 5   ILE A CD1   1 
ATOM   25   N  N     . LEU A 1 6   ? 1.32312   51.82804 5.01912   1.000 114.73578 ? 6   LEU A N     1 
ATOM   26   C  CA    . LEU A 1 6   ? 0.88955   51.38781 3.70041   1.000 108.47303 ? 6   LEU A CA    1 
ATOM   27   C  C     . LEU A 1 6   ? -0.04556  52.43520 3.11464   1.000 108.79186 ? 6   LEU A C     1 
ATOM   28   O  O     . LEU A 1 6   ? -1.04492  52.80227 3.74211   1.000 112.94410 ? 6   LEU A O     1 
ATOM   29   C  CB    . LEU A 1 6   ? 0.19009   50.02850 3.76716   1.000 116.84562 ? 6   LEU A CB    1 
ATOM   30   C  CG    . LEU A 1 6   ? -0.33150  49.48488 2.43400   1.000 111.10218 ? 6   LEU A CG    1 
ATOM   31   C  CD1   . LEU A 1 6   ? 0.80668   49.27548 1.44379   1.000 102.48949 ? 6   LEU A CD1   1 
ATOM   32   C  CD2   . LEU A 1 6   ? -1.11442  48.19651 2.64108   1.000 104.74395 ? 6   LEU A CD2   1 
ATOM   33   N  N     . LYS A 1 7   ? 0.28392   52.91461 1.91982   1.000 109.96768 ? 7   LYS A N     1 
ATOM   34   C  CA    . LYS A 1 7   ? -0.46304  53.97205 1.25348   1.000 108.37215 ? 7   LYS A CA    1 
ATOM   35   C  C     . LYS A 1 7   ? -1.24671  53.37949 0.09043   1.000 106.28246 ? 7   LYS A C     1 
ATOM   36   O  O     . LYS A 1 7   ? -0.68765  52.64357 -0.73024  1.000 102.66035 ? 7   LYS A O     1 
ATOM   37   C  CB    . LYS A 1 7   ? 0.48422   55.07448 0.77406   1.000 105.12605 ? 7   LYS A CB    1 
ATOM   38   C  CG    . LYS A 1 7   ? 1.32806   55.65746 1.90198   1.000 107.31495 ? 7   LYS A CG    1 
ATOM   39   C  CD    . LYS A 1 7   ? 2.66296   56.19606 1.41224   1.000 114.72098 ? 7   LYS A CD    1 
ATOM   40   C  CE    . LYS A 1 7   ? 2.52230   57.55522 0.74968   1.000 106.19910 ? 7   LYS A CE    1 
ATOM   41   N  NZ    . LYS A 1 7   ? 3.85076   58.09878 0.34832   1.000 114.63554 ? 7   LYS A NZ    1 
ATOM   42   N  N     . ILE A 1 8   ? -2.53963  53.69361 0.02968   1.000 108.58546 ? 8   ILE A N     1 
ATOM   43   C  CA    . ILE A 1 8   ? -3.44833  53.12663 -0.95966  1.000 110.11871 ? 8   ILE A CA    1 
ATOM   44   C  C     . ILE A 1 8   ? -4.13976  54.26198 -1.69944  1.000 111.39777 ? 8   ILE A C     1 
ATOM   45   O  O     . ILE A 1 8   ? -4.64176  55.20271 -1.07438  1.000 117.07662 ? 8   ILE A O     1 
ATOM   46   C  CB    . ILE A 1 8   ? -4.49502  52.19455 -0.31541  1.000 100.64978 ? 8   ILE A CB    1 
ATOM   47   C  CG1   . ILE A 1 8   ? -3.82653  50.95965 0.29073   1.000 102.49438 ? 8   ILE A CG1   1 
ATOM   48   C  CG2   . ILE A 1 8   ? -5.55512  51.78422 -1.33036  1.000 104.60753 ? 8   ILE A CG2   1 
ATOM   49   C  CD1   . ILE A 1 8   ? -3.48004  51.10924 1.74712   1.000 110.91190 ? 8   ILE A CD1   1 
ATOM   50   N  N     . LYS A 1 9   ? -4.16245  54.17317 -3.02543  1.000 103.62707 ? 9   LYS A N     1 
ATOM   51   C  CA    . LYS A 1 9   ? -4.94412  55.06381 -3.87091  1.000 112.17571 ? 9   LYS A CA    1 
ATOM   52   C  C     . LYS A 1 9   ? -6.07400  54.26172 -4.50014  1.000 114.55550 ? 9   LYS A C     1 
ATOM   53   O  O     . LYS A 1 9   ? -5.82599  53.24024 -5.14933  1.000 116.93272 ? 9   LYS A O     1 
ATOM   54   C  CB    . LYS A 1 9   ? -4.07300  55.70326 -4.95420  1.000 117.92654 ? 9   LYS A CB    1 
ATOM   55   N  N     . ARG A 1 10  ? -7.30743  54.71460 -4.30104  1.000 117.22915 ? 10  ARG A N     1 
ATOM   56   C  CA    . ARG A 1 10  ? -8.48130  53.98900 -4.76410  1.000 117.94339 ? 10  ARG A CA    1 
ATOM   57   C  C     . ARG A 1 10  ? -9.02025  54.60865 -6.04599  1.000 124.42981 ? 10  ARG A C     1 
ATOM   58   O  O     . ARG A 1 10  ? -9.01143  55.83211 -6.21095  1.000 130.61235 ? 10  ARG A O     1 
ATOM   59   C  CB    . ARG A 1 10  ? -9.57426  53.97168 -3.69428  1.000 125.76649 ? 10  ARG A CB    1 
ATOM   60   C  CG    . ARG A 1 10  ? -9.17551  53.26671 -2.40923  1.000 127.26814 ? 10  ARG A CG    1 
ATOM   61   C  CD    . ARG A 1 10  ? -10.40392 52.91031 -1.59231  1.000 131.54848 ? 10  ARG A CD    1 
ATOM   62   N  NE    . ARG A 1 10  ? -11.20831 54.08612 -1.28383  1.000 129.11647 ? 10  ARG A NE    1 
ATOM   63   C  CZ    . ARG A 1 10  ? -12.46123 54.04482 -0.85186  1.000 137.76837 ? 10  ARG A CZ    1 
ATOM   64   N  NH1   . ARG A 1 10  ? -13.09777 52.89694 -0.68551  1.000 140.85351 ? 10  ARG A NH1   1 
ATOM   65   N  NH2   . ARG A 1 10  ? -13.09309 55.18419 -0.58447  1.000 141.72437 ? 10  ARG A NH2   1 
ATOM   66   N  N     . LEU A 1 11  ? -9.49099  53.75292 -6.94898  1.000 128.91391 ? 11  LEU A N     1 
ATOM   67   C  CA    . LEU A 1 11  ? -10.02493 54.16538 -8.23515  1.000 130.12155 ? 11  LEU A CA    1 
ATOM   68   C  C     . LEU A 1 11  ? -11.53518 54.33986 -8.15239  1.000 142.28779 ? 11  LEU A C     1 
ATOM   69   O  O     . LEU A 1 11  ? -12.17904 53.82601 -7.23167  1.000 141.55525 ? 11  LEU A O     1 
ATOM   70   C  CB    . LEU A 1 11  ? -9.66512  53.13403 -9.30445  1.000 131.10271 ? 11  LEU A CB    1 
ATOM   71   C  CG    . LEU A 1 11  ? -8.18424  52.74763 -9.38638  1.000 122.55922 ? 11  LEU A CG    1 
ATOM   72   C  CD1   . LEU A 1 11  ? -7.90575  51.84220 -10.58137 1.000 109.62537 ? 11  LEU A CD1   1 
ATOM   73   C  CD2   . LEU A 1 11  ? -7.29711  53.98471 -9.42665  1.000 123.25739 ? 11  LEU A CD2   1 
ATOM   74   N  N     . PRO A 1 12  ? -12.12440 55.08942 -9.09433  1.000 154.54846 ? 12  PRO A N     1 
ATOM   75   C  CA    . PRO A 1 12  ? -13.58077 55.31976 -9.05981  1.000 158.90248 ? 12  PRO A CA    1 
ATOM   76   C  C     . PRO A 1 12  ? -14.41917 54.06706 -8.84422  1.000 156.96118 ? 12  PRO A C     1 
ATOM   77   O  O     . PRO A 1 12  ? -15.38825 54.10999 -8.07716  1.000 159.26970 ? 12  PRO A O     1 
ATOM   78   C  CB    . PRO A 1 12  ? -13.85969 55.95003 -10.43269 1.000 163.76617 ? 12  PRO A CB    1 
ATOM   79   C  CG    . PRO A 1 12  ? -12.53929 56.50301 -10.90923 1.000 162.61187 ? 12  PRO A CG    1 
ATOM   80   C  CD    . PRO A 1 12  ? -11.44055 56.02265 -10.00498 1.000 157.89448 ? 12  PRO A CD    1 
ATOM   81   N  N     . HIS A 1 13  ? -14.07647 52.94959 -9.48414  1.000 145.60074 ? 13  HIS A N     1 
ATOM   82   C  CA    . HIS A 1 13  ? -14.86860 51.73530 -9.32506  1.000 137.95129 ? 13  HIS A CA    1 
ATOM   83   C  C     . HIS A 1 13  ? -14.62096 51.02854 -7.99734  1.000 134.47833 ? 13  HIS A C     1 
ATOM   84   O  O     . HIS A 1 13  ? -15.16443 49.93905 -7.78712  1.000 136.08776 ? 13  HIS A O     1 
ATOM   85   C  CB    . HIS A 1 13  ? -14.60310 50.76706 -10.48300 1.000 132.81982 ? 13  HIS A CB    1 
ATOM   86   C  CG    . HIS A 1 13  ? -13.20907 50.22211 -10.51366 1.000 133.57161 ? 13  HIS A CG    1 
ATOM   87   N  ND1   . HIS A 1 13  ? -12.90300 48.99306 -11.05757 1.000 123.38035 ? 13  HIS A ND1   1 
ATOM   88   C  CD2   . HIS A 1 13  ? -12.03842 50.74046 -10.07423 1.000 131.52505 ? 13  HIS A CD2   1 
ATOM   89   C  CE1   . HIS A 1 13  ? -11.60468 48.77652 -10.94814 1.000 111.67166 ? 13  HIS A CE1   1 
ATOM   90   N  NE2   . HIS A 1 13  ? -11.05689 49.82250 -10.35684 1.000 114.79867 ? 13  HIS A NE2   1 
ATOM   91   N  N     . ALA A 1 14  ? -13.82207 51.61463 -7.10327  1.000 135.59873 ? 14  ALA A N     1 
ATOM   92   C  CA    . ALA A 1 14  ? -13.57938 51.06077 -5.77673  1.000 133.95636 ? 14  ALA A CA    1 
ATOM   93   C  C     . ALA A 1 14  ? -13.66914 52.14162 -4.70711  1.000 141.16800 ? 14  ALA A C     1 
ATOM   94   O  O     . ALA A 1 14  ? -13.04412 52.02984 -3.64851  1.000 136.57602 ? 14  ALA A O     1 
ATOM   95   C  CB    . ALA A 1 14  ? -12.22436 50.35987 -5.71095  1.000 122.71011 ? 14  ALA A CB    1 
ATOM   96   N  N     . GLN A 1 15  ? -14.44116 53.19648 -4.97101  1.000 139.40854 ? 15  GLN A N     1 
ATOM   97   C  CA    . GLN A 1 15  ? -14.57608 54.30266 -4.03284  1.000 140.42063 ? 15  GLN A CA    1 
ATOM   98   C  C     . GLN A 1 15  ? -15.68919 54.09282 -3.01430  1.000 150.40767 ? 15  GLN A C     1 
ATOM   99   O  O     . GLN A 1 15  ? -15.67538 54.74532 -1.96334  1.000 150.65760 ? 15  GLN A O     1 
ATOM   100  C  CB    . GLN A 1 15  ? -14.82808 55.61059 -4.79110  1.000 149.53060 ? 15  GLN A CB    1 
ATOM   101  C  CG    . GLN A 1 15  ? -14.35612 56.85446 -4.05940  1.000 150.12543 ? 15  GLN A CG    1 
ATOM   102  C  CD    . GLN A 1 15  ? -12.90227 57.17226 -4.34119  1.000 149.16048 ? 15  GLN A CD    1 
ATOM   103  O  OE1   . GLN A 1 15  ? -12.58368 57.84066 -5.32433  1.000 148.19997 ? 15  GLN A OE1   1 
ATOM   104  N  NE2   . GLN A 1 15  ? -12.01067 56.69205 -3.48157  1.000 140.94647 ? 15  GLN A NE2   1 
ATOM   105  N  N     . ASP A 1 16  ? -16.64698 53.20300 -3.29451  1.000 163.22185 ? 16  ASP A N     1 
ATOM   106  C  CA    . ASP A 1 16  ? -17.74500 52.93172 -2.37274  1.000 162.39386 ? 16  ASP A CA    1 
ATOM   107  C  C     . ASP A 1 16  ? -17.48006 51.76052 -1.43457  1.000 154.58476 ? 16  ASP A C     1 
ATOM   108  O  O     . ASP A 1 16  ? -18.13579 51.66818 -0.39089  1.000 150.20481 ? 16  ASP A O     1 
ATOM   109  C  CB    . ASP A 1 16  ? -19.04634 52.66266 -3.14714  1.000 164.87906 ? 16  ASP A CB    1 
ATOM   110  C  CG    . ASP A 1 16  ? -19.11521 51.25094 -3.71391  1.000 170.99534 ? 16  ASP A CG    1 
ATOM   111  O  OD1   . ASP A 1 16  ? -18.09838 50.77297 -4.25473  1.000 168.46078 ? 16  ASP A OD1   1 
ATOM   112  O  OD2   . ASP A 1 16  ? -20.18969 50.61770 -3.61631  1.000 179.22733 ? 16  ASP A OD2   1 
ATOM   113  N  N     . LEU A 1 17  ? -16.55353 50.86670 -1.77517  1.000 152.07260 ? 17  LEU A N     1 
ATOM   114  C  CA    . LEU A 1 17  ? -16.23678 49.76135 -0.88572  1.000 148.77699 ? 17  LEU A CA    1 
ATOM   115  C  C     . LEU A 1 17  ? -15.50378 50.27393 0.35385   1.000 149.05426 ? 17  LEU A C     1 
ATOM   116  O  O     . LEU A 1 17  ? -14.86051 51.32700 0.31436   1.000 148.34439 ? 17  LEU A O     1 
ATOM   117  C  CB    . LEU A 1 17  ? -15.36970 48.72019 -1.59273  1.000 143.57663 ? 17  LEU A CB    1 
ATOM   118  C  CG    . LEU A 1 17  ? -15.95790 47.92696 -2.76159  1.000 144.53447 ? 17  LEU A CG    1 
ATOM   119  C  CD1   . LEU A 1 17  ? -17.43971 47.65843 -2.54320  1.000 144.57040 ? 17  LEU A CD1   1 
ATOM   120  C  CD2   . LEU A 1 17  ? -15.71269 48.62800 -4.08945  1.000 143.18809 ? 17  LEU A CD2   1 
ATOM   121  N  N     . PRO A 1 18  ? -15.59473 49.55634 1.47178   1.000 147.49742 ? 18  PRO A N     1 
ATOM   122  C  CA    . PRO A 1 18  ? -14.77165 49.91041 2.63157   1.000 143.94933 ? 18  PRO A CA    1 
ATOM   123  C  C     . PRO A 1 18  ? -13.29531 49.72106 2.32398   1.000 137.73018 ? 18  PRO A C     1 
ATOM   124  O  O     . PRO A 1 18  ? -12.90544 48.84220 1.55145   1.000 140.56560 ? 18  PRO A O     1 
ATOM   125  C  CB    . PRO A 1 18  ? -15.24388 48.93718 3.71856   1.000 143.55010 ? 18  PRO A CB    1 
ATOM   126  C  CG    . PRO A 1 18  ? -16.58818 48.46788 3.26775   1.000 142.19684 ? 18  PRO A CG    1 
ATOM   127  C  CD    . PRO A 1 18  ? -16.52260 48.45245 1.77015   1.000 142.04996 ? 18  PRO A CD    1 
ATOM   128  N  N     . LEU A 1 19  ? -12.47023 50.56874 2.93298   1.000 134.32761 ? 19  LEU A N     1 
ATOM   129  C  CA    . LEU A 1 19  ? -11.03314 50.44357 2.75673   1.000 127.50578 ? 19  LEU A CA    1 
ATOM   130  C  C     . LEU A 1 19  ? -10.55752 49.10416 3.31871   1.000 127.41532 ? 19  LEU A C     1 
ATOM   131  O  O     . LEU A 1 19  ? -11.16316 48.56411 4.24993   1.000 131.37919 ? 19  LEU A O     1 
ATOM   132  C  CB    . LEU A 1 19  ? -10.29834 51.58989 3.45059   1.000 124.84962 ? 19  LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 19  ? -10.64562 53.01979 3.03256   1.000 139.03405 ? 19  LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 19  ? -11.70686 53.61418 3.95009   1.000 118.52203 ? 19  LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 19  ? -9.39651  53.88605 3.01250   1.000 135.77614 ? 19  LEU A CD2   1 
ATOM   136  N  N     . PRO A 1 20  ? -9.48888  48.53561 2.76199   1.000 117.84603 ? 20  PRO A N     1 
ATOM   137  C  CA    . PRO A 1 20  ? -8.94395  47.29496 3.32772   1.000 119.39251 ? 20  PRO A CA    1 
ATOM   138  C  C     . PRO A 1 20  ? -8.51259  47.50085 4.77259   1.000 114.64966 ? 20  PRO A C     1 
ATOM   139  O  O     . PRO A 1 20  ? -7.79205  48.44766 5.09672   1.000 113.34635 ? 20  PRO A O     1 
ATOM   140  C  CB    . PRO A 1 20  ? -7.75368  46.97897 2.41374   1.000 116.23273 ? 20  PRO A CB    1 
ATOM   141  C  CG    . PRO A 1 20  ? -7.42460  48.27739 1.74306   1.000 106.97349 ? 20  PRO A CG    1 
ATOM   142  C  CD    . PRO A 1 20  ? -8.73737  48.97478 1.57487   1.000 111.40990 ? 20  PRO A CD    1 
ATOM   143  N  N     . SER A 1 21  ? -8.97344  46.60818 5.64506   1.000 113.75569 ? 21  SER A N     1 
ATOM   144  C  CA    . SER A 1 21  ? -8.71318  46.72685 7.07109   1.000 110.50502 ? 21  SER A CA    1 
ATOM   145  C  C     . SER A 1 21  ? -8.59861  45.33431 7.67382   1.000 103.55880 ? 21  SER A C     1 
ATOM   146  O  O     . SER A 1 21  ? -8.82904  44.32229 7.00710   1.000 97.43673  ? 21  SER A O     1 
ATOM   147  C  CB    . SER A 1 21  ? -9.80838  47.53924 7.77021   1.000 101.27252 ? 21  SER A CB    1 
ATOM   148  O  OG    . SER A 1 21  ? -11.09226 47.01012 7.48797   1.000 96.47648  ? 21  SER A OG    1 
ATOM   149  N  N     . TYR A 1 22  ? -8.23228  45.29543 8.95215   1.000 106.28925 ? 22  TYR A N     1 
ATOM   150  C  CA    . TYR A 1 22  ? -8.09941  44.04355 9.68331   1.000 102.51327 ? 22  TYR A CA    1 
ATOM   151  C  C     . TYR A 1 22  ? -9.40097  43.73498 10.41236  1.000 99.09848  ? 22  TYR A C     1 
ATOM   152  O  O     . TYR A 1 22  ? -9.94996  44.59576 11.10805  1.000 107.44318 ? 22  TYR A O     1 
ATOM   153  C  CB    . TYR A 1 22  ? -6.93806  44.11667 10.67578  1.000 100.21277 ? 22  TYR A CB    1 
ATOM   154  C  CG    . TYR A 1 22  ? -5.59662  44.39791 10.03547  1.000 98.36987  ? 22  TYR A CG    1 
ATOM   155  C  CD1   . TYR A 1 22  ? -4.87571  43.38577 9.41481   1.000 89.59476  ? 22  TYR A CD1   1 
ATOM   156  C  CD2   . TYR A 1 22  ? -5.04839  45.67449 10.05785  1.000 98.70972  ? 22  TYR A CD2   1 
ATOM   157  C  CE1   . TYR A 1 22  ? -3.64774  43.63779 8.82946   1.000 90.81516  ? 22  TYR A CE1   1 
ATOM   158  C  CE2   . TYR A 1 22  ? -3.82099  45.93692 9.47620   1.000 99.25358  ? 22  TYR A CE2   1 
ATOM   159  C  CZ    . TYR A 1 22  ? -3.12479  44.91464 8.86354   1.000 94.77611  ? 22  TYR A CZ    1 
ATOM   160  O  OH    . TYR A 1 22  ? -1.90328  45.17005 8.28254   1.000 87.13731  ? 22  TYR A OH    1 
ATOM   161  N  N     . ALA A 1 23  ? -9.89245  42.50407 10.24703  1.000 92.50147  ? 23  ALA A N     1 
ATOM   162  C  CA    . ALA A 1 23  ? -11.13602 42.11066 10.90115  1.000 102.57828 ? 23  ALA A CA    1 
ATOM   163  C  C     . ALA A 1 23  ? -10.97248 42.01321 12.41239  1.000 97.76453  ? 23  ALA A C     1 
ATOM   164  O  O     . ALA A 1 23  ? -11.95229 42.16313 13.15094  1.000 95.95901  ? 23  ALA A O     1 
ATOM   165  C  CB    . ALA A 1 23  ? -11.63205 40.78038 10.33323  1.000 92.11353  ? 23  ALA A CB    1 
ATOM   166  N  N     . THR A 1 24  ? -9.75165  41.76877 12.88877  1.000 96.91678  ? 24  THR A N     1 
ATOM   167  C  CA    . THR A 1 24  ? -9.45779  41.64948 14.30758  1.000 99.98049  ? 24  THR A CA    1 
ATOM   168  C  C     . THR A 1 24  ? -8.11938  42.32858 14.56740  1.000 103.07208 ? 24  THR A C     1 
ATOM   169  O  O     . THR A 1 24  ? -7.22875  42.28395 13.70526  1.000 100.00910 ? 24  THR A O     1 
ATOM   170  C  CB    . THR A 1 24  ? -9.40345  40.17845 14.75335  1.000 99.24546  ? 24  THR A CB    1 
ATOM   171  O  OG1   . THR A 1 24  ? -10.56564 39.49071 14.27352  1.000 99.78097  ? 24  THR A OG1   1 
ATOM   172  C  CG2   . THR A 1 24  ? -9.35907  40.06667 16.27023  1.000 111.93241 ? 24  THR A CG2   1 
ATOM   173  N  N     . PRO A 1 25  ? -7.95895  42.99439 15.72686  1.000 107.39091 ? 25  PRO A N     1 
ATOM   174  C  CA    . PRO A 1 25  ? -6.67010  43.61976 16.06427  1.000 106.80307 ? 25  PRO A CA    1 
ATOM   175  C  C     . PRO A 1 25  ? -5.44636  42.74364 15.82358  1.000 106.93597 ? 25  PRO A C     1 
ATOM   176  O  O     . PRO A 1 25  ? -4.34238  43.26366 15.63308  1.000 101.87327 ? 25  PRO A O     1 
ATOM   177  C  CB    . PRO A 1 25  ? -6.82654  43.94016 17.55698  1.000 111.99121 ? 25  PRO A CB    1 
ATOM   178  C  CG    . PRO A 1 25  ? -8.32400  44.00056 17.80516  1.000 105.16199 ? 25  PRO A CG    1 
ATOM   179  C  CD    . PRO A 1 25  ? -9.04544  43.51661 16.57178  1.000 104.43782 ? 25  PRO A CD    1 
ATOM   180  N  N     . HIS A 1 26  ? -5.61893  41.42079 15.82958  1.000 116.64276 ? 26  HIS A N     1 
ATOM   181  C  CA    . HIS A 1 26  ? -4.52444  40.49345 15.57244  1.000 116.59097 ? 26  HIS A CA    1 
ATOM   182  C  C     . HIS A 1 26  ? -4.69664  39.73700 14.25744  1.000 120.03225 ? 26  HIS A C     1 
ATOM   183  O  O     . HIS A 1 26  ? -4.10014  38.67039 14.07855  1.000 117.79012 ? 26  HIS A O     1 
ATOM   184  C  CB    . HIS A 1 26  ? -4.37429  39.51135 16.73550  1.000 116.34642 ? 26  HIS A CB    1 
ATOM   185  C  CG    . HIS A 1 26  ? -4.00090  40.16108 18.03239  1.000 123.28972 ? 26  HIS A CG    1 
ATOM   186  N  ND1   . HIS A 1 26  ? -4.89591  40.32627 19.06760  1.000 129.17121 ? 26  HIS A ND1   1 
ATOM   187  C  CD2   . HIS A 1 26  ? -2.82945  40.68851 18.46086  1.000 128.38749 ? 26  HIS A CD2   1 
ATOM   188  C  CE1   . HIS A 1 26  ? -4.29181  40.92564 20.07821  1.000 138.15912 ? 26  HIS A CE1   1 
ATOM   189  N  NE2   . HIS A 1 26  ? -3.03729  41.15687 19.73563  1.000 136.81554 ? 26  HIS A NE2   1 
ATOM   190  N  N     . SER A 1 27  ? -5.49905  40.26304 13.33463  1.000 108.88976 ? 27  SER A N     1 
ATOM   191  C  CA    . SER A 1 27  ? -5.63628  39.63698 12.02670  1.000 96.11721  ? 27  SER A CA    1 
ATOM   192  C  C     . SER A 1 27  ? -4.37982  39.86599 11.19787  1.000 94.70163  ? 27  SER A C     1 
ATOM   193  O  O     . SER A 1 27  ? -3.76299  40.93296 11.25392  1.000 97.34917  ? 27  SER A O     1 
ATOM   194  C  CB    . SER A 1 27  ? -6.85944  40.18536 11.29267  1.000 92.35159  ? 27  SER A CB    1 
ATOM   195  O  OG    . SER A 1 27  ? -8.05973  39.70479 11.87048  1.000 103.61714 ? 27  SER A OG    1 
ATOM   196  N  N     . SER A 1 28  ? -4.00225  38.85224 10.41960  1.000 95.00918  ? 28  SER A N     1 
ATOM   197  C  CA    . SER A 1 28  ? -2.75030  38.91947 9.67459   1.000 92.02546  ? 28  SER A CA    1 
ATOM   198  C  C     . SER A 1 28  ? -2.90350  39.69617 8.37223   1.000 88.36685  ? 28  SER A C     1 
ATOM   199  O  O     . SER A 1 28  ? -2.00084  40.44387 7.98618   1.000 86.66077  ? 28  SER A O     1 
ATOM   200  C  CB    . SER A 1 28  ? -2.23359  37.50600 9.40051   1.000 88.34801  ? 28  SER A CB    1 
ATOM   201  O  OG    . SER A 1 28  ? -0.98606  37.54035 8.73128   1.000 91.69261  ? 28  SER A OG    1 
ATOM   202  N  N     . GLY A 1 29  ? -4.03030  39.54180 7.68647   1.000 95.52830  ? 29  GLY A N     1 
ATOM   203  C  CA    . GLY A 1 29  ? -4.20528  40.09990 6.36038   1.000 97.78350  ? 29  GLY A CA    1 
ATOM   204  C  C     . GLY A 1 29  ? -5.41219  41.01097 6.26302   1.000 97.86070  ? 29  GLY A C     1 
ATOM   205  O  O     . GLY A 1 29  ? -6.41064  40.82183 6.95747   1.000 94.33577  ? 29  GLY A O     1 
ATOM   206  N  N     . LEU A 1 30  ? -5.31536  41.99321 5.37189   1.000 88.39536  ? 30  LEU A N     1 
ATOM   207  C  CA    . LEU A 1 30  ? -6.42028  42.89419 5.08528   1.000 90.25119  ? 30  LEU A CA    1 
ATOM   208  C  C     . LEU A 1 30  ? -7.39960  42.23942 4.12232   1.000 91.83336  ? 30  LEU A C     1 
ATOM   209  O  O     . LEU A 1 30  ? -7.03063  41.37375 3.32534   1.000 92.25279  ? 30  LEU A O     1 
ATOM   210  C  CB    . LEU A 1 30  ? -5.90381  44.19628 4.47435   1.000 96.65556  ? 30  LEU A CB    1 
ATOM   211  C  CG    . LEU A 1 30  ? -4.77155  44.92154 5.20183   1.000 96.62686  ? 30  LEU A CG    1 
ATOM   212  C  CD1   . LEU A 1 30  ? -4.00280  45.80679 4.23647   1.000 95.59703  ? 30  LEU A CD1   1 
ATOM   213  C  CD2   . LEU A 1 30  ? -5.32482  45.74335 6.34534   1.000 98.75309  ? 30  LEU A CD2   1 
ATOM   214  N  N     . ASP A 1 31  ? -8.65596  42.67041 4.19102   1.000 98.49156  ? 31  ASP A N     1 
ATOM   215  C  CA    . ASP A 1 31  ? -9.66561  42.13766 3.28708   1.000 99.03059  ? 31  ASP A CA    1 
ATOM   216  C  C     . ASP A 1 31  ? -9.48585  42.70725 1.88557   1.000 104.35741 ? 31  ASP A C     1 
ATOM   217  O  O     . ASP A 1 31  ? -9.26681  43.90936 1.70819   1.000 103.25750 ? 31  ASP A O     1 
ATOM   218  C  CB    . ASP A 1 31  ? -11.06851 42.44744 3.80675   1.000 105.01526 ? 31  ASP A CB    1 
ATOM   219  C  CG    . ASP A 1 31  ? -11.28609 43.92689 4.06808   1.000 124.48029 ? 31  ASP A CG    1 
ATOM   220  O  OD1   . ASP A 1 31  ? -11.54798 44.67822 3.10293   1.000 121.30979 ? 31  ASP A OD1   1 
ATOM   221  O  OD2   . ASP A 1 31  ? -11.19379 44.33798 5.24463   1.000 122.26185 ? 31  ASP A OD2   1 
ATOM   222  N  N     . LEU A 1 32  ? -9.57272  41.82954 0.88817   1.000 95.39156  ? 32  LEU A N     1 
ATOM   223  C  CA    . LEU A 1 32  ? -9.51635  42.20959 -0.51847  1.000 88.55161  ? 32  LEU A CA    1 
ATOM   224  C  C     . LEU A 1 32  ? -10.87504 41.94128 -1.14998  1.000 93.42865  ? 32  LEU A C     1 
ATOM   225  O  O     . LEU A 1 32  ? -11.37296 40.81153 -1.10197  1.000 93.45570  ? 32  LEU A O     1 
ATOM   226  C  CB    . LEU A 1 32  ? -8.41615  41.44985 -1.26144  1.000 89.55463  ? 32  LEU A CB    1 
ATOM   227  C  CG    . LEU A 1 32  ? -6.98849  41.95706 -1.05679  1.000 94.78630  ? 32  LEU A CG    1 
ATOM   228  C  CD1   . LEU A 1 32  ? -6.02466  41.20154 -1.95818  1.000 84.21862  ? 32  LEU A CD1   1 
ATOM   229  C  CD2   . LEU A 1 32  ? -6.91274  43.45513 -1.31738  1.000 69.80836  ? 32  LEU A CD2   1 
ATOM   230  N  N     . ARG A 1 33  ? -11.46703 42.97792 -1.73772  1.000 87.90287  ? 33  ARG A N     1 
ATOM   231  C  CA    . ARG A 1 33  ? -12.82403 42.92739 -2.25617  1.000 104.60049 ? 33  ARG A CA    1 
ATOM   232  C  C     . ARG A 1 33  ? -12.82503 43.08543 -3.77079  1.000 99.67765  ? 33  ARG A C     1 
ATOM   233  O  O     . ARG A 1 33  ? -11.94346 43.72903 -4.34880  1.000 94.85783  ? 33  ARG A O     1 
ATOM   234  C  CB    . ARG A 1 33  ? -13.68671 44.01669 -1.61186  1.000 106.32243 ? 33  ARG A CB    1 
ATOM   235  C  CG    . ARG A 1 33  ? -13.74088 43.92093 -0.09559  1.000 96.66839  ? 33  ARG A CG    1 
ATOM   236  C  CD    . ARG A 1 33  ? -14.44130 45.11594 0.51906   1.000 105.94059 ? 33  ARG A CD    1 
ATOM   237  N  NE    . ARG A 1 33  ? -14.77270 44.87473 1.91746   1.000 115.69143 ? 33  ARG A NE    1 
ATOM   238  C  CZ    . ARG A 1 33  ? -15.87716 44.26581 2.32621   1.000 116.89939 ? 33  ARG A CZ    1 
ATOM   239  N  NH1   . ARG A 1 33  ? -16.78011 43.82285 1.46653   1.000 112.98767 ? 33  ARG A NH1   1 
ATOM   240  N  NH2   . ARG A 1 33  ? -16.08150 44.09781 3.62951   1.000 118.49825 ? 33  ARG A NH2   1 
ATOM   241  N  N     . ALA A 1 34  ? -13.83366 42.49333 -4.40529  1.000 104.30425 ? 34  ALA A N     1 
ATOM   242  C  CA    . ALA A 1 34  ? -13.96818 42.50868 -5.85722  1.000 106.73484 ? 34  ALA A CA    1 
ATOM   243  C  C     . ALA A 1 34  ? -14.71382 43.77120 -6.27226  1.000 106.91309 ? 34  ALA A C     1 
ATOM   244  O  O     . ALA A 1 34  ? -15.93181 43.86989 -6.09109  1.000 108.72538 ? 34  ALA A O     1 
ATOM   245  C  CB    . ALA A 1 34  ? -14.69603 41.25686 -6.33854  1.000 98.29603  ? 34  ALA A CB    1 
ATOM   246  N  N     . ALA A 1 35  ? -13.98337 44.73409 -6.83636  1.000 103.14996 ? 35  ALA A N     1 
ATOM   247  C  CA    . ALA A 1 35  ? -14.57448 45.98795 -7.30323  1.000 116.27326 ? 35  ALA A CA    1 
ATOM   248  C  C     . ALA A 1 35  ? -15.08148 45.78051 -8.72713  1.000 113.64180 ? 35  ALA A C     1 
ATOM   249  O  O     . ALA A 1 35  ? -14.48833 46.22795 -9.71094  1.000 111.10061 ? 35  ALA A O     1 
ATOM   250  C  CB    . ALA A 1 35  ? -13.56314 47.12360 -7.21894  1.000 116.92352 ? 35  ALA A CB    1 
ATOM   251  N  N     . ILE A 1 36  ? -16.20857 45.07791 -8.82878  1.000 114.74578 ? 36  ILE A N     1 
ATOM   252  C  CA    . ILE A 1 36  ? -16.81365 44.76744 -10.11884 1.000 118.60759 ? 36  ILE A CA    1 
ATOM   253  C  C     . ILE A 1 36  ? -18.19656 45.40025 -10.19307 1.000 128.65771 ? 36  ILE A C     1 
ATOM   254  O  O     . ILE A 1 36  ? -18.60795 46.12932 -9.28347  1.000 121.76473 ? 36  ILE A O     1 
ATOM   255  C  CB    . ILE A 1 36  ? -16.88574 43.24657 -10.34850 1.000 119.33162 ? 36  ILE A CB    1 
ATOM   256  C  CG1   . ILE A 1 36  ? -17.71693 42.57769 -9.25187  1.000 123.25589 ? 36  ILE A CG1   1 
ATOM   257  C  CG2   . ILE A 1 36  ? -15.48836 42.65010 -10.39528 1.000 107.57561 ? 36  ILE A CG2   1 
ATOM   258  C  CD1   . ILE A 1 36  ? -17.78201 41.06858 -9.36853  1.000 113.69969 ? 36  ILE A CD1   1 
ATOM   259  N  N     . GLU A 1 37  ? -18.92122 45.12609 -11.27799 1.000 150.76724 ? 37  GLU A N     1 
ATOM   260  C  CA    . GLU A 1 37  ? -20.25456 45.67967 -11.49296 1.000 151.31977 ? 37  GLU A CA    1 
ATOM   261  C  C     . GLU A 1 37  ? -21.31716 44.59574 -11.35042 1.000 158.43475 ? 37  GLU A C     1 
ATOM   262  O  O     . GLU A 1 37  ? -22.10453 44.62454 -10.40194 1.000 156.46460 ? 37  GLU A O     1 
ATOM   263  C  CB    . GLU A 1 37  ? -20.33243 46.35498 -12.86474 1.000 155.23655 ? 37  GLU A CB    1 
ATOM   264  N  N     . LYS A 1 38  ? -21.36389 43.64134 -12.26798 1.000 146.43199 ? 38  LYS A N     1 
ATOM   265  C  CA    . LYS A 1 38  ? -22.30329 42.53067 -12.21125 1.000 139.39071 ? 38  LYS A CA    1 
ATOM   266  C  C     . LYS A 1 38  ? -21.66139 41.34504 -11.50820 1.000 139.13999 ? 38  LYS A C     1 
ATOM   267  O  O     . LYS A 1 38  ? -20.45038 41.32371 -11.27688 1.000 124.02771 ? 38  LYS A O     1 
ATOM   268  C  CB    . LYS A 1 38  ? -22.74057 42.16203 -13.62770 1.000 126.77897 ? 38  LYS A CB    1 
ATOM   269  N  N     . PRO A 1 39  ? -22.44752 40.33422 -11.13180 1.000 140.20510 ? 39  PRO A N     1 
ATOM   270  C  CA    . PRO A 1 39  ? -21.85294 39.11482 -10.56945 1.000 132.67317 ? 39  PRO A CA    1 
ATOM   271  C  C     . PRO A 1 39  ? -20.95741 38.41512 -11.58169 1.000 128.97902 ? 39  PRO A C     1 
ATOM   272  O  O     . PRO A 1 39  ? -20.96751 38.70450 -12.77993 1.000 129.50153 ? 39  PRO A O     1 
ATOM   273  C  CB    . PRO A 1 39  ? -23.06870 38.25514 -10.20163 1.000 135.58385 ? 39  PRO A CB    1 
ATOM   274  C  CG    . PRO A 1 39  ? -24.20827 38.83436 -10.98229 1.000 134.04211 ? 39  PRO A CG    1 
ATOM   275  C  CD    . PRO A 1 39  ? -23.91857 40.29922 -11.05856 1.000 134.10936 ? 39  PRO A CD    1 
ATOM   276  N  N     . LEU A 1 40  ? -20.16500 37.47306 -11.07782 1.000 127.77454 ? 40  LEU A N     1 
ATOM   277  C  CA    . LEU A 1 40  ? -19.21027 36.72667 -11.88656 1.000 125.37147 ? 40  LEU A CA    1 
ATOM   278  C  C     . LEU A 1 40  ? -19.69155 35.29276 -12.05495 1.000 128.39065 ? 40  LEU A C     1 
ATOM   279  O  O     . LEU A 1 40  ? -19.97798 34.60912 -11.06634 1.000 132.64868 ? 40  LEU A O     1 
ATOM   280  C  CB    . LEU A 1 40  ? -17.81902 36.74417 -11.24915 1.000 120.60307 ? 40  LEU A CB    1 
ATOM   281  N  N     . LYS A 1 41  ? -19.77610 34.84194 -13.30574 1.000 132.93501 ? 41  LYS A N     1 
ATOM   282  C  CA    . LYS A 1 41  ? -20.18925 33.47411 -13.61857 1.000 135.88244 ? 41  LYS A CA    1 
ATOM   283  C  C     . LYS A 1 41  ? -18.94260 32.59909 -13.63123 1.000 132.68061 ? 41  LYS A C     1 
ATOM   284  O  O     . LYS A 1 41  ? -18.29220 32.41607 -14.66154 1.000 128.17412 ? 41  LYS A O     1 
ATOM   285  C  CB    . LYS A 1 41  ? -20.93180 33.42370 -14.94785 1.000 133.29534 ? 41  LYS A CB    1 
ATOM   286  N  N     . ILE A 1 42  ? -18.60453 32.05175 -12.46503 1.000 129.23680 ? 42  ILE A N     1 
ATOM   287  C  CA    . ILE A 1 42  ? -17.40999 31.22444 -12.30520 1.000 129.87347 ? 42  ILE A CA    1 
ATOM   288  C  C     . ILE A 1 42  ? -17.75580 29.81716 -12.78358 1.000 128.35634 ? 42  ILE A C     1 
ATOM   289  O  O     . ILE A 1 42  ? -18.42338 29.05662 -12.08096 1.000 126.67697 ? 42  ILE A O     1 
ATOM   290  C  CB    . ILE A 1 42  ? -16.90756 31.21763 -10.86000 1.000 130.40017 ? 42  ILE A CB    1 
ATOM   291  C  CG1   . ILE A 1 42  ? -16.57035 32.63808 -10.39601 1.000 128.81455 ? 42  ILE A CG1   1 
ATOM   292  C  CG2   . ILE A 1 42  ? -15.70674 30.29385 -10.72313 1.000 123.00790 ? 42  ILE A CG2   1 
ATOM   293  C  CD1   . ILE A 1 42  ? -15.09780 32.96938 -10.43284 1.000 116.38627 ? 42  ILE A CD1   1 
ATOM   294  N  N     . LYS A 1 43  ? -17.30741 29.46776 -13.98267 1.000 132.05028 ? 43  LYS A N     1 
ATOM   295  C  CA    . LYS A 1 43  ? -17.45648 28.09502 -14.43017 1.000 129.80781 ? 43  LYS A CA    1 
ATOM   296  C  C     . LYS A 1 43  ? -16.43264 27.20771 -13.72495 1.000 135.55292 ? 43  LYS A C     1 
ATOM   297  O  O     . LYS A 1 43  ? -15.33030 27.65972 -13.40305 1.000 130.77788 ? 43  LYS A O     1 
ATOM   298  C  CB    . LYS A 1 43  ? -17.27235 28.00070 -15.94155 1.000 129.63141 ? 43  LYS A CB    1 
ATOM   299  N  N     . PRO A 1 44  ? -16.77796 25.94879 -13.45488 1.000 131.23220 ? 44  PRO A N     1 
ATOM   300  C  CA    . PRO A 1 44  ? -15.81010 25.04836 -12.81683 1.000 119.11870 ? 44  PRO A CA    1 
ATOM   301  C  C     . PRO A 1 44  ? -14.56826 24.87427 -13.67949 1.000 113.86641 ? 44  PRO A C     1 
ATOM   302  O  O     . PRO A 1 44  ? -14.64667 24.80731 -14.90835 1.000 117.07256 ? 44  PRO A O     1 
ATOM   303  C  CB    . PRO A 1 44  ? -16.58793 23.73476 -12.66545 1.000 118.87760 ? 44  PRO A CB    1 
ATOM   304  C  CG    . PRO A 1 44  ? -17.72387 23.83893 -13.63786 1.000 122.62647 ? 44  PRO A CG    1 
ATOM   305  C  CD    . PRO A 1 44  ? -18.07636 25.29313 -13.68163 1.000 123.25047 ? 44  PRO A CD    1 
ATOM   306  N  N     . PHE A 1 45  ? -13.41221 24.82408 -13.01387 1.000 112.92011 ? 45  PHE A N     1 
ATOM   307  C  CA    . PHE A 1 45  ? -12.09823 24.69255 -13.63958 1.000 106.63509 ? 45  PHE A CA    1 
ATOM   308  C  C     . PHE A 1 45  ? -11.71903 25.90015 -14.48825 1.000 105.46233 ? 45  PHE A C     1 
ATOM   309  O  O     . PHE A 1 45  ? -10.84860 25.79368 -15.35839 1.000 109.38299 ? 45  PHE A O     1 
ATOM   310  C  CB    . PHE A 1 45  ? -12.00239 23.41675 -14.48519 1.000 103.80941 ? 45  PHE A CB    1 
ATOM   311  C  CG    . PHE A 1 45  ? -11.91794 22.15724 -13.67498 1.000 102.32748 ? 45  PHE A CG    1 
ATOM   312  C  CD1   . PHE A 1 45  ? -11.04016 22.06236 -12.60858 1.000 101.37628 ? 45  PHE A CD1   1 
ATOM   313  C  CD2   . PHE A 1 45  ? -12.71845 21.06833 -13.97723 1.000 105.03180 ? 45  PHE A CD2   1 
ATOM   314  C  CE1   . PHE A 1 45  ? -10.95764 20.90346 -11.86079 1.000 104.33724 ? 45  PHE A CE1   1 
ATOM   315  C  CE2   . PHE A 1 45  ? -12.64192 19.90622 -13.23169 1.000 103.34344 ? 45  PHE A CE2   1 
ATOM   316  C  CZ    . PHE A 1 45  ? -11.75998 19.82424 -12.17217 1.000 98.93332  ? 45  PHE A CZ    1 
ATOM   317  N  N     . GLU A 1 46  ? -12.33873 27.05414 -14.25341 1.000 107.73116 ? 46  GLU A N     1 
ATOM   318  C  CA    . GLU A 1 46  ? -12.03201 28.26451 -14.99845 1.000 109.33646 ? 46  GLU A CA    1 
ATOM   319  C  C     . GLU A 1 46  ? -11.47830 29.33205 -14.06296 1.000 108.56127 ? 46  GLU A C     1 
ATOM   320  O  O     . GLU A 1 46  ? -11.85949 29.41670 -12.89156 1.000 100.76105 ? 46  GLU A O     1 
ATOM   321  C  CB    . GLU A 1 46  ? -13.27120 28.79645 -15.73319 1.000 113.62269 ? 46  GLU A CB    1 
ATOM   322  C  CG    . GLU A 1 46  ? -12.98574 29.95735 -16.67249 1.000 126.71770 ? 46  GLU A CG    1 
ATOM   323  C  CD    . GLU A 1 46  ? -11.83587 29.66940 -17.62249 1.000 127.19721 ? 46  GLU A CD    1 
ATOM   324  O  OE1   . GLU A 1 46  ? -11.80575 28.56237 -18.19992 1.000 130.58651 ? 46  GLU A OE1   1 
ATOM   325  O  OE2   . GLU A 1 46  ? -10.95572 30.54354 -17.78264 1.000 125.30137 ? 46  GLU A OE2   1 
ATOM   326  N  N     . ARG A 1 47  ? -10.56777 30.14282 -14.59407 1.000 106.87231 ? 47  ARG A N     1 
ATOM   327  C  CA    . ARG A 1 47  ? -9.92806  31.22315 -13.86131 1.000 100.24858 ? 47  ARG A CA    1 
ATOM   328  C  C     . ARG A 1 47  ? -10.39311 32.56911 -14.40103 1.000 104.36514 ? 47  ARG A C     1 
ATOM   329  O  O     . ARG A 1 47  ? -10.85215 32.68216 -15.54083 1.000 97.15697  ? 47  ARG A O     1 
ATOM   330  C  CB    . ARG A 1 47  ? -8.40225  31.11905 -13.95932 1.000 91.55808  ? 47  ARG A CB    1 
ATOM   331  C  CG    . ARG A 1 47  ? -7.87873  31.19935 -15.38349 1.000 91.73566  ? 47  ARG A CG    1 
ATOM   332  C  CD    . ARG A 1 47  ? -6.37769  30.97484 -15.44652 1.000 89.23393  ? 47  ARG A CD    1 
ATOM   333  N  NE    . ARG A 1 47  ? -5.86562  31.15540 -16.79944 1.000 77.71873  ? 47  ARG A NE    1 
ATOM   334  C  CZ    . ARG A 1 47  ? -5.89492  30.22187 -17.74029 1.000 85.79713  ? 47  ARG A CZ    1 
ATOM   335  N  NH1   . ARG A 1 47  ? -6.39762  29.02094 -17.50608 1.000 83.88642  ? 47  ARG A NH1   1 
ATOM   336  N  NH2   . ARG A 1 47  ? -5.41194  30.50159 -18.94765 1.000 89.53445  ? 47  ARG A NH2   1 
ATOM   337  N  N     . VAL A 1 48  ? -10.26313 33.60053 -13.56404 1.000 98.42142  ? 48  VAL A N     1 
ATOM   338  C  CA    . VAL A 1 48  ? -10.70190 34.94664 -13.91458 1.000 95.94365  ? 48  VAL A CA    1 
ATOM   339  C  C     . VAL A 1 48  ? -9.78712  35.96058 -13.24302 1.000 96.02236  ? 48  VAL A C     1 
ATOM   340  O  O     . VAL A 1 48  ? -9.15291  35.68050 -12.22335 1.000 91.47665  ? 48  VAL A O     1 
ATOM   341  C  CB    . VAL A 1 48  ? -12.17345 35.19387 -13.51157 1.000 97.11041  ? 48  VAL A CB    1 
ATOM   342  C  CG1   . VAL A 1 48  ? -13.11315 34.75873 -14.62415 1.000 76.81324  ? 48  VAL A CG1   1 
ATOM   343  C  CG2   . VAL A 1 48  ? -12.48481 34.44774 -12.23617 1.000 86.77764  ? 48  VAL A CG2   1 
ATOM   344  N  N     . LEU A 1 49  ? -9.73160  37.15542 -13.82541 1.000 91.36438  ? 49  LEU A N     1 
ATOM   345  C  CA    . LEU A 1 49  ? -8.92179  38.26136 -13.32740 1.000 97.41175  ? 49  LEU A CA    1 
ATOM   346  C  C     . LEU A 1 49  ? -9.87199  39.32722 -12.79198 1.000 101.91630 ? 49  LEU A C     1 
ATOM   347  O  O     . LEU A 1 49  ? -10.58089 39.97761 -13.56759 1.000 109.08526 ? 49  LEU A O     1 
ATOM   348  C  CB    . LEU A 1 49  ? -8.03022  38.81402 -14.43884 1.000 92.33680  ? 49  LEU A CB    1 
ATOM   349  C  CG    . LEU A 1 49  ? -6.91902  39.80358 -14.08786 1.000 91.55243  ? 49  LEU A CG    1 
ATOM   350  C  CD1   . LEU A 1 49  ? -5.79182  39.10824 -13.33958 1.000 82.98022  ? 49  LEU A CD1   1 
ATOM   351  C  CD2   . LEU A 1 49  ? -6.39795  40.47376 -15.35160 1.000 98.18397  ? 49  LEU A CD2   1 
ATOM   352  N  N     . ILE A 1 50  ? -9.89238  39.50249 -11.47864 1.000 104.62146 ? 50  ILE A N     1 
ATOM   353  C  CA    . ILE A 1 50  ? -10.82308 40.41426 -10.81431 1.000 114.98025 ? 50  ILE A CA    1 
ATOM   354  C  C     . ILE A 1 50  ? -10.07638 41.68961 -10.44059 1.000 118.10530 ? 50  ILE A C     1 
ATOM   355  O  O     . ILE A 1 50  ? -8.99939  41.60435 -9.83355  1.000 110.28380 ? 50  ILE A O     1 
ATOM   356  C  CB    . ILE A 1 50  ? -11.46149 39.77753 -9.56566  1.000 107.80669 ? 50  ILE A CB    1 
ATOM   357  C  CG1   . ILE A 1 50  ? -12.65280 38.89819 -9.94979  1.000 107.82573 ? 50  ILE A CG1   1 
ATOM   358  C  CG2   . ILE A 1 50  ? -11.91204 40.85578 -8.59468  1.000 113.69060 ? 50  ILE A CG2   1 
ATOM   359  C  CD1   . ILE A 1 50  ? -12.27135 37.57824 -10.56357 1.000 111.52584 ? 50  ILE A CD1   1 
ATOM   360  N  N     . PRO A 1 51  ? -10.60006 42.86791 -10.77409 1.000 126.23674 ? 51  PRO A N     1 
ATOM   361  C  CA    . PRO A 1 51  ? -9.97464  44.11110 -10.31452 1.000 125.83993 ? 51  PRO A CA    1 
ATOM   362  C  C     . PRO A 1 51  ? -10.42825 44.48015 -8.90966  1.000 123.48833 ? 51  PRO A C     1 
ATOM   363  O  O     . PRO A 1 51  ? -11.59890 44.33040 -8.54958  1.000 118.97280 ? 51  PRO A O     1 
ATOM   364  C  CB    . PRO A 1 51  ? -10.45739 45.14126 -11.34205 1.000 119.89276 ? 51  PRO A CB    1 
ATOM   365  C  CG    . PRO A 1 51  ? -11.79823 44.63236 -11.75151 1.000 119.64666 ? 51  PRO A CG    1 
ATOM   366  C  CD    . PRO A 1 51  ? -11.71666 43.12102 -11.70255 1.000 116.69919 ? 51  PRO A CD    1 
ATOM   367  N  N     . THR A 1 52  ? -9.47892  44.96402 -8.10803  1.000 107.98703 ? 52  THR A N     1 
ATOM   368  C  CA    . THR A 1 52  ? -9.78282  45.44544 -6.76734  1.000 100.19038 ? 52  THR A CA    1 
ATOM   369  C  C     . THR A 1 52  ? -9.96544  46.95429 -6.70293  1.000 109.94768 ? 52  THR A C     1 
ATOM   370  O  O     . THR A 1 52  ? -10.62017 47.44372 -5.77596  1.000 104.04339 ? 52  THR A O     1 
ATOM   371  C  CB    . THR A 1 52  ? -8.67543  45.04249 -5.78508  1.000 99.53714  ? 52  THR A CB    1 
ATOM   372  O  OG1   . THR A 1 52  ? -7.47187  45.75286 -6.10230  1.000 98.70181  ? 52  THR A OG1   1 
ATOM   373  C  CG2   . THR A 1 52  ? -8.41177  43.54604 -5.86175  1.000 94.72963  ? 52  THR A CG2   1 
ATOM   374  N  N     . GLY A 1 53  ? -9.41211  47.69457 -7.66091  1.000 108.57266 ? 53  GLY A N     1 
ATOM   375  C  CA    . GLY A 1 53  ? -9.48033  49.14016 -7.62905  1.000 112.90368 ? 53  GLY A CA    1 
ATOM   376  C  C     . GLY A 1 53  ? -8.52367  49.79389 -6.66338  1.000 111.34130 ? 53  GLY A C     1 
ATOM   377  O  O     . GLY A 1 53  ? -8.78029  50.91672 -6.21799  1.000 117.04815 ? 53  GLY A O     1 
ATOM   378  N  N     . LEU A 1 54  ? -7.42530  49.12561 -6.32358  1.000 107.53149 ? 54  LEU A N     1 
ATOM   379  C  CA    . LEU A 1 54  ? -6.46195  49.62128 -5.35269  1.000 110.95186 ? 54  LEU A CA    1 
ATOM   380  C  C     . LEU A 1 54  ? -5.09509  49.77490 -6.00399  1.000 111.79521 ? 54  LEU A C     1 
ATOM   381  O  O     . LEU A 1 54  ? -4.69721  48.95688 -6.83978  1.000 109.90593 ? 54  LEU A O     1 
ATOM   382  C  CB    . LEU A 1 54  ? -6.35460  48.67912 -4.14564  1.000 109.41074 ? 54  LEU A CB    1 
ATOM   383  C  CG    . LEU A 1 54  ? -7.32183  48.84701 -2.96952  1.000 113.70030 ? 54  LEU A CG    1 
ATOM   384  C  CD1   . LEU A 1 54  ? -8.77500  48.69911 -3.39475  1.000 109.01572 ? 54  LEU A CD1   1 
ATOM   385  C  CD2   . LEU A 1 54  ? -6.98153  47.84303 -1.88027  1.000 108.39618 ? 54  LEU A CD2   1 
ATOM   386  N  N     . ILE A 1 55  ? -4.38387  50.83078 -5.61616  1.000 115.75826 ? 55  ILE A N     1 
ATOM   387  C  CA    . ILE A 1 55  ? -3.00090  51.06002 -6.01874  1.000 110.94447 ? 55  ILE A CA    1 
ATOM   388  C  C     . ILE A 1 55  ? -2.19990  51.32839 -4.75294  1.000 103.84531 ? 55  ILE A C     1 
ATOM   389  O  O     . ILE A 1 55  ? -2.49621  52.27730 -4.01664  1.000 106.98774 ? 55  ILE A O     1 
ATOM   390  C  CB    . ILE A 1 55  ? -2.86805  52.22729 -7.01105  1.000 106.23677 ? 55  ILE A CB    1 
ATOM   391  C  CG1   . ILE A 1 55  ? -3.56041  51.88285 -8.33201  1.000 106.03682 ? 55  ILE A CG1   1 
ATOM   392  C  CG2   . ILE A 1 55  ? -1.40405  52.56490 -7.24319  1.000 97.93763  ? 55  ILE A CG2   1 
ATOM   393  C  CD1   . ILE A 1 55  ? -3.52251  52.99827 -9.35072  1.000 110.20457 ? 55  ILE A CD1   1 
ATOM   394  N  N     . LEU A 1 56  ? -1.19464  50.49829 -4.49876  1.000 93.01751  ? 56  LEU A N     1 
ATOM   395  C  CA    . LEU A 1 56  ? -0.49019  50.49030 -3.22739  1.000 108.53492 ? 56  LEU A CA    1 
ATOM   396  C  C     . LEU A 1 56  ? 0.90710   51.07896 -3.37165  1.000 107.72650 ? 56  LEU A C     1 
ATOM   397  O  O     . LEU A 1 56  ? 1.48952   51.10598 -4.45910  1.000 101.38178 ? 56  LEU A O     1 
ATOM   398  C  CB    . LEU A 1 56  ? -0.39031  49.06495 -2.67363  1.000 105.65306 ? 56  LEU A CB    1 
ATOM   399  C  CG    . LEU A 1 56  ? -1.56852  48.12588 -2.94200  1.000 105.65362 ? 56  LEU A CG    1 
ATOM   400  C  CD1   . LEU A 1 56  ? -1.26170  46.73842 -2.40497  1.000 96.92241  ? 56  LEU A CD1   1 
ATOM   401  C  CD2   . LEU A 1 56  ? -2.85582  48.66427 -2.33686  1.000 106.86209 ? 56  LEU A CD2   1 
ATOM   402  N  N     . GLU A 1 57  ? 1.44155   51.55035 -2.24431  1.000 100.37902 ? 57  GLU A N     1 
ATOM   403  C  CA    . GLU A 1 57  ? 2.83395   51.98688 -2.13395  1.000 99.11795  ? 57  GLU A CA    1 
ATOM   404  C  C     . GLU A 1 57  ? 3.41603   51.26712 -0.92083  1.000 108.62382 ? 57  GLU A C     1 
ATOM   405  O  O     . GLU A 1 57  ? 3.39078   51.78832 0.19756   1.000 118.04290 ? 57  GLU A O     1 
ATOM   406  C  CB    . GLU A 1 57  ? 2.94918   53.50257 -2.00597  1.000 107.80680 ? 57  GLU A CB    1 
ATOM   407  C  CG    . GLU A 1 57  ? 4.33276   54.03740 -2.35187  1.000 110.75376 ? 57  GLU A CG    1 
ATOM   408  C  CD    . GLU A 1 57  ? 4.52678   55.48524 -1.94498  1.000 116.51137 ? 57  GLU A CD    1 
ATOM   409  O  OE1   . GLU A 1 57  ? 4.96111   55.72880 -0.79969  1.000 110.23008 ? 57  GLU A OE1   1 
ATOM   410  O  OE2   . GLU A 1 57  ? 4.24166   56.38019 -2.76788  1.000 121.23905 ? 57  GLU A OE2   1 
ATOM   411  N  N     . ILE A 1 58  ? 3.92965   50.06315 -1.14799  1.000 101.54662 ? 58  ILE A N     1 
ATOM   412  C  CA    . ILE A 1 58  ? 4.49319   49.23189 -0.08810  1.000 103.25683 ? 58  ILE A CA    1 
ATOM   413  C  C     . ILE A 1 58  ? 5.84843   49.80474 0.31175   1.000 111.60123 ? 58  ILE A C     1 
ATOM   414  O  O     . ILE A 1 58  ? 6.63079   50.20052 -0.56474  1.000 111.93019 ? 58  ILE A O     1 
ATOM   415  C  CB    . ILE A 1 58  ? 4.61246   47.76907 -0.54524  1.000 103.85520 ? 58  ILE A CB    1 
ATOM   416  C  CG1   . ILE A 1 58  ? 3.34191   47.34151 -1.28306  1.000 100.56687 ? 58  ILE A CG1   1 
ATOM   417  C  CG2   . ILE A 1 58  ? 4.86167   46.84818 0.63817   1.000 107.28428 ? 58  ILE A CG2   1 
ATOM   418  C  CD1   . ILE A 1 58  ? 3.39617   45.93046 -1.82996  1.000 92.33773  ? 58  ILE A CD1   1 
ATOM   419  N  N     . PRO A 1 59  ? 6.16578   49.88608 1.60503   1.000 116.48692 ? 59  PRO A N     1 
ATOM   420  C  CA    . PRO A 1 59  ? 7.48925   50.37922 2.00374   1.000 121.76898 ? 59  PRO A CA    1 
ATOM   421  C  C     . PRO A 1 59  ? 8.59502   49.46335 1.50299   1.000 125.50784 ? 59  PRO A C     1 
ATOM   422  O  O     . PRO A 1 59  ? 8.39094   48.26648 1.28607   1.000 123.14581 ? 59  PRO A O     1 
ATOM   423  C  CB    . PRO A 1 59  ? 7.42470   50.38364 3.53610   1.000 121.86656 ? 59  PRO A CB    1 
ATOM   424  C  CG    . PRO A 1 59  ? 5.98063   50.37880 3.86556   1.000 114.55590 ? 59  PRO A CG    1 
ATOM   425  C  CD    . PRO A 1 59  ? 5.29937   49.62740 2.76696   1.000 106.88389 ? 59  PRO A CD    1 
ATOM   426  N  N     . GLU A 1 60  ? 9.77903   50.04404 1.31837   1.000 140.91396 ? 60  GLU A N     1 
ATOM   427  C  CA    . GLU A 1 60  ? 10.92908  49.25909 0.89430   1.000 136.71860 ? 60  GLU A CA    1 
ATOM   428  C  C     . GLU A 1 60  ? 11.26333  48.20739 1.94620   1.000 131.03077 ? 60  GLU A C     1 
ATOM   429  O  O     . GLU A 1 60  ? 11.07358  48.41276 3.14872   1.000 133.21937 ? 60  GLU A O     1 
ATOM   430  C  CB    . GLU A 1 60  ? 12.13698  50.16528 0.64119   1.000 144.98065 ? 60  GLU A CB    1 
ATOM   431  C  CG    . GLU A 1 60  ? 12.75663  50.78676 1.89005   1.000 149.98304 ? 60  GLU A CG    1 
ATOM   432  C  CD    . GLU A 1 60  ? 12.00970  52.01342 2.38865   1.000 157.59932 ? 60  GLU A CD    1 
ATOM   433  O  OE1   . GLU A 1 60  ? 10.77296  52.08092 2.22464   1.000 155.61177 ? 60  GLU A OE1   1 
ATOM   434  O  OE2   . GLU A 1 60  ? 12.66744  52.91791 2.94514   1.000 158.79269 ? 60  GLU A OE2   1 
ATOM   435  N  N     . GLY A 1 61  ? 11.75400  47.06218 1.47964   1.000 119.68969 ? 61  GLY A N     1 
ATOM   436  C  CA    . GLY A 1 61  ? 11.97761  45.93043 2.35014   1.000 113.92823 ? 61  GLY A CA    1 
ATOM   437  C  C     . GLY A 1 61  ? 10.72743  45.18085 2.75229   1.000 113.68493 ? 61  GLY A C     1 
ATOM   438  O  O     . GLY A 1 61  ? 10.82755  44.19936 3.50013   1.000 116.80687 ? 61  GLY A O     1 
ATOM   439  N  N     . TYR A 1 62  ? 9.55784   45.60935 2.28838   1.000 107.90048 ? 62  TYR A N     1 
ATOM   440  C  CA    . TYR A 1 62  ? 8.29186   44.94991 2.56607   1.000 106.82215 ? 62  TYR A CA    1 
ATOM   441  C  C     . TYR A 1 62  ? 7.62488   44.54683 1.25708   1.000 101.65888 ? 62  TYR A C     1 
ATOM   442  O  O     . TYR A 1 62  ? 8.04715   44.94203 0.16719   1.000 104.99624 ? 62  TYR A O     1 
ATOM   443  C  CB    . TYR A 1 62  ? 7.35986   45.85492 3.38358   1.000 106.87665 ? 62  TYR A CB    1 
ATOM   444  C  CG    . TYR A 1 62  ? 7.81659   46.07485 4.80741   1.000 111.85806 ? 62  TYR A CG    1 
ATOM   445  C  CD1   . TYR A 1 62  ? 7.82842   45.02871 5.72010   1.000 113.36898 ? 62  TYR A CD1   1 
ATOM   446  C  CD2   . TYR A 1 62  ? 8.22395   47.32889 5.24274   1.000 110.32781 ? 62  TYR A CD2   1 
ATOM   447  C  CE1   . TYR A 1 62  ? 8.24291   45.22027 7.02376   1.000 111.85561 ? 62  TYR A CE1   1 
ATOM   448  C  CE2   . TYR A 1 62  ? 8.63794   47.53223 6.54701   1.000 116.18510 ? 62  TYR A CE2   1 
ATOM   449  C  CZ    . TYR A 1 62  ? 8.64481   46.47358 7.43310   1.000 116.94917 ? 62  TYR A CZ    1 
ATOM   450  O  OH    . TYR A 1 62  ? 9.05550   46.66731 8.73238   1.000 117.29862 ? 62  TYR A OH    1 
ATOM   451  N  N     . GLU A 1 63  ? 6.56751   43.74797 1.37779   1.000 100.06739 ? 63  GLU A N     1 
ATOM   452  C  CA    . GLU A 1 63  ? 5.84111   43.25459 0.21588   1.000 92.05197  ? 63  GLU A CA    1 
ATOM   453  C  C     . GLU A 1 63  ? 4.41655   42.91966 0.63240   1.000 85.98115  ? 63  GLU A C     1 
ATOM   454  O  O     . GLU A 1 63  ? 4.08740   42.87212 1.81995   1.000 85.68567  ? 63  GLU A O     1 
ATOM   455  C  CB    . GLU A 1 63  ? 6.52466   42.02731 -0.39412  1.000 91.35703  ? 63  GLU A CB    1 
ATOM   456  C  CG    . GLU A 1 63  ? 6.54184   40.81831 0.52931   1.000 87.43664  ? 63  GLU A CG    1 
ATOM   457  C  CD    . GLU A 1 63  ? 6.78303   39.51968 -0.21193  1.000 85.36306  ? 63  GLU A CD    1 
ATOM   458  O  OE1   . GLU A 1 63  ? 6.88785   39.55778 -1.45595  1.000 84.05958  ? 63  GLU A OE1   1 
ATOM   459  O  OE2   . GLU A 1 63  ? 6.86254   38.46184 0.44927   1.000 73.66872  ? 63  GLU A OE2   1 
ATOM   460  N  N     . GLY A 1 64  ? 3.57864   42.68336 -0.36603  1.000 76.83032  ? 64  GLY A N     1 
ATOM   461  C  CA    . GLY A 1 64  ? 2.20332   42.26030 -0.14682  1.000 77.08325  ? 64  GLY A CA    1 
ATOM   462  C  C     . GLY A 1 64  ? 1.96740   40.89356 -0.75825  1.000 78.64306  ? 64  GLY A C     1 
ATOM   463  O  O     . GLY A 1 64  ? 2.51619   40.57691 -1.81521  1.000 82.19966  ? 64  GLY A O     1 
ATOM   464  N  N     . GLN A 1 65  ? 1.15130   40.08599 -0.08549  1.000 72.76332  ? 65  GLN A N     1 
ATOM   465  C  CA    . GLN A 1 65  ? 0.87609   38.72056 -0.51238  1.000 67.51521  ? 65  GLN A CA    1 
ATOM   466  C  C     . GLN A 1 65  ? -0.62596  38.51452 -0.61246  1.000 70.91389  ? 65  GLN A C     1 
ATOM   467  O  O     . GLN A 1 65  ? -1.35759  38.79527 0.34217   1.000 72.49877  ? 65  GLN A O     1 
ATOM   468  C  CB    . GLN A 1 65  ? 1.47983   37.70230 0.46132   1.000 70.08299  ? 65  GLN A CB    1 
ATOM   469  C  CG    . GLN A 1 65  ? 2.97355   37.85141 0.68221   1.000 72.98844  ? 65  GLN A CG    1 
ATOM   470  C  CD    . GLN A 1 65  ? 3.50965   36.85020 1.68400   1.000 81.82829  ? 65  GLN A CD    1 
ATOM   471  O  OE1   . GLN A 1 65  ? 2.82779   35.89000 2.04182   1.000 78.00267  ? 65  GLN A OE1   1 
ATOM   472  N  NE2   . GLN A 1 65  ? 4.73494   37.07143 2.14684   1.000 80.02911  ? 65  GLN A NE2   1 
ATOM   473  N  N     . VAL A 1 66  ? -1.07909  38.02246 -1.76110  1.000 64.91067  ? 66  VAL A N     1 
ATOM   474  C  CA    . VAL A 1 66  ? -2.47993  37.66936 -1.95903  1.000 67.02536  ? 66  VAL A CA    1 
ATOM   475  C  C     . VAL A 1 66  ? -2.65987  36.23354 -1.47416  1.000 60.38305  ? 66  VAL A C     1 
ATOM   476  O  O     . VAL A 1 66  ? -2.09590  35.29887 -2.04994  1.000 66.81271  ? 66  VAL A O     1 
ATOM   477  C  CB    . VAL A 1 66  ? -2.89946  37.82342 -3.42648  1.000 64.67325  ? 66  VAL A CB    1 
ATOM   478  C  CG1   . VAL A 1 66  ? -4.38668  37.54776 -3.58478  1.000 66.13656  ? 66  VAL A CG1   1 
ATOM   479  C  CG2   . VAL A 1 66  ? -2.54813  39.21387 -3.93819  1.000 68.31501  ? 66  VAL A CG2   1 
ATOM   480  N  N     . ARG A 1 67  ? -3.44416  36.05422 -0.41376  1.000 70.33595  ? 67  ARG A N     1 
ATOM   481  C  CA    . ARG A 1 67  ? -3.64941  34.73295 0.15699   1.000 66.76587  ? 67  ARG A CA    1 
ATOM   482  C  C     . ARG A 1 67  ? -5.12024  34.33878 0.08769   1.000 64.91819  ? 67  ARG A C     1 
ATOM   483  O  O     . ARG A 1 67  ? -6.00315  35.19116 0.22700   1.000 69.80142  ? 67  ARG A O     1 
ATOM   484  C  CB    . ARG A 1 67  ? -3.17289  34.67922 1.61342   1.000 63.64438  ? 67  ARG A CB    1 
ATOM   485  C  CG    . ARG A 1 67  ? -1.69532  34.98405 1.78093   1.000 68.68647  ? 67  ARG A CG    1 
ATOM   486  C  CD    . ARG A 1 67  ? -1.22278  34.69321 3.19185   1.000 61.15602  ? 67  ARG A CD    1 
ATOM   487  N  NE    . ARG A 1 67  ? 0.14273   35.15184 3.41462   1.000 74.27337  ? 67  ARG A NE    1 
ATOM   488  C  CZ    . ARG A 1 67  ? 0.78996   35.03820 4.56601   1.000 80.73194  ? 67  ARG A CZ    1 
ATOM   489  N  NH1   . ARG A 1 67  ? 0.22803   34.47136 5.62120   1.000 76.39908  ? 67  ARG A NH1   1 
ATOM   490  N  NH2   . ARG A 1 67  ? 2.03110   35.50642 4.66182   1.000 76.11135  ? 67  ARG A NH2   1 
ATOM   491  N  N     . PRO A 1 68  ? -5.41267  33.05796 -0.12812  1.000 65.14430  ? 68  PRO A N     1 
ATOM   492  C  CA    . PRO A 1 68  ? -6.80906  32.63432 -0.27475  1.000 67.15721  ? 68  PRO A CA    1 
ATOM   493  C  C     . PRO A 1 68  ? -7.55154  32.66945 1.05013   1.000 69.72560  ? 68  PRO A C     1 
ATOM   494  O  O     . PRO A 1 68  ? -6.96664  32.50559 2.12366   1.000 74.67500  ? 68  PRO A O     1 
ATOM   495  C  CB    . PRO A 1 68  ? -6.69326  31.19442 -0.79805  1.000 68.08825  ? 68  PRO A CB    1 
ATOM   496  C  CG    . PRO A 1 68  ? -5.26056  31.02697 -1.21745  1.000 71.17380  ? 68  PRO A CG    1 
ATOM   497  C  CD    . PRO A 1 68  ? -4.47311  31.94625 -0.34461  1.000 68.94958  ? 68  PRO A CD    1 
ATOM   498  N  N     . ARG A 1 69  ? -8.86093  32.88516 0.96124   1.000 72.59704  ? 69  ARG A N     1 
ATOM   499  C  CA    . ARG A 1 69  ? -9.71506  32.83164 2.13773   1.000 79.32445  ? 69  ARG A CA    1 
ATOM   500  C  C     . ARG A 1 69  ? -10.08484 31.38738 2.44815   1.000 74.13082  ? 69  ARG A C     1 
ATOM   501  O  O     . ARG A 1 69  ? -10.36109 30.59326 1.54461   1.000 78.41403  ? 69  ARG A O     1 
ATOM   502  C  CB    . ARG A 1 69  ? -10.97826 33.66711 1.92808   1.000 78.72585  ? 69  ARG A CB    1 
ATOM   503  C  CG    . ARG A 1 69  ? -10.71188 35.14807 1.71376   1.000 84.35913  ? 69  ARG A CG    1 
ATOM   504  C  CD    . ARG A 1 69  ? -11.99791 35.96310 1.75033   1.000 91.88134  ? 69  ARG A CD    1 
ATOM   505  N  NE    . ARG A 1 69  ? -12.62005 35.95595 3.06982   1.000 108.34609 ? 69  ARG A NE    1 
ATOM   506  C  CZ    . ARG A 1 69  ? -13.65205 35.19584 3.41156   1.000 107.64856 ? 69  ARG A CZ    1 
ATOM   507  N  NH1   . ARG A 1 69  ? -14.21862 34.36932 2.54759   1.000 105.58777 ? 69  ARG A NH1   1 
ATOM   508  N  NH2   . ARG A 1 69  ? -14.12824 35.26757 4.65139   1.000 101.43064 ? 69  ARG A NH2   1 
ATOM   509  N  N     . SER A 1 70  ? -10.08249 31.04933 3.73914   1.000 70.05968  ? 70  SER A N     1 
ATOM   510  C  CA    . SER A 1 70  ? -10.34215 29.67147 4.14428   1.000 69.13206  ? 70  SER A CA    1 
ATOM   511  C  C     . SER A 1 70  ? -11.78473 29.26843 3.86460   1.000 75.48161  ? 70  SER A C     1 
ATOM   512  O  O     . SER A 1 70  ? -12.04359 28.15059 3.40319   1.000 67.01614  ? 70  SER A O     1 
ATOM   513  C  CB    . SER A 1 70  ? -10.01359 29.49531 5.62579   1.000 75.30239  ? 70  SER A CB    1 
ATOM   514  O  OG    . SER A 1 70  ? -10.77959 30.38326 6.42120   1.000 71.21593  ? 70  SER A OG    1 
ATOM   515  N  N     . GLY A 1 71  ? -12.73593 30.16330 4.13746   1.000 73.97591  ? 71  GLY A N     1 
ATOM   516  C  CA    . GLY A 1 71  ? -14.13678 29.82007 3.94563   1.000 73.28406  ? 71  GLY A CA    1 
ATOM   517  C  C     . GLY A 1 71  ? -14.48051 29.55885 2.49205   1.000 81.90079  ? 71  GLY A C     1 
ATOM   518  O  O     . GLY A 1 71  ? -15.15056 28.57594 2.16554   1.000 76.80218  ? 71  GLY A O     1 
ATOM   519  N  N     . LEU A 1 72  ? -14.02674 30.44063 1.59677   1.000 83.83919  ? 72  LEU A N     1 
ATOM   520  C  CA    . LEU A 1 72  ? -14.28887 30.24643 0.17443   1.000 78.66404  ? 72  LEU A CA    1 
ATOM   521  C  C     . LEU A 1 72  ? -13.63035 28.97852 -0.34908  1.000 80.20300  ? 72  LEU A C     1 
ATOM   522  O  O     . LEU A 1 72  ? -14.12888 28.36676 -1.29972  1.000 81.03294  ? 72  LEU A O     1 
ATOM   523  C  CB    . LEU A 1 72  ? -13.80253 31.45527 -0.62452  1.000 74.46986  ? 72  LEU A CB    1 
ATOM   524  C  CG    . LEU A 1 72  ? -14.56612 32.76793 -0.44675  1.000 93.57133  ? 72  LEU A CG    1 
ATOM   525  C  CD1   . LEU A 1 72  ? -13.91261 33.87705 -1.25657  1.000 94.41132  ? 72  LEU A CD1   1 
ATOM   526  C  CD2   . LEU A 1 72  ? -16.02362 32.59818 -0.84559  1.000 100.71233 ? 72  LEU A CD2   1 
ATOM   527  N  N     . ALA A 1 73  ? -12.51640 28.56624 0.25694   1.000 76.11470  ? 73  ALA A N     1 
ATOM   528  C  CA    . ALA A 1 73  ? -11.81138 27.38579 -0.22601  1.000 73.50188  ? 73  ALA A CA    1 
ATOM   529  C  C     . ALA A 1 73  ? -12.51772 26.10079 0.18098   1.000 77.65866  ? 73  ALA A C     1 
ATOM   530  O  O     . ALA A 1 73  ? -12.43759 25.09832 -0.53775  1.000 87.96534  ? 73  ALA A O     1 
ATOM   531  C  CB    . ALA A 1 73  ? -10.36776 27.38883 0.27934   1.000 71.40030  ? 73  ALA A CB    1 
ATOM   532  N  N     . TRP A 1 74  ? -13.20911 26.10567 1.31877   1.000 77.84624  ? 74  TRP A N     1 
ATOM   533  C  CA    . TRP A 1 74  ? -13.87319 24.90116 1.80081   1.000 83.06979  ? 74  TRP A CA    1 
ATOM   534  C  C     . TRP A 1 74  ? -15.33434 24.82328 1.37210   1.000 86.54546  ? 74  TRP A C     1 
ATOM   535  O  O     . TRP A 1 74  ? -15.80136 23.75489 0.96071   1.000 90.08930  ? 74  TRP A O     1 
ATOM   536  C  CB    . TRP A 1 74  ? -13.77157 24.82161 3.32678   1.000 83.15262  ? 74  TRP A CB    1 
ATOM   537  C  CG    . TRP A 1 74  ? -14.61190 23.73879 3.92796   1.000 88.60369  ? 74  TRP A CG    1 
ATOM   538  C  CD1   . TRP A 1 74  ? -15.65621 23.89640 4.79359   1.000 92.78371  ? 74  TRP A CD1   1 
ATOM   539  C  CD2   . TRP A 1 74  ? -14.49138 22.32937 3.69681   1.000 82.97746  ? 74  TRP A CD2   1 
ATOM   540  N  NE1   . TRP A 1 74  ? -16.18695 22.67224 5.12234   1.000 81.71354  ? 74  TRP A NE1   1 
ATOM   541  C  CE2   . TRP A 1 74  ? -15.49055 21.69418 4.46165   1.000 87.90997  ? 74  TRP A CE2   1 
ATOM   542  C  CE3   . TRP A 1 74  ? -13.63349 21.54275 2.92105   1.000 77.80576  ? 74  TRP A CE3   1 
ATOM   543  C  CZ2   . TRP A 1 74  ? -15.65566 20.30976 4.47267   1.000 85.55119  ? 74  TRP A CZ2   1 
ATOM   544  C  CZ3   . TRP A 1 74  ? -13.79988 20.16847 2.93300   1.000 86.66402  ? 74  TRP A CZ3   1 
ATOM   545  C  CH2   . TRP A 1 74  ? -14.80326 19.56666 3.70309   1.000 90.55475  ? 74  TRP A CH2   1 
ATOM   546  N  N     . LYS A 1 75  ? -16.06577 25.93719 1.44980   1.000 89.01618  ? 75  LYS A N     1 
ATOM   547  C  CA    . LYS A 1 75  ? -17.49080 25.91655 1.13650   1.000 94.34426  ? 75  LYS A CA    1 
ATOM   548  C  C     . LYS A 1 75  ? -17.75782 25.86884 -0.36323  1.000 93.20981  ? 75  LYS A C     1 
ATOM   549  O  O     . LYS A 1 75  ? -18.72570 25.23023 -0.79160  1.000 87.07849  ? 75  LYS A O     1 
ATOM   550  C  CB    . LYS A 1 75  ? -18.18346 27.13511 1.74995   1.000 84.15274  ? 75  LYS A CB    1 
ATOM   551  N  N     . LYS A 1 76  ? -16.92390 26.52722 -1.17434  1.000 95.77709  ? 76  LYS A N     1 
ATOM   552  C  CA    . LYS A 1 76  ? -17.14446 26.58333 -2.61262  1.000 91.68768  ? 76  LYS A CA    1 
ATOM   553  C  C     . LYS A 1 76  ? -15.93270 26.18349 -3.44474  1.000 93.29191  ? 76  LYS A C     1 
ATOM   554  O  O     . LYS A 1 76  ? -16.00945 26.23806 -4.67696  1.000 81.64627  ? 76  LYS A O     1 
ATOM   555  C  CB    . LYS A 1 76  ? -17.59442 27.99099 -3.03404  1.000 96.84968  ? 76  LYS A CB    1 
ATOM   556  C  CG    . LYS A 1 76  ? -18.81965 28.50876 -2.29701  1.000 88.18501  ? 76  LYS A CG    1 
ATOM   557  C  CD    . LYS A 1 76  ? -19.43155 29.68846 -3.03084  1.000 99.91100  ? 76  LYS A CD    1 
ATOM   558  C  CE    . LYS A 1 76  ? -19.93462 30.74901 -2.06843  1.000 98.82034  ? 76  LYS A CE    1 
ATOM   559  N  NZ    . LYS A 1 76  ? -20.49874 31.91915 -2.79562  1.000 104.75761 ? 76  LYS A NZ    1 
ATOM   560  N  N     . GLY A 1 77  ? -14.82293 25.79532 -2.82090  1.000 91.08947  ? 77  GLY A N     1 
ATOM   561  C  CA    . GLY A 1 77  ? -13.68858 25.29881 -3.57503  1.000 81.94670  ? 77  GLY A CA    1 
ATOM   562  C  C     . GLY A 1 77  ? -12.92791 26.33875 -4.36344  1.000 84.79906  ? 77  GLY A C     1 
ATOM   563  O  O     . GLY A 1 77  ? -12.16064 25.98018 -5.26037  1.000 87.48651  ? 77  GLY A O     1 
ATOM   564  N  N     . LEU A 1 78  ? -13.11731 27.61913 -4.06010  1.000 83.54462  ? 78  LEU A N     1 
ATOM   565  C  CA    . LEU A 1 78  ? -12.38415 28.67005 -4.74519  1.000 86.67811  ? 78  LEU A CA    1 
ATOM   566  C  C     . LEU A 1 78  ? -11.02808 28.89210 -4.08476  1.000 79.40217  ? 78  LEU A C     1 
ATOM   567  O  O     . LEU A 1 78  ? -10.82174 28.58400 -2.90917  1.000 79.11430  ? 78  LEU A O     1 
ATOM   568  C  CB    . LEU A 1 78  ? -13.18249 29.97283 -4.74775  1.000 84.46973  ? 78  LEU A CB    1 
ATOM   569  C  CG    . LEU A 1 78  ? -13.74465 30.41457 -6.09842  1.000 95.61416  ? 78  LEU A CG    1 
ATOM   570  C  CD1   . LEU A 1 78  ? -14.61840 29.32605 -6.69564  1.000 104.51210 ? 78  LEU A CD1   1 
ATOM   571  C  CD2   . LEU A 1 78  ? -14.52316 31.70767 -5.94685  1.000 100.39065 ? 78  LEU A CD2   1 
ATOM   572  N  N     . THR A 1 79  ? -10.09670 29.43817 -4.86063  1.000 69.14524  ? 79  THR A N     1 
ATOM   573  C  CA    . THR A 1 79  ? -8.76440  29.72939 -4.35092  1.000 75.32541  ? 79  THR A CA    1 
ATOM   574  C  C     . THR A 1 79  ? -8.07632  30.70240 -5.29495  1.000 75.33131  ? 79  THR A C     1 
ATOM   575  O  O     . THR A 1 79  ? -8.52493  30.93611 -6.41982  1.000 70.03797  ? 79  THR A O     1 
ATOM   576  C  CB    . THR A 1 79  ? -7.92842  28.45633 -4.19166  1.000 74.74837  ? 79  THR A CB    1 
ATOM   577  O  OG1   . THR A 1 79  ? -6.60783  28.80315 -3.75761  1.000 75.98343  ? 79  THR A OG1   1 
ATOM   578  C  CG2   . THR A 1 79  ? -7.84344  27.70785 -5.51290  1.000 81.82546  ? 79  THR A CG2   1 
ATOM   579  N  N     . VAL A 1 80  ? -6.97788  31.27275 -4.81195  1.000 73.18414  ? 80  VAL A N     1 
ATOM   580  C  CA    . VAL A 1 80  ? -6.11719  32.11060 -5.63771  1.000 65.46806  ? 80  VAL A CA    1 
ATOM   581  C  C     . VAL A 1 80  ? -5.17315  31.19605 -6.40734  1.000 68.90843  ? 80  VAL A C     1 
ATOM   582  O  O     . VAL A 1 80  ? -4.44117  30.40052 -5.80889  1.000 67.00090  ? 80  VAL A O     1 
ATOM   583  C  CB    . VAL A 1 80  ? -5.34120  33.12175 -4.78244  1.000 68.38744  ? 80  VAL A CB    1 
ATOM   584  C  CG1   . VAL A 1 80  ? -4.63785  34.13647 -5.66841  1.000 68.57571  ? 80  VAL A CG1   1 
ATOM   585  C  CG2   . VAL A 1 80  ? -6.27565  33.81360 -3.79857  1.000 66.72916  ? 80  VAL A CG2   1 
ATOM   586  N  N     . LEU A 1 81  ? -5.19584  31.30280 -7.73832  1.000 73.57199  ? 81  LEU A N     1 
ATOM   587  C  CA    . LEU A 1 81  ? -4.42922  30.38343 -8.57457  1.000 64.98161  ? 81  LEU A CA    1 
ATOM   588  C  C     . LEU A 1 81  ? -2.93349  30.51853 -8.31976  1.000 62.75698  ? 81  LEU A C     1 
ATOM   589  O  O     . LEU A 1 81  ? -2.22403  29.51645 -8.17266  1.000 63.00602  ? 81  LEU A O     1 
ATOM   590  C  CB    . LEU A 1 81  ? -4.74631  30.63002 -10.04885 1.000 78.78614  ? 81  LEU A CB    1 
ATOM   591  C  CG    . LEU A 1 81  ? -4.12474  29.64191 -11.03692 1.000 79.43791  ? 81  LEU A CG    1 
ATOM   592  C  CD1   . LEU A 1 81  ? -4.78699  28.27800 -10.91743 1.000 80.77477  ? 81  LEU A CD1   1 
ATOM   593  C  CD2   . LEU A 1 81  ? -4.22719  30.16822 -12.45516 1.000 76.76588  ? 81  LEU A CD2   1 
ATOM   594  N  N     . ASN A 1 82  ? -2.43537  31.75412 -8.26408  1.000 66.46204  ? 82  ASN A N     1 
ATOM   595  C  CA    . ASN A 1 82  ? -1.01897  32.02138 -8.05212  1.000 71.19183  ? 82  ASN A CA    1 
ATOM   596  C  C     . ASN A 1 82  ? -0.69344  32.28111 -6.58555  1.000 68.06585  ? 82  ASN A C     1 
ATOM   597  O  O     . ASN A 1 82  ? 0.22662   33.04704 -6.28156  1.000 67.81817  ? 82  ASN A O     1 
ATOM   598  C  CB    . ASN A 1 82  ? -0.57022  33.20355 -8.91034  1.000 71.21164  ? 82  ASN A CB    1 
ATOM   599  C  CG    . ASN A 1 82  ? -1.20450  34.51323 -8.47347  1.000 68.01240  ? 82  ASN A CG    1 
ATOM   600  O  OD1   . ASN A 1 82  ? -2.37159  34.55180 -8.08294  1.000 66.18338  ? 82  ASN A OD1   1 
ATOM   601  N  ND2   . ASN A 1 82  ? -0.43205  35.59258 -8.52862  1.000 75.52825  ? 82  ASN A ND2   1 
ATOM   602  N  N     . ALA A 1 83  ? -1.42527  31.65431 -5.67329  1.000 65.83498  ? 83  ALA A N     1 
ATOM   603  C  CA    . ALA A 1 83  ? -1.22268  31.90649 -4.25327  1.000 63.26075  ? 83  ALA A CA    1 
ATOM   604  C  C     . ALA A 1 83  ? 0.13173   31.36540 -3.80733  1.000 56.59645  ? 83  ALA A C     1 
ATOM   605  O  O     . ALA A 1 83  ? 0.48119   30.22825 -4.14250  1.000 62.40360  ? 83  ALA A O     1 
ATOM   606  C  CB    . ALA A 1 83  ? -2.34118  31.27248 -3.43221  1.000 59.70570  ? 83  ALA A CB    1 
ATOM   607  N  N     . PRO A 1 84  ? 0.92828   32.14812 -3.06710  1.000 61.87562  ? 84  PRO A N     1 
ATOM   608  C  CA    . PRO A 1 84  ? 0.67383   33.53534 -2.65298  1.000 62.92167  ? 84  PRO A CA    1 
ATOM   609  C  C     . PRO A 1 84  ? 1.00564   34.53447 -3.75702  1.000 63.93470  ? 84  PRO A C     1 
ATOM   610  O  O     . PRO A 1 84  ? 2.08044   34.48652 -4.35045  1.000 60.54887  ? 84  PRO A O     1 
ATOM   611  C  CB    . PRO A 1 84  ? 1.58756   33.69591 -1.43161  1.000 56.22093  ? 84  PRO A CB    1 
ATOM   612  C  CG    . PRO A 1 84  ? 2.74795   32.79620 -1.73070  1.000 53.92757  ? 84  PRO A CG    1 
ATOM   613  C  CD    . PRO A 1 84  ? 2.15451   31.60919 -2.45071  1.000 58.90251  ? 84  PRO A CD    1 
ATOM   614  N  N     . GLY A 1 85  ? 0.08560   35.44649 -4.06054  1.000 61.71577  ? 85  GLY A N     1 
ATOM   615  C  CA    . GLY A 1 85  ? 0.31835   36.44069 -5.08894  1.000 66.38666  ? 85  GLY A CA    1 
ATOM   616  C  C     . GLY A 1 85  ? 1.29506   37.51131 -4.65128  1.000 68.16712  ? 85  GLY A C     1 
ATOM   617  O  O     . GLY A 1 85  ? 0.97187   38.34737 -3.80279  1.000 74.16263  ? 85  GLY A O     1 
ATOM   618  N  N     . THR A 1 86  ? 2.49400   37.49956 -5.22740  1.000 69.03789  ? 86  THR A N     1 
ATOM   619  C  CA    . THR A 1 86  ? 3.55002   38.42455 -4.82868  1.000 71.28598  ? 86  THR A CA    1 
ATOM   620  C  C     . THR A 1 86  ? 3.24900   39.81195 -5.38577  1.000 79.82694  ? 86  THR A C     1 
ATOM   621  O  O     . THR A 1 86  ? 3.25208   40.01446 -6.60462  1.000 81.86727  ? 86  THR A O     1 
ATOM   622  C  CB    . THR A 1 86  ? 4.90790   37.92715 -5.31640  1.000 79.65137  ? 86  THR A CB    1 
ATOM   623  O  OG1   . THR A 1 86  ? 5.05694   36.53907 -4.99307  1.000 74.49034  ? 86  THR A OG1   1 
ATOM   624  C  CG2   . THR A 1 86  ? 6.02610   38.71798 -4.65541  1.000 84.73753  ? 86  THR A CG2   1 
ATOM   625  N  N     . ILE A 1 87  ? 2.98708   40.76635 -4.49798  1.000 74.60759  ? 87  ILE A N     1 
ATOM   626  C  CA    . ILE A 1 87  ? 2.80846   42.16556 -4.86878  1.000 86.67103  ? 87  ILE A CA    1 
ATOM   627  C  C     . ILE A 1 87  ? 4.13207   42.87074 -4.60141  1.000 86.41451  ? 87  ILE A C     1 
ATOM   628  O  O     . ILE A 1 87  ? 4.48888   43.12203 -3.44515  1.000 82.58691  ? 87  ILE A O     1 
ATOM   629  C  CB    . ILE A 1 87  ? 1.65738   42.82156 -4.09394  1.000 83.62224  ? 87  ILE A CB    1 
ATOM   630  C  CG1   . ILE A 1 87  ? 0.40020   41.95218 -4.16220  1.000 79.09576  ? 87  ILE A CG1   1 
ATOM   631  C  CG2   . ILE A 1 87  ? 1.36800   44.20669 -4.65210  1.000 82.37118  ? 87  ILE A CG2   1 
ATOM   632  C  CD1   . ILE A 1 87  ? -0.13108  41.76104 -5.56411  1.000 79.75007  ? 87  ILE A CD1   1 
ATOM   633  N  N     . ASP A 1 88  ? 4.86682   43.18297 -5.66715  1.000 85.05084  ? 88  ASP A N     1 
ATOM   634  C  CA    . ASP A 1 88  ? 6.18924   43.77607 -5.51960  1.000 88.41811  ? 88  ASP A CA    1 
ATOM   635  C  C     . ASP A 1 88  ? 6.09798   45.15343 -4.87061  1.000 94.34198  ? 88  ASP A C     1 
ATOM   636  O  O     . ASP A 1 88  ? 5.07661   45.83946 -4.95374  1.000 94.78364  ? 88  ASP A O     1 
ATOM   637  C  CB    . ASP A 1 88  ? 6.87944   43.87544 -6.88280  1.000 96.48829  ? 88  ASP A CB    1 
ATOM   638  C  CG    . ASP A 1 88  ? 7.23945   42.51622 -7.45639  1.000 93.15157  ? 88  ASP A CG    1 
ATOM   639  O  OD1   . ASP A 1 88  ? 8.04202   41.79228 -6.82772  1.000 93.29734  ? 88  ASP A OD1   1 
ATOM   640  O  OD2   . ASP A 1 88  ? 6.71024   42.16615 -8.53171  1.000 92.74373  ? 88  ASP A OD2   1 
ATOM   641  N  N     . ALA A 1 89  ? 7.18844   45.55432 -4.21138  1.000 97.53477  ? 89  ALA A N     1 
ATOM   642  C  CA    . ALA A 1 89  ? 7.20653   46.84115 -3.52409  1.000 103.42230 ? 89  ALA A CA    1 
ATOM   643  C  C     . ALA A 1 89  ? 7.10612   48.00465 -4.50177  1.000 103.54387 ? 89  ALA A C     1 
ATOM   644  O  O     . ALA A 1 89  ? 6.56858   49.06220 -4.15323  1.000 101.09207 ? 89  ALA A O     1 
ATOM   645  C  CB    . ALA A 1 89  ? 8.47263   46.96604 -2.67743  1.000 101.05409 ? 89  ALA A CB    1 
ATOM   646  N  N     . ASP A 1 90  ? 7.61044   47.83105 -5.72445  1.000 104.24291 ? 90  ASP A N     1 
ATOM   647  C  CA    . ASP A 1 90  ? 7.59035   48.88148 -6.73453  1.000 111.89673 ? 90  ASP A CA    1 
ATOM   648  C  C     . ASP A 1 90  ? 6.39131   48.77795 -7.66682  1.000 111.44897 ? 90  ASP A C     1 
ATOM   649  O  O     . ASP A 1 90  ? 6.46151   49.24503 -8.81103  1.000 111.75138 ? 90  ASP A O     1 
ATOM   650  C  CB    . ASP A 1 90  ? 8.89079   48.86919 -7.54030  1.000 114.75494 ? 90  ASP A CB    1 
ATOM   651  C  CG    . ASP A 1 90  ? 9.25365   47.48556 -8.05405  1.000 113.14246 ? 90  ASP A CG    1 
ATOM   652  O  OD1   . ASP A 1 90  ? 8.35189   46.62930 -8.17201  1.000 111.00010 ? 90  ASP A OD1   1 
ATOM   653  O  OD2   . ASP A 1 90  ? 10.44840  47.25138 -8.32723  1.000 109.55265 ? 90  ASP A OD2   1 
ATOM   654  N  N     . TYR A 1 91  ? 5.29656   48.17169 -7.21598  1.000 105.84979 ? 91  TYR A N     1 
ATOM   655  C  CA    . TYR A 1 91  ? 4.10058   48.07305 -8.04022  1.000 108.12995 ? 91  TYR A CA    1 
ATOM   656  C  C     . TYR A 1 91  ? 3.26222   49.33354 -7.86589  1.000 101.70764 ? 91  TYR A C     1 
ATOM   657  O  O     . TYR A 1 91  ? 2.84432   49.66081 -6.74920  1.000 109.15952 ? 91  TYR A O     1 
ATOM   658  C  CB    . TYR A 1 91  ? 3.29223   46.82847 -7.67942  1.000 100.51799 ? 91  TYR A CB    1 
ATOM   659  C  CG    . TYR A 1 91  ? 2.18346   46.53415 -8.66398  1.000 101.02947 ? 91  TYR A CG    1 
ATOM   660  C  CD1   . TYR A 1 91  ? 2.46743   46.28728 -10.00153 1.000 101.05228 ? 91  TYR A CD1   1 
ATOM   661  C  CD2   . TYR A 1 91  ? 0.85569   46.50155 -8.25933  1.000 101.92487 ? 91  TYR A CD2   1 
ATOM   662  C  CE1   . TYR A 1 91  ? 1.46236   46.01991 -10.90937 1.000 97.93568  ? 91  TYR A CE1   1 
ATOM   663  C  CE2   . TYR A 1 91  ? -0.15842  46.23242 -9.16010  1.000 100.66929 ? 91  TYR A CE2   1 
ATOM   664  C  CZ    . TYR A 1 91  ? 0.15156   45.99289 -10.48439 1.000 102.61207 ? 91  TYR A CZ    1 
ATOM   665  O  OH    . TYR A 1 91  ? -0.84756  45.72430 -11.39150 1.000 98.94971  ? 91  TYR A OH    1 
ATOM   666  N  N     . ARG A 1 92  ? 3.02991   50.04534 -8.96887  1.000 101.98643 ? 92  ARG A N     1 
ATOM   667  C  CA    . ARG A 1 92  ? 2.20742   51.24772 -8.96648  1.000 110.73586 ? 92  ARG A CA    1 
ATOM   668  C  C     . ARG A 1 92  ? 0.97990   51.09913 -9.85802  1.000 113.98116 ? 92  ARG A C     1 
ATOM   669  O  O     . ARG A 1 92  ? 0.38571   52.10298 -10.26567 1.000 107.59465 ? 92  ARG A O     1 
ATOM   670  C  CB    . ARG A 1 92  ? 3.03963   52.46129 -9.38538  1.000 112.69801 ? 92  ARG A CB    1 
ATOM   671  C  CG    . ARG A 1 92  ? 4.15900   52.78611 -8.41287  1.000 110.23719 ? 92  ARG A CG    1 
ATOM   672  C  CD    . ARG A 1 92  ? 3.61852   52.96989 -7.00525  1.000 101.94490 ? 92  ARG A CD    1 
ATOM   673  N  NE    . ARG A 1 92  ? 4.33290   52.14791 -6.03645  1.000 109.20610 ? 92  ARG A NE    1 
ATOM   674  C  CZ    . ARG A 1 92  ? 5.44655   52.51360 -5.41683  1.000 113.45073 ? 92  ARG A CZ    1 
ATOM   675  N  NH1   . ARG A 1 92  ? 6.00765   53.69050 -5.64030  1.000 114.58945 ? 92  ARG A NH1   1 
ATOM   676  N  NH2   . ARG A 1 92  ? 6.01264   51.67600 -4.55260  1.000 106.23869 ? 92  ARG A NH2   1 
ATOM   677  N  N     . GLY A 1 93  ? 0.59156   49.86273 -10.17163 1.000 109.49740 ? 93  GLY A N     1 
ATOM   678  C  CA    . GLY A 1 93  ? -0.60317  49.59482 -10.93860 1.000 107.42343 ? 93  GLY A CA    1 
ATOM   679  C  C     . GLY A 1 93  ? -1.73697  49.09299 -10.06220 1.000 107.11554 ? 93  GLY A C     1 
ATOM   680  O  O     . GLY A 1 93  ? -1.65932  49.08684 -8.83191  1.000 105.85070 ? 93  GLY A O     1 
ATOM   681  N  N     . GLU A 1 94  ? -2.81259  48.66236 -10.72011 1.000 107.10333 ? 94  GLU A N     1 
ATOM   682  C  CA    . GLU A 1 94  ? -3.97754  48.17108 -9.99977  1.000 104.62234 ? 94  GLU A CA    1 
ATOM   683  C  C     . GLU A 1 94  ? -3.76938  46.71540 -9.59956  1.000 103.04684 ? 94  GLU A C     1 
ATOM   684  O  O     . GLU A 1 94  ? -3.43375  45.87442 -10.43836 1.000 102.48101 ? 94  GLU A O     1 
ATOM   685  C  CB    . GLU A 1 94  ? -5.23553  48.31569 -10.85222 1.000 105.42672 ? 94  GLU A CB    1 
ATOM   686  C  CG    . GLU A 1 94  ? -6.50307  48.44336 -10.02855 1.000 112.12873 ? 94  GLU A CG    1 
ATOM   687  C  CD    . GLU A 1 94  ? -7.64448  47.62001 -10.57629 1.000 111.54821 ? 94  GLU A CD    1 
ATOM   688  O  OE1   . GLU A 1 94  ? -8.13341  47.93119 -11.68246 1.000 110.39664 ? 94  GLU A OE1   1 
ATOM   689  O  OE2   . GLU A 1 94  ? -8.04126  46.65039 -9.89882  1.000 115.00946 ? 94  GLU A OE2   1 
ATOM   690  N  N     . VAL A 1 95  ? -3.95475  46.42281 -8.31130  1.000 102.42400 ? 95  VAL A N     1 
ATOM   691  C  CA    . VAL A 1 95  ? -3.81668  45.05498 -7.82299  1.000 98.03303  ? 95  VAL A CA    1 
ATOM   692  C  C     . VAL A 1 95  ? -5.01375  44.23214 -8.27869  1.000 93.68150  ? 95  VAL A C     1 
ATOM   693  O  O     . VAL A 1 95  ? -6.17070  44.63723 -8.10512  1.000 85.87331  ? 95  VAL A O     1 
ATOM   694  C  CB    . VAL A 1 95  ? -3.67561  45.03785 -6.29295  1.000 99.80468  ? 95  VAL A CB    1 
ATOM   695  C  CG1   . VAL A 1 95  ? -3.76653  43.61135 -5.76388  1.000 93.03783  ? 95  VAL A CG1   1 
ATOM   696  C  CG2   . VAL A 1 95  ? -2.35868  45.67697 -5.87353  1.000 103.11340 ? 95  VAL A CG2   1 
ATOM   697  N  N     . LYS A 1 96  ? -4.74143  43.07085 -8.86802  1.000 87.55825  ? 96  LYS A N     1 
ATOM   698  C  CA    . LYS A 1 96  ? -5.78094  42.16890 -9.33893  1.000 86.43686  ? 96  LYS A CA    1 
ATOM   699  C  C     . LYS A 1 96  ? -5.59840  40.78975 -8.71788  1.000 85.56686  ? 96  LYS A C     1 
ATOM   700  O  O     . LYS A 1 96  ? -4.48144  40.37938 -8.38646  1.000 75.33836  ? 96  LYS A O     1 
ATOM   701  C  CB    . LYS A 1 96  ? -5.77467  42.06132 -10.86780 1.000 92.41712  ? 96  LYS A CB    1 
ATOM   702  C  CG    . LYS A 1 96  ? -5.89126  43.40033 -11.58205 1.000 91.18992  ? 96  LYS A CG    1 
ATOM   703  C  CD    . LYS A 1 96  ? -6.03207  43.20822 -13.08072 1.000 97.26074  ? 96  LYS A CD    1 
ATOM   704  C  CE    . LYS A 1 96  ? -5.79472  44.50126 -13.83694 1.000 101.74123 ? 96  LYS A CE    1 
ATOM   705  N  NZ    . LYS A 1 96  ? -5.24932  44.22604 -15.19509 1.000 92.49284  ? 96  LYS A NZ    1 
ATOM   706  N  N     . VAL A 1 97  ? -6.71104  40.07647 -8.56452  1.000 87.75949  ? 97  VAL A N     1 
ATOM   707  C  CA    . VAL A 1 97  ? -6.74144  38.78100 -7.89642  1.000 72.10318  ? 97  VAL A CA    1 
ATOM   708  C  C     . VAL A 1 97  ? -7.20142  37.73148 -8.89730  1.000 81.72465  ? 97  VAL A C     1 
ATOM   709  O  O     . VAL A 1 97  ? -8.19991  37.93112 -9.59898  1.000 96.60040  ? 97  VAL A O     1 
ATOM   710  C  CB    . VAL A 1 97  ? -7.66084  38.80307 -6.66127  1.000 78.06378  ? 97  VAL A CB    1 
ATOM   711  C  CG1   . VAL A 1 97  ? -7.71324  37.43276 -6.01059  1.000 78.04949  ? 97  VAL A CG1   1 
ATOM   712  C  CG2   . VAL A 1 97  ? -7.18105  39.84811 -5.66634  1.000 72.70603  ? 97  VAL A CG2   1 
ATOM   713  N  N     . ILE A 1 98  ? -6.47580  36.61877 -8.95942  1.000 71.15336  ? 98  ILE A N     1 
ATOM   714  C  CA    . ILE A 1 98  ? -6.76201  35.53320 -9.89049  1.000 83.51333  ? 98  ILE A CA    1 
ATOM   715  C  C     . ILE A 1 98  ? -7.48932  34.44282 -9.11072  1.000 81.47818  ? 98  ILE A C     1 
ATOM   716  O  O     . ILE A 1 98  ? -6.87777  33.69187 -8.34600  1.000 76.52005  ? 98  ILE A O     1 
ATOM   717  C  CB    . ILE A 1 98  ? -5.48764  34.99992 -10.55034 1.000 81.24939  ? 98  ILE A CB    1 
ATOM   718  C  CG1   . ILE A 1 98  ? -4.72104  36.13408 -11.23394 1.000 83.98725  ? 98  ILE A CG1   1 
ATOM   719  C  CG2   . ILE A 1 98  ? -5.82808  33.90552 -11.55259 1.000 72.69204  ? 98  ILE A CG2   1 
ATOM   720  C  CD1   . ILE A 1 98  ? -3.40484  35.70085 -11.83527 1.000 72.09575  ? 98  ILE A CD1   1 
ATOM   721  N  N     . LEU A 1 99  ? -8.79996  34.35319 -9.30314  1.000 82.18859  ? 99  LEU A N     1 
ATOM   722  C  CA    . LEU A 1 99  ? -9.59731  33.28851 -8.71611  1.000 77.24568  ? 99  LEU A CA    1 
ATOM   723  C  C     . LEU A 1 99  ? -9.65281  32.09203 -9.65962  1.000 82.81022  ? 99  LEU A C     1 
ATOM   724  O  O     . LEU A 1 99  ? -9.38957  32.20389 -10.85873 1.000 96.75079  ? 99  LEU A O     1 
ATOM   725  C  CB    . LEU A 1 99  ? -11.01223 33.78015 -8.40791  1.000 83.90900  ? 99  LEU A CB    1 
ATOM   726  C  CG    . LEU A 1 99  ? -11.35281 34.08579 -6.94824  1.000 89.41076  ? 99  LEU A CG    1 
ATOM   727  C  CD1   . LEU A 1 99  ? -10.26286 34.91518 -6.29550  1.000 81.64406  ? 99  LEU A CD1   1 
ATOM   728  C  CD2   . LEU A 1 99  ? -12.69213 34.80084 -6.86075  1.000 95.57197  ? 99  LEU A CD2   1 
ATOM   729  N  N     . VAL A 1 100 ? -9.99894  30.93572 -9.10000  1.000 83.79470  ? 100 VAL A N     1 
ATOM   730  C  CA    . VAL A 1 100 ? -10.13745 29.71427 -9.88677  1.000 89.65443  ? 100 VAL A CA    1 
ATOM   731  C  C     . VAL A 1 100 ? -11.01178 28.74181 -9.10730  1.000 90.81719  ? 100 VAL A C     1 
ATOM   732  O  O     . VAL A 1 100 ? -10.88504 28.60910 -7.88675  1.000 91.17578  ? 100 VAL A O     1 
ATOM   733  C  CB    . VAL A 1 100 ? -8.75638  29.10630 -10.23501 1.000 82.38543  ? 100 VAL A CB    1 
ATOM   734  C  CG1   . VAL A 1 100 ? -7.95332  28.82265 -8.97516  1.000 83.70210  ? 100 VAL A CG1   1 
ATOM   735  C  CG2   . VAL A 1 100 ? -8.91931  27.84655 -11.07479 1.000 89.87057  ? 100 VAL A CG2   1 
ATOM   736  N  N     . ASN A 1 101 ? -11.91068 28.07119 -9.82401  1.000 100.27085 ? 101 ASN A N     1 
ATOM   737  C  CA    . ASN A 1 101 ? -12.84839 27.13118 -9.22358  1.000 100.55313 ? 101 ASN A CA    1 
ATOM   738  C  C     . ASN A 1 101 ? -12.27006 25.72414 -9.30042  1.000 97.97910  ? 101 ASN A C     1 
ATOM   739  O  O     . ASN A 1 101 ? -11.97332 25.22835 -10.39264 1.000 103.20174 ? 101 ASN A O     1 
ATOM   740  C  CB    . ASN A 1 101 ? -14.20036 27.19286 -9.93433  1.000 107.10017 ? 101 ASN A CB    1 
ATOM   741  C  CG    . ASN A 1 101 ? -15.29735 26.45317 -9.18507  1.000 112.03105 ? 101 ASN A CG    1 
ATOM   742  O  OD1   . ASN A 1 101 ? -15.03443 25.53177 -8.41144  1.000 106.33558 ? 101 ASN A OD1   1 
ATOM   743  N  ND2   . ASN A 1 101 ? -16.54050 26.85616 -9.41856  1.000 122.57690 ? 101 ASN A ND2   1 
ATOM   744  N  N     . LEU A 1 102 ? -12.11579 25.08327 -8.14317  1.000 103.00267 ? 102 LEU A N     1 
ATOM   745  C  CA    . LEU A 1 102 ? -11.70959 23.68652 -8.07208  1.000 94.13987  ? 102 LEU A CA    1 
ATOM   746  C  C     . LEU A 1 102 ? -12.82443 22.79015 -7.55071  1.000 93.16047  ? 102 LEU A C     1 
ATOM   747  O  O     . LEU A 1 102 ? -12.59662 21.59633 -7.32920  1.000 97.95133  ? 102 LEU A O     1 
ATOM   748  C  CB    . LEU A 1 102 ? -10.45535 23.53391 -7.20820  1.000 90.06289  ? 102 LEU A CB    1 
ATOM   749  C  CG    . LEU A 1 102 ? -9.11777  23.78093 -7.91471  1.000 95.85095  ? 102 LEU A CG    1 
ATOM   750  C  CD1   . LEU A 1 102 ? -9.04415  22.98591 -9.21148  1.000 90.47660  ? 102 LEU A CD1   1 
ATOM   751  C  CD2   . LEU A 1 102 ? -8.87572  25.26242 -8.17491  1.000 93.72308  ? 102 LEU A CD2   1 
ATOM   752  N  N     . GLY A 1 103 ? -14.02384 23.33939 -7.34577  1.000 97.51317  ? 103 GLY A N     1 
ATOM   753  C  CA    . GLY A 1 103 ? -15.18083 22.54438 -6.99815  1.000 101.79036 ? 103 GLY A CA    1 
ATOM   754  C  C     . GLY A 1 103 ? -15.95120 22.10080 -8.22984  1.000 114.15880 ? 103 GLY A C     1 
ATOM   755  O  O     . GLY A 1 103 ? -15.59296 22.39766 -9.36858  1.000 122.35628 ? 103 GLY A O     1 
ATOM   756  N  N     . ASN A 1 104 ? -17.03788 21.37059 -7.98405  1.000 126.79002 ? 104 ASN A N     1 
ATOM   757  C  CA    . ASN A 1 104 ? -17.87719 20.84630 -9.05314  1.000 127.90021 ? 104 ASN A CA    1 
ATOM   758  C  C     . ASN A 1 104 ? -19.16098 21.64467 -9.24421  1.000 132.82135 ? 104 ASN A C     1 
ATOM   759  O  O     . ASN A 1 104 ? -20.07691 21.17074 -9.92374  1.000 131.69454 ? 104 ASN A O     1 
ATOM   760  C  CB    . ASN A 1 104 ? -18.21253 19.37540 -8.79285  1.000 128.29187 ? 104 ASN A CB    1 
ATOM   761  C  CG    . ASN A 1 104 ? -18.89880 19.15951 -7.45823  1.000 124.09990 ? 104 ASN A CG    1 
ATOM   762  O  OD1   . ASN A 1 104 ? -20.07557 19.47998 -7.29212  1.000 128.41939 ? 104 ASN A OD1   1 
ATOM   763  N  ND2   . ASN A 1 104 ? -18.16687 18.60240 -6.50076  1.000 121.82863 ? 104 ASN A ND2   1 
ATOM   764  N  N     . GLU A 1 105 ? -19.25074 22.83910 -8.66404  1.000 153.08022 ? 105 GLU A N     1 
ATOM   765  C  CA    . GLU A 1 105 ? -20.42398 23.68837 -8.79950  1.000 151.15872 ? 105 GLU A CA    1 
ATOM   766  C  C     . GLU A 1 105 ? -20.00011 25.06468 -9.29068  1.000 150.43023 ? 105 GLU A C     1 
ATOM   767  O  O     . GLU A 1 105 ? -18.89638 25.53239 -8.99756  1.000 150.84789 ? 105 GLU A O     1 
ATOM   768  C  CB    . GLU A 1 105 ? -21.18125 23.83087 -7.46764  1.000 153.96371 ? 105 GLU A CB    1 
ATOM   769  C  CG    . GLU A 1 105 ? -21.28257 22.55278 -6.64410  1.000 153.95225 ? 105 GLU A CG    1 
ATOM   770  C  CD    . GLU A 1 105 ? -22.39214 21.62812 -7.10891  1.000 161.05637 ? 105 GLU A CD    1 
ATOM   771  O  OE1   . GLU A 1 105 ? -23.04411 21.93502 -8.12886  1.000 162.81191 ? 105 GLU A OE1   1 
ATOM   772  O  OE2   . GLU A 1 105 ? -22.61555 20.59284 -6.44646  1.000 163.54681 ? 105 GLU A OE2   1 
ATOM   773  N  N     . GLU A 1 106 ? -20.88776 25.71053 -10.04248 1.000 138.04987 ? 106 GLU A N     1 
ATOM   774  C  CA    . GLU A 1 106 ? -20.63992 27.07994 -10.47063 1.000 132.04294 ? 106 GLU A CA    1 
ATOM   775  C  C     . GLU A 1 106 ? -20.79546 28.03161 -9.29070  1.000 127.62766 ? 106 GLU A C     1 
ATOM   776  O  O     . GLU A 1 106 ? -21.68521 27.86663 -8.45159  1.000 124.33215 ? 106 GLU A O     1 
ATOM   777  C  CB    . GLU A 1 106 ? -21.59601 27.47047 -11.59734 1.000 123.21169 ? 106 GLU A CB    1 
ATOM   778  N  N     . VAL A 1 107 ? -19.92071 29.03176 -9.22737  1.000 123.79537 ? 107 VAL A N     1 
ATOM   779  C  CA    . VAL A 1 107 ? -19.87812 29.97831 -8.12020  1.000 124.09843 ? 107 VAL A CA    1 
ATOM   780  C  C     . VAL A 1 107 ? -20.22518 31.36497 -8.64429  1.000 126.06326 ? 107 VAL A C     1 
ATOM   781  O  O     . VAL A 1 107 ? -19.83228 31.73652 -9.75537  1.000 128.17918 ? 107 VAL A O     1 
ATOM   782  C  CB    . VAL A 1 107 ? -18.49571 29.97336 -7.43308  1.000 122.23763 ? 107 VAL A CB    1 
ATOM   783  C  CG1   . VAL A 1 107 ? -18.47073 30.93550 -6.25546  1.000 122.49274 ? 107 VAL A CG1   1 
ATOM   784  C  CG2   . VAL A 1 107 ? -18.14184 28.56541 -6.97950  1.000 112.11740 ? 107 VAL A CG2   1 
ATOM   785  N  N     . VAL A 1 108 ? -20.97256 32.12333 -7.84671  1.000 131.96519 ? 108 VAL A N     1 
ATOM   786  C  CA    . VAL A 1 108 ? -21.37882 33.48165 -8.18811  1.000 132.24255 ? 108 VAL A CA    1 
ATOM   787  C  C     . VAL A 1 108 ? -20.67210 34.43254 -7.23244  1.000 129.43239 ? 108 VAL A C     1 
ATOM   788  O  O     . VAL A 1 108 ? -20.82933 34.32581 -6.00955  1.000 126.77693 ? 108 VAL A O     1 
ATOM   789  C  CB    . VAL A 1 108 ? -22.90342 33.65227 -8.11412  1.000 127.92386 ? 108 VAL A CB    1 
ATOM   790  C  CG1   . VAL A 1 108 ? -23.32788 34.93900 -8.80136  1.000 129.61241 ? 108 VAL A CG1   1 
ATOM   791  C  CG2   . VAL A 1 108 ? -23.60170 32.45140 -8.73284  1.000 130.05592 ? 108 VAL A CG2   1 
ATOM   792  N  N     . ILE A 1 109 ? -19.89582 35.35941 -7.78648  1.000 129.26924 ? 109 ILE A N     1 
ATOM   793  C  CA    . ILE A 1 109 ? -19.10640 36.30189 -7.00190  1.000 123.87919 ? 109 ILE A CA    1 
ATOM   794  C  C     . ILE A 1 109 ? -19.81699 37.64764 -7.00521  1.000 125.97982 ? 109 ILE A C     1 
ATOM   795  O  O     . ILE A 1 109 ? -19.99653 38.26341 -8.06285  1.000 126.23456 ? 109 ILE A O     1 
ATOM   796  C  CB    . ILE A 1 109 ? -17.67707 36.43045 -7.54968  1.000 118.09072 ? 109 ILE A CB    1 
ATOM   797  C  CG1   . ILE A 1 109 ? -17.02653 35.05128 -7.65590  1.000 120.58718 ? 109 ILE A CG1   1 
ATOM   798  C  CG2   . ILE A 1 109 ? -16.84924 37.34763 -6.66092  1.000 121.18546 ? 109 ILE A CG2   1 
ATOM   799  C  CD1   . ILE A 1 109 ? -16.99572 34.29776 -6.34888  1.000 118.80053 ? 109 ILE A CD1   1 
ATOM   800  N  N     . GLU A 1 110 ? -20.21377 38.10557 -5.82198  1.000 136.47086 ? 110 GLU A N     1 
ATOM   801  C  CA    . GLU A 1 110 ? -20.90633 39.37478 -5.67946  1.000 135.48569 ? 110 GLU A CA    1 
ATOM   802  C  C     . GLU A 1 110 ? -19.92656 40.54122 -5.78627  1.000 135.74300 ? 110 GLU A C     1 
ATOM   803  O  O     . GLU A 1 110 ? -18.71343 40.39065 -5.61477  1.000 132.18548 ? 110 GLU A O     1 
ATOM   804  C  CB    . GLU A 1 110 ? -21.64553 39.43090 -4.34127  1.000 132.58497 ? 110 GLU A CB    1 
ATOM   805  C  CG    . GLU A 1 110 ? -22.75208 38.39551 -4.19240  1.000 136.41251 ? 110 GLU A CG    1 
ATOM   806  C  CD    . GLU A 1 110 ? -24.08106 38.87435 -4.74469  1.000 155.74432 ? 110 GLU A CD    1 
ATOM   807  O  OE1   . GLU A 1 110 ? -24.37754 40.08144 -4.61933  1.000 156.78340 ? 110 GLU A OE1   1 
ATOM   808  O  OE2   . GLU A 1 110 ? -24.82839 38.04442 -5.30433  1.000 164.72209 ? 110 GLU A OE2   1 
ATOM   809  N  N     . ARG A 1 111 ? -20.47455 41.71874 -6.07812  1.000 126.09490 ? 111 ARG A N     1 
ATOM   810  C  CA    . ARG A 1 111 ? -19.66660 42.92918 -6.13723  1.000 119.01257 ? 111 ARG A CA    1 
ATOM   811  C  C     . ARG A 1 111 ? -19.29664 43.37870 -4.72908  1.000 116.07691 ? 111 ARG A C     1 
ATOM   812  O  O     . ARG A 1 111 ? -20.16375 43.51897 -3.86080  1.000 105.38109 ? 111 ARG A O     1 
ATOM   813  C  CB    . ARG A 1 111 ? -20.42153 44.03676 -6.87052  1.000 115.66087 ? 111 ARG A CB    1 
ATOM   814  N  N     . GLY A 1 112 ? -18.00438 43.60411 -4.50414  1.000 116.23062 ? 112 GLY A N     1 
ATOM   815  C  CA    . GLY A 1 112 ? -17.50921 43.95446 -3.19152  1.000 110.41526 ? 112 GLY A CA    1 
ATOM   816  C  C     . GLY A 1 112 ? -17.29809 42.78637 -2.25557  1.000 110.89476 ? 112 GLY A C     1 
ATOM   817  O  O     . GLY A 1 112 ? -16.96438 43.00617 -1.08428  1.000 108.06194 ? 112 GLY A O     1 
ATOM   818  N  N     . GLU A 1 113 ? -17.47960 41.55626 -2.72667  1.000 113.89389 ? 113 GLU A N     1 
ATOM   819  C  CA    . GLU A 1 113 ? -17.31538 40.39439 -1.86618  1.000 120.96278 ? 113 GLU A CA    1 
ATOM   820  C  C     . GLU A 1 113 ? -15.83652 40.12206 -1.61995  1.000 106.45524 ? 113 GLU A C     1 
ATOM   821  O  O     . GLU A 1 113 ? -15.00263 40.27090 -2.51768  1.000 103.43571 ? 113 GLU A O     1 
ATOM   822  C  CB    . GLU A 1 113 ? -17.98909 39.17433 -2.49590  1.000 125.80328 ? 113 GLU A CB    1 
ATOM   823  C  CG    . GLU A 1 113 ? -17.88017 37.89766 -1.67956  1.000 126.87452 ? 113 GLU A CG    1 
ATOM   824  C  CD    . GLU A 1 113 ? -18.72113 36.77191 -2.24769  1.000 127.90996 ? 113 GLU A CD    1 
ATOM   825  O  OE1   . GLU A 1 113 ? -19.58116 37.04747 -3.11129  1.000 119.76424 ? 113 GLU A OE1   1 
ATOM   826  O  OE2   . GLU A 1 113 ? -18.52166 35.61188 -1.83029  1.000 123.07567 ? 113 GLU A OE2   1 
ATOM   827  N  N     . ARG A 1 114 ? -15.51262 39.73732 -0.38691  1.000 106.44536 ? 114 ARG A N     1 
ATOM   828  C  CA    . ARG A 1 114 ? -14.13704 39.41292 -0.03032  1.000 101.62369 ? 114 ARG A CA    1 
ATOM   829  C  C     . ARG A 1 114 ? -13.68986 38.16821 -0.78681  1.000 101.52944 ? 114 ARG A C     1 
ATOM   830  O  O     . ARG A 1 114 ? -14.27570 37.09222 -0.62807  1.000 108.11654 ? 114 ARG A O     1 
ATOM   831  C  CB    . ARG A 1 114 ? -14.01651 39.20034 1.47655   1.000 104.31780 ? 114 ARG A CB    1 
ATOM   832  N  N     . ILE A 1 115 ? -12.65526 38.31596 -1.61007  1.000 93.60834  ? 115 ILE A N     1 
ATOM   833  C  CA    . ILE A 1 115 ? -12.16415 37.22178 -2.43581  1.000 86.47215  ? 115 ILE A CA    1 
ATOM   834  C  C     . ILE A 1 115 ? -10.81073 36.69615 -1.97597  1.000 88.00933  ? 115 ILE A C     1 
ATOM   835  O  O     . ILE A 1 115 ? -10.48186 35.53810 -2.27838  1.000 84.96182  ? 115 ILE A O     1 
ATOM   836  C  CB    . ILE A 1 115 ? -12.09247 37.63901 -3.91777  1.000 91.47525  ? 115 ILE A CB    1 
ATOM   837  C  CG1   . ILE A 1 115 ? -11.25200 38.90851 -4.05845  1.000 93.74578  ? 115 ILE A CG1   1 
ATOM   838  C  CG2   . ILE A 1 115 ? -13.48949 37.84813 -4.47889  1.000 85.74338  ? 115 ILE A CG2   1 
ATOM   839  C  CD1   . ILE A 1 115 ? -11.11955 39.39573 -5.47188  1.000 95.95713  ? 115 ILE A CD1   1 
ATOM   840  N  N     . ALA A 1 116 ? -10.02006 37.49629 -1.26874  1.000 83.46760  ? 116 ALA A N     1 
ATOM   841  C  CA    . ALA A 1 116 ? -8.71260  37.07699 -0.78409  1.000 75.53755  ? 116 ALA A CA    1 
ATOM   842  C  C     . ALA A 1 116 ? -8.30290  38.02020 0.33881   1.000 84.16782  ? 116 ALA A C     1 
ATOM   843  O  O     . ALA A 1 116 ? -9.04584  38.93175 0.71288   1.000 86.52804  ? 116 ALA A O     1 
ATOM   844  C  CB    . ALA A 1 116 ? -7.68037  37.06203 -1.91500  1.000 72.64923  ? 116 ALA A CB    1 
ATOM   845  N  N     . GLN A 1 117 ? -7.11054  37.79350 0.87973   1.000 75.90383  ? 117 GLN A N     1 
ATOM   846  C  CA    . GLN A 1 117 ? -6.55158  38.66965 1.89502   1.000 78.65867  ? 117 GLN A CA    1 
ATOM   847  C  C     . GLN A 1 117 ? -5.15229  39.10196 1.48574   1.000 79.85281  ? 117 GLN A C     1 
ATOM   848  O  O     . GLN A 1 117 ? -4.40447  38.34038 0.86682   1.000 72.48275  ? 117 GLN A O     1 
ATOM   849  C  CB    . GLN A 1 117 ? -6.51836  37.99895 3.27693   1.000 68.49682  ? 117 GLN A CB    1 
ATOM   850  C  CG    . GLN A 1 117 ? -6.00551  36.56852 3.28764   1.000 76.68257  ? 117 GLN A CG    1 
ATOM   851  C  CD    . GLN A 1 117 ? -6.00069  35.96686 4.68533   1.000 89.21752  ? 117 GLN A CD    1 
ATOM   852  O  OE1   . GLN A 1 117 ? -5.47152  36.55875 5.62735   1.000 78.96535  ? 117 GLN A OE1   1 
ATOM   853  N  NE2   . GLN A 1 117 ? -6.60034  34.78931 4.82621   1.000 86.84739  ? 117 GLN A NE2   1 
ATOM   854  N  N     . LEU A 1 118 ? -4.81309  40.34161 1.82990   1.000 83.03958  ? 118 LEU A N     1 
ATOM   855  C  CA    . LEU A 1 118 ? -3.51173  40.92588 1.53163   1.000 80.84092  ? 118 LEU A CA    1 
ATOM   856  C  C     . LEU A 1 118 ? -2.70313  41.00023 2.81887   1.000 75.64378  ? 118 LEU A C     1 
ATOM   857  O  O     . LEU A 1 118 ? -3.09022  41.70283 3.75881   1.000 88.67904  ? 118 LEU A O     1 
ATOM   858  C  CB    . LEU A 1 118 ? -3.66173  42.31347 0.90908   1.000 82.81607  ? 118 LEU A CB    1 
ATOM   859  C  CG    . LEU A 1 118 ? -2.35480  43.05348 0.62123   1.000 89.08244  ? 118 LEU A CG    1 
ATOM   860  C  CD1   . LEU A 1 118 ? -1.49694  42.27011 -0.36229  1.000 72.18970  ? 118 LEU A CD1   1 
ATOM   861  C  CD2   . LEU A 1 118 ? -2.64122  44.44916 0.09800   1.000 85.02318  ? 118 LEU A CD2   1 
ATOM   862  N  N     . VAL A 1 119 ? -1.58786  40.27680 2.85937   1.000 74.34814  ? 119 VAL A N     1 
ATOM   863  C  CA    . VAL A 1 119 ? -0.72740  40.20280 4.03415   1.000 82.91489  ? 119 VAL A CA    1 
ATOM   864  C  C     . VAL A 1 119 ? 0.57242   40.93064 3.72625   1.000 83.10566  ? 119 VAL A C     1 
ATOM   865  O  O     . VAL A 1 119 ? 1.22658   40.64503 2.71574   1.000 86.87421  ? 119 VAL A O     1 
ATOM   866  C  CB    . VAL A 1 119 ? -0.45515  38.74446 4.44178   1.000 82.10420  ? 119 VAL A CB    1 
ATOM   867  C  CG1   . VAL A 1 119 ? 0.41976   38.69408 5.68464   1.000 78.79239  ? 119 VAL A CG1   1 
ATOM   868  C  CG2   . VAL A 1 119 ? -1.76274  38.00491 4.67011   1.000 77.42125  ? 119 VAL A CG2   1 
ATOM   869  N  N     . ILE A 1 120 ? 0.94432   41.86737 4.59345   1.000 82.68974  ? 120 ILE A N     1 
ATOM   870  C  CA    . ILE A 1 120 ? 2.19964   42.59692 4.46140   1.000 88.60255  ? 120 ILE A CA    1 
ATOM   871  C  C     . ILE A 1 120 ? 3.26452   41.88501 5.28308   1.000 88.24631  ? 120 ILE A C     1 
ATOM   872  O  O     . ILE A 1 120 ? 3.06316   41.60559 6.47106   1.000 91.40422  ? 120 ILE A O     1 
ATOM   873  C  CB    . ILE A 1 120 ? 2.04050   44.05798 4.91086   1.000 87.34995  ? 120 ILE A CB    1 
ATOM   874  C  CG1   . ILE A 1 120 ? 0.91073   44.73422 4.13185   1.000 89.69129  ? 120 ILE A CG1   1 
ATOM   875  C  CG2   . ILE A 1 120 ? 3.34795   44.81241 4.72271   1.000 89.97437  ? 120 ILE A CG2   1 
ATOM   876  C  CD1   . ILE A 1 120 ? 1.13741   44.77214 2.63451   1.000 88.36943  ? 120 ILE A CD1   1 
ATOM   877  N  N     . ALA A 1 121 ? 4.39723   41.59152 4.65370   1.000 90.99926  ? 121 ALA A N     1 
ATOM   878  C  CA    . ALA A 1 121 ? 5.47763   40.85167 5.28405   1.000 100.89180 ? 121 ALA A CA    1 
ATOM   879  C  C     . ALA A 1 121 ? 6.81238   41.43039 4.84294   1.000 108.32055 ? 121 ALA A C     1 
ATOM   880  O  O     . ALA A 1 121 ? 6.92011   41.97893 3.73949   1.000 104.47489 ? 121 ALA A O     1 
ATOM   881  C  CB    . ALA A 1 121 ? 5.41881   39.35730 4.92868   1.000 96.96851  ? 121 ALA A CB    1 
ATOM   882  N  N     . PRO A 1 122 ? 7.84306   41.33233 5.68463   1.000 122.27554 ? 122 PRO A N     1 
ATOM   883  C  CA    . PRO A 1 122 ? 9.17027   41.82382 5.28860   1.000 123.22223 ? 122 PRO A CA    1 
ATOM   884  C  C     . PRO A 1 122 ? 9.84943   40.85492 4.32971   1.000 121.59752 ? 122 PRO A C     1 
ATOM   885  O  O     . PRO A 1 122 ? 9.86041   39.64174 4.55223   1.000 119.85877 ? 122 PRO A O     1 
ATOM   886  C  CB    . PRO A 1 122 ? 9.92581   41.91708 6.61897   1.000 127.07002 ? 122 PRO A CB    1 
ATOM   887  C  CG    . PRO A 1 122 ? 9.27105   40.89135 7.48198   1.000 125.30402 ? 122 PRO A CG    1 
ATOM   888  C  CD    . PRO A 1 122 ? 7.81730   40.87907 7.08694   1.000 122.21172 ? 122 PRO A CD    1 
ATOM   889  N  N     . VAL A 1 123 ? 10.41371  41.40061 3.25626   1.000 110.89548 ? 123 VAL A N     1 
ATOM   890  C  CA    . VAL A 1 123 ? 11.16516  40.63148 2.27264   1.000 109.48202 ? 123 VAL A CA    1 
ATOM   891  C  C     . VAL A 1 123 ? 12.62663  41.04687 2.36329   1.000 108.71943 ? 123 VAL A C     1 
ATOM   892  O  O     . VAL A 1 123 ? 12.93596  42.22118 2.59942   1.000 108.72206 ? 123 VAL A O     1 
ATOM   893  C  CB    . VAL A 1 123 ? 10.60692  40.83354 0.84832   1.000 105.51040 ? 123 VAL A CB    1 
ATOM   894  C  CG1   . VAL A 1 123 ? 10.68797  42.29883 0.43473   1.000 106.80940 ? 123 VAL A CG1   1 
ATOM   895  C  CG2   . VAL A 1 123 ? 11.33232  39.94058 -0.15119  1.000 100.72731 ? 123 VAL A CG2   1 
ATOM   896  N  N     . GLN A 1 124 ? 13.52419  40.08015 2.19528   1.000 102.70245 ? 124 GLN A N     1 
ATOM   897  C  CA    . GLN A 1 124 ? 14.95692  40.30086 2.33969   1.000 109.57756 ? 124 GLN A CA    1 
ATOM   898  C  C     . GLN A 1 124 ? 15.61169  40.28520 0.96540   1.000 110.36690 ? 124 GLN A C     1 
ATOM   899  O  O     . GLN A 1 124 ? 15.60069  39.25684 0.27940   1.000 102.99456 ? 124 GLN A O     1 
ATOM   900  C  CB    . GLN A 1 124 ? 15.58430  39.23984 3.24467   1.000 106.13650 ? 124 GLN A CB    1 
ATOM   901  C  CG    . GLN A 1 124 ? 16.98783  39.57896 3.72696   1.000 111.89983 ? 124 GLN A CG    1 
ATOM   902  C  CD    . GLN A 1 124 ? 16.99127  40.57708 4.87253   1.000 119.57771 ? 124 GLN A CD    1 
ATOM   903  O  OE1   . GLN A 1 124 ? 18.03941  41.09838 5.25286   1.000 123.78586 ? 124 GLN A OE1   1 
ATOM   904  N  NE2   . GLN A 1 124 ? 15.81668  40.84079 5.43370   1.000 125.94524 ? 124 GLN A NE2   1 
ATOM   905  N  N     . ARG A 1 125 ? 16.17144  41.42455 0.56735   1.000 108.46021 ? 125 ARG A N     1 
ATOM   906  C  CA    . ARG A 1 125 ? 16.97588  41.48200 -0.64391  1.000 103.58841 ? 125 ARG A CA    1 
ATOM   907  C  C     . ARG A 1 125 ? 18.30227  40.77169 -0.40903  1.000 102.43227 ? 125 ARG A C     1 
ATOM   908  O  O     . ARG A 1 125 ? 18.88685  40.85786 0.67492   1.000 102.13420 ? 125 ARG A O     1 
ATOM   909  C  CB    . ARG A 1 125 ? 17.21804  42.93474 -1.05273  1.000 106.95984 ? 125 ARG A CB    1 
ATOM   910  C  CG    . ARG A 1 125 ? 17.70755  43.12239 -2.48010  1.000 105.42602 ? 125 ARG A CG    1 
ATOM   911  C  CD    . ARG A 1 125 ? 16.55991  43.03427 -3.47244  1.000 105.19510 ? 125 ARG A CD    1 
ATOM   912  N  NE    . ARG A 1 125 ? 16.90332  43.65306 -4.74717  1.000 110.10603 ? 125 ARG A NE    1 
ATOM   913  C  CZ    . ARG A 1 125 ? 16.04515  43.86427 -5.73557  1.000 105.43766 ? 125 ARG A CZ    1 
ATOM   914  N  NH1   . ARG A 1 125 ? 14.76986  43.52983 -5.62750  1.000 99.86383  ? 125 ARG A NH1   1 
ATOM   915  N  NH2   . ARG A 1 125 ? 16.47818  44.42410 -6.86144  1.000 113.12080 ? 125 ARG A NH2   1 
ATOM   916  N  N     . VAL A 1 126 ? 18.77822  40.06112 -1.42907  1.000 105.13240 ? 126 VAL A N     1 
ATOM   917  C  CA    . VAL A 1 126 ? 19.97892  39.24772 -1.29926  1.000 108.20446 ? 126 VAL A CA    1 
ATOM   918  C  C     . VAL A 1 126 ? 20.87582  39.47030 -2.50992  1.000 100.53471 ? 126 VAL A C     1 
ATOM   919  O  O     . VAL A 1 126 ? 20.41097  39.80986 -3.60264  1.000 97.74371  ? 126 VAL A O     1 
ATOM   920  C  CB    . VAL A 1 126 ? 19.62998  37.75069 -1.12598  1.000 103.51231 ? 126 VAL A CB    1 
ATOM   921  C  CG1   . VAL A 1 126 ? 19.43394  37.07142 -2.47577  1.000 97.55682  ? 126 VAL A CG1   1 
ATOM   922  C  CG2   . VAL A 1 126 ? 20.69032  37.04992 -0.29734  1.000 104.27855 ? 126 VAL A CG2   1 
ATOM   923  N  N     . GLU A 1 127 ? 22.17696  39.29149 -2.29985  1.000 103.25678 ? 127 GLU A N     1 
ATOM   924  C  CA    . GLU A 1 127 ? 23.17694  39.45901 -3.34553  1.000 105.52224 ? 127 GLU A CA    1 
ATOM   925  C  C     . GLU A 1 127 ? 23.56128  38.08664 -3.88285  1.000 108.10593 ? 127 GLU A C     1 
ATOM   926  O  O     . GLU A 1 127 ? 24.02239  37.22582 -3.12550  1.000 108.76072 ? 127 GLU A O     1 
ATOM   927  C  CB    . GLU A 1 127 ? 24.40592  40.19523 -2.81243  1.000 105.29299 ? 127 GLU A CB    1 
ATOM   928  N  N     . VAL A 1 128 ? 23.37074  37.88677 -5.18367  1.000 111.51453 ? 128 VAL A N     1 
ATOM   929  C  CA    . VAL A 1 128 ? 23.64908  36.60186 -5.81701  1.000 111.73156 ? 128 VAL A CA    1 
ATOM   930  C  C     . VAL A 1 128 ? 25.13785  36.53704 -6.14100  1.000 110.30316 ? 128 VAL A C     1 
ATOM   931  O  O     . VAL A 1 128 ? 25.61448  37.20882 -7.05881  1.000 113.76764 ? 128 VAL A O     1 
ATOM   932  C  CB    . VAL A 1 128 ? 22.79936  36.39932 -7.07573  1.000 112.57869 ? 128 VAL A CB    1 
ATOM   933  C  CG1   . VAL A 1 128 ? 23.17536  35.09601 -7.76357  1.000 103.41702 ? 128 VAL A CG1   1 
ATOM   934  C  CG2   . VAL A 1 128 ? 21.31960  36.41620 -6.72290  1.000 107.55193 ? 128 VAL A CG2   1 
ATOM   935  N  N     . VAL A 1 129 ? 25.87387  35.72733 -5.38579  1.000 104.18693 ? 129 VAL A N     1 
ATOM   936  C  CA    . VAL A 1 129 ? 27.29118  35.48305 -5.62563  1.000 115.29671 ? 129 VAL A CA    1 
ATOM   937  C  C     . VAL A 1 129 ? 27.44738  33.99954 -5.93165  1.000 120.99945 ? 129 VAL A C     1 
ATOM   938  O  O     . VAL A 1 129 ? 27.18155  33.14734 -5.07316  1.000 118.83587 ? 129 VAL A O     1 
ATOM   939  C  CB    . VAL A 1 129 ? 28.16358  35.90928 -4.43526  1.000 112.52794 ? 129 VAL A CB    1 
ATOM   940  C  CG1   . VAL A 1 129 ? 27.49659  35.54065 -3.11361  1.000 116.78449 ? 129 VAL A CG1   1 
ATOM   941  C  CG2   . VAL A 1 129 ? 29.54917  35.28522 -4.53806  1.000 103.86630 ? 129 VAL A CG2   1 
ATOM   942  N  N     . GLU A 1 130 ? 27.85789  33.68731 -7.15815  1.000 118.78648 ? 130 GLU A N     1 
ATOM   943  C  CA    . GLU A 1 130 ? 28.02300  32.29584 -7.55267  1.000 118.58520 ? 130 GLU A CA    1 
ATOM   944  C  C     . GLU A 1 130 ? 29.25756  31.69396 -6.89578  1.000 116.79381 ? 130 GLU A C     1 
ATOM   945  O  O     . GLU A 1 130 ? 30.32897  32.30603 -6.86749  1.000 115.41109 ? 130 GLU A O     1 
ATOM   946  C  CB    . GLU A 1 130 ? 28.12932  32.17502 -9.07233  1.000 116.95155 ? 130 GLU A CB    1 
ATOM   947  C  CG    . GLU A 1 130 ? 28.37930  30.75141 -9.55561  1.000 121.88140 ? 130 GLU A CG    1 
ATOM   948  C  CD    . GLU A 1 130 ? 28.25171  30.60842 -11.05791 1.000 120.26004 ? 130 GLU A CD    1 
ATOM   949  O  OE1   . GLU A 1 130 ? 28.05034  31.63602 -11.73738 1.000 118.26881 ? 130 GLU A OE1   1 
ATOM   950  O  OE2   . GLU A 1 130 ? 28.34837  29.46744 -11.55840 1.000 119.37126 ? 130 GLU A OE2   1 
ATOM   951  N  N     . VAL A 1 131 ? 29.09749  30.48438 -6.36261  1.000 113.73506 ? 131 VAL A N     1 
ATOM   952  C  CA    . VAL A 1 131 ? 30.17329  29.76317 -5.70196  1.000 112.48388 ? 131 VAL A CA    1 
ATOM   953  C  C     . VAL A 1 131 ? 30.38486  28.43453 -6.41755  1.000 114.05888 ? 131 VAL A C     1 
ATOM   954  O  O     . VAL A 1 131 ? 29.56192  27.99330 -7.21965  1.000 109.67049 ? 131 VAL A O     1 
ATOM   955  C  CB    . VAL A 1 131 ? 29.89108  29.53512 -4.20478  1.000 117.16221 ? 131 VAL A CB    1 
ATOM   956  C  CG1   . VAL A 1 131 ? 29.78532  30.86355 -3.47588  1.000 117.92693 ? 131 VAL A CG1   1 
ATOM   957  C  CG2   . VAL A 1 131 ? 28.62018  28.71441 -4.02557  1.000 112.38628 ? 131 VAL A CG2   1 
ATOM   958  N  N     . GLU A 1 132 ? 31.51555  27.80170 -6.11400  1.000 120.04588 ? 132 GLU A N     1 
ATOM   959  C  CA    . GLU A 1 132 ? 31.83934  26.47711 -6.62179  1.000 118.58082 ? 132 GLU A CA    1 
ATOM   960  C  C     . GLU A 1 132 ? 31.63166  25.38680 -5.58091  1.000 117.70661 ? 132 GLU A C     1 
ATOM   961  O  O     . GLU A 1 132 ? 31.88218  24.21265 -5.87182  1.000 115.07755 ? 132 GLU A O     1 
ATOM   962  C  CB    . GLU A 1 132 ? 33.28676  26.44276 -7.12497  1.000 103.16914 ? 132 GLU A CB    1 
ATOM   963  N  N     . GLU A 1 133 ? 31.18087  25.74525 -4.38082  1.000 117.07056 ? 133 GLU A N     1 
ATOM   964  C  CA    . GLU A 1 133 ? 30.96141  24.77463 -3.31955  1.000 117.04501 ? 133 GLU A CA    1 
ATOM   965  C  C     . GLU A 1 133 ? 30.04446  25.38606 -2.27157  1.000 113.58838 ? 133 GLU A C     1 
ATOM   966  O  O     . GLU A 1 133 ? 30.19128  26.55906 -1.91936  1.000 115.65919 ? 133 GLU A O     1 
ATOM   967  C  CB    . GLU A 1 133 ? 32.28377  24.34045 -2.67639  1.000 112.32709 ? 133 GLU A CB    1 
ATOM   968  N  N     . VAL A 1 134 ? 29.10340  24.58580 -1.78259  1.000 113.01763 ? 134 VAL A N     1 
ATOM   969  C  CA    . VAL A 1 134 ? 28.21774  24.99203 -0.70262  1.000 109.83302 ? 134 VAL A CA    1 
ATOM   970  C  C     . VAL A 1 134 ? 28.63994  24.26529 0.56658   1.000 116.18402 ? 134 VAL A C     1 
ATOM   971  O  O     . VAL A 1 134 ? 29.27228  23.20439 0.52946   1.000 112.28887 ? 134 VAL A O     1 
ATOM   972  C  CB    . VAL A 1 134 ? 26.73524  24.71759 -1.02717  1.000 103.92781 ? 134 VAL A CB    1 
ATOM   973  C  CG1   . VAL A 1 134 ? 26.22744  25.71106 -2.05625  1.000 104.20052 ? 134 VAL A CG1   1 
ATOM   974  C  CG2   . VAL A 1 134 ? 26.55805  23.29190 -1.52612  1.000 104.75272 ? 134 VAL A CG2   1 
ATOM   975  N  N     . SER A 1 135 ? 28.28608  24.85504 1.70575   1.000 118.92804 ? 135 SER A N     1 
ATOM   976  C  CA    . SER A 1 135 ? 28.65009  24.27979 2.99163   1.000 113.88079 ? 135 SER A CA    1 
ATOM   977  C  C     . SER A 1 135 ? 27.89794  22.97556 3.23071   1.000 113.74007 ? 135 SER A C     1 
ATOM   978  O  O     . SER A 1 135 ? 26.75918  22.79706 2.79013   1.000 109.41802 ? 135 SER A O     1 
ATOM   979  C  CB    . SER A 1 135 ? 28.35749  25.26732 4.12147   1.000 112.60127 ? 135 SER A CB    1 
ATOM   980  O  OG    . SER A 1 135 ? 26.98237  25.60950 4.15675   1.000 115.84722 ? 135 SER A OG    1 
ATOM   981  N  N     . GLN A 1 136 ? 28.55503  22.05399 3.93039   1.000 106.87953 ? 136 GLN A N     1 
ATOM   982  C  CA    . GLN A 1 136 ? 27.94168  20.77758 4.26511   1.000 108.30248 ? 136 GLN A CA    1 
ATOM   983  C  C     . GLN A 1 136 ? 26.98561  20.93765 5.43819   1.000 102.80032 ? 136 GLN A C     1 
ATOM   984  O  O     . GLN A 1 136 ? 27.30224  21.59572 6.43330   1.000 95.96276  ? 136 GLN A O     1 
ATOM   985  C  CB    . GLN A 1 136 ? 29.00852  19.73544 4.60598   1.000 110.70251 ? 136 GLN A CB    1 
ATOM   986  C  CG    . GLN A 1 136 ? 28.43966  18.45115 5.19703   1.000 95.12456  ? 136 GLN A CG    1 
ATOM   987  C  CD    . GLN A 1 136 ? 29.48739  17.37478 5.40104   1.000 113.93837 ? 136 GLN A CD    1 
ATOM   988  O  OE1   . GLN A 1 136 ? 30.68539  17.65464 5.44436   1.000 111.51717 ? 136 GLN A OE1   1 
ATOM   989  N  NE2   . GLN A 1 136 ? 29.03793  16.13065 5.52298   1.000 125.20882 ? 136 GLN A NE2   1 
ATOM   990  N  N     . THR A 1 137 ? 25.81035  20.33205 5.31455   1.000 107.96310 ? 137 THR A N     1 
ATOM   991  C  CA    . THR A 1 137 ? 24.81597  20.32085 6.37388   1.000 109.87591 ? 137 THR A CA    1 
ATOM   992  C  C     . THR A 1 137 ? 24.46565  18.88429 6.73473   1.000 116.31400 ? 137 THR A C     1 
ATOM   993  O  O     . THR A 1 137 ? 24.83970  17.93158 6.04587   1.000 120.73014 ? 137 THR A O     1 
ATOM   994  C  CB    . THR A 1 137 ? 23.54936  21.08021 5.96118   1.000 104.36449 ? 137 THR A CB    1 
ATOM   995  O  OG1   . THR A 1 137 ? 22.99858  20.48668 4.77857   1.000 106.35040 ? 137 THR A OG1   1 
ATOM   996  C  CG2   . THR A 1 137 ? 23.86751  22.54134 5.69742   1.000 98.62408  ? 137 THR A CG2   1 
ATOM   997  N  N     . GLN A 1 138 ? 23.73338  18.74217 7.83983   1.000 124.11134 ? 138 GLN A N     1 
ATOM   998  C  CA    . GLN A 1 138 ? 23.27173  17.42468 8.25962   1.000 122.94011 ? 138 GLN A CA    1 
ATOM   999  C  C     . GLN A 1 138 ? 22.14683  16.91766 7.36750   1.000 124.68149 ? 138 GLN A C     1 
ATOM   1000 O  O     . GLN A 1 138 ? 22.01285  15.70422 7.17223   1.000 124.47961 ? 138 GLN A O     1 
ATOM   1001 C  CB    . GLN A 1 138 ? 22.82529  17.46180 9.72329   1.000 122.78743 ? 138 GLN A CB    1 
ATOM   1002 C  CG    . GLN A 1 138 ? 21.98821  18.67766 10.11000  1.000 129.15675 ? 138 GLN A CG    1 
ATOM   1003 C  CD    . GLN A 1 138 ? 22.82792  19.92397 10.34263  1.000 129.96590 ? 138 GLN A CD    1 
ATOM   1004 O  OE1   . GLN A 1 138 ? 23.18923  20.62711 9.39802   1.000 122.47735 ? 138 GLN A OE1   1 
ATOM   1005 N  NE2   . GLN A 1 138 ? 23.15118  20.19522 11.60107  1.000 124.15064 ? 138 GLN A NE2   1 
ATOM   1006 N  N     . ARG A 1 139 ? 21.33562  17.82411 6.81582   1.000 118.96265 ? 139 ARG A N     1 
ATOM   1007 C  CA    . ARG A 1 139 ? 20.31088  17.41112 5.86251   1.000 110.68523 ? 139 ARG A CA    1 
ATOM   1008 C  C     . ARG A 1 139 ? 20.93924  16.88822 4.57772   1.000 120.00813 ? 139 ARG A C     1 
ATOM   1009 O  O     . ARG A 1 139 ? 20.45584  15.91065 3.99517   1.000 122.09372 ? 139 ARG A O     1 
ATOM   1010 C  CB    . ARG A 1 139 ? 19.37077  18.57719 5.55980   1.000 103.99769 ? 139 ARG A CB    1 
ATOM   1011 C  CG    . ARG A 1 139 ? 18.14627  18.18748 4.74934   1.000 94.24997  ? 139 ARG A CG    1 
ATOM   1012 C  CD    . ARG A 1 139 ? 17.38575  19.41070 4.26849   1.000 89.25087  ? 139 ARG A CD    1 
ATOM   1013 N  NE    . ARG A 1 139 ? 15.95849  19.14031 4.15021   1.000 92.79757  ? 139 ARG A NE    1 
ATOM   1014 C  CZ    . ARG A 1 139 ? 15.05292  19.50134 5.04896   1.000 88.55738  ? 139 ARG A CZ    1 
ATOM   1015 N  NH1   . ARG A 1 139 ? 15.38758  20.18435 6.13156   1.000 89.11546  ? 139 ARG A NH1   1 
ATOM   1016 N  NH2   . ARG A 1 139 ? 13.77912  19.17235 4.85490   1.000 87.18564  ? 139 ARG A NH2   1 
ATOM   1017 N  N     . GLY A 1 140 ? 22.01456  17.52719 4.12189   1.000 134.19291 ? 140 GLY A N     1 
ATOM   1018 C  CA    . GLY A 1 140 ? 22.71553  17.07022 2.94135   1.000 134.94004 ? 140 GLY A CA    1 
ATOM   1019 C  C     . GLY A 1 140 ? 21.94941  17.35195 1.65748   1.000 136.72602 ? 140 GLY A C     1 
ATOM   1020 O  O     . GLY A 1 140 ? 21.01897  18.16128 1.60598   1.000 129.25144 ? 140 GLY A O     1 
ATOM   1021 N  N     . GLU A 1 141 ? 22.36586  16.65744 0.60141   1.000 136.47920 ? 141 GLU A N     1 
ATOM   1022 C  CA    . GLU A 1 141 ? 21.74234  16.78954 -0.71313  1.000 140.52261 ? 141 GLU A CA    1 
ATOM   1023 C  C     . GLU A 1 141 ? 20.43129  16.01377 -0.69827  1.000 141.86819 ? 141 GLU A C     1 
ATOM   1024 O  O     . GLU A 1 141 ? 20.41194  14.79631 -0.89274  1.000 148.70966 ? 141 GLU A O     1 
ATOM   1025 C  CB    . GLU A 1 141 ? 22.67604  16.28485 -1.80845  1.000 139.15457 ? 141 GLU A CB    1 
ATOM   1026 C  CG    . GLU A 1 141 ? 24.08987  16.85437 -1.75479  1.000 143.86481 ? 141 GLU A CG    1 
ATOM   1027 C  CD    . GLU A 1 141 ? 25.01292  16.05148 -0.85538  1.000 157.17372 ? 141 GLU A CD    1 
ATOM   1028 O  OE1   . GLU A 1 141 ? 24.64169  14.91941 -0.47995  1.000 163.58408 ? 141 GLU A OE1   1 
ATOM   1029 O  OE2   . GLU A 1 141 ? 26.10857  16.55184 -0.52354  1.000 155.93366 ? 141 GLU A OE2   1 
ATOM   1030 N  N     . GLY A 1 142 ? 19.32875  16.71873 -0.46455  1.000 117.59813 ? 142 GLY A N     1 
ATOM   1031 C  CA    . GLY A 1 142 ? 18.02019  16.09278 -0.40372  1.000 122.34068 ? 142 GLY A CA    1 
ATOM   1032 C  C     . GLY A 1 142 ? 17.52408  15.56365 -1.73568  1.000 122.11509 ? 142 GLY A C     1 
ATOM   1033 O  O     . GLY A 1 142 ? 18.10721  15.84019 -2.78367  1.000 107.69879 ? 142 GLY A O     1 
ATOM   1034 N  N     . LYS B 1 3   ? 13.99501  33.43764 22.62918  1.000 116.83927 ? 3   LYS B N     1 
ATOM   1035 C  CA    . LYS B 1 3   ? 13.36546  32.66724 21.56228  1.000 124.03591 ? 3   LYS B CA    1 
ATOM   1036 C  C     . LYS B 1 3   ? 11.84392  32.71212 21.67281  1.000 125.14068 ? 3   LYS B C     1 
ATOM   1037 O  O     . LYS B 1 3   ? 11.29506  32.86269 22.76293  1.000 129.47703 ? 3   LYS B O     1 
ATOM   1038 C  CB    . LYS B 1 3   ? 13.85220  31.21611 21.58897  1.000 116.83699 ? 3   LYS B CB    1 
ATOM   1039 N  N     . VAL B 1 4   ? 11.16776  32.57549 20.53757  1.000 102.32410 ? 4   VAL B N     1 
ATOM   1040 C  CA    . VAL B 1 4   ? 9.70966   32.61362 20.50741  1.000 100.43878 ? 4   VAL B CA    1 
ATOM   1041 C  C     . VAL B 1 4   ? 9.16495   31.24927 20.90892  1.000 92.49483  ? 4   VAL B C     1 
ATOM   1042 O  O     . VAL B 1 4   ? 9.62566   30.21301 20.41561  1.000 98.29465  ? 4   VAL B O     1 
ATOM   1043 C  CB    . VAL B 1 4   ? 9.20556   33.02458 19.11509  1.000 88.29696  ? 4   VAL B CB    1 
ATOM   1044 N  N     . ILE B 1 5   ? 8.18078   31.24552 21.80356  1.000 85.81946  ? 5   ILE B N     1 
ATOM   1045 C  CA    . ILE B 1 5   ? 7.55199   30.01825 22.27581  1.000 87.36965  ? 5   ILE B CA    1 
ATOM   1046 C  C     . ILE B 1 5   ? 6.23601   29.82350 21.53639  1.000 93.45204  ? 5   ILE B C     1 
ATOM   1047 O  O     . ILE B 1 5   ? 5.54865   30.78697 21.18255  1.000 91.40222  ? 5   ILE B O     1 
ATOM   1048 C  CB    . ILE B 1 5   ? 7.32980   30.04253 23.80085  1.000 101.59814 ? 5   ILE B CB    1 
ATOM   1049 C  CG1   . ILE B 1 5   ? 6.44371   31.22722 24.19799  1.000 101.01335 ? 5   ILE B CG1   1 
ATOM   1050 C  CG2   . ILE B 1 5   ? 8.66353   30.09010 24.53306  1.000 99.59908  ? 5   ILE B CG2   1 
ATOM   1051 C  CD1   . ILE B 1 5   ? 5.83296   31.09807 25.58251  1.000 113.10905 ? 5   ILE B CD1   1 
ATOM   1052 N  N     . LEU B 1 6   ? 5.88147   28.56220 21.29954  1.000 92.40891  ? 6   LEU B N     1 
ATOM   1053 C  CA    . LEU B 1 6   ? 4.64465   28.19460 20.61629  1.000 94.96079  ? 6   LEU B CA    1 
ATOM   1054 C  C     . LEU B 1 6   ? 3.91009   27.20195 21.50994  1.000 83.18287  ? 6   LEU B C     1 
ATOM   1055 O  O     . LEU B 1 6   ? 4.29945   26.03468 21.60293  1.000 89.34261  ? 6   LEU B O     1 
ATOM   1056 C  CB    . LEU B 1 6   ? 4.93127   27.61397 19.23394  1.000 92.67454  ? 6   LEU B CB    1 
ATOM   1057 C  CG    . LEU B 1 6   ? 3.76238   27.30332 18.29095  1.000 87.87624  ? 6   LEU B CG    1 
ATOM   1058 C  CD1   . LEU B 1 6   ? 3.25277   25.88155 18.48252  1.000 91.13676  ? 6   LEU B CD1   1 
ATOM   1059 C  CD2   . LEU B 1 6   ? 2.63364   28.31042 18.46649  1.000 93.14981  ? 6   LEU B CD2   1 
ATOM   1060 N  N     . LYS B 1 7   ? 2.84999   27.66948 22.16489  1.000 83.44484  ? 7   LYS B N     1 
ATOM   1061 C  CA    . LYS B 1 7   ? 2.04041   26.80814 23.01371  1.000 89.32764  ? 7   LYS B CA    1 
ATOM   1062 C  C     . LYS B 1 7   ? 1.08445   25.98917 22.15580  1.000 86.92784  ? 7   LYS B C     1 
ATOM   1063 O  O     . LYS B 1 7   ? 0.38046   26.53485 21.30038  1.000 84.05162  ? 7   LYS B O     1 
ATOM   1064 C  CB    . LYS B 1 7   ? 1.26523   27.64063 24.03314  1.000 83.82539  ? 7   LYS B CB    1 
ATOM   1065 N  N     . ILE B 1 8   ? 1.06452   24.67774 22.38279  1.000 83.65689  ? 8   ILE B N     1 
ATOM   1066 C  CA    . ILE B 1 8   ? 0.22700   23.75483 21.62617  1.000 89.96542  ? 8   ILE B CA    1 
ATOM   1067 C  C     . ILE B 1 8   ? -0.52987  22.87023 22.60632  1.000 87.29186  ? 8   ILE B C     1 
ATOM   1068 O  O     . ILE B 1 8   ? 0.06743   22.30925 23.53128  1.000 90.55893  ? 8   ILE B O     1 
ATOM   1069 C  CB    . ILE B 1 8   ? 1.05794   22.89589 20.65344  1.000 80.26811  ? 8   ILE B CB    1 
ATOM   1070 N  N     . LYS B 1 9   ? -1.83911  22.74538 22.40242  1.000 81.99451  ? 9   LYS B N     1 
ATOM   1071 C  CA    . LYS B 1 9   ? -2.69122  21.88281 23.20996  1.000 98.32223  ? 9   LYS B CA    1 
ATOM   1072 C  C     . LYS B 1 9   ? -3.26978  20.79247 22.32135  1.000 86.67575  ? 9   LYS B C     1 
ATOM   1073 O  O     . LYS B 1 9   ? -3.89713  21.08883 21.29925  1.000 86.21973  ? 9   LYS B O     1 
ATOM   1074 C  CB    . LYS B 1 9   ? -3.81702  22.67817 23.87749  1.000 87.91439  ? 9   LYS B CB    1 
ATOM   1075 N  N     . ARG B 1 10  ? -3.06189  19.53811 22.71311  1.000 95.67495  ? 10  ARG B N     1 
ATOM   1076 C  CA    . ARG B 1 10  ? -3.46372  18.39263 21.90571  1.000 93.17182  ? 10  ARG B CA    1 
ATOM   1077 C  C     . ARG B 1 10  ? -4.88092  17.96769 22.27547  1.000 93.11395  ? 10  ARG B C     1 
ATOM   1078 O  O     . ARG B 1 10  ? -5.14068  17.56993 23.41685  1.000 98.40031  ? 10  ARG B O     1 
ATOM   1079 C  CB    . ARG B 1 10  ? -2.47991  17.23840 22.09420  1.000 99.80520  ? 10  ARG B CB    1 
ATOM   1080 C  CG    . ARG B 1 10  ? -1.07718  17.55488 21.59380  1.000 98.61818  ? 10  ARG B CG    1 
ATOM   1081 C  CD    . ARG B 1 10  ? -0.01424  16.83217 22.40267  1.000 111.13820 ? 10  ARG B CD    1 
ATOM   1082 N  NE    . ARG B 1 10  ? 0.28627   15.49981 21.89357  1.000 101.63455 ? 10  ARG B NE    1 
ATOM   1083 C  CZ    . ARG B 1 10  ? 1.08615   14.63510 22.50262  1.000 107.51274 ? 10  ARG B CZ    1 
ATOM   1084 N  NH1   . ARG B 1 10  ? 1.65710   14.92056 23.66162  1.000 109.16960 ? 10  ARG B NH1   1 
ATOM   1085 N  NH2   . ARG B 1 10  ? 1.31719   13.45395 21.93672  1.000 110.50483 ? 10  ARG B NH2   1 
ATOM   1086 N  N     . LEU B 1 11  ? -5.79184  18.05328 21.30685  1.000 87.84227  ? 11  LEU B N     1 
ATOM   1087 C  CA    . LEU B 1 11  ? -7.16597  17.61938 21.49049  1.000 90.88423  ? 11  LEU B CA    1 
ATOM   1088 C  C     . LEU B 1 11  ? -7.21078  16.09918 21.65698  1.000 92.63292  ? 11  LEU B C     1 
ATOM   1089 O  O     . LEU B 1 11  ? -6.20508  15.41574 21.45063  1.000 93.34458  ? 11  LEU B O     1 
ATOM   1090 C  CB    . LEU B 1 11  ? -8.01612  18.08704 20.30788  1.000 91.43637  ? 11  LEU B CB    1 
ATOM   1091 C  CG    . LEU B 1 11  ? -8.31032  19.58888 20.25853  1.000 91.96975  ? 11  LEU B CG    1 
ATOM   1092 C  CD1   . LEU B 1 11  ? -9.26455  19.92008 19.12026  1.000 100.51747 ? 11  LEU B CD1   1 
ATOM   1093 C  CD2   . LEU B 1 11  ? -8.86956  20.07253 21.58849  1.000 79.54547  ? 11  LEU B CD2   1 
ATOM   1094 N  N     . PRO B 1 12  ? -8.36583  15.53999 22.05515  1.000 92.66606  ? 12  PRO B N     1 
ATOM   1095 C  CA    . PRO B 1 12  ? -8.43821  14.08156 22.27096  1.000 103.15615 ? 12  PRO B CA    1 
ATOM   1096 C  C     . PRO B 1 12  ? -7.92593  13.22976 21.11779  1.000 97.78696  ? 12  PRO B C     1 
ATOM   1097 O  O     . PRO B 1 12  ? -7.26983  12.21050 21.36497  1.000 102.38152 ? 12  PRO B O     1 
ATOM   1098 C  CB    . PRO B 1 12  ? -9.93516  13.85639 22.51576  1.000 83.52819  ? 12  PRO B CB    1 
ATOM   1099 C  CG    . PRO B 1 12  ? -10.36944 15.09831 23.19193  1.000 89.43235  ? 12  PRO B CG    1 
ATOM   1100 C  CD    . PRO B 1 12  ? -9.58799  16.21261 22.53982  1.000 95.56500  ? 12  PRO B CD    1 
ATOM   1101 N  N     . HIS B 1 13  ? -8.19830  13.60908 19.86936  1.000 94.50449  ? 13  HIS B N     1 
ATOM   1102 C  CA    . HIS B 1 13  ? -7.78358  12.80186 18.72777  1.000 98.83533  ? 13  HIS B CA    1 
ATOM   1103 C  C     . HIS B 1 13  ? -6.34274  13.06606 18.29421  1.000 92.29346  ? 13  HIS B C     1 
ATOM   1104 O  O     . HIS B 1 13  ? -5.95579  12.65746 17.19328  1.000 96.76707  ? 13  HIS B O     1 
ATOM   1105 C  CB    . HIS B 1 13  ? -8.74079  13.01222 17.54940  1.000 86.99239  ? 13  HIS B CB    1 
ATOM   1106 C  CG    . HIS B 1 13  ? -9.15656  14.43540 17.34354  1.000 93.52906  ? 13  HIS B CG    1 
ATOM   1107 N  ND1   . HIS B 1 13  ? -10.11459 15.05079 18.12050  1.000 99.47721  ? 13  HIS B ND1   1 
ATOM   1108 C  CD2   . HIS B 1 13  ? -8.76224  15.35703 16.43321  1.000 81.37111  ? 13  HIS B CD2   1 
ATOM   1109 C  CE1   . HIS B 1 13  ? -10.28314 16.29400 17.70626  1.000 95.00870  ? 13  HIS B CE1   1 
ATOM   1110 N  NE2   . HIS B 1 13  ? -9.47502  16.50493 16.68295  1.000 85.73859  ? 13  HIS B NE2   1 
ATOM   1111 N  N     . ALA B 1 14  ? -5.53568  13.72291 19.13304  1.000 101.95140 ? 14  ALA B N     1 
ATOM   1112 C  CA    . ALA B 1 14  ? -4.13391  13.97382 18.81864  1.000 96.86737  ? 14  ALA B CA    1 
ATOM   1113 C  C     . ALA B 1 14  ? -3.21993  13.63917 19.99178  1.000 102.75535 ? 14  ALA B C     1 
ATOM   1114 O  O     . ALA B 1 14  ? -2.06689  14.07848 20.01471  1.000 104.83400 ? 14  ALA B O     1 
ATOM   1115 C  CB    . ALA B 1 14  ? -3.92339  15.42698 18.39004  1.000 92.79127  ? 14  ALA B CB    1 
ATOM   1116 N  N     . GLN B 1 15  ? -3.71122  12.87588 20.96994  1.000 106.71325 ? 15  GLN B N     1 
ATOM   1117 C  CA    . GLN B 1 15  ? -2.89739  12.56526 22.14024  1.000 113.55284 ? 15  GLN B CA    1 
ATOM   1118 C  C     . GLN B 1 15  ? -1.83902  11.51905 21.81421  1.000 113.49768 ? 15  GLN B C     1 
ATOM   1119 O  O     . GLN B 1 15  ? -0.68675  11.63365 22.25102  1.000 115.76021 ? 15  GLN B O     1 
ATOM   1120 C  CB    . GLN B 1 15  ? -3.78890  12.08811 23.28873  1.000 115.84091 ? 15  GLN B CB    1 
ATOM   1121 C  CG    . GLN B 1 15  ? -4.80540  13.11201 23.76309  1.000 118.79595 ? 15  GLN B CG    1 
ATOM   1122 C  CD    . GLN B 1 15  ? -4.31380  13.91848 24.94975  1.000 125.63020 ? 15  GLN B CD    1 
ATOM   1123 O  OE1   . GLN B 1 15  ? -3.11753  13.95670 25.23708  1.000 133.07271 ? 15  GLN B OE1   1 
ATOM   1124 N  NE2   . GLN B 1 15  ? -5.23993  14.56167 25.65243  1.000 134.62702 ? 15  GLN B NE2   1 
ATOM   1125 N  N     . ASP B 1 16  ? -2.21379  10.48678 21.05561  1.000 110.25938 ? 16  ASP B N     1 
ATOM   1126 C  CA    . ASP B 1 16  ? -1.28964  9.40062  20.75332  1.000 112.15656 ? 16  ASP B CA    1 
ATOM   1127 C  C     . ASP B 1 16  ? -0.22454  9.80130  19.74125  1.000 113.83840 ? 16  ASP B C     1 
ATOM   1128 O  O     . ASP B 1 16  ? 0.82857   9.15626  19.68019  1.000 116.62897 ? 16  ASP B O     1 
ATOM   1129 C  CB    . ASP B 1 16  ? -2.06371  8.18993  20.23327  1.000 123.64718 ? 16  ASP B CB    1 
ATOM   1130 C  CG    . ASP B 1 16  ? -3.19989  7.78583  21.15047  1.000 139.71044 ? 16  ASP B CG    1 
ATOM   1131 O  OD1   . ASP B 1 16  ? -3.35547  8.40694  22.22415  1.000 143.14789 ? 16  ASP B OD1   1 
ATOM   1132 O  OD2   . ASP B 1 16  ? -3.94072  6.84587  20.79517  1.000 146.26573 ? 16  ASP B OD2   1 
ATOM   1133 N  N     . LEU B 1 17  ? -0.47278  10.84149 18.95164  1.000 109.15368 ? 17  LEU B N     1 
ATOM   1134 C  CA    . LEU B 1 17  ? 0.47016   11.26327 17.93118  1.000 92.61159  ? 17  LEU B CA    1 
ATOM   1135 C  C     . LEU B 1 17  ? 1.54460   12.16708 18.53448  1.000 100.63682 ? 17  LEU B C     1 
ATOM   1136 O  O     . LEU B 1 17  ? 1.29723   12.86174 19.52397  1.000 99.77593  ? 17  LEU B O     1 
ATOM   1137 C  CB    . LEU B 1 17  ? -0.25945  11.99455 16.81071  1.000 93.30121  ? 17  LEU B CB    1 
ATOM   1138 C  CG    . LEU B 1 17  ? -1.36659  11.18260 16.13898  1.000 84.63760  ? 17  LEU B CG    1 
ATOM   1139 C  CD1   . LEU B 1 17  ? -1.95573  11.95068 14.96881  1.000 87.26789  ? 17  LEU B CD1   1 
ATOM   1140 C  CD2   . LEU B 1 17  ? -0.83930  9.82741  15.69069  1.000 79.65478  ? 17  LEU B CD2   1 
ATOM   1141 N  N     . PRO B 1 18  ? 2.74563   12.17490 17.95966  1.000 99.27529  ? 18  PRO B N     1 
ATOM   1142 C  CA    . PRO B 1 18  ? 3.83576   12.95532 18.55024  1.000 96.85339  ? 18  PRO B CA    1 
ATOM   1143 C  C     . PRO B 1 18  ? 3.64816   14.44695 18.32339  1.000 99.23574  ? 18  PRO B C     1 
ATOM   1144 O  O     . PRO B 1 18  ? 2.84950   14.88848 17.49402  1.000 91.84417  ? 18  PRO B O     1 
ATOM   1145 C  CB    . PRO B 1 18  ? 5.07658   12.43541 17.81944  1.000 98.27820  ? 18  PRO B CB    1 
ATOM   1146 C  CG    . PRO B 1 18  ? 4.55968   12.02593 16.48821  1.000 102.48139 ? 18  PRO B CG    1 
ATOM   1147 C  CD    . PRO B 1 18  ? 3.17461   11.48007 16.73226  1.000 99.86426  ? 18  PRO B CD    1 
ATOM   1148 N  N     . LEU B 1 19  ? 4.40609   15.22683 19.09040  1.000 97.24533  ? 19  LEU B N     1 
ATOM   1149 C  CA    . LEU B 1 19  ? 4.35616   16.67214 18.95792  1.000 98.38188  ? 19  LEU B CA    1 
ATOM   1150 C  C     . LEU B 1 19  ? 4.88866   17.09326 17.58989  1.000 92.56951  ? 19  LEU B C     1 
ATOM   1151 O  O     . LEU B 1 19  ? 5.74098   16.41402 17.00918  1.000 96.25552  ? 19  LEU B O     1 
ATOM   1152 C  CB    . LEU B 1 19  ? 5.17795   17.34659 20.05630  1.000 95.34064  ? 19  LEU B CB    1 
ATOM   1153 C  CG    . LEU B 1 19  ? 4.50220   17.66965 21.39102  1.000 107.49415 ? 19  LEU B CG    1 
ATOM   1154 C  CD1   . LEU B 1 19  ? 3.24906   18.50732 21.17372  1.000 104.47089 ? 19  LEU B CD1   1 
ATOM   1155 C  CD2   . LEU B 1 19  ? 4.18574   16.40216 22.16662  1.000 115.85045 ? 19  LEU B CD2   1 
ATOM   1156 N  N     . PRO B 1 20  ? 4.39277   18.20079 17.04423  1.000 88.23783  ? 20  PRO B N     1 
ATOM   1157 C  CA    . PRO B 1 20  ? 5.03961   18.78455 15.86427  1.000 92.71976  ? 20  PRO B CA    1 
ATOM   1158 C  C     . PRO B 1 20  ? 6.46562   19.20316 16.19358  1.000 95.04125  ? 20  PRO B C     1 
ATOM   1159 O  O     . PRO B 1 20  ? 6.71284   19.92541 17.16233  1.000 91.56552  ? 20  PRO B O     1 
ATOM   1160 C  CB    . PRO B 1 20  ? 4.14905   19.98730 15.52808  1.000 83.03410  ? 20  PRO B CB    1 
ATOM   1161 C  CG    . PRO B 1 20  ? 3.38517   20.26950 16.78523  1.000 86.54671  ? 20  PRO B CG    1 
ATOM   1162 C  CD    . PRO B 1 20  ? 3.17613   18.93495 17.42652  1.000 90.43305  ? 20  PRO B CD    1 
ATOM   1163 N  N     . SER B 1 21  ? 7.41000   18.72401 15.38707  1.000 95.10618  ? 21  SER B N     1 
ATOM   1164 C  CA    . SER B 1 21  ? 8.82523   18.97435 15.61344  1.000 89.75058  ? 21  SER B CA    1 
ATOM   1165 C  C     . SER B 1 21  ? 9.49881   19.27821 14.28270  1.000 82.33131  ? 21  SER B C     1 
ATOM   1166 O  O     . SER B 1 21  ? 8.93118   19.06211 13.20873  1.000 84.34066  ? 21  SER B O     1 
ATOM   1167 C  CB    . SER B 1 21  ? 9.50195   17.78273 16.30449  1.000 89.71088  ? 21  SER B CB    1 
ATOM   1168 O  OG    . SER B 1 21  ? 9.38420   16.60386 15.52560  1.000 88.62477  ? 21  SER B OG    1 
ATOM   1169 N  N     . TYR B 1 22  ? 10.72304  19.79357 14.36330  1.000 82.73151  ? 22  TYR B N     1 
ATOM   1170 C  CA    . TYR B 1 22  ? 11.52520  20.07266 13.18021  1.000 81.86324  ? 22  TYR B CA    1 
ATOM   1171 C  C     . TYR B 1 22  ? 12.34326  18.83994 12.81833  1.000 88.81733  ? 22  TYR B C     1 
ATOM   1172 O  O     . TYR B 1 22  ? 12.97336  18.22901 13.68761  1.000 96.62828  ? 22  TYR B O     1 
ATOM   1173 C  CB    . TYR B 1 22  ? 12.44566  21.27090 13.41661  1.000 84.52214  ? 22  TYR B CB    1 
ATOM   1174 C  CG    . TYR B 1 22  ? 11.71248  22.57482 13.63465  1.000 92.80751  ? 22  TYR B CG    1 
ATOM   1175 C  CD1   . TYR B 1 22  ? 11.24498  23.31817 12.55830  1.000 88.37731  ? 22  TYR B CD1   1 
ATOM   1176 C  CD2   . TYR B 1 22  ? 11.49094  23.06483 14.91529  1.000 83.74458  ? 22  TYR B CD2   1 
ATOM   1177 C  CE1   . TYR B 1 22  ? 10.57366  24.51103 12.75053  1.000 85.18874  ? 22  TYR B CE1   1 
ATOM   1178 C  CE2   . TYR B 1 22  ? 10.82000  24.25699 15.11787  1.000 87.55503  ? 22  TYR B CE2   1 
ATOM   1179 C  CZ    . TYR B 1 22  ? 10.36428  24.97635 14.03168  1.000 91.71528  ? 22  TYR B CZ    1 
ATOM   1180 O  OH    . TYR B 1 22  ? 9.69643   26.16436 14.22519  1.000 90.71412  ? 22  TYR B OH    1 
ATOM   1181 N  N     . ALA B 1 23  ? 12.32307  18.47303 11.53516  1.000 87.89909  ? 23  ALA B N     1 
ATOM   1182 C  CA    . ALA B 1 23  ? 13.07032  17.30174 11.08860  1.000 92.93627  ? 23  ALA B CA    1 
ATOM   1183 C  C     . ALA B 1 23  ? 14.57001  17.52649 11.22246  1.000 92.75791  ? 23  ALA B C     1 
ATOM   1184 O  O     . ALA B 1 23  ? 15.28869  16.68977 11.78133  1.000 94.26400  ? 23  ALA B O     1 
ATOM   1185 C  CB    . ALA B 1 23  ? 12.70305  16.96389 9.64400   1.000 83.74589  ? 23  ALA B CB    1 
ATOM   1186 N  N     . THR B 1 24  ? 15.05773  18.65043 10.71827  1.000 95.71272  ? 24  THR B N     1 
ATOM   1187 C  CA    . THR B 1 24  ? 16.46075  19.02068 10.77554  1.000 97.12744  ? 24  THR B CA    1 
ATOM   1188 C  C     . THR B 1 24  ? 16.62131  20.29113 11.60111  1.000 94.57862  ? 24  THR B C     1 
ATOM   1189 O  O     . THR B 1 24  ? 15.67618  21.07838 11.72840  1.000 93.13797  ? 24  THR B O     1 
ATOM   1190 C  CB    . THR B 1 24  ? 17.02159  19.24039 9.36122   1.000 103.94484 ? 24  THR B CB    1 
ATOM   1191 O  OG1   . THR B 1 24  ? 16.51718  20.47147 8.82741   1.000 97.47575  ? 24  THR B OG1   1 
ATOM   1192 C  CG2   . THR B 1 24  ? 16.62561  18.09522 8.44409   1.000 91.18959  ? 24  THR B CG2   1 
ATOM   1193 N  N     . PRO B 1 25  ? 17.80623  20.53030 12.17549  1.000 103.11903 ? 25  PRO B N     1 
ATOM   1194 C  CA    . PRO B 1 25  ? 18.00377  21.74438 12.98670  1.000 104.34492 ? 25  PRO B CA    1 
ATOM   1195 C  C     . PRO B 1 25  ? 17.87041  23.05363 12.21448  1.000 105.54665 ? 25  PRO B C     1 
ATOM   1196 O  O     . PRO B 1 25  ? 18.02809  24.11876 12.81557  1.000 111.08614 ? 25  PRO B O     1 
ATOM   1197 C  CB    . PRO B 1 25  ? 19.43518  21.56807 13.53277  1.000 113.18860 ? 25  PRO B CB    1 
ATOM   1198 C  CG    . PRO B 1 25  ? 20.08303  20.60941 12.59586  1.000 113.85794 ? 25  PRO B CG    1 
ATOM   1199 C  CD    . PRO B 1 25  ? 18.99828  19.66454 12.19126  1.000 108.42350 ? 25  PRO B CD    1 
ATOM   1200 N  N     . HIS B 1 26  ? 17.59214  23.01890 10.90826  1.000 104.92950 ? 26  HIS B N     1 
ATOM   1201 C  CA    . HIS B 1 26  ? 17.33252  24.22663 10.13066  1.000 100.20505 ? 26  HIS B CA    1 
ATOM   1202 C  C     . HIS B 1 26  ? 16.06138  24.08315 9.30573   1.000 96.97785  ? 26  HIS B C     1 
ATOM   1203 O  O     . HIS B 1 26  ? 15.93226  24.70077 8.24764   1.000 98.31739  ? 26  HIS B O     1 
ATOM   1204 C  CB    . HIS B 1 26  ? 18.51356  24.57430 9.22395   1.000 101.88838 ? 26  HIS B CB    1 
ATOM   1205 C  CG    . HIS B 1 26  ? 19.62874  25.27816 9.92999   1.000 108.46056 ? 26  HIS B CG    1 
ATOM   1206 N  ND1   . HIS B 1 26  ? 19.49443  25.80169 11.19820  1.000 116.34017 ? 26  HIS B ND1   1 
ATOM   1207 C  CD2   . HIS B 1 26  ? 20.90165  25.53722 9.54859   1.000 116.67485 ? 26  HIS B CD2   1 
ATOM   1208 C  CE1   . HIS B 1 26  ? 20.63779  26.35135 11.56782  1.000 122.79165 ? 26  HIS B CE1   1 
ATOM   1209 N  NE2   . HIS B 1 26  ? 21.50804  26.20429 10.58499  1.000 122.41724 ? 26  HIS B NE2   1 
ATOM   1210 N  N     . SER B 1 27  ? 15.11005  23.28504 9.78270   1.000 96.90286  ? 27  SER B N     1 
ATOM   1211 C  CA    . SER B 1 27  ? 13.84373  23.13013 9.08487   1.000 93.19384  ? 27  SER B CA    1 
ATOM   1212 C  C     . SER B 1 27  ? 12.98285  24.37270 9.28198   1.000 89.86513  ? 27  SER B C     1 
ATOM   1213 O  O     . SER B 1 27  ? 13.01322  25.01570 10.33447  1.000 86.78486  ? 27  SER B O     1 
ATOM   1214 C  CB    . SER B 1 27  ? 13.11313  21.88609 9.58863   1.000 87.97016  ? 27  SER B CB    1 
ATOM   1215 O  OG    . SER B 1 27  ? 11.99308  21.59126 8.77764   1.000 98.97452  ? 27  SER B OG    1 
ATOM   1216 N  N     . SER B 1 28  ? 12.21467  24.71645 8.24729   1.000 86.95136  ? 28  SER B N     1 
ATOM   1217 C  CA    . SER B 1 28  ? 11.44110  25.95214 8.28665   1.000 84.95531  ? 28  SER B CA    1 
ATOM   1218 C  C     . SER B 1 28  ? 10.13057  25.79843 9.04454   1.000 78.07913  ? 28  SER B C     1 
ATOM   1219 O  O     . SER B 1 28  ? 9.66241   26.76581 9.65528   1.000 72.68062  ? 28  SER B O     1 
ATOM   1220 C  CB    . SER B 1 28  ? 11.15420  26.44741 6.86956   1.000 82.88457  ? 28  SER B CB    1 
ATOM   1221 O  OG    . SER B 1 28  ? 12.31318  27.00273 6.27531   1.000 88.49605  ? 28  SER B OG    1 
ATOM   1222 N  N     . GLY B 1 29  ? 9.52196   24.61357 9.02006   1.000 79.69959  ? 29  GLY B N     1 
ATOM   1223 C  CA    . GLY B 1 29  ? 8.21030   24.44172 9.60516   1.000 79.96761  ? 29  GLY B CA    1 
ATOM   1224 C  C     . GLY B 1 29  ? 8.08032   23.12286 10.33949  1.000 81.00684  ? 29  GLY B C     1 
ATOM   1225 O  O     . GLY B 1 29  ? 8.89290   22.20713 10.18495  1.000 77.94735  ? 29  GLY B O     1 
ATOM   1226 N  N     . LEU B 1 30  ? 7.02682   23.05123 11.15077  1.000 81.02956  ? 30  LEU B N     1 
ATOM   1227 C  CA    . LEU B 1 30  ? 6.66661   21.84787 11.88522  1.000 84.33024  ? 30  LEU B CA    1 
ATOM   1228 C  C     . LEU B 1 30  ? 5.67004   21.02954 11.07700  1.000 80.54329  ? 30  LEU B C     1 
ATOM   1229 O  O     . LEU B 1 30  ? 4.78958   21.58303 10.41448  1.000 80.96583  ? 30  LEU B O     1 
ATOM   1230 C  CB    . LEU B 1 30  ? 6.05652   22.20908 13.24037  1.000 87.84530  ? 30  LEU B CB    1 
ATOM   1231 C  CG    . LEU B 1 30  ? 6.85257   23.14794 14.14465  1.000 82.60837  ? 30  LEU B CG    1 
ATOM   1232 C  CD1   . LEU B 1 30  ? 5.94245   23.78220 15.18191  1.000 81.18374  ? 30  LEU B CD1   1 
ATOM   1233 C  CD2   . LEU B 1 30  ? 7.96841   22.38387 14.81821  1.000 83.89806  ? 30  LEU B CD2   1 
ATOM   1234 N  N     . ASP B 1 31  ? 5.80492   19.70944 11.14339  1.000 77.27333  ? 31  ASP B N     1 
ATOM   1235 C  CA    . ASP B 1 31  ? 4.92036   18.83034 10.39444  1.000 87.07399  ? 31  ASP B CA    1 
ATOM   1236 C  C     . ASP B 1 31  ? 3.54791   18.73846 11.05474  1.000 82.22986  ? 31  ASP B C     1 
ATOM   1237 O  O     . ASP B 1 31  ? 3.41657   18.76639 12.28202  1.000 72.73199  ? 31  ASP B O     1 
ATOM   1238 C  CB    . ASP B 1 31  ? 5.53570   17.43587 10.25968  1.000 93.51131  ? 31  ASP B CB    1 
ATOM   1239 C  CG    . ASP B 1 31  ? 6.38034   17.05144 11.45852  1.000 100.02784 ? 31  ASP B CG    1 
ATOM   1240 O  OD1   . ASP B 1 31  ? 5.84531   17.03483 12.58735  1.000 94.22994  ? 31  ASP B OD1   1 
ATOM   1241 O  OD2   . ASP B 1 31  ? 7.57953   16.75622 11.26746  1.000 102.90169 ? 31  ASP B OD2   1 
ATOM   1242 N  N     . LEU B 1 32  ? 2.51984   18.63474 10.21652  1.000 79.31015  ? 32  LEU B N     1 
ATOM   1243 C  CA    . LEU B 1 32  ? 1.13784   18.48708 10.64984  1.000 74.25882  ? 32  LEU B CA    1 
ATOM   1244 C  C     . LEU B 1 32  ? 0.62341   17.11638 10.23421  1.000 81.54300  ? 32  LEU B C     1 
ATOM   1245 O  O     . LEU B 1 32  ? 0.85914   16.67270 9.10607   1.000 79.42205  ? 32  LEU B O     1 
ATOM   1246 C  CB    . LEU B 1 32  ? 0.25218   19.58246 10.04877  1.000 76.46554  ? 32  LEU B CB    1 
ATOM   1247 C  CG    . LEU B 1 32  ? -0.03066  20.82602 10.89416  1.000 82.57169  ? 32  LEU B CG    1 
ATOM   1248 C  CD1   . LEU B 1 32  ? 1.20351   21.26138 11.66373  1.000 72.10412  ? 32  LEU B CD1   1 
ATOM   1249 C  CD2   . LEU B 1 32  ? -0.53068  21.95389 10.00468  1.000 72.19855  ? 32  LEU B CD2   1 
ATOM   1250 N  N     . ARG B 1 33  ? -0.08213  16.45099 11.14304  1.000 74.55779  ? 33  ARG B N     1 
ATOM   1251 C  CA    . ARG B 1 33  ? -0.55119  15.09269 10.92010  1.000 79.75751  ? 33  ARG B CA    1 
ATOM   1252 C  C     . ARG B 1 33  ? -2.07174  15.04329 10.84850  1.000 77.48714  ? 33  ARG B C     1 
ATOM   1253 O  O     . ARG B 1 33  ? -2.77481  15.92777 11.34480  1.000 77.76527  ? 33  ARG B O     1 
ATOM   1254 C  CB    . ARG B 1 33  ? -0.04867  14.15082 12.01992  1.000 84.15120  ? 33  ARG B CB    1 
ATOM   1255 C  CG    . ARG B 1 33  ? 1.41033   13.76483 11.86716  1.000 86.16152  ? 33  ARG B CG    1 
ATOM   1256 C  CD    . ARG B 1 33  ? 1.84117   12.77409 12.93424  1.000 91.33382  ? 33  ARG B CD    1 
ATOM   1257 N  NE    . ARG B 1 33  ? 3.05837   12.06997 12.54922  1.000 95.73567  ? 33  ARG B NE    1 
ATOM   1258 C  CZ    . ARG B 1 33  ? 4.28614   12.50906 12.78841  1.000 101.68796 ? 33  ARG B CZ    1 
ATOM   1259 N  NH1   . ARG B 1 33  ? 4.50070   13.64925 13.42421  1.000 99.26037  ? 33  ARG B NH1   1 
ATOM   1260 N  NH2   . ARG B 1 33  ? 5.32468   11.78692 12.37763  1.000 104.73593 ? 33  ARG B NH2   1 
ATOM   1261 N  N     . ALA B 1 34  ? -2.56931  13.98163 10.21829  1.000 77.77066  ? 34  ALA B N     1 
ATOM   1262 C  CA    . ALA B 1 34  ? -4.00343  13.76265 10.04821  1.000 74.67565  ? 34  ALA B CA    1 
ATOM   1263 C  C     . ALA B 1 34  ? -4.52665  13.04312 11.28394  1.000 80.92283  ? 34  ALA B C     1 
ATOM   1264 O  O     . ALA B 1 34  ? -4.38110  11.82581 11.41628  1.000 84.58739  ? 34  ALA B O     1 
ATOM   1265 C  CB    . ALA B 1 34  ? -4.27886  12.96287 8.78017   1.000 67.70152  ? 34  ALA B CB    1 
ATOM   1266 N  N     . ALA B 1 35  ? -5.14475  13.79764 12.19336  1.000 75.55754  ? 35  ALA B N     1 
ATOM   1267 C  CA    . ALA B 1 35  ? -5.71545  13.23557 13.41693  1.000 84.83619  ? 35  ALA B CA    1 
ATOM   1268 C  C     . ALA B 1 35  ? -7.06549  12.57335 13.12442  1.000 82.20459  ? 35  ALA B C     1 
ATOM   1269 O  O     . ALA B 1 35  ? -8.11104  12.93917 13.66106  1.000 79.29238  ? 35  ALA B O     1 
ATOM   1270 C  CB    . ALA B 1 35  ? -5.84332  14.31903 14.47942  1.000 75.89036  ? 35  ALA B CB    1 
ATOM   1271 N  N     . ILE B 1 36  ? -7.02185  11.56942 12.25386  1.000 80.03582  ? 36  ILE B N     1 
ATOM   1272 C  CA    . ILE B 1 36  ? -8.21944  10.88381 11.79494  1.000 80.19517  ? 36  ILE B CA    1 
ATOM   1273 C  C     . ILE B 1 36  ? -8.27738  9.49719  12.42136  1.000 88.93253  ? 36  ILE B C     1 
ATOM   1274 O  O     . ILE B 1 36  ? -7.26756  8.92665  12.84653  1.000 88.67768  ? 36  ILE B O     1 
ATOM   1275 C  CB    . ILE B 1 36  ? -8.27833  10.79072 10.25668  1.000 82.25099  ? 36  ILE B CB    1 
ATOM   1276 C  CG1   . ILE B 1 36  ? -7.04872  10.05227 9.72356   1.000 81.40415  ? 36  ILE B CG1   1 
ATOM   1277 C  CG2   . ILE B 1 36  ? -8.39269  12.17921 9.64404   1.000 86.90031  ? 36  ILE B CG2   1 
ATOM   1278 C  CD1   . ILE B 1 36  ? -7.09154  9.77808  8.23616   1.000 92.46157  ? 36  ILE B CD1   1 
ATOM   1279 N  N     . GLU B 1 37  ? -9.49291  8.95274  12.47344  1.000 93.00381  ? 37  GLU B N     1 
ATOM   1280 C  CA    . GLU B 1 37  ? -9.71095  7.62542  13.04717  1.000 98.44939  ? 37  GLU B CA    1 
ATOM   1281 C  C     . GLU B 1 37  ? -9.31802  6.54171  12.04863  1.000 102.43733 ? 37  GLU B C     1 
ATOM   1282 O  O     . GLU B 1 37  ? -8.30308  5.85833  12.21619  1.000 105.48847 ? 37  GLU B O     1 
ATOM   1283 C  CB    . GLU B 1 37  ? -11.17685 7.47849  13.46722  1.000 94.26829  ? 37  GLU B CB    1 
ATOM   1284 C  CG    . GLU B 1 37  ? -11.74561 8.71766  14.14196  1.000 102.08006 ? 37  GLU B CG    1 
ATOM   1285 C  CD    . GLU B 1 37  ? -13.25866 8.79579  14.05167  1.000 112.14704 ? 37  GLU B CD    1 
ATOM   1286 O  OE1   . GLU B 1 37  ? -13.86898 7.89340  13.43970  1.000 105.31271 ? 37  GLU B OE1   1 
ATOM   1287 O  OE2   . GLU B 1 37  ? -13.83834 9.75983  14.59618  1.000 99.67422  ? 37  GLU B OE2   1 
ATOM   1288 N  N     . LYS B 1 38  ? -10.11624 6.37719  11.00875  1.000 105.31012 ? 38  LYS B N     1 
ATOM   1289 C  CA    . LYS B 1 38  ? -9.86066  5.43412  9.93829   1.000 108.27031 ? 38  LYS B CA    1 
ATOM   1290 C  C     . LYS B 1 38  ? -9.21469  6.14568  8.76015   1.000 102.97861 ? 38  LYS B C     1 
ATOM   1291 O  O     . LYS B 1 38  ? -9.32183  7.36861  8.62939   1.000 92.02174  ? 38  LYS B O     1 
ATOM   1292 C  CB    . LYS B 1 38  ? -11.17266 4.76849  9.50053   1.000 102.52226 ? 38  LYS B CB    1 
ATOM   1293 N  N     . PRO B 1 39  ? -8.51452  5.41382  7.89091   1.000 100.58335 ? 39  PRO B N     1 
ATOM   1294 C  CA    . PRO B 1 39  ? -7.88593  6.05561  6.73165   1.000 107.90787 ? 39  PRO B CA    1 
ATOM   1295 C  C     . PRO B 1 39  ? -8.90872  6.75786  5.85008   1.000 105.72590 ? 39  PRO B C     1 
ATOM   1296 O  O     . PRO B 1 39  ? -10.08142 6.38116  5.79368   1.000 108.58830 ? 39  PRO B O     1 
ATOM   1297 C  CB    . PRO B 1 39  ? -7.22264  4.88454  5.99419   1.000 98.67726  ? 39  PRO B CB    1 
ATOM   1298 C  CG    . PRO B 1 39  ? -6.98097  3.86811  7.05626   1.000 95.98660  ? 39  PRO B CG    1 
ATOM   1299 C  CD    . PRO B 1 39  ? -8.14673  3.98984  7.99740   1.000 101.81909 ? 39  PRO B CD    1 
ATOM   1300 N  N     . LEU B 1 40  ? -8.44580  7.79616  5.15979   1.000 98.88660  ? 40  LEU B N     1 
ATOM   1301 C  CA    . LEU B 1 40  ? -9.29884  8.66429  4.36316   1.000 102.91865 ? 40  LEU B CA    1 
ATOM   1302 C  C     . LEU B 1 40  ? -9.03926  8.43604  2.87991   1.000 105.87519 ? 40  LEU B C     1 
ATOM   1303 O  O     . LEU B 1 40  ? -7.89011  8.27694  2.45777   1.000 98.10851  ? 40  LEU B O     1 
ATOM   1304 C  CB    . LEU B 1 40  ? -9.05484  10.13126 4.72614   1.000 102.65151 ? 40  LEU B CB    1 
ATOM   1305 C  CG    . LEU B 1 40  ? -10.15281 11.14433 4.41183   1.000 103.13235 ? 40  LEU B CG    1 
ATOM   1306 C  CD1   . LEU B 1 40  ? -11.52434 10.53700 4.63924   1.000 104.04782 ? 40  LEU B CD1   1 
ATOM   1307 C  CD2   . LEU B 1 40  ? -9.96469  12.36187 5.29361   1.000 86.57391  ? 40  LEU B CD2   1 
ATOM   1308 N  N     . LYS B 1 41  ? -10.11174 8.41889  2.09318   1.000 125.71230 ? 41  LYS B N     1 
ATOM   1309 C  CA    . LYS B 1 41  ? -10.03891 8.18431  0.65590   1.000 120.29010 ? 41  LYS B CA    1 
ATOM   1310 C  C     . LYS B 1 41  ? -10.41242 9.46740  -0.07288  1.000 116.68467 ? 41  LYS B C     1 
ATOM   1311 O  O     . LYS B 1 41  ? -11.54260 9.95147  0.05563   1.000 116.76418 ? 41  LYS B O     1 
ATOM   1312 C  CB    . LYS B 1 41  ? -10.96233 7.03885  0.24079   1.000 115.47714 ? 41  LYS B CB    1 
ATOM   1313 N  N     . ILE B 1 42  ? -9.46855  10.01104 -0.83530  1.000 98.19679  ? 42  ILE B N     1 
ATOM   1314 C  CA    . ILE B 1 42  ? -9.65603  11.26992 -1.54605  1.000 101.63975 ? 42  ILE B CA    1 
ATOM   1315 C  C     . ILE B 1 42  ? -9.70092  10.96466 -3.03667  1.000 109.82630 ? 42  ILE B C     1 
ATOM   1316 O  O     . ILE B 1 42  ? -8.68433  10.59769 -3.64029  1.000 102.26133 ? 42  ILE B O     1 
ATOM   1317 C  CB    . ILE B 1 42  ? -8.55135  12.28307 -1.22190  1.000 96.25386  ? 42  ILE B CB    1 
ATOM   1318 C  CG1   . ILE B 1 42  ? -8.40221  12.44504 0.29142   1.000 81.96080  ? 42  ILE B CG1   1 
ATOM   1319 C  CG2   . ILE B 1 42  ? -8.86492  13.62550 -1.86708  1.000 91.45671  ? 42  ILE B CG2   1 
ATOM   1320 C  CD1   . ILE B 1 42  ? -7.33517  13.43537 0.68494   1.000 79.59919  ? 42  ILE B CD1   1 
ATOM   1321 N  N     . LYS B 1 43  ? -10.88095 11.11447 -3.63202  1.000 107.85481 ? 43  LYS B N     1 
ATOM   1322 C  CA    . LYS B 1 43  ? -11.03629 10.95145 -5.06355  1.000 102.68877 ? 43  LYS B CA    1 
ATOM   1323 C  C     . LYS B 1 43  ? -10.35952 12.12282 -5.77246  1.000 104.34462 ? 43  LYS B C     1 
ATOM   1324 O  O     . LYS B 1 43  ? -10.03464 13.13252 -5.14405  1.000 107.40272 ? 43  LYS B O     1 
ATOM   1325 C  CB    . LYS B 1 43  ? -12.52032 10.85964 -5.41789  1.000 109.95367 ? 43  LYS B CB    1 
ATOM   1326 N  N     . PRO B 1 44  ? -10.11454 12.02134 -7.08034  1.000 99.25273  ? 44  PRO B N     1 
ATOM   1327 C  CA    . PRO B 1 44  ? -9.55954  13.17759 -7.79512  1.000 105.65855 ? 44  PRO B CA    1 
ATOM   1328 C  C     . PRO B 1 44  ? -10.55284 14.33494 -7.86084  1.000 106.07753 ? 44  PRO B C     1 
ATOM   1329 O  O     . PRO B 1 44  ? -11.76844 14.13113 -7.92011  1.000 105.17227 ? 44  PRO B O     1 
ATOM   1330 C  CB    . PRO B 1 44  ? -9.25140  12.62250 -9.19366  1.000 108.57971 ? 44  PRO B CB    1 
ATOM   1331 C  CG    . PRO B 1 44  ? -9.10621  11.15097 -9.00635  1.000 108.81547 ? 44  PRO B CG    1 
ATOM   1332 C  CD    . PRO B 1 44  ? -10.07726 10.79774 -7.90583  1.000 106.40947 ? 44  PRO B CD    1 
ATOM   1333 N  N     . PHE B 1 45  ? -10.00755 15.55935 -7.81423  1.000 103.20388 ? 45  PHE B N     1 
ATOM   1334 C  CA    . PHE B 1 45  ? -10.67297 16.83749 -8.11006  1.000 108.34437 ? 45  PHE B CA    1 
ATOM   1335 C  C     . PHE B 1 45  ? -11.62384 17.35225 -7.03598  1.000 113.30687 ? 45  PHE B C     1 
ATOM   1336 O  O     . PHE B 1 45  ? -12.44259 18.23163 -7.34366  1.000 118.05916 ? 45  PHE B O     1 
ATOM   1337 C  CB    . PHE B 1 45  ? -11.45191 16.79987 -9.43194  1.000 105.45568 ? 45  PHE B CB    1 
ATOM   1338 C  CG    . PHE B 1 45  ? -10.58962 16.58751 -10.64081 1.000 107.86285 ? 45  PHE B CG    1 
ATOM   1339 C  CD1   . PHE B 1 45  ? -9.20941  16.63158 -10.54602 1.000 102.24818 ? 45  PHE B CD1   1 
ATOM   1340 C  CD2   . PHE B 1 45  ? -11.16153 16.34840 -11.87184 1.000 110.58343 ? 45  PHE B CD2   1 
ATOM   1341 C  CE1   . PHE B 1 45  ? -8.41813  16.42974 -11.65590 1.000 108.52230 ? 45  PHE B CE1   1 
ATOM   1342 C  CE2   . PHE B 1 45  ? -10.37802 16.14758 -12.99412 1.000 116.42916 ? 45  PHE B CE2   1 
ATOM   1343 C  CZ    . PHE B 1 45  ? -8.99929  16.18784 -12.88658 1.000 116.79019 ? 45  PHE B CZ    1 
ATOM   1344 N  N     . GLU B 1 46  ? -11.55320 16.86498 -5.79680  1.000 136.53362 ? 46  GLU B N     1 
ATOM   1345 C  CA    . GLU B 1 46  ? -12.37035 17.41165 -4.72146  1.000 134.84180 ? 46  GLU B CA    1 
ATOM   1346 C  C     . GLU B 1 46  ? -11.52498 17.56666 -3.46492  1.000 131.70821 ? 46  GLU B C     1 
ATOM   1347 O  O     . GLU B 1 46  ? -10.46796 16.94907 -3.31884  1.000 130.67125 ? 46  GLU B O     1 
ATOM   1348 C  CB    . GLU B 1 46  ? -13.60769 16.54519 -4.42738  1.000 138.19395 ? 46  GLU B CB    1 
ATOM   1349 C  CG    . GLU B 1 46  ? -13.40109 15.47516 -3.35784  1.000 140.35715 ? 46  GLU B CG    1 
ATOM   1350 C  CD    . GLU B 1 46  ? -12.59878 14.29727 -3.86220  1.000 144.36901 ? 46  GLU B CD    1 
ATOM   1351 O  OE1   . GLU B 1 46  ? -12.59211 14.08103 -5.09081  1.000 143.25629 ? 46  GLU B OE1   1 
ATOM   1352 O  OE2   . GLU B 1 46  ? -11.97903 13.59090 -3.03709  1.000 142.97513 ? 46  GLU B OE2   1 
ATOM   1353 N  N     . ARG B 1 47  ? -12.02249 18.39390 -2.55078  1.000 110.27956 ? 47  ARG B N     1 
ATOM   1354 C  CA    . ARG B 1 47  ? -11.32464 18.78736 -1.33649  1.000 97.43983  ? 47  ARG B CA    1 
ATOM   1355 C  C     . ARG B 1 47  ? -11.82646 17.99980 -0.12999  1.000 93.11639  ? 47  ARG B C     1 
ATOM   1356 O  O     . ARG B 1 47  ? -12.91013 17.41099 -0.14537  1.000 91.22767  ? 47  ARG B O     1 
ATOM   1357 C  CB    . ARG B 1 47  ? -11.50849 20.28577 -1.09277  1.000 90.08630  ? 47  ARG B CB    1 
ATOM   1358 C  CG    . ARG B 1 47  ? -12.97173 20.70969 -1.02164  1.000 91.29215  ? 47  ARG B CG    1 
ATOM   1359 C  CD    . ARG B 1 47  ? -13.17026 22.11846 -1.55393  1.000 89.65294  ? 47  ARG B CD    1 
ATOM   1360 N  NE    . ARG B 1 47  ? -14.51667 22.62037 -1.30802  1.000 85.90124  ? 47  ARG B NE    1 
ATOM   1361 C  CZ    . ARG B 1 47  ? -15.51843 22.53659 -2.17249  1.000 86.35908  ? 47  ARG B CZ    1 
ATOM   1362 N  NH1   . ARG B 1 47  ? -15.36490 21.96431 -3.35519  1.000 85.05848  ? 47  ARG B NH1   1 
ATOM   1363 N  NH2   . ARG B 1 47  ? -16.70320 23.04358 -1.84346  1.000 91.61373  ? 47  ARG B NH2   1 
ATOM   1364 N  N     . VAL B 1 48  ? -11.02052 18.01234 0.92949   1.000 92.88071  ? 48  VAL B N     1 
ATOM   1365 C  CA    . VAL B 1 48  ? -11.32592 17.29817 2.16574   1.000 88.16346  ? 48  VAL B CA    1 
ATOM   1366 C  C     . VAL B 1 48  ? -10.75013 18.09078 3.33057   1.000 81.04823  ? 48  VAL B C     1 
ATOM   1367 O  O     . VAL B 1 48  ? -9.61404  18.56914 3.27038   1.000 68.34393  ? 48  VAL B O     1 
ATOM   1368 C  CB    . VAL B 1 48  ? -10.77106 15.85647 2.13520   1.000 84.93173  ? 48  VAL B CB    1 
ATOM   1369 C  CG1   . VAL B 1 48  ? -10.41284 15.39207 3.52999   1.000 82.76470  ? 48  VAL B CG1   1 
ATOM   1370 C  CG2   . VAL B 1 48  ? -11.78544 14.90712 1.51393   1.000 85.80326  ? 48  VAL B CG2   1 
ATOM   1371 N  N     . LEU B 1 49  ? -11.54145 18.23321 4.39113   1.000 83.39031  ? 49  LEU B N     1 
ATOM   1372 C  CA    . LEU B 1 49  ? -11.13454 18.96096 5.58694   1.000 88.24819  ? 49  LEU B CA    1 
ATOM   1373 C  C     . LEU B 1 49  ? -10.61729 17.95292 6.60647   1.000 85.45011  ? 49  LEU B C     1 
ATOM   1374 O  O     . LEU B 1 49  ? -11.39371 17.17308 7.16849   1.000 87.36297  ? 49  LEU B O     1 
ATOM   1375 C  CB    . LEU B 1 49  ? -12.30240 19.76935 6.14661   1.000 88.49573  ? 49  LEU B CB    1 
ATOM   1376 C  CG    . LEU B 1 49  ? -11.98102 20.73266 7.28635   1.000 91.35240  ? 49  LEU B CG    1 
ATOM   1377 C  CD1   . LEU B 1 49  ? -10.99191 21.78223 6.81344   1.000 91.33337  ? 49  LEU B CD1   1 
ATOM   1378 C  CD2   . LEU B 1 49  ? -13.24952 21.38268 7.81885   1.000 85.38277  ? 49  LEU B CD2   1 
ATOM   1379 N  N     . ILE B 1 50  ? -9.31362  17.95611 6.83566   1.000 81.80570  ? 50  ILE B N     1 
ATOM   1380 C  CA    . ILE B 1 50  ? -8.67019  17.00365 7.73706   1.000 84.48173  ? 50  ILE B CA    1 
ATOM   1381 C  C     . ILE B 1 50  ? -8.37524  17.71083 9.05398   1.000 75.62771  ? 50  ILE B C     1 
ATOM   1382 O  O     . ILE B 1 50  ? -7.75360  18.78310 9.03927   1.000 70.60109  ? 50  ILE B O     1 
ATOM   1383 C  CB    . ILE B 1 50  ? -7.38036  16.42581 7.13161   1.000 75.86238  ? 50  ILE B CB    1 
ATOM   1384 C  CG1   . ILE B 1 50  ? -7.68975  15.68026 5.83644   1.000 73.80025  ? 50  ILE B CG1   1 
ATOM   1385 C  CG2   . ILE B 1 50  ? -6.71605  15.49455 8.11956   1.000 71.95170  ? 50  ILE B CG2   1 
ATOM   1386 C  CD1   . ILE B 1 50  ? -6.50416  14.93872 5.27633   1.000 69.57840  ? 50  ILE B CD1   1 
ATOM   1387 N  N     . PRO B 1 51  ? -8.80063  17.16716 10.19104  1.000 73.33197  ? 51  PRO B N     1 
ATOM   1388 C  CA    . PRO B 1 51  ? -8.47833  17.80175 11.47059  1.000 72.27940  ? 51  PRO B CA    1 
ATOM   1389 C  C     . PRO B 1 51  ? -7.11741  17.35762 11.98687  1.000 68.08654  ? 51  PRO B C     1 
ATOM   1390 O  O     . PRO B 1 51  ? -6.69771  16.21095 11.80916  1.000 70.77335  ? 51  PRO B O     1 
ATOM   1391 C  CB    . PRO B 1 51  ? -9.61510  17.33091 12.38626  1.000 78.44879  ? 51  PRO B CB    1 
ATOM   1392 C  CG    . PRO B 1 51  ? -9.94916  15.98371 11.85914  1.000 78.43396  ? 51  PRO B CG    1 
ATOM   1393 C  CD    . PRO B 1 51  ? -9.73583  16.04006 10.35795  1.000 81.47249  ? 51  PRO B CD    1 
ATOM   1394 N  N     . THR B 1 52  ? -6.41300  18.29727 12.61704  1.000 66.19749  ? 52  THR B N     1 
ATOM   1395 C  CA    . THR B 1 52  ? -5.09359  18.02382 13.17234  1.000 59.37791  ? 52  THR B CA    1 
ATOM   1396 C  C     . THR B 1 52  ? -5.12011  17.73202 14.66401  1.000 83.47531  ? 52  THR B C     1 
ATOM   1397 O  O     . THR B 1 52  ? -4.18205  17.10825 15.17021  1.000 84.96557  ? 52  THR B O     1 
ATOM   1398 C  CB    . THR B 1 52  ? -4.14282  19.20400 12.92945  1.000 67.18757  ? 52  THR B CB    1 
ATOM   1399 O  OG1   . THR B 1 52  ? -4.53794  20.31144 13.74789  1.000 62.31805  ? 52  THR B OG1   1 
ATOM   1400 C  CG2   . THR B 1 52  ? -4.16445  19.62481 11.46702  1.000 78.09857  ? 52  THR B CG2   1 
ATOM   1401 N  N     . GLY B 1 53  ? -6.15932  18.16528 15.37482  1.000 75.62935  ? 53  GLY B N     1 
ATOM   1402 C  CA    . GLY B 1 53  ? -6.22143  17.97974 16.80843  1.000 82.46236  ? 53  GLY B CA    1 
ATOM   1403 C  C     . GLY B 1 53  ? -5.37958  18.94031 17.61425  1.000 85.09123  ? 53  GLY B C     1 
ATOM   1404 O  O     . GLY B 1 53  ? -5.17197  18.70368 18.81028  1.000 82.07522  ? 53  GLY B O     1 
ATOM   1405 N  N     . LEU B 1 54  ? -4.89284  20.01711 17.00476  1.000 70.42561  ? 54  LEU B N     1 
ATOM   1406 C  CA    . LEU B 1 54  ? -4.02391  20.97500 17.67026  1.000 77.33538  ? 54  LEU B CA    1 
ATOM   1407 C  C     . LEU B 1 54  ? -4.74233  22.30441 17.86065  1.000 78.21623  ? 54  LEU B C     1 
ATOM   1408 O  O     . LEU B 1 54  ? -5.46282  22.76821 16.97082  1.000 75.91860  ? 54  LEU B O     1 
ATOM   1409 C  CB    . LEU B 1 54  ? -2.73579  21.19587 16.87137  1.000 79.53798  ? 54  LEU B CB    1 
ATOM   1410 C  CG    . LEU B 1 54  ? -1.88282  19.96851 16.54214  1.000 79.61125  ? 54  LEU B CG    1 
ATOM   1411 C  CD1   . LEU B 1 54  ? -0.53883  20.39321 15.96424  1.000 87.51429  ? 54  LEU B CD1   1 
ATOM   1412 C  CD2   . LEU B 1 54  ? -1.69180  19.09283 17.76944  1.000 84.53436  ? 54  LEU B CD2   1 
ATOM   1413 N  N     . ILE B 1 55  ? -4.54238  22.90820 19.02959  1.000 78.86587  ? 55  ILE B N     1 
ATOM   1414 C  CA    . ILE B 1 55  ? -5.00143  24.26047 19.32654  1.000 76.83170  ? 55  ILE B CA    1 
ATOM   1415 C  C     . ILE B 1 55  ? -3.79017  25.04616 19.80518  1.000 78.40664  ? 55  ILE B C     1 
ATOM   1416 O  O     . ILE B 1 55  ? -3.19449  24.70518 20.83419  1.000 86.25636  ? 55  ILE B O     1 
ATOM   1417 C  CB    . ILE B 1 55  ? -6.11847  24.28005 20.38312  1.000 80.68835  ? 55  ILE B CB    1 
ATOM   1418 N  N     . LEU B 1 56  ? -3.42432  26.08753 19.06484  1.000 75.64377  ? 56  LEU B N     1 
ATOM   1419 C  CA    . LEU B 1 56  ? -2.15225  26.76685 19.25007  1.000 78.49310  ? 56  LEU B CA    1 
ATOM   1420 C  C     . LEU B 1 56  ? -2.34635  28.17958 19.78447  1.000 83.29158  ? 56  LEU B C     1 
ATOM   1421 O  O     . LEU B 1 56  ? -3.38460  28.81133 19.56801  1.000 82.28295  ? 56  LEU B O     1 
ATOM   1422 C  CB    . LEU B 1 56  ? -1.37917  26.82865 17.93138  1.000 84.53694  ? 56  LEU B CB    1 
ATOM   1423 C  CG    . LEU B 1 56  ? -1.40203  25.55023 17.09494  1.000 82.67664  ? 56  LEU B CG    1 
ATOM   1424 C  CD1   . LEU B 1 56  ? -0.83344  25.81898 15.71665  1.000 80.91595  ? 56  LEU B CD1   1 
ATOM   1425 C  CD2   . LEU B 1 56  ? -0.63263  24.44075 17.79055  1.000 86.17171  ? 56  LEU B CD2   1 
ATOM   1426 N  N     . GLU B 1 57  ? -1.32649  28.66720 20.48665  1.000 95.15767  ? 57  GLU B N     1 
ATOM   1427 C  CA    . GLU B 1 57  ? -1.22571  30.06869 20.88342  1.000 93.33469  ? 57  GLU B CA    1 
ATOM   1428 C  C     . GLU B 1 57  ? 0.00256   30.64371 20.18676  1.000 94.06145  ? 57  GLU B C     1 
ATOM   1429 O  O     . GLU B 1 57  ? 1.12942   30.49186 20.66639  1.000 92.30247  ? 57  GLU B O     1 
ATOM   1430 C  CB    . GLU B 1 57  ? -1.13103  30.22407 22.39930  1.000 94.71766  ? 57  GLU B CB    1 
ATOM   1431 C  CG    . GLU B 1 57  ? -0.79137  31.64614 22.84668  1.000 110.80496 ? 57  GLU B CG    1 
ATOM   1432 C  CD    . GLU B 1 57  ? -1.05055  31.88795 24.32328  1.000 119.99803 ? 57  GLU B CD    1 
ATOM   1433 O  OE1   . GLU B 1 57  ? -1.67658  31.02663 24.97619  1.000 117.69552 ? 57  GLU B OE1   1 
ATOM   1434 O  OE2   . GLU B 1 57  ? -0.62856  32.94812 24.83030  1.000 118.01128 ? 57  GLU B OE2   1 
ATOM   1435 N  N     . ILE B 1 58  ? -0.22128  31.28653 19.04970  1.000 90.04655  ? 58  ILE B N     1 
ATOM   1436 C  CA    . ILE B 1 58  ? 0.86468   31.92402 18.30494  1.000 90.46638  ? 58  ILE B CA    1 
ATOM   1437 C  C     . ILE B 1 58  ? 1.09392   33.31851 18.88257  1.000 95.43831  ? 58  ILE B C     1 
ATOM   1438 O  O     . ILE B 1 58  ? 0.13459   34.09588 19.00276  1.000 93.45142  ? 58  ILE B O     1 
ATOM   1439 C  CB    . ILE B 1 58  ? 0.53826   31.98426 16.81531  1.000 87.31402  ? 58  ILE B CB    1 
ATOM   1440 C  CG1   . ILE B 1 58  ? 0.42798   30.56831 16.23923  1.000 87.88370  ? 58  ILE B CG1   1 
ATOM   1441 C  CG2   . ILE B 1 58  ? 1.59892   32.78395 16.07042  1.000 87.38910  ? 58  ILE B CG2   1 
ATOM   1442 C  CD1   . ILE B 1 58  ? 0.10282   30.52543 14.77277  1.000 80.03398  ? 58  ILE B CD1   1 
ATOM   1443 N  N     . PRO B 1 59  ? 2.31920   33.66110 19.27019  1.000 97.05335  ? 59  PRO B N     1 
ATOM   1444 C  CA    . PRO B 1 59  ? 2.54839   34.94401 19.94365  1.000 100.84312 ? 59  PRO B CA    1 
ATOM   1445 C  C     . PRO B 1 59  ? 2.34927   36.12704 19.00747  1.000 101.57920 ? 59  PRO B C     1 
ATOM   1446 O  O     . PRO B 1 59  ? 2.28167   35.99352 17.78302  1.000 87.90029  ? 59  PRO B O     1 
ATOM   1447 C  CB    . PRO B 1 59  ? 4.00276   34.84381 20.40921  1.000 98.82052  ? 59  PRO B CB    1 
ATOM   1448 C  CG    . PRO B 1 59  ? 4.63222   33.88788 19.45065  1.000 98.30355  ? 59  PRO B CG    1 
ATOM   1449 C  CD    . PRO B 1 59  ? 3.56142   32.88397 19.12278  1.000 89.78912  ? 59  PRO B CD    1 
ATOM   1450 N  N     . GLU B 1 60  ? 2.25507   37.30601 19.61827  1.000 101.25133 ? 60  GLU B N     1 
ATOM   1451 C  CA    . GLU B 1 60  ? 2.00071   38.52824 18.87022  1.000 101.71810 ? 60  GLU B CA    1 
ATOM   1452 C  C     . GLU B 1 60  ? 3.14879   38.81756 17.91285  1.000 98.75094  ? 60  GLU B C     1 
ATOM   1453 O  O     . GLU B 1 60  ? 4.30569   38.47483 18.16793  1.000 97.61029  ? 60  GLU B O     1 
ATOM   1454 C  CB    . GLU B 1 60  ? 1.80318   39.70873 19.82335  1.000 111.73968 ? 60  GLU B CB    1 
ATOM   1455 C  CG    . GLU B 1 60  ? 0.73863   39.49761 20.89685  1.000 121.12535 ? 60  GLU B CG    1 
ATOM   1456 C  CD    . GLU B 1 60  ? 1.26047   38.75685 22.11714  1.000 127.75992 ? 60  GLU B CD    1 
ATOM   1457 O  OE1   . GLU B 1 60  ? 2.28027   38.04387 21.99869  1.000 126.81763 ? 60  GLU B OE1   1 
ATOM   1458 O  OE2   . GLU B 1 60  ? 0.65067   38.89301 23.19889  1.000 132.20542 ? 60  GLU B OE2   1 
ATOM   1459 N  N     . GLY B 1 61  ? 2.81926   39.45564 16.79492  1.000 94.30265  ? 61  GLY B N     1 
ATOM   1460 C  CA    . GLY B 1 61  ? 3.84118   39.74546 15.80959  1.000 92.33204  ? 61  GLY B CA    1 
ATOM   1461 C  C     . GLY B 1 61  ? 4.23676   38.57108 14.94794  1.000 96.76147  ? 61  GLY B C     1 
ATOM   1462 O  O     . GLY B 1 61  ? 5.13881   38.70771 14.11595  1.000 95.60404  ? 61  GLY B O     1 
ATOM   1463 N  N     . TYR B 1 62  ? 3.57980   37.42411 15.11077  1.000 97.63308  ? 62  TYR B N     1 
ATOM   1464 C  CA    . TYR B 1 62  ? 3.90821   36.22309 14.36134  1.000 95.75167  ? 62  TYR B CA    1 
ATOM   1465 C  C     . TYR B 1 62  ? 2.62382   35.53749 13.92139  1.000 79.12814  ? 62  TYR B C     1 
ATOM   1466 O  O     . TYR B 1 62  ? 1.54275   35.79397 14.45677  1.000 72.40871  ? 62  TYR B O     1 
ATOM   1467 C  CB    . TYR B 1 62  ? 4.77518   35.27096 15.19092  1.000 89.35812  ? 62  TYR B CB    1 
ATOM   1468 C  CG    . TYR B 1 62  ? 6.12822   35.84509 15.53871  1.000 89.81316  ? 62  TYR B CG    1 
ATOM   1469 C  CD1   . TYR B 1 62  ? 7.19102   35.75528 14.64667  1.000 94.53024  ? 62  TYR B CD1   1 
ATOM   1470 C  CD2   . TYR B 1 62  ? 6.34241   36.48501 16.75237  1.000 87.62421  ? 62  TYR B CD2   1 
ATOM   1471 C  CE1   . TYR B 1 62  ? 8.43136   36.28286 14.95585  1.000 96.65199  ? 62  TYR B CE1   1 
ATOM   1472 C  CE2   . TYR B 1 62  ? 7.57752   37.01379 17.07107  1.000 88.55411  ? 62  TYR B CE2   1 
ATOM   1473 C  CZ    . TYR B 1 62  ? 8.61915   36.90973 16.16989  1.000 94.18994  ? 62  TYR B CZ    1 
ATOM   1474 O  OH    . TYR B 1 62  ? 9.85171   37.43517 16.48415  1.000 99.74010  ? 62  TYR B OH    1 
ATOM   1475 N  N     . GLU B 1 63  ? 2.75799   34.65841 12.93062  1.000 80.09584  ? 63  GLU B N     1 
ATOM   1476 C  CA    . GLU B 1 63  ? 1.62465   33.94442 12.36561  1.000 82.48916  ? 63  GLU B CA    1 
ATOM   1477 C  C     . GLU B 1 63  ? 2.02738   32.50776 12.07189  1.000 78.29983  ? 63  GLU B C     1 
ATOM   1478 O  O     . GLU B 1 63  ? 3.20073   32.13489 12.15097  1.000 81.32605  ? 63  GLU B O     1 
ATOM   1479 C  CB    . GLU B 1 63  ? 1.12051   34.60639 11.07852  1.000 73.12061  ? 63  GLU B CB    1 
ATOM   1480 C  CG    . GLU B 1 63  ? 2.00191   34.32230 9.86862   1.000 81.18773  ? 63  GLU B CG    1 
ATOM   1481 C  CD    . GLU B 1 63  ? 1.41830   34.86428 8.58063   1.000 79.86605  ? 63  GLU B CD    1 
ATOM   1482 O  OE1   . GLU B 1 63  ? 0.32267   35.46179 8.63324   1.000 68.49653  ? 63  GLU B OE1   1 
ATOM   1483 O  OE2   . GLU B 1 63  ? 2.05458   34.69484 7.51816   1.000 75.63042  ? 63  GLU B OE2   1 
ATOM   1484 N  N     . GLY B 1 64  ? 1.03343   31.70591 11.72260  1.000 70.68916  ? 64  GLY B N     1 
ATOM   1485 C  CA    . GLY B 1 64  ? 1.25506   30.34443 11.26074  1.000 71.80316  ? 64  GLY B CA    1 
ATOM   1486 C  C     . GLY B 1 64  ? 0.76781   30.19495 9.83338   1.000 71.74917  ? 64  GLY B C     1 
ATOM   1487 O  O     . GLY B 1 64  ? -0.28319  30.72738 9.47096   1.000 63.24971  ? 64  GLY B O     1 
ATOM   1488 N  N     . GLN B 1 65  ? 1.54184   29.47612 9.02537   1.000 63.35298  ? 65  GLN B N     1 
ATOM   1489 C  CA    . GLN B 1 65  ? 1.23084   29.26805 7.61698   1.000 62.27083  ? 65  GLN B CA    1 
ATOM   1490 C  C     . GLN B 1 65  ? 1.17749   27.77408 7.33949   1.000 59.13338  ? 65  GLN B C     1 
ATOM   1491 O  O     . GLN B 1 65  ? 2.18662   27.07621 7.48626   1.000 58.09547  ? 65  GLN B O     1 
ATOM   1492 C  CB    . GLN B 1 65  ? 2.26753   29.94320 6.71700   1.000 56.71874  ? 65  GLN B CB    1 
ATOM   1493 C  CG    . GLN B 1 65  ? 2.39865   31.43990 6.92771   1.000 66.73302  ? 65  GLN B CG    1 
ATOM   1494 C  CD    . GLN B 1 65  ? 3.45917   32.05604 6.03962   1.000 71.77254  ? 65  GLN B CD    1 
ATOM   1495 O  OE1   . GLN B 1 65  ? 3.78230   31.52367 4.97713   1.000 68.07574  ? 65  GLN B OE1   1 
ATOM   1496 N  NE2   . GLN B 1 65  ? 4.01376   33.18066 6.47489   1.000 65.10855  ? 65  GLN B NE2   1 
ATOM   1497 N  N     . VAL B 1 66  ? 0.00483   27.28655 6.94544   1.000 49.23094  ? 66  VAL B N     1 
ATOM   1498 C  CA    . VAL B 1 66  ? -0.15052  25.89264 6.54309   1.000 61.49063  ? 66  VAL B CA    1 
ATOM   1499 C  C     . VAL B 1 66  ? 0.31695   25.77207 5.09572   1.000 58.65625  ? 66  VAL B C     1 
ATOM   1500 O  O     . VAL B 1 66  ? -0.35302  26.24510 4.17501   1.000 56.86846  ? 66  VAL B O     1 
ATOM   1501 C  CB    . VAL B 1 66  ? -1.59790  25.41551 6.70449   1.000 61.54935  ? 66  VAL B CB    1 
ATOM   1502 C  CG1   . VAL B 1 66  ? -1.72985  23.96544 6.26403   1.000 58.64385  ? 66  VAL B CG1   1 
ATOM   1503 C  CG2   . VAL B 1 66  ? -2.05528  25.58310 8.14818   1.000 60.21431  ? 66  VAL B CG2   1 
ATOM   1504 N  N     . ARG B 1 67  ? 1.47100   25.14908 4.89570   1.000 52.41599  ? 67  ARG B N     1 
ATOM   1505 C  CA    . ARG B 1 67  ? 2.07648   24.99548 3.58488   1.000 56.87642  ? 67  ARG B CA    1 
ATOM   1506 C  C     . ARG B 1 67  ? 2.05153   23.53805 3.14493   1.000 63.04304  ? 67  ARG B C     1 
ATOM   1507 O  O     . ARG B 1 67  ? 1.98467   22.62717 3.97787   1.000 61.85826  ? 67  ARG B O     1 
ATOM   1508 C  CB    . ARG B 1 67  ? 3.52421   25.50426 3.59227   1.000 55.43718  ? 67  ARG B CB    1 
ATOM   1509 C  CG    . ARG B 1 67  ? 3.65427   26.99969 3.80674   1.000 57.46758  ? 67  ARG B CG    1 
ATOM   1510 C  CD    . ARG B 1 67  ? 5.10854   27.42527 3.76243   1.000 54.15052  ? 67  ARG B CD    1 
ATOM   1511 N  NE    . ARG B 1 67  ? 5.27507   28.83269 4.10170   1.000 65.73254  ? 67  ARG B NE    1 
ATOM   1512 C  CZ    . ARG B 1 67  ? 6.44774   29.44182 4.20650   1.000 66.77516  ? 67  ARG B CZ    1 
ATOM   1513 N  NH1   . ARG B 1 67  ? 7.58293   28.79542 3.99724   1.000 63.71290  ? 67  ARG B NH1   1 
ATOM   1514 N  NH2   . ARG B 1 67  ? 6.48239   30.73089 4.53159   1.000 63.50627  ? 67  ARG B NH2   1 
ATOM   1515 N  N     . PRO B 1 68  ? 2.09421   23.27846 1.83938   1.000 59.53992  ? 68  PRO B N     1 
ATOM   1516 C  CA    . PRO B 1 68  ? 2.04090   21.89344 1.36446   1.000 57.84076  ? 68  PRO B CA    1 
ATOM   1517 C  C     . PRO B 1 68  ? 3.35057   21.15971 1.60707   1.000 65.11288  ? 68  PRO B C     1 
ATOM   1518 O  O     . PRO B 1 68  ? 4.41942   21.75461 1.76117   1.000 58.12506  ? 68  PRO B O     1 
ATOM   1519 C  CB    . PRO B 1 68  ? 1.76171   22.03612 -0.13817  1.000 57.45996  ? 68  PRO B CB    1 
ATOM   1520 C  CG    . PRO B 1 68  ? 1.31609   23.45917 -0.33180  1.000 58.00067  ? 68  PRO B CG    1 
ATOM   1521 C  CD    . PRO B 1 68  ? 2.02301   24.23994 0.72722   1.000 59.88718  ? 68  PRO B CD    1 
ATOM   1522 N  N     . ARG B 1 69  ? 3.24792   19.83390 1.63512   1.000 73.28172  ? 69  ARG B N     1 
ATOM   1523 C  CA    . ARG B 1 69  ? 4.41382   18.96318 1.68973   1.000 76.94394  ? 69  ARG B CA    1 
ATOM   1524 C  C     . ARG B 1 69  ? 4.86157   18.62751 0.27325   1.000 80.68055  ? 69  ARG B C     1 
ATOM   1525 O  O     . ARG B 1 69  ? 4.04675   18.21197 -0.55709  1.000 74.55443  ? 69  ARG B O     1 
ATOM   1526 C  CB    . ARG B 1 69  ? 4.09262   17.68362 2.46143   1.000 78.10254  ? 69  ARG B CB    1 
ATOM   1527 C  CG    . ARG B 1 69  ? 4.29313   17.79139 3.95902   1.000 86.21776  ? 69  ARG B CG    1 
ATOM   1528 C  CD    . ARG B 1 69  ? 5.75239   18.04964 4.28452   1.000 90.11934  ? 69  ARG B CD    1 
ATOM   1529 N  NE    . ARG B 1 69  ? 6.11138   17.55303 5.60645   1.000 97.62877  ? 69  ARG B NE    1 
ATOM   1530 C  CZ    . ARG B 1 69  ? 6.39996   16.28706 5.87422   1.000 101.81275 ? 69  ARG B CZ    1 
ATOM   1531 N  NH1   . ARG B 1 69  ? 6.35463   15.35407 4.93671   1.000 87.89473  ? 69  ARG B NH1   1 
ATOM   1532 N  NH2   . ARG B 1 69  ? 6.74282   15.94872 7.11306   1.000 107.08158 ? 69  ARG B NH2   1 
ATOM   1533 N  N     . SER B 1 70  ? 6.15792   18.80428 0.00353   1.000 80.08419  ? 70  SER B N     1 
ATOM   1534 C  CA    . SER B 1 70  ? 6.67663   18.56688 -1.34060  1.000 85.37808  ? 70  SER B CA    1 
ATOM   1535 C  C     . SER B 1 70  ? 6.57650   17.10097 -1.74522  1.000 74.46736  ? 70  SER B C     1 
ATOM   1536 O  O     . SER B 1 70  ? 6.34879   16.80109 -2.92237  1.000 72.95259  ? 70  SER B O     1 
ATOM   1537 C  CB    . SER B 1 70  ? 8.12683   19.04270 -1.42914  1.000 77.63276  ? 70  SER B CB    1 
ATOM   1538 O  OG    . SER B 1 70  ? 8.93890   18.39165 -0.46919  1.000 83.92110  ? 70  SER B OG    1 
ATOM   1539 N  N     . GLY B 1 71  ? 6.72764   16.17901 -0.79438  1.000 74.37597  ? 71  GLY B N     1 
ATOM   1540 C  CA    . GLY B 1 71  ? 6.65350   14.76831 -1.13755  1.000 77.89122  ? 71  GLY B CA    1 
ATOM   1541 C  C     . GLY B 1 71  ? 5.26342   14.34878 -1.57832  1.000 74.72655  ? 71  GLY B C     1 
ATOM   1542 O  O     . GLY B 1 71  ? 5.10243   13.66770 -2.59215  1.000 71.06144  ? 71  GLY B O     1 
ATOM   1543 N  N     . LEU B 1 72  ? 4.23881   14.73477 -0.81315  1.000 75.55386  ? 72  LEU B N     1 
ATOM   1544 C  CA    . LEU B 1 72  ? 2.87702   14.34752 -1.16940  1.000 77.60303  ? 72  LEU B CA    1 
ATOM   1545 C  C     . LEU B 1 72  ? 2.41895   15.04625 -2.43978  1.000 66.18973  ? 72  LEU B C     1 
ATOM   1546 O  O     . LEU B 1 72  ? 1.52644   14.55070 -3.13957  1.000 74.08091  ? 72  LEU B O     1 
ATOM   1547 C  CB    . LEU B 1 72  ? 1.91483   14.65435 -0.02066  1.000 73.71652  ? 72  LEU B CB    1 
ATOM   1548 C  CG    . LEU B 1 72  ? 1.83011   13.63096 1.11421   1.000 83.50490  ? 72  LEU B CG    1 
ATOM   1549 C  CD1   . LEU B 1 72  ? 0.92205   14.14038 2.22240   1.000 79.19372  ? 72  LEU B CD1   1 
ATOM   1550 C  CD2   . LEU B 1 72  ? 1.32923   12.30143 0.58467   1.000 86.31659  ? 72  LEU B CD2   1 
ATOM   1551 N  N     . ALA B 1 73  ? 3.01513   16.19835 -2.75066  1.000 64.98201  ? 73  ALA B N     1 
ATOM   1552 C  CA    . ALA B 1 73  ? 2.61505   16.95026 -3.93639  1.000 70.31450  ? 73  ALA B CA    1 
ATOM   1553 C  C     . ALA B 1 73  ? 3.08715   16.27088 -5.21842  1.000 68.27602  ? 73  ALA B C     1 
ATOM   1554 O  O     . ALA B 1 73  ? 2.32501   16.15221 -6.18567  1.000 65.39930  ? 73  ALA B O     1 
ATOM   1555 C  CB    . ALA B 1 73  ? 3.15293   18.37904 -3.84869  1.000 65.42121  ? 73  ALA B CB    1 
ATOM   1556 N  N     . TRP B 1 74  ? 4.32739   15.78916 -5.23499  1.000 63.49516  ? 74  TRP B N     1 
ATOM   1557 C  CA    . TRP B 1 74  ? 4.87434   15.21124 -6.45484  1.000 74.29803  ? 74  TRP B CA    1 
ATOM   1558 C  C     . TRP B 1 74  ? 4.48395   13.74821 -6.61921  1.000 70.10239  ? 74  TRP B C     1 
ATOM   1559 O  O     . TRP B 1 74  ? 4.21705   13.30159 -7.73933  1.000 75.14526  ? 74  TRP B O     1 
ATOM   1560 C  CB    . TRP B 1 74  ? 6.39468   15.36433 -6.46507  1.000 65.46633  ? 74  TRP B CB    1 
ATOM   1561 C  CG    . TRP B 1 74  ? 7.06125   14.59607 -7.55914  1.000 72.42901  ? 74  TRP B CG    1 
ATOM   1562 C  CD1   . TRP B 1 74  ? 7.99548   13.61310 -7.41808  1.000 73.97756  ? 74  TRP B CD1   1 
ATOM   1563 C  CD2   . TRP B 1 74  ? 6.83588   14.73731 -8.96610  1.000 77.72972  ? 74  TRP B CD2   1 
ATOM   1564 N  NE1   . TRP B 1 74  ? 8.37233   13.13736 -8.65068  1.000 82.42861  ? 74  TRP B NE1   1 
ATOM   1565 C  CE2   . TRP B 1 74  ? 7.67335   13.81101 -9.61768  1.000 82.42683  ? 74  TRP B CE2   1 
ATOM   1566 C  CE3   . TRP B 1 74  ? 6.00901   15.55969 -9.73865  1.000 69.71856  ? 74  TRP B CE3   1 
ATOM   1567 C  CZ2   . TRP B 1 74  ? 7.70702   13.68382 -11.00351 1.000 76.58786  ? 74  TRP B CZ2   1 
ATOM   1568 C  CZ3   . TRP B 1 74  ? 6.04368   15.43179 -11.11387 1.000 73.70208  ? 74  TRP B CZ3   1 
ATOM   1569 C  CH2   . TRP B 1 74  ? 6.88626   14.50173 -11.73226 1.000 71.86877  ? 74  TRP B CH2   1 
ATOM   1570 N  N     . LYS B 1 75  ? 4.43968   12.98891 -5.52384  1.000 77.29031  ? 75  LYS B N     1 
ATOM   1571 C  CA    . LYS B 1 75  ? 4.19913   11.55439 -5.63438  1.000 80.74647  ? 75  LYS B CA    1 
ATOM   1572 C  C     . LYS B 1 75  ? 2.73301   11.24200 -5.91490  1.000 85.29558  ? 75  LYS B C     1 
ATOM   1573 O  O     . LYS B 1 75  ? 2.43063   10.31936 -6.67950  1.000 82.79679  ? 75  LYS B O     1 
ATOM   1574 C  CB    . LYS B 1 75  ? 4.66073   10.84980 -4.35789  1.000 70.32448  ? 75  LYS B CB    1 
ATOM   1575 N  N     . LYS B 1 76  ? 1.81003   11.99619 -5.31396  1.000 91.83403  ? 76  LYS B N     1 
ATOM   1576 C  CA    . LYS B 1 76  ? 0.38843   11.68476 -5.39327  1.000 91.69148  ? 76  LYS B CA    1 
ATOM   1577 C  C     . LYS B 1 76  ? -0.46991  12.83195 -5.91062  1.000 86.44155  ? 76  LYS B C     1 
ATOM   1578 O  O     . LYS B 1 76  ? -1.68923  12.66091 -6.03827  1.000 86.96197  ? 76  LYS B O     1 
ATOM   1579 C  CB    . LYS B 1 76  ? -0.12944  11.24020 -4.01710  1.000 90.85864  ? 76  LYS B CB    1 
ATOM   1580 C  CG    . LYS B 1 76  ? 0.55723   9.99382  -3.48094  1.000 86.32075  ? 76  LYS B CG    1 
ATOM   1581 C  CD    . LYS B 1 76  ? 0.31987   9.81737  -1.99152  1.000 87.73997  ? 76  LYS B CD    1 
ATOM   1582 C  CE    . LYS B 1 76  ? 1.16253   8.68091  -1.43632  1.000 90.10277  ? 76  LYS B CE    1 
ATOM   1583 N  NZ    . LYS B 1 76  ? 1.10323   8.61750  0.04988   1.000 101.26731 ? 76  LYS B NZ    1 
ATOM   1584 N  N     . GLY B 1 77  ? 0.11824   13.98515 -6.21867  1.000 79.02962  ? 77  GLY B N     1 
ATOM   1585 C  CA    . GLY B 1 77  ? -0.66808  15.10279 -6.70887  1.000 75.53615  ? 77  GLY B CA    1 
ATOM   1586 C  C     . GLY B 1 77  ? -1.55559  15.74420 -5.66701  1.000 79.15736  ? 77  GLY B C     1 
ATOM   1587 O  O     . GLY B 1 77  ? -2.58241  16.33769 -6.01332  1.000 80.83902  ? 77  GLY B O     1 
ATOM   1588 N  N     . LEU B 1 78  ? -1.17890  15.64749 -4.39673  1.000 71.33675  ? 78  LEU B N     1 
ATOM   1589 C  CA    . LEU B 1 78  ? -1.96838  16.15561 -3.28500  1.000 77.46646  ? 78  LEU B CA    1 
ATOM   1590 C  C     . LEU B 1 78  ? -1.36947  17.46359 -2.78557  1.000 68.36685  ? 78  LEU B C     1 
ATOM   1591 O  O     . LEU B 1 78  ? -0.14787  17.59250 -2.67527  1.000 78.15507  ? 78  LEU B O     1 
ATOM   1592 C  CB    . LEU B 1 78  ? -2.00918  15.12829 -2.15184  1.000 75.39441  ? 78  LEU B CB    1 
ATOM   1593 C  CG    . LEU B 1 78  ? -3.05704  15.27890 -1.05162  1.000 82.30347  ? 78  LEU B CG    1 
ATOM   1594 C  CD1   . LEU B 1 78  ? -4.45621  15.17385 -1.63252  1.000 82.54066  ? 78  LEU B CD1   1 
ATOM   1595 C  CD2   . LEU B 1 78  ? -2.83611  14.22232 0.01766   1.000 84.45352  ? 78  LEU B CD2   1 
ATOM   1596 N  N     . THR B 1 79  ? -2.23025  18.43422 -2.48407  1.000 62.02447  ? 79  THR B N     1 
ATOM   1597 C  CA    . THR B 1 79  ? -1.75706  19.73540 -2.03316  1.000 61.86170  ? 79  THR B CA    1 
ATOM   1598 C  C     . THR B 1 79  ? -2.78875  20.37376 -1.11626  1.000 64.44013  ? 79  THR B C     1 
ATOM   1599 O  O     . THR B 1 79  ? -3.95566  19.97413 -1.08098  1.000 67.61473  ? 79  THR B O     1 
ATOM   1600 C  CB    . THR B 1 79  ? -1.46268  20.67157 -3.21045  1.000 62.63938  ? 79  THR B CB    1 
ATOM   1601 O  OG1   . THR B 1 79  ? -0.92104  21.90288 -2.71729  1.000 58.31506  ? 79  THR B OG1   1 
ATOM   1602 C  CG2   . THR B 1 79  ? -2.73766  20.96388 -3.98432  1.000 63.59227  ? 79  THR B CG2   1 
ATOM   1603 N  N     . VAL B 1 80  ? -2.33586  21.37714 -0.37123  1.000 56.41119  ? 80  VAL B N     1 
ATOM   1604 C  CA    . VAL B 1 80  ? -3.22031  22.17180 0.47297   1.000 59.15299  ? 80  VAL B CA    1 
ATOM   1605 C  C     . VAL B 1 80  ? -3.92644  23.19027 -0.41171  1.000 60.86640  ? 80  VAL B C     1 
ATOM   1606 O  O     . VAL B 1 80  ? -3.27654  23.96510 -1.12174  1.000 68.19488  ? 80  VAL B O     1 
ATOM   1607 C  CB    . VAL B 1 80  ? -2.44067  22.85894 1.60283   1.000 68.20870  ? 80  VAL B CB    1 
ATOM   1608 C  CG1   . VAL B 1 80  ? -3.37071  23.72098 2.44472   1.000 51.30762  ? 80  VAL B CG1   1 
ATOM   1609 C  CG2   . VAL B 1 80  ? -1.73872  21.82179 2.46810   1.000 55.46373  ? 80  VAL B CG2   1 
ATOM   1610 N  N     . LEU B 1 81  ? -5.26014  23.18659 -0.37137  1.000 68.34104  ? 81  LEU B N     1 
ATOM   1611 C  CA    . LEU B 1 81  ? -6.04347  23.99698 -1.29888  1.000 58.45396  ? 81  LEU B CA    1 
ATOM   1612 C  C     . LEU B 1 81  ? -5.76085  25.48312 -1.10844  1.000 66.94765  ? 81  LEU B C     1 
ATOM   1613 O  O     . LEU B 1 81  ? -5.35355  26.17735 -2.04661  1.000 61.82180  ? 81  LEU B O     1 
ATOM   1614 C  CB    . LEU B 1 81  ? -7.53290  23.69922 -1.11461  1.000 58.51105  ? 81  LEU B CB    1 
ATOM   1615 C  CG    . LEU B 1 81  ? -8.45312  23.70591 -2.33852  1.000 78.15419  ? 81  LEU B CG    1 
ATOM   1616 C  CD1   . LEU B 1 81  ? -9.87439  23.42406 -1.89968  1.000 73.41510  ? 81  LEU B CD1   1 
ATOM   1617 C  CD2   . LEU B 1 81  ? -8.38781  25.01729 -3.09966  1.000 81.76469  ? 81  LEU B CD2   1 
ATOM   1618 N  N     . ASN B 1 82  ? -5.97266  25.98999 0.10816   1.000 65.76332  ? 82  ASN B N     1 
ATOM   1619 C  CA    . ASN B 1 82  ? -5.83491  27.41096 0.40551   1.000 59.17411  ? 82  ASN B CA    1 
ATOM   1620 C  C     . ASN B 1 82  ? -4.41712  27.79504 0.82071   1.000 63.50513  ? 82  ASN B C     1 
ATOM   1621 O  O     . ASN B 1 82  ? -4.24054  28.73759 1.60507   1.000 65.31473  ? 82  ASN B O     1 
ATOM   1622 C  CB    . ASN B 1 82  ? -6.83253  27.81333 1.49231   1.000 61.90983  ? 82  ASN B CB    1 
ATOM   1623 C  CG    . ASN B 1 82  ? -6.55310  27.12949 2.81364   1.000 62.73416  ? 82  ASN B CG    1 
ATOM   1624 O  OD1   . ASN B 1 82  ? -6.24512  25.93857 2.85242   1.000 64.91440  ? 82  ASN B OD1   1 
ATOM   1625 N  ND2   . ASN B 1 82  ? -6.63685  27.88476 3.90392   1.000 61.14212  ? 82  ASN B ND2   1 
ATOM   1626 N  N     . ALA B 1 83  ? -3.40434  27.09349 0.31776   1.000 57.32107  ? 83  ALA B N     1 
ATOM   1627 C  CA    . ALA B 1 83  ? -2.03101  27.39445 0.69546   1.000 63.21757  ? 83  ALA B CA    1 
ATOM   1628 C  C     . ALA B 1 83  ? -1.62600  28.76686 0.16279   1.000 57.53927  ? 83  ALA B C     1 
ATOM   1629 O  O     . ALA B 1 83  ? -1.90975  29.09305 -0.99397  1.000 59.16394  ? 83  ALA B O     1 
ATOM   1630 C  CB    . ALA B 1 83  ? -1.07831  26.32866 0.16236   1.000 56.63125  ? 83  ALA B CB    1 
ATOM   1631 N  N     . PRO B 1 84  ? -0.97247  29.59808 0.98566   1.000 55.04416  ? 84  PRO B N     1 
ATOM   1632 C  CA    . PRO B 1 84  ? -0.60593  29.34263 2.38412   1.000 65.04191  ? 84  PRO B CA    1 
ATOM   1633 C  C     . PRO B 1 84  ? -1.76379  29.61732 3.33606   1.000 66.64165  ? 84  PRO B C     1 
ATOM   1634 O  O     . PRO B 1 84  ? -2.24848  30.74223 3.42519   1.000 63.00280  ? 84  PRO B O     1 
ATOM   1635 C  CB    . PRO B 1 84  ? 0.57172   30.30109 2.60250   1.000 58.91713  ? 84  PRO B CB    1 
ATOM   1636 C  CG    . PRO B 1 84  ? 0.24629   31.47734 1.72233   1.000 58.80281  ? 84  PRO B CG    1 
ATOM   1637 C  CD    . PRO B 1 84  ? -0.42040  30.87850 0.50082   1.000 60.19349  ? 84  PRO B CD    1 
ATOM   1638 N  N     . GLY B 1 85  ? -2.23381  28.59827 4.05328   1.000 60.83957  ? 85  GLY B N     1 
ATOM   1639 C  CA    . GLY B 1 85  ? -3.28627  28.77785 5.03588   1.000 57.91612  ? 85  GLY B CA    1 
ATOM   1640 C  C     . GLY B 1 85  ? -2.88379  29.69961 6.16780   1.000 62.05938  ? 85  GLY B C     1 
ATOM   1641 O  O     . GLY B 1 85  ? -1.95878  29.38782 6.93083   1.000 60.23153  ? 85  GLY B O     1 
ATOM   1642 N  N     . THR B 1 86  ? -3.56692  30.83366 6.29129   1.000 56.34304  ? 86  THR B N     1 
ATOM   1643 C  CA    . THR B 1 86  ? -3.19803  31.84778 7.27129   1.000 70.20762  ? 86  THR B CA    1 
ATOM   1644 C  C     . THR B 1 86  ? -3.78012  31.48039 8.63066   1.000 60.74623  ? 86  THR B C     1 
ATOM   1645 O  O     . THR B 1 86  ? -4.99940  31.51733 8.82303   1.000 69.25949  ? 86  THR B O     1 
ATOM   1646 C  CB    . THR B 1 86  ? -3.68924  33.21823 6.81736   1.000 72.65571  ? 86  THR B CB    1 
ATOM   1647 O  OG1   . THR B 1 86  ? -3.20915  33.48969 5.49480   1.000 66.16406  ? 86  THR B OG1   1 
ATOM   1648 C  CG2   . THR B 1 86  ? -3.17995  34.30114 7.76164   1.000 64.21592  ? 86  THR B CG2   1 
ATOM   1649 N  N     . ILE B 1 87  ? -2.91164  31.12914 9.57356   1.000 58.31357  ? 87  ILE B N     1 
ATOM   1650 C  CA    . ILE B 1 87  ? -3.30738  30.84764 10.94845  1.000 73.07156  ? 87  ILE B CA    1 
ATOM   1651 C  C     . ILE B 1 87  ? -3.02159  32.11298 11.74765  1.000 71.93936  ? 87  ILE B C     1 
ATOM   1652 O  O     . ILE B 1 87  ? -1.86871  32.40987 12.07366  1.000 69.89660  ? 87  ILE B O     1 
ATOM   1653 C  CB    . ILE B 1 87  ? -2.56838  29.63588 11.52145  1.000 73.35987  ? 87  ILE B CB    1 
ATOM   1654 C  CG1   . ILE B 1 87  ? -2.73440  28.42216 10.60419  1.000 62.44146  ? 87  ILE B CG1   1 
ATOM   1655 C  CG2   . ILE B 1 87  ? -3.07197  29.32458 12.92325  1.000 73.32768  ? 87  ILE B CG2   1 
ATOM   1656 C  CD1   . ILE B 1 87  ? -4.16988  27.98580 10.42003  1.000 65.16320  ? 87  ILE B CD1   1 
ATOM   1657 N  N     . ASP B 1 88  ? -4.07195  32.86631 12.05769  1.000 74.31874  ? 88  ASP B N     1 
ATOM   1658 C  CA    . ASP B 1 88  ? -3.90746  34.11700 12.78154  1.000 77.55657  ? 88  ASP B CA    1 
ATOM   1659 C  C     . ASP B 1 88  ? -3.46532  33.85261 14.21822  1.000 77.76269  ? 88  ASP B C     1 
ATOM   1660 O  O     . ASP B 1 88  ? -3.82726  32.84415 14.83064  1.000 71.77163  ? 88  ASP B O     1 
ATOM   1661 C  CB    . ASP B 1 88  ? -5.20992  34.91754 12.76059  1.000 83.84884  ? 88  ASP B CB    1 
ATOM   1662 C  CG    . ASP B 1 88  ? -5.78263  35.06316 11.36001  1.000 83.41429  ? 88  ASP B CG    1 
ATOM   1663 O  OD1   . ASP B 1 88  ? -6.49290  34.13990 10.90705  1.000 83.66212  ? 88  ASP B OD1   1 
ATOM   1664 O  OD2   . ASP B 1 88  ? -5.51636  36.09675 10.71024  1.000 81.56985  ? 88  ASP B OD2   1 
ATOM   1665 N  N     . ALA B 1 89  ? -2.66931  34.78123 14.75530  1.000 82.77799  ? 89  ALA B N     1 
ATOM   1666 C  CA    . ALA B 1 89  ? -2.07058  34.59125 16.07183  1.000 86.49095  ? 89  ALA B CA    1 
ATOM   1667 C  C     . ALA B 1 89  ? -3.10613  34.50440 17.18445  1.000 85.92536  ? 89  ALA B C     1 
ATOM   1668 O  O     . ALA B 1 89  ? -2.78436  34.02703 18.27827  1.000 85.76301  ? 89  ALA B O     1 
ATOM   1669 C  CB    . ALA B 1 89  ? -1.09025  35.72583 16.36885  1.000 88.03436  ? 89  ALA B CB    1 
ATOM   1670 N  N     . ASP B 1 90  ? -4.33420  34.95205 16.93637  1.000 90.18637  ? 90  ASP B N     1 
ATOM   1671 C  CA    . ASP B 1 90  ? -5.38973  34.94101 17.93790  1.000 91.95235  ? 90  ASP B CA    1 
ATOM   1672 C  C     . ASP B 1 90  ? -6.37641  33.79586 17.74402  1.000 91.77180  ? 90  ASP B C     1 
ATOM   1673 O  O     . ASP B 1 90  ? -7.44551  33.80193 18.36277  1.000 78.17726  ? 90  ASP B O     1 
ATOM   1674 C  CB    . ASP B 1 90  ? -6.12927  36.27977 17.93005  1.000 95.53766  ? 90  ASP B CB    1 
ATOM   1675 C  CG    . ASP B 1 90  ? -6.47737  36.74486 16.53075  1.000 96.50376  ? 90  ASP B CG    1 
ATOM   1676 O  OD1   . ASP B 1 90  ? -6.04424  36.09181 15.56023  1.000 90.10598  ? 90  ASP B OD1   1 
ATOM   1677 O  OD2   . ASP B 1 90  ? -7.18201  37.76586 16.40129  1.000 87.29081  ? 90  ASP B OD2   1 
ATOM   1678 N  N     . TYR B 1 91  ? -6.04414  32.81653 16.90554  1.000 87.47906  ? 91  TYR B N     1 
ATOM   1679 C  CA    . TYR B 1 91  ? -6.93246  31.68801 16.66429  1.000 84.70239  ? 91  TYR B CA    1 
ATOM   1680 C  C     . TYR B 1 91  ? -6.78937  30.65775 17.77683  1.000 76.31183  ? 91  TYR B C     1 
ATOM   1681 O  O     . TYR B 1 91  ? -5.67629  30.24210 18.11393  1.000 92.01964  ? 91  TYR B O     1 
ATOM   1682 C  CB    . TYR B 1 91  ? -6.63436  31.04995 15.30833  1.000 82.77005  ? 91  TYR B CB    1 
ATOM   1683 C  CG    . TYR B 1 91  ? -7.56972  29.91636 14.95011  1.000 72.35594  ? 91  TYR B CG    1 
ATOM   1684 C  CD1   . TYR B 1 91  ? -8.94585  30.06390 15.07098  1.000 82.49548  ? 91  TYR B CD1   1 
ATOM   1685 C  CD2   . TYR B 1 91  ? -7.07957  28.70540 14.47893  1.000 73.71564  ? 91  TYR B CD2   1 
ATOM   1686 C  CE1   . TYR B 1 91  ? -9.80683  29.03747 14.73913  1.000 86.71153  ? 91  TYR B CE1   1 
ATOM   1687 C  CE2   . TYR B 1 91  ? -7.93433  27.67092 14.14533  1.000 77.36213  ? 91  TYR B CE2   1 
ATOM   1688 C  CZ    . TYR B 1 91  ? -9.29711  27.84357 14.27777  1.000 74.13141  ? 91  TYR B CZ    1 
ATOM   1689 O  OH    . TYR B 1 91  ? -10.15755 26.82169 13.94968  1.000 72.86635  ? 91  TYR B OH    1 
ATOM   1690 N  N     . ARG B 1 92  ? -7.92285  30.24473 18.34258  1.000 76.32498  ? 92  ARG B N     1 
ATOM   1691 C  CA    . ARG B 1 92  ? -7.94635  29.30402 19.45170  1.000 88.20708  ? 92  ARG B CA    1 
ATOM   1692 C  C     . ARG B 1 92  ? -8.71560  28.03028 19.13616  1.000 86.50344  ? 92  ARG B C     1 
ATOM   1693 O  O     . ARG B 1 92  ? -8.81104  27.15144 20.00089  1.000 93.17814  ? 92  ARG B O     1 
ATOM   1694 C  CB    . ARG B 1 92  ? -8.54601  29.97146 20.69664  1.000 88.41901  ? 92  ARG B CB    1 
ATOM   1695 C  CG    . ARG B 1 92  ? -7.93342  31.32381 21.01632  1.000 89.79238  ? 92  ARG B CG    1 
ATOM   1696 C  CD    . ARG B 1 92  ? -6.47233  31.19208 21.40495  1.000 88.65934  ? 92  ARG B CD    1 
ATOM   1697 N  NE    . ARG B 1 92  ? -5.67523  32.30872 20.91261  1.000 101.04123 ? 92  ARG B NE    1 
ATOM   1698 C  CZ    . ARG B 1 92  ? -4.49397  32.65651 21.40298  1.000 105.01569 ? 92  ARG B CZ    1 
ATOM   1699 N  NH1   . ARG B 1 92  ? -3.96441  32.02690 22.43830  1.000 105.02051 ? 92  ARG B NH1   1 
ATOM   1700 N  NH2   . ARG B 1 92  ? -3.83030  33.66445 20.84398  1.000 105.42369 ? 92  ARG B NH2   1 
ATOM   1701 N  N     . GLY B 1 93  ? -9.27022  27.90413 17.93097  1.000 83.59539  ? 93  GLY B N     1 
ATOM   1702 C  CA    . GLY B 1 93  ? -9.94929  26.69295 17.52983  1.000 83.47080  ? 93  GLY B CA    1 
ATOM   1703 C  C     . GLY B 1 93  ? -8.98852  25.62434 17.03481  1.000 79.65474  ? 93  GLY B C     1 
ATOM   1704 O  O     . GLY B 1 93  ? -7.76690  25.77842 17.04954  1.000 83.81291  ? 93  GLY B O     1 
ATOM   1705 N  N     . GLU B 1 94  ? -9.57515  24.51648 16.58497  1.000 79.76383  ? 94  GLU B N     1 
ATOM   1706 C  CA    . GLU B 1 94  ? -8.80632  23.39826 16.05888  1.000 84.59879  ? 94  GLU B CA    1 
ATOM   1707 C  C     . GLU B 1 94  ? -8.26958  23.72533 14.67240  1.000 83.03790  ? 94  GLU B C     1 
ATOM   1708 O  O     . GLU B 1 94  ? -9.03292  24.06713 13.76356  1.000 79.47757  ? 94  GLU B O     1 
ATOM   1709 C  CB    . GLU B 1 94  ? -9.66723  22.13791 15.99761  1.000 87.79442  ? 94  GLU B CB    1 
ATOM   1710 C  CG    . GLU B 1 94  ? -8.92512  20.92532 15.45778  1.000 85.20784  ? 94  GLU B CG    1 
ATOM   1711 C  CD    . GLU B 1 94  ? -9.75403  19.65758 15.50237  1.000 92.91894  ? 94  GLU B CD    1 
ATOM   1712 O  OE1   . GLU B 1 94  ? -10.93396 19.69732 15.09738  1.000 96.34317  ? 94  GLU B OE1   1 
ATOM   1713 O  OE2   . GLU B 1 94  ? -9.22659  18.62026 15.95291  1.000 96.68045  ? 94  GLU B OE2   1 
ATOM   1714 N  N     . VAL B 1 95  ? -6.95414  23.60119 14.50833  1.000 83.83228  ? 95  VAL B N     1 
ATOM   1715 C  CA    . VAL B 1 95  ? -6.33852  23.82754 13.20860  1.000 72.03004  ? 95  VAL B CA    1 
ATOM   1716 C  C     . VAL B 1 95  ? -6.71280  22.68853 12.27157  1.000 74.02771  ? 95  VAL B C     1 
ATOM   1717 O  O     . VAL B 1 95  ? -6.58822  21.50710 12.62054  1.000 78.31790  ? 95  VAL B O     1 
ATOM   1718 C  CB    . VAL B 1 95  ? -4.81634  23.96199 13.35415  1.000 71.31120  ? 95  VAL B CB    1 
ATOM   1719 C  CG1   . VAL B 1 95  ? -4.15275  24.01152 11.98822  1.000 65.51816  ? 95  VAL B CG1   1 
ATOM   1720 C  CG2   . VAL B 1 95  ? -4.47613  25.20497 14.15931  1.000 72.95535  ? 95  VAL B CG2   1 
ATOM   1721 N  N     . LYS B 1 96  ? -7.18315  23.03927 11.07805  1.000 74.83078  ? 96  LYS B N     1 
ATOM   1722 C  CA    . LYS B 1 96  ? -7.58270  22.06295 10.07874  1.000 75.90514  ? 96  LYS B CA    1 
ATOM   1723 C  C     . LYS B 1 96  ? -6.87571  22.35731 8.76366   1.000 73.35376  ? 96  LYS B C     1 
ATOM   1724 O  O     . LYS B 1 96  ? -6.54586  23.50684 8.45814   1.000 71.91790  ? 96  LYS B O     1 
ATOM   1725 C  CB    . LYS B 1 96  ? -9.10238  22.06357 9.87378   1.000 62.73820  ? 96  LYS B CB    1 
ATOM   1726 N  N     . VAL B 1 97  ? -6.64596  21.30093 7.98878   1.000 76.22769  ? 97  VAL B N     1 
ATOM   1727 C  CA    . VAL B 1 97  ? -5.95301  21.38260 6.71002   1.000 59.30186  ? 97  VAL B CA    1 
ATOM   1728 C  C     . VAL B 1 97  ? -6.92262  20.96985 5.61271   1.000 65.75292  ? 97  VAL B C     1 
ATOM   1729 O  O     . VAL B 1 97  ? -7.60476  19.94593 5.73356   1.000 71.77809  ? 97  VAL B O     1 
ATOM   1730 C  CB    . VAL B 1 97  ? -4.69467  20.49648 6.69167   1.000 71.81206  ? 97  VAL B CB    1 
ATOM   1731 C  CG1   . VAL B 1 97  ? -4.03871  20.52985 5.32370   1.000 57.37555  ? 97  VAL B CG1   1 
ATOM   1732 C  CG2   . VAL B 1 97  ? -3.71739  20.94152 7.77047   1.000 66.54667  ? 97  VAL B CG2   1 
ATOM   1733 N  N     . ILE B 1 98  ? -6.97997  21.76408 4.54777   1.000 73.04974  ? 98  ILE B N     1 
ATOM   1734 C  CA    . ILE B 1 98  ? -7.83980  21.49955 3.40011   1.000 67.87828  ? 98  ILE B CA    1 
ATOM   1735 C  C     . ILE B 1 98  ? -6.97233  20.85122 2.32586   1.000 69.31369  ? 98  ILE B C     1 
ATOM   1736 O  O     . ILE B 1 98  ? -6.29871  21.53698 1.55190   1.000 70.45148  ? 98  ILE B O     1 
ATOM   1737 C  CB    . ILE B 1 98  ? -8.51132  22.77675 2.89021   1.000 66.84938  ? 98  ILE B CB    1 
ATOM   1738 C  CG1   . ILE B 1 98  ? -9.24878  23.48931 4.02641   1.000 64.11352  ? 98  ILE B CG1   1 
ATOM   1739 C  CG2   . ILE B 1 98  ? -9.45859  22.45713 1.74185   1.000 70.27195  ? 98  ILE B CG2   1 
ATOM   1740 C  CD1   . ILE B 1 98  ? -9.89602  24.78632 3.60200   1.000 61.96859  ? 98  ILE B CD1   1 
ATOM   1741 N  N     . LEU B 1 99  ? -6.98253  19.52229 2.27699   1.000 73.41611  ? 99  LEU B N     1 
ATOM   1742 C  CA    . LEU B 1 99  ? -6.27405  18.78626 1.24057   1.000 73.75316  ? 99  LEU B CA    1 
ATOM   1743 C  C     . LEU B 1 99  ? -7.17321  18.58269 0.02867   1.000 83.47006  ? 99  LEU B C     1 
ATOM   1744 O  O     . LEU B 1 99  ? -8.36626  18.29542 0.16319   1.000 79.99601  ? 99  LEU B O     1 
ATOM   1745 C  CB    . LEU B 1 99  ? -5.79274  17.43178 1.76355   1.000 61.60390  ? 99  LEU B CB    1 
ATOM   1746 C  CG    . LEU B 1 99  ? -4.61277  17.44942 2.73639   1.000 68.24489  ? 99  LEU B CG    1 
ATOM   1747 C  CD1   . LEU B 1 99  ? -4.03513  16.05236 2.91750   1.000 75.87083  ? 99  LEU B CD1   1 
ATOM   1748 C  CD2   . LEU B 1 99  ? -3.54458  18.41406 2.25538   1.000 62.57858  ? 99  LEU B CD2   1 
ATOM   1749 N  N     . VAL B 1 100 ? -6.58782  18.72274 -1.15681  1.000 83.09337  ? 100 VAL B N     1 
ATOM   1750 C  CA    . VAL B 1 100 ? -7.30764  18.57318 -2.41549  1.000 77.24123  ? 100 VAL B CA    1 
ATOM   1751 C  C     . VAL B 1 100 ? -6.44506  17.74409 -3.35718  1.000 79.67445  ? 100 VAL B C     1 
ATOM   1752 O  O     . VAL B 1 100 ? -5.21451  17.85659 -3.35074  1.000 74.74877  ? 100 VAL B O     1 
ATOM   1753 C  CB    . VAL B 1 100 ? -7.66430  19.94664 -3.02622  1.000 77.31486  ? 100 VAL B CB    1 
ATOM   1754 C  CG1   . VAL B 1 100 ? -6.40869  20.77303 -3.26616  1.000 78.73091  ? 100 VAL B CG1   1 
ATOM   1755 C  CG2   . VAL B 1 100 ? -8.47028  19.78358 -4.31045  1.000 86.72382  ? 100 VAL B CG2   1 
ATOM   1756 N  N     . ASN B 1 101 ? -7.08966  16.89762 -4.15527  1.000 88.12356  ? 101 ASN B N     1 
ATOM   1757 C  CA    . ASN B 1 101 ? -6.39628  15.94617 -5.02001  1.000 86.63473  ? 101 ASN B CA    1 
ATOM   1758 C  C     . ASN B 1 101 ? -6.43308  16.47005 -6.45229  1.000 93.19868  ? 101 ASN B C     1 
ATOM   1759 O  O     . ASN B 1 101 ? -7.46698  16.40550 -7.12215  1.000 97.86294  ? 101 ASN B O     1 
ATOM   1760 C  CB    . ASN B 1 101 ? -7.03588  14.56567 -4.90932  1.000 86.05165  ? 101 ASN B CB    1 
ATOM   1761 C  CG    . ASN B 1 101 ? -6.26062  13.50078 -5.65528  1.000 95.76621  ? 101 ASN B CG    1 
ATOM   1762 O  OD1   . ASN B 1 101 ? -5.08939  13.68493 -5.98592  1.000 88.08596  ? 101 ASN B OD1   1 
ATOM   1763 N  ND2   . ASN B 1 101 ? -6.91081  12.37386 -5.92049  1.000 99.43341  ? 101 ASN B ND2   1 
ATOM   1764 N  N     . LEU B 1 102 ? -5.29975  16.98843 -6.92204  1.000 87.08162  ? 102 LEU B N     1 
ATOM   1765 C  CA    . LEU B 1 102 ? -5.17506  17.45217 -8.29776  1.000 89.66830  ? 102 LEU B CA    1 
ATOM   1766 C  C     . LEU B 1 102 ? -4.63154  16.38404 -9.23594  1.000 98.26874  ? 102 LEU B C     1 
ATOM   1767 O  O     . LEU B 1 102 ? -4.46754  16.65363 -10.43048 1.000 87.31194  ? 102 LEU B O     1 
ATOM   1768 C  CB    . LEU B 1 102 ? -4.28638  18.69807 -8.36830  1.000 89.41228  ? 102 LEU B CB    1 
ATOM   1769 C  CG    . LEU B 1 102 ? -4.99209  20.03663 -8.13725  1.000 91.75175  ? 102 LEU B CG    1 
ATOM   1770 C  CD1   . LEU B 1 102 ? -6.29376  20.10236 -8.92659  1.000 92.06297  ? 102 LEU B CD1   1 
ATOM   1771 C  CD2   . LEU B 1 102 ? -5.24222  20.27781 -6.66090  1.000 87.01533  ? 102 LEU B CD2   1 
ATOM   1772 N  N     . GLY B 1 103 ? -4.33888  15.18916 -8.72814  1.000 93.38210  ? 103 GLY B N     1 
ATOM   1773 C  CA    . GLY B 1 103 ? -4.00658  14.08059 -9.59261  1.000 93.04229  ? 103 GLY B CA    1 
ATOM   1774 C  C     . GLY B 1 103 ? -5.24609  13.45183 -10.19669 1.000 104.10953 ? 103 GLY B C     1 
ATOM   1775 O  O     . GLY B 1 103 ? -6.37933  13.78214 -9.85117  1.000 105.02699 ? 103 GLY B O     1 
ATOM   1776 N  N     . ASN B 1 104 ? -5.01776  12.52575 -11.12623 1.000 110.01169 ? 104 ASN B N     1 
ATOM   1777 C  CA    . ASN B 1 104 ? -6.09691  11.81384 -11.79632 1.000 116.83120 ? 104 ASN B CA    1 
ATOM   1778 C  C     . ASN B 1 104 ? -6.27898  10.39884 -11.25873 1.000 117.10799 ? 104 ASN B C     1 
ATOM   1779 O  O     . ASN B 1 104 ? -6.87448  9.55488  -11.93687 1.000 106.31318 ? 104 ASN B O     1 
ATOM   1780 C  CB    . ASN B 1 104 ? -5.84694  11.77855 -13.30497 1.000 109.58967 ? 104 ASN B CB    1 
ATOM   1781 C  CG    . ASN B 1 104 ? -4.64040  10.93690 -13.67540 1.000 113.51395 ? 104 ASN B CG    1 
ATOM   1782 O  OD1   . ASN B 1 104 ? -3.72604  10.75356 -12.87158 1.000 114.82679 ? 104 ASN B OD1   1 
ATOM   1783 N  ND2   . ASN B 1 104 ? -4.63306  10.41907 -14.89851 1.000 123.98848 ? 104 ASN B ND2   1 
ATOM   1784 N  N     . GLU B 1 105 ? -5.78731  10.12621 -10.05246 1.000 119.31175 ? 105 GLU B N     1 
ATOM   1785 C  CA    . GLU B 1 105 ? -5.77736  8.77455  -9.51497  1.000 124.69066 ? 105 GLU B CA    1 
ATOM   1786 C  C     . GLU B 1 105 ? -6.03779  8.83114  -8.01537  1.000 122.90020 ? 105 GLU B C     1 
ATOM   1787 O  O     . GLU B 1 105 ? -5.65143  9.79133  -7.34352  1.000 114.65706 ? 105 GLU B O     1 
ATOM   1788 C  CB    . GLU B 1 105 ? -4.44214  8.08561  -9.81960  1.000 129.24823 ? 105 GLU B CB    1 
ATOM   1789 C  CG    . GLU B 1 105 ? -4.33801  6.65549  -9.33872  1.000 139.49653 ? 105 GLU B CG    1 
ATOM   1790 C  CD    . GLU B 1 105 ? -3.13318  6.44292  -8.44930  1.000 153.13459 ? 105 GLU B CD    1 
ATOM   1791 O  OE1   . GLU B 1 105 ? -2.07921  7.05614  -8.72191  1.000 156.62972 ? 105 GLU B OE1   1 
ATOM   1792 O  OE2   . GLU B 1 105 ? -3.24343  5.67454  -7.47113  1.000 152.53642 ? 105 GLU B OE2   1 
ATOM   1793 N  N     . GLU B 1 106 ? -6.68749  7.78509  -7.49974  1.000 118.99694 ? 106 GLU B N     1 
ATOM   1794 C  CA    . GLU B 1 106 ? -7.14837  7.77046  -6.11559  1.000 106.52383 ? 106 GLU B CA    1 
ATOM   1795 C  C     . GLU B 1 106 ? -5.98268  7.88432  -5.13807  1.000 106.71818 ? 106 GLU B C     1 
ATOM   1796 O  O     . GLU B 1 106 ? -4.87043  7.41789  -5.39919  1.000 108.02563 ? 106 GLU B O     1 
ATOM   1797 C  CB    . GLU B 1 106 ? -7.94079  6.49215  -5.83187  1.000 107.20173 ? 106 GLU B CB    1 
ATOM   1798 N  N     . VAL B 1 107 ? -6.25443  8.52083  -3.99739  1.000 93.30030  ? 107 VAL B N     1 
ATOM   1799 C  CA    . VAL B 1 107 ? -5.26870  8.75468  -2.95028  1.000 90.83222  ? 107 VAL B CA    1 
ATOM   1800 C  C     . VAL B 1 107 ? -5.87526  8.35096  -1.61266  1.000 101.71678 ? 107 VAL B C     1 
ATOM   1801 O  O     . VAL B 1 107 ? -7.08680  8.46247  -1.39992  1.000 101.70982 ? 107 VAL B O     1 
ATOM   1802 C  CB    . VAL B 1 107 ? -4.80616  10.23277 -2.91656  1.000 98.78088  ? 107 VAL B CB    1 
ATOM   1803 C  CG1   . VAL B 1 107 ? -3.63324  10.41726 -1.96156  1.000 91.38282  ? 107 VAL B CG1   1 
ATOM   1804 C  CG2   . VAL B 1 107 ? -4.43797  10.71751 -4.31166  1.000 85.04966  ? 107 VAL B CG2   1 
ATOM   1805 N  N     . VAL B 1 108 ? -5.02273  7.87332  -0.70697  1.000 92.04094  ? 108 VAL B N     1 
ATOM   1806 C  CA    . VAL B 1 108 ? -5.42971  7.47599  0.63603   1.000 91.86252  ? 108 VAL B CA    1 
ATOM   1807 C  C     . VAL B 1 108 ? -4.49898  8.13799  1.64356   1.000 100.35765 ? 108 VAL B C     1 
ATOM   1808 O  O     . VAL B 1 108 ? -3.27349  8.08660  1.48983   1.000 98.20695  ? 108 VAL B O     1 
ATOM   1809 C  CB    . VAL B 1 108 ? -5.41719  5.94430  0.80994   1.000 95.45166  ? 108 VAL B CB    1 
ATOM   1810 C  CG1   . VAL B 1 108 ? -5.48556  5.57069  2.28359   1.000 90.75095  ? 108 VAL B CG1   1 
ATOM   1811 C  CG2   . VAL B 1 108 ? -6.57615  5.31588  0.05063   1.000 91.99450  ? 108 VAL B CG2   1 
ATOM   1812 N  N     . ILE B 1 109 ? -5.08049  8.76123  2.66697   1.000 98.96296  ? 109 ILE B N     1 
ATOM   1813 C  CA    . ILE B 1 109 ? -4.33519  9.37151  3.76378   1.000 98.05358  ? 109 ILE B CA    1 
ATOM   1814 C  C     . ILE B 1 109 ? -4.57083  8.53393  5.01351   1.000 102.68191 ? 109 ILE B C     1 
ATOM   1815 O  O     . ILE B 1 109 ? -5.71902  8.33410  5.43029   1.000 97.72332  ? 109 ILE B O     1 
ATOM   1816 C  CB    . ILE B 1 109 ? -4.74649  10.83509 3.98845   1.000 90.58577  ? 109 ILE B CB    1 
ATOM   1817 C  CG1   . ILE B 1 109 ? -4.14299  11.72902 2.90404   1.000 91.03093  ? 109 ILE B CG1   1 
ATOM   1818 C  CG2   . ILE B 1 109 ? -4.31617  11.30932 5.36775   1.000 76.39676  ? 109 ILE B CG2   1 
ATOM   1819 C  CD1   . ILE B 1 109 ? -2.62962  11.71237 2.87738   1.000 89.58221  ? 109 ILE B CD1   1 
ATOM   1820 N  N     . GLU B 1 110 ? -3.48718  8.04711  5.60952   1.000 111.34839 ? 110 GLU B N     1 
ATOM   1821 C  CA    . GLU B 1 110 ? -3.56584  7.16952  6.76577   1.000 104.74983 ? 110 GLU B CA    1 
ATOM   1822 C  C     . GLU B 1 110 ? -3.63779  7.97816  8.05892   1.000 107.39901 ? 110 GLU B C     1 
ATOM   1823 O  O     . GLU B 1 110 ? -3.48283  9.20104  8.07235   1.000 114.15104 ? 110 GLU B O     1 
ATOM   1824 C  CB    . GLU B 1 110 ? -2.36570  6.22432  6.79736   1.000 111.58885 ? 110 GLU B CB    1 
ATOM   1825 C  CG    . GLU B 1 110 ? -2.09301  5.53312  5.47281   1.000 125.98538 ? 110 GLU B CG    1 
ATOM   1826 C  CD    . GLU B 1 110 ? -0.93215  4.56266  5.54949   1.000 149.82927 ? 110 GLU B CD    1 
ATOM   1827 O  OE1   . GLU B 1 110 ? -0.53436  4.19835  6.67592   1.000 161.42311 ? 110 GLU B OE1   1 
ATOM   1828 O  OE2   . GLU B 1 110 ? -0.41644  4.16531  4.48345   1.000 152.33429 ? 110 GLU B OE2   1 
ATOM   1829 N  N     . ARG B 1 111 ? -3.87564  7.27029  9.16097   1.000 95.27727  ? 111 ARG B N     1 
ATOM   1830 C  CA    . ARG B 1 111 ? -3.94164  7.91224  10.46674  1.000 99.77085  ? 111 ARG B CA    1 
ATOM   1831 C  C     . ARG B 1 111 ? -2.55070  8.35347  10.90444  1.000 99.24283  ? 111 ARG B C     1 
ATOM   1832 O  O     . ARG B 1 111 ? -1.59246  7.57736  10.84135  1.000 96.97640  ? 111 ARG B O     1 
ATOM   1833 C  CB    . ARG B 1 111 ? -4.54585  6.95915  11.49730  1.000 103.63245 ? 111 ARG B CB    1 
ATOM   1834 N  N     . GLY B 1 112 ? -2.44117  9.60449  11.34518  1.000 91.99530  ? 112 GLY B N     1 
ATOM   1835 C  CA    . GLY B 1 112 ? -1.16337  10.12979 11.78072  1.000 91.86353  ? 112 GLY B CA    1 
ATOM   1836 C  C     . GLY B 1 112 ? -0.15269  10.35198 10.68011  1.000 93.57878  ? 112 GLY B C     1 
ATOM   1837 O  O     . GLY B 1 112 ? 1.04846   10.38267 10.95523  1.000 87.93514  ? 112 GLY B O     1 
ATOM   1838 N  N     . GLU B 1 113 ? -0.59864  10.50393 9.43647   1.000 92.49961  ? 113 GLU B N     1 
ATOM   1839 C  CA    . GLU B 1 113 ? 0.30781   10.75990 8.32722   1.000 90.74296  ? 113 GLU B CA    1 
ATOM   1840 C  C     . GLU B 1 113 ? 0.57156   12.25516 8.20544   1.000 80.90089  ? 113 GLU B C     1 
ATOM   1841 O  O     . GLU B 1 113 ? -0.33822  13.07456 8.36090   1.000 79.02641  ? 113 GLU B O     1 
ATOM   1842 C  CB    . GLU B 1 113 ? -0.26642  10.21238 7.01851   1.000 91.37270  ? 113 GLU B CB    1 
ATOM   1843 C  CG    . GLU B 1 113 ? 0.64048   10.40657 5.80846   1.000 95.87504  ? 113 GLU B CG    1 
ATOM   1844 C  CD    . GLU B 1 113 ? 0.08902   9.76131  4.55334   1.000 96.43127  ? 113 GLU B CD    1 
ATOM   1845 O  OE1   . GLU B 1 113 ? -0.73508  8.83008  4.67672   1.000 96.52284  ? 113 GLU B OE1   1 
ATOM   1846 O  OE2   . GLU B 1 113 ? 0.47931   10.18784 3.44531   1.000 87.92680  ? 113 GLU B OE2   1 
ATOM   1847 N  N     . ARG B 1 114 ? 1.82756   12.60499 7.93849   1.000 86.84979  ? 114 ARG B N     1 
ATOM   1848 C  CA    . ARG B 1 114 ? 2.22122   14.00464 7.81243   1.000 82.03900  ? 114 ARG B CA    1 
ATOM   1849 C  C     . ARG B 1 114 ? 1.67711   14.56443 6.50308   1.000 74.94636  ? 114 ARG B C     1 
ATOM   1850 O  O     . ARG B 1 114 ? 2.11924   14.17317 5.41815   1.000 88.19029  ? 114 ARG B O     1 
ATOM   1851 C  CB    . ARG B 1 114 ? 3.73974   14.12635 7.89154   1.000 82.38562  ? 114 ARG B CB    1 
ATOM   1852 C  CG    . ARG B 1 114 ? 4.31786   13.48519 9.14745   1.000 86.45763  ? 114 ARG B CG    1 
ATOM   1853 C  CD    . ARG B 1 114 ? 5.78159   13.83365 9.35753   1.000 94.91707  ? 114 ARG B CD    1 
ATOM   1854 N  NE    . ARG B 1 114 ? 6.64823   13.24493 8.34377   1.000 92.71165  ? 114 ARG B NE    1 
ATOM   1855 C  CZ    . ARG B 1 114 ? 7.26893   12.08044 8.47317   1.000 102.83401 ? 114 ARG B CZ    1 
ATOM   1856 N  NH1   . ARG B 1 114 ? 7.13047   11.34031 9.56125   1.000 101.27655 ? 114 ARG B NH1   1 
ATOM   1857 N  NH2   . ARG B 1 114 ? 8.05006   11.64866 7.48702   1.000 100.50457 ? 114 ARG B NH2   1 
ATOM   1858 N  N     . ILE B 1 115 ? 0.71498   15.48161 6.60422   1.000 71.79839  ? 115 ILE B N     1 
ATOM   1859 C  CA    . ILE B 1 115 ? -0.03337  15.96165 5.44572   1.000 74.42118  ? 115 ILE B CA    1 
ATOM   1860 C  C     . ILE B 1 115 ? 0.29834   17.39587 5.06897   1.000 66.09468  ? 115 ILE B C     1 
ATOM   1861 O  O     . ILE B 1 115 ? -0.08704  17.83246 3.97151   1.000 73.77830  ? 115 ILE B O     1 
ATOM   1862 C  CB    . ILE B 1 115 ? -1.55477  15.82565 5.66485   1.000 76.56211  ? 115 ILE B CB    1 
ATOM   1863 C  CG1   . ILE B 1 115 ? -1.97670  16.60101 6.91582   1.000 77.39951  ? 115 ILE B CG1   1 
ATOM   1864 C  CG2   . ILE B 1 115 ? -1.95157  14.35982 5.76699   1.000 81.72274  ? 115 ILE B CG2   1 
ATOM   1865 C  CD1   . ILE B 1 115 ? -3.47108  16.71771 7.09218   1.000 74.91233  ? 115 ILE B CD1   1 
ATOM   1866 N  N     . ALA B 1 116 ? 0.98005   18.14290 5.92823   1.000 64.57082  ? 116 ALA B N     1 
ATOM   1867 C  CA    . ALA B 1 116 ? 1.30749   19.53920 5.66023   1.000 63.87156  ? 116 ALA B CA    1 
ATOM   1868 C  C     . ALA B 1 116 ? 2.39571   19.95817 6.63961   1.000 71.75788  ? 116 ALA B C     1 
ATOM   1869 O  O     . ALA B 1 116 ? 2.89505   19.14804 7.42665   1.000 73.40192  ? 116 ALA B O     1 
ATOM   1870 C  CB    . ALA B 1 116 ? 0.07460   20.43766 5.77463   1.000 67.02610  ? 116 ALA B CB    1 
ATOM   1871 N  N     . GLN B 1 117 ? 2.76164   21.23677 6.58599   1.000 67.17425  ? 117 GLN B N     1 
ATOM   1872 C  CA    . GLN B 1 117 ? 3.74349   21.78975 7.50795   1.000 71.48362  ? 117 GLN B CA    1 
ATOM   1873 C  C     . GLN B 1 117 ? 3.32899   23.19601 7.90811   1.000 65.05222  ? 117 GLN B C     1 
ATOM   1874 O  O     . GLN B 1 117 ? 3.00726   24.02202 7.04932   1.000 64.46558  ? 117 GLN B O     1 
ATOM   1875 C  CB    . GLN B 1 117 ? 5.15314   21.79936 6.89838   1.000 76.52811  ? 117 GLN B CB    1 
ATOM   1876 C  CG    . GLN B 1 117 ? 5.24990   22.37576 5.49484   1.000 76.48947  ? 117 GLN B CG    1 
ATOM   1877 C  CD    . GLN B 1 117 ? 6.67710   22.39278 4.97282   1.000 84.86327  ? 117 GLN B CD    1 
ATOM   1878 O  OE1   . GLN B 1 117 ? 7.62836   22.56912 5.73557   1.000 82.32812  ? 117 GLN B OE1   1 
ATOM   1879 N  NE2   . GLN B 1 117 ? 6.83211   22.20274 3.66733   1.000 86.21459  ? 117 GLN B NE2   1 
ATOM   1880 N  N     . LEU B 1 118 ? 3.32940   23.45578 9.21223   1.000 62.23406  ? 118 LEU B N     1 
ATOM   1881 C  CA    . LEU B 1 118 ? 3.01421   24.77185 9.74781   1.000 62.49413  ? 118 LEU B CA    1 
ATOM   1882 C  C     . LEU B 1 118 ? 4.30096   25.56378 9.92947   1.000 68.09571  ? 118 LEU B C     1 
ATOM   1883 O  O     . LEU B 1 118 ? 5.22606   25.10616 10.60699  1.000 65.25480  ? 118 LEU B O     1 
ATOM   1884 C  CB    . LEU B 1 118 ? 2.28040   24.64931 11.08208  1.000 63.32389  ? 118 LEU B CB    1 
ATOM   1885 C  CG    . LEU B 1 118 ? 2.03822   25.94818 11.84947  1.000 64.36119  ? 118 LEU B CG    1 
ATOM   1886 C  CD1   . LEU B 1 118 ? 0.84410   26.70024 11.28200  1.000 63.82808  ? 118 LEU B CD1   1 
ATOM   1887 C  CD2   . LEU B 1 118 ? 1.85043   25.65383 13.32613  1.000 62.00209  ? 118 LEU B CD2   1 
ATOM   1888 N  N     . VAL B 1 119 ? 4.35731   26.74740 9.32617   1.000 64.81470  ? 119 VAL B N     1 
ATOM   1889 C  CA    . VAL B 1 119 ? 5.53431   27.60699 9.37299   1.000 66.00300  ? 119 VAL B CA    1 
ATOM   1890 C  C     . VAL B 1 119 ? 5.18612   28.86080 10.16204  1.000 68.00654  ? 119 VAL B C     1 
ATOM   1891 O  O     . VAL B 1 119 ? 4.17733   29.51865 9.88043   1.000 72.83428  ? 119 VAL B O     1 
ATOM   1892 C  CB    . VAL B 1 119 ? 6.02736   27.96102 7.95927   1.000 63.91294  ? 119 VAL B CB    1 
ATOM   1893 C  CG1   . VAL B 1 119 ? 7.18088   28.94351 8.03012   1.000 63.60960  ? 119 VAL B CG1   1 
ATOM   1894 C  CG2   . VAL B 1 119 ? 6.44149   26.70153 7.21523   1.000 61.08301  ? 119 VAL B CG2   1 
ATOM   1895 N  N     . ILE B 1 120 ? 6.01567   29.18790 11.14902  1.000 68.40847  ? 120 ILE B N     1 
ATOM   1896 C  CA    . ILE B 1 120 ? 5.83572   30.37888 11.97122  1.000 73.85255  ? 120 ILE B CA    1 
ATOM   1897 C  C     . ILE B 1 120 ? 6.74328   31.47315 11.42761  1.000 75.36153  ? 120 ILE B C     1 
ATOM   1898 O  O     . ILE B 1 120 ? 7.96373   31.29316 11.33721  1.000 76.62732  ? 120 ILE B O     1 
ATOM   1899 C  CB    . ILE B 1 120 ? 6.13523   30.09456 13.45047  1.000 70.84329  ? 120 ILE B CB    1 
ATOM   1900 C  CG1   . ILE B 1 120 ? 5.27384   28.93504 13.95428  1.000 63.26751  ? 120 ILE B CG1   1 
ATOM   1901 C  CG2   . ILE B 1 120 ? 5.88821   31.33911 14.28464  1.000 72.17655  ? 120 ILE B CG2   1 
ATOM   1902 C  CD1   . ILE B 1 120 ? 3.78753   29.20173 13.87203  1.000 63.21999  ? 120 ILE B CD1   1 
ATOM   1903 N  N     . ALA B 1 121 ? 6.15185   32.60817 11.06991  1.000 76.82960  ? 121 ALA B N     1 
ATOM   1904 C  CA    . ALA B 1 121 ? 6.86570   33.70917 10.44017  1.000 78.92224  ? 121 ALA B CA    1 
ATOM   1905 C  C     . ALA B 1 121 ? 6.39936   35.03081 11.03097  1.000 78.64972  ? 121 ALA B C     1 
ATOM   1906 O  O     . ALA B 1 121 ? 5.27410   35.12670 11.53846  1.000 84.30703  ? 121 ALA B O     1 
ATOM   1907 C  CB    . ALA B 1 121 ? 6.64678   33.72340 8.91797   1.000 75.98114  ? 121 ALA B CB    1 
ATOM   1908 N  N     . PRO B 1 122 ? 7.24358   36.06191 10.99062  1.000 83.67848  ? 122 PRO B N     1 
ATOM   1909 C  CA    . PRO B 1 122 ? 6.82307   37.37922 11.48019  1.000 94.07928  ? 122 PRO B CA    1 
ATOM   1910 C  C     . PRO B 1 122 ? 5.86713   38.05805 10.51265  1.000 93.09986  ? 122 PRO B C     1 
ATOM   1911 O  O     . PRO B 1 122 ? 5.99878   37.94719 9.29137   1.000 95.30117  ? 122 PRO B O     1 
ATOM   1912 C  CB    . PRO B 1 122 ? 8.14200   38.15926 11.58948  1.000 89.71120  ? 122 PRO B CB    1 
ATOM   1913 C  CG    . PRO B 1 122 ? 9.23114   37.12479 11.49957  1.000 86.92174  ? 122 PRO B CG    1 
ATOM   1914 C  CD    . PRO B 1 122 ? 8.67321   36.03820 10.64474  1.000 82.73337  ? 122 PRO B CD    1 
ATOM   1915 N  N     . VAL B 1 123 ? 4.89556   38.77195 11.07509  1.000 114.48063 ? 123 VAL B N     1 
ATOM   1916 C  CA    . VAL B 1 123 ? 3.94371   39.55425 10.29644  1.000 115.28986 ? 123 VAL B CA    1 
ATOM   1917 C  C     . VAL B 1 123 ? 4.21202   41.03016 10.53604  1.000 115.48059 ? 123 VAL B C     1 
ATOM   1918 O  O     . VAL B 1 123 ? 4.68936   41.43468 11.60263  1.000 116.35472 ? 123 VAL B O     1 
ATOM   1919 C  CB    . VAL B 1 123 ? 2.47921   39.21435 10.64247  1.000 116.91620 ? 123 VAL B CB    1 
ATOM   1920 C  CG1   . VAL B 1 123 ? 2.08744   37.89175 10.03061  1.000 112.37732 ? 123 VAL B CG1   1 
ATOM   1921 C  CG2   . VAL B 1 123 ? 2.27800   39.19380 12.14908  1.000 112.79987 ? 123 VAL B CG2   1 
ATOM   1922 N  N     . GLN B 1 124 ? 3.89618   41.83927 9.53073   1.000 106.34793 ? 124 GLN B N     1 
ATOM   1923 C  CA    . GLN B 1 124 ? 4.00116   43.28950 9.62603   1.000 105.54462 ? 124 GLN B CA    1 
ATOM   1924 C  C     . GLN B 1 124 ? 2.60678   43.87789 9.46772   1.000 101.25267 ? 124 GLN B C     1 
ATOM   1925 O  O     . GLN B 1 124 ? 2.05591   43.89527 8.36146   1.000 97.60633  ? 124 GLN B O     1 
ATOM   1926 C  CB    . GLN B 1 124 ? 4.95556   43.85108 8.57515   1.000 101.06278 ? 124 GLN B CB    1 
ATOM   1927 C  CG    . GLN B 1 124 ? 5.14811   45.35138 8.69035   1.000 106.01922 ? 124 GLN B CG    1 
ATOM   1928 C  CD    . GLN B 1 124 ? 5.53168   45.77571 10.09559  1.000 111.56698 ? 124 GLN B CD    1 
ATOM   1929 O  OE1   . GLN B 1 124 ? 4.67342   46.11493 10.91155  1.000 104.55436 ? 124 GLN B OE1   1 
ATOM   1930 N  NE2   . GLN B 1 124 ? 6.82703   45.75424 10.38695  1.000 113.06458 ? 124 GLN B NE2   1 
ATOM   1931 N  N     . ARG B 1 125 ? 2.03685   44.34943 10.57161  1.000 98.49582  ? 125 ARG B N     1 
ATOM   1932 C  CA    . ARG B 1 125 ? 0.72952   44.98952 10.55639  1.000 102.18305 ? 125 ARG B CA    1 
ATOM   1933 C  C     . ARG B 1 125 ? 0.91761   46.46731 10.23689  1.000 108.94405 ? 125 ARG B C     1 
ATOM   1934 O  O     . ARG B 1 125 ? 1.59160   47.18755 10.98147  1.000 112.26032 ? 125 ARG B O     1 
ATOM   1935 C  CB    . ARG B 1 125 ? 0.02148   44.79792 11.89630  1.000 96.36213  ? 125 ARG B CB    1 
ATOM   1936 C  CG    . ARG B 1 125 ? -1.43253  45.22511 11.89694  1.000 92.48085  ? 125 ARG B CG    1 
ATOM   1937 C  CD    . ARG B 1 125 ? -2.20761  44.52533 12.99955  1.000 94.84556  ? 125 ARG B CD    1 
ATOM   1938 N  NE    . ARG B 1 125 ? -3.62161  44.87857 12.97905  1.000 98.18954  ? 125 ARG B NE    1 
ATOM   1939 C  CZ    . ARG B 1 125 ? -4.14819  45.89656 13.64586  1.000 106.08464 ? 125 ARG B CZ    1 
ATOM   1940 N  NH1   . ARG B 1 125 ? -3.40340  46.68756 14.40075  1.000 96.91494  ? 125 ARG B NH1   1 
ATOM   1941 N  NH2   . ARG B 1 125 ? -5.45497  46.12659 13.55344  1.000 103.76555 ? 125 ARG B NH2   1 
ATOM   1942 N  N     . VAL B 1 126 ? 0.33067   46.91282 9.13099   1.000 104.16029 ? 126 VAL B N     1 
ATOM   1943 C  CA    . VAL B 1 126 ? 0.56220   48.25233 8.60662   1.000 102.76311 ? 126 VAL B CA    1 
ATOM   1944 C  C     . VAL B 1 126 ? -0.60947  49.15241 8.95901   1.000 105.95293 ? 126 VAL B C     1 
ATOM   1945 O  O     . VAL B 1 126 ? -1.74208  48.69679 9.15637   1.000 107.29291 ? 126 VAL B O     1 
ATOM   1946 C  CB    . VAL B 1 126 ? 0.78615   48.22295 7.08082   1.000 108.16071 ? 126 VAL B CB    1 
ATOM   1947 C  CG1   . VAL B 1 126 ? 2.08998   47.52421 6.75258   1.000 109.80375 ? 126 VAL B CG1   1 
ATOM   1948 C  CG2   . VAL B 1 126 ? -0.38308  47.53615 6.39233   1.000 99.38237  ? 126 VAL B CG2   1 
ATOM   1949 N  N     . GLU B 1 127 ? -0.32978  50.44964 9.04099   1.000 111.04638 ? 127 GLU B N     1 
ATOM   1950 C  CA    . GLU B 1 127 ? -1.36953  51.45973 9.16013   1.000 107.70052 ? 127 GLU B CA    1 
ATOM   1951 C  C     . GLU B 1 127 ? -1.84493  51.83508 7.76340   1.000 107.15256 ? 127 GLU B C     1 
ATOM   1952 O  O     . GLU B 1 127 ? -1.02960  52.09775 6.87305   1.000 103.05810 ? 127 GLU B O     1 
ATOM   1953 C  CB    . GLU B 1 127 ? -0.85254  52.69233 9.90274   1.000 107.40652 ? 127 GLU B CB    1 
ATOM   1954 N  N     . VAL B 1 128 ? -3.15991  51.84930 7.57317   1.000 100.90841 ? 128 VAL B N     1 
ATOM   1955 C  CA    . VAL B 1 128 ? -3.76455  52.06598 6.26463   1.000 109.92791 ? 128 VAL B CA    1 
ATOM   1956 C  C     . VAL B 1 128 ? -4.16302  53.52880 6.13982   1.000 110.29999 ? 128 VAL B C     1 
ATOM   1957 O  O     . VAL B 1 128 ? -4.87872  54.06233 6.99730   1.000 114.87995 ? 128 VAL B O     1 
ATOM   1958 C  CB    . VAL B 1 128 ? -4.97688  51.14417 6.05421   1.000 105.37234 ? 128 VAL B CB    1 
ATOM   1959 C  CG1   . VAL B 1 128 ? -5.60887  51.40932 4.69702   1.000 96.34417  ? 128 VAL B CG1   1 
ATOM   1960 C  CG2   . VAL B 1 128 ? -4.55545  49.68898 6.18110   1.000 93.63543  ? 128 VAL B CG2   1 
ATOM   1961 N  N     . VAL B 1 129 ? -3.69847  54.17755 5.07488   1.000 100.44925 ? 129 VAL B N     1 
ATOM   1962 C  CA    . VAL B 1 129 ? -4.03085  55.56806 4.78896   1.000 119.27964 ? 129 VAL B CA    1 
ATOM   1963 C  C     . VAL B 1 129 ? -4.35897  55.68936 3.30798   1.000 115.08978 ? 129 VAL B C     1 
ATOM   1964 O  O     . VAL B 1 129 ? -3.68161  55.09582 2.46193   1.000 116.02227 ? 129 VAL B O     1 
ATOM   1965 C  CB    . VAL B 1 129 ? -2.88275  56.52391 5.17545   1.000 109.97063 ? 129 VAL B CB    1 
ATOM   1966 N  N     . GLU B 1 130 ? -5.40049  56.45870 2.99481   1.000 125.78968 ? 130 GLU B N     1 
ATOM   1967 C  CA    . GLU B 1 130 ? -5.81671  56.66823 1.61521   1.000 126.89249 ? 130 GLU B CA    1 
ATOM   1968 C  C     . GLU B 1 130 ? -5.11711  57.89338 1.04274   1.000 133.81072 ? 130 GLU B C     1 
ATOM   1969 O  O     . GLU B 1 130 ? -5.15626  58.97321 1.64058   1.000 139.08496 ? 130 GLU B O     1 
ATOM   1970 C  CB    . GLU B 1 130 ? -7.33489  56.83484 1.52199   1.000 130.38887 ? 130 GLU B CB    1 
ATOM   1971 C  CG    . GLU B 1 130 ? -7.84596  56.98707 0.09593   1.000 134.16508 ? 130 GLU B CG    1 
ATOM   1972 C  CD    . GLU B 1 130 ? -9.33772  56.74093 -0.02318  1.000 138.06370 ? 130 GLU B CD    1 
ATOM   1973 O  OE1   . GLU B 1 130 ? -9.98799  56.50308 1.01608   1.000 135.33278 ? 130 GLU B OE1   1 
ATOM   1974 O  OE2   . GLU B 1 130 ? -9.85773  56.78051 -1.15826  1.000 145.33732 ? 130 GLU B OE2   1 
ATOM   1975 N  N     . VAL B 1 131 ? -4.48405  57.72284 -0.11707  1.000 127.21312 ? 131 VAL B N     1 
ATOM   1976 C  CA    . VAL B 1 131 ? -3.75090  58.79142 -0.78049  1.000 123.15859 ? 131 VAL B CA    1 
ATOM   1977 C  C     . VAL B 1 131 ? -4.37487  59.03495 -2.15189  1.000 130.67444 ? 131 VAL B C     1 
ATOM   1978 O  O     . VAL B 1 131 ? -5.23935  58.28714 -2.60969  1.000 128.60169 ? 131 VAL B O     1 
ATOM   1979 C  CB    . VAL B 1 131 ? -2.24729  58.47512 -0.90859  1.000 119.50267 ? 131 VAL B CB    1 
ATOM   1980 C  CG1   . VAL B 1 131 ? -1.63166  58.24742 0.46430   1.000 118.51826 ? 131 VAL B CG1   1 
ATOM   1981 C  CG2   . VAL B 1 131 ? -2.02871  57.25981 -1.80404  1.000 119.46606 ? 131 VAL B CG2   1 
ATOM   1982 N  N     . GLU B 1 132 ? -3.92030  60.09929 -2.80486  1.000 128.91142 ? 132 GLU B N     1 
ATOM   1983 C  CA    . GLU B 1 132 ? -4.38873  60.43397 -4.14549  1.000 133.25496 ? 132 GLU B CA    1 
ATOM   1984 C  C     . GLU B 1 132 ? -3.21457  60.60329 -5.10503  1.000 130.46751 ? 132 GLU B C     1 
ATOM   1985 O  O     . GLU B 1 132 ? -2.05595  60.45641 -4.71427  1.000 127.12662 ? 132 GLU B O     1 
ATOM   1986 C  CB    . GLU B 1 132 ? -5.23802  61.70798 -4.12200  1.000 138.19167 ? 132 GLU B CB    1 
ATOM   1987 C  CG    . GLU B 1 132 ? -6.73428  61.46904 -4.27244  1.000 141.40350 ? 132 GLU B CG    1 
ATOM   1988 C  CD    . GLU B 1 132 ? -7.46306  61.41487 -2.94325  1.000 149.89202 ? 132 GLU B CD    1 
ATOM   1989 O  OE1   . GLU B 1 132 ? -6.79923  61.52330 -1.89121  1.000 149.40909 ? 132 GLU B OE1   1 
ATOM   1990 O  OE2   . GLU B 1 132 ? -8.70385  61.27029 -2.95267  1.000 146.75942 ? 132 GLU B OE2   1 
ATOM   1991 N  N     . VAL B 1 134 ? 0.44674   57.93133 -6.12351  1.000 150.92973 ? 134 VAL B N     1 
ATOM   1992 C  CA    . VAL B 1 134 ? 1.55871   57.27596 -5.44193  1.000 140.67170 ? 134 VAL B CA    1 
ATOM   1993 C  C     . VAL B 1 134 ? 2.88008   57.63791 -6.11357  1.000 145.46211 ? 134 VAL B C     1 
ATOM   1994 O  O     . VAL B 1 134 ? 2.89720   58.31228 -7.14342  1.000 141.73940 ? 134 VAL B O     1 
ATOM   1995 C  CB    . VAL B 1 134 ? 1.36843   55.74773 -5.40082  1.000 125.77916 ? 134 VAL B CB    1 
ATOM   1996 N  N     . SER B 1 135 ? 3.98363   57.18031 -5.52543  1.000 150.07177 ? 135 SER B N     1 
ATOM   1997 C  CA    . SER B 1 135 ? 5.30589   57.51945 -6.03240  1.000 152.14553 ? 135 SER B CA    1 
ATOM   1998 C  C     . SER B 1 135 ? 5.54314   56.88449 -7.39816  1.000 141.73417 ? 135 SER B C     1 
ATOM   1999 O  O     . SER B 1 135 ? 5.07424   55.78056 -7.68486  1.000 136.38488 ? 135 SER B O     1 
ATOM   2000 C  CB    . SER B 1 135 ? 6.38715   57.06229 -5.05155  1.000 145.15566 ? 135 SER B CB    1 
ATOM   2001 O  OG    . SER B 1 135 ? 6.21600   57.66928 -3.78256  1.000 142.74538 ? 135 SER B OG    1 
ATOM   2002 N  N     . GLN B 1 136 ? 6.27441   57.60278 -8.24797  1.000 135.32278 ? 136 GLN B N     1 
ATOM   2003 C  CA    . GLN B 1 136 ? 6.64836   57.08973 -9.55950  1.000 126.42953 ? 136 GLN B CA    1 
ATOM   2004 C  C     . GLN B 1 136 ? 7.86350   56.17627 -9.44101  1.000 115.07240 ? 136 GLN B C     1 
ATOM   2005 O  O     . GLN B 1 136 ? 8.82750   56.49201 -8.73828  1.000 114.34498 ? 136 GLN B O     1 
ATOM   2006 C  CB    . GLN B 1 136 ? 6.94084   58.24923 -10.51340 1.000 125.69066 ? 136 GLN B CB    1 
ATOM   2007 C  CG    . GLN B 1 136 ? 7.98627   57.95021 -11.57193 1.000 121.90239 ? 136 GLN B CG    1 
ATOM   2008 C  CD    . GLN B 1 136 ? 7.39063   57.63233 -12.92592 1.000 120.67387 ? 136 GLN B CD    1 
ATOM   2009 O  OE1   . GLN B 1 136 ? 6.88110   58.51542 -13.61639 1.000 106.35299 ? 136 GLN B OE1   1 
ATOM   2010 N  NE2   . GLN B 1 136 ? 7.46252   56.36705 -13.31991 1.000 119.06681 ? 136 GLN B NE2   1 
ATOM   2011 N  N     . THR B 1 137 ? 7.81304   55.03559 -10.12767 1.000 114.22934 ? 137 THR B N     1 
ATOM   2012 C  CA    . THR B 1 137 ? 8.87072   54.03678 -10.05518 1.000 121.07224 ? 137 THR B CA    1 
ATOM   2013 C  C     . THR B 1 137 ? 9.26203   53.58979 -11.45741 1.000 125.31542 ? 137 THR B C     1 
ATOM   2014 O  O     . THR B 1 137 ? 8.62302   53.94465 -12.45117 1.000 121.21633 ? 137 THR B O     1 
ATOM   2015 C  CB    . THR B 1 137 ? 8.44218   52.82029 -9.22508  1.000 125.95931 ? 137 THR B CB    1 
ATOM   2016 O  OG1   . THR B 1 137 ? 9.56405   51.94786 -9.04312  1.000 130.10856 ? 137 THR B OG1   1 
ATOM   2017 C  CG2   . THR B 1 137 ? 7.33917   52.06355 -9.94015  1.000 123.96617 ? 137 THR B CG2   1 
ATOM   2018 N  N     . GLN B 1 138 ? 10.33166  52.79293 -11.52719 1.000 141.51795 ? 138 GLN B N     1 
ATOM   2019 C  CA    . GLN B 1 138 ? 10.79593  52.28090 -12.81152 1.000 141.88599 ? 138 GLN B CA    1 
ATOM   2020 C  C     . GLN B 1 138 ? 9.95183   51.11106 -13.29757 1.000 147.79111 ? 138 GLN B C     1 
ATOM   2021 O  O     . GLN B 1 138 ? 9.80493   50.92166 -14.51050 1.000 142.00685 ? 138 GLN B O     1 
ATOM   2022 C  CB    . GLN B 1 138 ? 12.26388  51.86040 -12.71558 1.000 135.32799 ? 138 GLN B CB    1 
ATOM   2023 N  N     . ARG B 1 139 ? 9.39546   50.32085 -12.37485 1.000 135.73870 ? 139 ARG B N     1 
ATOM   2024 C  CA    . ARG B 1 139 ? 8.55468   49.19643 -12.77143 1.000 129.31534 ? 139 ARG B CA    1 
ATOM   2025 C  C     . ARG B 1 139 ? 7.25236   49.66667 -13.40514 1.000 134.94433 ? 139 ARG B C     1 
ATOM   2026 O  O     . ARG B 1 139 ? 6.71500   48.98877 -14.28825 1.000 130.24948 ? 139 ARG B O     1 
ATOM   2027 C  CB    . ARG B 1 139 ? 8.26824   48.30158 -11.56481 1.000 120.86096 ? 139 ARG B CB    1 
ATOM   2028 N  N     . GLY B 1 140 ? 6.73793   50.81482 -12.97735 1.000 145.11084 ? 140 GLY B N     1 
ATOM   2029 C  CA    . GLY B 1 140 ? 5.52566   51.34395 -13.58196 1.000 139.87193 ? 140 GLY B CA    1 
ATOM   2030 C  C     . GLY B 1 140 ? 4.31378   50.53061 -13.17613 1.000 131.69042 ? 140 GLY B C     1 
ATOM   2031 O  O     . GLY B 1 140 ? 4.13119   50.18470 -12.00329 1.000 119.21063 ? 140 GLY B O     1 
ATOM   2032 N  N     . GLU B 1 141 ? 3.47194   50.21837 -14.15532 1.000 127.56788 ? 141 GLU B N     1 
ATOM   2033 C  CA    . GLU B 1 141 ? 2.26258   49.44407 -13.91059 1.000 124.94026 ? 141 GLU B CA    1 
ATOM   2034 C  C     . GLU B 1 141 ? 2.44983   47.99050 -14.33219 1.000 116.95574 ? 141 GLU B C     1 
ATOM   2035 O  O     . GLU B 1 141 ? 1.61104   47.13739 -14.04295 1.000 111.19706 ? 141 GLU B O     1 
ATOM   2036 C  CB    . GLU B 1 141 ? 1.07461   50.06048 -14.65160 1.000 113.42915 ? 141 GLU B CB    1 
ATOM   2037 N  N     . LYS C 1 3   ? 23.00547  43.73483 4.71932   1.000 122.32434 ? 3   LYS C N     1 
ATOM   2038 C  CA    . LYS C 1 3   ? 23.42213  43.06984 3.49018   1.000 128.05429 ? 3   LYS C CA    1 
ATOM   2039 C  C     . LYS C 1 3   ? 23.54425  41.56182 3.69413   1.000 128.46209 ? 3   LYS C C     1 
ATOM   2040 O  O     . LYS C 1 3   ? 24.25801  41.10177 4.58449   1.000 125.84374 ? 3   LYS C O     1 
ATOM   2041 C  CB    . LYS C 1 3   ? 24.75001  43.64297 2.99103   1.000 122.17950 ? 3   LYS C CB    1 
ATOM   2042 N  N     . VAL C 1 4   ? 22.83706  40.79976 2.86276   1.000 123.51228 ? 4   VAL C N     1 
ATOM   2043 C  CA    . VAL C 1 4   ? 22.83566  39.34419 2.93126   1.000 118.48728 ? 4   VAL C CA    1 
ATOM   2044 C  C     . VAL C 1 4   ? 23.21068  38.79594 1.56081   1.000 114.28517 ? 4   VAL C C     1 
ATOM   2045 O  O     . VAL C 1 4   ? 22.85898  39.37085 0.52491   1.000 114.78998 ? 4   VAL C O     1 
ATOM   2046 C  CB    . VAL C 1 4   ? 21.46763  38.78699 3.38538   1.000 107.42396 ? 4   VAL C CB    1 
ATOM   2047 C  CG1   . VAL C 1 4   ? 21.63135  37.39039 3.93167   1.000 103.49622 ? 4   VAL C CG1   1 
ATOM   2048 C  CG2   . VAL C 1 4   ? 20.83515  39.69844 4.42315   1.000 114.35031 ? 4   VAL C CG2   1 
ATOM   2049 N  N     . ILE C 1 5   ? 23.93026  37.67368 1.55802   1.000 110.51991 ? 5   ILE C N     1 
ATOM   2050 C  CA    . ILE C 1 5   ? 24.41338  37.06657 0.32519   1.000 104.37867 ? 5   ILE C CA    1 
ATOM   2051 C  C     . ILE C 1 5   ? 23.78837  35.68901 0.15939   1.000 106.22028 ? 5   ILE C C     1 
ATOM   2052 O  O     . ILE C 1 5   ? 23.47639  34.99993 1.13593   1.000 107.80321 ? 5   ILE C O     1 
ATOM   2053 C  CB    . ILE C 1 5   ? 25.95605  36.97170 0.28667   1.000 104.68407 ? 5   ILE C CB    1 
ATOM   2054 C  CG1   . ILE C 1 5   ? 26.46762  35.96726 1.32014   1.000 103.75394 ? 5   ILE C CG1   1 
ATOM   2055 C  CG2   . ILE C 1 5   ? 26.58047  38.34236 0.51658   1.000 109.96123 ? 5   ILE C CG2   1 
ATOM   2056 C  CD1   . ILE C 1 5   ? 27.96579  35.75294 1.26228   1.000 116.56847 ? 5   ILE C CD1   1 
ATOM   2057 N  N     . LEU C 1 6   ? 23.59492  35.29874 -1.09917  1.000 107.42984 ? 6   LEU C N     1 
ATOM   2058 C  CA    . LEU C 1 6   ? 23.02687  34.00691 -1.46530  1.000 99.79544  ? 6   LEU C CA    1 
ATOM   2059 C  C     . LEU C 1 6   ? 23.99671  33.30197 -2.40080  1.000 103.51050 ? 6   LEU C C     1 
ATOM   2060 O  O     . LEU C 1 6   ? 24.23703  33.77168 -3.51822  1.000 109.29725 ? 6   LEU C O     1 
ATOM   2061 C  CB    . LEU C 1 6   ? 21.66088  34.17600 -2.13421  1.000 96.82502  ? 6   LEU C CB    1 
ATOM   2062 C  CG    . LEU C 1 6   ? 21.03396  32.94948 -2.79770  1.000 94.55617  ? 6   LEU C CG    1 
ATOM   2063 C  CD1   . LEU C 1 6   ? 20.80170  31.83550 -1.78825  1.000 92.59551  ? 6   LEU C CD1   1 
ATOM   2064 C  CD2   . LEU C 1 6   ? 19.73433  33.32639 -3.49496  1.000 86.33728  ? 6   LEU C CD2   1 
ATOM   2065 N  N     . LYS C 1 7   ? 24.55064  32.18222 -1.94579  1.000 99.24896  ? 7   LYS C N     1 
ATOM   2066 C  CA    . LYS C 1 7   ? 25.51103  31.41631 -2.72899  1.000 108.04634 ? 7   LYS C CA    1 
ATOM   2067 C  C     . LYS C 1 7   ? 24.76432  30.41169 -3.59842  1.000 100.19651 ? 7   LYS C C     1 
ATOM   2068 O  O     . LYS C 1 7   ? 24.00748  29.58007 -3.08520  1.000 102.26590 ? 7   LYS C O     1 
ATOM   2069 C  CB    . LYS C 1 7   ? 26.50654  30.70761 -1.81262  1.000 108.31000 ? 7   LYS C CB    1 
ATOM   2070 N  N     . ILE C 1 8   ? 24.97862  30.48933 -4.90970  1.000 106.46606 ? 8   ILE C N     1 
ATOM   2071 C  CA    . ILE C 1 8   ? 24.31415  29.62604 -5.87852  1.000 99.51084  ? 8   ILE C CA    1 
ATOM   2072 C  C     . ILE C 1 8   ? 25.37653  28.91524 -6.70406  1.000 108.77044 ? 8   ILE C C     1 
ATOM   2073 O  O     . ILE C 1 8   ? 26.28450  29.55867 -7.24277  1.000 113.58426 ? 8   ILE C O     1 
ATOM   2074 C  CB    . ILE C 1 8   ? 23.36268  30.42129 -6.79090  1.000 95.10909  ? 8   ILE C CB    1 
ATOM   2075 C  CG1   . ILE C 1 8   ? 22.35462  31.20973 -5.95464  1.000 99.37146  ? 8   ILE C CG1   1 
ATOM   2076 C  CG2   . ILE C 1 8   ? 22.64575  29.48800 -7.75407  1.000 97.65748  ? 8   ILE C CG2   1 
ATOM   2077 C  CD1   . ILE C 1 8   ? 21.38026  32.01545 -6.78006  1.000 98.23464  ? 8   ILE C CD1   1 
ATOM   2078 N  N     . LYS C 1 9   ? 25.26156  27.59364 -6.80159  1.000 104.27681 ? 9   LYS C N     1 
ATOM   2079 C  CA    . LYS C 1 9   ? 26.13091  26.77796 -7.64030  1.000 100.25980 ? 9   LYS C CA    1 
ATOM   2080 C  C     . LYS C 1 9   ? 25.30870  26.24869 -8.80687  1.000 104.80093 ? 9   LYS C C     1 
ATOM   2081 O  O     . LYS C 1 9   ? 24.31578  25.54232 -8.59967  1.000 103.99252 ? 9   LYS C O     1 
ATOM   2082 C  CB    . LYS C 1 9   ? 26.74773  25.62809 -6.84402  1.000 96.45474  ? 9   LYS C CB    1 
ATOM   2083 N  N     . ARG C 1 10  ? 25.71939  26.59191 -10.02497 1.000 106.18431 ? 10  ARG C N     1 
ATOM   2084 C  CA    . ARG C 1 10  ? 24.97026  26.24153 -11.22506 1.000 100.61063 ? 10  ARG C CA    1 
ATOM   2085 C  C     . ARG C 1 10  ? 25.42374  24.87905 -11.73781 1.000 104.67227 ? 10  ARG C C     1 
ATOM   2086 O  O     . ARG C 1 10  ? 26.59693  24.69797 -12.08404 1.000 114.71236 ? 10  ARG C O     1 
ATOM   2087 C  CB    . ARG C 1 10  ? 25.14917  27.31204 -12.30153 1.000 106.91026 ? 10  ARG C CB    1 
ATOM   2088 C  CG    . ARG C 1 10  ? 24.66743  28.69129 -11.87620 1.000 107.06270 ? 10  ARG C CG    1 
ATOM   2089 C  CD    . ARG C 1 10  ? 24.63772  29.67398 -13.03984 1.000 111.79764 ? 10  ARG C CD    1 
ATOM   2090 N  NE    . ARG C 1 10  ? 25.96941  30.07915 -13.47500 1.000 115.70586 ? 10  ARG C NE    1 
ATOM   2091 C  CZ    . ARG C 1 10  ? 26.20330  30.99121 -14.40931 1.000 119.93240 ? 10  ARG C CZ    1 
ATOM   2092 N  NH1   . ARG C 1 10  ? 25.21451  31.61565 -15.02833 1.000 116.50544 ? 10  ARG C NH1   1 
ATOM   2093 N  NH2   . ARG C 1 10  ? 27.46025  31.28538 -14.72978 1.000 115.20509 ? 10  ARG C NH2   1 
ATOM   2094 N  N     . LEU C 1 11  ? 24.49370  23.92581 -11.78215 1.000 105.27161 ? 11  LEU C N     1 
ATOM   2095 C  CA    . LEU C 1 11  ? 24.77850  22.61677 -12.33771 1.000 102.17621 ? 11  LEU C CA    1 
ATOM   2096 C  C     . LEU C 1 11  ? 25.06656  22.73076 -13.83379 1.000 105.91427 ? 11  LEU C C     1 
ATOM   2097 O  O     . LEU C 1 11  ? 24.70554  23.72420 -14.46852 1.000 111.91723 ? 11  LEU C O     1 
ATOM   2098 C  CB    . LEU C 1 11  ? 23.60754  21.66805 -12.08850 1.000 100.17165 ? 11  LEU C CB    1 
ATOM   2099 C  CG    . LEU C 1 11  ? 23.48587  21.10747 -10.67063 1.000 93.05274  ? 11  LEU C CG    1 
ATOM   2100 C  CD1   . LEU C 1 11  ? 22.46018  19.98451 -10.61857 1.000 87.38162  ? 11  LEU C CD1   1 
ATOM   2101 C  CD2   . LEU C 1 11  ? 24.83850  20.62761 -10.16021 1.000 84.70846  ? 11  LEU C CD2   1 
ATOM   2102 N  N     . PRO C 1 12  ? 25.73630  21.72726 -14.41466 1.000 110.37972 ? 12  PRO C N     1 
ATOM   2103 C  CA    . PRO C 1 12  ? 26.09102  21.79983 -15.84422 1.000 111.86995 ? 12  PRO C CA    1 
ATOM   2104 C  C     . PRO C 1 12  ? 24.93142  22.11976 -16.77400 1.000 114.88250 ? 12  PRO C C     1 
ATOM   2105 O  O     . PRO C 1 12  ? 25.14618  22.77991 -17.79857 1.000 113.59107 ? 12  PRO C O     1 
ATOM   2106 C  CB    . PRO C 1 12  ? 26.66411  20.40404 -16.11814 1.000 111.87344 ? 12  PRO C CB    1 
ATOM   2107 C  CG    . PRO C 1 12  ? 27.27055  20.00752 -14.81935 1.000 113.28077 ? 12  PRO C CG    1 
ATOM   2108 C  CD    . PRO C 1 12  ? 26.34616  20.55346 -13.76123 1.000 115.10416 ? 12  PRO C CD    1 
ATOM   2109 N  N     . HIS C 1 13  ? 23.71158  21.68493 -16.45966 1.000 106.20443 ? 13  HIS C N     1 
ATOM   2110 C  CA    . HIS C 1 13  ? 22.56485  22.04844 -17.28375 1.000 103.24617 ? 13  HIS C CA    1 
ATOM   2111 C  C     . HIS C 1 13  ? 21.99522  23.41698 -16.92796 1.000 101.60120 ? 13  HIS C C     1 
ATOM   2112 O  O     . HIS C 1 13  ? 20.89699  23.75615 -17.38110 1.000 100.82423 ? 13  HIS C O     1 
ATOM   2113 C  CB    . HIS C 1 13  ? 21.47354  20.97536 -17.19385 1.000 91.36453  ? 13  HIS C CB    1 
ATOM   2114 C  CG    . HIS C 1 13  ? 21.08055  20.61427 -15.79560 1.000 108.89181 ? 13  HIS C CG    1 
ATOM   2115 N  ND1   . HIS C 1 13  ? 20.52520  19.39414 -15.47542 1.000 113.90820 ? 13  HIS C ND1   1 
ATOM   2116 C  CD2   . HIS C 1 13  ? 21.15272  21.31015 -14.63661 1.000 102.51809 ? 13  HIS C CD2   1 
ATOM   2117 C  CE1   . HIS C 1 13  ? 20.27722  19.35162 -14.17886 1.000 96.33455  ? 13  HIS C CE1   1 
ATOM   2118 N  NE2   . HIS C 1 13  ? 20.64856  20.50181 -13.64649 1.000 97.85340  ? 13  HIS C NE2   1 
ATOM   2119 N  N     . ALA C 1 14  ? 22.72012  24.20548 -16.13217 1.000 105.44074 ? 14  ALA C N     1 
ATOM   2120 C  CA    . ALA C 1 14  ? 22.34598  25.58193 -15.84022 1.000 102.27794 ? 14  ALA C CA    1 
ATOM   2121 C  C     . ALA C 1 14  ? 23.52308  26.53813 -15.98973 1.000 107.60213 ? 14  ALA C C     1 
ATOM   2122 O  O     . ALA C 1 14  ? 23.38462  27.72523 -15.67353 1.000 111.05221 ? 14  ALA C O     1 
ATOM   2123 C  CB    . ALA C 1 14  ? 21.75726  25.69619 -14.42956 1.000 93.71363  ? 14  ALA C CB    1 
ATOM   2124 N  N     . GLN C 1 15  ? 24.67476  26.05535 -16.46468 1.000 106.74475 ? 15  GLN C N     1 
ATOM   2125 C  CA    . GLN C 1 15  ? 25.84280  26.91972 -16.60005 1.000 113.34253 ? 15  GLN C CA    1 
ATOM   2126 C  C     . GLN C 1 15  ? 25.69649  27.89705 -17.75996 1.000 116.24672 ? 15  GLN C C     1 
ATOM   2127 O  O     . GLN C 1 15  ? 26.24702  29.00287 -17.70720 1.000 117.71392 ? 15  GLN C O     1 
ATOM   2128 C  CB    . GLN C 1 15  ? 27.10473  26.07454 -16.77511 1.000 121.34884 ? 15  GLN C CB    1 
ATOM   2129 C  CG    . GLN C 1 15  ? 27.47852  25.25546 -15.54986 1.000 118.42744 ? 15  GLN C CG    1 
ATOM   2130 C  CD    . GLN C 1 15  ? 28.76964  24.48127 -15.73532 1.000 130.07148 ? 15  GLN C CD    1 
ATOM   2131 O  OE1   . GLN C 1 15  ? 29.28671  24.36883 -16.84726 1.000 133.12252 ? 15  GLN C OE1   1 
ATOM   2132 N  NE2   . GLN C 1 15  ? 29.29966  23.94495 -14.64212 1.000 130.14045 ? 15  GLN C NE2   1 
ATOM   2133 N  N     . ASP C 1 16  ? 24.97281  27.51115 -18.81368 1.000 109.70419 ? 16  ASP C N     1 
ATOM   2134 C  CA    . ASP C 1 16  ? 24.74448  28.42097 -19.93087 1.000 112.85981 ? 16  ASP C CA    1 
ATOM   2135 C  C     . ASP C 1 16  ? 23.58772  29.37494 -19.66161 1.000 104.86865 ? 16  ASP C C     1 
ATOM   2136 O  O     . ASP C 1 16  ? 23.56986  30.48748 -20.20005 1.000 101.91837 ? 16  ASP C O     1 
ATOM   2137 C  CB    . ASP C 1 16  ? 24.48404  27.62992 -21.21500 1.000 115.58639 ? 16  ASP C CB    1 
ATOM   2138 C  CG    . ASP C 1 16  ? 23.28321  26.70951 -21.10115 1.000 121.42043 ? 16  ASP C CG    1 
ATOM   2139 O  OD1   . ASP C 1 16  ? 23.09620  26.10425 -20.02413 1.000 112.01711 ? 16  ASP C OD1   1 
ATOM   2140 O  OD2   . ASP C 1 16  ? 22.52602  26.59353 -22.08861 1.000 115.11955 ? 16  ASP C OD2   1 
ATOM   2141 N  N     . LEU C 1 17  ? 22.62362  28.96359 -18.84244 1.000 106.10261 ? 17  LEU C N     1 
ATOM   2142 C  CA    . LEU C 1 17  ? 21.51207  29.83326 -18.49906 1.000 99.17502  ? 17  LEU C CA    1 
ATOM   2143 C  C     . LEU C 1 17  ? 21.99485  30.98323 -17.61485 1.000 99.07247  ? 17  LEU C C     1 
ATOM   2144 O  O     . LEU C 1 17  ? 22.95823  30.83245 -16.85880 1.000 107.84638 ? 17  LEU C O     1 
ATOM   2145 C  CB    . LEU C 1 17  ? 20.42352  29.04425 -17.77739 1.000 101.14929 ? 17  LEU C CB    1 
ATOM   2146 C  CG    . LEU C 1 17  ? 19.87149  27.82759 -18.52053 1.000 104.54388 ? 17  LEU C CG    1 
ATOM   2147 C  CD1   . LEU C 1 17  ? 18.88722  27.07000 -17.64542 1.000 90.59360  ? 17  LEU C CD1   1 
ATOM   2148 C  CD2   . LEU C 1 17  ? 19.21856  28.24925 -19.82678 1.000 93.48371  ? 17  LEU C CD2   1 
ATOM   2149 N  N     . PRO C 1 18  ? 21.34504  32.14347 -17.69189 1.000 96.89472  ? 18  PRO C N     1 
ATOM   2150 C  CA    . PRO C 1 18  ? 21.78705  33.28526 -16.88359 1.000 106.78654 ? 18  PRO C CA    1 
ATOM   2151 C  C     . PRO C 1 18  ? 21.49155  33.08039 -15.40622 1.000 107.58292 ? 18  PRO C C     1 
ATOM   2152 O  O     . PRO C 1 18  ? 20.57821  32.34367 -15.02705 1.000 105.08546 ? 18  PRO C O     1 
ATOM   2153 C  CB    . PRO C 1 18  ? 20.97832  34.45673 -17.45226 1.000 104.26675 ? 18  PRO C CB    1 
ATOM   2154 C  CG    . PRO C 1 18  ? 19.76018  33.81985 -18.03499 1.000 94.75127  ? 18  PRO C CG    1 
ATOM   2155 C  CD    . PRO C 1 18  ? 20.21147  32.48969 -18.56785 1.000 93.33319  ? 18  PRO C CD    1 
ATOM   2156 N  N     . LEU C 1 19  ? 22.28422  33.75004 -14.56924 1.000 115.51284 ? 19  LEU C N     1 
ATOM   2157 C  CA    . LEU C 1 19  ? 22.08152  33.68675 -13.12953 1.000 116.24396 ? 19  LEU C CA    1 
ATOM   2158 C  C     . LEU C 1 19  ? 20.71502  34.26133 -12.76026 1.000 118.52217 ? 19  LEU C C     1 
ATOM   2159 O  O     . LEU C 1 19  ? 20.19683  35.14434 -13.45080 1.000 122.45424 ? 19  LEU C O     1 
ATOM   2160 C  CB    . LEU C 1 19  ? 23.17258  34.46343 -12.39239 1.000 116.91549 ? 19  LEU C CB    1 
ATOM   2161 C  CG    . LEU C 1 19  ? 24.40281  33.71453 -11.88160 1.000 125.58063 ? 19  LEU C CG    1 
ATOM   2162 C  CD1   . LEU C 1 19  ? 25.37191  34.69272 -11.23992 1.000 122.77443 ? 19  LEU C CD1   1 
ATOM   2163 C  CD2   . LEU C 1 19  ? 24.00662  32.63073 -10.89174 1.000 121.35137 ? 19  LEU C CD2   1 
ATOM   2164 N  N     . PRO C 1 20  ? 20.10499  33.77171 -11.68206 1.000 117.94280 ? 20  PRO C N     1 
ATOM   2165 C  CA    . PRO C 1 20  ? 18.89218  34.41885 -11.16715 1.000 112.49803 ? 20  PRO C CA    1 
ATOM   2166 C  C     . PRO C 1 20  ? 19.18108  35.85448 -10.75366 1.000 111.24107 ? 20  PRO C C     1 
ATOM   2167 O  O     . PRO C 1 20  ? 20.13498  36.12931 -10.02188 1.000 113.40409 ? 20  PRO C O     1 
ATOM   2168 C  CB    . PRO C 1 20  ? 18.50974  33.54785 -9.96507  1.000 106.66270 ? 20  PRO C CB    1 
ATOM   2169 C  CG    . PRO C 1 20  ? 19.14314  32.23004 -10.24052 1.000 107.07709 ? 20  PRO C CG    1 
ATOM   2170 C  CD    . PRO C 1 20  ? 20.42775  32.54096 -10.94186 1.000 115.44462 ? 20  PRO C CD    1 
ATOM   2171 N  N     . SER C 1 21  ? 18.34887  36.77407 -11.23493 1.000 112.30812 ? 21  SER C N     1 
ATOM   2172 C  CA    . SER C 1 21  ? 18.52370  38.19039 -10.95799 1.000 112.36762 ? 21  SER C CA    1 
ATOM   2173 C  C     . SER C 1 21  ? 17.16994  38.82077 -10.67016 1.000 104.81483 ? 21  SER C C     1 
ATOM   2174 O  O     . SER C 1 21  ? 16.14362  38.39858 -11.20953 1.000 106.64731 ? 21  SER C O     1 
ATOM   2175 C  CB    . SER C 1 21  ? 19.20388  38.91268 -12.13013 1.000 111.30779 ? 21  SER C CB    1 
ATOM   2176 O  OG    . SER C 1 21  ? 20.44062  38.30159 -12.45554 1.000 118.53866 ? 21  SER C OG    1 
ATOM   2177 N  N     . TYR C 1 22  ? 17.17599  39.82852 -9.80105  1.000 100.30228 ? 22  TYR C N     1 
ATOM   2178 C  CA    . TYR C 1 22  ? 15.97325  40.61515 -9.56992  1.000 100.70188 ? 22  TYR C CA    1 
ATOM   2179 C  C     . TYR C 1 22  ? 15.64055  41.41756 -10.82167 1.000 97.42906  ? 22  TYR C C     1 
ATOM   2180 O  O     . TYR C 1 22  ? 16.50563  42.09603 -11.38486 1.000 98.73039  ? 22  TYR C O     1 
ATOM   2181 C  CB    . TYR C 1 22  ? 16.16097  41.54782 -8.37343  1.000 103.04138 ? 22  TYR C CB    1 
ATOM   2182 C  CG    . TYR C 1 22  ? 16.31419  40.84015 -7.04350  1.000 100.01658 ? 22  TYR C CG    1 
ATOM   2183 C  CD1   . TYR C 1 22  ? 15.20225  40.41513 -6.32764  1.000 99.06094  ? 22  TYR C CD1   1 
ATOM   2184 C  CD2   . TYR C 1 22  ? 17.56977  40.60780 -6.49869  1.000 97.37069  ? 22  TYR C CD2   1 
ATOM   2185 C  CE1   . TYR C 1 22  ? 15.33752  39.77156 -5.11044  1.000 96.51962  ? 22  TYR C CE1   1 
ATOM   2186 C  CE2   . TYR C 1 22  ? 17.71437  39.96504 -5.28229  1.000 99.12257  ? 22  TYR C CE2   1 
ATOM   2187 C  CZ    . TYR C 1 22  ? 16.59521  39.55020 -4.59251  1.000 100.49967 ? 22  TYR C CZ    1 
ATOM   2188 O  OH    . TYR C 1 22  ? 16.73124  38.90946 -3.38186  1.000 95.34427  ? 22  TYR C OH    1 
ATOM   2189 N  N     . ALA C 1 23  ? 14.38516  41.32977 -11.26502 1.000 96.70492  ? 23  ALA C N     1 
ATOM   2190 C  CA    . ALA C 1 23  ? 13.97622  42.03252 -12.47741 1.000 94.69040  ? 23  ALA C CA    1 
ATOM   2191 C  C     . ALA C 1 23  ? 14.06539  43.54249 -12.29284 1.000 103.76181 ? 23  ALA C C     1 
ATOM   2192 O  O     . ALA C 1 23  ? 14.73313  44.23763 -13.06668 1.000 99.72444  ? 23  ALA C O     1 
ATOM   2193 C  CB    . ALA C 1 23  ? 12.55866  41.61784 -12.87419 1.000 78.20419  ? 23  ALA C CB    1 
ATOM   2194 N  N     . THR C 1 24  ? 13.40154  44.06552 -11.27072 1.000 104.50962 ? 24  THR C N     1 
ATOM   2195 C  CA    . THR C 1 24  ? 13.38450  45.48496 -10.96416 1.000 103.43983 ? 24  THR C CA    1 
ATOM   2196 C  C     . THR C 1 24  ? 14.19962  45.76584 -9.70629  1.000 100.21965 ? 24  THR C C     1 
ATOM   2197 O  O     . THR C 1 24  ? 14.48252  44.85272 -8.92331  1.000 101.71259 ? 24  THR C O     1 
ATOM   2198 C  CB    . THR C 1 24  ? 11.94142  45.97230 -10.76939 1.000 98.61254  ? 24  THR C CB    1 
ATOM   2199 O  OG1   . THR C 1 24  ? 11.42334  45.45736 -9.53700  1.000 101.45448 ? 24  THR C OG1   1 
ATOM   2200 C  CG2   . THR C 1 24  ? 11.06034  45.50183 -11.91698 1.000 98.64047  ? 24  THR C CG2   1 
ATOM   2201 N  N     . PRO C 1 25  ? 14.61057  47.01963 -9.48375  1.000 105.28460 ? 25  PRO C N     1 
ATOM   2202 C  CA    . PRO C 1 25  ? 15.39034  47.33317 -8.27337  1.000 101.87738 ? 25  PRO C CA    1 
ATOM   2203 C  C     . PRO C 1 25  ? 14.66792  47.03954 -6.96730  1.000 103.57829 ? 25  PRO C C     1 
ATOM   2204 O  O     . PRO C 1 25  ? 15.30400  47.11327 -5.90854  1.000 109.41962 ? 25  PRO C O     1 
ATOM   2205 C  CB    . PRO C 1 25  ? 15.67560  48.83350 -8.41866  1.000 102.48698 ? 25  PRO C CB    1 
ATOM   2206 C  CG    . PRO C 1 25  ? 15.64056  49.07288 -9.88431  1.000 103.43045 ? 25  PRO C CG    1 
ATOM   2207 C  CD    . PRO C 1 25  ? 14.57111  48.16151 -10.41523 1.000 101.58251 ? 25  PRO C CD    1 
ATOM   2208 N  N     . HIS C 1 26  ? 13.37294  46.71176 -6.99762  1.000 104.25135 ? 26  HIS C N     1 
ATOM   2209 C  CA    . HIS C 1 26  ? 12.64501  46.41439 -5.76992  1.000 103.84774 ? 26  HIS C CA    1 
ATOM   2210 C  C     . HIS C 1 26  ? 11.73077  45.20427 -5.93298  1.000 100.32391 ? 26  HIS C C     1 
ATOM   2211 O  O     . HIS C 1 26  ? 10.65745  45.14611 -5.32239  1.000 99.27441  ? 26  HIS C O     1 
ATOM   2212 C  CB    . HIS C 1 26  ? 11.83749  47.62725 -5.30331  1.000 105.15161 ? 26  HIS C CB    1 
ATOM   2213 C  CG    . HIS C 1 26  ? 12.67990  48.82027 -4.97364  1.000 109.50332 ? 26  HIS C CG    1 
ATOM   2214 N  ND1   . HIS C 1 26  ? 13.59966  48.82094 -3.94691  1.000 105.96731 ? 26  HIS C ND1   1 
ATOM   2215 C  CD2   . HIS C 1 26  ? 12.74270  50.05062 -5.53549  1.000 103.15334 ? 26  HIS C CD2   1 
ATOM   2216 C  CE1   . HIS C 1 26  ? 14.19285  50.00000 -3.89072  1.000 107.70708 ? 26  HIS C CE1   1 
ATOM   2217 N  NE2   . HIS C 1 26  ? 13.69076  50.76460 -4.84359  1.000 109.40098 ? 26  HIS C NE2   1 
ATOM   2218 N  N     . SER C 1 27  ? 12.13541  44.23410 -6.74741  1.000 98.59248  ? 27  SER C N     1 
ATOM   2219 C  CA    . SER C 1 27  ? 11.39589  42.98808 -6.85529  1.000 94.99155  ? 27  SER C CA    1 
ATOM   2220 C  C     . SER C 1 27  ? 11.66087  42.11384 -5.63355  1.000 94.74414  ? 27  SER C C     1 
ATOM   2221 O  O     . SER C 1 27  ? 12.68031  42.24583 -4.95094  1.000 92.89927  ? 27  SER C O     1 
ATOM   2222 C  CB    . SER C 1 27  ? 11.77590  42.24022 -8.13365  1.000 98.13693  ? 27  SER C CB    1 
ATOM   2223 O  OG    . SER C 1 27  ? 11.40593  42.97731 -9.28592  1.000 102.31990 ? 27  SER C OG    1 
ATOM   2224 N  N     . SER C 1 28  ? 10.72298  41.20718 -5.36313  1.000 95.16873  ? 28  SER C N     1 
ATOM   2225 C  CA    . SER C 1 28  ? 10.79487  40.37657 -4.16871  1.000 88.92092  ? 28  SER C CA    1 
ATOM   2226 C  C     . SER C 1 28  ? 11.44923  39.02293 -4.40724  1.000 90.40977  ? 28  SER C C     1 
ATOM   2227 O  O     . SER C 1 28  ? 11.90259  38.39500 -3.44335  1.000 83.74415  ? 28  SER C O     1 
ATOM   2228 C  CB    . SER C 1 28  ? 9.39177   40.15858 -3.59203  1.000 75.99919  ? 28  SER C CB    1 
ATOM   2229 O  OG    . SER C 1 28  ? 8.79448   41.38910 -3.22266  1.000 92.56654  ? 28  SER C OG    1 
ATOM   2230 N  N     . GLY C 1 29  ? 11.51850  38.55797 -5.65358  1.000 87.46940  ? 29  GLY C N     1 
ATOM   2231 C  CA    . GLY C 1 29  ? 11.99501  37.21841 -5.92193  1.000 91.25586  ? 29  GLY C CA    1 
ATOM   2232 C  C     . GLY C 1 29  ? 12.94540  37.17505 -7.10132  1.000 92.69096  ? 29  GLY C C     1 
ATOM   2233 O  O     . GLY C 1 29  ? 12.98274  38.07770 -7.94129  1.000 93.68828  ? 29  GLY C O     1 
ATOM   2234 N  N     . LEU C 1 30  ? 13.71899  36.09340 -7.14323  1.000 92.59283  ? 30  LEU C N     1 
ATOM   2235 C  CA    . LEU C 1 30  ? 14.62851  35.80775 -8.24235  1.000 92.14095  ? 30  LEU C CA    1 
ATOM   2236 C  C     . LEU C 1 30  ? 13.92757  34.94429 -9.28342  1.000 90.09386  ? 30  LEU C C     1 
ATOM   2237 O  O     . LEU C 1 30  ? 13.03388  34.15748 -8.96361  1.000 90.25197  ? 30  LEU C O     1 
ATOM   2238 C  CB    . LEU C 1 30  ? 15.88581  35.08832 -7.74325  1.000 95.12053  ? 30  LEU C CB    1 
ATOM   2239 C  CG    . LEU C 1 30  ? 16.95938  35.82273 -6.92891  1.000 94.42620  ? 30  LEU C CG    1 
ATOM   2240 C  CD1   . LEU C 1 30  ? 17.50254  37.02445 -7.68604  1.000 103.65918 ? 30  LEU C CD1   1 
ATOM   2241 C  CD2   . LEU C 1 30  ? 16.45906  36.23016 -5.54811  1.000 98.39630  ? 30  LEU C CD2   1 
ATOM   2242 N  N     . ASP C 1 31  ? 14.34567  35.09169 -10.53698 1.000 98.19005  ? 31  ASP C N     1 
ATOM   2243 C  CA    . ASP C 1 31  ? 13.75711  34.30160 -11.61006 1.000 88.88782  ? 31  ASP C CA    1 
ATOM   2244 C  C     . ASP C 1 31  ? 14.24449  32.85959 -11.53633 1.000 89.52883  ? 31  ASP C C     1 
ATOM   2245 O  O     . ASP C 1 31  ? 15.44791  32.60342 -11.43647 1.000 94.92401  ? 31  ASP C O     1 
ATOM   2246 C  CB    . ASP C 1 31  ? 14.10308  34.90698 -12.96901 1.000 92.65437  ? 31  ASP C CB    1 
ATOM   2247 C  CG    . ASP C 1 31  ? 13.44264  36.25063 -13.19244 1.000 112.43439 ? 31  ASP C CG    1 
ATOM   2248 O  OD1   . ASP C 1 31  ? 13.82789  37.22420 -12.51152 1.000 112.31908 ? 31  ASP C OD1   1 
ATOM   2249 O  OD2   . ASP C 1 31  ? 12.53600  36.33251 -14.04791 1.000 118.77197 ? 31  ASP C OD2   1 
ATOM   2250 N  N     . LEU C 1 32  ? 13.30612  31.91846 -11.58187 1.000 83.33592  ? 32  LEU C N     1 
ATOM   2251 C  CA    . LEU C 1 32  ? 13.60673  30.49261 -11.62161 1.000 76.33705  ? 32  LEU C CA    1 
ATOM   2252 C  C     . LEU C 1 32  ? 13.33443  29.98310 -13.03004 1.000 87.69015  ? 32  LEU C C     1 
ATOM   2253 O  O     . LEU C 1 32  ? 12.21348  30.11505 -13.53288 1.000 84.61858  ? 32  LEU C O     1 
ATOM   2254 C  CB    . LEU C 1 32  ? 12.77145  29.72855 -10.59492 1.000 77.76392  ? 32  LEU C CB    1 
ATOM   2255 C  CG    . LEU C 1 32  ? 13.50242  29.27366 -9.33099  1.000 84.44157  ? 32  LEU C CG    1 
ATOM   2256 C  CD1   . LEU C 1 32  ? 14.45105  30.35285 -8.83923  1.000 82.17673  ? 32  LEU C CD1   1 
ATOM   2257 C  CD2   . LEU C 1 32  ? 12.50572  28.90158 -8.24490  1.000 70.81429  ? 32  LEU C CD2   1 
ATOM   2258 N  N     . ARG C 1 33  ? 14.35268  29.40409 -13.66090 1.000 86.16895  ? 33  ARG C N     1 
ATOM   2259 C  CA    . ARG C 1 33  ? 14.27598  28.99493 -15.05463 1.000 88.62791  ? 33  ARG C CA    1 
ATOM   2260 C  C     . ARG C 1 33  ? 14.30026  27.47777 -15.18869 1.000 86.58374  ? 33  ARG C C     1 
ATOM   2261 O  O     . ARG C 1 33  ? 14.91692  26.77102 -14.38648 1.000 70.41577  ? 33  ARG C O     1 
ATOM   2262 C  CB    . ARG C 1 33  ? 15.42164  29.60320 -15.86860 1.000 83.95813  ? 33  ARG C CB    1 
ATOM   2263 C  CG    . ARG C 1 33  ? 15.19517  31.05789 -16.23783 1.000 87.91059  ? 33  ARG C CG    1 
ATOM   2264 C  CD    . ARG C 1 33  ? 16.24126  31.55379 -17.21702 1.000 85.24569  ? 33  ARG C CD    1 
ATOM   2265 N  NE    . ARG C 1 33  ? 15.73456  32.65414 -18.02881 1.000 85.36402  ? 33  ARG C NE    1 
ATOM   2266 C  CZ    . ARG C 1 33  ? 15.92522  33.93802 -17.75845 1.000 86.62564  ? 33  ARG C CZ    1 
ATOM   2267 N  NH1   . ARG C 1 33  ? 16.62195  34.32647 -16.70294 1.000 97.06886  ? 33  ARG C NH1   1 
ATOM   2268 N  NH2   . ARG C 1 33  ? 15.40662  34.85537 -18.56972 1.000 82.70584  ? 33  ARG C NH2   1 
ATOM   2269 N  N     . ALA C 1 34  ? 13.62092  26.98859 -16.22404 1.000 87.22314  ? 34  ALA C N     1 
ATOM   2270 C  CA    . ALA C 1 34  ? 13.55960  25.56060 -16.51756 1.000 80.44430  ? 34  ALA C CA    1 
ATOM   2271 C  C     . ALA C 1 34  ? 14.86165  25.12867 -17.18204 1.000 92.77960  ? 34  ALA C C     1 
ATOM   2272 O  O     . ALA C 1 34  ? 15.10086  25.43047 -18.35620 1.000 80.19772  ? 34  ALA C O     1 
ATOM   2273 C  CB    . ALA C 1 34  ? 12.36043  25.25565 -17.40947 1.000 77.17968  ? 34  ALA C CB    1 
ATOM   2274 N  N     . ALA C 1 35  ? 15.70345  24.41649 -16.43471 1.000 85.90434  ? 35  ALA C N     1 
ATOM   2275 C  CA    . ALA C 1 35  ? 16.99325  23.95167 -16.94671 1.000 85.44872  ? 35  ALA C CA    1 
ATOM   2276 C  C     . ALA C 1 35  ? 16.81454  22.59300 -17.62642 1.000 82.67173  ? 35  ALA C C     1 
ATOM   2277 O  O     . ALA C 1 35  ? 17.31189  21.55698 -17.18097 1.000 87.87088  ? 35  ALA C O     1 
ATOM   2278 C  CB    . ALA C 1 35  ? 18.01956  23.89065 -15.82369 1.000 86.16132  ? 35  ALA C CB    1 
ATOM   2279 N  N     . ILE C 1 36  ? 16.08327  22.62195 -18.74048 1.000 87.39462  ? 36  ILE C N     1 
ATOM   2280 C  CA    . ILE C 1 36  ? 15.77438  21.42985 -19.51647 1.000 93.28124  ? 36  ILE C CA    1 
ATOM   2281 C  C     . ILE C 1 36  ? 16.21239  21.65779 -20.95732 1.000 100.14412 ? 36  ILE C C     1 
ATOM   2282 O  O     . ILE C 1 36  ? 16.29540  22.79565 -21.43114 1.000 97.84357  ? 36  ILE C O     1 
ATOM   2283 C  CB    . ILE C 1 36  ? 14.27017  21.07093 -19.43733 1.000 97.89759  ? 36  ILE C CB    1 
ATOM   2284 C  CG1   . ILE C 1 36  ? 14.03106  19.63740 -19.91559 1.000 113.25369 ? 36  ILE C CG1   1 
ATOM   2285 C  CG2   . ILE C 1 36  ? 13.43133  22.06557 -20.23225 1.000 90.88086  ? 36  ILE C CG2   1 
ATOM   2286 C  CD1   . ILE C 1 36  ? 14.82329  18.60005 -19.14491 1.000 112.09048 ? 36  ILE C CD1   1 
ATOM   2287 N  N     . GLU C 1 37  ? 16.51413  20.55860 -21.65235 1.000 99.36202  ? 37  GLU C N     1 
ATOM   2288 C  CA    . GLU C 1 37  ? 16.97818  20.63782 -23.03559 1.000 97.33193  ? 37  GLU C CA    1 
ATOM   2289 C  C     . GLU C 1 37  ? 15.81817  20.85240 -24.00317 1.000 108.00872 ? 37  GLU C C     1 
ATOM   2290 O  O     . GLU C 1 37  ? 15.75444  21.87175 -24.69694 1.000 104.11657 ? 37  GLU C O     1 
ATOM   2291 C  CB    . GLU C 1 37  ? 17.75351  19.36887 -23.39868 1.000 85.07111  ? 37  GLU C CB    1 
ATOM   2292 N  N     . LYS C 1 38  ? 14.87978  19.89090 -24.05915 1.000 106.34517 ? 38  LYS C N     1 
ATOM   2293 C  CA    . LYS C 1 38  ? 13.77147  19.94066 -24.99964 1.000 105.29224 ? 38  LYS C CA    1 
ATOM   2294 C  C     . LYS C 1 38  ? 12.56462  20.63217 -24.37522 1.000 102.18176 ? 38  LYS C C     1 
ATOM   2295 O  O     . LYS C 1 38  ? 12.39118  20.60761 -23.15248 1.000 102.63903 ? 38  LYS C O     1 
ATOM   2296 C  CB    . LYS C 1 38  ? 13.38111  18.53067 -25.43549 1.000 102.52216 ? 38  LYS C CB    1 
ATOM   2297 N  N     . PRO C 1 39  ? 11.72529  21.26309 -25.19594 1.000 104.05089 ? 39  PRO C N     1 
ATOM   2298 C  CA    . PRO C 1 39  ? 10.49574  21.86480 -24.66669 1.000 94.86578  ? 39  PRO C CA    1 
ATOM   2299 C  C     . PRO C 1 39  ? 9.56211   20.80653 -24.09423 1.000 100.74325 ? 39  PRO C C     1 
ATOM   2300 O  O     . PRO C 1 39  ? 9.36086   19.74187 -24.68235 1.000 98.15729  ? 39  PRO C O     1 
ATOM   2301 C  CB    . PRO C 1 39  ? 9.88464   22.56152 -25.88922 1.000 95.46083  ? 39  PRO C CB    1 
ATOM   2302 C  CG    . PRO C 1 39  ? 10.51094  21.89188 -27.07319 1.000 95.14050  ? 39  PRO C CG    1 
ATOM   2303 C  CD    . PRO C 1 39  ? 11.89127  21.51201 -26.63853 1.000 92.83791  ? 39  PRO C CD    1 
ATOM   2304 N  N     . LEU C 1 40  ? 8.99212   21.11275 -22.93185 1.000 99.31274  ? 40  LEU C N     1 
ATOM   2305 C  CA    . LEU C 1 40  ? 8.12319   20.19533 -22.20712 1.000 97.92921  ? 40  LEU C CA    1 
ATOM   2306 C  C     . LEU C 1 40  ? 6.66140   20.49588 -22.50518 1.000 100.38659 ? 40  LEU C C     1 
ATOM   2307 O  O     . LEU C 1 40  ? 6.24855   21.65824 -22.51930 1.000 107.64833 ? 40  LEU C O     1 
ATOM   2308 C  CB    . LEU C 1 40  ? 8.36751   20.29356 -20.70051 1.000 94.61134  ? 40  LEU C CB    1 
ATOM   2309 C  CG    . LEU C 1 40  ? 9.27388   19.23736 -20.07212 1.000 88.78496  ? 40  LEU C CG    1 
ATOM   2310 C  CD1   . LEU C 1 40  ? 9.66894   19.64717 -18.66450 1.000 93.67104  ? 40  LEU C CD1   1 
ATOM   2311 C  CD2   . LEU C 1 40  ? 8.57376   17.88889 -20.05961 1.000 95.00104  ? 40  LEU C CD2   1 
ATOM   2312 N  N     . LYS C 1 41  ? 5.88063   19.44188 -22.72974 1.000 93.87184  ? 41  LYS C N     1 
ATOM   2313 C  CA    . LYS C 1 41  ? 4.44661   19.55287 -22.96130 1.000 100.13499 ? 41  LYS C CA    1 
ATOM   2314 C  C     . LYS C 1 41  ? 3.69426   19.01113 -21.75385 1.000 95.34639  ? 41  LYS C C     1 
ATOM   2315 O  O     . LYS C 1 41  ? 3.91809   17.86890 -21.33816 1.000 95.80402  ? 41  LYS C O     1 
ATOM   2316 C  CB    . LYS C 1 41  ? 4.03086   18.80167 -24.22845 1.000 95.54005  ? 41  LYS C CB    1 
ATOM   2317 C  CG    . LYS C 1 41  ? 4.58261   19.40412 -25.50905 1.000 102.96224 ? 41  LYS C CG    1 
ATOM   2318 C  CD    . LYS C 1 41  ? 3.55380   19.36080 -26.62663 1.000 96.49632  ? 41  LYS C CD    1 
ATOM   2319 C  CE    . LYS C 1 41  ? 4.04521   20.10376 -27.85860 1.000 93.35589  ? 41  LYS C CE    1 
ATOM   2320 N  NZ    . LYS C 1 41  ? 2.97564   20.24545 -28.88537 1.000 103.79477 ? 41  LYS C NZ    1 
ATOM   2321 N  N     . ILE C 1 42  ? 2.80957   19.83305 -21.19459 1.000 92.69608  ? 42  ILE C N     1 
ATOM   2322 C  CA    . ILE C 1 42  ? 2.01868   19.47756 -20.02178 1.000 93.79943  ? 42  ILE C CA    1 
ATOM   2323 C  C     . ILE C 1 42  ? 0.55591   19.46388 -20.44194 1.000 91.86178  ? 42  ILE C C     1 
ATOM   2324 O  O     . ILE C 1 42  ? -0.01704  20.51580 -20.75628 1.000 90.23073  ? 42  ILE C O     1 
ATOM   2325 C  CB    . ILE C 1 42  ? 2.24184   20.45035 -18.85736 1.000 85.38850  ? 42  ILE C CB    1 
ATOM   2326 C  CG1   . ILE C 1 42  ? 3.72403   20.79805 -18.72199 1.000 81.36127  ? 42  ILE C CG1   1 
ATOM   2327 C  CG2   . ILE C 1 42  ? 1.72184   19.85143 -17.55857 1.000 83.02249  ? 42  ILE C CG2   1 
ATOM   2328 C  CD1   . ILE C 1 42  ? 3.99057   21.84907 -17.67421 1.000 72.57560  ? 42  ILE C CD1   1 
ATOM   2329 N  N     . LYS C 1 43  ? -0.04941  18.27775 -20.44800 1.000 93.94356  ? 43  LYS C N     1 
ATOM   2330 C  CA    . LYS C 1 43  ? -1.45904  18.14396 -20.75212 1.000 99.25939  ? 43  LYS C CA    1 
ATOM   2331 C  C     . LYS C 1 43  ? -2.27960  18.77493 -19.62745 1.000 97.41671  ? 43  LYS C C     1 
ATOM   2332 O  O     . LYS C 1 43  ? -1.75667  19.05642 -18.54696 1.000 92.86213  ? 43  LYS C O     1 
ATOM   2333 C  CB    . LYS C 1 43  ? -1.81906  16.66884 -20.93700 1.000 99.03244  ? 43  LYS C CB    1 
ATOM   2334 C  CG    . LYS C 1 43  ? -0.79393  15.85001 -21.70485 1.000 107.80468 ? 43  LYS C CG    1 
ATOM   2335 C  CD    . LYS C 1 43  ? -1.38599  14.52348 -22.17435 1.000 110.80793 ? 43  LYS C CD    1 
ATOM   2336 C  CE    . LYS C 1 43  ? -2.25054  13.88378 -21.09509 1.000 110.90558 ? 43  LYS C CE    1 
ATOM   2337 N  NZ    . LYS C 1 43  ? -1.49161  13.59782 -19.84528 1.000 98.26606  ? 43  LYS C NZ    1 
ATOM   2338 N  N     . PRO C 1 44  ? -3.56983  19.02437 -19.85387 1.000 100.00328 ? 44  PRO C N     1 
ATOM   2339 C  CA    . PRO C 1 44  ? -4.42342  19.50097 -18.76029 1.000 95.50388  ? 44  PRO C CA    1 
ATOM   2340 C  C     . PRO C 1 44  ? -4.39120  18.54575 -17.57392 1.000 93.02432  ? 44  PRO C C     1 
ATOM   2341 O  O     . PRO C 1 44  ? -4.34591  17.32386 -17.73683 1.000 86.85827  ? 44  PRO C O     1 
ATOM   2342 C  CB    . PRO C 1 44  ? -5.81320  19.56151 -19.40223 1.000 96.27421  ? 44  PRO C CB    1 
ATOM   2343 C  CG    . PRO C 1 44  ? -5.54106  19.82658 -20.83808 1.000 103.62867 ? 44  PRO C CG    1 
ATOM   2344 C  CD    . PRO C 1 44  ? -4.25828  19.09780 -21.15651 1.000 101.16692 ? 44  PRO C CD    1 
ATOM   2345 N  N     . PHE C 1 45  ? -4.38685  19.12296 -16.37055 1.000 92.30145  ? 45  PHE C N     1 
ATOM   2346 C  CA    . PHE C 1 45  ? -4.39441  18.38907 -15.10492 1.000 90.15419  ? 45  PHE C CA    1 
ATOM   2347 C  C     . PHE C 1 45  ? -3.15405  17.51814 -14.92258 1.000 84.67959  ? 45  PHE C C     1 
ATOM   2348 O  O     . PHE C 1 45  ? -3.18854  16.52968 -14.18111 1.000 79.22358  ? 45  PHE C O     1 
ATOM   2349 C  CB    . PHE C 1 45  ? -5.66394  17.53944 -14.96333 1.000 88.98136  ? 45  PHE C CB    1 
ATOM   2350 C  CG    . PHE C 1 45  ? -6.93660  18.33156 -15.06294 1.000 96.97754  ? 45  PHE C CG    1 
ATOM   2351 C  CD1   . PHE C 1 45  ? -7.02917  19.59234 -14.49485 1.000 95.18428  ? 45  PHE C CD1   1 
ATOM   2352 C  CD2   . PHE C 1 45  ? -8.03487  17.82131 -15.73552 1.000 100.36336 ? 45  PHE C CD2   1 
ATOM   2353 C  CE1   . PHE C 1 45  ? -8.19599  20.32593 -14.58796 1.000 97.31321  ? 45  PHE C CE1   1 
ATOM   2354 C  CE2   . PHE C 1 45  ? -9.20575  18.54861 -15.83343 1.000 104.77347 ? 45  PHE C CE2   1 
ATOM   2355 C  CZ    . PHE C 1 45  ? -9.28633  19.80399 -15.25873 1.000 102.30447 ? 45  PHE C CZ    1 
ATOM   2356 N  N     . GLU C 1 46  ? -2.05217  17.87107 -15.57661 1.000 79.57625  ? 46  GLU C N     1 
ATOM   2357 C  CA    . GLU C 1 46  ? -0.79762  17.14505 -15.46172 1.000 78.69533  ? 46  GLU C CA    1 
ATOM   2358 C  C     . GLU C 1 46  ? 0.20988   17.97463 -14.67500 1.000 72.79916  ? 46  GLU C C     1 
ATOM   2359 O  O     . GLU C 1 46  ? 0.15220   19.20760 -14.66610 1.000 76.80836  ? 46  GLU C O     1 
ATOM   2360 C  CB    . GLU C 1 46  ? -0.23293  16.80405 -16.84638 1.000 78.15801  ? 46  GLU C CB    1 
ATOM   2361 C  CG    . GLU C 1 46  ? 0.90766   15.79594 -16.83616 1.000 82.21372  ? 46  GLU C CG    1 
ATOM   2362 C  CD    . GLU C 1 46  ? 1.48863   15.55688 -18.21712 1.000 101.86972 ? 46  GLU C CD    1 
ATOM   2363 O  OE1   . GLU C 1 46  ? 1.16772   16.33289 -19.14167 1.000 98.07563  ? 46  GLU C OE1   1 
ATOM   2364 O  OE2   . GLU C 1 46  ? 2.26620   14.59213 -18.37853 1.000 108.77049 ? 46  GLU C OE2   1 
ATOM   2365 N  N     . ARG C 1 47  ? 1.13370   17.28453 -14.00963 1.000 61.94529  ? 47  ARG C N     1 
ATOM   2366 C  CA    . ARG C 1 47  ? 2.16534   17.92076 -13.20505 1.000 67.48770  ? 47  ARG C CA    1 
ATOM   2367 C  C     . ARG C 1 47  ? 3.53372   17.39890 -13.61981 1.000 67.72726  ? 47  ARG C C     1 
ATOM   2368 O  O     . ARG C 1 47  ? 3.68198   16.23441 -14.00048 1.000 69.36350  ? 47  ARG C O     1 
ATOM   2369 C  CB    . ARG C 1 47  ? 1.93615   17.66707 -11.71298 1.000 64.46820  ? 47  ARG C CB    1 
ATOM   2370 C  CG    . ARG C 1 47  ? 1.80936   16.19624 -11.36921 1.000 70.34904  ? 47  ARG C CG    1 
ATOM   2371 C  CD    . ARG C 1 47  ? 0.68651   15.95134 -10.38063 1.000 69.12153  ? 47  ARG C CD    1 
ATOM   2372 N  NE    . ARG C 1 47  ? 0.43020   14.52671 -10.20860 1.000 62.45885  ? 47  ARG C NE    1 
ATOM   2373 C  CZ    . ARG C 1 47  ? 1.08619   13.74823 -9.36000  1.000 63.45453  ? 47  ARG C CZ    1 
ATOM   2374 N  NH1   . ARG C 1 47  ? 2.04304   14.22726 -8.58236  1.000 79.04070  ? 47  ARG C NH1   1 
ATOM   2375 N  NH2   . ARG C 1 47  ? 0.77302   12.45811 -9.28814  1.000 61.60670  ? 47  ARG C NH2   1 
ATOM   2376 N  N     . VAL C 1 48  ? 4.53686   18.27436 -13.54616 1.000 57.08461  ? 48  VAL C N     1 
ATOM   2377 C  CA    . VAL C 1 48  ? 5.89610   17.93949 -13.95334 1.000 63.77929  ? 48  VAL C CA    1 
ATOM   2378 C  C     . VAL C 1 48  ? 6.87841   18.46429 -12.91635 1.000 66.05120  ? 48  VAL C C     1 
ATOM   2379 O  O     . VAL C 1 48  ? 6.63700   19.48143 -12.25910 1.000 62.24520  ? 48  VAL C O     1 
ATOM   2380 C  CB    . VAL C 1 48  ? 6.24353   18.50586 -15.34779 1.000 64.41792  ? 48  VAL C CB    1 
ATOM   2381 C  CG1   . VAL C 1 48  ? 5.41113   17.82875 -16.42432 1.000 58.46503  ? 48  VAL C CG1   1 
ATOM   2382 C  CG2   . VAL C 1 48  ? 6.03853   20.01033 -15.37143 1.000 61.02985  ? 48  VAL C CG2   1 
ATOM   2383 N  N     . LEU C 1 49  ? 7.99786   17.75720 -12.77820 1.000 66.96721  ? 49  LEU C N     1 
ATOM   2384 C  CA    . LEU C 1 49  ? 9.08064   18.12705 -11.86939 1.000 68.34379  ? 49  LEU C CA    1 
ATOM   2385 C  C     . LEU C 1 49  ? 10.23247  18.63565 -12.73000 1.000 73.86352  ? 49  LEU C C     1 
ATOM   2386 O  O     . LEU C 1 49  ? 10.94155  17.84810 -13.36339 1.000 79.96182  ? 49  LEU C O     1 
ATOM   2387 C  CB    . LEU C 1 49  ? 9.49804   16.93989 -11.00493 1.000 72.96703  ? 49  LEU C CB    1 
ATOM   2388 C  CG    . LEU C 1 49  ? 10.51664  17.19691 -9.89082  1.000 75.84012  ? 49  LEU C CG    1 
ATOM   2389 C  CD1   . LEU C 1 49  ? 9.94797   18.14413 -8.84680  1.000 67.46858  ? 49  LEU C CD1   1 
ATOM   2390 C  CD2   . LEU C 1 49  ? 10.95464  15.88907 -9.24720  1.000 61.56026  ? 49  LEU C CD2   1 
ATOM   2391 N  N     . ILE C 1 50  ? 10.41183  19.94758 -12.75414 1.000 67.92111  ? 50  ILE C N     1 
ATOM   2392 C  CA    . ILE C 1 50  ? 11.36476  20.60373 -13.64632 1.000 82.65361  ? 50  ILE C CA    1 
ATOM   2393 C  C     . ILE C 1 50  ? 12.61346  20.96304 -12.84954 1.000 72.25440  ? 50  ILE C C     1 
ATOM   2394 O  O     . ILE C 1 50  ? 12.49849  21.63626 -11.81597 1.000 62.80356  ? 50  ILE C O     1 
ATOM   2395 C  CB    . ILE C 1 50  ? 10.75668  21.85872 -14.29567 1.000 80.64695  ? 50  ILE C CB    1 
ATOM   2396 C  CG1   . ILE C 1 50  ? 9.46838   21.49988 -15.03863 1.000 79.98724  ? 50  ILE C CG1   1 
ATOM   2397 C  CG2   . ILE C 1 50  ? 11.76066  22.49994 -15.23585 1.000 69.56905  ? 50  ILE C CG2   1 
ATOM   2398 C  CD1   . ILE C 1 50  ? 8.71822   22.69783 -15.57943 1.000 76.57770  ? 50  ILE C CD1   1 
ATOM   2399 N  N     . PRO C 1 51  ? 13.79941  20.55153 -13.28556 1.000 74.84484  ? 51  PRO C N     1 
ATOM   2400 C  CA    . PRO C 1 51  ? 15.02154  20.93402 -12.57672 1.000 72.28789  ? 51  PRO C CA    1 
ATOM   2401 C  C     . PRO C 1 51  ? 15.46202  22.34384 -12.93495 1.000 78.00396  ? 51  PRO C C     1 
ATOM   2402 O  O     . PRO C 1 51  ? 15.27299  22.81878 -14.05711 1.000 81.35853  ? 51  PRO C O     1 
ATOM   2403 C  CB    . PRO C 1 51  ? 16.04133  19.89872 -13.06336 1.000 73.97854  ? 51  PRO C CB    1 
ATOM   2404 C  CG    . PRO C 1 51  ? 15.58211  19.57105 -14.44561 1.000 61.90475  ? 51  PRO C CG    1 
ATOM   2405 C  CD    . PRO C 1 51  ? 14.07370  19.64471 -14.41486 1.000 76.68937  ? 51  PRO C CD    1 
ATOM   2406 N  N     . THR C 1 52  ? 16.05801  23.01670 -11.95047 1.000 75.99700  ? 52  THR C N     1 
ATOM   2407 C  CA    . THR C 1 52  ? 16.59690  24.35389 -12.15459 1.000 78.91953  ? 52  THR C CA    1 
ATOM   2408 C  C     . THR C 1 52  ? 18.10320  24.36648 -12.36401 1.000 83.20611  ? 52  THR C C     1 
ATOM   2409 O  O     . THR C 1 52  ? 18.63268  25.35994 -12.87392 1.000 83.49524  ? 52  THR C O     1 
ATOM   2410 C  CB    . THR C 1 52  ? 16.26070  25.25871 -10.96195 1.000 71.18714  ? 52  THR C CB    1 
ATOM   2411 O  OG1   . THR C 1 52  ? 16.84259  24.71582 -9.76982  1.000 70.89126  ? 52  THR C OG1   1 
ATOM   2412 C  CG2   . THR C 1 52  ? 14.75437  25.37166 -10.78344 1.000 73.15698  ? 52  THR C CG2   1 
ATOM   2413 N  N     . GLY C 1 53  ? 18.79867  23.29269 -11.99815 1.000 81.36815  ? 53  GLY C N     1 
ATOM   2414 C  CA    . GLY C 1 53  ? 20.24507  23.30489 -12.04490 1.000 86.82786  ? 53  GLY C CA    1 
ATOM   2415 C  C     . GLY C 1 53  ? 20.88186  24.20350 -11.01568 1.000 89.09888  ? 53  GLY C C     1 
ATOM   2416 O  O     . GLY C 1 53  ? 22.02486  24.62841 -11.19610 1.000 91.68603  ? 53  GLY C O     1 
ATOM   2417 N  N     . LEU C 1 54  ? 20.16835  24.50867 -9.93695  1.000 88.97192  ? 54  LEU C N     1 
ATOM   2418 C  CA    . LEU C 1 54  ? 20.61514  25.45399 -8.92695  1.000 88.92618  ? 54  LEU C CA    1 
ATOM   2419 C  C     . LEU C 1 54  ? 20.72231  24.75694 -7.58002  1.000 87.34697  ? 54  LEU C C     1 
ATOM   2420 O  O     . LEU C 1 54  ? 19.82357  24.00793 -7.18511  1.000 83.66550  ? 54  LEU C O     1 
ATOM   2421 C  CB    . LEU C 1 54  ? 19.64977  26.63948 -8.81926  1.000 76.65595  ? 54  LEU C CB    1 
ATOM   2422 C  CG    . LEU C 1 54  ? 19.89261  27.89380 -9.66217  1.000 86.68114  ? 54  LEU C CG    1 
ATOM   2423 C  CD1   . LEU C 1 54  ? 20.21570  27.56651 -11.11120 1.000 91.14476  ? 54  LEU C CD1   1 
ATOM   2424 C  CD2   . LEU C 1 54  ? 18.67035  28.78611 -9.58514  1.000 79.62756  ? 54  LEU C CD2   1 
ATOM   2425 N  N     . ILE C 1 55  ? 21.82719  25.00610 -6.88351  1.000 90.77598  ? 55  ILE C N     1 
ATOM   2426 C  CA    . ILE C 1 55  ? 22.03342  24.55041 -5.51415  1.000 89.96697  ? 55  ILE C CA    1 
ATOM   2427 C  C     . ILE C 1 55  ? 22.31171  25.78300 -4.66852  1.000 96.63042  ? 55  ILE C C     1 
ATOM   2428 O  O     . ILE C 1 55  ? 23.29946  26.49133 -4.90135  1.000 103.03661 ? 55  ILE C O     1 
ATOM   2429 C  CB    . ILE C 1 55  ? 23.18184  23.53619 -5.41315  1.000 92.92854  ? 55  ILE C CB    1 
ATOM   2430 C  CG1   . ILE C 1 55  ? 22.82224  22.25902 -6.17465  1.000 86.80072  ? 55  ILE C CG1   1 
ATOM   2431 C  CG2   . ILE C 1 55  ? 23.49561  23.23639 -3.95924  1.000 94.05997  ? 55  ILE C CG2   1 
ATOM   2432 C  CD1   . ILE C 1 55  ? 23.96073  21.27670 -6.28974  1.000 76.88638  ? 55  ILE C CD1   1 
ATOM   2433 N  N     . LEU C 1 56  ? 21.44457  26.04108 -3.69698  1.000 92.15188  ? 56  LEU C N     1 
ATOM   2434 C  CA    . LEU C 1 56  ? 21.45056  27.29613 -2.96372  1.000 95.59463  ? 56  LEU C CA    1 
ATOM   2435 C  C     . LEU C 1 56  ? 22.08397  27.13265 -1.58987  1.000 100.39082 ? 56  LEU C C     1 
ATOM   2436 O  O     . LEU C 1 56  ? 22.01218  26.06771 -0.97124  1.000 97.99908  ? 56  LEU C O     1 
ATOM   2437 C  CB    . LEU C 1 56  ? 20.02797  27.83012 -2.79940  1.000 89.88968  ? 56  LEU C CB    1 
ATOM   2438 C  CG    . LEU C 1 56  ? 19.12735  27.76433 -4.02950  1.000 92.60693  ? 56  LEU C CG    1 
ATOM   2439 C  CD1   . LEU C 1 56  ? 17.73276  28.22387 -3.65746  1.000 84.96081  ? 56  LEU C CD1   1 
ATOM   2440 C  CD2   . LEU C 1 56  ? 19.69573  28.60763 -5.15882  1.000 92.39878  ? 56  LEU C CD2   1 
ATOM   2441 N  N     . GLU C 1 57  ? 22.70660  28.20988 -1.11827  1.000 104.76680 ? 57  GLU C N     1 
ATOM   2442 C  CA    . GLU C 1 57  ? 23.13537  28.33710 0.27219   1.000 104.71942 ? 57  GLU C CA    1 
ATOM   2443 C  C     . GLU C 1 57  ? 22.34001  29.49078 0.87031   1.000 103.45491 ? 57  GLU C C     1 
ATOM   2444 O  O     . GLU C 1 57  ? 22.82528  30.61944 0.97881   1.000 104.52076 ? 57  GLU C O     1 
ATOM   2445 C  CB    . GLU C 1 57  ? 24.64942  28.55309 0.40936   1.000 109.31235 ? 57  GLU C CB    1 
ATOM   2446 C  CG    . GLU C 1 57  ? 25.10892  28.62551 1.86371   1.000 118.21032 ? 57  GLU C CG    1 
ATOM   2447 C  CD    . GLU C 1 57  ? 26.58085  28.31303 2.04493   1.000 119.37176 ? 57  GLU C CD    1 
ATOM   2448 O  OE1   . GLU C 1 57  ? 27.31986  28.30428 1.03883   1.000 118.27982 ? 57  GLU C OE1   1 
ATOM   2449 O  OE2   . GLU C 1 57  ? 26.99655  28.07017 3.19836   1.000 115.84759 ? 57  GLU C OE2   1 
ATOM   2450 N  N     . ILE C 1 58  ? 21.09755  29.20219 1.24038   1.000 95.81750  ? 58  ILE C N     1 
ATOM   2451 C  CA    . ILE C 1 58  ? 20.24960  30.18018 1.91180   1.000 94.84152  ? 58  ILE C CA    1 
ATOM   2452 C  C     . ILE C 1 58  ? 20.83170  30.41870 3.29852   1.000 99.42705  ? 58  ILE C C     1 
ATOM   2453 O  O     . ILE C 1 58  ? 21.01461  29.46084 4.06388   1.000 100.86222 ? 58  ILE C O     1 
ATOM   2454 C  CB    . ILE C 1 58  ? 18.79218  29.70418 1.98684   1.000 96.30178  ? 58  ILE C CB    1 
ATOM   2455 C  CG1   . ILE C 1 58  ? 18.27698  29.36293 0.58878   1.000 82.91175  ? 58  ILE C CG1   1 
ATOM   2456 C  CG2   . ILE C 1 58  ? 17.91975  30.76648 2.63702   1.000 89.30077  ? 58  ILE C CG2   1 
ATOM   2457 C  CD1   . ILE C 1 58  ? 16.85513  28.86110 0.57532   1.000 76.76659  ? 58  ILE C CD1   1 
ATOM   2458 N  N     . PRO C 1 59  ? 21.14458  31.66129 3.65924   1.000 102.94832 ? 59  PRO C N     1 
ATOM   2459 C  CA    . PRO C 1 59  ? 21.77901  31.91667 4.95572   1.000 98.41807  ? 59  PRO C CA    1 
ATOM   2460 C  C     . PRO C 1 59  ? 20.86788  31.54269 6.11480   1.000 104.78563 ? 59  PRO C C     1 
ATOM   2461 O  O     . PRO C 1 59  ? 19.64507  31.45306 5.98220   1.000 105.85836 ? 59  PRO C O     1 
ATOM   2462 C  CB    . PRO C 1 59  ? 22.05283  33.42458 4.92504   1.000 96.30296  ? 59  PRO C CB    1 
ATOM   2463 C  CG    . PRO C 1 59  ? 21.06209  33.95734 3.94283   1.000 101.94010 ? 59  PRO C CG    1 
ATOM   2464 C  CD    . PRO C 1 59  ? 20.93578  32.90037 2.89368   1.000 96.63448  ? 59  PRO C CD    1 
ATOM   2465 N  N     . GLU C 1 60  ? 21.49433  31.31736 7.26793   1.000 125.08269 ? 60  GLU C N     1 
ATOM   2466 C  CA    . GLU C 1 60  ? 20.76135  30.91112 8.45881   1.000 118.90274 ? 60  GLU C CA    1 
ATOM   2467 C  C     . GLU C 1 60  ? 19.76328  31.98826 8.86418   1.000 112.69415 ? 60  GLU C C     1 
ATOM   2468 O  O     . GLU C 1 60  ? 20.03777  33.18694 8.75936   1.000 110.84123 ? 60  GLU C O     1 
ATOM   2469 C  CB    . GLU C 1 60  ? 21.73636  30.62770 9.60347   1.000 128.24247 ? 60  GLU C CB    1 
ATOM   2470 C  CG    . GLU C 1 60  ? 21.07941  30.19379 10.90443  1.000 135.22040 ? 60  GLU C CG    1 
ATOM   2471 C  CD    . GLU C 1 60  ? 21.41140  31.11856 12.06026  1.000 146.35240 ? 60  GLU C CD    1 
ATOM   2472 O  OE1   . GLU C 1 60  ? 22.11081  32.12844 11.83351  1.000 147.00127 ? 60  GLU C OE1   1 
ATOM   2473 O  OE2   . GLU C 1 60  ? 20.97347  30.83612 13.19552  1.000 150.20656 ? 60  GLU C OE2   1 
ATOM   2474 N  N     . GLY C 1 61  ? 18.59145  31.55178 9.32214   1.000 109.06809 ? 61  GLY C N     1 
ATOM   2475 C  CA    . GLY C 1 61  ? 17.52899  32.45618 9.69614   1.000 106.70159 ? 61  GLY C CA    1 
ATOM   2476 C  C     . GLY C 1 61  ? 16.61112  32.86402 8.56536   1.000 100.51019 ? 61  GLY C C     1 
ATOM   2477 O  O     . GLY C 1 61  ? 15.61179  33.54964 8.81748   1.000 96.84847  ? 61  GLY C O     1 
ATOM   2478 N  N     . TYR C 1 62  ? 16.91467  32.46734 7.33205   1.000 101.83292 ? 62  TYR C N     1 
ATOM   2479 C  CA    . TYR C 1 62  ? 16.09617  32.79050 6.17542   1.000 95.49804  ? 62  TYR C CA    1 
ATOM   2480 C  C     . TYR C 1 62  ? 15.72462  31.50755 5.44598   1.000 89.95545  ? 62  TYR C C     1 
ATOM   2481 O  O     . TYR C 1 62  ? 16.38936  30.47651 5.57830   1.000 92.71708  ? 62  TYR C O     1 
ATOM   2482 C  CB    . TYR C 1 62  ? 16.82193  33.74795 5.22046   1.000 90.02611  ? 62  TYR C CB    1 
ATOM   2483 C  CG    . TYR C 1 62  ? 17.25866  35.04323 5.86659   1.000 98.55599  ? 62  TYR C CG    1 
ATOM   2484 C  CD1   . TYR C 1 62  ? 16.41403  36.14527 5.89668   1.000 101.07031 ? 62  TYR C CD1   1 
ATOM   2485 C  CD2   . TYR C 1 62  ? 18.51615  35.16533 6.44451   1.000 103.51096 ? 62  TYR C CD2   1 
ATOM   2486 C  CE1   . TYR C 1 62  ? 16.80708  37.33217 6.48445   1.000 105.30887 ? 62  TYR C CE1   1 
ATOM   2487 C  CE2   . TYR C 1 62  ? 18.91895  36.34979 7.03533   1.000 107.42740 ? 62  TYR C CE2   1 
ATOM   2488 C  CZ    . TYR C 1 62  ? 18.05939  37.43014 7.05163   1.000 113.07146 ? 62  TYR C CZ    1 
ATOM   2489 O  OH    . TYR C 1 62  ? 18.45034  38.61335 7.63646   1.000 108.92031 ? 62  TYR C OH    1 
ATOM   2490 N  N     . GLU C 1 63  ? 14.64623  31.58200 4.67150   1.000 81.57566  ? 63  GLU C N     1 
ATOM   2491 C  CA    . GLU C 1 63  ? 14.15817  30.44866 3.90371   1.000 79.60641  ? 63  GLU C CA    1 
ATOM   2492 C  C     . GLU C 1 63  ? 13.91390  30.87752 2.46449   1.000 80.41597  ? 63  GLU C C     1 
ATOM   2493 O  O     . GLU C 1 63  ? 13.93615  32.06466 2.12965   1.000 84.43060  ? 63  GLU C O     1 
ATOM   2494 C  CB    . GLU C 1 63  ? 12.86958  29.87121 4.50372   1.000 79.09858  ? 63  GLU C CB    1 
ATOM   2495 C  CG    . GLU C 1 63  ? 11.67255  30.79776 4.39792   1.000 78.00389  ? 63  GLU C CG    1 
ATOM   2496 C  CD    . GLU C 1 63  ? 10.36062  30.08541 4.65410   1.000 80.13209  ? 63  GLU C CD    1 
ATOM   2497 O  OE1   . GLU C 1 63  ? 10.37579  28.84772 4.82298   1.000 80.69125  ? 63  GLU C OE1   1 
ATOM   2498 O  OE2   . GLU C 1 63  ? 9.31214   30.76318 4.68239   1.000 82.56381  ? 63  GLU C OE2   1 
ATOM   2499 N  N     . GLY C 1 64  ? 13.67581  29.89030 1.61113   1.000 72.31720  ? 64  GLY C N     1 
ATOM   2500 C  CA    . GLY C 1 64  ? 13.34203  30.12037 0.21406   1.000 73.51237  ? 64  GLY C CA    1 
ATOM   2501 C  C     . GLY C 1 64  ? 11.92740  29.64581 -0.06631  1.000 72.55593  ? 64  GLY C C     1 
ATOM   2502 O  O     . GLY C 1 64  ? 11.52879  28.56469 0.37465   1.000 72.39991  ? 64  GLY C O     1 
ATOM   2503 N  N     . GLN C 1 65  ? 11.17430  30.46015 -0.80024  1.000 69.55495  ? 65  GLN C N     1 
ATOM   2504 C  CA    . GLN C 1 65  ? 9.79103   30.15570 -1.14242  1.000 62.44681  ? 65  GLN C CA    1 
ATOM   2505 C  C     . GLN C 1 65  ? 9.63999   30.15504 -2.65496  1.000 68.91735  ? 65  GLN C C     1 
ATOM   2506 O  O     . GLN C 1 65  ? 9.80781   31.19624 -3.29888  1.000 69.53891  ? 65  GLN C O     1 
ATOM   2507 C  CB    . GLN C 1 65  ? 8.83010   31.16470 -0.51138  1.000 59.87827  ? 65  GLN C CB    1 
ATOM   2508 C  CG    . GLN C 1 65  ? 8.83964   31.17452 1.00559   1.000 67.63375  ? 65  GLN C CG    1 
ATOM   2509 C  CD    . GLN C 1 65  ? 7.87015   32.18620 1.58269   1.000 70.43680  ? 65  GLN C CD    1 
ATOM   2510 O  OE1   . GLN C 1 65  ? 6.84611   32.50107 0.97469   1.000 68.24669  ? 65  GLN C OE1   1 
ATOM   2511 N  NE2   . GLN C 1 65  ? 8.19221   32.70709 2.76029   1.000 59.91761  ? 65  GLN C NE2   1 
ATOM   2512 N  N     . VAL C 1 66  ? 9.32911   28.99192 -3.21703  1.000 64.94340  ? 66  VAL C N     1 
ATOM   2513 C  CA    . VAL C 1 66  ? 8.99795   28.89533 -4.63387  1.000 64.36072  ? 66  VAL C CA    1 
ATOM   2514 C  C     . VAL C 1 66  ? 7.56325   29.37313 -4.81347  1.000 63.67438  ? 66  VAL C C     1 
ATOM   2515 O  O     . VAL C 1 66  ? 6.63011   28.78594 -4.25610  1.000 57.80039  ? 66  VAL C O     1 
ATOM   2516 C  CB    . VAL C 1 66  ? 9.17631   27.46177 -5.15237  1.000 57.99619  ? 66  VAL C CB    1 
ATOM   2517 C  CG1   . VAL C 1 66  ? 8.74331   27.37036 -6.60614  1.000 57.02262  ? 66  VAL C CG1   1 
ATOM   2518 C  CG2   . VAL C 1 66  ? 10.62096  27.01897 -4.99411  1.000 60.31980  ? 66  VAL C CG2   1 
ATOM   2519 N  N     . ARG C 1 67  ? 7.38659   30.44790 -5.57982  1.000 66.80745  ? 67  ARG C N     1 
ATOM   2520 C  CA    . ARG C 1 67  ? 6.08339   31.06235 -5.76723  1.000 61.49782  ? 67  ARG C CA    1 
ATOM   2521 C  C     . ARG C 1 67  ? 5.69200   31.05835 -7.24156  1.000 68.46745  ? 67  ARG C C     1 
ATOM   2522 O  O     . ARG C 1 67  ? 6.56112   31.04656 -8.11960  1.000 68.02654  ? 67  ARG C O     1 
ATOM   2523 C  CB    . ARG C 1 67  ? 6.07440   32.50204 -5.23615  1.000 68.05104  ? 67  ARG C CB    1 
ATOM   2524 C  CG    . ARG C 1 67  ? 6.26122   32.60457 -3.72992  1.000 63.98174  ? 67  ARG C CG    1 
ATOM   2525 C  CD    . ARG C 1 67  ? 6.26303   34.05431 -3.27355  1.000 62.54261  ? 67  ARG C CD    1 
ATOM   2526 N  NE    . ARG C 1 67  ? 6.36298   34.17681 -1.82395  1.000 62.94482  ? 67  ARG C NE    1 
ATOM   2527 C  CZ    . ARG C 1 67  ? 6.42187   35.33028 -1.17214  1.000 64.39215  ? 67  ARG C CZ    1 
ATOM   2528 N  NH1   . ARG C 1 67  ? 6.39835   36.48802 -1.81194  1.000 73.68902  ? 67  ARG C NH1   1 
ATOM   2529 N  NH2   . ARG C 1 67  ? 6.50783   35.32209 0.15492   1.000 71.19774  ? 67  ARG C NH2   1 
ATOM   2530 N  N     . PRO C 1 68  ? 4.39538   31.05697 -7.54401  1.000 60.95008  ? 68  PRO C N     1 
ATOM   2531 C  CA    . PRO C 1 68  ? 3.96878   31.02462 -8.94605  1.000 64.01630  ? 68  PRO C CA    1 
ATOM   2532 C  C     . PRO C 1 68  ? 4.19621   32.35496 -9.64540  1.000 73.55536  ? 68  PRO C C     1 
ATOM   2533 O  O     . PRO C 1 68  ? 4.23985   33.41880 -9.02248  1.000 69.46316  ? 68  PRO C O     1 
ATOM   2534 C  CB    . PRO C 1 68  ? 2.47014   30.70363 -8.85703  1.000 63.26448  ? 68  PRO C CB    1 
ATOM   2535 C  CG    . PRO C 1 68  ? 2.24617   30.21394 -7.45797  1.000 67.75618  ? 68  PRO C CG    1 
ATOM   2536 C  CD    . PRO C 1 68  ? 3.25613   30.92539 -6.62296  1.000 61.29682  ? 68  PRO C CD    1 
ATOM   2537 N  N     . ARG C 1 69  ? 4.33938   32.27884 -10.96594 1.000 71.54685  ? 69  ARG C N     1 
ATOM   2538 C  CA    . ARG C 1 69  ? 4.44764   33.47215 -11.79261 1.000 77.99296  ? 69  ARG C CA    1 
ATOM   2539 C  C     . ARG C 1 69  ? 3.05741   33.99018 -12.13149 1.000 74.00404  ? 69  ARG C C     1 
ATOM   2540 O  O     . ARG C 1 69  ? 2.18874   33.22381 -12.55831 1.000 77.54951  ? 69  ARG C O     1 
ATOM   2541 C  CB    . ARG C 1 69  ? 5.22297   33.17315 -13.07463 1.000 74.37703  ? 69  ARG C CB    1 
ATOM   2542 C  CG    . ARG C 1 69  ? 6.71939   33.03284 -12.87979 1.000 81.44571  ? 69  ARG C CG    1 
ATOM   2543 C  CD    . ARG C 1 69  ? 7.44446   33.13080 -14.20790 1.000 81.97507  ? 69  ARG C CD    1 
ATOM   2544 N  NE    . ARG C 1 69  ? 7.01951   34.30405 -14.96144 1.000 96.05214  ? 69  ARG C NE    1 
ATOM   2545 C  CZ    . ARG C 1 69  ? 7.52845   35.51839 -14.80685 1.000 99.09329  ? 69  ARG C CZ    1 
ATOM   2546 N  NH1   . ARG C 1 69  ? 8.49427   35.75731 -13.93449 1.000 96.41556  ? 69  ARG C NH1   1 
ATOM   2547 N  NH2   . ARG C 1 69  ? 7.05508   36.51847 -15.54458 1.000 98.87282  ? 69  ARG C NH2   1 
ATOM   2548 N  N     . SER C 1 70  ? 2.84953   35.29515 -11.94375 1.000 64.02044  ? 70  SER C N     1 
ATOM   2549 C  CA    . SER C 1 70  ? 1.54229   35.87966 -12.22604 1.000 76.74662  ? 70  SER C CA    1 
ATOM   2550 C  C     . SER C 1 70  ? 1.20734   35.79682 -13.71003 1.000 72.81245  ? 70  SER C C     1 
ATOM   2551 O  O     . SER C 1 70  ? 0.04138   35.61784 -14.08217 1.000 66.35772  ? 70  SER C O     1 
ATOM   2552 C  CB    . SER C 1 70  ? 1.50242   37.33018 -11.74733 1.000 79.64477  ? 70  SER C CB    1 
ATOM   2553 O  OG    . SER C 1 70  ? 2.49909   38.10490 -12.39155 1.000 88.90866  ? 70  SER C OG    1 
ATOM   2554 N  N     . GLY C 1 71  ? 2.21408   35.92570 -14.57085 1.000 71.34817  ? 71  GLY C N     1 
ATOM   2555 C  CA    . GLY C 1 71  ? 2.00197   35.85408 -16.00283 1.000 75.03218  ? 71  GLY C CA    1 
ATOM   2556 C  C     . GLY C 1 71  ? 1.52120   34.49435 -16.46399 1.000 75.74741  ? 71  GLY C C     1 
ATOM   2557 O  O     . GLY C 1 71  ? 0.43309   34.37751 -17.03571 1.000 74.05108  ? 71  GLY C O     1 
ATOM   2558 N  N     . LEU C 1 72  ? 2.32246   33.45487 -16.21250 1.000 73.34581  ? 72  LEU C N     1 
ATOM   2559 C  CA    . LEU C 1 72  ? 1.94062   32.10990 -16.63095 1.000 79.60180  ? 72  LEU C CA    1 
ATOM   2560 C  C     . LEU C 1 72  ? 0.65051   31.65547 -15.96225 1.000 78.06545  ? 72  LEU C C     1 
ATOM   2561 O  O     . LEU C 1 72  ? -0.08789  30.84225 -16.52982 1.000 80.04972  ? 72  LEU C O     1 
ATOM   2562 C  CB    . LEU C 1 72  ? 3.06601   31.12010 -16.32774 1.000 74.77900  ? 72  LEU C CB    1 
ATOM   2563 C  CG    . LEU C 1 72  ? 4.39879   31.33916 -17.04516 1.000 88.59202  ? 72  LEU C CG    1 
ATOM   2564 C  CD1   . LEU C 1 72  ? 5.33026   30.16207 -16.79881 1.000 78.89150  ? 72  LEU C CD1   1 
ATOM   2565 C  CD2   . LEU C 1 72  ? 4.18445   31.55967 -18.53560 1.000 87.29086  ? 72  LEU C CD2   1 
ATOM   2566 N  N     . ALA C 1 73  ? 0.36033   32.16624 -14.76387 1.000 71.68912  ? 73  ALA C N     1 
ATOM   2567 C  CA    . ALA C 1 73  ? -0.86491  31.77958 -14.07265 1.000 73.72069  ? 73  ALA C CA    1 
ATOM   2568 C  C     . ALA C 1 73  ? -2.09632  32.25748 -14.82960 1.000 80.49707  ? 73  ALA C C     1 
ATOM   2569 O  O     . ALA C 1 73  ? -3.04227  31.49273 -15.04707 1.000 77.43320  ? 73  ALA C O     1 
ATOM   2570 C  CB    . ALA C 1 73  ? -0.86216  32.32928 -12.64629 1.000 71.22061  ? 73  ALA C CB    1 
ATOM   2571 N  N     . TRP C 1 74  ? -2.10155  33.52187 -15.24885 1.000 83.75875  ? 74  TRP C N     1 
ATOM   2572 C  CA    . TRP C 1 74  ? -3.29003  34.05782 -15.90005 1.000 85.45059  ? 74  TRP C CA    1 
ATOM   2573 C  C     . TRP C 1 74  ? -3.35458  33.66204 -17.36985 1.000 77.90071  ? 74  TRP C C     1 
ATOM   2574 O  O     . TRP C 1 74  ? -4.41448  33.26236 -17.86435 1.000 87.93289  ? 74  TRP C O     1 
ATOM   2575 C  CB    . TRP C 1 74  ? -3.33984  35.57872 -15.75085 1.000 84.65213  ? 74  TRP C CB    1 
ATOM   2576 C  CG    . TRP C 1 74  ? -4.47008  36.20865 -16.51172 1.000 87.59469  ? 74  TRP C CG    1 
ATOM   2577 C  CD1   . TRP C 1 74  ? -4.39084  37.27041 -17.36439 1.000 84.97160  ? 74  TRP C CD1   1 
ATOM   2578 C  CD2   . TRP C 1 74  ? -5.84705  35.80337 -16.50371 1.000 89.60653  ? 74  TRP C CD2   1 
ATOM   2579 N  NE1   . TRP C 1 74  ? -5.63148  37.55867 -17.87915 1.000 91.24514  ? 74  TRP C NE1   1 
ATOM   2580 C  CE2   . TRP C 1 74  ? -6.54185  36.67193 -17.36750 1.000 90.72323  ? 74  TRP C CE2   1 
ATOM   2581 C  CE3   . TRP C 1 74  ? -6.56014  34.79491 -15.84577 1.000 88.49545  ? 74  TRP C CE3   1 
ATOM   2582 C  CZ2   . TRP C 1 74  ? -7.91182  36.56207 -17.59162 1.000 98.42490  ? 74  TRP C CZ2   1 
ATOM   2583 C  CZ3   . TRP C 1 74  ? -7.91750  34.68690 -16.07133 1.000 90.13166  ? 74  TRP C CZ3   1 
ATOM   2584 C  CH2   . TRP C 1 74  ? -8.57998  35.56547 -16.93528 1.000 97.95627  ? 74  TRP C CH2   1 
ATOM   2585 N  N     . LYS C 1 75  ? -2.23088  33.76252 -18.08234 1.000 86.25491  ? 75  LYS C N     1 
ATOM   2586 C  CA    . LYS C 1 75  ? -2.24217  33.48607 -19.51569 1.000 89.51999  ? 75  LYS C CA    1 
ATOM   2587 C  C     . LYS C 1 75  ? -2.54641  32.02104 -19.80416 1.000 90.24538  ? 75  LYS C C     1 
ATOM   2588 O  O     . LYS C 1 75  ? -3.31731  31.71227 -20.72001 1.000 85.66860  ? 75  LYS C O     1 
ATOM   2589 C  CB    . LYS C 1 75  ? -0.90309  33.87542 -20.13947 1.000 93.62881  ? 75  LYS C CB    1 
ATOM   2590 C  CG    . LYS C 1 75  ? -0.51682  35.33392 -19.96359 1.000 91.99280  ? 75  LYS C CG    1 
ATOM   2591 C  CD    . LYS C 1 75  ? 0.85802   35.59733 -20.55832 1.000 95.59279  ? 75  LYS C CD    1 
ATOM   2592 C  CE    . LYS C 1 75  ? 1.89635   34.64769 -19.97763 1.000 100.20131 ? 75  LYS C CE    1 
ATOM   2593 N  NZ    . LYS C 1 75  ? 3.22914   34.79973 -20.62393 1.000 110.68919 ? 75  LYS C NZ    1 
ATOM   2594 N  N     . LYS C 1 76  ? -1.95697  31.10393 -19.03527 1.000 90.80247  ? 76  LYS C N     1 
ATOM   2595 C  CA    . LYS C 1 76  ? -2.02377  29.68561 -19.35118 1.000 88.32253  ? 76  LYS C CA    1 
ATOM   2596 C  C     . LYS C 1 76  ? -2.60566  28.81556 -18.24625 1.000 82.60705  ? 76  LYS C C     1 
ATOM   2597 O  O     . LYS C 1 76  ? -2.90651  27.64538 -18.50718 1.000 86.43921  ? 76  LYS C O     1 
ATOM   2598 C  CB    . LYS C 1 76  ? -0.62529  29.15679 -19.70778 1.000 78.27635  ? 76  LYS C CB    1 
ATOM   2599 C  CG    . LYS C 1 76  ? 0.00404   29.83380 -20.91033 1.000 88.23862  ? 76  LYS C CG    1 
ATOM   2600 C  CD    . LYS C 1 76  ? 1.41516   29.32652 -21.15239 1.000 86.83910  ? 76  LYS C CD    1 
ATOM   2601 C  CE    . LYS C 1 76  ? 1.98175   29.88475 -22.44669 1.000 79.86517  ? 76  LYS C CE    1 
ATOM   2602 N  NZ    . LYS C 1 76  ? 1.94401   31.37413 -22.46211 1.000 99.85420  ? 76  LYS C NZ    1 
ATOM   2603 N  N     . GLY C 1 77  ? -2.77641  29.33518 -17.03414 1.000 79.10636  ? 77  GLY C N     1 
ATOM   2604 C  CA    . GLY C 1 77  ? -3.25315  28.51307 -15.94178 1.000 82.00374  ? 77  GLY C CA    1 
ATOM   2605 C  C     . GLY C 1 77  ? -2.18628  27.70879 -15.23645 1.000 75.53743  ? 77  GLY C C     1 
ATOM   2606 O  O     . GLY C 1 77  ? -2.52299  26.86722 -14.39603 1.000 77.57062  ? 77  GLY C O     1 
ATOM   2607 N  N     . LEU C 1 78  ? -0.91316  27.93352 -15.55287 1.000 70.49558  ? 78  LEU C N     1 
ATOM   2608 C  CA    . LEU C 1 78  ? 0.17518   27.23057 -14.88899 1.000 68.77077  ? 78  LEU C CA    1 
ATOM   2609 C  C     . LEU C 1 78  ? 0.42983   27.82103 -13.51082 1.000 70.77102  ? 78  LEU C C     1 
ATOM   2610 O  O     . LEU C 1 78  ? 0.47111   29.04168 -13.34008 1.000 73.47946  ? 78  LEU C O     1 
ATOM   2611 C  CB    . LEU C 1 78  ? 1.45460   27.30976 -15.72063 1.000 68.69597  ? 78  LEU C CB    1 
ATOM   2612 C  CG    . LEU C 1 78  ? 1.55489   26.40867 -16.94780 1.000 85.70056  ? 78  LEU C CG    1 
ATOM   2613 C  CD1   . LEU C 1 78  ? 2.78931   26.77238 -17.74944 1.000 83.94598  ? 78  LEU C CD1   1 
ATOM   2614 C  CD2   . LEU C 1 78  ? 1.59572   24.94939 -16.52646 1.000 71.63321  ? 78  LEU C CD2   1 
ATOM   2615 N  N     . THR C 1 79  ? 0.61401   26.94689 -12.52606 1.000 64.38645  ? 79  THR C N     1 
ATOM   2616 C  CA    . THR C 1 79  ? 0.92031   27.39374 -11.17736 1.000 64.54359  ? 79  THR C CA    1 
ATOM   2617 C  C     . THR C 1 79  ? 1.75639   26.32831 -10.48495 1.000 65.56038  ? 79  THR C C     1 
ATOM   2618 O  O     . THR C 1 79  ? 1.82713   25.17904 -10.92877 1.000 65.01161  ? 79  THR C O     1 
ATOM   2619 C  CB    . THR C 1 79  ? -0.35435  27.69112 -10.37708 1.000 60.40406  ? 79  THR C CB    1 
ATOM   2620 O  OG1   . THR C 1 79  ? -0.03015  28.51276 -9.24933  1.000 62.29510  ? 79  THR C OG1   1 
ATOM   2621 C  CG2   . THR C 1 79  ? -0.99101  26.39940 -9.88691  1.000 65.81650  ? 79  THR C CG2   1 
ATOM   2622 N  N     . VAL C 1 80  ? 2.39844   26.72800 -9.39289  1.000 64.50785  ? 80  VAL C N     1 
ATOM   2623 C  CA    . VAL C 1 80  ? 3.20074   25.80572 -8.59816  1.000 57.84156  ? 80  VAL C CA    1 
ATOM   2624 C  C     . VAL C 1 80  ? 2.27585   25.00316 -7.69269  1.000 61.08824  ? 80  VAL C C     1 
ATOM   2625 O  O     . VAL C 1 80  ? 1.47433   25.57073 -6.94085  1.000 64.15621  ? 80  VAL C O     1 
ATOM   2626 C  CB    . VAL C 1 80  ? 4.26158   26.56676 -7.78867  1.000 61.93785  ? 80  VAL C CB    1 
ATOM   2627 C  CG1   . VAL C 1 80  ? 5.08527   25.59957 -6.95699  1.000 61.08985  ? 80  VAL C CG1   1 
ATOM   2628 C  CG2   . VAL C 1 80  ? 5.15782   27.37418 -8.72112  1.000 59.72538  ? 80  VAL C CG2   1 
ATOM   2629 N  N     . LEU C 1 81  ? 2.38694   23.67451 -7.76344  1.000 62.54450  ? 81  LEU C N     1 
ATOM   2630 C  CA    . LEU C 1 81  ? 1.43474   22.81101 -7.07153  1.000 58.66228  ? 81  LEU C CA    1 
ATOM   2631 C  C     . LEU C 1 81  ? 1.57891   22.91495 -5.55811  1.000 66.34690  ? 81  LEU C C     1 
ATOM   2632 O  O     . LEU C 1 81  ? 0.57580   22.98060 -4.83729  1.000 58.99195  ? 81  LEU C O     1 
ATOM   2633 C  CB    . LEU C 1 81  ? 1.61397   21.36489 -7.53354  1.000 63.83075  ? 81  LEU C CB    1 
ATOM   2634 C  CG    . LEU C 1 81  ? 0.62343   20.33751 -6.98473  1.000 69.08674  ? 81  LEU C CG    1 
ATOM   2635 C  CD1   . LEU C 1 81  ? -0.80534  20.80486 -7.20721  1.000 72.34309  ? 81  LEU C CD1   1 
ATOM   2636 C  CD2   . LEU C 1 81  ? 0.84934   18.97967 -7.63293  1.000 65.71518  ? 81  LEU C CD2   1 
ATOM   2637 N  N     . ASN C 1 82  ? 2.81460   22.93134 -5.05699  1.000 67.13687  ? 82  ASN C N     1 
ATOM   2638 C  CA    . ASN C 1 82  ? 3.08430   23.00971 -3.62633  1.000 58.69475  ? 82  ASN C CA    1 
ATOM   2639 C  C     . ASN C 1 82  ? 3.37642   24.43476 -3.16885  1.000 59.94049  ? 82  ASN C C     1 
ATOM   2640 O  O     . ASN C 1 82  ? 4.14033   24.63597 -2.21878  1.000 54.77855  ? 82  ASN C O     1 
ATOM   2641 C  CB    . ASN C 1 82  ? 4.24728   22.08930 -3.25586  1.000 63.61006  ? 82  ASN C CB    1 
ATOM   2642 C  CG    . ASN C 1 82  ? 5.54661   22.49088 -3.92990  1.000 57.63562  ? 82  ASN C CG    1 
ATOM   2643 O  OD1   . ASN C 1 82  ? 5.55969   22.87470 -5.09870  1.000 63.51327  ? 82  ASN C OD1   1 
ATOM   2644 N  ND2   . ASN C 1 82  ? 6.64725   22.40966 -3.19087  1.000 58.65742  ? 82  ASN C ND2   1 
ATOM   2645 N  N     . ALA C 1 83  ? 2.77971   25.42631 -3.82250  1.000 61.20518  ? 83  ALA C N     1 
ATOM   2646 C  CA    . ALA C 1 83  ? 3.09618   26.81153 -3.51382  1.000 59.69804  ? 83  ALA C CA    1 
ATOM   2647 C  C     . ALA C 1 83  ? 2.52166   27.19768 -2.15266  1.000 61.09978  ? 83  ALA C C     1 
ATOM   2648 O  O     . ALA C 1 83  ? 1.38022   26.84894 -1.83754  1.000 68.03977  ? 83  ALA C O     1 
ATOM   2649 C  CB    . ALA C 1 83  ? 2.54783   27.74217 -4.59461  1.000 53.92760  ? 83  ALA C CB    1 
ATOM   2650 N  N     . PRO C 1 84  ? 3.29068   27.90862 -1.31991  1.000 60.95112  ? 84  PRO C N     1 
ATOM   2651 C  CA    . PRO C 1 84  ? 4.69064   28.29930 -1.53618  1.000 61.18638  ? 84  PRO C CA    1 
ATOM   2652 C  C     . PRO C 1 84  ? 5.64835   27.15206 -1.21896  1.000 62.24178  ? 84  PRO C C     1 
ATOM   2653 O  O     . PRO C 1 84  ? 5.66565   26.64203 -0.10274  1.000 61.53588  ? 84  PRO C O     1 
ATOM   2654 C  CB    . PRO C 1 84  ? 4.86016   29.49578 -0.58901  1.000 57.63546  ? 84  PRO C CB    1 
ATOM   2655 C  CG    . PRO C 1 84  ? 3.90836   29.21024 0.53886   1.000 57.84226  ? 84  PRO C CG    1 
ATOM   2656 C  CD    . PRO C 1 84  ? 2.72682   28.52115 -0.10167  1.000 56.79454  ? 84  PRO C CD    1 
ATOM   2657 N  N     . GLY C 1 85  ? 6.44637   26.72828 -2.19573  1.000 60.76482  ? 85  GLY C N     1 
ATOM   2658 C  CA    . GLY C 1 85  ? 7.36951   25.63203 -1.97329  1.000 57.01194  ? 85  GLY C CA    1 
ATOM   2659 C  C     . GLY C 1 85  ? 8.44856   26.02701 -0.98299  1.000 63.10901  ? 85  GLY C C     1 
ATOM   2660 O  O     . GLY C 1 85  ? 9.15887   27.02585 -1.19124  1.000 69.84461  ? 85  GLY C O     1 
ATOM   2661 N  N     . THR C 1 86  ? 8.59462   25.25434 0.08709   1.000 63.94783  ? 86  THR C N     1 
ATOM   2662 C  CA    . THR C 1 86  ? 9.51130   25.59490 1.16768   1.000 71.68939  ? 86  THR C CA    1 
ATOM   2663 C  C     . THR C 1 86  ? 10.90483  25.06691 0.84176   1.000 69.56087  ? 86  THR C C     1 
ATOM   2664 O  O     . THR C 1 86  ? 11.09422  23.85671 0.68157   1.000 72.53162  ? 86  THR C O     1 
ATOM   2665 C  CB    . THR C 1 86  ? 9.01941   25.02434 2.49852   1.000 76.27837  ? 86  THR C CB    1 
ATOM   2666 O  OG1   . THR C 1 86  ? 7.59980   25.18999 2.59599   1.000 82.11917  ? 86  THR C OG1   1 
ATOM   2667 C  CG2   . THR C 1 86  ? 9.68428   25.74077 3.65693   1.000 75.09259  ? 86  THR C CG2   1 
ATOM   2668 N  N     . ILE C 1 87  ? 11.87359  25.97229 0.74679   1.000 66.32912  ? 87  ILE C N     1 
ATOM   2669 C  CA    . ILE C 1 87  ? 13.27579  25.62439 0.55322   1.000 67.78787  ? 87  ILE C CA    1 
ATOM   2670 C  C     . ILE C 1 87  ? 13.98831  25.89760 1.86966   1.000 71.65725  ? 87  ILE C C     1 
ATOM   2671 O  O     . ILE C 1 87  ? 14.23350  27.05743 2.22385   1.000 72.04732  ? 87  ILE C O     1 
ATOM   2672 C  CB    . ILE C 1 87  ? 13.91359  26.41541 -0.59680  1.000 74.86100  ? 87  ILE C CB    1 
ATOM   2673 C  CG1   . ILE C 1 87  ? 13.04265  26.33891 -1.85299  1.000 75.64523  ? 87  ILE C CG1   1 
ATOM   2674 C  CG2   . ILE C 1 87  ? 15.30802  25.88324 -0.89672  1.000 67.83790  ? 87  ILE C CG2   1 
ATOM   2675 C  CD1   . ILE C 1 87  ? 12.98461  24.96464 -2.47350  1.000 67.64015  ? 87  ILE C CD1   1 
ATOM   2676 N  N     . ASP C 1 88  ? 14.32060  24.83422 2.59540   1.000 68.61008  ? 88  ASP C N     1 
ATOM   2677 C  CA    . ASP C 1 88  ? 14.96150  24.97698 3.89182   1.000 77.46235  ? 88  ASP C CA    1 
ATOM   2678 C  C     . ASP C 1 88  ? 16.38817  25.50139 3.73613   1.000 81.25644  ? 88  ASP C C     1 
ATOM   2679 O  O     . ASP C 1 88  ? 17.02780  25.35353 2.69113   1.000 80.10639  ? 88  ASP C O     1 
ATOM   2680 C  CB    . ASP C 1 88  ? 14.95812  23.64127 4.63349   1.000 82.29872  ? 88  ASP C CB    1 
ATOM   2681 C  CG    . ASP C 1 88  ? 13.55422  23.15745 4.95012   1.000 85.72503  ? 88  ASP C CG    1 
ATOM   2682 O  OD1   . ASP C 1 88  ? 12.80946  23.89432 5.63020   1.000 83.79743  ? 88  ASP C OD1   1 
ATOM   2683 O  OD2   . ASP C 1 88  ? 13.18953  22.04779 4.50700   1.000 81.66124  ? 88  ASP C OD2   1 
ATOM   2684 N  N     . ALA C 1 89  ? 16.88398  26.12840 4.80574   1.000 89.10616  ? 89  ALA C N     1 
ATOM   2685 C  CA    . ALA C 1 89  ? 18.19598  26.76671 4.75207   1.000 86.27736  ? 89  ALA C CA    1 
ATOM   2686 C  C     . ALA C 1 89  ? 19.31729  25.74408 4.61558   1.000 84.66016  ? 89  ALA C C     1 
ATOM   2687 O  O     . ALA C 1 89  ? 20.31720  26.00268 3.93605   1.000 90.60316  ? 89  ALA C O     1 
ATOM   2688 C  CB    . ALA C 1 89  ? 18.41072  27.62956 5.99255   1.000 93.64292  ? 89  ALA C CB    1 
ATOM   2689 N  N     . ASP C 1 90  ? 19.17230  24.57909 5.24618   1.000 89.52745  ? 90  ASP C N     1 
ATOM   2690 C  CA    . ASP C 1 90  ? 20.19138  23.54060 5.20643   1.000 95.29428  ? 90  ASP C CA    1 
ATOM   2691 C  C     . ASP C 1 90  ? 20.03405  22.60670 4.01316   1.000 96.54060  ? 90  ASP C C     1 
ATOM   2692 O  O     . ASP C 1 90  ? 20.53690  21.47828 4.05074   1.000 91.82927  ? 90  ASP C O     1 
ATOM   2693 C  CB    . ASP C 1 90  ? 20.17690  22.73787 6.50933   1.000 94.65470  ? 90  ASP C CB    1 
ATOM   2694 C  CG    . ASP C 1 90  ? 18.81081  22.15959 6.82653   1.000 92.58827  ? 90  ASP C CG    1 
ATOM   2695 O  OD1   . ASP C 1 90  ? 17.86932  22.35622 6.02907   1.000 90.16347  ? 90  ASP C OD1   1 
ATOM   2696 O  OD2   . ASP C 1 90  ? 18.67954  21.51175 7.88459   1.000 96.66295  ? 90  ASP C OD2   1 
ATOM   2697 N  N     . TYR C 1 91  ? 19.35021  23.04622 2.96148   1.000 88.68383  ? 91  TYR C N     1 
ATOM   2698 C  CA    . TYR C 1 91  ? 19.12998  22.21920 1.78325   1.000 88.67637  ? 91  TYR C CA    1 
ATOM   2699 C  C     . TYR C 1 91  ? 20.29396  22.39789 0.81593   1.000 93.27996  ? 91  TYR C C     1 
ATOM   2700 O  O     . TYR C 1 91  ? 20.56168  23.51365 0.35656   1.000 96.14415  ? 91  TYR C O     1 
ATOM   2701 C  CB    . TYR C 1 91  ? 17.80511  22.57827 1.11322   1.000 82.41618  ? 91  TYR C CB    1 
ATOM   2702 C  CG    . TYR C 1 91  ? 17.48172  21.72648 -0.09128  1.000 88.03098  ? 91  TYR C CG    1 
ATOM   2703 C  CD1   . TYR C 1 91  ? 17.27658  20.35972 0.03756   1.000 81.65842  ? 91  TYR C CD1   1 
ATOM   2704 C  CD2   . TYR C 1 91  ? 17.37392  22.28924 -1.35618  1.000 84.37442  ? 91  TYR C CD2   1 
ATOM   2705 C  CE1   . TYR C 1 91  ? 16.97988  19.57607 -1.05977  1.000 85.82544  ? 91  TYR C CE1   1 
ATOM   2706 C  CE2   . TYR C 1 91  ? 17.07580  21.51341 -2.45957  1.000 80.06063  ? 91  TYR C CE2   1 
ATOM   2707 C  CZ    . TYR C 1 91  ? 16.87936  20.15835 -2.30516  1.000 86.07892  ? 91  TYR C CZ    1 
ATOM   2708 O  OH    . TYR C 1 91  ? 16.58362  19.38171 -3.40077  1.000 81.02568  ? 91  TYR C OH    1 
ATOM   2709 N  N     . ARG C 1 92  ? 20.98453  21.29953 0.51252   1.000 96.26420  ? 92  ARG C N     1 
ATOM   2710 C  CA    . ARG C 1 92  ? 22.11279  21.30988 -0.40850  1.000 94.58843  ? 92  ARG C CA    1 
ATOM   2711 C  C     . ARG C 1 92  ? 21.79603  20.61430 -1.72398  1.000 99.57768  ? 92  ARG C C     1 
ATOM   2712 O  O     . ARG C 1 92  ? 22.69432  20.43716 -2.55311  1.000 100.95730 ? 92  ARG C O     1 
ATOM   2713 C  CB    . ARG C 1 92  ? 23.33716  20.66352 0.24312   1.000 100.19704 ? 92  ARG C CB    1 
ATOM   2714 C  CG    . ARG C 1 92  ? 23.78391  21.35581 1.51376   1.000 105.05204 ? 92  ARG C CG    1 
ATOM   2715 C  CD    . ARG C 1 92  ? 23.83688  22.85586 1.30696   1.000 98.45119  ? 92  ARG C CD    1 
ATOM   2716 N  NE    . ARG C 1 92  ? 23.86555  23.58117 2.56989   1.000 104.02383 ? 92  ARG C NE    1 
ATOM   2717 C  CZ    . ARG C 1 92  ? 23.45198  24.83136 2.71733   1.000 104.99663 ? 92  ARG C CZ    1 
ATOM   2718 N  NH1   . ARG C 1 92  ? 22.95627  25.51662 1.70200   1.000 104.91306 ? 92  ARG C NH1   1 
ATOM   2719 N  NH2   . ARG C 1 92  ? 23.52857  25.40437 3.91496   1.000 111.86079 ? 92  ARG C NH2   1 
ATOM   2720 N  N     . GLY C 1 93  ? 20.54559  20.21422 -1.93524  1.000 93.17228  ? 93  GLY C N     1 
ATOM   2721 C  CA    . GLY C 1 93  ? 20.15913  19.57073 -3.16893  1.000 90.14181  ? 93  GLY C CA    1 
ATOM   2722 C  C     . GLY C 1 93  ? 19.84397  20.56624 -4.26765  1.000 89.49363  ? 93  GLY C C     1 
ATOM   2723 O  O     . GLY C 1 93  ? 19.91379  21.78382 -4.09861  1.000 85.25708  ? 93  GLY C O     1 
ATOM   2724 N  N     . GLU C 1 94  ? 19.49056  20.01930 -5.42754  1.000 82.60125  ? 94  GLU C N     1 
ATOM   2725 C  CA    . GLU C 1 94  ? 19.11292  20.83164 -6.57657  1.000 81.59837  ? 94  GLU C CA    1 
ATOM   2726 C  C     . GLU C 1 94  ? 17.65552  21.25198 -6.44117  1.000 76.89656  ? 94  GLU C C     1 
ATOM   2727 O  O     . GLU C 1 94  ? 16.76757  20.40160 -6.31540  1.000 73.12338  ? 94  GLU C O     1 
ATOM   2728 C  CB    . GLU C 1 94  ? 19.32965  20.05714 -7.87375  1.000 85.54113  ? 94  GLU C CB    1 
ATOM   2729 C  CG    . GLU C 1 94  ? 18.85659  20.78821 -9.11962  1.000 83.20334  ? 94  GLU C CG    1 
ATOM   2730 C  CD    . GLU C 1 94  ? 18.92781  19.92100 -10.35905 1.000 84.14785  ? 94  GLU C CD    1 
ATOM   2731 O  OE1   . GLU C 1 94  ? 19.16310  18.70185 -10.21858 1.000 76.89970  ? 94  GLU C OE1   1 
ATOM   2732 O  OE2   . GLU C 1 94  ? 18.75123  20.45802 -11.47221 1.000 85.22919  ? 94  GLU C OE2   1 
ATOM   2733 N  N     . VAL C 1 95  ? 17.40984  22.56117 -6.47076  1.000 77.34081  ? 95  VAL C N     1 
ATOM   2734 C  CA    . VAL C 1 95  ? 16.05290  23.07229 -6.33054  1.000 74.89611  ? 95  VAL C CA    1 
ATOM   2735 C  C     . VAL C 1 95  ? 15.23756  22.69540 -7.55848  1.000 76.56458  ? 95  VAL C C     1 
ATOM   2736 O  O     . VAL C 1 95  ? 15.64314  22.95387 -8.69910  1.000 77.43815  ? 95  VAL C O     1 
ATOM   2737 C  CB    . VAL C 1 95  ? 16.06962  24.59184 -6.11609  1.000 72.89782  ? 95  VAL C CB    1 
ATOM   2738 C  CG1   . VAL C 1 95  ? 14.65956  25.15231 -6.20064  1.000 66.91512  ? 95  VAL C CG1   1 
ATOM   2739 C  CG2   . VAL C 1 95  ? 16.69756  24.92134 -4.77352  1.000 70.98207  ? 95  VAL C CG2   1 
ATOM   2740 N  N     . LYS C 1 96  ? 14.08378  22.07638 -7.32892  1.000 69.57370  ? 96  LYS C N     1 
ATOM   2741 C  CA    . LYS C 1 96  ? 13.18116  21.66822 -8.39157  1.000 70.50177  ? 96  LYS C CA    1 
ATOM   2742 C  C     . LYS C 1 96  ? 11.82900  22.34332 -8.20568  1.000 69.18799  ? 96  LYS C C     1 
ATOM   2743 O  O     . LYS C 1 96  ? 11.47620  22.78469 -7.10896  1.000 69.98265  ? 96  LYS C O     1 
ATOM   2744 C  CB    . LYS C 1 96  ? 13.01619  20.14477 -8.42327  1.000 66.86566  ? 96  LYS C CB    1 
ATOM   2745 C  CG    . LYS C 1 96  ? 14.30375  19.40084 -8.73052  1.000 71.65647  ? 96  LYS C CG    1 
ATOM   2746 C  CD    . LYS C 1 96  ? 14.05279  17.91944 -8.94157  1.000 81.95912  ? 96  LYS C CD    1 
ATOM   2747 C  CE    . LYS C 1 96  ? 15.10703  17.31159 -9.85462  1.000 81.66631  ? 96  LYS C CE    1 
ATOM   2748 N  NZ    . LYS C 1 96  ? 14.80990  15.88823 -10.17715 1.000 71.49985  ? 96  LYS C NZ    1 
ATOM   2749 N  N     . VAL C 1 97  ? 11.07203  22.42246 -9.29680  1.000 68.45260  ? 97  VAL C N     1 
ATOM   2750 C  CA    . VAL C 1 97  ? 9.78900   23.11287 -9.32153  1.000 59.72887  ? 97  VAL C CA    1 
ATOM   2751 C  C     . VAL C 1 97  ? 8.72020   22.14549 -9.80822  1.000 64.09991  ? 97  VAL C C     1 
ATOM   2752 O  O     . VAL C 1 97  ? 8.92974   21.41346 -10.78179 1.000 69.90766  ? 97  VAL C O     1 
ATOM   2753 C  CB    . VAL C 1 97  ? 9.84071   24.36960 -10.21678 1.000 62.61115  ? 97  VAL C CB    1 
ATOM   2754 C  CG1   . VAL C 1 97  ? 8.48702   25.06477 -10.25044 1.000 61.16937  ? 97  VAL C CG1   1 
ATOM   2755 C  CG2   . VAL C 1 97  ? 10.91872  25.32293 -9.72754  1.000 62.09983  ? 97  VAL C CG2   1 
ATOM   2756 N  N     . ILE C 1 98  ? 7.57634   22.14466 -9.12860  1.000 64.87758  ? 98  ILE C N     1 
ATOM   2757 C  CA    . ILE C 1 98  ? 6.43872   21.30222 -9.48085  1.000 63.44087  ? 98  ILE C CA    1 
ATOM   2758 C  C     . ILE C 1 98  ? 5.37769   22.21085 -10.08839 1.000 62.89875  ? 98  ILE C C     1 
ATOM   2759 O  O     . ILE C 1 98  ? 4.62326   22.87347 -9.36671  1.000 67.02135  ? 98  ILE C O     1 
ATOM   2760 C  CB    . ILE C 1 98  ? 5.88840   20.53839 -8.27159  1.000 60.39592  ? 98  ILE C CB    1 
ATOM   2761 C  CG1   . ILE C 1 98  ? 7.01523   19.81705 -7.53264  1.000 65.24395  ? 98  ILE C CG1   1 
ATOM   2762 C  CG2   . ILE C 1 98  ? 4.81971   19.54878 -8.71390  1.000 47.40326  ? 98  ILE C CG2   1 
ATOM   2763 C  CD1   . ILE C 1 98  ? 6.55510   19.07228 -6.29978  1.000 56.36691  ? 98  ILE C CD1   1 
ATOM   2764 N  N     . LEU C 1 99  ? 5.31469   22.24657 -11.41624 1.000 60.93614  ? 99  LEU C N     1 
ATOM   2765 C  CA    . LEU C 1 99  ? 4.27658   22.98538 -12.11881 1.000 63.39997  ? 99  LEU C CA    1 
ATOM   2766 C  C     . LEU C 1 99  ? 3.10786   22.06434 -12.43413 1.000 60.68530  ? 99  LEU C C     1 
ATOM   2767 O  O     . LEU C 1 99  ? 3.29805   20.89529 -12.78201 1.000 63.57466  ? 99  LEU C O     1 
ATOM   2768 C  CB    . LEU C 1 99  ? 4.81441   23.59608 -13.41368 1.000 57.48531  ? 99  LEU C CB    1 
ATOM   2769 C  CG    . LEU C 1 99  ? 5.78902   24.76688 -13.30289 1.000 68.59953  ? 99  LEU C CG    1 
ATOM   2770 C  CD1   . LEU C 1 99  ? 6.20926   25.21282 -14.69120 1.000 75.91941  ? 99  LEU C CD1   1 
ATOM   2771 C  CD2   . LEU C 1 99  ? 5.16006   25.91790 -12.53596 1.000 56.69763  ? 99  LEU C CD2   1 
ATOM   2772 N  N     . VAL C 1 100 ? 1.89682   22.59885 -12.30512 1.000 62.63670  ? 100 VAL C N     1 
ATOM   2773 C  CA    . VAL C 1 100 ? 0.67749   21.88519 -12.65870 1.000 64.04082  ? 100 VAL C CA    1 
ATOM   2774 C  C     . VAL C 1 100 ? -0.11721  22.74972 -13.62818 1.000 71.28628  ? 100 VAL C C     1 
ATOM   2775 O  O     . VAL C 1 100 ? -0.25691  23.96130 -13.42265 1.000 63.23358  ? 100 VAL C O     1 
ATOM   2776 C  CB    . VAL C 1 100 ? -0.16209  21.52372 -11.41469 1.000 69.10531  ? 100 VAL C CB    1 
ATOM   2777 C  CG1   . VAL C 1 100 ? -0.45724  22.75767 -10.57765 1.000 65.28143  ? 100 VAL C CG1   1 
ATOM   2778 C  CG2   . VAL C 1 100 ? -1.44950  20.81416 -11.82064 1.000 70.84120  ? 100 VAL C CG2   1 
ATOM   2779 N  N     . ASN C 1 101 ? -0.61232  22.13202 -14.69627 1.000 79.19386  ? 101 ASN C N     1 
ATOM   2780 C  CA    . ASN C 1 101 ? -1.41137  22.82849 -15.70135 1.000 72.75867  ? 101 ASN C CA    1 
ATOM   2781 C  C     . ASN C 1 101 ? -2.87857  22.71095 -15.30956 1.000 75.55948  ? 101 ASN C C     1 
ATOM   2782 O  O     . ASN C 1 101 ? -3.50436  21.66604 -15.50331 1.000 81.90840  ? 101 ASN C O     1 
ATOM   2783 C  CB    . ASN C 1 101 ? -1.15403  22.25174 -17.08871 1.000 85.25053  ? 101 ASN C CB    1 
ATOM   2784 C  CG    . ASN C 1 101 ? -2.08725  22.82436 -18.14266 1.000 91.97641  ? 101 ASN C CG    1 
ATOM   2785 O  OD1   . ASN C 1 101 ? -2.60767  23.93057 -17.99525 1.000 88.11752  ? 101 ASN C OD1   1 
ATOM   2786 N  ND2   . ASN C 1 101 ? -2.30440  22.06859 -19.21403 1.000 100.66354 ? 101 ASN C ND2   1 
ATOM   2787 N  N     . LEU C 1 102 ? -3.43230  23.78885 -14.75788 1.000 80.36107  ? 102 LEU C N     1 
ATOM   2788 C  CA    . LEU C 1 102 ? -4.84329  23.84425 -14.40558 1.000 87.90569  ? 102 LEU C CA    1 
ATOM   2789 C  C     . LEU C 1 102 ? -5.67530  24.56700 -15.45572 1.000 84.26117  ? 102 LEU C C     1 
ATOM   2790 O  O     . LEU C 1 102 ? -6.82620  24.92517 -15.18556 1.000 83.60674  ? 102 LEU C O     1 
ATOM   2791 C  CB    . LEU C 1 102 ? -5.02168  24.50259 -13.03645 1.000 77.42340  ? 102 LEU C CB    1 
ATOM   2792 C  CG    . LEU C 1 102 ? -4.48279  23.67682 -11.86573 1.000 79.75546  ? 102 LEU C CG    1 
ATOM   2793 C  CD1   . LEU C 1 102 ? -4.74680  24.36478 -10.53389 1.000 74.96301  ? 102 LEU C CD1   1 
ATOM   2794 C  CD2   . LEU C 1 102 ? -5.08453  22.27914 -11.88040 1.000 76.40855  ? 102 LEU C CD2   1 
ATOM   2795 N  N     . GLY C 1 103 ? -5.11531  24.79381 -16.64473 1.000 99.26147  ? 103 GLY C N     1 
ATOM   2796 C  CA    . GLY C 1 103 ? -5.87221  25.32044 -17.75760 1.000 105.69117 ? 103 GLY C CA    1 
ATOM   2797 C  C     . GLY C 1 103 ? -6.52933  24.21473 -18.56381 1.000 110.53254 ? 103 GLY C C     1 
ATOM   2798 O  O     . GLY C 1 103 ? -6.41753  23.02717 -18.26277 1.000 110.77400 ? 103 GLY C O     1 
ATOM   2799 N  N     . ASN C 1 104 ? -7.22845  24.62838 -19.61713 1.000 109.79327 ? 104 ASN C N     1 
ATOM   2800 C  CA    . ASN C 1 104 ? -7.96078  23.70919 -20.47648 1.000 110.46637 ? 104 ASN C CA    1 
ATOM   2801 C  C     . ASN C 1 104 ? -7.21721  23.37451 -21.76256 1.000 111.13102 ? 104 ASN C C     1 
ATOM   2802 O  O     . ASN C 1 104 ? -7.76803  22.67280 -22.61655 1.000 103.03100 ? 104 ASN C O     1 
ATOM   2803 C  CB    . ASN C 1 104 ? -9.33806  24.29173 -20.81046 1.000 120.09878 ? 104 ASN C CB    1 
ATOM   2804 C  CG    . ASN C 1 104 ? -9.27351  25.75944 -21.18894 1.000 126.82447 ? 104 ASN C CG    1 
ATOM   2805 O  OD1   . ASN C 1 104 ? -8.55846  26.54314 -20.56304 1.000 121.37769 ? 104 ASN C OD1   1 
ATOM   2806 N  ND2   . ASN C 1 104 ? -10.01855 26.13813 -22.22123 1.000 106.52696 ? 104 ASN C ND2   1 
ATOM   2807 N  N     . GLU C 1 105 ? -5.98485  23.84964 -21.91970 1.000 114.51079 ? 105 GLU C N     1 
ATOM   2808 C  CA    . GLU C 1 105 ? -5.21946  23.64539 -23.13819 1.000 113.94137 ? 105 GLU C CA    1 
ATOM   2809 C  C     . GLU C 1 105 ? -3.83708  23.11082 -22.79300 1.000 106.93359 ? 105 GLU C C     1 
ATOM   2810 O  O     . GLU C 1 105 ? -3.37946  23.19841 -21.65084 1.000 104.06430 ? 105 GLU C O     1 
ATOM   2811 C  CB    . GLU C 1 105 ? -5.09150  24.94756 -23.94200 1.000 121.45492 ? 105 GLU C CB    1 
ATOM   2812 C  CG    . GLU C 1 105 ? -6.41757  25.63654 -24.21904 1.000 131.12906 ? 105 GLU C CG    1 
ATOM   2813 C  CD    . GLU C 1 105 ? -6.25535  27.11287 -24.51478 1.000 146.26923 ? 105 GLU C CD    1 
ATOM   2814 O  OE1   . GLU C 1 105 ? -5.12372  27.53452 -24.83360 1.000 150.01053 ? 105 GLU C OE1   1 
ATOM   2815 O  OE2   . GLU C 1 105 ? -7.25802  27.85243 -24.42005 1.000 152.93506 ? 105 GLU C OE2   1 
ATOM   2816 N  N     . GLU C 1 106 ? -3.17342  22.55128 -23.80029 1.000 120.03250 ? 106 GLU C N     1 
ATOM   2817 C  CA    . GLU C 1 106 ? -1.80629  22.08776 -23.61971 1.000 110.87096 ? 106 GLU C CA    1 
ATOM   2818 C  C     . GLU C 1 106 ? -0.85284  23.27497 -23.57450 1.000 108.93580 ? 106 GLU C C     1 
ATOM   2819 O  O     . GLU C 1 106 ? -1.01938  24.25488 -24.30544 1.000 113.46711 ? 106 GLU C O     1 
ATOM   2820 C  CB    . GLU C 1 106 ? -1.41296  21.13291 -24.74667 1.000 115.45991 ? 106 GLU C CB    1 
ATOM   2821 C  CG    . GLU C 1 106 ? -2.36954  19.96428 -24.92258 1.000 127.14842 ? 106 GLU C CG    1 
ATOM   2822 C  CD    . GLU C 1 106 ? -1.66554  18.69172 -25.35076 1.000 131.70627 ? 106 GLU C CD    1 
ATOM   2823 O  OE1   . GLU C 1 106 ? -0.42603  18.71893 -25.50102 1.000 130.80398 ? 106 GLU C OE1   1 
ATOM   2824 O  OE2   . GLU C 1 106 ? -2.35042  17.66227 -25.53095 1.000 121.26034 ? 106 GLU C OE2   1 
ATOM   2825 N  N     . VAL C 1 107 ? 0.14814   23.18822 -22.70361 1.000 88.94058  ? 107 VAL C N     1 
ATOM   2826 C  CA    . VAL C 1 107 ? 1.11981   24.25851 -22.52298 1.000 90.31652  ? 107 VAL C CA    1 
ATOM   2827 C  C     . VAL C 1 107 ? 2.51326   23.70195 -22.76980 1.000 89.94256  ? 107 VAL C C     1 
ATOM   2828 O  O     . VAL C 1 107 ? 2.79814   22.53619 -22.47636 1.000 96.22450  ? 107 VAL C O     1 
ATOM   2829 C  CB    . VAL C 1 107 ? 1.02404   24.89281 -21.11847 1.000 91.96047  ? 107 VAL C CB    1 
ATOM   2830 C  CG1   . VAL C 1 107 ? -0.26459  25.68487 -20.98437 1.000 89.09815  ? 107 VAL C CG1   1 
ATOM   2831 C  CG2   . VAL C 1 107 ? 1.10603   23.81960 -20.04367 1.000 81.99111  ? 107 VAL C CG2   1 
ATOM   2832 N  N     . VAL C 1 108 ? 3.38286   24.54639 -23.31970 1.000 78.84415  ? 108 VAL C N     1 
ATOM   2833 C  CA    . VAL C 1 108 ? 4.75417   24.17656 -23.64402 1.000 86.54044  ? 108 VAL C CA    1 
ATOM   2834 C  C     . VAL C 1 108 ? 5.69603   25.02318 -22.80018 1.000 83.17107  ? 108 VAL C C     1 
ATOM   2835 O  O     . VAL C 1 108 ? 5.59016   26.25523 -22.78677 1.000 80.12221  ? 108 VAL C O     1 
ATOM   2836 C  CB    . VAL C 1 108 ? 5.05433   24.35735 -25.14290 1.000 86.63161  ? 108 VAL C CB    1 
ATOM   2837 C  CG1   . VAL C 1 108 ? 6.39125   23.72486 -25.49218 1.000 86.54243  ? 108 VAL C CG1   1 
ATOM   2838 C  CG2   . VAL C 1 108 ? 3.93311   23.76486 -25.98448 1.000 76.04279  ? 108 VAL C CG2   1 
ATOM   2839 N  N     . ILE C 1 109 ? 6.60778   24.36299 -22.09454 1.000 85.64720  ? 109 ILE C N     1 
ATOM   2840 C  CA    . ILE C 1 109 ? 7.65762   25.03375 -21.33868 1.000 83.08824  ? 109 ILE C CA    1 
ATOM   2841 C  C     . ILE C 1 109 ? 8.94768   24.88435 -22.13081 1.000 88.04517  ? 109 ILE C C     1 
ATOM   2842 O  O     . ILE C 1 109 ? 9.43376   23.76649 -22.34108 1.000 90.01418  ? 109 ILE C O     1 
ATOM   2843 C  CB    . ILE C 1 109 ? 7.79285   24.46216 -19.91745 1.000 90.53210  ? 109 ILE C CB    1 
ATOM   2844 C  CG1   . ILE C 1 109 ? 6.77273   25.10651 -18.97445 1.000 79.76762  ? 109 ILE C CG1   1 
ATOM   2845 C  CG2   . ILE C 1 109 ? 9.18995   24.69648 -19.37026 1.000 85.95410  ? 109 ILE C CG2   1 
ATOM   2846 C  CD1   . ILE C 1 109 ? 5.33330   24.75213 -19.26041 1.000 84.86660  ? 109 ILE C CD1   1 
ATOM   2847 N  N     . GLU C 1 110 ? 9.48858   26.00580 -22.59121 1.000 92.48303  ? 110 GLU C N     1 
ATOM   2848 C  CA    . GLU C 1 110 ? 10.62970  25.99655 -23.48998 1.000 93.97247  ? 110 GLU C CA    1 
ATOM   2849 C  C     . GLU C 1 110 ? 11.93537  25.98637 -22.70029 1.000 90.48876  ? 110 GLU C C     1 
ATOM   2850 O  O     . GLU C 1 110 ? 11.95404  25.85916 -21.47307 1.000 85.87911  ? 110 GLU C O     1 
ATOM   2851 C  CB    . GLU C 1 110 ? 10.56181  27.19130 -24.43618 1.000 90.20160  ? 110 GLU C CB    1 
ATOM   2852 C  CG    . GLU C 1 110 ? 10.08898  26.84143 -25.83190 1.000 100.21637 ? 110 GLU C CG    1 
ATOM   2853 C  CD    . GLU C 1 110 ? 11.13349  26.08294 -26.62745 1.000 108.22343 ? 110 GLU C CD    1 
ATOM   2854 O  OE1   . GLU C 1 110 ? 12.30911  26.05478 -26.20287 1.000 104.13011 ? 110 GLU C OE1   1 
ATOM   2855 O  OE2   . GLU C 1 110 ? 10.77688  25.51695 -27.68137 1.000 106.92172 ? 110 GLU C OE2   1 
ATOM   2856 N  N     . ARG C 1 111 ? 13.04832  26.12004 -23.41573 1.000 99.44037  ? 111 ARG C N     1 
ATOM   2857 C  CA    . ARG C 1 111 ? 14.35285  26.14555 -22.77341 1.000 98.90231  ? 111 ARG C CA    1 
ATOM   2858 C  C     . ARG C 1 111 ? 14.50369  27.40184 -21.92684 1.000 101.00440 ? 111 ARG C C     1 
ATOM   2859 O  O     . ARG C 1 111 ? 14.08619  28.49324 -22.32649 1.000 111.72814 ? 111 ARG C O     1 
ATOM   2860 C  CB    . ARG C 1 111 ? 15.45998  26.08351 -23.82606 1.000 111.16897 ? 111 ARG C CB    1 
ATOM   2861 N  N     . GLY C 1 112 ? 15.09914  27.23209 -20.74603 1.000 93.27320  ? 112 GLY C N     1 
ATOM   2862 C  CA    . GLY C 1 112 ? 15.39336  28.32249 -19.83322 1.000 96.45411  ? 112 GLY C CA    1 
ATOM   2863 C  C     . GLY C 1 112 ? 14.28194  29.33647 -19.65786 1.000 87.42048  ? 112 GLY C C     1 
ATOM   2864 O  O     . GLY C 1 112 ? 14.53420  30.54436 -19.65177 1.000 87.41870  ? 112 GLY C O     1 
ATOM   2865 N  N     . GLU C 1 113 ? 13.04697  28.86168 -19.52677 1.000 90.20815  ? 113 GLU C N     1 
ATOM   2866 C  CA    . GLU C 1 113 ? 11.89611  29.74180 -19.39169 1.000 86.26315  ? 113 GLU C CA    1 
ATOM   2867 C  C     . GLU C 1 113 ? 11.62474  30.04098 -17.92478 1.000 78.57196  ? 113 GLU C C     1 
ATOM   2868 O  O     . GLU C 1 113 ? 11.69020  29.14887 -17.07459 1.000 83.02745  ? 113 GLU C O     1 
ATOM   2869 C  CB    . GLU C 1 113 ? 10.65524  29.11403 -20.02929 1.000 85.29598  ? 113 GLU C CB    1 
ATOM   2870 C  CG    . GLU C 1 113 ? 9.40359   29.96725 -19.90402 1.000 79.66895  ? 113 GLU C CG    1 
ATOM   2871 C  CD    . GLU C 1 113 ? 8.23013   29.40197 -20.67607 1.000 89.72674  ? 113 GLU C CD    1 
ATOM   2872 O  OE1   . GLU C 1 113 ? 8.45378   28.54640 -21.55865 1.000 82.94205  ? 113 GLU C OE1   1 
ATOM   2873 O  OE2   . GLU C 1 113 ? 7.08382   29.81383 -20.39860 1.000 87.22592  ? 113 GLU C OE2   1 
ATOM   2874 N  N     . ARG C 1 114 ? 11.32069  31.30595 -17.63458 1.000 83.95074  ? 114 ARG C N     1 
ATOM   2875 C  CA    . ARG C 1 114 ? 10.90062  31.69572 -16.29559 1.000 77.23956  ? 114 ARG C CA    1 
ATOM   2876 C  C     . ARG C 1 114 ? 9.62293   30.95304 -15.92733 1.000 79.10914  ? 114 ARG C C     1 
ATOM   2877 O  O     . ARG C 1 114 ? 8.56148   31.20768 -16.50541 1.000 84.77305  ? 114 ARG C O     1 
ATOM   2878 C  CB    . ARG C 1 114 ? 10.69209  33.20979 -16.21172 1.000 77.09260  ? 114 ARG C CB    1 
ATOM   2879 N  N     . ILE C 1 115 ? 9.72019   30.02419 -14.97897 1.000 74.77158  ? 115 ILE C N     1 
ATOM   2880 C  CA    . ILE C 1 115 ? 8.58694   29.19568 -14.58249 1.000 75.28845  ? 115 ILE C CA    1 
ATOM   2881 C  C     . ILE C 1 115 ? 8.17356   29.40311 -13.13391 1.000 72.57721  ? 115 ILE C C     1 
ATOM   2882 O  O     . ILE C 1 115 ? 7.10316   28.91561 -12.73844 1.000 65.94179  ? 115 ILE C O     1 
ATOM   2883 C  CB    . ILE C 1 115 ? 8.86574   27.69904 -14.84721 1.000 69.66042  ? 115 ILE C CB    1 
ATOM   2884 C  CG1   . ILE C 1 115 ? 10.27941  27.31711 -14.39737 1.000 77.45503  ? 115 ILE C CG1   1 
ATOM   2885 C  CG2   . ILE C 1 115 ? 8.67948   27.37798 -16.32277 1.000 82.82993  ? 115 ILE C CG2   1 
ATOM   2886 C  CD1   . ILE C 1 115 ? 10.38466  26.90494 -12.94712 1.000 80.44510  ? 115 ILE C CD1   1 
ATOM   2887 N  N     . ALA C 1 116 ? 8.97167   30.10252 -12.33274 1.000 69.48863  ? 116 ALA C N     1 
ATOM   2888 C  CA    . ALA C 1 116 ? 8.63716   30.39152 -10.94331 1.000 74.31699  ? 116 ALA C CA    1 
ATOM   2889 C  C     . ALA C 1 116 ? 9.54849   31.51282 -10.46186 1.000 77.60684  ? 116 ALA C C     1 
ATOM   2890 O  O     . ALA C 1 116 ? 10.43799  31.97082 -11.18478 1.000 80.67493  ? 116 ALA C O     1 
ATOM   2891 C  CB    . ALA C 1 116 ? 8.76925   29.14486 -10.06187 1.000 74.93695  ? 116 ALA C CB    1 
ATOM   2892 N  N     . GLN C 1 117 ? 9.31745   31.95597 -9.23013  1.000 75.54848  ? 117 GLN C N     1 
ATOM   2893 C  CA    . GLN C 1 117 ? 10.15763  32.95901 -8.59559  1.000 76.16372  ? 117 GLN C CA    1 
ATOM   2894 C  C     . GLN C 1 117 ? 10.50360  32.51350 -7.18261  1.000 78.69154  ? 117 GLN C C     1 
ATOM   2895 O  O     . GLN C 1 117 ? 9.68002   31.90568 -6.49197  1.000 78.27757  ? 117 GLN C O     1 
ATOM   2896 C  CB    . GLN C 1 117 ? 9.47739   34.33342 -8.57732  1.000 77.50992  ? 117 GLN C CB    1 
ATOM   2897 C  CG    . GLN C 1 117 ? 8.01509   34.31313 -8.17435  1.000 75.70218  ? 117 GLN C CG    1 
ATOM   2898 C  CD    . GLN C 1 117 ? 7.34521   35.66044 -8.37380  1.000 91.99640  ? 117 GLN C CD    1 
ATOM   2899 O  OE1   . GLN C 1 117 ? 7.35892   36.51129 -7.48425  1.000 92.65907  ? 117 GLN C OE1   1 
ATOM   2900 N  NE2   . GLN C 1 117 ? 6.75832   35.86222 -9.54894  1.000 92.32471  ? 117 GLN C NE2   1 
ATOM   2901 N  N     . LEU C 1 118 ? 11.73042  32.81281 -6.76422  1.000 79.34394  ? 118 LEU C N     1 
ATOM   2902 C  CA    . LEU C 1 118 ? 12.25923  32.39937 -5.46935  1.000 70.98041  ? 118 LEU C CA    1 
ATOM   2903 C  C     . LEU C 1 118 ? 12.42874  33.63377 -4.59497  1.000 77.53987  ? 118 LEU C C     1 
ATOM   2904 O  O     . LEU C 1 118 ? 13.26095  34.49873 -4.88803  1.000 86.13910  ? 118 LEU C O     1 
ATOM   2905 C  CB    . LEU C 1 118 ? 13.58702  31.66626 -5.63566  1.000 70.58095  ? 118 LEU C CB    1 
ATOM   2906 C  CG    . LEU C 1 118 ? 14.42043  31.45679 -4.37116  1.000 72.18310  ? 118 LEU C CG    1 
ATOM   2907 C  CD1   . LEU C 1 118 ? 13.76572  30.44560 -3.44230  1.000 68.50237  ? 118 LEU C CD1   1 
ATOM   2908 C  CD2   . LEU C 1 118 ? 15.83138  31.03083 -4.73509  1.000 68.70410  ? 118 LEU C CD2   1 
ATOM   2909 N  N     . VAL C 1 119 ? 11.65146  33.70737 -3.51907  1.000 70.13546  ? 119 VAL C N     1 
ATOM   2910 C  CA    . VAL C 1 119 ? 11.69977  34.82544 -2.58562  1.000 72.19586  ? 119 VAL C CA    1 
ATOM   2911 C  C     . VAL C 1 119 ? 12.44862  34.38468 -1.33853  1.000 79.09070  ? 119 VAL C C     1 
ATOM   2912 O  O     . VAL C 1 119 ? 12.12479  33.34862 -0.74415  1.000 77.43907  ? 119 VAL C O     1 
ATOM   2913 C  CB    . VAL C 1 119 ? 10.28682  35.31949 -2.23078  1.000 71.82016  ? 119 VAL C CB    1 
ATOM   2914 C  CG1   . VAL C 1 119 ? 10.35770  36.41973 -1.18175  1.000 76.26666  ? 119 VAL C CG1   1 
ATOM   2915 C  CG2   . VAL C 1 119 ? 9.56677   35.81024 -3.47413  1.000 65.79707  ? 119 VAL C CG2   1 
ATOM   2916 N  N     . ILE C 1 120 ? 13.45099  35.16283 -0.94561  1.000 79.12794  ? 120 ILE C N     1 
ATOM   2917 C  CA    . ILE C 1 120 ? 14.16851  34.93352 0.30225   1.000 80.68321  ? 120 ILE C CA    1 
ATOM   2918 C  C     . ILE C 1 120 ? 13.48595  35.75136 1.39134   1.000 82.49070  ? 120 ILE C C     1 
ATOM   2919 O  O     . ILE C 1 120 ? 13.34551  36.97332 1.26715   1.000 91.26508  ? 120 ILE C O     1 
ATOM   2920 C  CB    . ILE C 1 120 ? 15.65235  35.30860 0.17234   1.000 82.60740  ? 120 ILE C CB    1 
ATOM   2921 C  CG1   . ILE C 1 120 ? 16.25897  34.67152 -1.08210  1.000 72.76860  ? 120 ILE C CG1   1 
ATOM   2922 C  CG2   . ILE C 1 120 ? 16.41768  34.87100 1.41136   1.000 70.29579  ? 120 ILE C CG2   1 
ATOM   2923 C  CD1   . ILE C 1 120 ? 16.23755  33.16061 -1.07539  1.000 68.94421  ? 120 ILE C CD1   1 
ATOM   2924 N  N     . ALA C 1 121 ? 13.05809  35.08106 2.45489   1.000 75.99239  ? 121 ALA C N     1 
ATOM   2925 C  CA    . ALA C 1 121 ? 12.31246  35.72020 3.52626   1.000 87.29879  ? 121 ALA C CA    1 
ATOM   2926 C  C     . ALA C 1 121 ? 12.77382  35.16415 4.86329   1.000 87.66721  ? 121 ALA C C     1 
ATOM   2927 O  O     . ALA C 1 121 ? 13.24348  34.02236 4.93291   1.000 89.18000  ? 121 ALA C O     1 
ATOM   2928 C  CB    . ALA C 1 121 ? 10.79964  35.50189 3.36562   1.000 78.93832  ? 121 ALA C CB    1 
ATOM   2929 N  N     . PRO C 1 122 ? 12.66337  35.94748 5.93837   1.000 88.32869  ? 122 PRO C N     1 
ATOM   2930 C  CA    . PRO C 1 122 ? 13.06146  35.44500 7.26047   1.000 85.30651  ? 122 PRO C CA    1 
ATOM   2931 C  C     . PRO C 1 122 ? 12.01695  34.48914 7.82158   1.000 84.14749  ? 122 PRO C C     1 
ATOM   2932 O  O     . PRO C 1 122 ? 10.81487  34.76324 7.78108   1.000 86.03056  ? 122 PRO C O     1 
ATOM   2933 C  CB    . PRO C 1 122 ? 13.16773  36.71857 8.10770   1.000 84.14020  ? 122 PRO C CB    1 
ATOM   2934 C  CG    . PRO C 1 122 ? 12.21284  37.66591 7.46329   1.000 85.85945  ? 122 PRO C CG    1 
ATOM   2935 C  CD    . PRO C 1 122 ? 12.28000  37.37039 5.98408   1.000 96.25211  ? 122 PRO C CD    1 
ATOM   2936 N  N     . VAL C 1 123 ? 12.48631  33.35777 8.33901   1.000 87.49218  ? 123 VAL C N     1 
ATOM   2937 C  CA    . VAL C 1 123 ? 11.63722  32.38523 9.01199   1.000 90.30369  ? 123 VAL C CA    1 
ATOM   2938 C  C     . VAL C 1 123 ? 12.05898  32.32754 10.47352  1.000 88.06909  ? 123 VAL C C     1 
ATOM   2939 O  O     . VAL C 1 123 ? 13.22283  32.56706 10.81336  1.000 88.96707  ? 123 VAL C O     1 
ATOM   2940 C  CB    . VAL C 1 123 ? 11.71194  30.99124 8.34592   1.000 82.51020  ? 123 VAL C CB    1 
ATOM   2941 C  CG1   . VAL C 1 123 ? 13.05447  30.32713 8.61747   1.000 92.28188  ? 123 VAL C CG1   1 
ATOM   2942 C  CG2   . VAL C 1 123 ? 10.55819  30.10909 8.80437   1.000 87.41606  ? 123 VAL C CG2   1 
ATOM   2943 N  N     . GLN C 1 124 ? 11.10006  32.02568 11.34465  1.000 96.18533  ? 124 GLN C N     1 
ATOM   2944 C  CA    . GLN C 1 124 ? 11.30593  32.08942 12.78601  1.000 96.44495  ? 124 GLN C CA    1 
ATOM   2945 C  C     . GLN C 1 124 ? 11.28088  30.68602 13.37934  1.000 92.90408  ? 124 GLN C C     1 
ATOM   2946 O  O     . GLN C 1 124 ? 10.27035  29.98076 13.27978  1.000 91.89731  ? 124 GLN C O     1 
ATOM   2947 C  CB    . GLN C 1 124 ? 10.24885  32.97336 13.44861  1.000 92.47496  ? 124 GLN C CB    1 
ATOM   2948 C  CG    . GLN C 1 124 ? 10.56887  33.34855 14.89173  1.000 100.14809 ? 124 GLN C CG    1 
ATOM   2949 C  CD    . GLN C 1 124 ? 11.73360  34.32314 15.00677  1.000 108.96020 ? 124 GLN C CD    1 
ATOM   2950 O  OE1   . GLN C 1 124 ? 12.88179  33.96615 14.74672  1.000 113.07267 ? 124 GLN C OE1   1 
ATOM   2951 N  NE2   . GLN C 1 124 ? 11.43928  35.56204 15.39526  1.000 109.19283 ? 124 GLN C NE2   1 
ATOM   2952 N  N     . ARG C 1 125 ? 12.39423  30.28954 13.99294  1.000 86.81914  ? 125 ARG C N     1 
ATOM   2953 C  CA    . ARG C 1 125 ? 12.46553  29.03800 14.73457  1.000 95.04453  ? 125 ARG C CA    1 
ATOM   2954 C  C     . ARG C 1 125 ? 11.80435  29.21366 16.09691  1.000 90.71343  ? 125 ARG C C     1 
ATOM   2955 O  O     . ARG C 1 125 ? 12.11316  30.15978 16.82823  1.000 89.06820  ? 125 ARG C O     1 
ATOM   2956 C  CB    . ARG C 1 125 ? 13.92350  28.60016 14.89340  1.000 101.09909 ? 125 ARG C CB    1 
ATOM   2957 C  CG    . ARG C 1 125 ? 14.17570  27.57958 15.99745  1.000 90.99393  ? 125 ARG C CG    1 
ATOM   2958 C  CD    . ARG C 1 125 ? 13.47764  26.26123 15.71219  1.000 102.49021 ? 125 ARG C CD    1 
ATOM   2959 N  NE    . ARG C 1 125 ? 13.97089  25.61638 14.50078  1.000 104.95774 ? 125 ARG C NE    1 
ATOM   2960 C  CZ    . ARG C 1 125 ? 14.72089  24.52273 14.48488  1.000 105.62929 ? 125 ARG C CZ    1 
ATOM   2961 N  NH1   . ARG C 1 125 ? 15.07304  23.90889 15.60321  1.000 98.39162  ? 125 ARG C NH1   1 
ATOM   2962 N  NH2   . ARG C 1 125 ? 15.12256  24.02898 13.31721  1.000 93.19651  ? 125 ARG C NH2   1 
ATOM   2963 N  N     . VAL C 1 126 ? 10.89007  28.30520 16.43534  1.000 84.94983  ? 126 VAL C N     1 
ATOM   2964 C  CA    . VAL C 1 126 ? 10.13408  28.39374 17.67619  1.000 91.88841  ? 126 VAL C CA    1 
ATOM   2965 C  C     . VAL C 1 126 ? 10.46671  27.19661 18.55703  1.000 92.65717  ? 126 VAL C C     1 
ATOM   2966 O  O     . VAL C 1 126 ? 10.94024  26.15667 18.09178  1.000 98.06355  ? 126 VAL C O     1 
ATOM   2967 C  CB    . VAL C 1 126 ? 8.61331   28.47531 17.42840  1.000 88.42013  ? 126 VAL C CB    1 
ATOM   2968 C  CG1   . VAL C 1 126 ? 8.29892   29.57957 16.43401  1.000 84.99541  ? 126 VAL C CG1   1 
ATOM   2969 C  CG2   . VAL C 1 126 ? 8.07654   27.13613 16.94511  1.000 77.75246  ? 126 VAL C CG2   1 
ATOM   2970 N  N     . GLU C 1 127 ? 10.21432  27.36324 19.85393  1.000 79.92507  ? 127 GLU C N     1 
ATOM   2971 C  CA    . GLU C 1 127 ? 10.38125  26.30150 20.84005  1.000 91.01211  ? 127 GLU C CA    1 
ATOM   2972 C  C     . GLU C 1 127 ? 9.00308   25.73245 21.15613  1.000 93.60045  ? 127 GLU C C     1 
ATOM   2973 O  O     . GLU C 1 127 ? 8.15114   26.42763 21.71956  1.000 89.82104  ? 127 GLU C O     1 
ATOM   2974 C  CB    . GLU C 1 127 ? 11.06438  26.82753 22.10057  1.000 79.04706  ? 127 GLU C CB    1 
ATOM   2975 N  N     . VAL C 1 128 ? 8.78446   24.47068 20.78804  1.000 90.11980  ? 128 VAL C N     1 
ATOM   2976 C  CA    . VAL C 1 128 ? 7.48089   23.84939 20.98221  1.000 90.68681  ? 128 VAL C CA    1 
ATOM   2977 C  C     . VAL C 1 128 ? 7.26257   23.57918 22.46406  1.000 93.38236  ? 128 VAL C C     1 
ATOM   2978 O  O     . VAL C 1 128 ? 8.11300   22.98177 23.13706  1.000 93.70816  ? 128 VAL C O     1 
ATOM   2979 C  CB    . VAL C 1 128 ? 7.37127   22.55949 20.15680  1.000 93.07186  ? 128 VAL C CB    1 
ATOM   2980 C  CG1   . VAL C 1 128 ? 5.95413   22.01058 20.21935  1.000 94.32702  ? 128 VAL C CG1   1 
ATOM   2981 C  CG2   . VAL C 1 128 ? 7.78983   22.81635 18.71741  1.000 86.15498  ? 128 VAL C CG2   1 
ATOM   2982 N  N     . VAL C 1 129 ? 6.12094   24.02712 22.98118  1.000 94.56192  ? 129 VAL C N     1 
ATOM   2983 C  CA    . VAL C 1 129 ? 5.74731   23.82506 24.37693  1.000 86.93835  ? 129 VAL C CA    1 
ATOM   2984 C  C     . VAL C 1 129 ? 4.29603   23.37003 24.42095  1.000 93.03883  ? 129 VAL C C     1 
ATOM   2985 O  O     . VAL C 1 129 ? 3.41852   24.02385 23.84780  1.000 87.77797  ? 129 VAL C O     1 
ATOM   2986 C  CB    . VAL C 1 129 ? 5.93802   25.10346 25.21742  1.000 90.80805  ? 129 VAL C CB    1 
ATOM   2987 C  CG1   . VAL C 1 129 ? 5.27516   24.94805 26.57658  1.000 87.44668  ? 129 VAL C CG1   1 
ATOM   2988 C  CG2   . VAL C 1 129 ? 7.41838   25.41926 25.37951  1.000 91.43501  ? 129 VAL C CG2   1 
ATOM   2989 N  N     . GLU C 1 130 ? 4.04227   22.25138 25.09541  1.000 91.33706  ? 130 GLU C N     1 
ATOM   2990 C  CA    . GLU C 1 130 ? 2.69433   21.71370 25.21480  1.000 89.09879  ? 130 GLU C CA    1 
ATOM   2991 C  C     . GLU C 1 130 ? 2.03135   22.24714 26.47810  1.000 92.18786  ? 130 GLU C C     1 
ATOM   2992 O  O     . GLU C 1 130 ? 2.60500   22.17099 27.56952  1.000 92.61038  ? 130 GLU C O     1 
ATOM   2993 C  CB    . GLU C 1 130 ? 2.71641   20.18473 25.23314  1.000 88.96088  ? 130 GLU C CB    1 
ATOM   2994 C  CG    . GLU C 1 130 ? 1.33989   19.55039 25.37308  1.000 93.56232  ? 130 GLU C CG    1 
ATOM   2995 C  CD    . GLU C 1 130 ? 1.38018   18.03787 25.27231  1.000 101.70885 ? 130 GLU C CD    1 
ATOM   2996 O  OE1   . GLU C 1 130 ? 2.41581   17.49693 24.83106  1.000 96.41086  ? 130 GLU C OE1   1 
ATOM   2997 O  OE2   . GLU C 1 130 ? 0.37590   17.38827 25.63281  1.000 113.47185 ? 130 GLU C OE2   1 
ATOM   2998 N  N     . VAL C 1 131 ? 0.82377   22.78733 26.32426  1.000 92.24500  ? 131 VAL C N     1 
ATOM   2999 C  CA    . VAL C 1 131 ? 0.05447   23.31737 27.43999  1.000 90.73675  ? 131 VAL C CA    1 
ATOM   3000 C  C     . VAL C 1 131 ? -1.28490  22.59448 27.49593  1.000 93.48195  ? 131 VAL C C     1 
ATOM   3001 O  O     . VAL C 1 131 ? -1.74702  22.00682 26.51427  1.000 89.68979  ? 131 VAL C O     1 
ATOM   3002 C  CB    . VAL C 1 131 ? -0.15339  24.84314 27.33666  1.000 92.63473  ? 131 VAL C CB    1 
ATOM   3003 C  CG1   . VAL C 1 131 ? 1.18514   25.55454 27.20087  1.000 86.29970  ? 131 VAL C CG1   1 
ATOM   3004 C  CG2   . VAL C 1 131 ? -1.06616  25.18078 26.16800  1.000 93.24912  ? 131 VAL C CG2   1 
ATOM   3005 N  N     . GLU C 1 132 ? -1.90652  22.63995 28.67144  1.000 92.26853  ? 132 GLU C N     1 
ATOM   3006 C  CA    . GLU C 1 132 ? -3.20160  22.01071 28.89026  1.000 98.13168  ? 132 GLU C CA    1 
ATOM   3007 C  C     . GLU C 1 132 ? -4.36792  22.97024 28.69388  1.000 101.24238 ? 132 GLU C C     1 
ATOM   3008 O  O     . GLU C 1 132 ? -5.52372  22.53975 28.76528  1.000 107.73216 ? 132 GLU C O     1 
ATOM   3009 C  CB    . GLU C 1 132 ? -3.26357  21.40681 30.29738  1.000 96.58714  ? 132 GLU C CB    1 
ATOM   3010 N  N     . GLU C 1 133 ? -4.09642  24.25010 28.44866  1.000 99.57464  ? 133 GLU C N     1 
ATOM   3011 C  CA    . GLU C 1 133 ? -5.14768  25.23572 28.24646  1.000 93.17424  ? 133 GLU C CA    1 
ATOM   3012 C  C     . GLU C 1 133 ? -4.54981  26.45016 27.55344  1.000 90.10570  ? 133 GLU C C     1 
ATOM   3013 O  O     . GLU C 1 133 ? -3.41735  26.84194 27.84600  1.000 97.21906  ? 133 GLU C O     1 
ATOM   3014 C  CB    . GLU C 1 133 ? -5.79727  25.64454 29.57407  1.000 102.81870 ? 133 GLU C CB    1 
ATOM   3015 N  N     . VAL C 1 134 ? -5.31375  27.03423 26.63655  1.000 95.63508  ? 134 VAL C N     1 
ATOM   3016 C  CA    . VAL C 1 134 ? -4.89024  28.21886 25.90865  1.000 99.12004  ? 134 VAL C CA    1 
ATOM   3017 C  C     . VAL C 1 134 ? -5.65880  29.42356 26.44356  1.000 91.14408  ? 134 VAL C C     1 
ATOM   3018 O  O     . VAL C 1 134 ? -6.59942  29.29526 27.22707  1.000 94.22982  ? 134 VAL C O     1 
ATOM   3019 C  CB    . VAL C 1 134 ? -5.08373  28.06569 24.38712  1.000 93.53668  ? 134 VAL C CB    1 
ATOM   3020 C  CG1   . VAL C 1 134 ? -4.39305  26.80563 23.88776  1.000 91.19545  ? 134 VAL C CG1   1 
ATOM   3021 C  CG2   . VAL C 1 134 ? -6.56398  28.04792 24.03861  1.000 89.04749  ? 134 VAL C CG2   1 
ATOM   3022 N  N     . SER C 1 135 ? -5.24642  30.60875 26.00579  1.000 96.37840  ? 135 SER C N     1 
ATOM   3023 C  CA    . SER C 1 135 ? -5.87212  31.84119 26.46082  1.000 108.01429 ? 135 SER C CA    1 
ATOM   3024 C  C     . SER C 1 135 ? -7.13759  32.12960 25.66477  1.000 102.50144 ? 135 SER C C     1 
ATOM   3025 O  O     . SER C 1 135 ? -7.17055  31.96527 24.44249  1.000 99.54953  ? 135 SER C O     1 
ATOM   3026 C  CB    . SER C 1 135 ? -4.89904  33.01279 26.32936  1.000 101.72679 ? 135 SER C CB    1 
ATOM   3027 O  OG    . SER C 1 135 ? -4.51193  33.20099 24.97937  1.000 97.89630  ? 135 SER C OG    1 
ATOM   3028 N  N     . GLN C 1 136 ? -8.18447  32.55645 26.36709  1.000 108.53069 ? 136 GLN C N     1 
ATOM   3029 C  CA    . GLN C 1 136 ? -9.39570  33.00712 25.69563  1.000 114.06197 ? 136 GLN C CA    1 
ATOM   3030 C  C     . GLN C 1 136 ? -9.11781  34.31166 24.95889  1.000 114.31519 ? 136 GLN C C     1 
ATOM   3031 O  O     . GLN C 1 136 ? -8.45958  35.21167 25.48781  1.000 120.35645 ? 136 GLN C O     1 
ATOM   3032 C  CB    . GLN C 1 136 ? -10.52791 33.19244 26.70519  1.000 98.49109  ? 136 GLN C CB    1 
ATOM   3033 N  N     . THR C 1 137 ? -9.61722  34.41248 23.72838  1.000 126.51142 ? 137 THR C N     1 
ATOM   3034 C  CA    . THR C 1 137 ? -9.22895  35.51026 22.85580  1.000 132.37868 ? 137 THR C CA    1 
ATOM   3035 C  C     . THR C 1 137 ? -10.37880 35.85655 21.92125  1.000 136.85985 ? 137 THR C C     1 
ATOM   3036 O  O     . THR C 1 137 ? -11.16593 34.98794 21.53399  1.000 139.79205 ? 137 THR C O     1 
ATOM   3037 C  CB    . THR C 1 137 ? -7.96310  35.15259 22.06368  1.000 132.45091 ? 137 THR C CB    1 
ATOM   3038 O  OG1   . THR C 1 137 ? -6.88950  34.90550 22.98139  1.000 151.18255 ? 137 THR C OG1   1 
ATOM   3039 C  CG2   . THR C 1 137 ? -7.55379  36.27887 21.13633  1.000 127.60427 ? 137 THR C CG2   1 
ATOM   3040 N  N     . GLN C 1 138 ? -10.45516 37.14814 21.57616  1.000 148.22887 ? 138 GLN C N     1 
ATOM   3041 C  CA    . GLN C 1 138 ? -11.46294 37.77044 20.71876  1.000 150.87684 ? 138 GLN C CA    1 
ATOM   3042 C  C     . GLN C 1 138 ? -12.06763 36.84861 19.66407  1.000 157.39174 ? 138 GLN C C     1 
ATOM   3043 O  O     . GLN C 1 138 ? -13.20675 36.39418 19.81744  1.000 156.66740 ? 138 GLN C O     1 
ATOM   3044 C  CB    . GLN C 1 138 ? -10.85809 38.99675 20.02768  1.000 153.83735 ? 138 GLN C CB    1 
ATOM   3045 N  N     . ARG C 1 139 ? -11.31708 36.56702 18.59303  1.000 126.18502 ? 139 ARG C N     1 
ATOM   3046 C  CA    . ARG C 1 139 ? -11.87987 35.84227 17.45681  1.000 121.00536 ? 139 ARG C CA    1 
ATOM   3047 C  C     . ARG C 1 139 ? -12.37820 34.45447 17.83989  1.000 117.85199 ? 139 ARG C C     1 
ATOM   3048 O  O     . ARG C 1 139 ? -13.25160 33.91339 17.15291  1.000 112.31240 ? 139 ARG C O     1 
ATOM   3049 C  CB    . ARG C 1 139 ? -10.85103 35.73693 16.32389  1.000 103.49302 ? 139 ARG C CB    1 
ATOM   3050 C  CG    . ARG C 1 139 ? -10.01478 34.46650 16.34567  1.000 99.63998  ? 139 ARG C CG    1 
ATOM   3051 C  CD    . ARG C 1 139 ? -9.00196  34.41561 15.20442  1.000 94.71472  ? 139 ARG C CD    1 
ATOM   3052 N  NE    . ARG C 1 139 ? -9.62026  34.24069 13.89442  1.000 96.12961  ? 139 ARG C NE    1 
ATOM   3053 C  CZ    . ARG C 1 139 ? -9.65718  35.17198 12.95067  1.000 96.25576  ? 139 ARG C CZ    1 
ATOM   3054 N  NH1   . ARG C 1 139 ? -9.12120  36.36714 13.13722  1.000 98.86634  ? 139 ARG C NH1   1 
ATOM   3055 N  NH2   . ARG C 1 139 ? -10.23989 34.89457 11.78750  1.000 90.91191  ? 139 ARG C NH2   1 
ATOM   3056 N  N     . GLY C 1 140 ? -11.85794 33.87507 18.92084  1.000 113.97550 ? 140 GLY C N     1 
ATOM   3057 C  CA    . GLY C 1 140 ? -12.34932 32.58227 19.36953  1.000 106.12977 ? 140 GLY C CA    1 
ATOM   3058 C  C     . GLY C 1 140 ? -12.02615 31.48047 18.37835  1.000 109.73110 ? 140 GLY C C     1 
ATOM   3059 O  O     . GLY C 1 140 ? -10.91090 31.38458 17.85397  1.000 99.29444  ? 140 GLY C O     1 
ATOM   3060 N  N     . GLU C 1 141 ? -13.01823 30.63545 18.11568  1.000 114.43245 ? 141 GLU C N     1 
ATOM   3061 C  CA    . GLU C 1 141 ? -12.85742 29.52220 17.18773  1.000 105.04775 ? 141 GLU C CA    1 
ATOM   3062 C  C     . GLU C 1 141 ? -13.53255 29.81903 15.85207  1.000 93.94067  ? 141 GLU C C     1 
ATOM   3063 O  O     . GLU C 1 141 ? -13.00529 29.48479 14.79094  1.000 102.04788 ? 141 GLU C O     1 
ATOM   3064 C  CB    . GLU C 1 141 ? -13.42524 28.23555 17.79110  1.000 97.84128  ? 141 GLU C CB    1 
HETATM 3065 O  OP3   . DU  D 2 .   ? 5.06514   38.89698 -12.92791 1.000 98.64706  ? 201 DU  A OP3   1 
HETATM 3066 P  P     . DU  D 2 .   ? 5.12710   40.47560 -13.18376 1.000 105.12946 ? 201 DU  A P     1 
HETATM 3067 O  OP1   . DU  D 2 .   ? 6.39212   40.97104 -12.58367 1.000 94.84417  ? 201 DU  A OP1   1 
HETATM 3068 O  OP2   . DU  D 2 .   ? 4.84831   40.74584 -14.61837 1.000 96.92864  ? 201 DU  A OP2   1 
HETATM 3069 O  "O5'" . DU  D 2 .   ? 3.92060   41.05062 -12.31556 1.000 107.82649 ? 201 DU  A "O5'" 1 
HETATM 3070 C  "C5'" . DU  D 2 .   ? 4.07057   41.26334 -10.89697 1.000 93.82032  ? 201 DU  A "C5'" 1 
HETATM 3071 C  "C4'" . DU  D 2 .   ? 3.05998   42.27177 -10.40121 1.000 97.52453  ? 201 DU  A "C4'" 1 
HETATM 3072 O  "O4'" . DU  D 2 .   ? 1.72211   41.77783 -10.62516 1.000 95.67793  ? 201 DU  A "O4'" 1 
HETATM 3073 C  "C3'" . DU  D 2 .   ? 3.12797   42.55736 -8.90504  1.000 93.30471  ? 201 DU  A "C3'" 1 
HETATM 3074 O  "O3'" . DU  D 2 .   ? 4.05774   43.61228 -8.64067  1.000 91.82188  ? 201 DU  A "O3'" 1 
HETATM 3075 C  "C2'" . DU  D 2 .   ? 1.71096   42.99419 -8.57981  1.000 86.87369  ? 201 DU  A "C2'" 1 
HETATM 3076 C  "C1'" . DU  D 2 .   ? 0.85119   42.25439 -9.60404  1.000 93.75124  ? 201 DU  A "C1'" 1 
HETATM 3077 N  N1    . DU  D 2 .   ? 0.12101   41.10110 -9.05697  1.000 86.34380  ? 201 DU  A N1    1 
HETATM 3078 C  C2    . DU  D 2 .   ? -1.23506  41.24455 -8.84799  1.000 86.37298  ? 201 DU  A C2    1 
HETATM 3079 O  O2    . DU  D 2 .   ? -1.83998  42.27219 -9.09707  1.000 90.79202  ? 201 DU  A O2    1 
HETATM 3080 N  N3    . DU  D 2 .   ? -1.86109  40.13365 -8.33248  1.000 71.13214  ? 201 DU  A N3    1 
HETATM 3081 C  C4    . DU  D 2 .   ? -1.27586  38.92491 -8.01500  1.000 79.34589  ? 201 DU  A C4    1 
HETATM 3082 O  O4    . DU  D 2 .   ? -1.97393  38.01735 -7.55846  1.000 67.58016  ? 201 DU  A O4    1 
HETATM 3083 C  C5    . DU  D 2 .   ? 0.13064   38.85954 -8.26152  1.000 83.15683  ? 201 DU  A C5    1 
HETATM 3084 C  C6    . DU  D 2 .   ? 0.76699   39.92384 -8.76306  1.000 78.06782  ? 201 DU  A C6    1 
HETATM 3085 MG MG    . MG  E 3 .   ? -13.58970 29.35248 9.16525   1.000 90.74263  ? 202 MG  A MG    1 
HETATM 3086 O  OP3   . DU  F 2 .   ? -11.24283 33.03036 6.90108   1.000 93.03780  ? 201 DU  B OP3   1 
HETATM 3087 P  P     . DU  F 2 .   ? -11.62275 33.41001 8.40814   1.000 100.85247 ? 201 DU  B P     1 
HETATM 3088 O  OP1   . DU  F 2 .   ? -13.10423 33.45715 8.51119   1.000 86.52389  ? 201 DU  B OP1   1 
HETATM 3089 O  OP2   . DU  F 2 .   ? -10.81843 34.59434 8.80477   1.000 101.61236 ? 201 DU  B OP2   1 
HETATM 3090 O  "O5'" . DU  F 2 .   ? -11.11066 32.16230 9.25407   1.000 89.17386  ? 201 DU  B "O5'" 1 
HETATM 3091 C  "C5'" . DU  F 2 .   ? -9.75316  31.70280 9.13378   1.000 88.19036  ? 201 DU  B "C5'" 1 
HETATM 3092 C  "C4'" . DU  F 2 .   ? -9.39655  30.84155 10.32202  1.000 77.33533  ? 201 DU  B "C4'" 1 
HETATM 3093 O  "O4'" . DU  F 2 .   ? -9.20046  29.47435 9.89134   1.000 78.52670  ? 201 DU  B "O4'" 1 
HETATM 3094 C  "C3'" . DU  F 2 .   ? -8.11886  31.26324 11.04965  1.000 76.99080  ? 201 DU  B "C3'" 1 
HETATM 3095 O  "O3'" . DU  F 2 .   ? -8.34290  31.33455 12.45886  1.000 96.20975  ? 201 DU  B "O3'" 1 
HETATM 3096 C  "C2'" . DU  F 2 .   ? -7.10876  30.18516 10.69795  1.000 78.38207  ? 201 DU  B "C2'" 1 
HETATM 3097 C  "C1'" . DU  F 2 .   ? -7.95612  28.97428 10.34939  1.000 83.96036  ? 201 DU  B "C1'" 1 
HETATM 3098 N  N1    . DU  F 2 .   ? -7.38206  28.15046 9.27888   1.000 72.00957  ? 201 DU  B N1    1 
HETATM 3099 C  C2    . DU  F 2 .   ? -7.27443  26.78818 9.49265   1.000 65.10348  ? 201 DU  B C2    1 
HETATM 3100 O  O2    . DU  F 2 .   ? -7.63542  26.25370 10.52797  1.000 80.93584  ? 201 DU  B O2    1 
HETATM 3101 N  N3    . DU  F 2 .   ? -6.72752  26.07930 8.45409   1.000 63.55078  ? 201 DU  B N3    1 
HETATM 3102 C  C4    . DU  F 2 .   ? -6.28695  26.58060 7.24661   1.000 62.41801  ? 201 DU  B C4    1 
HETATM 3103 O  O4    . DU  F 2 .   ? -5.81754  25.81241 6.40529   1.000 69.53576  ? 201 DU  B O4    1 
HETATM 3104 C  C5    . DU  F 2 .   ? -6.43152  27.99757 7.10026   1.000 67.33440  ? 201 DU  B C5    1 
HETATM 3105 C  C6    . DU  F 2 .   ? -6.96296  28.71296 8.09599   1.000 68.77658  ? 201 DU  B C6    1 
HETATM 3106 O  OP3   . DU  G 2 .   ? 9.60324   19.31535 2.78765   1.000 94.31496  ? 201 DU  C OP3   1 
HETATM 3107 P  P     . DU  G 2 .   ? 10.59614  18.16386 2.28856   1.000 114.88196 ? 201 DU  C P     1 
HETATM 3108 O  OP1   . DU  G 2 .   ? 9.78349   17.11034 1.62901   1.000 98.08330  ? 201 DU  C OP1   1 
HETATM 3109 O  OP2   . DU  G 2 .   ? 11.49947  17.78964 3.40747   1.000 89.55520  ? 201 DU  C OP2   1 
HETATM 3110 O  "O5'" . DU  G 2 .   ? 11.47574  18.86286 1.15866   1.000 93.77762  ? 201 DU  C "O5'" 1 
HETATM 3111 C  "C5'" . DU  G 2 .   ? 12.89929  18.65877 1.11985   1.000 89.80351  ? 201 DU  C "C5'" 1 
HETATM 3112 C  "C4'" . DU  G 2 .   ? 13.58354  19.74466 0.32171   1.000 89.62657  ? 201 DU  C "C4'" 1 
HETATM 3113 O  "O4'" . DU  G 2 .   ? 13.00698  19.85545 -0.99442  1.000 80.53013  ? 201 DU  C "O4'" 1 
HETATM 3114 C  "C3'" . DU  G 2 .   ? 13.47061  21.14776 0.90588   1.000 77.63670  ? 201 DU  C "C3'" 1 
HETATM 3115 O  "O3'" . DU  G 2 .   ? 14.50995  21.37867 1.86148   1.000 81.32936  ? 201 DU  C "O3'" 1 
HETATM 3116 C  "C2'" . DU  G 2 .   ? 13.65145  22.04007 -0.31171  1.000 78.13358  ? 201 DU  C "C2'" 1 
HETATM 3117 C  "C1'" . DU  G 2 .   ? 13.32146  21.14323 -1.50803  1.000 73.70285  ? 201 DU  C "C1'" 1 
HETATM 3118 N  N1    . DU  G 2 .   ? 12.18152  21.60610 -2.31114  1.000 73.75564  ? 201 DU  C N1    1 
HETATM 3119 C  C2    . DU  G 2 .   ? 12.39508  21.82964 -3.65655  1.000 63.94364  ? 201 DU  C C2    1 
HETATM 3120 O  O2    . DU  G 2 .   ? 13.47536  21.65465 -4.19293  1.000 78.88624  ? 201 DU  C O2    1 
HETATM 3121 N  N3    . DU  G 2 .   ? 11.29517  22.26864 -4.35226  1.000 50.25927  ? 201 DU  C N3    1 
HETATM 3122 C  C4    . DU  G 2 .   ? 10.03178  22.50091 -3.84736  1.000 68.90276  ? 201 DU  C C4    1 
HETATM 3123 O  O4    . DU  G 2 .   ? 9.14154   22.89477 -4.60251  1.000 55.48306  ? 201 DU  C O4    1 
HETATM 3124 C  C5    . DU  G 2 .   ? 9.89409   22.24726 -2.44632  1.000 70.03899  ? 201 DU  C C5    1 
HETATM 3125 C  C6    . DU  G 2 .   ? 10.94750  21.81859 -1.74327  1.000 70.69030  ? 201 DU  C C6    1 
HETATM 3126 MG MG    . MG  H 3 .   ? 1.08393   40.73231 -15.73700 1.000 109.43583 ? 202 MG  C MG    1 
HETATM 3127 O  O     . HOH I 4 .   ? -4.82774  32.12223 3.65397   1.000 60.48370  ? 301 HOH A O     1 
HETATM 3128 O  O     . HOH I 4 .   ? 2.41380   42.26424 -14.64502 1.000 99.99257  ? 302 HOH A O     1 
HETATM 3129 O  O     . HOH I 4 .   ? 16.28154  17.08819 2.15097   1.000 82.90810  ? 303 HOH A O     1 
HETATM 3130 O  O     . HOH I 4 .   ? 8.09410   44.81412 -10.45329 1.000 97.18534  ? 304 HOH A O     1 
HETATM 3131 O  O     . HOH J 4 .   ? -14.49959 19.39551 -7.43542  1.000 103.10460 ? 301 HOH B O     1 
HETATM 3132 O  O     . HOH J 4 .   ? 3.59639   10.57424 7.83696   1.000 72.27991  ? 302 HOH B O     1 
HETATM 3133 O  O     . HOH J 4 .   ? 10.21319  19.58692 9.21216   1.000 80.90190  ? 303 HOH B O     1 
HETATM 3134 O  O     . HOH J 4 .   ? -4.30650  57.79187 -7.48051  1.000 112.94164 ? 304 HOH B O     1 
HETATM 3135 O  O     . HOH K 4 .   ? 7.65976   23.48633 -6.86726  1.000 55.08137  ? 301 HOH C 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     . LYS A 3   ? 2.67418 1.50130 1.85746 -0.21472 0.02356  -0.21003 3   LYS A N     
2    C  CA    . LYS A 3   ? 2.66261 1.48312 1.85048 -0.14530 0.04961  -0.20265 3   LYS A CA    
3    C  C     . LYS A 3   ? 2.59192 1.46475 1.84699 -0.11694 0.05068  -0.17202 3   LYS A C     
4    O  O     . LYS A 3   ? 2.68123 1.52105 1.93983 -0.13775 0.05327  -0.16124 3   LYS A O     
5    C  CB    . LYS A 3   ? 2.73064 1.42139 1.83588 -0.12382 0.08375  -0.22118 3   LYS A CB    
6    C  CG    . LYS A 3   ? 2.73310 1.41834 1.84542 -0.04827 0.11054  -0.21228 3   LYS A CG    
7    C  CD    . LYS A 3   ? 2.65749 1.41169 1.78781 -0.01752 0.10997  -0.21988 3   LYS A CD    
8    C  CE    . LYS A 3   ? 2.71185 1.40450 1.76765 -0.03986 0.11751  -0.25207 3   LYS A CE    
9    N  NZ    . LYS A 3   ? 2.70311 1.29354 1.69869 -0.02406 0.14785  -0.26238 3   LYS A NZ    
10   N  N     . VAL A 4   ? 2.46118 1.41424 1.76638 -0.07208 0.04969  -0.15891 4   VAL A N     
11   C  CA    . VAL A 4   ? 2.38435 1.38650 1.74628 -0.03958 0.05192  -0.13203 4   VAL A CA    
12   C  C     . VAL A 4   ? 2.40686 1.36273 1.74423 0.02212  0.07921  -0.13066 4   VAL A C     
13   O  O     . VAL A 4   ? 2.47174 1.40804 1.77861 0.04970  0.09255  -0.14733 4   VAL A O     
14   C  CB    . VAL A 4   ? 2.16682 1.29103 1.60170 -0.03433 0.03120  -0.11828 4   VAL A CB    
15   C  CG1   . VAL A 4   ? 2.09257 1.25073 1.52540 0.00027  0.03714  -0.12913 4   VAL A CG1   
16   C  CG2   . VAL A 4   ? 2.01699 1.18763 1.50588 -0.01193 0.03155  -0.09191 4   VAL A CG2   
17   N  N     . ILE A 5   ? 2.20060 1.13877 1.54963 0.04508  0.08827  -0.11028 5   ILE A N     
18   C  CA    . ILE A 5   ? 2.08811 0.97799 1.41152 0.10558  0.11206  -0.10528 5   ILE A CA    
19   C  C     . ILE A 5   ? 2.03279 0.98653 1.40918 0.13830  0.10707  -0.07763 5   ILE A C     
20   O  O     . ILE A 5   ? 2.00528 0.96683 1.40166 0.11281  0.09950  -0.06086 5   ILE A O     
21   C  CB    . ILE A 5   ? 2.19564 0.94844 1.44276 0.10113  0.13492  -0.11153 5   ILE A CB    
22   C  CG1   . ILE A 5   ? 2.19440 0.89925 1.41743 0.17091  0.15856  -0.10128 5   ILE A CG1   
23   C  CG2   . ILE A 5   ? 2.17843 0.90111 1.42567 0.05181  0.12898  -0.09919 5   ILE A CG2   
24   C  CD1   . ILE A 5   ? 2.15287 0.87200 1.36823 0.21839  0.17082  -0.11702 5   ILE A CD1   
25   N  N     . LEU A 6   ? 1.98601 0.98832 1.38511 0.19299  0.11167  -0.07373 6   LEU A N     
26   C  CA    . LEU A 6   ? 1.87461 0.93231 1.31456 0.22934  0.10729  -0.04973 6   LEU A CA    
27   C  C     . LEU A 6   ? 1.91366 0.90530 1.31463 0.28717  0.12742  -0.04215 6   LEU A C     
28   O  O     . LEU A 6   ? 1.97858 0.95281 1.35997 0.32364  0.14116  -0.05568 6   LEU A O     
29   C  CB    . LEU A 6   ? 1.91999 1.09725 1.42236 0.24482  0.09345  -0.04988 6   LEU A CB    
30   C  CG    . LEU A 6   ? 1.81209 1.05364 1.35564 0.27986  0.08675  -0.02820 6   LEU A CG    
31   C  CD1   . LEU A 6   ? 1.69786 0.94110 1.25518 0.24960  0.07746  -0.00893 6   LEU A CD1   
32   C  CD2   . LEU A 6   ? 1.67646 1.02805 1.27528 0.29144  0.07605  -0.03319 6   LEU A CD2   
33   N  N     . LYS A 7   ? 1.94519 0.89946 1.33362 0.29711  0.13037  -0.01966 7   LYS A N     
34   C  CA    . LYS A 7   ? 1.95875 0.85044 1.30846 0.34888  0.14713  -0.00707 7   LYS A CA    
35   C  C     . LYS A 7   ? 1.88928 0.86597 1.28300 0.39366  0.13546  0.01460  7   LYS A C     
36   O  O     . LYS A 7   ? 1.82039 0.83818 1.24206 0.37859  0.12207  0.02950  7   LYS A O     
37   C  CB    . LYS A 7   ? 1.96409 0.76345 1.26678 0.31826  0.15824  0.00321  7   LYS A CB    
38   C  CG    . LYS A 7   ? 2.03169 0.75353 1.29226 0.26561  0.16699  -0.01966 7   LYS A CG    
39   C  CD    . LYS A 7   ? 2.15318 0.81513 1.39056 0.21360  0.17035  -0.01072 7   LYS A CD    
40   C  CE    . LYS A 7   ? 2.08478 0.67432 1.27598 0.23092  0.18970  0.00243  7   LYS A CE    
41   N  NZ    . LYS A 7   ? 2.21778 0.75092 1.38692 0.17548  0.19575  0.00839  7   LYS A NZ    
42   N  N     . ILE A 8   ? 1.90379 0.91522 1.30674 0.44406  0.13959  0.01579  8   ILE A N     
43   C  CA    . ILE A 8   ? 1.87788 0.98138 1.32475 0.48515  0.12576  0.03240  8   ILE A CA    
44   C  C     . ILE A 8   ? 1.91352 0.98604 1.33305 0.52441  0.13384  0.04885  8   ILE A C     
45   O  O     . ILE A 8   ? 2.01164 1.03499 1.40174 0.54213  0.15045  0.04035  8   ILE A O     
46   C  CB    . ILE A 8   ? 1.70805 0.90974 1.20644 0.50806  0.11915  0.01706  8   ILE A CB    
47   C  CG1   . ILE A 8   ? 1.70799 0.95079 1.23555 0.46898  0.10904  0.00320  8   ILE A CG1   
48   C  CG2   . ILE A 8   ? 1.71219 1.00884 1.25358 0.54871  0.10488  0.03258  8   ILE A CG2   
49   C  CD1   . ILE A 8   ? 1.83451 1.03849 1.34115 0.43517  0.11954  -0.02229 8   ILE A CD1   
50   N  N     . LYS A 9   ? 1.80446 0.90285 1.23004 0.53824  0.12270  0.07225  9   LYS A N     
51   C  CA    . LYS A 9   ? 1.92378 1.00995 1.32844 0.58113  0.12550  0.09007  9   LYS A CA    
52   C  C     . LYS A 9   ? 1.89734 1.10012 1.35512 0.61782  0.10545  0.09697  9   LYS A C     
53   O  O     . LYS A 9   ? 1.89572 1.16225 1.38494 0.60484  0.08783  0.10313  9   LYS A O     
54   C  CB    . LYS A 9   ? 2.03504 1.05100 1.39464 0.56629  0.12957  0.11145  9   LYS A CB    
55   N  N     . ARG A 10  ? 1.91810 1.14972 1.38636 0.66161  0.10850  0.09526  10  ARG A N     
56   C  CA    . ARG A 10  ? 1.86978 1.21847 1.39307 0.69394  0.08972  0.09846  10  ARG A CA    
57   C  C     . ARG A 10  ? 1.95784 1.30764 1.46229 0.73054  0.08135  0.12287  10  ARG A C     
58   O  O     . ARG A 10  ? 2.08107 1.34657 1.53504 0.74966  0.09608  0.13328  10  ARG A O     
59   C  CB    . ARG A 10  ? 1.94187 1.33771 1.49898 0.71799  0.09780  0.07997  10  ARG A CB    
60   C  CG    . ARG A 10  ? 1.95167 1.35608 1.52785 0.68461  0.10542  0.05459  10  ARG A CG    
61   C  CD    . ARG A 10  ? 1.96293 1.44790 1.58741 0.70823  0.10940  0.03789  10  ARG A CD    
62   N  NE    . ARG A 10  ? 1.95262 1.39757 1.55564 0.74710  0.12691  0.03893  10  ARG A NE    
63   C  CZ    . ARG A 10  ? 2.02562 1.53942 1.66953 0.77943  0.13150  0.03084  10  ARG A CZ    
64   N  NH1   . ARG A 10  ? 2.00473 1.63345 1.71362 0.77556  0.11998  0.02059  10  ARG A NH1   
65   N  NH2   . ARG A 10  ? 2.09976 1.56588 1.71924 0.81568  0.14948  0.03298  10  ARG A NH2   
66   N  N     . LEU A 11  ? 1.97078 1.41455 1.51282 0.73948  0.05774  0.13132  11  LEU A N     
67   C  CA    . LEU A 11  ? 1.98677 1.44416 1.51309 0.77263  0.04521  0.15390  11  LEU A CA    
68   C  C     . LEU A 11  ? 2.10400 1.63571 1.66658 0.82039  0.03846  0.15296  11  LEU A C     
69   O  O     . LEU A 11  ? 2.05671 1.65321 1.66854 0.82219  0.03983  0.13413  11  LEU A O     
70   C  CB    . LEU A 11  ? 1.97461 1.49014 1.51655 0.75293  0.02278  0.16265  11  LEU A CB    
71   C  CG    . LEU A 11  ? 1.89273 1.35265 1.41132 0.70407  0.02854  0.16299  11  LEU A CG    
72   C  CD1   . LEU A 11  ? 1.70919 1.22034 1.23574 0.69098  0.00857  0.17422  11  LEU A CD1   
73   C  CD2   . LEU A 11  ? 1.96699 1.29765 1.41858 0.69535  0.05077  0.17330  11  LEU A CD2   
74   N  N     . PRO A 12  ? 2.27024 1.79299 1.80890 0.86010  0.03228  0.17351  12  PRO A N     
75   C  CA    . PRO A 12  ? 2.28912 1.88414 1.86431 0.90868  0.02535  0.17467  12  PRO A CA    
76   C  C     . PRO A 12  ? 2.19221 1.92562 1.84598 0.90411  0.00626  0.15954  12  PRO A C     
77   O  O     . PRO A 12  ? 2.19035 1.97551 1.88566 0.92640  0.01213  0.14769  12  PRO A O     
78   C  CB    . PRO A 12  ? 2.36803 1.94728 1.90706 0.94219  0.01253  0.20192  12  PRO A CB    
79   C  CG    . PRO A 12  ? 2.41638 1.87792 1.88421 0.91647  0.02497  0.21428  12  PRO A CG    
80   C  CD    . PRO A 12  ? 2.36897 1.79255 1.83775 0.86432  0.03883  0.19571  12  PRO A CD    
81   N  N     . HIS A 13  ? 2.02127 1.81488 1.69601 0.87445  -0.01448 0.15880  13  HIS A N     
82   C  CA    . HIS A 13  ? 1.85702 1.78086 1.60364 0.86612  -0.03209 0.14364  13  HIS A CA    
83   C  C     . HIS A 13  ? 1.79519 1.73751 1.57686 0.83399  -0.01839 0.11807  13  HIS A C     
84   O  O     . HIS A 13  ? 1.76195 1.80726 1.60150 0.81975  -0.02994 0.10354  13  HIS A O     
85   C  CB    . HIS A 13  ? 1.77182 1.75048 1.52424 0.84465  -0.05818 0.15046  13  HIS A CB    
86   C  CG    . HIS A 13  ? 1.80813 1.73301 1.53397 0.79868  -0.05351 0.14802  13  HIS A CG    
87   N  ND1   . HIS A 13  ? 1.65178 1.63748 1.39863 0.76773  -0.07125 0.14358  13  HIS A ND1   
88   C  CD2   . HIS A 13  ? 1.83329 1.65005 1.51401 0.77807  -0.03281 0.14942  13  HIS A CD2   
89   C  CE1   . HIS A 13  ? 1.53556 1.45401 1.25345 0.73300  -0.06117 0.14359  13  HIS A CE1   
90   N  NE2   . HIS A 13  ? 1.62171 1.43931 1.30081 0.73735  -0.03853 0.14706  13  HIS A NE2   
91   N  N     . ALA A 14  ? 1.85382 1.69856 1.59975 0.82072  0.00599  0.11170  14  ALA A N     
92   C  CA    . ALA A 14  ? 1.82216 1.67415 1.59342 0.79309  0.02053  0.08764  14  ALA A CA    
93   C  C     . ALA A 14  ? 1.94892 1.72195 1.69287 0.80988  0.04834  0.08007  14  ALA A C     
94   O  O     . ALA A 14  ? 1.90886 1.63756 1.64285 0.78291  0.06488  0.06335  14  ALA A O     
95   C  CB    . ALA A 14  ? 1.69789 1.51235 1.45218 0.74499  0.01969  0.08332  14  ALA A CB    
96   N  N     . GLN A 15  ? 1.93853 1.69109 1.66727 0.85479  0.05389  0.09193  15  GLN A N     
97   C  CA    . GLN A 15  ? 1.98875 1.66047 1.68612 0.87422  0.08176  0.08553  15  GLN A CA    
98   C  C     . GLN A 15  ? 2.07412 1.81638 1.82431 0.89237  0.09285  0.06665  15  GLN A C     
99   O  O     . GLN A 15  ? 2.10586 1.78484 1.83360 0.89683  0.11889  0.05388  15  GLN A O     
100  C  CB    . GLN A 15  ? 2.14239 1.74696 1.79213 0.91602  0.08586  0.10830  15  GLN A CB    
101  C  CG    . GLN A 15  ? 2.21424 1.68863 1.80121 0.92056  0.11593  0.10537  15  GLN A CG    
102  C  CD    . GLN A 15  ? 2.25912 1.62574 1.78256 0.88236  0.12125  0.11179  15  GLN A CD    
103  O  OE1   . GLN A 15  ? 2.28043 1.59127 1.75923 0.89361  0.11840  0.13332  15  GLN A OE1   
104  N  NE2   . GLN A 15  ? 2.16614 1.50388 1.68530 0.83623  0.12944  0.09315  15  GLN A NE2   
105  N  N     . ASP A 16  ? 2.17107 2.04140 1.98922 0.90053  0.07509  0.06356  16  ASP A N     
106  C  CA    . ASP A 16  ? 2.11599 2.06343 1.99080 0.91499  0.08661  0.04556  16  ASP A CA    
107  C  C     . ASP A 16  ? 1.98975 1.98431 1.89946 0.87136  0.09163  0.02106  16  ASP A C     
108  O  O     . ASP A 16  ? 1.91334 1.93990 1.85386 0.87613  0.11064  0.00267  16  ASP A O     
109  C  CB    . ASP A 16  ? 2.08846 2.15438 2.02181 0.94795  0.06632  0.05471  16  ASP A CB    
110  C  CG    . ASP A 16  ? 2.11357 2.28755 2.09592 0.91585  0.03968  0.05055  16  ASP A CG    
111  O  OD1   . ASP A 16  ? 2.10086 2.24469 2.05519 0.88329  0.02696  0.05559  16  ASP A OD1   
112  O  OD2   . ASP A 16  ? 2.15743 2.44604 2.20634 0.92201  0.03266  0.04163  16  ASP A OD2   
113  N  N     . LEU A 17  ? 1.95803 1.95715 1.86289 0.83020  0.07671  0.02048  17  LEU A N     
114  C  CA    . LEU A 17  ? 1.89451 1.93134 1.82699 0.78962  0.08217  -0.00162 17  LEU A CA    
115  C  C     . LEU A 17  ? 1.94682 1.88277 1.83378 0.77449  0.10964  -0.01650 17  LEU A C     
116  O  O     . LEU A 17  ? 1.99452 1.82093 1.82097 0.78197  0.11924  -0.00792 17  LEU A O     
117  C  CB    . LEU A 17  ? 1.82030 1.87985 1.75511 0.75202  0.06009  0.00270  17  LEU A CB    
118  C  CG    . LEU A 17  ? 1.78354 1.94707 1.76104 0.75365  0.03159  0.01215  17  LEU A CG    
119  C  CD1   . LEU A 17  ? 1.72643 1.99918 1.76741 0.77434  0.03116  0.00331  17  LEU A CD1   
120  C  CD2   . LEU A 17  ? 1.79326 1.91528 1.73196 0.77492  0.01530  0.03787  17  LEU A CD2   
121  N  N     . PRO A 18  ? 1.90822 1.87668 1.81933 0.75109  0.12342  -0.03963 18  PRO A N     
122  C  CA    . PRO A 18  ? 1.91204 1.78402 1.77336 0.72957  0.14639  -0.05544 18  PRO A CA    
123  C  C     . PRO A 18  ? 1.87198 1.67217 1.68896 0.69469  0.13580  -0.04953 18  PRO A C     
124  O  O     . PRO A 18  ? 1.88459 1.73273 1.72354 0.67647  0.11404  -0.04131 18  PRO A O     
125  C  CB    . PRO A 18  ? 1.86985 1.81238 1.77202 0.70948  0.15926  -0.07989 18  PRO A CB    
126  C  CG    . PRO A 18  ? 1.78767 1.85379 1.76137 0.73143  0.15089  -0.07731 18  PRO A CG    
127  C  CD    . PRO A 18  ? 1.77452 1.86684 1.75589 0.74295  0.12094  -0.05332 18  PRO A CD    
128  N  N     . LEU A 19  ? 1.88904 1.57224 1.64255 0.68396  0.15205  -0.05441 19  LEU A N     
129  C  CA    . LEU A 19  ? 1.84079 1.45147 1.55238 0.64755  0.14437  -0.05065 19  LEU A CA    
130  C  C     . LEU A 19  ? 1.81530 1.47457 1.55133 0.61054  0.13881  -0.06628 19  LEU A C     
131  O  O     . LEU A 19  ? 1.84011 1.55005 1.60165 0.60718  0.15048  -0.08549 19  LEU A O     
132  C  CB    . LEU A 19  ? 1.87516 1.35405 1.51451 0.63675  0.16411  -0.05721 19  LEU A CB    
133  C  CG    . LEU A 19  ? 2.08993 1.50027 1.69246 0.67055  0.17464  -0.04345 19  LEU A CG    
134  C  CD1   . LEU A 19  ? 1.82889 1.24056 1.43385 0.69984  0.19804  -0.05780 19  LEU A CD1   
135  C  CD2   . LEU A 19  ? 2.11528 1.39736 1.64623 0.64370  0.18114  -0.03947 19  LEU A CD2   
136  N  N     . PRO A 20  ? 1.70124 1.34673 1.42964 0.58279  0.12254  -0.05801 20  PRO A N     
137  C  CA    . PRO A 20  ? 1.70013 1.38723 1.44901 0.53907  0.11604  -0.07103 20  PRO A CA    
138  C  C     . PRO A 20  ? 1.67300 1.29960 1.38357 0.50835  0.13308  -0.09234 20  PRO A C     
139  O  O     . PRO A 20  ? 1.71081 1.23233 1.36351 0.49924  0.14190  -0.09417 20  PRO A O     
140  C  CB    . PRO A 20  ? 1.66890 1.33627 1.41115 0.50401  0.09532  -0.05316 20  PRO A CB    
141  C  CG    . PRO A 20  ? 1.59982 1.17205 1.29263 0.53142  0.10047  -0.03754 20  PRO A CG    
142  C  CD    . PRO A 20  ? 1.64386 1.24146 1.34775 0.58143  0.10880  -0.03449 20  PRO A CD    
143  N  N     . SER A 21  ? 1.63037 1.32210 1.36973 0.49055  0.13816  -0.10898 21  SER A N     
144  C  CA    . SER A 21  ? 1.61827 1.26125 1.31917 0.46384  0.15451  -0.13009 21  SER A CA    
145  C  C     . SER A 21  ? 1.49598 1.21057 1.22821 0.42057  0.14659  -0.13811 21  SER A C     
146  O  O     . SER A 21  ? 1.37262 1.17250 1.15703 0.41433  0.13204  -0.12940 21  SER A O     
147  C  CB    . SER A 21  ? 1.51335 1.13661 1.19793 0.50930  0.18459  -0.14583 21  SER A CB    
148  O  OG    . SER A 21  ? 1.39617 1.12635 1.14314 0.54422  0.18914  -0.14649 21  SER A OG    
149  N  N     . TYR A 22  ? 1.55706 1.23046 1.25099 0.38995  0.15675  -0.15489 22  TYR A N     
150  C  CA    . TYR A 22  ? 1.48602 1.21213 1.19688 0.34984  0.15195  -0.16197 22  TYR A CA    
151  C  C     . TYR A 22  ? 1.41785 1.19914 1.14831 0.37011  0.17656  -0.17869 22  TYR A C     
152  O  O     . TYR A 22  ? 1.54876 1.28697 1.24662 0.39519  0.20151  -0.19355 22  TYR A O     
153  C  CB    . TYR A 22  ? 1.49898 1.15394 1.15471 0.30348  0.14628  -0.16904 22  TYR A CB    
154  C  CG    . TYR A 22  ? 1.49619 1.10368 1.13774 0.27835  0.12343  -0.15375 22  TYR A CG    
155  C  CD1   . TYR A 22  ? 1.35657 1.01237 1.03525 0.25098  0.10019  -0.13778 22  TYR A CD1   
156  C  CD2   . TYR A 22  ? 1.54930 1.06166 1.13955 0.28098  0.12785  -0.15596 22  TYR A CD2   
157  C  CE1   . TYR A 22  ? 1.38721 1.00563 1.05771 0.22835  0.08233  -0.12396 22  TYR A CE1   
158  C  CE2   . TYR A 22  ? 1.57270 1.04549 1.15299 0.25443  0.10941  -0.14252 22  TYR A CE2   
159  C  CZ    . TYR A 22  ? 1.48262 1.01262 1.10583 0.22881  0.08685  -0.12634 22  TYR A CZ    
160  O  OH    . TYR A 22  ? 1.39874 0.89531 1.01677 0.20287  0.07139  -0.11309 22  TYR A OH    
161  N  N     . ALA A 23  ? 1.28576 1.16040 1.06848 0.35812  0.17196  -0.17697 23  ALA A N     
162  C  CA    . ALA A 23  ? 1.38396 1.32130 1.19225 0.37204  0.19671  -0.19262 23  ALA A CA    
163  C  C     . ALA A 23  ? 1.35486 1.24767 1.11208 0.34468  0.21534  -0.21028 23  ALA A C     
164  O  O     . ALA A 23  ? 1.32581 1.23747 1.08273 0.36301  0.24469  -0.22678 23  ALA A O     
165  C  CB    . ALA A 23  ? 1.19484 1.23754 1.06751 0.35809  0.18716  -0.18710 23  ALA A CB    
166  N  N     . THR A 24  ? 1.37744 1.21393 1.09102 0.30171  0.19895  -0.20688 24  THR A N     
167  C  CA    . THR A 24  ? 1.45069 1.24080 1.10731 0.27191  0.21075  -0.22150 24  THR A CA    
168  C  C     . THR A 24  ? 1.54082 1.23752 1.13793 0.24727  0.19263  -0.21882 24  THR A C     
169  O  O     . THR A 24  ? 1.49870 1.18978 1.11141 0.23588  0.16621  -0.20174 24  THR A O     
170  C  CB    . THR A 24  ? 1.41776 1.26219 1.09093 0.23456  0.20587  -0.21866 24  THR A CB    
171  O  OG1   . THR A 24  ? 1.37206 1.30992 1.10925 0.25174  0.21870  -0.21942 24  THR A OG1   
172  C  CG2   . THR A 24  ? 1.61304 1.41538 1.22450 0.21039  0.22294  -0.23433 24  THR A CG2   
173  N  N     . PRO A 25  ? 1.64323 1.26606 1.17108 0.23759  0.20736  -0.23651 25  PRO A N     
174  C  CA    . PRO A 25  ? 1.68397 1.22099 1.15307 0.20696  0.18871  -0.23667 25  PRO A CA    
175  C  C     . PRO A 25  ? 1.67398 1.23123 1.15787 0.16481  0.15307  -0.21861 25  PRO A C     
176  O  O     . PRO A 25  ? 1.63423 1.14135 1.09515 0.14413  0.13274  -0.21282 25  PRO A O     
177  C  CB    . PRO A 25  ? 1.79311 1.27343 1.18862 0.19267  0.20934  -0.26010 25  PRO A CB    
178  C  CG    . PRO A 25  ? 1.68847 1.20514 1.10207 0.23265  0.24766  -0.27387 25  PRO A CG    
179  C  CD    . PRO A 25  ? 1.61951 1.22765 1.12100 0.26394  0.24510  -0.25844 25  PRO A CD    
180  N  N     . HIS A 26  ? 1.76010 1.38935 1.28244 0.15164  0.14684  -0.20963 26  HIS A N     
181  C  CA    . HIS A 26  ? 1.74552 1.39807 1.28633 0.11780  0.11592  -0.19099 26  HIS A CA    
182  C  C     . HIS A 26  ? 1.74117 1.46457 1.35494 0.13051  0.10652  -0.17293 26  HIS A C     
183  O  O     . HIS A 26  ? 1.69374 1.45132 1.33043 0.10764  0.08886  -0.15864 26  HIS A O     
184  C  CB    . HIS A 26  ? 1.74895 1.41100 1.26068 0.08721  0.11438  -0.19345 26  HIS A CB    
185  C  CG    . HIS A 26  ? 1.88712 1.47787 1.31945 0.06740  0.11721  -0.20969 26  HIS A CG    
186  N  ND1   . HIS A 26  ? 1.98231 1.55431 1.37129 0.07412  0.14671  -0.22977 26  HIS A ND1   
187  C  CD2   . HIS A 26  ? 1.98553 1.52029 1.37231 0.03899  0.09447  -0.21001 26  HIS A CD2   
188  C  CE1   . HIS A 26  ? 2.14435 1.64645 1.45863 0.05099  0.14177  -0.24216 26  HIS A CE1   
189  N  NE2   . HIS A 26  ? 2.13520 1.61544 1.44773 0.02824  0.10874  -0.23078 26  HIS A NE2   
190  N  N     . SER A 27  ? 1.58188 1.32608 1.22935 0.16762  0.11789  -0.17312 27  SER A N     
191  C  CA    . SER A 27  ? 1.37859 1.18534 1.08809 0.17861  0.10697  -0.15708 27  SER A CA    
192  C  C     . SER A 27  ? 1.36840 1.14794 1.08189 0.16526  0.08213  -0.13995 27  SER A C     
193  O  O     . SER A 27  ? 1.43538 1.14948 1.11396 0.16417  0.07870  -0.14143 27  SER A O     
194  C  CB    . SER A 27  ? 1.30934 1.14887 1.05073 0.22375  0.12333  -0.16129 27  SER A CB    
195  O  OG    . SER A 27  ? 1.42962 1.32017 1.18719 0.23389  0.14586  -0.17478 27  SER A OG    
196  N  N     . SER A 28  ? 1.34221 1.17039 1.09732 0.15366  0.06721  -0.12443 28  SER A N     
197  C  CA    . SER A 28  ? 1.30821 1.11752 1.07082 0.13818  0.04608  -0.10769 28  SER A CA    
198  C  C     . SER A 28  ? 1.25796 1.06139 1.03819 0.16608  0.04586  -0.09949 28  SER A C     
199  O  O     . SER A 28  ? 1.25739 1.01343 1.02189 0.15931  0.03722  -0.09176 28  SER A O     
200  C  CB    . SER A 28  ? 1.23497 1.09181 1.03004 0.11612  0.03325  -0.09444 28  SER A CB    
201  O  OG    . SER A 28  ? 1.27860 1.12131 1.08398 0.10163  0.01540  -0.07846 28  SER A OG    
202  N  N     . GLY A 29  ? 1.32226 1.17381 1.13356 0.19633  0.05495  -0.10058 29  GLY A N     
203  C  CA    . GLY A 29  ? 1.34408 1.19877 1.17248 0.22395  0.05152  -0.08954 29  GLY A CA    
204  C  C     . GLY A 29  ? 1.34675 1.20026 1.17125 0.26755  0.06717  -0.09796 29  GLY A C     
205  O  O     . GLY A 29  ? 1.28903 1.17471 1.12059 0.27927  0.08184  -0.11221 29  GLY A O     
206  N  N     . LEU A 30  ? 1.24272 1.05954 1.05636 0.29308  0.06529  -0.08781 30  LEU A N     
207  C  CA    . LEU A 30  ? 1.26738 1.08259 1.07917 0.34210  0.07813  -0.09089 30  LEU A CA    
208  C  C     . LEU A 30  ? 1.24000 1.14589 1.10336 0.36643  0.07202  -0.08504 30  LEU A C     
209  O  O     . LEU A 30  ? 1.22319 1.16961 1.11239 0.34819  0.05664  -0.07467 30  LEU A O     
210  C  CB    . LEU A 30  ? 1.38875 1.12144 1.16228 0.36040  0.07852  -0.07971 30  LEU A CB    
211  C  CG    . LEU A 30  ? 1.43740 1.07559 1.15840 0.32998  0.08142  -0.08414 30  LEU A CG    
212  C  CD1   . LEU A 30  ? 1.45461 1.02734 1.15030 0.33366  0.07690  -0.06733 30  LEU A CD1   
213  C  CD2   . LEU A 30  ? 1.49457 1.08177 1.17583 0.34503  0.10272  -0.10368 30  LEU A CD2   
214  N  N     . ASP A 31  ? 1.30849 1.24719 1.18656 0.40810  0.08446  -0.09241 31  ASP A N     
215  C  CA    . ASP A 31  ? 1.26713 1.29939 1.19620 0.43226  0.07658  -0.08805 31  ASP A CA    
216  C  C     . ASP A 31  ? 1.34135 1.35869 1.26506 0.45887  0.06133  -0.06738 31  ASP A C     
217  O  O     . ASP A 31  ? 1.36509 1.30780 1.25043 0.48597  0.06657  -0.05927 31  ASP A O     
218  C  CB    . ASP A 31  ? 1.31866 1.39996 1.27148 0.47053  0.09456  -0.10169 31  ASP A CB    
219  C  CG    . ASP A 31  ? 1.60266 1.60997 1.51705 0.51442  0.11048  -0.10171 31  ASP A CG    
220  O  OD1   . ASP A 31  ? 1.56656 1.56394 1.47872 0.55586  0.10353  -0.08664 31  ASP A OD1   
221  O  OD2   . ASP A 31  ? 1.60334 1.55742 1.48464 0.50773  0.13072  -0.11670 31  ASP A OD2   
222  N  N     . LEU A 32  ? 1.19493 1.27797 1.15155 0.44960  0.04367  -0.05906 32  LEU A N     
223  C  CA    . LEU A 32  ? 1.11048 1.19191 1.06216 0.47400  0.02784  -0.03943 32  LEU A CA    
224  C  C     . LEU A 32  ? 1.12408 1.30508 1.12070 0.50791  0.01922  -0.04039 32  LEU A C     
225  O  O     . LEU A 32  ? 1.08241 1.34745 1.12103 0.48563  0.01463  -0.05132 32  LEU A O     
226  C  CB    . LEU A 32  ? 1.12829 1.19975 1.07463 0.43450  0.01379  -0.02869 32  LEU A CB    
227  C  CG    . LEU A 32  ? 1.24124 1.21578 1.14443 0.40916  0.01767  -0.02069 32  LEU A CG    
228  C  CD1   . LEU A 32  ? 1.10541 1.08327 1.01124 0.37799  0.00553  -0.00861 32  LEU A CD1   
229  C  CD2   . LEU A 32  ? 0.96590 0.86038 0.82612 0.44455  0.02427  -0.00965 32  LEU A CD2   
230  N  N     . ARG A 33  ? 1.06099 1.23136 1.04756 0.55857  0.01675  -0.02847 33  ARG A N     
231  C  CA    . ARG A 33  ? 1.22982 1.48841 1.25612 0.57936  0.00728  -0.02746 33  ARG A CA    
232  C  C     . ARG A 33  ? 1.16832 1.43576 1.18322 0.59149  -0.01583 -0.00663 33  ARG A C     
233  O  O     . ARG A 33  ? 1.15048 1.33584 1.11784 0.59597  -0.01831 0.01019  33  ARG A O     
234  C  CB    . ARG A 33  ? 1.25894 1.49871 1.28212 0.61314  0.02398  -0.03012 33  ARG A CB    
235  C  CG    . ARG A 33  ? 1.13973 1.36621 1.16702 0.60211  0.04942  -0.05178 33  ARG A CG    
236  C  CD    . ARG A 33  ? 1.27401 1.46318 1.28807 0.63641  0.06869  -0.05354 33  ARG A CD    
237  N  NE    . ARG A 33  ? 1.39025 1.58946 1.41604 0.62586  0.09337  -0.07637 33  ARG A NE    
238  C  CZ    . ARG A 33  ? 1.35577 1.65020 1.43568 0.62491  0.10011  -0.08934 33  ARG A CZ    
239  N  NH1   . ARG A 33  ? 1.25737 1.64841 1.38724 0.63287  0.08232  -0.08306 33  ARG A NH1   
240  N  NH2   . ARG A 33  ? 1.37676 1.66783 1.45780 0.61335  0.12596  -0.10964 33  ARG A NH2   
241  N  N     . ALA A 34  ? 1.17992 1.54685 1.23631 0.59458  -0.03177 -0.00863 34  ALA A N     
242  C  CA    . ALA A 34  ? 1.20702 1.59536 1.25306 0.60455  -0.05541 0.00825  34  ALA A CA    
243  C  C     . ALA A 34  ? 1.22089 1.59013 1.25119 0.64951  -0.05680 0.02303  34  ALA A C     
244  O  O     . ALA A 34  ? 1.20770 1.64662 1.27676 0.66926  -0.05778 0.01710  34  ALA A O     
245  C  CB    . ALA A 34  ? 1.04573 1.54889 1.14018 0.58335  -0.07281 -0.00302 34  ALA A CB    
246  N  N     . ALA A 35  ? 1.22349 1.49836 1.19738 0.66521  -0.05576 0.04268  35  ALA A N     
247  C  CA    . ALA A 35  ? 1.40792 1.65179 1.35815 0.70869  -0.05595 0.05911  35  ALA A CA    
248  C  C     . ALA A 35  ? 1.35523 1.65521 1.30743 0.72078  -0.08263 0.07296  35  ALA A C     
249  O  O     . ALA A 35  ? 1.35801 1.60116 1.26215 0.72703  -0.09016 0.09207  35  ALA A O     
250  C  CB    . ALA A 35  ? 1.48153 1.59419 1.36684 0.71600  -0.03989 0.07256  35  ALA A CB    
251  N  N     . ILE A 36  ? 1.31267 1.72673 1.32042 0.72198  -0.09647 0.06231  36  ILE A N     
252  C  CA    . ILE A 36  ? 1.33676 1.81805 1.35174 0.73032  -0.12412 0.07168  36  ILE A CA    
253  C  C     . ILE A 36  ? 1.43397 1.97456 1.47988 0.77193  -0.12998 0.07570  36  ILE A C     
254  O  O     . ILE A 36  ? 1.34986 1.87001 1.40663 0.79566  -0.11059 0.07255  36  ILE A O     
255  C  CB    . ILE A 36  ? 1.30375 1.87396 1.35635 0.68845  -0.13917 0.05497  36  ILE A CB    
256  C  CG1   . ILE A 36  ? 1.30426 1.95716 1.42174 0.67398  -0.12952 0.03091  36  ILE A CG1   
257  C  CG2   . ILE A 36  ? 1.18572 1.69578 1.20588 0.65224  -0.13440 0.05409  36  ILE A CG2   
258  C  CD1   . ILE A 36  ? 1.14417 1.87875 1.29716 0.62829  -0.14030 0.01223  36  ILE A CD1   
259  N  N     . GLU A 37  ? 1.68469 2.29928 1.74450 0.78145  -0.15675 0.08257  37  GLU A N     
260  C  CA    . GLU A 37  ? 1.65870 2.33950 1.75126 0.82240  -0.16672 0.08853  37  GLU A CA    
261  C  C     . GLU A 37  ? 1.67910 2.49571 1.84499 0.80218  -0.17980 0.06859  37  GLU A C     
262  O  O     . GLU A 37  ? 1.62149 2.48631 1.83714 0.81012  -0.16583 0.05576  37  GLU A O     
263  C  CB    . GLU A 37  ? 1.73004 2.38876 1.77948 0.85359  -0.18825 0.11413  37  GLU A CB    
264  N  N     . LYS A 38  ? 1.50458 2.38232 1.67685 0.77432  -0.20481 0.06491  38  LYS A N     
265  C  CA    . LYS A 38  ? 1.35185 2.35528 1.58907 0.74668  -0.21759 0.04439  38  LYS A CA    
266  C  C     . LYS A 38  ? 1.34258 2.35069 1.59342 0.69195  -0.20449 0.02143  38  LYS A C     
267  O  O     . LYS A 38  ? 1.19461 2.11476 1.40312 0.67621  -0.19152 0.02362  38  LYS A O     
268  C  CB    . LYS A 38  ? 1.17323 2.23830 1.40549 0.74495  -0.25278 0.05201  38  LYS A CB    
269  N  N     . PRO A 39  ? 1.30243 2.41200 1.61272 0.66103  -0.20652 -0.00088 39  PRO A N     
270  C  CA    . PRO A 39  ? 1.20164 2.31746 1.52187 0.60643  -0.19540 -0.02244 39  PRO A CA    
271  C  C     . PRO A 39  ? 1.17743 2.26787 1.45532 0.57655  -0.21260 -0.01992 39  PRO A C     
272  O  O     . PRO A 39  ? 1.19550 2.28244 1.44253 0.59222  -0.23582 -0.00454 39  PRO A O     
273  C  CB    . PRO A 39  ? 1.17505 2.41126 1.56526 0.58169  -0.19715 -0.04448 39  PRO A CB    
274  C  CG    . PRO A 39  ? 1.12535 2.42930 1.53834 0.61796  -0.21973 -0.03311 39  PRO A CG    
275  C  CD    . PRO A 39  ? 1.16737 2.38721 1.54097 0.67454  -0.21479 -0.00791 39  PRO A CD    
276  N  N     . LEU A 40  ? 1.16955 2.24068 1.44462 0.53322  -0.20005 -0.03513 40  LEU A N     
277  C  CA    . LEU A 40  ? 1.16186 2.20385 1.39783 0.50220  -0.21143 -0.03487 40  LEU A CA    
278  C  C     . LEU A 40  ? 1.15940 2.28934 1.42952 0.45086  -0.22002 -0.05945 40  LEU A C     
279  O  O     . LEU A 40  ? 1.18739 2.35439 1.49826 0.42209  -0.20266 -0.07975 40  LEU A O     
280  C  CB    . LEU A 40  ? 1.14462 2.09054 1.34720 0.49215  -0.19075 -0.03192 40  LEU A CB    
281  N  N     . LYS A 41  ? 1.21466 2.37264 1.46363 0.43719  -0.24537 -0.05804 41  LYS A N     
282  C  CA    . LYS A 41  ? 1.21989 2.45204 1.49098 0.38404  -0.25459 -0.08211 41  LYS A CA    
283  C  C     . LYS A 41  ? 1.20959 2.38610 1.44556 0.34495  -0.24581 -0.08993 41  LYS A C     
284  O  O     . LYS A 41  ? 1.18063 2.32239 1.36701 0.33807  -0.26044 -0.08243 41  LYS A O     
285  C  CB    . LYS A 41  ? 1.17093 2.45987 1.43382 0.38693  -0.28667 -0.07820 41  LYS A CB    
286  N  N     . ILE A 42  ? 1.16106 2.32803 1.42132 0.31947  -0.22088 -0.10482 42  ILE A N     
287  C  CA    . ILE A 42  ? 1.19510 2.31091 1.42860 0.28414  -0.21005 -0.11225 42  ILE A CA    
288  C  C     . ILE A 42  ? 1.15524 2.32673 1.39498 0.22602  -0.21709 -0.13725 42  ILE A C     
289  O  O     . ILE A 42  ? 1.10202 2.32671 1.38442 0.19153  -0.20409 -0.15898 42  ILE A O     
290  C  CB    . ILE A 42  ? 1.20601 2.28726 1.46134 0.28050  -0.18077 -0.11724 42  ILE A CB    
291  C  CG1   . ILE A 42  ? 1.21202 2.22844 1.45390 0.33459  -0.17241 -0.09442 42  ILE A CG1   
292  C  CG2   . ILE A 42  ? 1.15185 2.15183 1.37006 0.23525  -0.16237 -0.12236 42  ILE A CG2   
293  C  CD1   . ILE A 42  ? 1.10945 2.01388 1.29882 0.33958  -0.16272 -0.07776 42  ILE A CD1   
294  N  N     . LYS A 43  ? 1.22450 2.37682 1.41599 0.21278  -0.23531 -0.13472 43  LYS A N     
295  C  CA    . LYS A 43  ? 1.18812 2.37168 1.37230 0.15272  -0.23809 -0.16015 43  LYS A CA    
296  C  C     . LYS A 43  ? 1.29297 2.39871 1.45871 0.11193  -0.20636 -0.17014 43  LYS A C     
297  O  O     . LYS A 43  ? 1.27544 2.28267 1.41085 0.12997  -0.18831 -0.15180 43  LYS A O     
298  C  CB    . LYS A 43  ? 1.20978 2.37883 1.33679 0.14945  -0.26262 -0.15439 43  LYS A CB    
299  N  N     . PRO A 44  ? 1.22417 2.35761 1.40444 0.05532  -0.19430 -0.19700 44  PRO A N     
300  C  CA    . PRO A 44  ? 1.11046 2.15034 1.26517 0.01750  -0.15946 -0.20292 44  PRO A CA    
301  C  C     . PRO A 44  ? 1.10051 2.04003 1.18587 0.01461  -0.15527 -0.19108 44  PRO A C     
302  O  O     . PRO A 44  ? 1.14911 2.10024 1.19887 0.01190  -0.17646 -0.19223 44  PRO A O     
303  C  CB    . PRO A 44  ? 1.08188 2.17752 1.25741 -0.04296 -0.15240 -0.23463 44  PRO A CB    
304  C  CG    . PRO A 44  ? 1.08580 2.29310 1.28034 -0.04400 -0.18876 -0.24593 44  PRO A CG    
305  C  CD    . PRO A 44  ? 1.07389 2.31605 1.29302 0.02274  -0.20828 -0.22145 44  PRO A CD    
306  N  N     . PHE A 45  ? 1.12689 1.97007 1.19349 0.01615  -0.12760 -0.17921 45  PHE A N     
307  C  CA    . PHE A 45  ? 1.09917 1.84388 1.10860 0.01606  -0.11668 -0.16603 45  PHE A CA    
308  C  C     . PHE A 45  ? 1.10013 1.82517 1.08179 0.06212  -0.13531 -0.14156 45  PHE A C     
309  O  O     . PHE A 45  ? 1.18772 1.85010 1.11823 0.06025  -0.13148 -0.13301 45  PHE A O     
310  C  CB    . PHE A 45  ? 1.08230 1.81002 1.05196 -0.03093 -0.11193 -0.18582 45  PHE A CB    
311  C  CG    . PHE A 45  ? 1.06944 1.77182 1.04673 -0.07655 -0.08370 -0.20447 45  PHE A CG    
312  C  CD1   . PHE A 45  ? 1.07783 1.71272 1.06128 -0.07230 -0.05659 -0.19319 45  PHE A CD1   
313  C  CD2   . PHE A 45  ? 1.09043 1.83468 1.06561 -0.12474 -0.08470 -0.23293 45  PHE A CD2   
314  C  CE1   . PHE A 45  ? 1.12461 1.73045 1.10928 -0.11116 -0.03060 -0.20744 45  PHE A CE1   
315  C  CE2   . PHE A 45  ? 1.07985 1.79094 1.05579 -0.16703 -0.05602 -0.24889 45  PHE A CE2   
316  C  CZ    . PHE A 45  ? 1.04653 1.68654 1.02594 -0.15814 -0.02876 -0.23486 45  PHE A CZ    
317  N  N     . GLU A 46  ? 1.10324 1.87546 1.11459 0.10451  -0.15264 -0.12941 46  GLU A N     
318  C  CA    . GLU A 46  ? 1.14164 1.88910 1.12355 0.15075  -0.16880 -0.10421 46  GLU A CA    
319  C  C     . GLU A 46  ? 1.14369 1.84171 1.13944 0.18651  -0.15526 -0.08431 46  GLU A C     
320  O  O     . GLU A 46  ? 1.02233 1.74403 1.06210 0.18830  -0.14512 -0.09081 46  GLU A O     
321  C  CB    . GLU A 46  ? 1.16015 2.00201 1.15499 0.17603  -0.20455 -0.10442 46  GLU A CB    
322  C  CG    . GLU A 46  ? 1.35073 2.16134 1.30262 0.22289  -0.22256 -0.07702 46  GLU A CG    
323  C  CD    . GLU A 46  ? 1.40897 2.13220 1.29174 0.20769  -0.21300 -0.06848 46  GLU A CD    
324  O  OE1   . GLU A 46  ? 1.45785 2.18618 1.31766 0.16575  -0.21199 -0.08719 46  GLU A OE1   
325  O  OE2   . GLU A 46  ? 1.42110 2.06830 1.27149 0.23617  -0.20399 -0.04399 46  GLU A OE2   
326  N  N     . ARG A 47  ? 1.16016 1.78634 1.11417 0.21228  -0.15367 -0.06095 47  ARG A N     
327  C  CA    . ARG A 47  ? 1.09488 1.66287 1.05124 0.24309  -0.14130 -0.04167 47  ARG A CA    
328  C  C     . ARG A 47  ? 1.14832 1.72581 1.09127 0.29468  -0.16144 -0.02176 47  ARG A C     
329  O  O     . ARG A 47  ? 1.05541 1.66351 0.97261 0.30712  -0.18405 -0.01688 47  ARG A O     
330  C  CB    . ARG A 47  ? 1.02914 1.50009 0.94957 0.22906  -0.11916 -0.02968 47  ARG A CB    
331  C  CG    . ARG A 47  ? 1.06178 1.49711 0.92665 0.23204  -0.12524 -0.01763 47  ARG A CG    
332  C  CD    . ARG A 47  ? 1.06749 1.41708 0.90591 0.21500  -0.09948 -0.00804 47  ARG A CD    
333  N  NE    . ARG A 47  ? 0.95287 1.26473 0.73537 0.22004  -0.10143 0.00466  47  ARG A NE    
334  C  CZ    . ARG A 47  ? 1.06274 1.38247 0.81469 0.19589  -0.10270 -0.00676 47  ARG A CZ    
335  N  NH1   . ARG A 47  ? 1.01814 1.37937 0.78978 0.16314  -0.10208 -0.03148 47  ARG A NH1   
336  N  NH2   . ARG A 47  ? 1.14207 1.42229 0.83754 0.20320  -0.10283 0.00634  47  ARG A NH2   
337  N  N     . VAL A 48  ? 1.07919 1.62538 1.03500 0.32535  -0.15280 -0.00988 48  VAL A N     
338  C  CA    . VAL A 48  ? 1.05315 1.59676 0.99550 0.37871  -0.16737 0.01011  48  VAL A CA    
339  C  C     . VAL A 48  ? 1.09068 1.54206 1.01567 0.39658  -0.14724 0.02644  48  VAL A C     
340  O  O     . VAL A 48  ? 1.03914 1.45624 0.98031 0.37248  -0.12627 0.01859  48  VAL A O     
341  C  CB    . VAL A 48  ? 1.01835 1.66017 1.01123 0.40581  -0.18361 0.00082  48  VAL A CB    
342  C  CG1   . VAL A 48  ? 0.73193 1.46075 0.72587 0.40724  -0.21422 -0.00427 48  VAL A CG1   
343  C  CG2   . VAL A 48  ? 0.85732 1.53697 0.90287 0.37590  -0.16683 -0.02267 48  VAL A CG2   
344  N  N     . LEU A 49  ? 1.05775 1.46741 0.94627 0.43852  -0.15442 0.04959  49  LEU A N     
345  C  CA    . LEU A 49  ? 1.17350 1.49023 1.03748 0.45667  -0.13643 0.06598  49  LEU A CA    
346  C  C     . LEU A 49  ? 1.21888 1.55382 1.09966 0.50647  -0.14159 0.07090  49  LEU A C     
347  O  O     . LEU A 49  ? 1.31045 1.65930 1.17499 0.53740  -0.15566 0.08255  49  LEU A O     
348  C  CB    . LEU A 49  ? 1.15611 1.39542 0.95686 0.46360  -0.13492 0.08970  49  LEU A CB    
349  C  CG    . LEU A 49  ? 1.19239 1.32527 0.96092 0.46748  -0.11289 0.10598  49  LEU A CG    
350  C  CD1   . LEU A 49  ? 1.08837 1.18996 0.87455 0.41952  -0.09135 0.09457  49  LEU A CD1   
351  C  CD2   . LEU A 49  ? 1.31887 1.38892 1.02276 0.48374  -0.11447 0.13155  49  LEU A CD2   
352  N  N     . ILE A 50  ? 1.24627 1.57169 1.15718 0.50322  -0.12468 0.05939  50  ILE A N     
353  C  CA    . ILE A 50  ? 1.36681 1.70508 1.29684 0.53905  -0.12112 0.05800  50  ILE A CA    
354  C  C     . ILE A 50  ? 1.45750 1.68461 1.34535 0.55597  -0.10270 0.07287  50  ILE A C     
355  O  O     . ILE A 50  ? 1.38245 1.54951 1.25831 0.53548  -0.08792 0.07192  50  ILE A O     
356  C  CB    . ILE A 50  ? 1.23466 1.63896 1.22254 0.52554  -0.11281 0.03339  50  ILE A CB    
357  C  CG1   . ILE A 50  ? 1.18146 1.70178 1.21364 0.51636  -0.13012 0.01883  50  ILE A CG1   
358  C  CG2   . ILE A 50  ? 1.31884 1.69036 1.31052 0.55184  -0.09626 0.03235  50  ILE A CG2   
359  C  CD1   . ILE A 50  ? 1.21437 1.77337 1.24973 0.47733  -0.14126 0.01027  50  ILE A CD1   
360  N  N     . PRO A 51  ? 1.57858 1.77492 1.44292 0.58991  -0.10249 0.08593  51  PRO A N     
361  C  CA    . PRO A 51  ? 1.62243 1.71236 1.44656 0.60300  -0.08269 0.09668  51  PRO A CA    
362  C  C     . PRO A 51  ? 1.58402 1.67347 1.43450 0.61089  -0.06652 0.08107  51  PRO A C     
363  O  O     . PRO A 51  ? 1.48784 1.65294 1.37965 0.62582  -0.07058 0.06972  51  PRO A O     
364  C  CB    . PRO A 51  ? 1.56775 1.63228 1.35535 0.63745  -0.09003 0.11680  51  PRO A CB    
365  C  CG    . PRO A 51  ? 1.51367 1.68916 1.34320 0.65258  -0.11085 0.10997  51  PRO A CG    
366  C  CD    . PRO A 51  ? 1.43763 1.69061 1.30580 0.61685  -0.12130 0.09299  51  PRO A CD    
367  N  N     . THR A 52  ? 1.42527 1.42773 1.25002 0.59895  -0.04718 0.08005  52  THR A N     
368  C  CA    . THR A 52  ? 1.32946 1.31229 1.16502 0.60619  -0.02927 0.06554  52  THR A CA    
369  C  C     . THR A 52  ? 1.49320 1.39680 1.28751 0.63662  -0.01630 0.07628  52  THR A C     
370  O  O     . THR A 52  ? 1.41476 1.31822 1.22019 0.65369  -0.00341 0.06521  52  THR A O     
371  C  CB    . THR A 52  ? 1.33851 1.27428 1.16917 0.57315  -0.01598 0.05424  52  THR A CB    
372  O  OG1   . THR A 52  ? 1.38071 1.21122 1.15828 0.56234  -0.00802 0.06920  52  THR A OG1   
373  C  CG2   . THR A 52  ? 1.24113 1.24860 1.10957 0.53823  -0.02670 0.04440  52  THR A CG2   
374  N  N     . GLY A 53  ? 1.51502 1.34999 1.26025 0.64332  -0.01744 0.09719  53  GLY A N     
375  C  CA    . GLY A 53  ? 1.61334 1.36321 1.31328 0.66922  -0.00306 0.10787  53  GLY A CA    
376  C  C     . GLY A 53  ? 1.63964 1.28676 1.30406 0.64964  0.01984  0.10141  53  GLY A C     
377  O  O     . GLY A 53  ? 1.74217 1.32749 1.37763 0.67014  0.03562  0.10185  53  GLY A O     
378  N  N     . LEU A 54  ? 1.59835 1.22443 1.26292 0.61000  0.02207  0.09506  54  LEU A N     
379  C  CA    . LEU A 54  ? 1.68260 1.21702 1.31605 0.58489  0.04119  0.08633  54  LEU A CA    
380  C  C     . LEU A 54  ? 1.73022 1.19178 1.32571 0.55392  0.04398  0.10094  54  LEU A C     
381  O  O     . LEU A 54  ? 1.68903 1.18882 1.29807 0.54031  0.03125  0.11045  54  LEU A O     
382  C  CB    . LEU A 54  ? 1.63783 1.21177 1.30751 0.56298  0.04309  0.06303  54  LEU A CB    
383  C  CG    . LEU A 54  ? 1.67694 1.27709 1.36607 0.58122  0.05389  0.04283  54  LEU A CG    
384  C  CD1   . LEU A 54  ? 1.57272 1.26723 1.30216 0.61763  0.04412  0.04472  54  LEU A CD1   
385  C  CD2   . LEU A 54  ? 1.59138 1.22067 1.30651 0.55333  0.05640  0.02120  54  LEU A CD2   
386  N  N     . ILE A 55  ? 1.83146 1.18799 1.37884 0.54073  0.06226  0.10193  55  ILE A N     
387  C  CA    . ILE A 55  ? 1.80703 1.08834 1.32002 0.50340  0.06957  0.11262  55  ILE A CA    
388  C  C     . ILE A 55  ? 1.74479 0.95921 1.24165 0.46919  0.08377  0.09511  55  ILE A C     
389  O  O     . ILE A 55  ? 1.81255 0.97156 1.28094 0.47802  0.09784  0.08508  55  ILE A O     
390  C  CB    . ILE A 55  ? 1.78771 0.99954 1.24927 0.51581  0.07843  0.13309  55  ILE A CB    
391  C  CG1   . ILE A 55  ? 1.76030 1.03635 1.23227 0.54552  0.06186  0.15049  55  ILE A CG1   
392  C  CG2   . ILE A 55  ? 1.72144 0.85123 1.14851 0.47098  0.09117  0.14079  55  ILE A CG2   
393  C  CD1   . ILE A 55  ? 1.85287 1.06324 1.27117 0.56252  0.06974  0.17140  55  ILE A CD1   
394  N  N     . LEU A 56  ? 1.59741 0.82314 1.11370 0.42576  0.07944  0.09033  56  LEU A N     
395  C  CA    . LEU A 56  ? 1.80078 1.00344 1.31961 0.38007  0.08516  0.06914  56  LEU A CA    
396  C  C     . LEU A 56  ? 1.82807 0.95051 1.31453 0.33329  0.09515  0.07543  56  LEU A C     
397  O  O     . LEU A 56  ? 1.75472 0.86401 1.23331 0.32544  0.09626  0.09528  56  LEU A O     
398  C  CB    . LEU A 56  ? 1.70861 1.01589 1.28983 0.35015  0.06952  0.05524  56  LEU A CB    
399  C  CG    . LEU A 56  ? 1.65978 1.06892 1.28566 0.38363  0.05675  0.05357  56  LEU A CG    
400  C  CD1   . LEU A 56  ? 1.50379 0.99697 1.18186 0.34612  0.04502  0.04129  56  LEU A CD1   
401  C  CD2   . LEU A 56  ? 1.67841 1.08598 1.29588 0.43042  0.06393  0.04286  56  LEU A CD2   
402  N  N     . GLU A 57  ? 1.75897 0.82925 1.22573 0.29981  0.10307  0.05722  57  GLU A N     
403  C  CA    . GLU A 57  ? 1.76945 0.78003 1.21655 0.24379  0.10988  0.05739  57  GLU A CA    
404  C  C     . GLU A 57  ? 1.86148 0.92186 1.34388 0.19691  0.09792  0.03600  57  GLU A C     
405  O  O     . GLU A 57  ? 2.00557 1.01995 1.45957 0.18373  0.10308  0.01614  57  GLU A O     
406  C  CB    . GLU A 57  ? 1.94869 0.82625 1.32123 0.24742  0.13214  0.05698  57  GLU A CB    
407  C  CG    . GLU A 57  ? 2.01483 0.82860 1.36471 0.19372  0.14192  0.06438  57  GLU A CG    
408  C  CD    . GLU A 57  ? 2.14429 0.85081 1.43181 0.18039  0.16166  0.05584  57  GLU A CD    
409  O  OE1   . GLU A 57  ? 2.08135 0.75325 1.35364 0.14286  0.16298  0.03302  57  GLU A OE1   
410  O  OE2   . GLU A 57  ? 2.22805 0.89489 1.48359 0.20493  0.17434  0.07091  57  GLU A OE2   
411  N  N     . ILE A 58  ? 1.72229 0.87363 1.26239 0.17352  0.08231  0.04049  58  ILE A N     
412  C  CA    . ILE A 58  ? 1.71271 0.92070 1.28988 0.13339  0.06815  0.02482  58  ILE A CA    
413  C  C     . ILE A 58  ? 1.84022 0.99804 1.40208 0.07751  0.07042  0.02079  58  ILE A C     
414  O  O     . ILE A 58  ? 1.85663 0.98354 1.41267 0.06026  0.07870  0.03600  58  ILE A O     
415  C  CB    . ILE A 58  ? 1.66383 0.97779 1.30440 0.13041  0.05317  0.03322  58  ILE A CB    
416  C  CG1   . ILE A 58  ? 1.60436 0.96111 1.25561 0.18226  0.05221  0.04027  58  ILE A CG1   
417  C  CG2   . ILE A 58  ? 1.67650 1.04947 1.35035 0.10319  0.03851  0.01786  58  ILE A CG2   
418  C  CD1   . ILE A 58  ? 1.45097 0.90138 1.15606 0.17907  0.04017  0.04724  58  ILE A CD1   
419  N  N     . PRO A 59  ? 1.90802 1.05677 1.46119 0.04620  0.06364  0.00044  59  PRO A N     
420  C  CA    . PRO A 59  ? 1.98998 1.10291 1.53377 -0.01200 0.06189  -0.00467 59  PRO A CA    
421  C  C     . PRO A 59  ? 1.99030 1.18169 1.59674 -0.04412 0.04946  0.00931  59  PRO A C     
422  O  O     . PRO A 59  ? 1.91484 1.19281 1.57133 -0.02881 0.03800  0.01642  59  PRO A O     
423  C  CB    . PRO A 59  ? 1.99865 1.10705 1.52468 -0.03317 0.05168  -0.02990 59  PRO A CB    
424  C  CG    . PRO A 59  ? 1.91537 1.01729 1.41994 0.01852  0.05911  -0.03868 59  PRO A CG    
425  C  CD    . PRO A 59  ? 1.78356 0.94881 1.32873 0.06181  0.05877  -0.01961 59  PRO A CD    
426  N  N     . GLU A 60  ? 2.19738 1.35619 1.80051 -0.08966 0.05392  0.01272  60  GLU A N     
427  C  CA    . GLU A 60  ? 2.09840 1.33215 1.76413 -0.12185 0.04474  0.02540  60  GLU A CA    
428  C  C     . GLU A 60  ? 1.98293 1.30134 1.69430 -0.14060 0.01914  0.01588  60  GLU A C     
429  O  O     . GLU A 60  ? 2.02484 1.32632 1.71057 -0.15307 0.00844  -0.00327 60  GLU A O     
430  C  CB    . GLU A 60  ? 2.22305 1.40775 1.87780 -0.17218 0.05535  0.02802  60  GLU A CB    
431  C  CG    . GLU A 60  ? 2.30452 1.45726 1.93690 -0.22211 0.04507  0.00621  60  GLU A CG    
432  C  CD    . GLU A 60  ? 2.46746 1.50469 2.01591 -0.21246 0.05939  -0.01058 60  GLU A CD    
433  O  OE1   . GLU A 60  ? 2.46187 1.47059 1.98009 -0.15832 0.06830  -0.01000 60  GLU A OE1   
434  O  OE2   . GLU A 60  ? 2.51516 1.49022 2.02802 -0.25958 0.06246  -0.02495 60  GLU A OE2   
435  N  N     . GLY A 61  ? 1.78896 1.19490 1.56380 -0.14073 0.01055  0.03000  61  GLY A N     
436  C  CA    . GLY A 61  ? 1.67482 1.16146 1.49247 -0.14886 -0.01247 0.02570  61  GLY A CA    
437  C  C     . GLY A 61  ? 1.66574 1.17682 1.47695 -0.10822 -0.01765 0.01952  61  GLY A C     
438  O  O     . GLY A 61  ? 1.67557 1.24702 1.51554 -0.11267 -0.03503 0.01686  61  GLY A O     
439  N  N     . TYR A 62  ? 1.61902 1.08675 1.39396 -0.06885 -0.00291 0.01794  62  TYR A N     
440  C  CA    . TYR A 62  ? 1.59689 1.09223 1.36963 -0.03013 -0.00491 0.01184  62  TYR A CA    
441  C  C     . TYR A 62  ? 1.51947 1.03615 1.30696 0.00790  0.00541  0.02639  62  TYR A C     
442  O  O     . TYR A 62  ? 1.56916 1.06435 1.35587 0.00793  0.01611  0.04055  62  TYR A O     
443  C  CB    . TYR A 62  ? 1.63814 1.06892 1.35376 -0.01524 0.00191  -0.00682 62  TYR A CB    
444  C  CG    . TYR A 62  ? 1.71368 1.12842 1.40799 -0.05033 -0.01001 -0.02479 62  TYR A CG    
445  C  CD1   . TYR A 62  ? 1.70459 1.18070 1.42222 -0.05873 -0.02705 -0.03009 62  TYR A CD1   
446  C  CD2   . TYR A 62  ? 1.73794 1.07134 1.38268 -0.07600 -0.00397 -0.03663 62  TYR A CD2   
447  C  CE1   . TYR A 62  ? 1.69879 1.16035 1.39086 -0.09067 -0.04010 -0.04574 62  TYR A CE1   
448  C  CE2   . TYR A 62  ? 1.82569 1.14366 1.44516 -0.11085 -0.01655 -0.05486 62  TYR A CE2   
449  C  CZ    . TYR A 62  ? 1.80532 1.18980 1.44841 -0.11736 -0.03575 -0.05892 62  TYR A CZ    
450  O  OH    . TYR A 62  ? 1.82513 1.19439 1.43729 -0.15187 -0.05034 -0.07625 62  TYR A OH    
451  N  N     . GLU A 63  ? 1.48136 1.04089 1.27985 0.03822  0.00233  0.02226  63  GLU A N     
452  C  CA    . GLU A 63  ? 1.36531 0.95442 1.17782 0.07230  0.00828  0.03321  63  GLU A CA    
453  C  C     . GLU A 63  ? 1.28251 0.89505 1.08933 0.10539  0.00766  0.02162  63  GLU A C     
454  O  O     . GLU A 63  ? 1.28182 0.89469 1.07916 0.10004  0.00388  0.00641  63  GLU A O     
455  C  CB    . GLU A 63  ? 1.31878 0.97231 1.18006 0.06045  0.00326  0.04550  63  GLU A CB    
456  C  CG    . GLU A 63  ? 1.23936 0.95135 1.13149 0.05000  -0.00923 0.03852  63  GLU A CG    
457  C  CD    . GLU A 63  ? 1.18004 0.95043 1.11293 0.05271  -0.00965 0.04945  63  GLU A CD    
458  O  OE1   . GLU A 63  ? 1.16329 0.93127 1.09932 0.06278  -0.00041 0.06094  63  GLU A OE1   
459  O  OE2   . GLU A 63  ? 1.00975 0.82301 0.96631 0.04514  -0.01789 0.04663  63  GLU A OE2   
460  N  N     . GLY A 64  ? 1.15727 0.79223 0.96970 0.13827  0.01162  0.02878  64  GLY A N     
461  C  CA    . GLY A 64  ? 1.14585 0.81920 0.96376 0.16912  0.01098  0.01902  64  GLY A CA    
462  C  C     . GLY A 64  ? 1.12810 0.87476 0.98521 0.17115  0.00514  0.02361  64  GLY A C     
463  O  O     . GLY A 64  ? 1.16631 0.92228 1.03462 0.16684  0.00532  0.03724  64  GLY A O     
464  N  N     . GLN A 65  ? 1.03200 0.82642 0.90625 0.17594  0.00235  0.01133  65  GLN A N     
465  C  CA    . GLN A 65  ? 0.93293 0.79197 0.84037 0.17321  -0.00152 0.01236  65  GLN A CA    
466  C  C     . GLN A 65  ? 0.95995 0.86052 0.87394 0.20149  -0.00009 0.00253  65  GLN A C     
467  O  O     . GLN A 65  ? 0.98200 0.88337 0.88925 0.21029  0.00389  -0.01071 65  GLN A O     
468  C  CB    . GLN A 65  ? 0.95161 0.83363 0.87760 0.14340  -0.00575 0.00793  65  GLN A CB    
469  C  CG    . GLN A 65  ? 0.99687 0.85167 0.92469 0.11503  -0.00996 0.01725  65  GLN A CG    
470  C  CD    . GLN A 65  ? 1.09481 0.97500 1.03929 0.09122  -0.01680 0.01501  65  GLN A CD    
471  O  OE1   . GLN A 65  ? 1.03133 0.94682 0.98559 0.09424  -0.01592 0.00854  65  GLN A OE1   
472  N  NE2   . GLN A 65  ? 1.07696 0.93981 1.02397 0.06683  -0.02385 0.02100  65  GLN A NE2   
473  N  N     . VAL A 66  ? 0.86719 0.80476 0.79436 0.21441  -0.00291 0.00823  66  VAL A N     
474  C  CA    . VAL A 66  ? 0.87061 0.86348 0.81257 0.23675  -0.00441 -0.00115 66  VAL A CA    
475  C  C     . VAL A 66  ? 0.76045 0.80437 0.72947 0.21277  -0.00408 -0.01123 66  VAL A C     
476  O  O     . VAL A 66  ? 0.83364 0.89152 0.81342 0.19433  -0.00587 -0.00574 66  VAL A O     
477  C  CB    . VAL A 66  ? 0.83633 0.84600 0.77496 0.25963  -0.01042 0.00906  66  VAL A CB    
478  C  CG1   . VAL A 66  ? 0.82633 0.90200 0.78455 0.28281  -0.01492 -0.00137 66  VAL A CG1   
479  C  CG2   . VAL A 66  ? 0.91514 0.86104 0.81948 0.28097  -0.00865 0.02278  66  VAL A CG2   
480  N  N     . ARG A 67  ? 0.87630 0.94323 0.85291 0.21319  0.00096  -0.02591 67  ARG A N     
481  C  CA    . ARG A 67  ? 0.81150 0.91798 0.80731 0.18915  0.00424  -0.03516 67  ARG A CA    
482  C  C     . ARG A 67  ? 0.75939 0.93018 0.77702 0.20147  0.00738  -0.04873 67  ARG A C     
483  O  O     . ARG A 67  ? 0.81720 0.99937 0.83556 0.22922  0.00972  -0.05445 67  ARG A O     
484  C  CB    . ARG A 67  ? 0.78565 0.86356 0.76898 0.17017  0.00926  -0.04049 67  ARG A CB    
485  C  CG    . ARG A 67  ? 0.87188 0.89793 0.83997 0.15334  0.00366  -0.02824 67  ARG A CG    
486  C  CD    . ARG A 67  ? 0.78643 0.79475 0.74248 0.13137  0.00434  -0.03293 67  ARG A CD    
487  N  NE    . ARG A 67  ? 0.97087 0.93628 0.91490 0.11568  -0.00374 -0.02254 67  ARG A NE    
488  C  CZ    . ARG A 67  ? 1.06354 1.01009 0.99381 0.09538  -0.00842 -0.02373 67  ARG A CZ    
489  N  NH1   . ARG A 67  ? 1.00765 0.96667 0.92850 0.08877  -0.00406 -0.03374 67  ARG A NH1   
490  N  NH2   . ARG A 67  ? 1.01696 0.93315 0.94177 0.08002  -0.01787 -0.01449 67  ARG A NH2   
491  N  N     . PRO A 68  ? 0.74157 0.95559 0.77803 0.18120  0.00864  -0.05442 68  PRO A N     
492  C  CA    . PRO A 68  ? 0.73549 1.01888 0.79729 0.18729  0.01101  -0.06845 68  PRO A CA    
493  C  C     . PRO A 68  ? 0.76058 1.06013 0.82854 0.18592  0.02437  -0.08264 68  PRO A C     
494  O  O     . PRO A 68  ? 0.84174 1.10326 0.89231 0.16875  0.03197  -0.08323 68  PRO A O     
495  C  CB    . PRO A 68  ? 0.73553 1.04420 0.80732 0.15747  0.01127  -0.07107 68  PRO A CB    
496  C  CG    . PRO A 68  ? 0.79900 1.05327 0.85200 0.14621  0.00784  -0.05555 68  PRO A CG    
497  C  CD    . PRO A 68  ? 0.79433 0.99544 0.82999 0.15237  0.00873  -0.04804 68  PRO A CD    
498  N  N     . ARG A 69  ? 0.76854 1.12836 0.86146 0.20480  0.02719  -0.09386 69  ARG A N     
499  C  CA    . ARG A 69  ? 0.84135 1.22766 0.94496 0.20328  0.04396  -0.10914 69  ARG A CA    
500  C  C     . ARG A 69  ? 0.75699 1.18309 0.87655 0.16611  0.05341  -0.11992 69  ARG A C     
501  O  O     . ARG A 69  ? 0.79127 1.25878 0.92932 0.15258  0.04653  -0.12191 69  ARG A O     
502  C  CB    . ARG A 69  ? 0.80679 1.24772 0.93672 0.24127  0.04546  -0.11637 69  ARG A CB    
503  C  CG    . ARG A 69  ? 0.90168 1.29378 1.00980 0.28144  0.04031  -0.10581 69  ARG A CG    
504  C  CD    . ARG A 69  ? 0.97170 1.41424 1.10513 0.32361  0.04629  -0.11306 69  ARG A CD    
505  N  NE    . ARG A 69  ? 1.17397 1.62910 1.31358 0.32104  0.06961  -0.12932 69  ARG A NE    
506  C  CZ    . ARG A 69  ? 1.12535 1.66046 1.30434 0.30917  0.08100  -0.14440 69  ARG A CZ    
507  N  NH1   . ARG A 69  ? 1.06058 1.67331 1.27797 0.29696  0.06959  -0.14692 69  ARG A NH1   
508  N  NH2   . ARG A 69  ? 1.04676 1.58300 1.22415 0.30699  0.10560  -0.15826 69  ARG A NH2   
509  N  N     . SER A 70  ? 0.71593 1.12365 0.82237 0.14804  0.07019  -0.12713 70  SER A N     
510  C  CA    . SER A 70  ? 0.69486 1.12484 0.80701 0.11063  0.08250  -0.13539 70  SER A CA    
511  C  C     . SER A 70  ? 0.73158 1.25037 0.88600 0.10772  0.09065  -0.15200 70  SER A C     
512  O  O     . SER A 70  ? 0.60950 1.15976 0.77705 0.07869  0.09204  -0.15766 70  SER A O     
513  C  CB    . SER A 70  ? 0.79823 1.18350 0.87942 0.09454  0.09856  -0.13733 70  SER A CB    
514  O  OG    . SER A 70  ? 0.74152 1.13992 0.82445 0.11559  0.11175  -0.14798 70  SER A OG    
515  N  N     . GLY A 71  ? 0.69105 1.25186 0.86783 0.13704  0.09699  -0.16058 71  GLY A N     
516  C  CA    . GLY A 71  ? 0.63409 1.29121 0.85915 0.13492  0.10506  -0.17673 71  GLY A CA    
517  C  C     . GLY A 71  ? 0.71445 1.42873 0.96868 0.13717  0.08353  -0.17584 71  GLY A C     
518  O  O     . GLY A 71  ? 0.62072 1.39576 0.90165 0.10759  0.08629  -0.18796 71  GLY A O     
519  N  N     . LEU A 72  ? 0.74925 1.44190 0.99435 0.17021  0.06221  -0.16186 72  LEU A N     
520  C  CA    . LEU A 72  ? 0.66178 1.40213 0.92497 0.17389  0.03977  -0.15939 72  LEU A CA    
521  C  C     . LEU A 72  ? 0.69533 1.41189 0.94013 0.13033  0.03640  -0.15930 72  LEU A C     
522  O  O     . LEU A 72  ? 0.68167 1.45286 0.94435 0.11559  0.02501  -0.16635 72  LEU A O     
523  C  CB    . LEU A 72  ? 0.62640 1.33148 0.87164 0.21718  0.02048  -0.14157 72  LEU A CB    
524  C  CG    . LEU A 72  ? 0.85340 1.58530 1.11659 0.26846  0.02057  -0.13997 72  LEU A CG    
525  C  CD1   . LEU A 72  ? 0.89265 1.56900 1.12554 0.30598  0.00361  -0.11985 72  LEU A CD1   
526  C  CD2   . LEU A 72  ? 0.88577 1.73557 1.20527 0.27920  0.01536  -0.15250 72  LEU A CD2   
527  N  N     . ALA A 73  ? 0.68279 1.31848 0.89074 0.11001  0.04605  -0.15167 73  ALA A N     
528  C  CA    . ALA A 73  ? 0.66683 1.27110 0.85480 0.07420  0.04556  -0.14973 73  ALA A CA    
529  C  C     . ALA A 73  ? 0.70269 1.34395 0.90403 0.03218  0.06256  -0.16721 73  ALA A C     
530  O  O     . ALA A 73  ? 0.83426 1.47837 1.02965 0.00322  0.06083  -0.17211 73  ALA A O     
531  C  CB    . ALA A 73  ? 0.68426 1.19564 0.83299 0.07056  0.04915  -0.13374 73  ALA A CB    
532  N  N     . TRP A 74  ? 0.69244 1.35752 0.90785 0.02663  0.08146  -0.17741 74  TRP A N     
533  C  CA    . TRP A 74  ? 0.74590 1.43992 0.97045 -0.01642 0.10191  -0.19349 74  TRP A CA    
534  C  C     . TRP A 74  ? 0.73615 1.53952 1.01267 -0.02221 0.10107  -0.21276 74  TRP A C     
535  O  O     . TRP A 74  ? 0.76668 1.60356 1.05274 -0.06160 0.10561  -0.22627 74  TRP A O     
536  C  CB    . TRP A 74  ? 0.76631 1.42158 0.97153 -0.02504 0.12639  -0.19358 74  TRP A CB    
537  C  CG    . TRP A 74  ? 0.82101 1.50935 1.03618 -0.06684 0.15173  -0.21021 74  TRP A CG    
538  C  CD1   . TRP A 74  ? 0.84793 1.58898 1.08845 -0.07022 0.17280  -0.22400 74  TRP A CD1   
539  C  CD2   . TRP A 74  ? 0.76238 1.43004 0.96035 -0.11251 0.16188  -0.21526 74  TRP A CD2   
540  N  NE1   . TRP A 74  ? 0.70267 1.45861 0.94347 -0.11791 0.19543  -0.23692 74  TRP A NE1   
541  C  CE2   . TRP A 74  ? 0.80647 1.51446 1.01925 -0.14471 0.18898  -0.23189 74  TRP A CE2   
542  C  CE3   . TRP A 74  ? 0.72394 1.33902 0.89330 -0.12907 0.15351  -0.20767 74  TRP A CE3   
543  C  CZ2   . TRP A 74  ? 0.78714 1.47953 0.98389 -0.19474 0.20725  -0.24084 74  TRP A CZ2   
544  C  CZ3   . TRP A 74  ? 0.84719 1.44546 1.00019 -0.17547 0.17178  -0.21696 74  TRP A CZ3   
545  C  CH2   . TRP A 74  ? 0.88035 1.51476 1.04556 -0.20882 0.19804  -0.23326 74  TRP A CH2   
546  N  N     . LYS A 75  ? 0.73698 1.59747 1.04775 0.01638  0.09548  -0.21453 75  LYS A N     
547  C  CA    . LYS A 75  ? 0.74642 1.72307 1.11517 0.01481  0.09455  -0.23202 75  LYS A CA    
548  C  C     . LYS A 75  ? 0.70803 1.73874 1.09479 0.01861  0.06465  -0.23301 75  LYS A C     
549  O  O     . LYS A 75  ? 0.58885 1.70657 1.01316 -0.00844 0.06234  -0.25041 75  LYS A O     
550  C  CB    . LYS A 75  ? 0.59273 1.61193 0.99277 0.06046  0.10062  -0.23242 75  LYS A CB    
551  N  N     . LYS A 76  ? 0.76630 1.74791 1.12488 0.04917  0.04188  -0.21517 76  LYS A N     
552  C  CA    . LYS A 76  ? 0.69671 1.72350 1.06350 0.05687  0.01260  -0.21403 76  LYS A CA    
553  C  C     . LYS A 76  ? 0.76191 1.70607 1.07669 0.04478  0.00187  -0.20213 76  LYS A C     
554  O  O     . LYS A 76  ? 0.60718 1.57713 0.91788 0.05082  -0.02183 -0.20014 76  LYS A O     
555  C  CB    . LYS A 76  ? 0.74022 1.80967 1.12995 0.11681  -0.00725 -0.20303 76  LYS A CB    
556  C  CG    . LYS A 76  ? 0.58602 1.73639 1.02821 0.13765  0.00357  -0.21268 76  LYS A CG    
557  C  CD    . LYS A 76  ? 0.72203 1.90010 1.17403 0.18995  -0.02050 -0.19876 76  LYS A CD    
558  C  CE    . LYS A 76  ? 0.70671 1.87617 1.17184 0.22955  -0.00455 -0.19364 76  LYS A CE    
559  N  NZ    . LYS A 76  ? 0.77383 1.96156 1.24493 0.28172  -0.02568 -0.17818 76  LYS A NZ    
560  N  N     . GLY A 77  ? 0.77916 1.62777 1.05406 0.02954  0.01844  -0.19368 77  GLY A N     
561  C  CA    . GLY A 77  ? 0.70209 1.47818 0.93333 0.01641  0.01266  -0.18365 77  GLY A CA    
562  C  C     . GLY A 77  ? 0.75835 1.49573 0.96789 0.05639  -0.00662 -0.16342 77  GLY A C     
563  O  O     . GLY A 77  ? 0.81673 1.51212 0.99524 0.04780  -0.01355 -0.15666 77  GLY A O     
564  N  N     . LEU A 78  ? 0.73553 1.48136 0.95742 0.09953  -0.01280 -0.15376 78  LEU A N     
565  C  CA    . LEU A 78  ? 0.79888 1.49885 0.99564 0.13653  -0.02794 -0.13351 78  LEU A CA    
566  C  C     . LEU A 78  ? 0.75010 1.35295 0.91387 0.13649  -0.01569 -0.11905 78  LEU A C     
567  O  O     . LEU A 78  ? 0.75476 1.33266 0.91857 0.12112  0.00183  -0.12300 78  LEU A O     
568  C  CB    . LEU A 78  ? 0.74854 1.49256 0.96836 0.18458  -0.03876 -0.12877 78  LEU A CB    
569  C  CG    . LEU A 78  ? 0.87078 1.66684 1.09528 0.20981  -0.06540 -0.12364 78  LEU A CG    
570  C  CD1   . LEU A 78  ? 0.94748 1.82710 1.19640 0.17610  -0.07436 -0.14264 78  LEU A CD1   
571  C  CD2   . LEU A 78  ? 0.91102 1.74481 1.15856 0.26259  -0.07289 -0.11692 78  LEU A CD2   
572  N  N     . THR A 79  ? 0.64746 1.19765 0.78210 0.15297  -0.02549 -0.10182 79  THR A N     
573  C  CA    . THR A 79  ? 0.76261 1.22879 0.87062 0.15287  -0.01670 -0.08737 79  THR A CA    
574  C  C     . THR A 79  ? 0.78422 1.21030 0.86773 0.17989  -0.02856 -0.06889 79  THR A C     
575  O  O     . THR A 79  ? 0.70847 1.16437 0.78828 0.19472  -0.04312 -0.06637 79  THR A O     
576  C  CB    . THR A 79  ? 0.77196 1.20163 0.86651 0.11500  -0.00467 -0.08884 79  THR A CB    
577  O  OG1   . THR A 79  ? 0.81801 1.17648 0.89253 0.11776  0.00046  -0.07318 79  THR A OG1   
578  C  CG2   . THR A 79  ? 0.86252 1.30154 0.94494 0.10036  -0.01104 -0.09085 79  THR A CG2   
579  N  N     . VAL A 80  ? 0.78596 1.14402 0.85068 0.18446  -0.02230 -0.05579 80  VAL A N     
580  C  CA    . VAL A 80  ? 0.71361 1.02201 0.75187 0.20215  -0.02842 -0.03747 80  VAL A CA    
581  C  C     . VAL A 80  ? 0.77032 1.05390 0.79399 0.17755  -0.02489 -0.03231 80  VAL A C     
582  O  O     . VAL A 80  ? 0.75318 1.01315 0.77940 0.15266  -0.01366 -0.03349 80  VAL A O     
583  C  CB    . VAL A 80  ? 0.77467 1.02321 0.80053 0.21270  -0.02230 -0.02765 80  VAL A CB    
584  C  CG1   . VAL A 80  ? 0.80243 1.00233 0.80080 0.23210  -0.02711 -0.00939 80  VAL A CG1   
585  C  CG2   . VAL A 80  ? 0.74286 1.01131 0.78123 0.23232  -0.01982 -0.03697 80  VAL A CG2   
586  N  N     . LEU A 81  ? 0.83395 1.12171 0.83975 0.18650  -0.03376 -0.02603 81  LEU A N     
587  C  CA    . LEU A 81  ? 0.73756 1.00486 0.72659 0.16433  -0.02781 -0.02379 81  LEU A CA    
588  C  C     . LEU A 81  ? 0.73378 0.93717 0.71353 0.15709  -0.01514 -0.00918 81  LEU A C     
589  O  O     . LEU A 81  ? 0.74137 0.92867 0.72391 0.13389  -0.00321 -0.01073 81  LEU A O     
590  C  CB    . LEU A 81  ? 0.91663 1.19642 0.88047 0.17767  -0.04004 -0.01907 81  LEU A CB    
591  C  CG    . LEU A 81  ? 0.93878 1.20032 0.87917 0.15507  -0.03253 -0.02025 81  LEU A CG    
592  C  CD1   . LEU A 81  ? 0.93821 1.24012 0.89075 0.12548  -0.02981 -0.04185 81  LEU A CD1   
593  C  CD2   . LEU A 81  ? 0.91803 1.17606 0.82266 0.17213  -0.04393 -0.01086 81  LEU A CD2   
594  N  N     . ASN A 82  ? 0.79640 0.96315 0.76571 0.17676  -0.01694 0.00526  82  ASN A N     
595  C  CA    . ASN A 82  ? 0.87573 0.98893 0.84030 0.16846  -0.00645 0.01913  82  ASN A CA    
596  C  C     . ASN A 82  ? 0.83511 0.93430 0.81678 0.16207  -0.00368 0.01739  82  ASN A C     
597  O  O     . ASN A 82  ? 0.84721 0.90559 0.82398 0.16224  -0.00077 0.02852  82  ASN A O     
598  C  CB    . ASN A 82  ? 0.89776 0.97244 0.83551 0.18733  -0.00785 0.03580  82  ASN A CB    
599  C  CG    . ASN A 82  ? 0.86269 0.92803 0.79343 0.21353  -0.01598 0.03821  82  ASN A CG    
600  O  OD1   . ASN A 82  ? 0.82233 0.92779 0.76454 0.22685  -0.02445 0.02697  82  ASN A OD1   
601  N  ND2   . ASN A 82  ? 0.98224 0.99321 0.89427 0.22054  -0.01122 0.05245  82  ASN A ND2   
602  N  N     . ALA A 83  ? 0.79034 0.92192 0.78917 0.15385  -0.00406 0.00310  83  ALA A N     
603  C  CA    . ALA A 83  ? 0.75937 0.87736 0.76689 0.14821  -0.00200 0.00042  83  ALA A CA    
604  C  C     . ALA A 83  ? 0.68294 0.77170 0.69577 0.12748  0.00430  0.00941  83  ALA A C     
605  O  O     . ALA A 83  ? 0.75206 0.84800 0.77099 0.11315  0.01076  0.00973  83  ALA A O     
606  C  CB    . ALA A 83  ? 0.69576 0.85551 0.71727 0.14256  -0.00074 -0.01656 83  ALA A CB    
607  N  N     . PRO A 84  ? 0.76157 0.81749 0.77194 0.12561  0.00259  0.01672  84  PRO A N     
608  C  CA    . PRO A 84  ? 0.78733 0.81987 0.78354 0.14049  -0.00195 0.01623  84  PRO A CA    
609  C  C     . PRO A 84  ? 0.81534 0.81900 0.79489 0.15502  -0.00219 0.02812  84  PRO A C     
610  O  O     . PRO A 84  ? 0.77893 0.76253 0.75912 0.14487  0.00193  0.04036  84  PRO A O     
611  C  CB    . PRO A 84  ? 0.71052 0.71756 0.70806 0.12318  -0.00329 0.01843  84  PRO A CB    
612  C  CG    . PRO A 84  ? 0.67546 0.68405 0.68949 0.10565  -0.00063 0.02943  84  PRO A CG    
613  C  CD    . PRO A 84  ? 0.72536 0.76576 0.74691 0.10639  0.00500  0.02490  84  PRO A CD    
614  N  N     . GLY A 85  ? 0.79342 0.79429 0.75721 0.18040  -0.00549 0.02578  85  GLY A N     
615  C  CA    . GLY A 85  ? 0.87207 0.83826 0.81206 0.19699  -0.00510 0.03887  85  GLY A CA    
616  C  C     . GLY A 85  ? 0.91966 0.82653 0.84385 0.18955  -0.00080 0.04700  85  GLY A C     
617  O  O     . GLY A 85  ? 1.00798 0.89011 0.91976 0.19750  -0.00110 0.04078  85  GLY A O     
618  N  N     . THR A 86  ? 0.93866 0.82194 0.86252 0.17270  0.00489  0.05980  86  THR A N     
619  C  CA    . THR A 86  ? 0.98737 0.81989 0.90128 0.15726  0.00936  0.06676  86  THR A CA    
620  C  C     . THR A 86  ? 1.12640 0.90542 1.00125 0.17863  0.01340  0.07422  86  THR A C     
621  O  O     . THR A 86  ? 1.16221 0.92907 1.01931 0.19099  0.01773  0.08649  86  THR A O     
622  C  CB    . THR A 86  ? 1.08669 0.92030 1.01940 0.13258  0.01628  0.07833  86  THR A CB    
623  O  OG1   . THR A 86  ? 0.99461 0.87607 0.95961 0.12074  0.01402  0.07351  86  THR A OG1   
624  C  CG2   . THR A 86  ? 1.16309 0.95992 1.09664 0.10871  0.01828  0.08216  86  THR A CG2   
625  N  N     . ILE A 87  ? 1.07906 0.82065 0.93504 0.18379  0.01321  0.06717  87  ILE A N     
626  C  CA    . ILE A 87  ? 1.26794 0.94367 1.08150 0.20315  0.01988  0.07449  87  ILE A CA    
627  C  C     . ILE A 87  ? 1.28692 0.90714 1.08930 0.17080  0.02784  0.07987  87  ILE A C     
628  O  O     . ILE A 87  ? 1.24312 0.84774 1.04706 0.15022  0.02577  0.06878  87  ILE A O     
629  C  CB    . ILE A 87  ? 1.23956 0.90222 1.03548 0.23124  0.01844  0.06229  87  ILE A CB    
630  C  CG1   . ILE A 87  ? 1.14969 0.88522 0.97037 0.25505  0.00998  0.05385  87  ILE A CG1   
631  C  CG2   . ILE A 87  ? 1.26316 0.85488 1.01168 0.25958  0.02668  0.07265  87  ILE A CG2   
632  C  CD1   . ILE A 87  ? 1.15117 0.91156 0.96741 0.27987  0.00565  0.06595  87  ILE A CD1   
633  N  N     . ASP A 88  ? 1.28321 0.87520 1.07314 0.16380  0.03720  0.09627  88  ASP A N     
634  C  CA    . ASP A 88  ? 1.34143 0.89019 1.12787 0.12794  0.04635  0.10176  88  ASP A CA    
635  C  C     . ASP A 88  ? 1.45663 0.92767 1.20027 0.12747  0.05189  0.09624  88  ASP A C     
636  O  O     . ASP A 88  ? 1.48607 0.92165 1.19362 0.16281  0.05389  0.09521  88  ASP A O     
637  C  CB    . ASP A 88  ? 1.45240 0.98399 1.22973 0.12299  0.05970  0.12092  88  ASP A CB    
638  C  CG    . ASP A 88  ? 1.37358 0.97369 1.19206 0.11586  0.05838  0.12478  88  ASP A CG    
639  O  OD1   . ASP A 88  ? 1.34779 0.98769 1.20939 0.08839  0.05506  0.11995  88  ASP A OD1   
640  O  OD2   . ASP A 88  ? 1.36874 0.98136 1.17374 0.13878  0.06042  0.13260  88  ASP A OD2   
641  N  N     . ALA A 89  ? 1.50430 0.94936 1.25222 0.08683  0.05454  0.09222  89  ALA A N     
642  C  CA    . ALA A 89  ? 1.62066 0.98518 1.32374 0.07866  0.06104  0.08389  89  ALA A CA    
643  C  C     . ALA A 89  ? 1.66800 0.94871 1.31748 0.09527  0.07897  0.09848  89  ALA A C     
644  O  O     . ALA A 89  ? 1.67798 0.88493 1.27813 0.11166  0.08646  0.09321  89  ALA A O     
645  C  CB    . ALA A 89  ? 1.58581 0.94724 1.30655 0.02545  0.05777  0.07607  89  ALA A CB    
646  N  N     . ASP A 90  ? 1.67383 0.95940 1.32753 0.09274  0.08795  0.11732  90  ASP A N     
647  C  CA    . ASP A 90  ? 1.81666 1.02007 1.41484 0.10708  0.10619  0.13459  90  ASP A CA    
648  C  C     . ASP A 90  ? 1.81664 1.02674 1.39117 0.16251  0.10321  0.14641  90  ASP A C     
649  O  O     . ASP A 90  ? 1.84753 1.01381 1.38471 0.17579  0.11547  0.16617  90  ASP A O     
650  C  CB    . ASP A 90  ? 1.85134 1.04843 1.46039 0.06933  0.12108  0.14911  90  ASP A CB    
651  C  CG    . ASP A 90  ? 1.78040 1.07182 1.44668 0.06377  0.11451  0.15372  90  ASP A CG    
652  O  OD1   . ASP A 90  ? 1.72914 1.07678 1.41158 0.09578  0.10082  0.15060  90  ASP A OD1   
653  O  OD2   . ASP A 90  ? 1.71914 1.02841 1.41495 0.02646  0.12449  0.15971  90  ASP A OD2   
654  N  N     . TYR A 91  ? 1.72020 0.98659 1.31502 0.19386  0.08698  0.13520  91  TYR A N     
655  C  CA    . TYR A 91  ? 1.74882 1.03297 1.32666 0.24568  0.08059  0.14478  91  TYR A CA    
656  C  C     . TYR A 91  ? 1.71138 0.91817 1.23488 0.28453  0.08709  0.14704  91  TYR A C     
657  O  O     . TYR A 91  ? 1.81026 1.00398 1.33333 0.28905  0.08607  0.12991  91  TYR A O     
658  C  CB    . TYR A 91  ? 1.60219 0.98696 1.23008 0.25911  0.06182  0.13140  91  TYR A CB    
659  C  CG    . TYR A 91  ? 1.59892 1.02088 1.21886 0.30406  0.05218  0.14094  91  TYR A CG    
660  C  CD1   . TYR A 91  ? 1.60320 1.02809 1.20824 0.30666  0.05430  0.15891  91  TYR A CD1   
661  C  CD2   . TYR A 91  ? 1.59594 1.05352 1.22322 0.34277  0.04096  0.13150  91  TYR A CD2   
662  C  CE1   . TYR A 91  ? 1.55528 1.01651 1.14932 0.34538  0.04219  0.16703  91  TYR A CE1   
663  C  CE2   . TYR A 91  ? 1.56646 1.06773 1.19078 0.38197  0.02900  0.13984  91  TYR A CE2   
664  C  CZ    . TYR A 91  ? 1.59680 1.09929 1.20270 0.38249  0.02797  0.15750  91  TYR A CZ    
665  O  OH    . TYR A 91  ? 1.53749 1.08553 1.13662 0.41918  0.01290  0.16525  91  TYR A OH    
666  N  N     . ARG A 92  ? 1.74996 0.90134 1.22372 0.31390  0.09526  0.16882  92  ARG A N     
667  C  CA    . ARG A 92  ? 1.89755 0.98638 1.32352 0.35313  0.10139  0.17240  92  ARG A CA    
668  C  C     . ARG A 92  ? 1.91943 1.06482 1.34652 0.40307  0.08701  0.18170  92  ARG A C     
669  O  O     . ARG A 92  ? 1.86259 0.97180 1.25371 0.43175  0.09156  0.18916  92  ARG A O     
670  C  CB    . ARG A 92  ? 1.97064 0.96482 1.34655 0.32928  0.12271  0.18263  92  ARG A CB    
671  C  CG    . ARG A 92  ? 1.95904 0.89702 1.33245 0.27691  0.13593  0.17009  92  ARG A CG    
672  C  CD    . ARG A 92  ? 1.85513 0.78504 1.23327 0.28368  0.13216  0.14676  92  ARG A CD    
673  N  NE    . ARG A 92  ? 1.91766 0.89086 1.34081 0.23872  0.12438  0.12905  92  ARG A NE    
674  C  CZ    . ARG A 92  ? 1.98623 0.91893 1.40545 0.18433  0.13265  0.11940  92  ARG A CZ    
675  N  NH1   . ARG A 92  ? 2.05569 0.87998 1.41821 0.16743  0.15349  0.12649  92  ARG A NH1   
676  N  NH2   . ARG A 92  ? 1.85393 0.85654 1.32611 0.14504  0.11929  0.10263  92  ARG A NH2   
677  N  N     . GLY A 93  ? 1.81993 1.05369 1.28678 0.41266  0.06943  0.18120  93  GLY A N     
678  C  CA    . GLY A 93  ? 1.76916 1.06903 1.24341 0.45430  0.05223  0.18649  93  GLY A CA    
679  C  C     . GLY A 93  ? 1.72603 1.09995 1.24392 0.47906  0.03819  0.16798  93  GLY A C     
680  O  O     . GLY A 93  ? 1.70766 1.07188 1.24230 0.46862  0.04366  0.15107  93  GLY A O     
681  N  N     . GLU A 94  ? 1.69452 1.14492 1.23000 0.51037  0.02022  0.17050  94  GLU A N     
682  C  CA    . GLU A 94  ? 1.62061 1.15244 1.20212 0.53268  0.00786  0.15322  94  GLU A CA    
683  C  C     . GLU A 94  ? 1.56047 1.16462 1.19023 0.51002  -0.00199 0.14023  94  GLU A C     
684  O  O     . GLU A 94  ? 1.53876 1.17957 1.17548 0.49410  -0.01082 0.14647  94  GLU A O     
685  C  CB    . GLU A 94  ? 1.61062 1.20004 1.19507 0.57204  -0.00798 0.16041  94  GLU A CB    
686  C  CG    . GLU A 94  ? 1.66543 1.30981 1.28514 0.60070  -0.01194 0.14543  94  GLU A CG    
687  C  CD    . GLU A 94  ? 1.60675 1.36407 1.26750 0.61925  -0.03483 0.14201  94  GLU A CD    
688  O  OE1   . GLU A 94  ? 1.59450 1.36444 1.23563 0.64202  -0.04649 0.15704  94  GLU A OE1   
689  O  OE2   . GLU A 94  ? 1.60836 1.44166 1.31982 0.60888  -0.04106 0.12369  94  GLU A OE2   
690  N  N     . VAL A 95  ? 1.53367 1.16104 1.19694 0.49959  0.00178  0.11912  95  VAL A N     
691  C  CA    . VAL A 95  ? 1.43385 1.14101 1.14995 0.46129  -0.00499 0.10091  95  VAL A CA    
692  C  C     . VAL A 95  ? 1.33283 1.14201 1.08463 0.48369  -0.02306 0.09589  95  VAL A C     
693  O  O     . VAL A 95  ? 1.22069 1.06069 0.98142 0.52554  -0.02798 0.09329  95  VAL A O     
694  C  CB    . VAL A 95  ? 1.45285 1.15162 1.18766 0.44010  0.00502  0.08006  95  VAL A CB    
695  C  CG1   . VAL A 95  ? 1.32149 1.10534 1.10819 0.40889  -0.00226 0.06273  95  VAL A CG1   
696  C  CG2   . VAL A 95  ? 1.53493 1.14401 1.23890 0.40657  0.01920  0.08285  95  VAL A CG2   
697  N  N     . LYS A 96  ? 1.23024 1.09329 1.00329 0.45538  -0.03213 0.09381  96  LYS A N     
698  C  CA    . LYS A 96  ? 1.17265 1.13322 0.97834 0.46578  -0.04965 0.08642  96  LYS A CA    
699  C  C     . LYS A 96  ? 1.12800 1.14576 0.97739 0.42226  -0.04878 0.06638  96  LYS A C     
700  O  O     . LYS A 96  ? 1.00970 0.99409 0.85872 0.38435  -0.03855 0.06468  96  LYS A O     
701  C  CB    . LYS A 96  ? 1.25554 1.22301 1.03288 0.47644  -0.06254 0.10364  96  LYS A CB    
702  C  CG    . LYS A 96  ? 1.27908 1.18155 1.00418 0.52007  -0.06313 0.12757  96  LYS A CG    
703  C  CD    . LYS A 96  ? 1.36055 1.27967 1.05525 0.53160  -0.07859 0.14379  96  LYS A CD    
704  C  CE    . LYS A 96  ? 1.46376 1.30048 1.10146 0.54961  -0.07062 0.16524  96  LYS A CE    
705  N  NZ    . LYS A 96  ? 1.36653 1.18551 0.96227 0.54093  -0.07508 0.18167  96  LYS A NZ    
706  N  N     . VAL A 97  ? 1.11388 1.21911 1.00147 0.42841  -0.05920 0.05192  97  VAL A N     
707  C  CA    . VAL A 97  ? 0.88472 1.04341 0.81147 0.39030  -0.05660 0.03219  97  VAL A CA    
708  C  C     . VAL A 97  ? 0.97979 1.20644 0.91893 0.37909  -0.07097 0.02821  97  VAL A C     
709  O  O     . VAL A 97  ? 1.15013 1.42755 1.09269 0.40797  -0.08695 0.03064  97  VAL A O     
710  C  CB    . VAL A 97  ? 0.93537 1.13481 0.89588 0.39932  -0.05107 0.01475  97  VAL A CB    
711  C  CG1   . VAL A 97  ? 0.90704 1.15662 0.90186 0.35880  -0.04693 -0.00390 97  VAL A CG1   
712  C  CG2   . VAL A 97  ? 0.89946 1.02393 0.83911 0.40801  -0.03598 0.01650  97  VAL A CG2   
713  N  N     . ILE A 98  ? 0.84398 1.07114 0.78838 0.33782  -0.06557 0.02195  98  ILE A N     
714  C  CA    . ILE A 98  ? 0.98233 1.26020 0.93060 0.31982  -0.07547 0.01567  98  ILE A CA    
715  C  C     . ILE A 98  ? 0.92034 1.26484 0.91062 0.29575  -0.07365 -0.00717 98  ILE A C     
716  O  O     . ILE A 98  ? 0.85980 1.18692 0.86069 0.26401  -0.05986 -0.01505 98  ILE A O     
717  C  CB    . ILE A 98  ? 0.97887 1.20729 0.90095 0.29210  -0.06664 0.02377  98  ILE A CB    
718  C  CG1   . ILE A 98  ? 1.05094 1.20905 0.93114 0.31234  -0.06399 0.04664  98  ILE A CG1   
719  C  CG2   . ILE A 98  ? 0.85700 1.13036 0.77461 0.27413  -0.07520 0.01532  98  ILE A CG2   
720  C  CD1   . ILE A 98  ? 0.92354 1.03381 0.78196 0.28606  -0.05105 0.05529  98  ILE A CD1   
721  N  N     . LEU A 99  ? 0.89537 1.31769 0.90973 0.31080  -0.08739 -0.01698 99  LEU A N     
722  C  CA    . LEU A 99  ? 0.79629 1.28856 0.85014 0.28473  -0.08512 -0.03938 99  LEU A CA    
723  C  C     . LEU A 99  ? 0.85827 1.38234 0.90580 0.25281  -0.09244 -0.04853 99  LEU A C     
724  O  O     . LEU A 99  ? 1.04993 1.56054 1.06562 0.25928  -0.10400 -0.03847 99  LEU A O     
725  C  CB    . LEU A 99  ? 0.84287 1.41230 0.93300 0.31452  -0.09440 -0.04717 99  LEU A CB    
726  C  CG    . LEU A 99  ? 0.90228 1.47493 1.01999 0.32017  -0.07751 -0.05637 99  LEU A CG    
727  C  CD1   . LEU A 99  ? 0.84629 1.32245 0.93337 0.32855  -0.06362 -0.04370 99  LEU A CD1   
728  C  CD2   . LEU A 99  ? 0.94527 1.58999 1.09604 0.36095  -0.08596 -0.05961 99  LEU A CD2   
729  N  N     . VAL A 100 ? 0.85004 1.41091 0.92286 0.21675  -0.08374 -0.06828 100 VAL A N     
730  C  CA    . VAL A 100 ? 0.91768 1.50579 0.98299 0.18161  -0.08759 -0.08125 100 VAL A CA    
731  C  C     . VAL A 100 ? 0.89968 1.54819 1.00277 0.15068  -0.07975 -0.10465 100 VAL A C     
732  O  O     . VAL A 100 ? 0.90396 1.53623 1.02407 0.14189  -0.06206 -0.10864 100 VAL A O     
733  C  CB    . VAL A 100 ? 0.86427 1.37321 0.89279 0.15795  -0.07342 -0.07404 100 VAL A CB    
734  C  CG1   . VAL A 100 ? 0.89443 1.35396 0.93191 0.14286  -0.05143 -0.07296 100 VAL A CG1   
735  C  CG2   . VAL A 100 ? 0.95758 1.48585 0.97125 0.12248  -0.07450 -0.08919 100 VAL A CG2   
736  N  N     . ASN A 101 ? 0.99279 1.71098 1.10607 0.13221  -0.09300 -0.12038 101 ASN A N     
737  C  CA    . ASN A 101 ? 0.96257 1.74575 1.11224 0.09822  -0.08572 -0.14424 101 ASN A CA    
738  C  C     . ASN A 101 ? 0.95257 1.69279 1.07740 0.04824  -0.06879 -0.15613 101 ASN A C     
739  O  O     . ASN A 101 ? 1.03507 1.75939 1.12673 0.03308  -0.07612 -0.15834 101 ASN A O     
740  C  CB    . ASN A 101 ? 0.99982 1.89071 1.17879 0.10294  -0.11048 -0.15638 101 ASN A CB    
741  C  CG    . ASN A 101 ? 1.01926 1.99020 1.24721 0.07184  -0.10165 -0.18056 101 ASN A CG    
742  O  OD1   . ASN A 101 ? 0.95823 1.89733 1.18471 0.03371  -0.07709 -0.19166 101 ASN A OD1   
743  N  ND2   . ASN A 101 ? 1.10278 2.17980 1.37479 0.08869  -0.12110 -0.18787 101 ASN A ND2   
744  N  N     . LEU A 102 ? 1.02012 1.73719 1.15632 0.02403  -0.04494 -0.16338 102 LEU A N     
745  C  CA    . LEU A 102 ? 0.92842 1.60551 1.04296 -0.02238 -0.02587 -0.17522 102 LEU A CA    
746  C  C     . LEU A 102 ? 0.88560 1.62484 1.02923 -0.06086 -0.01657 -0.19978 102 LEU A C     
747  O  O     . LEU A 102 ? 0.96477 1.66719 1.08974 -0.10149 0.00314  -0.21067 102 LEU A O     
748  C  CB    . LEU A 102 ? 0.91375 1.50005 1.00818 -0.02170 -0.00425 -0.16069 102 LEU A CB    
749  C  CG    . LEU A 102 ? 1.02410 1.53625 1.08155 -0.00610 -0.00510 -0.14167 102 LEU A CG    
750  C  CD1   . LEU A 102 ? 0.96857 1.47412 0.99501 -0.02810 -0.00820 -0.15078 102 LEU A CD1   
751  C  CD2   . LEU A 102 ? 0.99683 1.50775 1.05648 0.03889  -0.02148 -0.12291 102 LEU A CD2   
752  N  N     . GLY A 103 ? 0.89466 1.72648 1.08391 -0.04856 -0.02838 -0.20833 103 GLY A N     
753  C  CA    . GLY A 103 ? 0.91273 1.81908 1.13576 -0.08703 -0.02097 -0.23301 103 GLY A CA    
754  C  C     . GLY A 103 ? 1.04484 2.02125 1.27143 -0.10983 -0.04290 -0.25016 103 GLY A C     
755  O  O     . GLY A 103 ? 1.16235 2.12640 1.36023 -0.09442 -0.06399 -0.24240 103 GLY A O     
756  N  N     . ASN A 104 ? 1.16820 2.22039 1.42885 -0.14986 -0.03735 -0.27456 104 ASN A N     
757  C  CA    . ASN A 104 ? 1.15420 2.28347 1.42196 -0.18091 -0.05851 -0.29534 104 ASN A CA    
758  C  C     . ASN A 104 ? 1.15026 2.41466 1.48168 -0.15636 -0.08507 -0.30029 104 ASN A C     
759  O  O     . ASN A 104 ? 1.11766 2.43307 1.45306 -0.18129 -0.09620 -0.31376 104 ASN A O     
760  C  CB    . ASN A 104 ? 1.16400 2.28695 1.42356 -0.25064 -0.03484 -0.32190 104 ASN A CB    
761  C  CG    . ASN A 104 ? 1.08298 2.24406 1.38818 -0.26812 -0.00897 -0.33128 104 ASN A CG    
762  O  OD1   . ASN A 104 ? 1.09147 2.34343 1.44445 -0.26216 -0.01591 -0.33817 104 ASN A OD1   
763  N  ND2   . ASN A 104 ? 1.09579 2.16175 1.37140 -0.28277 0.02438  -0.32549 104 ASN A ND2   
764  N  N     . GLU A 105 ? 1.39131 2.67216 1.75288 -0.10100 -0.08776 -0.28185 105 GLU A N     
765  C  CA    . GLU A 105 ? 1.32913 2.68520 1.72900 -0.06412 -0.10370 -0.27560 105 GLU A CA    
766  C  C     . GLU A 105 ? 1.32908 2.66854 1.71804 0.00249  -0.12642 -0.24911 105 GLU A C     
767  O  O     . GLU A 105 ? 1.36376 2.63719 1.73058 0.02630  -0.12093 -0.23478 105 GLU A O     
768  C  CB    . GLU A 105 ? 1.33959 2.72586 1.78447 -0.06158 -0.07837 -0.28034 105 GLU A CB    
769  C  CG    . GLU A 105 ? 1.34455 2.71518 1.78975 -0.12342 -0.04623 -0.30139 105 GLU A CG    
770  C  CD    . GLU A 105 ? 1.40967 2.84175 1.86799 -0.17037 -0.04895 -0.32279 105 GLU A CD    
771  O  OE1   . GLU A 105 ? 1.40889 2.90007 1.87715 -0.15686 -0.07791 -0.32190 105 GLU A OE1   
772  O  OE2   . GLU A 105 ? 1.44655 2.86471 1.90277 -0.22104 -0.02144 -0.33976 105 GLU A OE2   
773  N  N     . GLU A 106 ? 1.14832 2.54536 1.55158 0.03204  -0.15121 -0.24184 106 GLU A N     
774  C  CA    . GLU A 106 ? 1.08314 2.45988 1.47401 0.09705  -0.16981 -0.21514 106 GLU A CA    
775  C  C     . GLU A 106 ? 1.02114 2.38708 1.44106 0.13801  -0.15145 -0.20445 106 GLU A C     
776  O  O     . GLU A 106 ? 0.94913 2.36316 1.41177 0.12756  -0.13534 -0.21616 106 GLU A O     
777  C  CB    . GLU A 106 ? 0.94799 2.38839 1.34511 0.11584  -0.20052 -0.20984 106 GLU A CB    
778  N  N     . VAL A 107 ? 1.00455 2.30204 1.39707 0.18333  -0.15245 -0.18249 107 VAL A N     
779  C  CA    . VAL A 107 ? 1.01393 2.28037 1.42087 0.22142  -0.13329 -0.17227 107 VAL A CA    
780  C  C     . VAL A 107 ? 1.04316 2.30393 1.44273 0.28228  -0.15032 -0.14959 107 VAL A C     
781  O  O     . VAL A 107 ? 1.09011 2.32655 1.45357 0.30091  -0.17273 -0.13458 107 VAL A O     
782  C  CB    . VAL A 107 ? 1.02913 2.20795 1.40740 0.21930  -0.11468 -0.16685 107 VAL A CB    
783  C  CG1   . VAL A 107 ? 1.04172 2.18349 1.42895 0.25480  -0.09371 -0.15873 107 VAL A CG1   
784  C  CG2   . VAL A 107 ? 0.89946 2.07896 1.28152 0.15816  -0.09710 -0.18779 107 VAL A CG2   
785  N  N     . VAL A 108 ? 1.10120 2.38095 1.53193 0.31247  -0.13803 -0.14699 108 VAL A N     
786  C  CA    . VAL A 108 ? 1.10930 2.37994 1.53537 0.37120  -0.14917 -0.12611 108 VAL A CA    
787  C  C     . VAL A 108 ? 1.10950 2.29351 1.51483 0.40338  -0.12713 -0.11464 108 VAL A C     
788  O  O     . VAL A 108 ? 1.06841 2.25181 1.49673 0.39444  -0.10147 -0.12600 108 VAL A O     
789  C  CB    . VAL A 108 ? 1.00468 2.37099 1.48486 0.38305  -0.15350 -0.13229 108 VAL A CB    
790  C  CG1   . VAL A 108 ? 1.03009 2.39308 1.50151 0.44184  -0.17143 -0.10934 108 VAL A CG1   
791  C  CG2   . VAL A 108 ? 0.99354 2.44790 1.50010 0.33545  -0.16808 -0.15110 108 VAL A CG2   
792  N  N     . ILE A 109 ? 1.14873 2.25602 1.50690 0.43848  -0.13590 -0.09259 109 ILE A N     
793  C  CA    . ILE A 109 ? 1.12168 2.13465 1.45052 0.46615  -0.11646 -0.08124 109 ILE A CA    
794  C  C     . ILE A 109 ? 1.15068 2.15511 1.48087 0.51949  -0.11670 -0.06643 109 ILE A C     
795  O  O     . ILE A 109 ? 1.16183 2.16282 1.47168 0.54804  -0.13723 -0.04927 109 ILE A O     
796  C  CB    . ILE A 109 ? 1.09717 2.02017 1.36957 0.46525  -0.12190 -0.06687 109 ILE A CB    
797  C  CG1   . ILE A 109 ? 1.12307 2.06174 1.39696 0.41429  -0.12303 -0.08119 109 ILE A CG1   
798  C  CG2   . ILE A 109 ? 1.17895 2.00395 1.42159 0.48719  -0.10055 -0.05781 109 ILE A CG2   
799  C  CD1   . ILE A 109 ? 1.08569 2.03863 1.38956 0.38167  -0.09801 -0.10158 109 ILE A CD1   
800  N  N     . GLU A 110 ? 1.27861 2.27671 1.62996 0.53319  -0.09263 -0.07295 110 GLU A N     
801  C  CA    . GLU A 110 ? 1.26854 2.25596 1.62334 0.58400  -0.08807 -0.06092 110 GLU A CA    
802  C  C     . GLU A 110 ? 1.33182 2.20064 1.62516 0.61583  -0.08326 -0.04090 110 GLU A C     
803  O  O     . GLU A 110 ? 1.32465 2.11834 1.57945 0.59733  -0.07690 -0.03935 110 GLU A O     
804  C  CB    . GLU A 110 ? 1.20796 2.22569 1.60397 0.58567  -0.06065 -0.07644 110 GLU A CB    
805  C  CG    . GLU A 110 ? 1.19594 2.33175 1.65537 0.55565  -0.06198 -0.09554 110 GLU A CG    
806  C  CD    . GLU A 110 ? 1.39994 2.61728 1.90036 0.58857  -0.07616 -0.08954 110 GLU A CD    
807  O  OE1   . GLU A 110 ? 1.42623 2.61131 1.91952 0.63825  -0.07021 -0.07599 110 GLU A OE1   
808  O  OE2   . GLU A 110 ? 1.46884 2.78176 2.00808 0.56433  -0.09300 -0.09868 110 GLU A OE2   
809  N  N     . ARG A 111 ? 1.21799 2.07028 1.50276 0.66363  -0.08570 -0.02533 111 ARG A N     
810  C  CA    . ARG A 111 ? 1.18689 1.92310 1.41195 0.69400  -0.07780 -0.00688 111 ARG A CA    
811  C  C     . ARG A 111 ? 1.17484 1.84549 1.39006 0.69517  -0.04598 -0.01664 111 ARG A C     
812  O  O     . ARG A 111 ? 1.01362 1.72408 1.26630 0.70647  -0.02924 -0.02828 111 ARG A O     
813  C  CB    . ARG A 111 ? 1.14626 1.88446 1.36387 0.74488  -0.08863 0.01241  111 ARG A CB    
814  N  N     . GLY A 112 ? 1.22745 1.79742 1.39136 0.68263  -0.03705 -0.01238 112 GLY A N     
815  C  CA    . GLY A 112 ? 1.18215 1.68408 1.32905 0.67782  -0.00875 -0.02318 112 GLY A CA    
816  C  C     . GLY A 112 ? 1.16643 1.70563 1.34144 0.63557  0.00272  -0.04553 112 GLY A C     
817  O  O     . GLY A 112 ? 1.15174 1.64118 1.31295 0.63016  0.02695  -0.05690 112 GLY A O     
818  N  N     . GLU A 113 ? 1.16549 1.78691 1.37505 0.60434  -0.01284 -0.05287 113 GLU A N     
819  C  CA    . GLU A 113 ? 1.23443 1.89206 1.46954 0.56230  -0.00060 -0.07383 113 GLU A CA    
820  C  C     . GLU A 113 ? 1.09128 1.66889 1.28464 0.53811  0.00363  -0.07314 113 GLU A C     
821  O  O     . GLU A 113 ? 1.07920 1.61119 1.23970 0.53922  -0.01200 -0.05778 113 GLU A O     
822  C  CB    . GLU A 113 ? 1.24396 2.01017 1.52582 0.53382  -0.01764 -0.08256 113 GLU A CB    
823  C  CG    . GLU A 113 ? 1.23603 2.04127 1.54335 0.48644  -0.00384 -0.10405 113 GLU A CG    
824  C  CD    . GLU A 113 ? 1.19825 2.10998 1.55177 0.45671  -0.01753 -0.11487 113 GLU A CD    
825  O  OE1   . GLU A 113 ? 1.07038 2.03668 1.44343 0.47657  -0.03624 -0.10792 113 GLU A OE1   
826  O  OE2   . GLU A 113 ? 1.12340 2.06183 1.49109 0.41216  -0.00909 -0.13065 113 GLU A OE2   
827  N  N     . ARG A 114 ? 1.09710 1.65699 1.29035 0.51666  0.02587  -0.08957 114 ARG A N     
828  C  CA    . ARG A 114 ? 1.07207 1.56064 1.22852 0.49074  0.03038  -0.09040 114 ARG A CA    
829  C  C     . ARG A 114 ? 1.05668 1.57785 1.22313 0.44632  0.01287  -0.08862 114 ARG A C     
830  O  O     . ARG A 114 ? 1.10192 1.69961 1.30641 0.41827  0.01445  -0.10265 114 ARG A O     
831  C  CB    . ARG A 114 ? 1.11857 1.57887 1.26616 0.46583  0.05625  -0.10753 114 ARG A CB    
832  N  N     . ILE A 115 ? 0.98883 1.44875 1.11910 0.43907  -0.00111 -0.07202 115 ILE A N     
833  C  CA    . ILE A 115 ? 0.89075 1.37107 1.02373 0.40175  -0.01574 -0.06924 115 ILE A CA    
834  C  C     . ILE A 115 ? 0.94453 1.35215 1.04727 0.35869  -0.00872 -0.06741 115 ILE A C     
835  O  O     . ILE A 115 ? 0.89658 1.32467 1.00691 0.32171  -0.01288 -0.07071 115 ILE A O     
836  C  CB    . ILE A 115 ? 0.95873 1.43973 1.07718 0.42643  -0.03774 -0.05121 115 ILE A CB    
837  C  CG1   . ILE A 115 ? 1.03741 1.41762 1.10688 0.45238  -0.03501 -0.03287 115 ILE A CG1   
838  C  CG2   . ILE A 115 ? 0.84176 1.41779 0.99831 0.46363  -0.05077 -0.05324 115 ILE A CG2   
839  C  CD1   . ILE A 115 ? 1.07769 1.44526 1.12299 0.47743  -0.05354 -0.01265 115 ILE A CD1   
840  N  N     . ALA A 116 ? 0.92600 1.25068 0.99471 0.36228  0.00150  -0.06251 116 ALA A N     
841  C  CA    . ALA A 116 ? 0.85465 1.11693 0.89850 0.32387  0.00568  -0.05967 116 ALA A CA    
842  C  C     . ALA A 116 ? 0.99696 1.18980 1.01123 0.33010  0.01886  -0.06218 116 ALA A C     
843  O  O     . ALA A 116 ? 1.02899 1.21841 1.04026 0.36388  0.02743  -0.06700 116 ALA A O     
844  C  CB    . ALA A 116 ? 0.83757 1.06190 0.86087 0.31559  -0.00661 -0.04223 116 ALA A CB    
845  N  N     . GLN A 117 ? 0.91816 1.05604 0.90980 0.29759  0.02049  -0.05936 117 GLN A N     
846  C  CA    . GLN A 117 ? 0.98836 1.05487 0.94545 0.29604  0.02972  -0.06213 117 GLN A CA    
847  C  C     . GLN A 117 ? 1.03536 1.03395 0.96474 0.28061  0.02214  -0.04728 117 GLN A C     
848  O  O     . GLN A 117 ? 0.93527 0.94378 0.87497 0.25791  0.01330  -0.03790 117 GLN A O     
849  C  CB    . GLN A 117 ? 0.85872 0.92969 0.81417 0.26759  0.03966  -0.07626 117 GLN A CB    
850  C  CG    . GLN A 117 ? 0.94697 1.04736 0.91925 0.23002  0.03398  -0.07437 117 GLN A CG    
851  C  CD    . GLN A 117 ? 1.10984 1.20757 1.07244 0.20511  0.04414  -0.08584 117 GLN A CD    
852  O  OE1   . GLN A 117 ? 1.00872 1.05312 0.93849 0.19834  0.04747  -0.08875 117 GLN A OE1   
853  N  NE2   . GLN A 117 ? 1.05364 1.20595 1.04022 0.18960  0.04947  -0.09270 117 GLN A NE2   
854  N  N     . LEU A 118 ? 1.11097 1.03940 1.00476 0.29263  0.02789  -0.04600 118 LEU A N     
855  C  CA    . LEU A 118 ? 1.11503 0.97537 0.98119 0.27586  0.02349  -0.03364 118 LEU A CA    
856  C  C     . LEU A 118 ? 1.07050 0.88861 0.91501 0.24352  0.02624  -0.04257 118 LEU A C     
857  O  O     . LEU A 118 ? 1.25579 1.03958 1.07404 0.25208  0.03668  -0.05543 118 LEU A O     
858  C  CB    . LEU A 118 ? 1.16940 0.97262 1.00462 0.30925  0.02816  -0.02499 118 LEU A CB    
859  C  CG    . LEU A 118 ? 1.28527 1.01128 1.08818 0.28951  0.02754  -0.01326 118 LEU A CG    
860  C  CD1   . LEU A 118 ? 1.05594 0.80713 0.87981 0.26705  0.01730  0.00157  118 LEU A CD1   
861  C  CD2   . LEU A 118 ? 1.26849 0.92871 1.03329 0.32468  0.03600  -0.00531 118 LEU A CD2   
862  N  N     . VAL A 119 ? 1.04971 0.87123 0.90394 0.20774  0.01685  -0.03580 119 VAL A N     
863  C  CA    . VAL A 119 ? 1.17336 0.96623 1.01079 0.17452  0.01392  -0.04190 119 VAL A CA    
864  C  C     . VAL A 119 ? 1.19969 0.93797 1.01997 0.15497  0.00833  -0.03139 119 VAL A C     
865  O  O     . VAL A 119 ? 1.23705 0.98689 1.07689 0.14888  0.00313  -0.01632 119 VAL A O     
866  C  CB    . VAL A 119 ? 1.13678 0.98141 1.00140 0.14965  0.00695  -0.04136 119 VAL A CB    
867  C  CG1   . VAL A 119 ? 1.11076 0.92818 0.95482 0.11832  0.00062  -0.04573 119 VAL A CG1   
868  C  CG2   . VAL A 119 ? 1.05362 0.95229 0.93574 0.16452  0.01510  -0.05207 119 VAL A CG2   
869  N  N     . ILE A 120 ? 1.22700 0.90545 1.00938 0.14298  0.01103  -0.04048 120 ILE A N     
870  C  CA    . ILE A 120 ? 1.32506 0.95134 1.09009 0.11686  0.00629  -0.03360 120 ILE A CA    
871  C  C     . ILE A 120 ? 1.30955 0.95645 1.08696 0.07627  -0.00846 -0.03377 120 ILE A C     
872  O  O     . ILE A 120 ? 1.35313 1.00417 1.11564 0.06574  -0.01153 -0.04651 120 ILE A O     
873  C  CB    . ILE A 120 ? 1.35451 0.89784 1.06655 0.12327  0.01760  -0.04455 120 ILE A CB    
874  C  CG1   . ILE A 120 ? 1.39394 0.91949 1.09444 0.17111  0.03195  -0.04214 120 ILE A CG1   
875  C  CG2   . ILE A 120 ? 1.41159 0.90090 1.10613 0.09053  0.01388  -0.03826 120 ILE A CG2   
876  C  CD1   . ILE A 120 ? 1.36910 0.90189 1.08665 0.18424  0.03054  -0.02153 120 ILE A CD1   
877  N  N     . ALA A 121 ? 1.33082 0.99198 1.13476 0.05501  -0.01710 -0.01879 121 ALA A N     
878  C  CA    . ALA A 121 ? 1.43899 1.13042 1.26402 0.02112  -0.03296 -0.01474 121 ALA A CA    
879  C  C     . ALA A 121 ? 1.53735 1.20786 1.37047 -0.00647 -0.03791 -0.00466 121 ALA A C     
880  O  O     . ALA A 121 ? 1.49543 1.14410 1.33004 0.00276  -0.02755 0.00458  121 ALA A O     
881  C  CB    . ALA A 121 ? 1.35184 1.11188 1.22065 0.02715  -0.03719 -0.00443 121 ALA A CB    
882  N  N     . PRO A 122 ? 1.70983 1.38839 1.54769 -0.04138 -0.05370 -0.00582 122 PRO A N     
883  C  CA    . PRO A 122 ? 1.71867 1.38980 1.57341 -0.07207 -0.05872 0.00341  122 PRO A CA    
884  C  C     . PRO A 122 ? 1.65920 1.38952 1.57144 -0.07019 -0.05940 0.02342  122 PRO A C     
885  O  O     . PRO A 122 ? 1.60917 1.39366 1.55125 -0.06388 -0.06743 0.02931  122 PRO A O     
886  C  CB    . PRO A 122 ? 1.77068 1.44365 1.61376 -0.10839 -0.07902 -0.00587 122 PRO A CB    
887  C  CG    . PRO A 122 ? 1.73728 1.44535 1.57835 -0.09481 -0.08719 -0.01027 122 PRO A CG    
888  C  CD    . PRO A 122 ? 1.70956 1.40151 1.53242 -0.05567 -0.06779 -0.01649 122 PRO A CD    
889  N  N     . VAL A 123 ? 1.52535 1.23942 1.44875 -0.07536 -0.04824 0.03390  123 VAL A N     
890  C  CA    . VAL A 123 ? 1.47434 1.23691 1.44856 -0.07558 -0.04430 0.05220  123 VAL A CA    
891  C  C     . VAL A 123 ? 1.45260 1.22506 1.45318 -0.11496 -0.05060 0.05832  123 VAL A C     
892  O  O     . VAL A 123 ? 1.47917 1.20124 1.45053 -0.13889 -0.04909 0.05055  123 VAL A O     
893  C  CB    . VAL A 123 ? 1.43370 1.17542 1.39979 -0.04858 -0.02382 0.06064  123 VAL A CB    
894  C  CG1   . VAL A 123 ? 1.48730 1.15699 1.41398 -0.05646 -0.01148 0.05918  123 VAL A CG1   
895  C  CG2   . VAL A 123 ? 1.34119 1.13127 1.35472 -0.04770 -0.01702 0.07769  123 VAL A CG2   
896  N  N     . GLN A 124 ? 1.33604 1.17380 1.39238 -0.12217 -0.05681 0.07174  124 GLN A N     
897  C  CA    . GLN A 124 ? 1.39990 1.26814 1.49541 -0.15880 -0.06508 0.07864  124 GLN A CA    
898  C  C     . GLN A 124 ? 1.39400 1.27540 1.52404 -0.15842 -0.04366 0.09446  124 GLN A C     
899  O  O     . GLN A 124 ? 1.27692 1.19774 1.43866 -0.13519 -0.03503 0.10620  124 GLN A O     
900  C  CB    . GLN A 124 ? 1.31927 1.25726 1.45617 -0.16542 -0.08855 0.08392  124 GLN A CB    
901  C  CG    . GLN A 124 ? 1.36700 1.34298 1.54170 -0.20622 -0.10519 0.08749  124 GLN A CG    
902  C  CD    . GLN A 124 ? 1.49220 1.42913 1.62208 -0.23862 -0.12339 0.06899  124 GLN A CD    
903  O  OE1   . GLN A 124 ? 1.53192 1.48910 1.68229 -0.27840 -0.13698 0.06756  124 GLN A OE1   
904  N  NE2   . GLN A 124 ? 1.61150 1.49385 1.67999 -0.22293 -0.12294 0.05364  124 GLN A NE2   
905  N  N     . ARG A 125 ? 1.38627 1.22938 1.50533 -0.18541 -0.03280 0.09405  125 ARG A N     
906  C  CA    . ARG A 125 ? 1.30869 1.16583 1.46136 -0.19275 -0.01112 0.10931  125 ARG A CA    
907  C  C     . ARG A 125 ? 1.24079 1.18278 1.46838 -0.21393 -0.02109 0.11972  125 ARG A C     
908  O  O     . ARG A 125 ? 1.22096 1.19335 1.46633 -0.24095 -0.04530 0.11376  125 ARG A O     
909  C  CB    . ARG A 125 ? 1.38710 1.17403 1.50286 -0.21954 0.00477  0.10603  125 ARG A CB    
910  C  CG    . ARG A 125 ? 1.36625 1.14465 1.49481 -0.22001 0.03437  0.12174  125 ARG A CG    
911  C  CD    . ARG A 125 ? 1.39311 1.12694 1.47688 -0.17652 0.05137  0.12652  125 ARG A CD    
912  N  NE    . ARG A 125 ? 1.47380 1.16797 1.54175 -0.18159 0.08040  0.13915  125 ARG A NE    
913  C  CZ    . ARG A 125 ? 1.44724 1.09159 1.46732 -0.14972 0.09647  0.14544  125 ARG A CZ    
914  N  NH1   . ARG A 125 ? 1.39088 1.02398 1.37951 -0.11084 0.08631  0.13939  125 ARG A NH1   
915  N  NH2   . ARG A 125 ? 1.56242 1.16998 1.56567 -0.15775 0.12323  0.15858  125 ARG A NH2   
916  N  N     . VAL A 126 ? 1.24733 1.22909 1.51813 -0.20025 -0.00247 0.13543  126 VAL A N     
917  C  CA    . VAL A 126 ? 1.23172 1.30002 1.57954 -0.21027 -0.00855 0.14762  126 VAL A CA    
918  C  C     . VAL A 126 ? 1.11780 1.20044 1.50163 -0.22237 0.02129  0.16064  126 VAL A C     
919  O  O     . VAL A 126 ? 1.11153 1.14262 1.45966 -0.20961 0.04792  0.16358  126 VAL A O     
920  C  CB    . VAL A 126 ? 1.14966 1.26336 1.51997 -0.17270 -0.01584 0.15413  126 VAL A CB    
921  C  CG1   . VAL A 126 ? 1.07246 1.18475 1.44950 -0.14315 0.01434  0.16465  126 VAL A CG1   
922  C  CG2   . VAL A 126 ? 1.11009 1.30629 1.54573 -0.18318 -0.03777 0.16262  126 VAL A CG2   
923  N  N     . GLU A 127 ? 1.10423 1.25998 1.55908 -0.24735 0.01661  0.16895  127 GLU A N     
924  C  CA    . GLU A 127 ? 1.10866 1.29161 1.60910 -0.26274 0.04631  0.18146  127 GLU A CA    
925  C  C     . GLU A 127 ? 1.10084 1.34930 1.65739 -0.22914 0.05890  0.19649  127 GLU A C     
926  O  O     . GLU A 127 ? 1.06875 1.38728 1.67638 -0.22043 0.03748  0.20162  127 GLU A O     
927  C  CB    . GLU A 127 ? 1.07449 1.30250 1.62367 -0.31476 0.03590  0.18024  127 GLU A CB    
928  N  N     . VAL A 128 ? 1.15788 1.37915 1.70001 -0.20936 0.09402  0.20379  128 VAL A N     
929  C  CA    . VAL A 128 ? 1.13148 1.39922 1.71459 -0.17584 0.11205  0.21592  128 VAL A CA    
930  C  C     . VAL A 128 ? 1.05978 1.40383 1.72741 -0.19584 0.12922  0.22883  128 VAL A C     
931  O  O     . VAL A 128 ? 1.10847 1.43646 1.77772 -0.21616 0.15992  0.23299  128 VAL A O     
932  C  CB    . VAL A 128 ? 1.18184 1.38754 1.70810 -0.14781 0.14190  0.21645  128 VAL A CB    
933  C  CG1   . VAL A 128 ? 1.03875 1.28672 1.60391 -0.11713 0.16444  0.22705  128 VAL A CG1   
934  C  CG2   . VAL A 128 ? 1.16310 1.30750 1.61589 -0.12710 0.12327  0.20379  128 VAL A CG2   
935  N  N     . VAL A 129 ? 0.93055 1.35925 1.66883 -0.18919 0.11015  0.23620  129 VAL A N     
936  C  CA    . VAL A 129 ? 1.01024 1.52879 1.84173 -0.20062 0.12455  0.24994  129 VAL A CA    
937  C  C     . VAL A 129 ? 1.05594 1.61649 1.92500 -0.15272 0.13765  0.26226  129 VAL A C     
938  O  O     . VAL A 129 ? 1.01919 1.60174 1.89429 -0.12761 0.11032  0.26404  129 VAL A O     
939  C  CB    . VAL A 129 ? 0.93153 1.52299 1.82103 -0.23642 0.08838  0.24940  129 VAL A CB    
940  C  CG1   . VAL A 129 ? 0.99697 1.58319 1.85712 -0.22411 0.04287  0.24236  129 VAL A CG1   
941  C  CG2   . VAL A 129 ? 0.74758 1.45278 1.74608 -0.23388 0.09707  0.26617  129 VAL A CG2   
942  N  N     . GLU A 130 ? 1.02045 1.58471 1.90818 -0.13982 0.18164  0.27059  130 GLU A N     
943  C  CA    . GLU A 130 ? 0.99829 1.59173 1.91568 -0.09401 0.20060  0.28098  130 GLU A CA    
944  C  C     . GLU A 130 ? 0.90401 1.60840 1.92522 -0.08773 0.18863  0.29576  130 GLU A C     
945  O  O     . GLU A 130 ? 0.84821 1.61142 1.92547 -0.11785 0.18984  0.29792  130 GLU A O     
946  C  CB    . GLU A 130 ? 0.99327 1.55506 1.89529 -0.08334 0.25357  0.28426  130 GLU A CB    
947  C  CG    . GLU A 130 ? 1.03800 1.62432 1.96861 -0.03722 0.27930  0.29353  130 GLU A CG    
948  C  CD    . GLU A 130 ? 1.04691 1.58335 1.93907 -0.02593 0.33051  0.29283  130 GLU A CD    
949  O  OE1   . GLU A 130 ? 1.05215 1.54107 1.90046 -0.05385 0.34586  0.28792  130 GLU A OE1   
950  O  OE2   . GLU A 130 ? 1.03799 1.57025 1.92733 0.01125  0.35163  0.29401  130 GLU A OE2   
951  N  N     . VAL A 131 ? 0.85469 1.57895 1.88777 -0.04699 0.17461  0.30258  131 VAL A N     
952  C  CA    . VAL A 131 ? 0.78983 1.59573 1.88832 -0.02926 0.15652  0.31176  131 VAL A CA    
953  C  C     . VAL A 131 ? 0.81281 1.60937 1.91154 0.02063  0.18828  0.31785  131 VAL A C     
954  O  O     . VAL A 131 ? 0.79694 1.52595 1.84409 0.04108  0.21719  0.31460  131 VAL A O     
955  C  CB    . VAL A 131 ? 0.84048 1.67054 1.94062 -0.02682 0.10397  0.31430  131 VAL A CB    
956  C  CG1   . VAL A 131 ? 0.84868 1.68633 1.94567 -0.07981 0.07188  0.30599  131 VAL A CG1   
957  C  CG2   . VAL A 131 ? 0.82237 1.58648 1.86131 0.00636  0.10082  0.31350  131 VAL A CG2   
958  N  N     . GLU A 132 ? 0.84724 1.71139 2.00257 0.03908  0.18247  0.32582  132 GLU A N     
959  C  CA    . GLU A 132 ? 0.82955 1.68737 1.98860 0.08719  0.20874  0.33272  132 GLU A CA    
960  C  C     . GLU A 132 ? 0.81908 1.68069 1.97254 0.12271  0.17914  0.34168  132 GLU A C     
961  O  O     . GLU A 132 ? 0.78997 1.64014 1.94231 0.16361  0.19859  0.34830  132 GLU A O     
962  C  CB    . GLU A 132 ? 0.58879 1.51625 1.81491 0.08810  0.22954  0.33659  132 GLU A CB    
963  N  N     . GLU A 133 ? 0.81059 1.68239 1.95517 0.10717  0.13390  0.34196  133 GLU A N     
964  C  CA    . GLU A 133 ? 0.81481 1.68602 1.94635 0.13789  0.10413  0.35102  133 GLU A CA    
965  C  C     . GLU A 133 ? 0.78872 1.64203 1.88509 0.11340  0.06278  0.34633  133 GLU A C     
966  O  O     . GLU A 133 ? 0.79959 1.68280 1.91213 0.07074  0.04112  0.33983  133 GLU A O     
967  C  CB    . GLU A 133 ? 0.70586 1.66080 1.90126 0.15261  0.08463  0.36268  133 GLU A CB    
968  N  N     . VAL A 134 ? 0.81602 1.61693 1.86120 0.13874  0.05350  0.34863  134 VAL A N     
969  C  CA    . VAL A 134 ? 0.79423 1.57672 1.80220 0.12130  0.01391  0.34506  134 VAL A CA    
970  C  C     . VAL A 134 ? 0.86239 1.67669 1.87539 0.14115  -0.02289 0.35717  134 VAL A C     
971  O  O     . VAL A 134 ? 0.80309 1.63032 1.83305 0.17776  -0.01211 0.36868  134 VAL A O     
972  C  CB    . VAL A 134 ? 0.77189 1.46751 1.70938 0.13080  0.02917  0.33593  134 VAL A CB    
973  C  CG1   . VAL A 134 ? 0.80274 1.45133 1.70507 0.10065  0.05371  0.31616  134 VAL A CG1   
974  C  CG2   . VAL A 134 ? 0.80385 1.45713 1.71915 0.17645  0.06015  0.34191  134 VAL A CG2   
975  N  N     . SER A 135 ? 0.90041 1.72400 1.89431 0.11639  -0.06651 0.35440  135 SER A N     
976  C  CA    . SER A 135 ? 0.82852 1.67996 1.81847 0.13112  -0.10488 0.36530  135 SER A CA    
977  C  C     . SER A 135 ? 0.86520 1.65391 1.80249 0.17303  -0.09605 0.37364  135 SER A C     
978  O  O     . SER A 135 ? 0.84960 1.56915 1.73864 0.17782  -0.07572 0.36648  135 SER A O     
979  C  CB    . SER A 135 ? 0.81482 1.68000 1.78352 0.09088  -0.15182 0.35744  135 SER A CB    
980  O  OG    . SER A 135 ? 0.89816 1.69593 1.80757 0.07835  -0.15207 0.34735  135 SER A OG    
981  N  N     . GLN A 136 ? 0.76729 1.58000 1.71365 0.20310  -0.11085 0.38858  136 GLN A N     
982  C  CA    . GLN A 136 ? 0.82338 1.57427 1.71735 0.24127  -0.10329 0.39785  136 GLN A CA    
983  C  C     . GLN A 136 ? 0.78606 1.50177 1.61811 0.22795  -0.13833 0.39614  136 GLN A C     
984  O  O     . GLN A 136 ? 0.68352 1.44230 1.52032 0.20438  -0.18027 0.39623  136 GLN A O     
985  C  CB    . GLN A 136 ? 0.83209 1.61790 1.75620 0.27984  -0.10624 0.41590  136 GLN A CB    
986  C  CG    . GLN A 136 ? 0.67615 1.39708 1.54107 0.31598  -0.10507 0.42723  136 GLN A CG    
987  C  CD    . GLN A 136 ? 0.89541 1.64374 1.79000 0.35828  -0.10307 0.44582  136 GLN A CD    
988  O  OE1   . GLN A 136 ? 0.81517 1.64552 1.77645 0.35928  -0.11603 0.45173  136 GLN A OE1   
989  N  NE2   . GLN A 136 ? 1.07784 1.75655 1.92297 0.39320  -0.08606 0.45487  136 GLN A NE2   
990  N  N     . THR A 137 ? 0.89870 1.53419 1.66922 0.24138  -0.12000 0.39330  137 THR A N     
991  C  CA    . THR A 137 ? 0.95922 1.55168 1.66388 0.23292  -0.14670 0.39260  137 THR A CA    
992  C  C     . THR A 137 ? 1.07662 1.60992 1.73286 0.27124  -0.13420 0.40519  137 THR A C     
993  O  O     . THR A 137 ? 1.13416 1.64992 1.80312 0.30256  -0.10153 0.41140  137 THR A O     
994  C  CB    . THR A 137 ? 0.92330 1.46082 1.58126 0.20284  -0.13535 0.36902  137 THR A CB    
995  O  OG1   . THR A 137 ? 0.97269 1.45421 1.61393 0.21905  -0.08845 0.36042  137 THR A OG1   
996  C  CG2   . THR A 137 ? 0.82622 1.40568 1.51537 0.16083  -0.14713 0.35266  137 THR A CG2   
997  N  N     . GLN A 138 ? 1.20753 1.70528 1.80286 0.26657  -0.15942 0.40850  138 GLN A N     
998  C  CA    . GLN A 138 ? 1.23384 1.66470 1.77263 0.29790  -0.14697 0.42019  138 GLN A CA    
999  C  C     . GLN A 138 ? 1.29574 1.64700 1.79460 0.30349  -0.10369 0.40966  138 GLN A C     
1000 O  O     . GLN A 138 ? 1.32123 1.61737 1.79106 0.33208  -0.07639 0.41634  138 GLN A O     
1001 C  CB    . GLN A 138 ? 1.25692 1.67139 1.73705 0.28838  -0.18529 0.42712  138 GLN A CB    
1002 C  CG    . GLN A 138 ? 1.34916 1.75994 1.79827 0.24431  -0.20621 0.40803  138 GLN A CG    
1003 C  CD    . GLN A 138 ? 1.31338 1.80823 1.81650 0.21535  -0.24132 0.40392  138 GLN A CD    
1004 O  OE1   . GLN A 138 ? 1.18941 1.71855 1.74562 0.20066  -0.22746 0.39212  138 GLN A OE1   
1005 N  NE2   . GLN A 138 ? 1.23805 1.75932 1.71979 0.20354  -0.28419 0.40978  138 GLN A NE2   
1006 N  N     . ARG A 139 ? 1.23461 1.56828 1.71715 0.26887  -0.09445 0.38251  139 ARG A N     
1007 C  CA    . ARG A 139 ? 1.16823 1.42896 1.60834 0.26606  -0.05276 0.36211  139 ARG A CA    
1008 C  C     . ARG A 139 ? 1.26838 1.53586 1.75552 0.29170  -0.01549 0.36774  139 ARG A C     
1009 O  O     . ARG A 139 ? 1.32705 1.53124 1.78071 0.30884  0.01962  0.36471  139 ARG A O     
1010 C  CB    . ARG A 139 ? 1.09728 1.34412 1.51004 0.22399  -0.05398 0.33018  139 ARG A CB    
1011 C  CG    . ARG A 139 ? 1.01449 1.19052 1.37606 0.21726  -0.01862 0.30782  139 ARG A CG    
1012 C  CD    . ARG A 139 ? 0.95591 1.13069 1.30452 0.18272  -0.01936 0.27974  139 ARG A CD    
1013 N  NE    . ARG A 139 ? 1.04223 1.15607 1.32759 0.17009  -0.00300 0.25846  139 ARG A NE    
1014 C  CZ    . ARG A 139 ? 1.01019 1.10495 1.24964 0.15052  -0.01936 0.24659  139 ARG A CZ    
1015 N  NH1   . ARG A 139 ? 1.00695 1.13085 1.24818 0.13981  -0.05277 0.25215  139 ARG A NH1   
1016 N  NH2   . ARG A 139 ? 1.02503 1.07217 1.21545 0.14013  -0.00107 0.22766  139 ARG A NH2   
1017 N  N     . GLY A 140 ? 1.39811 1.74001 1.96060 0.29241  -0.02063 0.37475  140 GLY A N     
1018 C  CA    . GLY A 140 ? 1.39142 1.74145 1.99423 0.31318  0.01634  0.37653  140 GLY A CA    
1019 C  C     . GLY A 140 ? 1.43484 1.74213 2.01799 0.29896  0.05219  0.35403  140 GLY A C     
1020 O  O     . GLY A 140 ? 1.36154 1.64494 1.90448 0.26412  0.04469  0.33054  140 GLY A O     
1021 N  N     . GLU A 141 ? 1.43245 1.72319 2.02995 0.32118  0.09177  0.35487  141 GLU A N     
1022 C  CA    . GLU A 141 ? 1.50530 1.75351 2.08041 0.31110  0.12861  0.33429  141 GLU A CA    
1023 C  C     . GLU A 141 ? 1.58033 1.73876 2.07125 0.30690  0.14278  0.31832  141 GLU A C     
1024 O  O     . GLU A 141 ? 1.69118 1.79980 2.15931 0.33424  0.16971  0.32496  141 GLU A O     
1025 C  CB    . GLU A 141 ? 1.47467 1.73097 2.08160 0.33102  0.16564  0.33723  141 GLU A CB    
1026 C  CG    . GLU A 141 ? 1.48020 1.82342 2.16259 0.33101  0.15243  0.34990  141 GLU A CG    
1027 C  CD    . GLU A 141 ? 1.63167 2.00393 2.33628 0.35776  0.13532  0.37024  141 GLU A CD    
1028 O  OE1   . GLU A 141 ? 1.74677 2.06262 2.40606 0.38025  0.14286  0.37521  141 GLU A OE1   
1029 O  OE2   . GLU A 141 ? 1.56927 2.02003 2.33546 0.35572  0.11457  0.38092  141 GLU A OE2   
1030 N  N     . GLY A 142 ? 1.29534 1.43260 1.74025 0.27213  0.12611  0.29680  142 GLY A N     
1031 C  CA    . GLY A 142 ? 1.40480 1.46833 1.77525 0.26193  0.13705  0.27958  142 GLY A CA    
1032 C  C     . GLY A 142 ? 1.42957 1.44126 1.76899 0.26186  0.17776  0.26180  142 GLY A C     
1033 O  O     . GLY A 142 ? 1.23054 1.26088 1.60064 0.26691  0.19790  0.26032  142 GLY A O     
1034 N  N     . LYS B 3   ? 1.65998 1.60251 1.17688 -0.25366 -0.41001 0.04613  3   LYS B N     
1035 C  CA    . LYS B 3   ? 1.73180 1.68060 1.30040 -0.21723 -0.37455 0.05797  3   LYS B CA    
1036 C  C     . LYS B 3   ? 1.78427 1.67068 1.29982 -0.20439 -0.33336 0.03818  3   LYS B C     
1037 O  O     . LYS B 3   ? 1.88022 1.72386 1.31546 -0.21495 -0.33267 0.02481  3   LYS B O     
1038 C  CB    . LYS B 3   ? 1.61476 1.60892 1.21559 -0.19089 -0.38753 0.09337  3   LYS B CB    
1039 N  N     . VAL B 4   ? 1.48063 1.36544 1.04178 -0.18182 -0.29897 0.03630  4   VAL B N     
1040 C  CA    . VAL B 4   ? 1.48375 1.32311 1.00936 -0.16787 -0.25945 0.01808  4   VAL B CA    
1041 C  C     . VAL B 4   ? 1.38913 1.22942 0.89583 -0.14881 -0.24811 0.03441  4   VAL B C     
1042 O  O     . VAL B 4   ? 1.43523 1.31110 0.98841 -0.13211 -0.25287 0.05982  4   VAL B O     
1043 C  CB    . VAL B 4   ? 1.31058 1.15251 0.89179 -0.15207 -0.23061 0.01011  4   VAL B CB    
1044 N  N     . ILE B 5   ? 1.34252 1.13966 0.77857 -0.15156 -0.23017 0.01958  5   ILE B N     
1045 C  CA    . ILE B 5   ? 1.37485 1.16289 0.78191 -0.13824 -0.21444 0.03244  5   ILE B CA    
1046 C  C     . ILE B 5   ? 1.44778 1.22726 0.87571 -0.12126 -0.17008 0.01964  5   ILE B C     
1047 O  O     . ILE B 5   ? 1.42591 1.19050 0.85645 -0.12131 -0.15047 -0.00469 5   ILE B O     
1048 C  CB    . ILE B 5   ? 1.60016 1.34832 0.91179 -0.15440 -0.22195 0.02611  5   ILE B CB    
1049 C  CG1   . ILE B 5   ? 1.62407 1.32768 0.88630 -0.16645 -0.19973 -0.00917 5   ILE B CG1   
1050 C  CG2   . ILE B 5   ? 1.57567 1.34103 0.86762 -0.17079 -0.27098 0.04194  5   ILE B CG2   
1051 C  CD1   . ILE B 5   ? 1.82494 1.48251 0.99017 -0.17742 -0.19040 -0.01867 5   ILE B CD1   
1052 N  N     . LEU B 6   ? 1.42667 1.21553 0.86892 -0.10652 -0.15437 0.03638  6   LEU B N     
1053 C  CA    . LEU B 6   ? 1.45176 1.24046 0.91586 -0.09377 -0.11445 0.02575  6   LEU B CA    
1054 C  C     . LEU B 6   ? 1.32972 1.09260 0.73825 -0.09590 -0.09486 0.03043  6   LEU B C     
1055 O  O     . LEU B 6   ? 1.40764 1.17190 0.81507 -0.09039 -0.10000 0.05496  6   LEU B O     
1056 C  CB    . LEU B 6   ? 1.38521 1.20954 0.92646 -0.07773 -0.11067 0.03955  6   LEU B CB    
1057 C  CG    . LEU B 6   ? 1.30999 1.14417 0.88473 -0.06641 -0.07479 0.02790  6   LEU B CG    
1058 C  CD1   . LEU B 6   ? 1.35891 1.18507 0.91880 -0.06395 -0.05515 0.03986  6   LEU B CD1   
1059 C  CD2   . LEU B 6   ? 1.38780 1.20912 0.94234 -0.06857 -0.05296 -0.00141 6   LEU B CD2   
1060 N  N     . LYS B 7   ? 1.35772 1.09413 0.71867 -0.10313 -0.06993 0.00734  7   LYS B N     
1061 C  CA    . LYS B 7   ? 1.45924 1.16957 0.76524 -0.10822 -0.04509 0.00897  7   LYS B CA    
1062 C  C     . LYS B 7   ? 1.40757 1.13725 0.75804 -0.09936 -0.01042 0.00751  7   LYS B C     
1063 O  O     . LYS B 7   ? 1.34732 1.10136 0.74489 -0.09197 0.00772  -0.01103 7   LYS B O     
1064 C  CB    . LYS B 7   ? 1.42278 1.09983 0.66238 -0.11967 -0.02795 -0.01666 7   LYS B CB    
1065 N  N     . ILE B 8   ? 1.37619 1.09336 0.70904 -0.10061 -0.00188 0.02737  8   ILE B N     
1066 C  CA    . ILE B 8   ? 1.43990 1.17032 0.80806 -0.09801 0.03021  0.02674  8   ILE B CA    
1067 C  C     . ILE B 8   ? 1.43933 1.13409 0.74327 -0.11155 0.05842  0.02935  8   ILE B C     
1068 O  O     . ILE B 8   ? 1.51259 1.17103 0.75720 -0.11539 0.04472  0.05018  8   ILE B O     
1069 C  CB    . ILE B 8   ? 1.29533 1.04075 0.71375 -0.08613 0.01619  0.05035  8   ILE B CB    
1070 N  N     . LYS B 9   ? 1.36420 1.07128 0.67993 -0.11897 0.09765  0.00910  9   LYS B N     
1071 C  CA    . LYS B 9   ? 1.59872 1.27615 0.86093 -0.13561 0.13192  0.00907  9   LYS B CA    
1072 C  C     . LYS B 9   ? 1.43217 1.12456 0.73655 -0.14083 0.15762  0.01149  9   LYS B C     
1073 O  O     . LYS B 9   ? 1.38899 1.12798 0.75899 -0.13771 0.16922  -0.00650 9   LYS B O     
1074 C  CB    . LYS B 9   ? 1.47434 1.15566 0.71034 -0.14450 0.16098  -0.01962 9   LYS B CB    
1075 N  N     . ARG B 10  ? 1.57425 1.22410 0.83686 -0.14913 0.16619  0.03371  10  ARG B N     
1076 C  CA    . ARG B 10  ? 1.53244 1.18288 0.82478 -0.15695 0.18956  0.03793  10  ARG B CA    
1077 C  C     . ARG B 10  ? 1.53831 1.18811 0.81148 -0.18289 0.23688  0.01917  10  ARG B C     
1078 O  O     . ARG B 10  ? 1.64457 1.24936 0.84483 -0.19704 0.25477  0.02564  10  ARG B O     
1079 C  CB    . ARG B 10  ? 1.64605 1.24394 0.90215 -0.15050 0.17685  0.07262  10  ARG B CB    
1080 C  CG    . ARG B 10  ? 1.61580 1.22617 0.90507 -0.12450 0.13256  0.09161  10  ARG B CG    
1081 C  CD    . ARG B 10  ? 1.81062 1.37022 1.04190 -0.11339 0.11117  0.12717  10  ARG B CD    
1082 N  NE    . ARG B 10  ? 1.70068 1.22675 0.93422 -0.10689 0.12281  0.14902  10  ARG B NE    
1083 C  CZ    . ARG B 10  ? 1.80889 1.28433 0.99178 -0.09400 0.11141  0.18275  10  ARG B CZ    
1084 N  NH1   . ARG B 10  ? 1.85569 1.31202 0.98023 -0.08823 0.08570  0.19923  10  ARG B NH1   
1085 N  NH2   . ARG B 10  ? 1.85670 1.29766 1.04432 -0.08586 0.12601  0.20054  10  ARG B NH2   
1086 N  N     . LEU B 11  ? 1.43223 1.13467 0.77071 -0.18990 0.25687  -0.00371 11  LEU B N     
1087 C  CA    . LEU B 11  ? 1.46630 1.18371 0.80318 -0.21676 0.30194  -0.02325 11  LEU B CA    
1088 C  C     . LEU B 11  ? 1.52050 1.18317 0.81595 -0.23882 0.32546  -0.00619 11  LEU B C     
1089 O  O     . LEU B 11  ? 1.54980 1.16871 0.82816 -0.22805 0.30614  0.01972  11  LEU B O     
1090 C  CB    . LEU B 11  ? 1.41843 1.21393 0.84181 -0.21638 0.31003  -0.04976 11  LEU B CB    
1091 C  CG    . LEU B 11  ? 1.39679 1.24296 0.85468 -0.19647 0.29894  -0.06996 11  LEU B CG    
1092 C  CD1   . LEU B 11  ? 1.45178 1.37604 0.99138 -0.19535 0.30920  -0.09365 11  LEU B CD1   
1093 C  CD2   . LEU B 11  ? 1.26318 1.09279 0.66639 -0.20340 0.32067  -0.07996 11  LEU B CD2   
1094 N  N     . PRO B 12  ? 1.52740 1.18899 0.80450 -0.26982 0.36952  -0.01984 12  PRO B N     
1095 C  CA    . PRO B 12  ? 1.69773 1.29564 0.92610 -0.29442 0.39613  -0.00365 12  PRO B CA    
1096 C  C     . PRO B 12  ? 1.62286 1.20811 0.88448 -0.29182 0.38690  0.00679  12  PRO B C     
1097 O  O     . PRO B 12  ? 1.72369 1.23399 0.93235 -0.29178 0.38838  0.03345  12  PRO B O     
1098 C  CB    . PRO B 12  ? 1.42749 1.06306 0.68314 -0.32319 0.43291  -0.03029 12  PRO B CB    
1099 C  CG    . PRO B 12  ? 1.48819 1.16403 0.74580 -0.31318 0.43331  -0.04678 12  PRO B CG    
1100 C  CD    . PRO B 12  ? 1.54530 1.25332 0.83242 -0.28350 0.39938  -0.04785 12  PRO B CD    
1101 N  N     . HIS B 13  ? 1.53172 1.18405 0.87497 -0.28794 0.37820  -0.01269 13  HIS B N     
1102 C  CA    . HIS B 13  ? 1.58145 1.22085 0.95299 -0.28797 0.37314  -0.00635 13  HIS B CA    
1103 C  C     . HIS B 13  ? 1.50065 1.12345 0.88262 -0.24966 0.33067  0.01679  13  HIS B C     
1104 O  O     . HIS B 13  ? 1.54458 1.16997 0.96216 -0.24348 0.32312  0.01862  13  HIS B O     
1105 C  CB    . HIS B 13  ? 1.37943 1.09753 0.82835 -0.30364 0.38306  -0.03745 13  HIS B CB    
1106 C  CG    . HIS B 13  ? 1.41549 1.21722 0.92097 -0.28622 0.36651  -0.05789 13  HIS B CG    
1107 N  ND1   . HIS B 13  ? 1.47916 1.31757 0.98296 -0.29615 0.38649  -0.07554 13  HIS B ND1   
1108 C  CD2   . HIS B 13  ? 1.22572 1.07737 0.78864 -0.25854 0.33474  -0.06315 13  HIS B CD2   
1109 C  CE1   . HIS B 13  ? 1.38255 1.28742 0.93992 -0.27276 0.36707  -0.09033 13  HIS B CE1   
1110 N  NE2   . HIS B 13  ? 1.25091 1.16349 0.84327 -0.25064 0.33517  -0.08268 13  HIS B NE2   
1111 N  N     . ALA B 14  ? 1.63867 1.24542 0.98960 -0.22574 0.30374  0.03373  14  ALA B N     
1112 C  CA    . ALA B 14  ? 1.57366 1.17046 0.93640 -0.19181 0.26345  0.05656  14  ALA B CA    
1113 C  C     . ALA B 14  ? 1.69372 1.22690 0.98362 -0.17867 0.24862  0.08842  14  ALA B C     
1114 O  O     . ALA B 14  ? 1.71640 1.25274 1.01407 -0.15099 0.21117  0.10651  14  ALA B O     
1115 C  CB    . ALA B 14  ? 1.48115 1.14459 0.89990 -0.17230 0.23362  0.04224  14  ALA B CB    
1116 N  N     . GLN B 15  ? 1.78616 1.26370 1.00476 -0.19882 0.27685  0.09613  15  GLN B N     
1117 C  CA    . GLN B 15  ? 1.91905 1.33512 1.06032 -0.18570 0.26159  0.12776  15  GLN B CA    
1118 C  C     . GLN B 15  ? 1.94050 1.30377 1.06812 -0.16416 0.25013  0.16110  15  GLN B C     
1119 O  O     . GLN B 15  ? 1.98058 1.32920 1.08859 -0.13580 0.21472  0.18855  15  GLN B O     
1120 C  CB    . GLN B 15  ? 1.99001 1.35851 1.05291 -0.21416 0.29832  0.12633  15  GLN B CB    
1121 C  CG    . GLN B 15  ? 2.00895 1.42598 1.07877 -0.23195 0.31281  0.09515  15  GLN B CG    
1122 C  CD    . GLN B 15  ? 2.11836 1.52268 1.13233 -0.21976 0.28809  0.10388  15  GLN B CD    
1123 O  OE1   . GLN B 15  ? 2.22803 1.60947 1.21865 -0.19523 0.24954  0.13037  15  GLN B OE1   
1124 N  NE2   . GLN B 15  ? 2.23418 1.65499 1.22604 -0.23744 0.31073  0.08090  15  GLN B NE2   
1125 N  N     . ASP B 16  ? 1.90579 1.24045 1.04311 -0.17722 0.28020  0.15877  16  ASP B N     
1126 C  CA    . ASP B 16  ? 1.95661 1.23013 1.07470 -0.15577 0.27695  0.18978  16  ASP B CA    
1127 C  C     . ASP B 16  ? 1.94003 1.25659 1.12873 -0.12229 0.24232  0.19618  16  ASP B C     
1128 O  O     . ASP B 16  ? 1.99271 1.26981 1.16885 -0.09293 0.22865  0.22709  16  ASP B O     
1129 C  CB    . ASP B 16  ? 2.12459 1.34723 1.22621 -0.18408 0.32348  0.18162  16  ASP B CB    
1130 C  CG    . ASP B 16  ? 2.34853 1.55077 1.40907 -0.21760 0.35436  0.16632  16  ASP B CG    
1131 O  OD1   . ASP B 16  ? 2.40020 1.61190 1.42686 -0.21912 0.34611  0.16776  16  ASP B OD1   
1132 O  OD2   . ASP B 16  ? 2.43768 1.61676 1.50299 -0.24232 0.38535  0.15055  16  ASP B OD2   
1133 N  N     . LEU B 17  ? 1.83015 1.22555 1.09164 -0.12462 0.22954  0.16890  17  LEU B N     
1134 C  CA    . LEU B 17  ? 1.58441 1.02144 0.91298 -0.09680 0.20099  0.17282  17  LEU B CA    
1135 C  C     . LEU B 17  ? 1.67466 1.14046 1.00862 -0.06990 0.15608  0.19035  17  LEU B C     
1136 O  O     . LEU B 17  ? 1.67116 1.14670 0.97317 -0.07822 0.14582  0.18591  17  LEU B O     
1137 C  CB    . LEU B 17  ? 1.54740 1.05197 0.94565 -0.11093 0.20661  0.13776  17  LEU B CB    
1138 C  CG    . LEU B 17  ? 1.44191 0.93197 0.84196 -0.14205 0.24723  0.11631  17  LEU B CG    
1139 C  CD1   . LEU B 17  ? 1.42673 0.99074 0.89831 -0.15014 0.24507  0.08512  17  LEU B CD1   
1140 C  CD2   . LEU B 17  ? 1.40989 0.83037 0.78626 -0.13511 0.26385  0.13577  17  LEU B CD2   
1141 N  N     . PRO B 18  ? 1.63932 1.11989 1.01280 -0.03930 0.12991  0.20923  18  PRO B N     
1142 C  CA    . PRO B 18  ? 1.59642 1.10709 0.97648 -0.01688 0.08596  0.22710  18  PRO B CA    
1143 C  C     . PRO B 18  ? 1.58839 1.16771 1.01440 -0.02539 0.06657  0.20080  18  PRO B C     
1144 O  O     . PRO B 18  ? 1.47094 1.08177 0.93695 -0.03985 0.08315  0.17231  18  PRO B O     
1145 C  CB    . PRO B 18  ? 1.60068 1.11281 1.02063 0.01646  0.07118  0.25232  18  PRO B CB    
1146 C  CG    . PRO B 18  ? 1.64024 1.15274 1.10085 0.00855  0.10127  0.23320  18  PRO B CG    
1147 C  CD    . PRO B 18  ? 1.63568 1.10830 1.05040 -0.02510 0.14041  0.21394  18  PRO B CD    
1148 N  N     . LEU B 19  ? 1.55935 1.15965 0.97587 -0.01612 0.03019  0.21125  19  LEU B N     
1149 C  CA    . LEU B 19  ? 1.54364 1.19853 0.99589 -0.02333 0.01067  0.18846  19  LEU B CA    
1150 C  C     . LEU B 19  ? 1.42730 1.12883 0.96109 -0.01060 0.00187  0.18276  19  LEU B C     
1151 O  O     . LEU B 19  ? 1.46559 1.16462 1.02706 0.00980  -0.00300 0.20360  19  LEU B O     
1152 C  CB    . LEU B 19  ? 1.51296 1.17566 0.93389 -0.01885 -0.02803 0.20155  19  LEU B CB    
1153 C  CG    . LEU B 19  ? 1.70191 1.33620 1.04618 -0.03824 -0.02417 0.19279  19  LEU B CG    
1154 C  CD1   . LEU B 19  ? 1.65447 1.30601 1.00894 -0.05929 0.00111  0.15510  19  LEU B CD1   
1155 C  CD2   . LEU B 19  ? 1.85283 1.42365 1.12530 -0.03998 -0.00319 0.21291  19  LEU B CD2   
1156 N  N     . PRO B 20  ? 1.34682 1.08823 0.91758 -0.02063 0.00198  0.15542  20  PRO B N     
1157 C  CA    . PRO B 20  ? 1.36582 1.15037 1.00673 -0.00863 -0.01123 0.15240  20  PRO B CA    
1158 C  C     . PRO B 20  ? 1.38264 1.18880 1.03969 0.00595  -0.04978 0.17383  20  PRO B C     
1159 O  O     . PRO B 20  ? 1.34661 1.15748 0.97498 -0.00142 -0.07314 0.17350  20  PRO B O     
1160 C  CB    . PRO B 20  ? 1.22728 1.04100 0.88664 -0.02238 -0.00514 0.12065  20  PRO B CB    
1161 C  CG    . PRO B 20  ? 1.29866 1.09122 0.89850 -0.03820 0.00054  0.11021  20  PRO B CG    
1162 C  CD    . PRO B 20  ? 1.37977 1.12652 0.92976 -0.04134 0.01788  0.12657  20  PRO B CD    
1163 N  N     . SER B 21  ? 1.36337 1.18400 1.06623 0.02572  -0.05556 0.19189  21  SER B N     
1164 C  CA    . SER B 21  ? 1.27674 1.12747 1.00590 0.04107  -0.09066 0.21466  21  SER B CA    
1165 C  C     . SER B 21  ? 1.14476 1.03517 0.94829 0.05247  -0.09130 0.21415  21  SER B C     
1166 O  O     . SER B 21  ? 1.16429 1.04978 0.99049 0.05217  -0.06441 0.20069  21  SER B O     
1167 C  CB    . SER B 21  ? 1.29546 1.11853 0.99462 0.06103  -0.09798 0.24829  21  SER B CB    
1168 O  OG    . SER B 21  ? 1.28844 1.08156 0.99735 0.07618  -0.06837 0.25730  21  SER B OG    
1169 N  N     . TYR B 22  ? 1.12371 1.05567 0.96405 0.06061  -0.12242 0.22855  22  TYR B N     
1170 C  CA    . TYR B 22  ? 1.07561 1.04778 0.98704 0.07151  -0.12318 0.23153  22  TYR B CA    
1171 C  C     . TYR B 22  ? 1.15679 1.12593 1.09194 0.10123  -0.11625 0.25974  22  TYR B C     
1172 O  O     . TYR B 22  ? 1.26310 1.22853 1.17981 0.11627  -0.13403 0.28519  22  TYR B O     
1173 C  CB    . TYR B 22  ? 1.08184 1.10392 1.02570 0.06187  -0.15741 0.23159  22  TYR B CB    
1174 C  CG    . TYR B 22  ? 1.19493 1.21397 1.11736 0.03490  -0.16106 0.20279  22  TYR B CG    
1175 C  CD1   . TYR B 22  ? 1.12723 1.15248 1.07823 0.02779  -0.14380 0.18180  22  TYR B CD1   
1176 C  CD2   . TYR B 22  ? 1.10218 1.10823 0.97151 0.01846  -0.18084 0.19712  22  TYR B CD2   
1177 C  CE1   . TYR B 22  ? 1.09635 1.11405 1.02639 0.00805  -0.14543 0.15712  22  TYR B CE1   
1178 C  CE2   . TYR B 22  ? 1.16092 1.15795 1.00783 -0.00342 -0.18071 0.17013  22  TYR B CE2   
1179 C  CZ    . TYR B 22  ? 1.20110 1.20364 1.08002 -0.00703 -0.16266 0.15080  22  TYR B CZ    
1180 O  OH    . TYR B 22  ? 1.20073 1.18983 1.05616 -0.02408 -0.16097 0.12557  22  TYR B OH    
1181 N  N     . ALA B 23  ? 1.13316 1.10116 1.10544 0.11130  -0.08984 0.25550  23  ALA B N     
1182 C  CA    . ALA B 23  ? 1.19283 1.15152 1.18681 0.14172  -0.07724 0.27999  23  ALA B CA    
1183 C  C     . ALA B 23  ? 1.15319 1.16941 1.20178 0.16099  -0.10616 0.30464  23  ALA B C     
1184 O  O     . ALA B 23  ? 1.17388 1.18798 1.21975 0.18692  -0.11612 0.33347  23  ALA B O     
1185 C  CB    . ALA B 23  ? 1.07350 1.01743 1.09103 0.14479  -0.04183 0.26612  23  ALA B CB    
1186 N  N     . THR B 24  ? 1.15619 1.22529 1.25516 0.14877  -0.11960 0.29449  24  THR B N     
1187 C  CA    . THR B 24  ? 1.13182 1.26706 1.29152 0.15977  -0.14676 0.31380  24  THR B CA    
1188 C  C     . THR B 24  ? 1.08952 1.25978 1.24426 0.13093  -0.18313 0.30390  24  THR B C     
1189 O  O     . THR B 24  ? 1.09157 1.23743 1.20982 0.10404  -0.17987 0.27793  24  THR B O     
1190 C  CB    . THR B 24  ? 1.18529 1.35220 1.41194 0.16720  -0.12685 0.31050  24  THR B CB    
1191 O  OG1   . THR B 24  ? 1.09928 1.27369 1.33066 0.13732  -0.12449 0.28311  24  THR B OG1   
1192 C  CG2   . THR B 24  ? 1.04248 1.16170 1.26061 0.18876  -0.08585 0.31163  24  THR B CG2   
1193 N  N     . PRO B 25  ? 1.16632 1.39468 1.35705 0.13547  -0.21810 0.32335  25  PRO B N     
1194 C  CA    . PRO B 25  ? 1.17494 1.43356 1.35612 0.10355  -0.25380 0.31202  25  PRO B CA    
1195 C  C     . PRO B 25  ? 1.17609 1.44961 1.38458 0.07467  -0.24721 0.28565  25  PRO B C     
1196 O  O     . PRO B 25  ? 1.24386 1.53484 1.44206 0.04575  -0.27330 0.27365  25  PRO B O     
1197 C  CB    . PRO B 25  ? 1.24768 1.57661 1.47636 0.11752  -0.29070 0.34093  25  PRO B CB    
1198 C  CG    . PRO B 25  ? 1.23005 1.57840 1.51763 0.15509  -0.26780 0.36221  25  PRO B CG    
1199 C  CD    . PRO B 25  ? 1.20410 1.47306 1.44244 0.17051  -0.22777 0.35688  25  PRO B CD    
1200 N  N     . HIS B 26  ? 1.16226 1.42480 1.39977 0.08102  -0.21304 0.27635  26  HIS B N     
1201 C  CA    . HIS B 26  ? 1.09680 1.36124 1.34929 0.05637  -0.20332 0.25252  26  HIS B CA    
1202 C  C     . HIS B 26  ? 1.08448 1.29460 1.30563 0.05844  -0.16716 0.23310  26  HIS B C     
1203 O  O     . HIS B 26  ? 1.09368 1.30454 1.33739 0.05161  -0.14959 0.22044  26  HIS B O     
1204 C  CB    . HIS B 26  ? 1.07266 1.39486 1.40378 0.05821  -0.20205 0.26188  26  HIS B CB    
1205 C  CG    . HIS B 26  ? 1.12406 1.50750 1.48944 0.03981  -0.23991 0.27003  26  HIS B CG    
1206 N  ND1   . HIS B 26  ? 1.24014 1.61935 1.56090 0.01754  -0.27293 0.26367  26  HIS B ND1   
1207 C  CD2   . HIS B 26  ? 1.17999 1.63314 1.61998 0.03808  -0.24982 0.28304  26  HIS B CD2   
1208 C  CE1   . HIS B 26  ? 1.28563 1.72931 1.65059 0.00121  -0.30409 0.27183  26  HIS B CE1   
1209 N  NE2   . HIS B 26  ? 1.23909 1.73193 1.68028 0.01302  -0.29072 0.28396  26  HIS B NE2   
1210 N  N     . SER B 27  ? 1.11661 1.28078 1.28449 0.06633  -0.15626 0.23076  27  SER B N     
1211 C  CA    . SER B 27  ? 1.09396 1.21413 1.23286 0.06501  -0.12486 0.21105  27  SER B CA    
1212 C  C     . SER B 27  ? 1.06677 1.17220 1.17549 0.04030  -0.12863 0.18495  27  SER B C     
1213 O  O     . SER B 27  ? 1.03646 1.14264 1.11832 0.02453  -0.15195 0.18059  27  SER B O     
1214 C  CB    . SER B 27  ? 1.05743 1.13504 1.15000 0.07688  -0.11095 0.21629  27  SER B CB    
1215 O  OG    . SER B 27  ? 1.21376 1.25826 1.28856 0.07515  -0.07975 0.19839  27  SER B OG    
1216 N  N     . SER B 28  ? 1.03417 1.12461 1.14497 0.03835  -0.10529 0.16762  28  SER B N     
1217 C  CA    . SER B 28  ? 1.02103 1.09809 1.10879 0.02082  -0.10661 0.14461  28  SER B CA    
1218 C  C     . SER B 28  ? 0.96329 1.00731 0.99605 0.01584  -0.09955 0.12930  28  SER B C     
1219 O  O     . SER B 28  ? 0.90824 0.94073 0.91257 0.00210  -0.10794 0.11399  28  SER B O     
1220 C  CB    . SER B 28  ? 0.98717 1.06404 1.09803 0.02345  -0.08674 0.13436  28  SER B CB    
1221 O  OG    . SER B 28  ? 1.03370 1.13893 1.18982 0.02075  -0.09337 0.14408  28  SER B OG    
1222 N  N     . GLY B 29  ? 0.99531 1.02167 1.01124 0.02557  -0.08179 0.13220  29  GLY B N     
1223 C  CA    . GLY B 29  ? 1.02309 1.02277 0.99254 0.01865  -0.06972 0.11632  29  GLY B CA    
1224 C  C     . GLY B 29  ? 1.05339 1.03144 0.99306 0.02328  -0.06367 0.12901  29  GLY B C     
1225 O  O     . GLY B 29  ? 1.00867 0.98806 0.96492 0.03678  -0.06428 0.14997  29  GLY B O     
1226 N  N     . LEU B 30  ? 1.07661 1.03204 0.97011 0.01287  -0.05545 0.11629  30  LEU B N     
1227 C  CA    . LEU B 30  ? 1.14151 1.06699 0.99567 0.01311  -0.04433 0.12543  30  LEU B CA    
1228 C  C     . LEU B 30  ? 1.09800 1.00979 0.95249 0.01169  -0.01244 0.11434  30  LEU B C     
1229 O  O     . LEU B 30  ? 1.09472 1.02025 0.96137 0.00524  -0.00051 0.09278  30  LEU B O     
1230 C  CB    . LEU B 30  ? 1.21017 1.11743 1.01011 -0.00081 -0.04964 0.11694  30  LEU B CB    
1231 C  CG    . LEU B 30  ? 1.14484 1.06163 0.93227 -0.00614 -0.08159 0.12146  30  LEU B CG    
1232 C  CD1   . LEU B 30  ? 1.15113 1.04804 0.88544 -0.02177 -0.07839 0.10250  30  LEU B CD1   
1233 C  CD2   . LEU B 30  ? 1.16498 1.07950 0.94327 0.00323  -0.10276 0.15068  30  LEU B CD2   
1234 N  N     . ASP B 31  ? 1.07116 0.95477 0.91011 0.01753  0.00087  0.12922  31  ASP B N     
1235 C  CA    . ASP B 31  ? 1.20263 1.06826 1.03753 0.01159  0.03157  0.11814  31  ASP B CA    
1236 C  C     . ASP B 31  ? 1.15886 1.01110 0.95440 -0.00897 0.04890  0.09944  31  ASP B C     
1237 O  O     . ASP B 31  ? 1.05779 0.89287 0.81282 -0.01522 0.04359  0.10391  31  ASP B O     
1238 C  CB    . ASP B 31  ? 1.29916 1.12890 1.12494 0.02418  0.04344  0.13984  31  ASP B CB    
1239 C  CG    . ASP B 31  ? 1.39760 1.20759 1.19541 0.03575  0.02573  0.16674  31  ASP B CG    
1240 O  OD1   . ASP B 31  ? 1.34649 1.13680 1.09701 0.02373  0.02450  0.16545  31  ASP B OD1   
1241 O  OD2   . ASP B 31  ? 1.42362 1.23972 1.24645 0.05778  0.01331  0.18973  31  ASP B OD2   
1242 N  N     . LEU B 32  ? 1.11395 0.97750 0.92198 -0.02019 0.06991  0.07806  32  LEU B N     
1243 C  CA    . LEU B 32  ? 1.05891 0.92107 0.84152 -0.04110 0.09044  0.05807  32  LEU B CA    
1244 C  C     . LEU B 32  ? 1.16615 0.99862 0.93349 -0.05428 0.11876  0.05592  32  LEU B C     
1245 O  O     . LEU B 32  ? 1.13166 0.96377 0.92224 -0.05012 0.12529  0.05528  32  LEU B O     
1246 C  CB    . LEU B 32  ? 1.06103 0.97027 0.87404 -0.04480 0.09008  0.03289  32  LEU B CB    
1247 C  CG    . LEU B 32  ? 1.13560 1.06188 0.93986 -0.04366 0.07770  0.02387  32  LEU B CG    
1248 C  CD1   . LEU B 32  ? 1.01332 0.92275 0.80356 -0.03313 0.05195  0.04330  32  LEU B CD1   
1249 C  CD2   . LEU B 32  ? 0.97759 0.94588 0.81974 -0.03649 0.07312  0.00595  32  LEU B CD2   
1250 N  N     . ARG B 33  ? 1.10179 0.90525 0.82582 -0.07224 0.13750  0.05390  33  ARG B N     
1251 C  CA    . ARG B 33  ? 1.18918 0.95266 0.88858 -0.08936 0.16683  0.05274  33  ARG B CA    
1252 C  C     . ARG B 33  ? 1.15223 0.94040 0.85153 -0.11943 0.19064  0.02430  33  ARG B C     
1253 O  O     . ARG B 33  ? 1.14082 0.96710 0.84681 -0.12480 0.18753  0.00990  33  ARG B O     
1254 C  CB    . ARG B 33  ? 1.28489 0.98423 0.92825 -0.08712 0.17314  0.07775  33  ARG B CB    
1255 C  CG    . ARG B 33  ? 1.31818 0.99036 0.96521 -0.05735 0.15646  0.10737  33  ARG B CG    
1256 C  CD    . ARG B 33  ? 1.42501 1.03202 1.01324 -0.05186 0.16272  0.13416  33  ARG B CD    
1257 N  NE    . ARG B 33  ? 1.48877 1.06533 1.08341 -0.02309 0.15688  0.16096  33  ARG B NE    
1258 C  CZ    . ARG B 33  ? 1.55084 1.14689 1.16595 0.00606  0.12578  0.18379  33  ARG B CZ    
1259 N  NH1   . ARG B 33  ? 1.50210 1.14166 1.12768 0.00755  0.09643  0.18263  33  ARG B NH1   
1260 N  NH2   . ARG B 33  ? 1.59385 1.16591 1.21973 0.03376  0.12509  0.20753  33  ARG B NH2   
1261 N  N     . ALA B 34  ? 1.16550 0.93188 0.85754 -0.13948 0.21573  0.01569  34  ALA B N     
1262 C  CA    . ALA B 34  ? 1.11546 0.90991 0.81197 -0.17287 0.23965  -0.01189 34  ALA B CA    
1263 C  C     . ALA B 34  ? 1.22680 0.97793 0.86998 -0.19548 0.26423  -0.00798 34  ALA B C     
1264 O  O     . ALA B 34  ? 1.30855 0.99459 0.91079 -0.20838 0.28542  0.00229  34  ALA B O     
1265 C  CB    . ALA B 34  ? 1.02416 0.81429 0.73390 -0.18907 0.25436  -0.02502 34  ALA B CB    
1266 N  N     . ALA B 35  ? 1.14982 0.93187 0.78915 -0.20002 0.26397  -0.01611 35  ALA B N     
1267 C  CA    . ALA B 35  ? 1.29744 1.04225 0.88370 -0.22268 0.28937  -0.01375 35  ALA B CA    
1268 C  C     . ALA B 35  ? 1.25565 1.01957 0.84818 -0.26402 0.32414  -0.03920 35  ALA B C     
1269 O  O     . ALA B 35  ? 1.20335 1.00756 0.80184 -0.28278 0.34010  -0.05713 35  ALA B O     
1270 C  CB    . ALA B 35  ? 1.17912 0.94824 0.75613 -0.21188 0.27807  -0.01445 35  ALA B CB    
1271 N  N     . ILE B 36  ? 1.23840 0.97301 0.82959 -0.27934 0.33713  -0.04144 36  ILE B N     
1272 C  CA    . ILE B 36  ? 1.23080 0.98505 0.83119 -0.32289 0.36735  -0.06735 36  ILE B CA    
1273 C  C     . ILE B 36  ? 1.39425 1.05806 0.92672 -0.35135 0.40184  -0.05656 36  ILE B C     
1274 O  O     . ILE B 36  ? 1.43451 1.01697 0.91787 -0.33202 0.39969  -0.02777 36  ILE B O     
1275 C  CB    . ILE B 36  ? 1.23044 1.01919 0.87553 -0.32633 0.35852  -0.08356 36  ILE B CB    
1276 C  CG1   . ILE B 36  ? 1.25400 0.96686 0.87213 -0.30720 0.35308  -0.06196 36  ILE B CG1   
1277 C  CG2   . ILE B 36  ? 1.23817 1.11681 0.94683 -0.30082 0.32773  -0.09495 36  ILE B CG2   
1278 C  CD1   . ILE B 36  ? 1.37859 1.10889 1.02564 -0.31487 0.35054  -0.07819 36  ILE B CD1   
1279 N  N     . GLU B 37  ? 1.44077 1.12088 0.97206 -0.39734 0.43375  -0.07973 37  GLU B N     
1280 C  CA    . GLU B 37  ? 1.55453 1.15330 1.03279 -0.41884 0.45595  -0.07538 37  GLU B CA    
1281 C  C     . GLU B 37  ? 1.62928 1.16997 1.09290 -0.42697 0.46272  -0.07635 37  GLU B C     
1282 O  O     . GLU B 37  ? 1.71355 1.16556 1.12897 -0.40595 0.46400  -0.04996 37  GLU B O     
1283 C  CB    . GLU B 37  ? 1.47985 1.12560 0.97631 -0.45579 0.47411  -0.10325 37  GLU B CB    
1284 C  CG    . GLU B 37  ? 1.54101 1.26680 1.07077 -0.44707 0.46776  -0.11067 37  GLU B CG    
1285 C  CD    . GLU B 37  ? 1.62572 1.43175 1.20361 -0.47957 0.48042  -0.14357 37  GLU B CD    
1286 O  OE1   . GLU B 37  ? 1.53832 1.34055 1.12254 -0.51245 0.49237  -0.16173 37  GLU B OE1   
1287 O  OE2   . GLU B 37  ? 1.43557 1.30805 1.04355 -0.47150 0.47869  -0.15162 37  GLU B OE2   
1288 N  N     . LYS B 38  ? 1.63569 1.22632 1.13929 -0.45561 0.46647  -0.10693 38  LYS B N     
1289 C  CA    . LYS B 38  ? 1.69341 1.23655 1.18383 -0.46724 0.47352  -0.11451 38  LYS B CA    
1290 C  C     . LYS B 38  ? 1.59974 1.18315 1.12983 -0.44635 0.45335  -0.11379 38  LYS B C     
1291 O  O     . LYS B 38  ? 1.41637 1.08483 0.99521 -0.43256 0.43492  -0.11729 38  LYS B O     
1292 C  CB    . LYS B 38  ? 1.60692 1.17905 1.10941 -0.51639 0.48974  -0.15085 38  LYS B CB    
1293 N  N     . PRO B 39  ? 1.59758 1.11865 1.10548 -0.44107 0.45764  -0.10936 39  PRO B N     
1294 C  CA    . PRO B 39  ? 1.66578 1.22315 1.21108 -0.41805 0.43658  -0.10956 39  PRO B CA    
1295 C  C     . PRO B 39  ? 1.58100 1.24878 1.18732 -0.44001 0.42252  -0.14315 39  PRO B C     
1296 O  O     . PRO B 39  ? 1.60402 1.30488 1.21696 -0.48553 0.43843  -0.16993 39  PRO B O     
1297 C  CB    . PRO B 39  ? 1.59610 1.05659 1.09659 -0.42092 0.45538  -0.10494 39  PRO B CB    
1298 C  CG    . PRO B 39  ? 1.61330 0.98001 1.05374 -0.41592 0.47307  -0.08697 39  PRO B CG    
1299 C  CD    . PRO B 39  ? 1.67128 1.08081 1.11657 -0.44560 0.47914  -0.10167 39  PRO B CD    
1300 N  N     . LEU B 40  ? 1.45898 1.18631 1.11195 -0.40300 0.38825  -0.14092 40  LEU B N     
1301 C  CA    . LEU B 40  ? 1.45396 1.29016 1.16631 -0.41102 0.36812  -0.16664 40  LEU B CA    
1302 C  C     . LEU B 40  ? 1.48980 1.32527 1.20771 -0.41275 0.35932  -0.17890 40  LEU B C     
1303 O  O     . LEU B 40  ? 1.41711 1.19463 1.11594 -0.38238 0.35399  -0.16076 40  LEU B O     
1304 C  CB    . LEU B 40  ? 1.41366 1.31668 1.16995 -0.36758 0.33661  -0.15508 40  LEU B CB    
1305 C  CG    . LEU B 40  ? 1.36146 1.37992 1.17718 -0.37247 0.32034  -0.17778 40  LEU B CG    
1306 C  CD1   . LEU B 40  ? 1.35889 1.41456 1.17989 -0.42513 0.34570  -0.20399 40  LEU B CD1   
1307 C  CD2   . LEU B 40  ? 1.13306 1.18590 0.97046 -0.33568 0.30290  -0.16372 40  LEU B CD2   
1308 N  N     . LYS B 41  ? 1.70984 1.61278 1.45387 -0.44852 0.35799  -0.20990 41  LYS B N     
1309 C  CA    . LYS B 41  ? 1.63972 1.54728 1.38348 -0.45744 0.34966  -0.22605 41  LYS B CA    
1310 C  C     . LYS B 41  ? 1.53804 1.55457 1.34087 -0.43538 0.31347  -0.23483 41  LYS B C     
1311 O  O     . LYS B 41  ? 1.49467 1.60299 1.33885 -0.45314 0.30604  -0.25274 41  LYS B O     
1312 C  CB    . LYS B 41  ? 1.59231 1.48496 1.31034 -0.52103 0.37572  -0.25607 41  LYS B CB    
1313 N  N     . ILE B 42  ? 1.30614 1.31217 1.11271 -0.39577 0.29267  -0.22135 42  ILE B N     
1314 C  CA    . ILE B 42  ? 1.30483 1.39849 1.15853 -0.36842 0.25867  -0.22433 42  ILE B CA    
1315 C  C     . ILE B 42  ? 1.41099 1.50915 1.25276 -0.38256 0.25135  -0.24157 42  ILE B C     
1316 O  O     . ILE B 42  ? 1.34928 1.37781 1.15837 -0.36749 0.25637  -0.23124 42  ILE B O     
1317 C  CB    . ILE B 42  ? 1.23633 1.31788 1.10300 -0.31278 0.24001  -0.19482 42  ILE B CB    
1318 C  CG1   . ILE B 42  ? 1.06220 1.12457 0.92737 -0.30209 0.24863  -0.17789 42  ILE B CG1   
1319 C  CG2   . ILE B 42  ? 1.13180 1.29968 1.04346 -0.28625 0.20785  -0.19788 42  ILE B CG2   
1320 C  CD1   . ILE B 42  ? 1.03185 1.08406 0.90850 -0.25315 0.22931  -0.15101 42  ILE B CD1   
1321 N  N     . LYS B 43  ? 1.34910 1.53179 1.21709 -0.41119 0.23958  -0.26802 43  LYS B N     
1322 C  CA    . LYS B 43  ? 1.28193 1.48162 1.13816 -0.42532 0.22709  -0.28594 43  LYS B CA    
1323 C  C     . LYS B 43  ? 1.28885 1.51325 1.16253 -0.37402 0.19740  -0.26895 43  LYS B C     
1324 O  O     . LYS B 43  ? 1.31006 1.55681 1.21394 -0.33379 0.18441  -0.24843 43  LYS B O     
1325 C  CB    . LYS B 43  ? 1.33214 1.62838 1.21721 -0.46915 0.21833  -0.31755 43  LYS B CB    
1326 N  N     . PRO B 44  ? 1.23522 1.45055 1.08538 -0.37566 0.18778  -0.27718 44  PRO B N     
1327 C  CA    . PRO B 44  ? 1.30282 1.54429 1.16743 -0.32958 0.16060  -0.26129 44  PRO B CA    
1328 C  C     . PRO B 44  ? 1.25320 1.60756 1.16970 -0.31547 0.12933  -0.26583 44  PRO B C     
1329 O  O     . PRO B 44  ? 1.21060 1.63705 1.14842 -0.34798 0.12335  -0.28887 44  PRO B O     
1330 C  CB    . PRO B 44  ? 1.36727 1.57208 1.18619 -0.34426 0.16186  -0.27388 44  PRO B CB    
1331 C  CG    . PRO B 44  ? 1.41331 1.53488 1.18630 -0.38431 0.19683  -0.28659 44  PRO B CG    
1332 C  CD    . PRO B 44  ? 1.36328 1.51918 1.16061 -0.41600 0.20680  -0.29741 44  PRO B CD    
1333 N  N     . PHE B 45  ? 1.20504 1.57339 1.14285 -0.26595 0.11078  -0.24298 45  PHE B N     
1334 C  CA    . PHE B 45  ? 1.22690 1.68492 1.20477 -0.23792 0.07969  -0.24089 45  PHE B CA    
1335 C  C     . PHE B 45  ? 1.24979 1.77828 1.27707 -0.23484 0.07671  -0.24421 45  PHE B C     
1336 O  O     . PHE B 45  ? 1.26967 1.88353 1.33251 -0.21755 0.05281  -0.24801 45  PHE B O     
1337 C  CB    . PHE B 45  ? 1.17236 1.68993 1.14455 -0.25480 0.05818  -0.26047 45  PHE B CB    
1338 C  CG    . PHE B 45  ? 1.23891 1.69787 1.16152 -0.25010 0.05674  -0.25661 45  PHE B CG    
1339 C  CD1   . PHE B 45  ? 1.20531 1.57686 1.10280 -0.22483 0.07196  -0.23436 45  PHE B CD1   
1340 C  CD2   . PHE B 45  ? 1.26858 1.76329 1.16980 -0.27144 0.04033  -0.27562 45  PHE B CD2   
1341 C  CE1   . PHE B 45  ? 1.31697 1.63616 1.17022 -0.22022 0.07482  -0.23130 45  PHE B CE1   
1342 C  CE2   . PHE B 45  ? 1.37910 1.81620 1.22848 -0.26785 0.04169  -0.27311 45  PHE B CE2   
1343 C  CZ    . PHE B 45  ? 1.42115 1.76923 1.24712 -0.24157 0.06096  -0.25085 45  PHE B CZ    
1344 N  N     . GLU B 46  ? 1.55418 2.05017 1.58331 -0.24821 0.10060  -0.24199 46  GLU B N     
1345 C  CA    . GLU B 46  ? 1.49856 2.05450 1.57032 -0.24223 0.10158  -0.24391 46  GLU B CA    
1346 C  C     . GLU B 46  ? 1.48438 1.97448 1.54545 -0.22323 0.11770  -0.22321 46  GLU B C     
1347 O  O     . GLU B 46  ? 1.51257 1.91612 1.53622 -0.22524 0.13181  -0.21081 46  GLU B O     
1348 C  CB    . GLU B 46  ? 1.51758 2.12686 1.60630 -0.29231 0.11575  -0.27065 46  GLU B CB    
1349 C  CG    . GLU B 46  ? 1.57653 2.11775 1.63865 -0.32492 0.15059  -0.27162 46  GLU B CG    
1350 C  CD    . GLU B 46  ? 1.67774 2.12398 1.68364 -0.35000 0.16737  -0.27234 46  GLU B CD    
1351 O  OE1   . GLU B 46  ? 1.66669 2.11866 1.65773 -0.35979 0.15532  -0.28302 46  GLU B OE1   
1352 O  OE2   . GLU B 46  ? 1.69823 2.06232 1.67186 -0.35828 0.19296  -0.26189 46  GLU B OE2   
1353 N  N     . ARG B 47  ? 1.18737 1.72154 1.28121 -0.20410 0.11541  -0.21999 47  ARG B N     
1354 C  CA    . ARG B 47  ? 1.04441 1.52852 1.12934 -0.18267 0.12507  -0.20134 47  ARG B CA    
1355 C  C     . ARG B 47  ? 0.99487 1.46893 1.07419 -0.21450 0.15250  -0.20936 47  ARG B C     
1356 O  O     . ARG B 47  ? 0.94853 1.47344 1.04427 -0.24962 0.16340  -0.23065 47  ARG B O     
1357 C  CB    . ARG B 47  ? 0.92636 1.45459 1.04192 -0.13944 0.10700  -0.19295 47  ARG B CB    
1358 C  CG    . ARG B 47  ? 0.89260 1.52177 1.05431 -0.14153 0.10330  -0.21123 47  ARG B CG    
1359 C  CD    . ARG B 47  ? 0.84727 1.52374 1.03539 -0.09547 0.07800  -0.20425 47  ARG B CD    
1360 N  NE    . ARG B 47  ? 0.75140 1.52455 0.98791 -0.08864 0.07629  -0.21851 47  ARG B NE    
1361 C  CZ    . ARG B 47  ? 0.71706 1.57768 0.98651 -0.09696 0.06233  -0.23367 47  ARG B CZ    
1362 N  NH1   . ARG B 47  ? 0.70622 1.56624 0.95938 -0.11537 0.04858  -0.23835 47  ARG B NH1   
1363 N  NH2   . ARG B 47  ? 0.73599 1.68918 1.05574 -0.08606 0.06207  -0.24472 47  ARG B NH2   
1364 N  N     . VAL B 48  ? 1.02175 1.43080 1.07650 -0.20297 0.16330  -0.19167 48  VAL B N     
1365 C  CA    . VAL B 48  ? 0.97627 1.35974 1.01380 -0.22924 0.19019  -0.19419 48  VAL B CA    
1366 C  C     . VAL B 48  ? 0.89907 1.25291 0.92748 -0.19942 0.18869  -0.17612 48  VAL B C     
1367 O  O     . VAL B 48  ? 0.75812 1.06648 0.77216 -0.17057 0.17428  -0.15651 48  VAL B O     
1368 C  CB    . VAL B 48  ? 0.97742 1.28057 0.96902 -0.26070 0.21089  -0.19131 48  VAL B CB    
1369 C  CG1   . VAL B 48  ? 0.98212 1.22315 0.93941 -0.26698 0.23217  -0.17807 48  VAL B CG1   
1370 C  CG2   . VAL B 48  ? 0.97574 1.31228 0.97212 -0.30765 0.22432  -0.21724 48  VAL B CG2   
1371 N  N     . LEU B 49  ? 0.91704 1.29828 0.95313 -0.20852 0.20444  -0.18388 49  LEU B N     
1372 C  CA    . LEU B 49  ? 0.99272 1.34646 1.01384 -0.18518 0.20540  -0.17061 49  LEU B CA    
1373 C  C     . LEU B 49  ? 0.99996 1.27627 0.97048 -0.20680 0.22678  -0.15928 49  LEU B C     
1374 O  O     . LEU B 49  ? 1.02614 1.30654 0.98671 -0.24038 0.25295  -0.17043 49  LEU B O     
1375 C  CB    . LEU B 49  ? 0.96019 1.38686 1.01539 -0.17855 0.21220  -0.18572 49  LEU B CB    
1376 C  CG    . LEU B 49  ? 1.00953 1.41257 1.04887 -0.15135 0.21203  -0.17594 49  LEU B CG    
1377 C  CD1   . LEU B 49  ? 1.01706 1.39705 1.05615 -0.11213 0.18341  -0.16072 49  LEU B CD1   
1378 C  CD2   . LEU B 49  ? 0.89876 1.37392 0.97148 -0.14683 0.22590  -0.19359 49  LEU B CD2   
1379 N  N     . ILE B 50  ? 0.98739 1.19474 0.92611 -0.18793 0.21599  -0.13641 50  ILE B N     
1380 C  CA    . ILE B 50  ? 1.06431 1.19370 0.95191 -0.20139 0.23164  -0.12064 50  ILE B CA    
1381 C  C     . ILE B 50  ? 0.96590 1.07622 0.83138 -0.18450 0.22887  -0.10946 50  ILE B C     
1382 O  O     . ILE B 50  ? 0.89679 1.01270 0.77304 -0.15368 0.20561  -0.10103 50  ILE B O     
1383 C  CB    . ILE B 50  ? 0.98232 1.05027 0.84984 -0.19077 0.22176  -0.10133 50  ILE B CB    
1384 C  CG1   . ILE B 50  ? 0.94850 1.02707 0.82850 -0.21013 0.22751  -0.11475 50  ILE B CG1   
1385 C  CG2   . ILE B 50  ? 0.97665 0.96568 0.79151 -0.19818 0.23611  -0.08199 50  ILE B CG2   
1386 C  CD1   . ILE B 50  ? 0.92542 0.93722 0.78103 -0.20204 0.22618  -0.09769 50  ILE B CD1   
1387 N  N     . PRO B 51  ? 0.95687 1.04184 0.78756 -0.20549 0.25258  -0.10978 51  PRO B N     
1388 C  CA    . PRO B 51  ? 0.96210 1.02239 0.76179 -0.19105 0.24974  -0.09936 51  PRO B CA    
1389 C  C     . PRO B 51  ? 0.95046 0.93326 0.70326 -0.18005 0.23819  -0.07116 51  PRO B C     
1390 O  O     . PRO B 51  ? 1.00888 0.94312 0.73707 -0.19230 0.24743  -0.05968 51  PRO B O     
1391 C  CB    . PRO B 51  ? 1.04339 1.11282 0.82448 -0.22123 0.28362  -0.11297 51  PRO B CB    
1392 C  CG    . PRO B 51  ? 1.05091 1.10342 0.82581 -0.25497 0.30425  -0.11749 51  PRO B CG    
1393 C  CD    . PRO B 51  ? 1.06467 1.14814 0.88278 -0.24647 0.28495  -0.12291 51  PRO B CD    
1394 N  N     . THR B 52  ? 0.93413 0.90614 0.67494 -0.15580 0.21721  -0.06008 52  THR B N     
1395 C  CA    . THR B 52  ? 0.88082 0.79244 0.58283 -0.14287 0.20081  -0.03283 52  THR B CA    
1396 C  C     . THR B 52  ? 1.22124 1.08857 0.86187 -0.15274 0.21215  -0.02345 52  THR B C     
1397 O  O     . THR B 52  ? 1.27179 1.08419 0.87233 -0.14755 0.20424  0.00095  52  THR B O     
1398 C  CB    . THR B 52  ? 0.96806 0.89296 0.69180 -0.11371 0.16721  -0.02497 52  THR B CB    
1399 O  OG1   . THR B 52  ? 0.90395 0.84569 0.61815 -0.10834 0.16388  -0.03551 52  THR B OG1   
1400 C  CG2   . THR B 52  ? 1.07339 1.04110 0.85290 -0.10283 0.15698  -0.03410 52  THR B CG2   
1401 N  N     . GLY B 53  ? 1.11738 1.00766 0.74852 -0.16498 0.23083  -0.04127 53  GLY B N     
1402 C  CA    . GLY B 53  ? 1.23966 1.08694 0.80660 -0.17472 0.24311  -0.03373 53  GLY B CA    
1403 C  C     . GLY B 53  ? 1.28846 1.11767 0.82695 -0.15430 0.21586  -0.02322 53  GLY B C     
1404 O  O     . GLY B 53  ? 1.28663 1.07024 0.76161 -0.16047 0.21968  -0.01176 53  GLY B O     
1405 N  N     . LEU B 54  ? 1.07867 0.93947 0.65771 -0.13236 0.18878  -0.02704 54  LEU B N     
1406 C  CA    . LEU B 54  ? 1.17984 1.02392 0.73464 -0.11670 0.16083  -0.01897 54  LEU B CA    
1407 C  C     . LEU B 54  ? 1.17594 1.05261 0.74332 -0.11017 0.16497  -0.04310 54  LEU B C     
1408 O  O     . LEU B 54  ? 1.11302 1.03808 0.73346 -0.10394 0.17268  -0.06061 54  LEU B O     
1409 C  CB    . LEU B 54  ? 1.19641 1.04247 0.78320 -0.09774 0.12676  -0.00228 54  LEU B CB    
1410 C  CG    . LEU B 54  ? 1.20875 1.02482 0.79130 -0.09622 0.12112  0.02287  54  LEU B CG    
1411 C  CD1   . LEU B 54  ? 1.29625 1.11951 0.90938 -0.07586 0.08706  0.03900  54  LEU B CD1   
1412 C  CD2   . LEU B 54  ? 1.31220 1.07432 0.82541 -0.10590 0.12825  0.04079  54  LEU B CD2   
1413 N  N     . ILE B 55  ? 1.21141 1.05893 0.72620 -0.11039 0.15985  -0.04361 55  ILE B N     
1414 C  CA    . ILE B 55  ? 1.18042 1.04325 0.69559 -0.10087 0.16163  -0.06465 55  ILE B CA    
1415 C  C     . ILE B 55  ? 1.22127 1.05212 0.70571 -0.09281 0.12695  -0.05442 55  ILE B C     
1416 O  O     . ILE B 55  ? 1.35478 1.14388 0.77869 -0.10212 0.11703  -0.04072 55  ILE B O     
1417 C  CB    . ILE B 55  ? 1.24538 1.10161 0.71879 -0.11366 0.19669  -0.08143 55  ILE B CB    
1418 N  N     . LEU B 56  ? 1.16678 1.01684 0.69050 -0.07709 0.10814  -0.06063 56  LEU B N     
1419 C  CA    . LEU B 56  ? 1.21533 1.04280 0.72426 -0.07309 0.07268  -0.04998 56  LEU B CA    
1420 C  C     . LEU B 56  ? 1.29014 1.10196 0.77260 -0.06915 0.07197  -0.07008 56  LEU B C     
1421 O  O     . LEU B 56  ? 1.26617 1.09517 0.76503 -0.05958 0.09560  -0.09122 56  LEU B O     
1422 C  CB    . LEU B 56  ? 1.26256 1.11569 0.83376 -0.06125 0.05139  -0.03878 56  LEU B CB    
1423 C  CG    . LEU B 56  ? 1.22090 1.09248 0.82795 -0.06151 0.05902  -0.02516 56  LEU B CG    
1424 C  CD1   . LEU B 56  ? 1.16953 1.06800 0.83691 -0.04829 0.04392  -0.01991 56  LEU B CD1   
1425 C  CD2   . LEU B 56  ? 1.28817 1.12855 0.85742 -0.07008 0.04962  -0.00105 56  LEU B CD2   
1426 N  N     . GLU B 57  ? 1.46521 1.24430 0.90605 -0.07632 0.04442  -0.06341 57  GLU B N     
1427 C  CA    . GLU B 57  ? 1.45915 1.21422 0.87292 -0.07528 0.03789  -0.08138 57  GLU B CA    
1428 C  C     . GLU B 57  ? 1.45586 1.21572 0.90232 -0.07346 0.00324  -0.07096 57  GLU B C     
1429 O  O     . GLU B 57  ? 1.44544 1.19245 0.86919 -0.08595 -0.02697 -0.05585 57  GLU B O     
1430 C  CB    . GLU B 57  ? 1.52083 1.22994 0.84807 -0.09180 0.03669  -0.08677 57  GLU B CB    
1431 C  CG    . GLU B 57  ? 1.74846 1.42276 1.03886 -0.09558 0.02507  -0.10473 57  GLU B CG    
1432 C  CD    . GLU B 57  ? 1.91145 1.53782 1.11011 -0.11070 0.03444  -0.11776 57  GLU B CD    
1433 O  OE1   . GLU B 57  ? 1.89467 1.51672 1.06051 -0.11580 0.05608  -0.11475 57  GLU B OE1   
1434 O  OE2   . GLU B 57  ? 1.91321 1.50231 1.06837 -0.11942 0.02162  -0.13180 57  GLU B OE2   
1435 N  N     . ILE B 58  ? 1.37988 1.16118 0.88030 -0.05800 0.00784  -0.07815 58  ILE B N     
1436 C  CA    . ILE B 58  ? 1.37340 1.15788 0.90603 -0.05727 -0.01942 -0.06992 58  ILE B CA    
1437 C  C     . ILE B 58  ? 1.46439 1.20735 0.95447 -0.06445 -0.02635 -0.08738 58  ILE B C     
1438 O  O     . ILE B 58  ? 1.45081 1.17587 0.92405 -0.05353 -0.00209 -0.10874 58  ILE B O     
1439 C  CB    . ILE B 58  ? 1.29922 1.11829 0.90002 -0.03830 -0.01062 -0.06851 58  ILE B CB    
1440 C  CG1   . ILE B 58  ? 1.28277 1.13652 0.91990 -0.03564 -0.00513 -0.05233 58  ILE B CG1   
1441 C  CG2   . ILE B 58  ? 1.29209 1.10820 0.92010 -0.03872 -0.03366 -0.06186 58  ILE B CG2   
1442 C  CD1   . ILE B 58  ? 1.15165 1.03963 0.84964 -0.01956 0.00246  -0.05138 58  ILE B CD1   
1443 N  N     . PRO B 59  ? 1.49658 1.22339 0.96761 -0.08287 -0.05773 -0.07983 59  PRO B N     
1444 C  CA    . PRO B 59  ? 1.57756 1.25702 0.99700 -0.09624 -0.06402 -0.09889 59  PRO B CA    
1445 C  C     . PRO B 59  ? 1.58221 1.24831 1.02902 -0.08338 -0.05396 -0.11143 59  PRO B C     
1446 O  O     . PRO B 59  ? 1.37796 1.07560 0.88626 -0.06658 -0.04978 -0.10210 59  PRO B O     
1447 C  CB    . PRO B 59  ? 1.55554 1.23668 0.96250 -0.12153 -0.10433 -0.08417 59  PRO B CB    
1448 C  CG    . PRO B 59  ? 1.50822 1.24128 0.98559 -0.11284 -0.11717 -0.05766 59  PRO B CG    
1449 C  CD    . PRO B 59  ? 1.38736 1.14036 0.88386 -0.09275 -0.08870 -0.05398 59  PRO B CD    
1450 N  N     . GLU B 60  ? 1.61382 1.22619 1.00708 -0.09155 -0.04918 -0.13294 60  GLU B N     
1451 C  CA    . GLU B 60  ? 1.62547 1.20939 1.02997 -0.07783 -0.03615 -0.14588 60  GLU B CA    
1452 C  C     . GLU B 60  ? 1.56837 1.16544 1.01828 -0.08775 -0.06040 -0.13099 60  GLU B C     
1453 O  O     . GLU B 60  ? 1.54725 1.16001 1.00148 -0.11311 -0.09059 -0.11803 60  GLU B O     
1454 C  CB    . GLU B 60  ? 1.80181 1.31404 1.12975 -0.08827 -0.02630 -0.17221 60  GLU B CB    
1455 C  CG    . GLU B 60  ? 1.94472 1.43847 1.21902 -0.08126 0.00015  -0.18885 60  GLU B CG    
1456 C  CD    . GLU B 60  ? 2.04638 1.53822 1.26969 -0.10997 -0.01909 -0.18425 60  GLU B CD    
1457 O  OE1   . GLU B 60  ? 2.01457 1.54075 1.26317 -0.12684 -0.05178 -0.16243 60  GLU B OE1   
1458 O  OE2   . GLU B 60  ? 2.13727 1.59263 1.29331 -0.11393 -0.00080 -0.20178 60  GLU B OE2   
1459 N  N     . GLY B 61  ? 1.50184 1.09482 0.98641 -0.06652 -0.04644 -0.13200 61  GLY B N     
1460 C  CA    . GLY B 61  ? 1.45929 1.06277 0.98614 -0.07529 -0.06402 -0.11779 61  GLY B CA    
1461 C  C     . GLY B 61  ? 1.47111 1.14068 1.06471 -0.06888 -0.07438 -0.09315 61  GLY B C     
1462 O  O     . GLY B 61  ? 1.43888 1.12276 1.07088 -0.07636 -0.08740 -0.07992 61  GLY B O     
1463 N  N     . TYR B 62  ? 1.46549 1.17224 1.07188 -0.05614 -0.06612 -0.08737 62  TYR B N     
1464 C  CA    . TYR B 62  ? 1.40496 1.16634 1.06683 -0.05030 -0.07296 -0.06560 62  TYR B CA    
1465 C  C     . TYR B 62  ? 1.17900 0.96697 0.86055 -0.02514 -0.04810 -0.06822 62  TYR B C     
1466 O  O     . TYR B 62  ? 1.10864 0.88174 0.76082 -0.01502 -0.02805 -0.08501 62  TYR B O     
1467 C  CB    . TYR B 62  ? 1.32031 1.10088 0.97401 -0.07039 -0.09594 -0.05136 62  TYR B CB    
1468 C  CG    . TYR B 62  ? 1.33166 1.10292 0.97792 -0.09717 -0.12502 -0.04677 62  TYR B CG    
1469 C  CD1   . TYR B 62  ? 1.36308 1.16527 1.06337 -0.10194 -0.13994 -0.02955 62  TYR B CD1   
1470 C  CD2   . TYR B 62  ? 1.33688 1.07049 0.92195 -0.11967 -0.13674 -0.06081 62  TYR B CD2   
1471 C  CE1   . TYR B 62  ? 1.38964 1.19258 1.09011 -0.12931 -0.16638 -0.02595 62  TYR B CE1   
1472 C  CE2   . TYR B 62  ? 1.35142 1.08208 0.93115 -0.14859 -0.16549 -0.05823 62  TYR B CE2   
1473 C  CZ    . TYR B 62  ? 1.38961 1.15854 1.03063 -0.15376 -0.18055 -0.04055 62  TYR B CZ    
1474 O  OH    . TYR B 62  ? 1.45748 1.23240 1.09979 -0.18530 -0.20905 -0.03853 62  TYR B OH    
1475 N  N     . GLU B 63  ? 1.16058 0.98982 0.89288 -0.01638 -0.04863 -0.05238 63  GLU B N     
1476 C  CA    . GLU B 63  ? 1.17240 1.03295 0.92886 0.00265  -0.02787 -0.05464 63  GLU B CA    
1477 C  C     . GLU B 63  ? 1.09856 0.99287 0.88361 -0.00232 -0.03305 -0.03676 63  GLU B C     
1478 O  O     . GLU B 63  ? 1.13312 1.03016 0.92674 -0.01438 -0.05229 -0.02073 63  GLU B O     
1479 C  CB    . GLU B 63  ? 1.04057 0.90949 0.82819 0.02469  -0.01777 -0.05781 63  GLU B CB    
1480 C  CG    . GLU B 63  ? 1.12222 1.01028 0.95226 0.02474  -0.02882 -0.04003 63  GLU B CG    
1481 C  CD    . GLU B 63  ? 1.09467 0.99112 0.94875 0.04740  -0.01875 -0.04170 63  GLU B CD    
1482 O  OE1   . GLU B 63  ? 0.95633 0.84781 0.79841 0.06556  -0.00480 -0.05571 63  GLU B OE1   
1483 O  OE2   . GLU B 63  ? 1.02702 0.93572 0.91087 0.04860  -0.02436 -0.02836 63  GLU B OE2   
1484 N  N     . GLY B 64  ? 0.98823 0.90884 0.78880 0.00731  -0.01474 -0.04003 64  GLY B N     
1485 C  CA    . GLY B 64  ? 0.98544 0.93119 0.81157 0.00449  -0.01391 -0.02553 64  GLY B CA    
1486 C  C     . GLY B 64  ? 0.96132 0.93574 0.82908 0.01864  -0.00417 -0.02628 64  GLY B C     
1487 O  O     . GLY B 64  ? 0.84770 0.83441 0.72109 0.03142  0.00858  -0.04061 64  GLY B O     
1488 N  N     . GLN B 65  ? 0.84184 0.82774 0.73755 0.01768  -0.01036 -0.01061 65  GLN B N     
1489 C  CA    . GLN B 65  ? 0.80912 0.81843 0.73846 0.02857  -0.00287 -0.01022 65  GLN B CA    
1490 C  C     . GLN B 65  ? 0.76188 0.78381 0.70111 0.02225  0.00620  -0.00328 65  GLN B C     
1491 O  O     . GLN B 65  ? 0.75129 0.76312 0.69296 0.01688  -0.00082 0.01296  65  GLN B O     
1492 C  CB    . GLN B 65  ? 0.73378 0.73726 0.68401 0.03361  -0.01476 0.00077  65  GLN B CB    
1493 C  CG    . GLN B 65  ? 0.87291 0.85362 0.80902 0.03715  -0.02200 -0.00560 65  GLN B CG    
1494 C  CD    . GLN B 65  ? 0.93294 0.90564 0.88845 0.03759  -0.03089 0.00607  65  GLN B CD    
1495 O  OE1   . GLN B 65  ? 0.87194 0.86087 0.85375 0.04203  -0.02755 0.01570  65  GLN B OE1   
1496 N  NE2   . GLN B 65  ? 0.86313 0.80792 0.80278 0.03068  -0.04028 0.00436  65  GLN B NE2   
1497 N  N     . VAL B 66  ? 0.62717 0.67120 0.57218 0.02290  0.02219  -0.01570 66  VAL B N     
1498 C  CA    . VAL B 66  ? 0.77818 0.82888 0.72931 0.01397  0.03389  -0.01242 66  VAL B CA    
1499 C  C     . VAL B 66  ? 0.73045 0.79012 0.70810 0.02155  0.03180  -0.00620 66  VAL B C     
1500 O  O     . VAL B 66  ? 0.69538 0.77809 0.68727 0.02964  0.03378  -0.01610 66  VAL B O     
1501 C  CB    . VAL B 66  ? 0.77242 0.84651 0.71967 0.00578  0.05218  -0.03025 66  VAL B CB    
1502 C  CG1   . VAL B 66  ? 0.73564 0.80849 0.68407 -0.00819 0.06571  -0.02834 66  VAL B CG1   
1503 C  CG2   . VAL B 66  ? 0.76913 0.83202 0.68672 -0.00151 0.05797  -0.03665 66  VAL B CG2   
1504 N  N     . ARG B 67  ? 0.65544 0.69766 0.63847 0.02066  0.02809  0.01088  67  ARG B N     
1505 C  CA    . ARG B 67  ? 0.70368 0.74906 0.70831 0.02765  0.02899  0.01815  67  ARG B CA    
1506 C  C     . ARG B 67  ? 0.78559 0.82219 0.78757 0.02065  0.04453  0.02039  67  ARG B C     
1507 O  O     . ARG B 67  ? 0.78222 0.80176 0.76634 0.01173  0.05167  0.02361  67  ARG B O     
1508 C  CB    . ARG B 67  ? 0.68452 0.71903 0.70280 0.03377  0.01542  0.03601  67  ARG B CB    
1509 C  CG    . ARG B 67  ? 0.70995 0.74501 0.72855 0.03772  0.00189  0.03304  67  ARG B CG    
1510 C  CD    . ARG B 67  ? 0.66416 0.69330 0.70001 0.03782  -0.01033 0.04966  67  ARG B CD    
1511 N  NE    . ARG B 67  ? 0.81566 0.83661 0.84527 0.03615  -0.02233 0.04575  67  ARG B NE    
1512 C  CZ    . ARG B 67  ? 0.82574 0.84308 0.86833 0.03049  -0.03450 0.05657  67  ARG B CZ    
1513 N  NH1   . ARG B 67  ? 0.77429 0.80337 0.84314 0.02916  -0.03717 0.07330  67  ARG B NH1   
1514 N  NH2   . ARG B 67  ? 0.79384 0.79566 0.82345 0.02571  -0.04298 0.04999  67  ARG B NH2   
1515 N  N     . PRO B 68  ? 0.73566 0.77749 0.74911 0.02391  0.05158  0.01854  68  PRO B N     
1516 C  CA    . PRO B 68  ? 0.72237 0.74808 0.72724 0.01562  0.06902  0.01785  68  PRO B CA    
1517 C  C     . PRO B 68  ? 0.82350 0.81992 0.83057 0.02237  0.07194  0.03881  68  PRO B C     
1518 O  O     . PRO B 68  ? 0.72843 0.72699 0.75307 0.03374  0.05951  0.05405  68  PRO B O     
1519 C  CB    . PRO B 68  ? 0.71039 0.75000 0.72283 0.01819  0.07327  0.00899  68  PRO B CB    
1520 C  CG    . PRO B 68  ? 0.70464 0.77202 0.72710 0.02767  0.05854  0.00305  68  PRO B CG    
1521 C  CD    . PRO B 68  ? 0.72993 0.78870 0.75681 0.03402  0.04584  0.01467  68  PRO B CD    
1522 N  N     . ARG B 69  ? 0.94190 0.91114 0.93133 0.01502  0.08948  0.03944  69  ARG B N     
1523 C  CA    . ARG B 69  ? 0.99805 0.93666 0.98880 0.02609  0.09672  0.05953  69  ARG B CA    
1524 C  C     . ARG B 69  ? 1.04445 0.97572 1.04532 0.03291  0.11033  0.05901  69  ARG B C     
1525 O  O     . ARG B 69  ? 0.97333 0.90027 0.95913 0.02067  0.12380  0.04143  69  ARG B O     
1526 C  CB    . ARG B 69  ? 1.03599 0.93681 0.99474 0.01686  0.11202  0.06195  69  ARG B CB    
1527 C  CG    . ARG B 69  ? 1.14505 1.03990 1.09094 0.01827  0.09914  0.07462  69  ARG B CG    
1528 C  CD    . ARG B 69  ? 1.18577 1.08437 1.15398 0.03962  0.08266  0.09985  69  ARG B CD    
1529 N  NE    . ARG B 69  ? 1.29576 1.17270 1.24099 0.04335  0.07562  0.11713  69  ARG B NE    
1530 C  CZ    . ARG B 69  ? 1.37044 1.20507 1.29291 0.05032  0.09045  0.13135  69  ARG B CZ    
1531 N  NH1   . ARG B 69  ? 1.20523 1.01083 1.12354 0.05234  0.11541  0.12819  69  ARG B NH1   
1532 N  NH2   . ARG B 69  ? 1.45139 1.26765 1.34957 0.05579  0.08050  0.14936  69  ARG B NH2   
1533 N  N     . SER B 70  ? 1.02824 0.96039 1.05420 0.05103  0.10720  0.07761  70  SER B N     
1534 C  CA    . SER B 70  ? 1.09472 1.01949 1.12977 0.05905  0.12265  0.07792  70  SER B CA    
1535 C  C     . SER B 70  ? 0.98015 0.86041 0.98886 0.05689  0.14965  0.07473  70  SER B C     
1536 O  O     . SER B 70  ? 0.96889 0.83737 0.96561 0.05240  0.16567  0.06248  70  SER B O     
1537 C  CB    . SER B 70  ? 0.97913 0.91896 1.05160 0.07814  0.11612  0.09940  70  SER B CB    
1538 O  OG    . SER B 70  ? 1.05952 0.98883 1.14026 0.09032  0.11381  0.11946  70  SER B OG    
1539 N  N     . GLY B 71  ? 0.99422 0.84408 0.98766 0.05936  0.15570  0.08528  71  GLY B N     
1540 C  CA    . GLY B 71  ? 1.06696 0.86303 1.02952 0.05751  0.18422  0.08282  71  GLY B CA    
1541 C  C     . GLY B 71  ? 1.04297 0.82586 0.97044 0.02786  0.19647  0.05491  71  GLY B C     
1542 O  O     . GLY B 71  ? 1.01301 0.76703 0.91997 0.02067  0.21787  0.04255  71  GLY B O     
1543 N  N     . LEU B 72  ? 1.04845 0.85390 0.96835 0.00905  0.18384  0.04371  72  LEU B N     
1544 C  CA    . LEU B 72  ? 1.08321 0.88810 0.97725 -0.02137 0.19425  0.01678  72  LEU B CA    
1545 C  C     . LEU B 72  ? 0.92254 0.76471 0.82765 -0.02713 0.18780  -0.00106 72  LEU B C     
1546 O  O     . LEU B 72  ? 1.03072 0.86972 0.91430 -0.05042 0.19874  -0.02322 72  LEU B O     
1547 C  CB    . LEU B 72  ? 1.02803 0.85562 0.91724 -0.03781 0.18408  0.00990  72  LEU B CB    
1548 C  CG    . LEU B 72  ? 1.17853 0.95855 1.03572 -0.04626 0.19854  0.01850  72  LEU B CG    
1549 C  CD1   . LEU B 72  ? 1.11504 0.92430 0.96966 -0.06100 0.18838  0.01160  72  LEU B CD1   
1550 C  CD2   . LEU B 72  ? 1.24344 0.97268 1.06352 -0.06908 0.22839  0.00459  72  LEU B CD2   
1551 N  N     . ALA B 73  ? 0.88556 0.76223 0.82124 -0.00763 0.16965  0.00848  73  ALA B N     
1552 C  CA    . ALA B 73  ? 0.94045 0.84919 0.88199 -0.00961 0.16214  -0.00485 73  ALA B CA    
1553 C  C     . ALA B 73  ? 0.93137 0.80777 0.85504 -0.00838 0.18219  -0.00843 73  ALA B C     
1554 O  O     . ALA B 73  ? 0.89913 0.78280 0.80295 -0.02437 0.18541  -0.02837 73  ALA B O     
1555 C  CB    . ALA B 73  ? 0.85613 0.80031 0.82926 0.00979  0.14011  0.00782  73  ALA B CB    
1556 N  N     . TRP B 74  ? 0.88058 0.72219 0.80975 0.01062  0.19629  0.01017  74  TRP B N     
1557 C  CA    . TRP B 74  ? 1.03405 0.84265 0.94629 0.01546  0.21878  0.00746  74  TRP B CA    
1558 C  C     . TRP B 74  ? 1.01394 0.76598 0.88365 -0.00169 0.24586  -0.00591 74  TRP B C     
1559 O  O     . TRP B 74  ? 1.09529 0.82541 0.93447 -0.01397 0.26133  -0.02302 74  TRP B O     
1560 C  CB    . TRP B 74  ? 0.91468 0.71601 0.85673 0.04545  0.22500  0.03297  74  TRP B CB    
1561 C  CG    . TRP B 74  ? 1.02276 0.78237 0.94685 0.05407  0.25493  0.03212  74  TRP B CG    
1562 C  CD1   . TRP B 74  ? 1.05706 0.77299 0.98076 0.07276  0.27939  0.04625  74  TRP B CD1   
1563 C  CD2   . TRP B 74  ? 1.09956 0.85440 0.99942 0.04611  0.26502  0.01631  74  TRP B CD2   
1564 N  NE1   . TRP B 74  ? 1.18258 0.86510 1.08422 0.07694  0.30689  0.03886  74  TRP B NE1   
1565 C  CE2   . TRP B 74  ? 1.18097 0.88579 1.06508 0.05904  0.29818  0.02006  74  TRP B CE2   
1566 C  CE3   . TRP B 74  ? 0.99153 0.77859 0.87887 0.03134  0.24914  0.00027  74  TRP B CE3   
1567 C  CZ2   . TRP B 74  ? 1.12461 0.80829 0.97710 0.05452  0.31694  0.00654  74  TRP B CZ2   
1568 C  CZ3   . TRP B 74  ? 1.05871 0.82712 0.91451 0.02742  0.26456  -0.01130 74  TRP B CZ3   
1569 C  CH2   . TRP B 74  ? 1.05930 0.77528 0.89611 0.03737  0.29867  -0.00901 74  TRP B CH2   
1570 N  N     . LYS B 75  ? 1.11748 0.84034 0.97885 -0.00429 0.25266  0.00125  75  LYS B N     
1571 C  CA    . LYS B 75  ? 1.19859 0.85420 1.01521 -0.01928 0.28254  -0.00868 75  LYS B CA    
1572 C  C     . LYS B 75  ? 1.26485 0.92593 1.05007 -0.06049 0.28375  -0.03967 75  LYS B C     
1573 O  O     . LYS B 75  ? 1.26213 0.87732 1.00645 -0.08025 0.30698  -0.05790 75  LYS B O     
1574 C  CB    . LYS B 75  ? 1.08047 0.69781 0.89373 -0.00681 0.29001  0.01219  75  LYS B CB    
1575 N  N     . LYS B 76  ? 1.32237 1.04048 1.12643 -0.07467 0.25986  -0.04705 76  LYS B N     
1576 C  CA    . LYS B 76  ? 1.32172 1.05663 1.10550 -0.11410 0.26031  -0.07497 76  LYS B CA    
1577 C  C     . LYS B 76  ? 1.22076 1.03478 1.02884 -0.12123 0.23306  -0.08961 76  LYS B C     
1578 O  O     . LYS B 76  ? 1.22035 1.06379 1.02002 -0.15295 0.23022  -0.11329 76  LYS B O     
1579 C  CB    . LYS B 76  ? 1.31678 1.04057 1.09486 -0.12851 0.26451  -0.07200 76  LYS B CB    
1580 C  CG    . LYS B 76  ? 1.29887 0.93734 1.04358 -0.12325 0.29264  -0.05764 76  LYS B CG    
1581 C  CD    . LYS B 76  ? 1.32079 0.95056 1.06238 -0.12669 0.29175  -0.04542 76  LYS B CD    
1582 C  CE    . LYS B 76  ? 1.39050 0.93402 1.09898 -0.11179 0.31638  -0.02434 76  LYS B CE    
1583 N  NZ    . LYS B 76  ? 1.53684 1.07139 1.23946 -0.10881 0.31191  -0.00690 76  LYS B NZ    
1584 N  N     . GLY B 77  ? 1.10513 0.95461 0.94302 -0.09292 0.21366  -0.07593 77  GLY B N     
1585 C  CA    . GLY B 77  ? 1.03182 0.94939 0.88881 -0.09437 0.18843  -0.08673 77  GLY B CA    
1586 C  C     . GLY B 77  ? 1.05215 1.02089 0.93458 -0.09938 0.17113  -0.08969 77  GLY B C     
1587 O  O     . GLY B 77  ? 1.05086 1.07640 0.94426 -0.10841 0.15507  -0.10510 77  GLY B O     
1588 N  N     . LEU B 78  ? 0.95620 0.90707 0.84720 -0.09190 0.17416  -0.07475 78  LEU B N     
1589 C  CA    . LEU B 78  ? 1.01511 1.00469 0.92358 -0.09728 0.16309  -0.07759 78  LEU B CA    
1590 C  C     . LEU B 78  ? 0.88254 0.89575 0.81934 -0.06731 0.14233  -0.05953 78  LEU B C     
1591 O  O     . LEU B 78  ? 1.01468 0.99881 0.95605 -0.04658 0.14185  -0.03900 78  LEU B O     
1592 C  CB    . LEU B 78  ? 1.00991 0.95672 0.89801 -0.11270 0.18188  -0.07401 78  LEU B CB    
1593 C  CG    . LEU B 78  ? 1.08480 1.06344 0.97891 -0.12960 0.18040  -0.08311 78  LEU B CG    
1594 C  CD1   . LEU B 78  ? 1.06935 1.09821 0.96861 -0.15910 0.18118  -0.11162 78  LEU B CD1   
1595 C  CD2   . LEU B 78  ? 1.14134 1.06172 1.00579 -0.14111 0.20112  -0.07382 78  LEU B CD2   
1596 N  N     . THR B 79  ? 0.77793 0.84439 0.73432 -0.06546 0.12615  -0.06777 79  THR B N     
1597 C  CA    . THR B 79  ? 0.76326 0.84653 0.74067 -0.03979 0.10783  -0.05380 79  THR B CA    
1598 C  C     . THR B 79  ? 0.77847 0.90208 0.76788 -0.04271 0.10034  -0.06343 79  THR B C     
1599 O  O     . THR B 79  ? 0.80832 0.96248 0.79825 -0.06252 0.10659  -0.08202 79  THR B O     
1600 C  CB    . THR B 79  ? 0.76392 0.86486 0.75123 -0.02158 0.09461  -0.05084 79  THR B CB    
1601 O  OG1   . THR B 79  ? 0.70201 0.80838 0.70532 0.00023  0.07978  -0.03697 79  THR B OG1   
1602 C  CG2   . THR B 79  ? 0.75827 0.90911 0.74884 -0.02893 0.08667  -0.07058 79  THR B CG2   
1603 N  N     . VAL B 80  ? 0.67341 0.79735 0.67261 -0.02391 0.08823  -0.05151 80  VAL B N     
1604 C  CA    . VAL B 80  ? 0.69376 0.85140 0.70238 -0.02096 0.08226  -0.06007 80  VAL B CA    
1605 C  C     . VAL B 80  ? 0.69412 0.89777 0.72075 -0.00632 0.06930  -0.06911 80  VAL B C     
1606 O  O     . VAL B 80  ? 0.78853 0.98413 0.81843 0.01262  0.05802  -0.05892 80  VAL B O     
1607 C  CB    . VAL B 80  ? 0.81800 0.95112 0.82250 -0.00812 0.07462  -0.04542 80  VAL B CB    
1608 C  CG1   . VAL B 80  ? 0.59281 0.75486 0.60178 -0.00364 0.07177  -0.05617 80  VAL B CG1   
1609 C  CG2   . VAL B 80  ? 0.67759 0.76770 0.66207 -0.01946 0.08452  -0.03374 80  VAL B CG2   
1610 N  N     . LEU B 81  ? 0.76827 1.02150 0.80688 -0.01461 0.07150  -0.08729 81  LEU B N     
1611 C  CA    . LEU B 81  ? 0.62025 0.92407 0.67667 0.00059  0.05823  -0.09557 81  LEU B CA    
1612 C  C     . LEU B 81  ? 0.72714 1.02739 0.78917 0.03259  0.04501  -0.08520 81  LEU B C     
1613 O  O     . LEU B 81  ? 0.66484 0.95915 0.72496 0.05120  0.03330  -0.07660 81  LEU B O     
1614 C  CB    . LEU B 81  ? 0.59366 0.96036 0.66913 -0.01414 0.06341  -0.11662 81  LEU B CB    
1615 C  CG    . LEU B 81  ? 0.81722 1.24381 0.90847 -0.01548 0.05255  -0.12980 81  LEU B CG    
1616 C  CD1   . LEU B 81  ? 0.72536 1.22079 0.84329 -0.03200 0.05915  -0.15014 81  LEU B CD1   
1617 C  CD2   . LEU B 81  ? 0.85552 1.29764 0.95353 0.02118  0.03230  -0.12046 81  LEU B CD2   
1618 N  N     . ASN B 82  ? 0.71236 1.01035 0.77600 0.03809  0.04867  -0.08629 82  ASN B N     
1619 C  CA    . ASN B 82  ? 0.63160 0.92108 0.69567 0.06614  0.03932  -0.08003 82  ASN B CA    
1620 C  C     . ASN B 82  ? 0.71253 0.94195 0.75843 0.06961  0.03518  -0.06281 82  ASN B C     
1621 O  O     . ASN B 82  ? 0.74456 0.95455 0.78256 0.08156  0.03245  -0.06036 82  ASN B O     
1622 C  CB    . ASN B 82  ? 0.65451 0.97134 0.72643 0.07047  0.04747  -0.09252 82  ASN B CB    
1623 C  CG    . ASN B 82  ? 0.68031 0.96825 0.73505 0.04880  0.06087  -0.09306 82  ASN B CG    
1624 O  OD1   . ASN B 82  ? 0.71544 0.98915 0.76187 0.02451  0.06850  -0.09141 82  ASN B OD1   
1625 N  ND2   . ASN B 82  ? 0.66880 0.94187 0.71245 0.05831  0.06449  -0.09478 82  ASN B ND2   
1626 N  N     . ALA B 83  ? 0.64574 0.84685 0.68535 0.05896  0.03531  -0.05171 83  ALA B N     
1627 C  CA    . ALA B 83  ? 0.73870 0.89422 0.76906 0.06077  0.03061  -0.03505 83  ALA B CA    
1628 C  C     . ALA B 83  ? 0.67106 0.81396 0.70121 0.08155  0.01972  -0.02738 83  ALA B C     
1629 O  O     . ALA B 83  ? 0.68578 0.84268 0.71950 0.09327  0.01616  -0.02736 83  ALA B O     
1630 C  CB    . ALA B 83  ? 0.66267 0.79713 0.69193 0.04898  0.03563  -0.02460 83  ALA B CB    
1631 N  N     . PRO B 84  ? 0.65228 0.76548 0.67366 0.08499  0.01439  -0.02096 84  PRO B N     
1632 C  CA    . PRO B 84  ? 0.78847 0.88371 0.79912 0.07200  0.01515  -0.02032 84  PRO B CA    
1633 C  C     . PRO B 84  ? 0.80666 0.91691 0.80850 0.07435  0.02117  -0.03593 84  PRO B C     
1634 O  O     . PRO B 84  ? 0.76254 0.87154 0.75975 0.09084  0.01943  -0.04211 84  PRO B O     
1635 C  CB    . PRO B 84  ? 0.72454 0.78512 0.72893 0.07414  0.00464  -0.00847 84  PRO B CB    
1636 C  CG    . PRO B 84  ? 0.72426 0.78182 0.72816 0.09321  0.00214  -0.00980 84  PRO B CG    
1637 C  CD    . PRO B 84  ? 0.72711 0.81635 0.74362 0.09986  0.00659  -0.01253 84  PRO B CD    
1638 N  N     . GLY B 85  ? 0.73078 0.85246 0.72839 0.05875  0.03104  -0.04231 85  GLY B N     
1639 C  CA    . GLY B 85  ? 0.69185 0.82808 0.68061 0.05825  0.04083  -0.05703 85  GLY B CA    
1640 C  C     . GLY B 85  ? 0.76435 0.86590 0.72772 0.06144  0.03665  -0.05665 85  GLY B C     
1641 O  O     . GLY B 85  ? 0.75773 0.82854 0.70225 0.04798  0.03090  -0.04707 85  GLY B O     
1642 N  N     . THR B 86  ? 0.69175 0.79686 0.65217 0.07985  0.03915  -0.06704 86  THR B N     
1643 C  CA    . THR B 86  ? 0.89100 0.95522 0.82135 0.08300  0.03635  -0.06932 86  THR B CA    
1644 C  C     . THR B 86  ? 0.77976 0.84215 0.68617 0.07141  0.04972  -0.08040 86  THR B C     
1645 O  O     . THR B 86  ? 0.87468 0.96806 0.78880 0.07987  0.06595  -0.09486 86  THR B O     
1646 C  CB    . THR B 86  ? 0.92352 0.98220 0.85486 0.11019  0.03706  -0.07558 86  THR B CB    
1647 O  OG1   . THR B 86  ? 0.83505 0.89458 0.78431 0.12030  0.02646  -0.06400 86  THR B OG1   
1648 C  CG2   . THR B 86  ? 0.84724 0.85158 0.74108 0.11018  0.03484  -0.07884 86  THR B CG2   
1649 N  N     . ILE B 87  ? 0.76978 0.79866 0.64721 0.05245  0.04311  -0.07308 87  ILE B N     
1650 C  CA    . ILE B 87  ? 0.97270 0.98850 0.81518 0.04006  0.05462  -0.08146 87  ILE B CA    
1651 C  C     . ILE B 87  ? 0.98469 0.95813 0.79055 0.04475  0.05024  -0.08864 87  ILE B C     
1652 O  O     . ILE B 87  ? 0.97709 0.91600 0.76267 0.03400  0.03183  -0.07920 87  ILE B O     
1653 C  CB    . ILE B 87  ? 0.98644 0.98870 0.81221 0.01771  0.04912  -0.06764 87  ILE B CB    
1654 C  CG1   . ILE B 87  ? 0.82718 0.85982 0.68549 0.01291  0.05446  -0.06069 87  ILE B CG1   
1655 C  CG2   . ILE B 87  ? 1.00561 0.99192 0.78859 0.00494  0.06317  -0.07564 87  ILE B CG2   
1656 C  CD1   . ILE B 87  ? 0.84269 0.91563 0.71758 0.01240  0.07717  -0.07649 87  ILE B CD1   
1657 N  N     . ASP B 88  ? 1.01631 0.99329 0.81417 0.06049  0.06782  -0.10615 88  ASP B N     
1658 C  CA    . ASP B 88  ? 1.08667 1.01573 0.84440 0.06642  0.06813  -0.11605 88  ASP B CA    
1659 C  C     . ASP B 88  ? 1.11927 1.01203 0.82332 0.04279  0.06671  -0.11815 88  ASP B C     
1660 O  O     . ASP B 88  ? 1.04156 0.94955 0.73588 0.02950  0.07688  -0.11775 88  ASP B O     
1661 C  CB    . ASP B 88  ? 1.16002 1.10258 0.92328 0.09380  0.09120  -0.13406 88  ASP B CB    
1662 C  CG    . ASP B 88  ? 1.12194 1.10966 0.93776 0.11893  0.09105  -0.13082 88  ASP B CG    
1663 O  OD1   . ASP B 88  ? 1.09369 1.13887 0.94622 0.11787  0.09815  -0.13101 88  ASP B OD1   
1664 O  OD2   . ASP B 88  ? 1.10633 1.06982 0.92313 0.13809  0.08357  -0.12798 88  ASP B OD2   
1665 N  N     . ALA B 89  ? 1.21298 1.05445 0.87776 0.03582  0.05380  -0.12043 89  ALA B N     
1666 C  CA    . ALA B 89  ? 1.29046 1.09617 0.89963 0.01130  0.04541  -0.12081 89  ALA B CA    
1667 C  C     . ALA B 89  ? 1.30000 1.09662 0.86815 0.01106  0.07206  -0.13798 89  ALA B C     
1668 O  O     . ALA B 89  ? 1.32123 1.09570 0.84168 -0.00971 0.06826  -0.13623 89  ALA B O     
1669 C  CB    . ALA B 89  ? 1.33854 1.09281 0.91356 0.00138  0.02655  -0.12371 89  ALA B CB    
1670 N  N     . ASP B 90  ? 1.34217 1.15717 0.92733 0.03463  0.09924  -0.15364 90  ASP B N     
1671 C  CA    . ASP B 90  ? 1.37672 1.18822 0.92883 0.03687  0.12986  -0.17150 90  ASP B CA    
1672 C  C     . ASP B 90  ? 1.34174 1.21344 0.93173 0.03687  0.15058  -0.17057 90  ASP B C     
1673 O  O     . ASP B 90  ? 1.16923 1.05320 0.74794 0.04229  0.18140  -0.18636 90  ASP B O     
1674 C  CB    . ASP B 90  ? 1.43179 1.22277 0.97544 0.06485  0.15016  -0.19137 90  ASP B CB    
1675 C  CG    . ASP B 90  ? 1.41168 1.23761 1.01742 0.09467  0.14803  -0.18742 90  ASP B CG    
1676 O  OD1   . ASP B 90  ? 1.30377 1.16514 0.95471 0.09030  0.12921  -0.17045 90  ASP B OD1   
1677 O  OD2   . ASP B 90  ? 1.29852 1.11372 0.90442 0.12408  0.16580  -0.20077 90  ASP B OD2   
1678 N  N     . TYR B 91  ? 1.26074 1.16888 0.89419 0.02928  0.13651  -0.15360 91  TYR B N     
1679 C  CA    . TYR B 91  ? 1.19656 1.15779 0.86395 0.02373  0.15553  -0.15365 91  TYR B CA    
1680 C  C     . TYR B 91  ? 1.11320 1.05272 0.73358 -0.00407 0.16331  -0.14830 91  TYR B C     
1681 O  O     . TYR B 91  ? 1.33388 1.23859 0.92385 -0.01991 0.14040  -0.13184 91  TYR B O     
1682 C  CB    . TYR B 91  ? 1.14016 1.14005 0.86467 0.02544  0.13931  -0.13933 91  TYR B CB    
1683 C  CG    . TYR B 91  ? 0.97842 1.03234 0.73843 0.01632  0.15836  -0.14189 91  TYR B CG    
1684 C  CD1   . TYR B 91  ? 1.08471 1.18353 0.86621 0.02524  0.18682  -0.16032 91  TYR B CD1   
1685 C  CD2   . TYR B 91  ? 0.98908 1.04965 0.76212 -0.00177 0.14920  -0.12670 91  TYR B CD2   
1686 C  CE1   . TYR B 91  ? 1.10866 1.26115 0.92484 0.01165  0.20402  -0.16442 91  TYR B CE1   
1687 C  CE2   . TYR B 91  ? 1.01162 1.11539 0.81240 -0.01476 0.16779  -0.13112 91  TYR B CE2   
1688 C  CZ    . TYR B 91  ? 0.94739 1.09891 0.77036 -0.01033 0.19435  -0.15045 91  TYR B CZ    
1689 O  OH    . TYR B 91  ? 0.90567 1.10455 0.75837 -0.02839 0.21276  -0.15656 91  TYR B OH    
1690 N  N     . ARG B 92  ? 1.10768 1.06963 0.72270 -0.00918 0.19628  -0.16122 92  ARG B N     
1691 C  CA    . ARG B 92  ? 1.28385 1.22059 0.84703 -0.03519 0.20995  -0.15700 92  ARG B CA    
1692 C  C     . ARG B 92  ? 1.23708 1.21738 0.83227 -0.05056 0.23124  -0.15502 92  ARG B C     
1693 O  O     . ARG B 92  ? 1.34387 1.30103 0.89544 -0.07337 0.24657  -0.15016 92  ARG B O     
1694 C  CB    . ARG B 92  ? 1.31470 1.22259 0.82223 -0.03451 0.23588  -0.17556 92  ARG B CB    
1695 C  CG    . ARG B 92  ? 1.35985 1.22027 0.83159 -0.02095 0.21976  -0.18279 92  ARG B CG    
1696 C  CD    . ARG B 92  ? 1.37780 1.18724 0.80362 -0.03808 0.18286  -0.16469 92  ARG B CD    
1697 N  NE    . ARG B 92  ? 1.53928 1.32736 0.97246 -0.02590 0.15622  -0.16519 92  ARG B NE    
1698 C  CZ    . ARG B 92  ? 1.61995 1.36189 1.00827 -0.03943 0.12655  -0.15752 92  ARG B CZ    
1699 N  NH1   . ARG B 92  ? 1.64966 1.36163 0.97902 -0.06197 0.11697  -0.14810 92  ARG B NH1   
1700 N  NH2   . ARG B 92  ? 1.62587 1.35211 1.02764 -0.03108 0.10567  -0.15890 92  ARG B NH2   
1701 N  N     . GLY B 93  ? 1.15702 1.19668 0.82254 -0.04062 0.23279  -0.15880 93  GLY B N     
1702 C  CA    . GLY B 93  ? 1.13129 1.21205 0.82817 -0.05979 0.25054  -0.15857 93  GLY B CA    
1703 C  C     . GLY B 93  ? 1.09162 1.14899 0.78591 -0.07525 0.22986  -0.13666 93  GLY B C     
1704 O  O     . GLY B 93  ? 1.16609 1.18096 0.83746 -0.07047 0.20136  -0.12006 93  GLY B O     
1705 N  N     . GLU B 94  ? 1.07457 1.16188 0.79421 -0.09464 0.24628  -0.13761 94  GLU B N     
1706 C  CA    . GLU B 94  ? 1.14453 1.20789 0.86195 -0.10874 0.23346  -0.11889 94  GLU B CA    
1707 C  C     . GLU B 94  ? 1.10022 1.18729 0.86756 -0.09074 0.20658  -0.11390 94  GLU B C     
1708 O  O     . GLU B 94  ? 1.01843 1.16328 0.83807 -0.08204 0.20962  -0.12772 94  GLU B O     
1709 C  CB    . GLU B 94  ? 1.17675 1.25831 0.90072 -0.13847 0.26300  -0.12453 94  GLU B CB    
1710 C  CG    . GLU B 94  ? 1.15809 1.20548 0.87394 -0.15257 0.25468  -0.10635 94  GLU B CG    
1711 C  CD    . GLU B 94  ? 1.25611 1.30739 0.96700 -0.18680 0.28694  -0.11262 94  GLU B CD    
1712 O  OE1   . GLU B 94  ? 1.26368 1.37890 1.01803 -0.19800 0.30611  -0.13422 94  GLU B OE1   
1713 O  OE2   . GLU B 94  ? 1.34002 1.33034 1.00306 -0.20279 0.29341  -0.09556 94  GLU B OE2   
1714 N  N     . VAL B 95  ? 1.12978 1.17469 0.88078 -0.08497 0.18050  -0.09338 95  VAL B N     
1715 C  CA    . VAL B 95  ? 0.96099 1.02197 0.75385 -0.07004 0.15776  -0.08672 95  VAL B CA    
1716 C  C     . VAL B 95  ? 0.96999 1.05259 0.79014 -0.08528 0.16840  -0.08774 95  VAL B C     
1717 O  O     . VAL B 95  ? 1.04373 1.09521 0.83678 -0.10571 0.18092  -0.07928 95  VAL B O     
1718 C  CB    . VAL B 95  ? 0.97456 0.98946 0.74549 -0.06165 0.12997  -0.06468 95  VAL B CB    
1719 C  CG1   . VAL B 95  ? 0.88254 0.91173 0.69512 -0.04953 0.11191  -0.05655 95  VAL B CG1   
1720 C  CG2   . VAL B 95  ? 1.01011 1.00636 0.75550 -0.05003 0.11749  -0.06754 95  VAL B CG2   
1721 N  N     . LYS B 96  ? 0.94743 1.07936 0.81643 -0.07582 0.16376  -0.09821 96  LYS B N     
1722 C  CA    . LYS B 96  ? 0.94460 1.10057 0.83889 -0.09181 0.17174  -0.10282 96  LYS B CA    
1723 C  C     . LYS B 96  ? 0.90090 1.06331 0.82290 -0.07479 0.14915  -0.09542 96  LYS B C     
1724 O  O     . LYS B 96  ? 0.87496 1.04639 0.81120 -0.05013 0.13134  -0.09346 96  LYS B O     
1725 C  CB    . LYS B 96  ? 0.74451 0.96748 0.67178 -0.10286 0.19122  -0.12650 96  LYS B CB    
1726 N  N     . VAL B 97  ? 0.93980 1.09187 0.86464 -0.08921 0.15261  -0.09164 97  VAL B N     
1727 C  CA    . VAL B 97  ? 0.71867 0.87110 0.66343 -0.07661 0.13596  -0.08458 97  VAL B CA    
1728 C  C     . VAL B 97  ? 0.77491 0.97584 0.74756 -0.08982 0.14280  -0.10226 97  VAL B C     
1729 O  O     . VAL B 97  ? 0.85219 1.05727 0.81778 -0.11846 0.16258  -0.11266 97  VAL B O     
1730 C  CB    . VAL B 97  ? 0.90512 0.99805 0.82536 -0.07915 0.13387  -0.06396 97  VAL B CB    
1731 C  CG1   . VAL B 97  ? 0.71481 0.80965 0.65555 -0.06751 0.12198  -0.05860 97  VAL B CG1   
1732 C  CG2   . VAL B 97  ? 0.85927 0.91416 0.75504 -0.06638 0.12209  -0.04604 97  VAL B CG2   
1733 N  N     . ILE B 98  ? 0.84618 1.08216 0.84721 -0.07078 0.12621  -0.10553 98  ILE B N     
1734 C  CA    . ILE B 98  ? 0.75505 1.04237 0.78165 -0.08037 0.12620  -0.12138 98  ILE B CA    
1735 C  C     . ILE B 98  ? 0.78804 1.04140 0.80416 -0.08364 0.12116  -0.11282 98  ILE B C     
1736 O  O     . ILE B 98  ? 0.80191 1.05031 0.82462 -0.06092 0.10454  -0.10324 98  ILE B O     
1737 C  CB    . ILE B 98  ? 0.71132 1.05804 0.77061 -0.05442 0.11108  -0.12905 98  ILE B CB    
1738 C  CG1   . ILE B 98  ? 0.66585 1.03749 0.73268 -0.04582 0.11920  -0.13640 98  ILE B CG1   
1739 C  CG2   . ILE B 98  ? 0.72559 1.13358 0.81084 -0.06542 0.10786  -0.14527 98  ILE B CG2   
1740 C  CD1   . ILE B 98  ? 0.61132 1.03493 0.70827 -0.01424 0.10655  -0.14213 98  ILE B CD1   
1741 N  N     . LEU B 99  ? 0.85599 1.08105 0.85244 -0.11229 0.13838  -0.11641 99  LEU B N     
1742 C  CA    . LEU B 99  ? 0.87638 1.06656 0.85935 -0.11726 0.13913  -0.11168 99  LEU B CA    
1743 C  C     . LEU B 99  ? 0.97823 1.21730 0.97595 -0.13267 0.13654  -0.13206 99  LEU B C     
1744 O  O     . LEU B 99  ? 0.91427 1.20045 0.92476 -0.15634 0.14435  -0.15151 99  LEU B O     
1745 C  CB    . LEU B 99  ? 0.75612 0.88066 0.70389 -0.13830 0.16076  -0.10485 99  LEU B CB    
1746 C  CG    . LEU B 99  ? 0.86536 0.93413 0.79351 -0.12034 0.15949  -0.07992 99  LEU B CG    
1747 C  CD1   . LEU B 99  ? 0.99675 0.99674 0.88926 -0.13435 0.17958  -0.07036 99  LEU B CD1   
1748 C  CD2   . LEU B 99  ? 0.78865 0.85632 0.73273 -0.08790 0.13798  -0.06408 99  LEU B CD2   
1749 N  N     . VAL B 100 ? 0.97731 1.20725 0.97261 -0.12061 0.12567  -0.12769 100 VAL B N     
1750 C  CA    . VAL B 100 ? 0.88688 1.15916 0.88878 -0.13334 0.11910  -0.14535 100 VAL B CA    
1751 C  C     . VAL B 100 ? 0.94660 1.16262 0.91805 -0.14044 0.12700  -0.14160 100 VAL B C     
1752 O  O     . VAL B 100 ? 0.90494 1.06990 0.86527 -0.11939 0.12786  -0.12161 100 VAL B O     
1753 C  CB    . VAL B 100 ? 0.85925 1.18982 0.88854 -0.10375 0.09397  -0.14461 100 VAL B CB    
1754 C  CG1   . VAL B 100 ? 0.89281 1.18305 0.91556 -0.07009 0.08330  -0.12186 100 VAL B CG1   
1755 C  CG2   . VAL B 100 ? 0.96024 1.34091 0.99396 -0.11664 0.08351  -0.16220 100 VAL B CG2   
1756 N  N     . ASN B 101 ? 1.05462 1.28097 1.01271 -0.17132 0.13400  -0.16185 101 ASN B N     
1757 C  CA    . ASN B 101 ? 1.06805 1.23405 0.98963 -0.18325 0.14743  -0.16289 101 ASN B CA    
1758 C  C     . ASN B 101 ? 1.14227 1.33698 1.06187 -0.17341 0.12951  -0.16841 101 ASN B C     
1759 O  O     . ASN B 101 ? 1.18209 1.43075 1.10550 -0.19412 0.11970  -0.18949 101 ASN B O     
1760 C  CB    . ASN B 101 ? 1.07680 1.21969 0.97308 -0.22896 0.17081  -0.18310 101 ASN B CB    
1761 C  CG    . ASN B 101 ? 1.24091 1.30536 1.09241 -0.24003 0.19052  -0.18392 101 ASN B CG    
1762 O  OD1   . ASN B 101 ? 1.16141 1.18198 1.00348 -0.21077 0.19130  -0.16507 101 ASN B OD1   
1763 N  ND2   . ASN B 101 ? 1.30304 1.34848 1.12650 -0.28344 0.20873  -0.20666 101 ASN B ND2   
1764 N  N     . LEU B 102 ? 1.07834 1.23908 0.99129 -0.14271 0.12505  -0.14905 102 LEU B N     
1765 C  CA    . LEU B 102 ? 1.11057 1.28452 1.01190 -0.13209 0.11172  -0.15099 102 LEU B CA    
1766 C  C     . LEU B 102 ? 1.25364 1.36861 1.11151 -0.14933 0.13101  -0.15829 102 LEU B C     
1767 O  O     . LEU B 102 ? 1.12062 1.23753 0.95931 -0.14309 0.12339  -0.16062 102 LEU B O     
1768 C  CB    . LEU B 102 ? 1.10340 1.27408 1.01978 -0.09119 0.09842  -0.12677 102 LEU B CB    
1769 C  CG    . LEU B 102 ? 1.10103 1.33617 1.04895 -0.07005 0.07346  -0.12400 102 LEU B CG    
1770 C  CD1   . LEU B 102 ? 1.08231 1.38346 1.03221 -0.08356 0.05728  -0.14462 102 LEU B CD1   
1771 C  CD2   . LEU B 102 ? 1.02806 1.27542 1.00271 -0.06715 0.07538  -0.12005 102 LEU B CD2   
1772 N  N     . GLY B 103 ? 1.21790 1.27519 1.05500 -0.16936 0.15735  -0.16137 103 GLY B N     
1773 C  CA    . GLY B 103 ? 1.24874 1.24662 1.03983 -0.18940 0.17923  -0.17299 103 GLY B CA    
1774 C  C     . GLY B 103 ? 1.38593 1.41328 1.15648 -0.23305 0.17734  -0.20504 103 GLY B C     
1775 O  O     . GLY B 103 ? 1.36478 1.46306 1.16271 -0.24859 0.16074  -0.21762 103 GLY B O     
1776 N  N     . ASN B 104 ? 1.49504 1.46824 1.21666 -0.25386 0.19554  -0.21940 104 ASN B N     
1777 C  CA    . ASN B 104 ? 1.58445 1.57664 1.27796 -0.30134 0.19515  -0.25248 104 ASN B CA    
1778 C  C     . ASN B 104 ? 1.61999 1.54743 1.28215 -0.34059 0.22783  -0.26723 104 ASN B C     
1779 O  O     . ASN B 104 ? 1.50157 1.41356 1.12429 -0.38391 0.23693  -0.29559 104 ASN B O     
1780 C  CB    . ASN B 104 ? 1.51298 1.48808 1.16285 -0.30351 0.19185  -0.26299 104 ASN B CB    
1781 C  CG    . ASN B 104 ? 1.61387 1.48258 1.21656 -0.29577 0.22691  -0.25663 104 ASN B CG    
1782 O  OD1   . ASN B 104 ? 1.64323 1.46178 1.25789 -0.27119 0.24623  -0.23443 104 ASN B OD1   
1783 N  ND2   . ASN B 104 ? 1.77604 1.61109 1.32387 -0.31565 0.23528  -0.27616 104 ASN B ND2   
1784 N  N     . GLU B 105 ? 1.65739 1.54388 1.33204 -0.32765 0.24541  -0.24858 105 GLU B N     
1785 C  CA    . GLU B 105 ? 1.76462 1.57142 1.40163 -0.35805 0.28028  -0.25660 105 GLU B CA    
1786 C  C     . GLU B 105 ? 1.72748 1.54709 1.39507 -0.35636 0.28335  -0.24350 105 GLU B C     
1787 O  O     . GLU B 105 ? 1.59759 1.45265 1.30620 -0.31865 0.26632  -0.21990 105 GLU B O     
1788 C  CB    . GLU B 105 ? 1.87117 1.57259 1.46708 -0.33504 0.30944  -0.24181 105 GLU B CB    
1789 C  CG    . GLU B 105 ? 2.04940 1.65301 1.59782 -0.36072 0.34850  -0.24758 105 GLU B CG    
1790 C  CD    . GLU B 105 ? 2.24280 1.78111 1.79451 -0.31862 0.36624  -0.21340 105 GLU B CD    
1791 O  OE1   . GLU B 105 ? 2.28026 1.81955 1.85141 -0.27328 0.35907  -0.19099 105 GLU B OE1   
1792 O  OE2   . GLU B 105 ? 2.25731 1.74595 1.79243 -0.33129 0.38680  -0.20824 105 GLU B OE2   
1793 N  N     . GLU B 106 ? 1.69799 1.48331 1.34004 -0.39976 0.30692  -0.25965 106 GLU B N     
1794 C  CA    . GLU B 106 ? 1.52748 1.32824 1.19170 -0.40728 0.31210  -0.25185 106 GLU B CA    
1795 C  C     . GLU B 106 ? 1.54773 1.29313 1.21394 -0.36247 0.32006  -0.21590 106 GLU B C     
1796 O  O     . GLU B 106 ? 1.59995 1.26731 1.23722 -0.33855 0.33574  -0.20038 106 GLU B O     
1797 C  CB    . GLU B 106 ? 1.56388 1.32001 1.18928 -0.46519 0.34231  -0.27510 106 GLU B CB    
1798 N  N     . VAL B 107 ? 1.35122 1.14122 1.05255 -0.35081 0.30883  -0.20306 107 VAL B N     
1799 C  CA    . VAL B 107 ? 1.33061 1.08358 1.03702 -0.31121 0.31000  -0.16991 107 VAL B CA    
1800 C  C     . VAL B 107 ? 1.47449 1.21720 1.17308 -0.33287 0.32454  -0.16812 107 VAL B C     
1801 O  O     . VAL B 107 ? 1.44920 1.25089 1.16442 -0.36681 0.32305  -0.18926 107 VAL B O     
1802 C  CB    . VAL B 107 ? 1.39279 1.21207 1.14836 -0.26723 0.27667  -0.15269 107 VAL B CB    
1803 C  CG1   . VAL B 107 ? 1.31216 1.09017 1.06980 -0.22823 0.27628  -0.11919 107 VAL B CG1   
1804 C  CG2   . VAL B 107 ? 1.20974 1.04945 0.97230 -0.25228 0.26238  -0.15784 107 VAL B CG2   
1805 N  N     . VAL B 108 ? 1.38497 1.05426 1.05791 -0.31240 0.33915  -0.14191 108 VAL B N     
1806 C  CA    . VAL B 108 ? 1.39635 1.04225 1.05176 -0.32796 0.35435  -0.13473 108 VAL B CA    
1807 C  C     . VAL B 108 ? 1.50103 1.14274 1.16937 -0.28241 0.33857  -0.10143 108 VAL B C     
1808 O  O     . VAL B 108 ? 1.48982 1.08903 1.15257 -0.24549 0.33485  -0.07830 108 VAL B O     
1809 C  CB    . VAL B 108 ? 1.49810 1.03862 1.09000 -0.35691 0.39349  -0.13662 108 VAL B CB    
1810 C  CG1   . VAL B 108 ? 1.46125 0.96020 1.02667 -0.36006 0.40871  -0.11851 108 VAL B CG1   
1811 C  CG2   . VAL B 108 ? 1.45473 1.00757 1.03307 -0.41454 0.40949  -0.17413 108 VAL B CG2   
1812 N  N     . ILE B 109 ? 1.46195 1.15029 1.14791 -0.28591 0.32972  -0.09996 109 ILE B N     
1813 C  CA    . ILE B 109 ? 1.45024 1.13440 1.14095 -0.25041 0.31484  -0.07163 109 ILE B CA    
1814 C  C     . ILE B 109 ? 1.54452 1.16875 1.18818 -0.26826 0.33905  -0.06169 109 ILE B C     
1815 O  O     . ILE B 109 ? 1.47688 1.12186 1.11430 -0.30595 0.35458  -0.08044 109 ILE B O     
1816 C  CB    . ILE B 109 ? 1.30841 1.08500 1.04843 -0.23687 0.28626  -0.07695 109 ILE B CB    
1817 C  CG1   . ILE B 109 ? 1.28793 1.10495 1.06588 -0.20785 0.26070  -0.07573 109 ILE B CG1   
1818 C  CG2   . ILE B 109 ? 1.13455 0.90188 0.86629 -0.21591 0.27735  -0.05461 109 ILE B CG2   
1819 C  CD1   . ILE B 109 ? 1.28704 1.05725 1.05942 -0.16998 0.25281  -0.04714 109 ILE B CD1   
1820 N  N     . GLU B 110 ? 1.68924 1.24140 1.30010 -0.24075 0.34264  -0.03134 110 GLU B N     
1821 C  CA    . GLU B 110 ? 1.64796 1.12854 1.20352 -0.25273 0.36593  -0.01664 110 GLU B CA    
1822 C  C     . GLU B 110 ? 1.66949 1.18275 1.22843 -0.24107 0.34960  -0.00377 110 GLU B C     
1823 O  O     . GLU B 110 ? 1.71698 1.30029 1.31995 -0.22005 0.32007  -0.00417 110 GLU B O     
1824 C  CB    . GLU B 110 ? 1.77963 1.16530 1.29493 -0.22451 0.37698  0.01219  110 GLU B CB    
1825 C  CG    . GLU B 110 ? 1.97541 1.32469 1.48677 -0.22758 0.39232  0.00105  110 GLU B CG    
1826 C  CD    . GLU B 110 ? 2.32314 1.57532 1.79437 -0.19578 0.40762  0.03023  110 GLU B CD    
1827 O  OE1   . GLU B 110 ? 2.49802 1.70121 1.93411 -0.17990 0.41105  0.05768  110 GLU B OE1   
1828 O  OE2   . GLU B 110 ? 2.36350 1.58794 1.83657 -0.18482 0.41666  0.02631  110 GLU B OE2   
1829 N  N     . ARG B 111 ? 1.55335 1.00807 1.05868 -0.25603 0.37106  0.00759  111 ARG B N     
1830 C  CA    . ARG B 111 ? 1.60790 1.08060 1.10234 -0.24751 0.35950  0.02010  111 ARG B CA    
1831 C  C     . ARG B 111 ? 1.60559 1.06491 1.10028 -0.19846 0.32934  0.05324  111 ARG B C     
1832 O  O     . ARG B 111 ? 1.60782 1.00107 1.07578 -0.17586 0.33272  0.07766  111 ARG B O     
1833 C  CB    . ARG B 111 ? 1.70100 1.10681 1.12975 -0.27807 0.39332  0.02479  111 ARG B CB    
1834 N  N     . GLY B 112 ? 1.48222 1.00529 1.00789 -0.18209 0.30030  0.05360  112 GLY B N     
1835 C  CA    . GLY B 112 ? 1.47935 1.00121 1.00984 -0.14119 0.26871  0.08190  112 GLY B CA    
1836 C  C     . GLY B 112 ? 1.48031 1.01960 1.05565 -0.11188 0.25028  0.08896  112 GLY B C     
1837 O  O     . GLY B 112 ? 1.41411 0.93757 0.98946 -0.07869 0.23079  0.11661  112 GLY B O     
1838 N  N     . GLU B 113 ? 1.44229 1.01650 1.05577 -0.12346 0.25590  0.06507  113 GLU B N     
1839 C  CA    . GLU B 113 ? 1.40085 0.99225 1.05472 -0.09774 0.24163  0.06988  113 GLU B CA    
1840 C  C     . GLU B 113 ? 1.23482 0.90084 0.93821 -0.08124 0.20874  0.06632  113 GLU B C     
1841 O  O     . GLU B 113 ? 1.18963 0.90505 0.90796 -0.09695 0.20358  0.04624  113 GLU B O     
1842 C  CB    . GLU B 113 ? 1.40707 0.99497 1.06971 -0.11868 0.26287  0.04612  113 GLU B CB    
1843 C  CG    . GLU B 113 ? 1.44879 1.04796 1.14607 -0.09371 0.25324  0.05001  113 GLU B CG    
1844 C  CD    . GLU B 113 ? 1.46174 1.04720 1.15501 -0.11636 0.27548  0.02634  113 GLU B CD    
1845 O  OE1   . GLU B 113 ? 1.48890 1.03408 1.14445 -0.14898 0.30231  0.01299  113 GLU B OE1   
1846 O  OE2   . GLU B 113 ? 1.33428 0.94764 1.05889 -0.10386 0.26667  0.02054  113 GLU B OE2   
1847 N  N     . ARG B 114 ? 1.29944 0.97222 1.02823 -0.04920 0.18829  0.08621  114 ARG B N     
1848 C  CA    . ARG B 114 ? 1.20357 0.93778 0.97576 -0.03457 0.15832  0.08490  114 ARG B CA    
1849 C  C     . ARG B 114 ? 1.08712 0.86455 0.89595 -0.04256 0.15985  0.06075  114 ARG B C     
1850 O  O     . ARG B 114 ? 1.25338 1.02112 1.07633 -0.03493 0.16751  0.06109  114 ARG B O     
1851 C  CB    . ARG B 114 ? 1.20291 0.93385 0.99351 -0.00201 0.13834  0.11325  114 ARG B CB    
1852 C  CG    . ARG B 114 ? 1.28139 0.97026 1.03334 0.00929  0.13413  0.14011  114 ARG B CG    
1853 C  CD    . ARG B 114 ? 1.37356 1.08009 1.15277 0.04068  0.10687  0.16725  114 ARG B CD    
1854 N  NE    . ARG B 114 ? 1.34001 1.03573 1.14688 0.06259  0.11649  0.17863  114 ARG B NE    
1855 C  CZ    . ARG B 114 ? 1.49199 1.13709 1.27814 0.08234  0.12988  0.20129  114 ARG B CZ    
1856 N  NH1   . ARG B 114 ? 1.50558 1.10259 1.23988 0.08263  0.13436  0.21691  114 ARG B NH1   
1857 N  NH2   . ARG B 114 ? 1.45487 1.09392 1.26993 0.10397  0.14086  0.20923  114 ARG B NH2   
1858 N  N     . ILE B 115 ? 1.02746 0.85146 0.84908 -0.05605 0.15317  0.04037  115 ILE B N     
1859 C  CA    . ILE B 115 ? 1.03689 0.90371 0.88707 -0.06504 0.15470  0.01685  115 ILE B CA    
1860 C  C     . ILE B 115 ? 0.90348 0.81746 0.79035 -0.04693 0.12980  0.01606  115 ILE B C     
1861 O  O     . ILE B 115 ? 0.98262 0.92815 0.89247 -0.04738 0.12797  0.00198  115 ILE B O     
1862 C  CB    . ILE B 115 ? 1.05978 0.94878 0.90045 -0.09432 0.16992  -0.00796 115 ILE B CB    
1863 C  CG1   . ILE B 115 ? 1.06613 0.97471 0.89999 -0.09479 0.16177  -0.00881 115 ILE B CG1   
1864 C  CG2   . ILE B 115 ? 1.15390 0.99317 0.95802 -0.11877 0.19877  -0.01100 115 ILE B CG2   
1865 C  CD1   . ILE B 115 ? 1.02075 0.96760 0.85798 -0.11896 0.17576  -0.03398 115 ILE B CD1   
1866 N  N     . ALA B 116 ? 0.88247 0.79952 0.77140 -0.03262 0.11069  0.03033  116 ALA B N     
1867 C  CA    . ALA B 116 ? 0.85202 0.80489 0.76991 -0.01862 0.08899  0.02926  116 ALA B CA    
1868 C  C     . ALA B 116 ? 0.95727 0.89859 0.87061 -0.00640 0.06968  0.04959  116 ALA B C     
1869 O  O     . ALA B 116 ? 0.99636 0.90623 0.88634 -0.00542 0.07154  0.06574  116 ALA B O     
1870 C  CB    . ALA B 116 ? 0.87797 0.86791 0.80080 -0.02648 0.08799  0.00729  116 ALA B CB    
1871 N  N     . GLN B 117 ? 0.88444 0.85013 0.81774 0.00231  0.05045  0.04898  117 GLN B N     
1872 C  CA    . GLN B 117 ? 0.94163 0.90301 0.87141 0.00881  0.02904  0.06443  117 GLN B CA    
1873 C  C     . GLN B 117 ? 0.85496 0.83370 0.78303 0.00636  0.01667  0.05102  117 GLN B C     
1874 O  O     . GLN B 117 ? 0.83400 0.83227 0.78313 0.01071  0.01637  0.03983  117 GLN B O     
1875 C  CB    . GLN B 117 ? 0.99334 0.95965 0.95473 0.02303  0.01789  0.08364  117 GLN B CB    
1876 C  CG    . GLN B 117 ? 0.97520 0.96142 0.96963 0.02893  0.02100  0.07694  117 GLN B CG    
1877 C  CD    . GLN B 117 ? 1.06799 1.06144 1.09499 0.04143  0.01333  0.09615  117 GLN B CD    
1878 O  OE1   . GLN B 117 ? 1.03184 1.03039 1.06586 0.04477  -0.00406 0.11176  117 GLN B OE1   
1879 N  NE2   . GLN B 117 ? 1.07720 1.07425 1.12431 0.04763  0.02647  0.09478  117 GLN B NE2   
1880 N  N     . LEU B 118 ? 0.83345 0.80000 0.73116 0.00034  0.00757  0.05247  118 LEU B N     
1881 C  CA    . LEU B 118 ? 0.83823 0.81070 0.72556 -0.00210 -0.00255 0.03957  118 LEU B CA    
1882 C  C     . LEU B 118 ? 0.90529 0.87851 0.80353 0.00070  -0.02770 0.05187  118 LEU B C     
1883 O  O     . LEU B 118 ? 0.87471 0.84034 0.76434 -0.00054 -0.04187 0.06944  118 LEU B O     
1884 C  CB    . LEU B 118 ? 0.86948 0.82508 0.71146 -0.01285 0.00377  0.03178  118 LEU B CB    
1885 C  CG    . LEU B 118 ? 0.89131 0.84254 0.71158 -0.01545 -0.00500 0.01855  118 LEU B CG    
1886 C  CD1   . LEU B 118 ? 0.87384 0.84373 0.70760 -0.00987 0.01033  -0.00373 118 LEU B CD1   
1887 C  CD2   . LEU B 118 ? 0.88738 0.81346 0.65496 -0.02663 -0.00420 0.01920  118 LEU B CD2   
1888 N  N     . VAL B 119 ? 0.85432 0.83731 0.77104 0.00400  -0.03339 0.04323  119 VAL B N     
1889 C  CA    . VAL B 119 ? 0.86432 0.84912 0.79438 0.00170  -0.05477 0.05200  119 VAL B CA    
1890 C  C     . VAL B 119 ? 0.90532 0.87371 0.80491 -0.00620 -0.06213 0.03656  119 VAL B C     
1891 O  O     . VAL B 119 ? 0.97039 0.93428 0.86271 -0.00081 -0.04915 0.01924  119 VAL B O     
1892 C  CB    . VAL B 119 ? 0.81890 0.81870 0.79080 0.00977  -0.05241 0.05629  119 VAL B CB    
1893 C  CG1   . VAL B 119 ? 0.80959 0.81175 0.79553 0.00254  -0.07173 0.06317  119 VAL B CG1   
1894 C  CG2   . VAL B 119 ? 0.77110 0.78154 0.76823 0.01779  -0.04297 0.07062  119 VAL B CG2   
1895 N  N     . ILE B 120 ? 0.91974 0.87921 0.80026 -0.01812 -0.08301 0.04260  120 ILE B N     
1896 C  CA    . ILE B 120 ? 1.00867 0.94455 0.85284 -0.02900 -0.09075 0.02721  120 ILE B CA    
1897 C  C     . ILE B 120 ? 1.02028 0.95630 0.88681 -0.03554 -0.10424 0.02837  120 ILE B C     
1898 O  O     . ILE B 120 ? 1.02106 0.97635 0.91408 -0.04292 -0.12225 0.04456  120 ILE B O     
1899 C  CB    . ILE B 120 ? 0.99019 0.91210 0.78943 -0.04260 -0.10606 0.03061  120 ILE B CB    
1900 C  CG1   . ILE B 120 ? 0.90404 0.82111 0.67872 -0.03777 -0.08930 0.03185  120 ILE B CG1   
1901 C  CG2   . ILE B 120 ? 1.03246 0.92322 0.78670 -0.05530 -0.11098 0.01125  120 ILE B CG2   
1902 C  CD1   . ILE B 120 ? 0.91155 0.81973 0.67079 -0.03213 -0.06194 0.01004  120 ILE B CD1   
1903 N  N     . ALA B 121 ? 1.04938 0.96403 0.90576 -0.03244 -0.09431 0.01187  121 ALA B N     
1904 C  CA    . ALA B 121 ? 1.07382 0.97877 0.94610 -0.03902 -0.10118 0.01176  121 ALA B CA    
1905 C  C     . ALA B 121 ? 1.10020 0.96065 0.92748 -0.04563 -0.09859 -0.00851 121 ALA B C     
1906 O  O     . ALA B 121 ? 1.18852 1.03156 0.98320 -0.03587 -0.08429 -0.02344 121 ALA B O     
1907 C  CB    . ALA B 121 ? 1.01965 0.93727 0.93001 -0.02171 -0.08602 0.01637  121 ALA B CB    
1908 N  N     . PRO B 122 ? 1.17197 1.01168 0.99575 -0.06301 -0.11001 -0.01018 122 PRO B N     
1909 C  CA    . PRO B 122 ? 1.33771 1.12342 1.11346 -0.06922 -0.10439 -0.03052 122 PRO B CA    
1910 C  C     . PRO B 122 ? 1.33215 1.09569 1.10953 -0.04341 -0.08083 -0.03809 122 PRO B C     
1911 O  O     . PRO B 122 ? 1.34115 1.12296 1.15690 -0.03125 -0.07509 -0.02657 122 PRO B O     
1912 C  CB    . PRO B 122 ? 1.28595 1.05936 1.06330 -0.09988 -0.12391 -0.02790 122 PRO B CB    
1913 C  CG    . PRO B 122 ? 1.21585 1.04651 1.04026 -0.10959 -0.14363 -0.00630 122 PRO B CG    
1914 C  CD    . PRO B 122 ? 1.13944 1.00370 1.00036 -0.08112 -0.12848 0.00567  122 PRO B CD    
1915 N  N     . VAL B 123 ? 1.63108 1.35458 1.36408 -0.03335 -0.06679 -0.05719 123 VAL B N     
1916 C  CA    . VAL B 123 ? 1.65079 1.34988 1.37982 -0.00497 -0.04563 -0.06467 123 VAL B CA    
1917 C  C     . VAL B 123 ? 1.69072 1.32041 1.37660 -0.01476 -0.04272 -0.07697 123 VAL B C     
1918 O  O     . VAL B 123 ? 1.72596 1.32321 1.37178 -0.04107 -0.05221 -0.08797 123 VAL B O     
1919 C  CB    . VAL B 123 ? 1.67093 1.38234 1.38901 0.02121  -0.02667 -0.07671 123 VAL B CB    
1920 C  CG1   . VAL B 123 ? 1.57733 1.35155 1.34095 0.03284  -0.02472 -0.06505 123 VAL B CG1   
1921 C  CG2   . VAL B 123 ? 1.64203 1.33178 1.31207 0.00646  -0.02668 -0.09172 123 VAL B CG2   
1922 N  N     . GLN B 124 ? 1.58293 1.18562 1.27218 0.00602  -0.02933 -0.07508 124 GLN B N     
1923 C  CA    . GLN B 124 ? 1.61386 1.13898 1.25738 0.00213  -0.02070 -0.08634 124 GLN B CA    
1924 C  C     . GLN B 124 ? 1.57603 1.07357 1.19754 0.04415  0.00345  -0.09697 124 GLN B C     
1925 O  O     . GLN B 124 ? 1.51548 1.02990 1.16322 0.07542  0.01229  -0.08660 124 GLN B O     
1926 C  CB    . GLN B 124 ? 1.55752 1.06420 1.21820 -0.01028 -0.02437 -0.07237 124 GLN B CB    
1927 C  CG    . GLN B 124 ? 1.66783 1.08461 1.27581 -0.01962 -0.01404 -0.08372 124 GLN B CG    
1928 C  CD    . GLN B 124 ? 1.76800 1.14445 1.32659 -0.05343 -0.02196 -0.10366 124 GLN B CD    
1929 O  OE1   . GLN B 124 ? 1.70586 1.04682 1.21991 -0.03920 -0.00954 -0.12193 124 GLN B OE1   
1930 N  NE2   . GLN B 124 ? 1.78166 1.16636 1.34793 -0.09879 -0.04262 -0.10071 124 GLN B NE2   
1931 N  N     . ARG B 125 ? 1.57057 1.02819 1.14364 0.04603  0.01401  -0.11739 125 ARG B N     
1932 C  CA    . ARG B 125 ? 1.63371 1.06373 1.18505 0.08782  0.03927  -0.12901 125 ARG B CA    
1933 C  C     . ARG B 125 ? 1.76391 1.10369 1.27178 0.09407  0.05119  -0.13355 125 ARG B C     
1934 O  O     . ARG B 125 ? 1.84432 1.11857 1.30250 0.06285  0.04922  -0.14633 125 ARG B O     
1935 C  CB    . ARG B 125 ? 1.57256 0.99885 1.08991 0.08814  0.04991  -0.14936 125 ARG B CB    
1936 C  CG    . ARG B 125 ? 1.52797 0.94825 1.03763 0.13531  0.07795  -0.16050 125 ARG B CG    
1937 C  CD    . ARG B 125 ? 1.54978 1.00319 1.05073 0.13598  0.08859  -0.17489 125 ARG B CD    
1938 N  NE    . ARG B 125 ? 1.58845 1.04970 1.09261 0.18216  0.11697  -0.18526 125 ARG B NE    
1939 C  CZ    . ARG B 125 ? 1.72795 1.12286 1.17992 0.19986  0.14099  -0.20442 125 ARG B CZ    
1940 N  NH1   . ARG B 125 ? 1.66248 0.97159 1.04825 0.17213  0.14018  -0.21741 125 ARG B NH1   
1941 N  NH2   . ARG B 125 ? 1.68653 1.10280 1.15328 0.24628  0.16698  -0.21147 125 ARG B NH2   
1942 N  N     . VAL B 126 ? 1.70036 1.03412 1.22314 0.13311  0.06308  -0.12291 126 VAL B N     
1943 C  CA    . VAL B 126 ? 1.72522 0.97079 1.20852 0.14166  0.07487  -0.12131 126 VAL B CA    
1944 C  C     . VAL B 126 ? 1.79759 0.98866 1.23948 0.18525  0.10167  -0.13584 126 VAL B C     
1945 O  O     . VAL B 126 ? 1.79060 1.03229 1.25375 0.21984  0.11131  -0.14083 126 VAL B O     
1946 C  CB    . VAL B 126 ? 1.77496 1.04037 1.29428 0.15735  0.07034  -0.09652 126 VAL B CB    
1947 C  CG1   . VAL B 126 ? 1.77134 1.07555 1.32516 0.11266  0.04865  -0.08346 126 VAL B CG1   
1948 C  CG2   . VAL B 126 ? 1.62382 0.96420 1.18806 0.20376  0.07331  -0.08763 126 VAL B CG2   
1949 N  N     . GLU B 127 ? 1.91704 1.00282 1.29940 0.18320  0.11572  -0.14302 127 GLU B N     
1950 C  CA    . GLU B 127 ? 1.91074 0.93046 1.25093 0.23153  0.14435  -0.15298 127 GLU B CA    
1951 C  C     . GLU B 127 ? 1.89654 0.91703 1.25774 0.27910  0.14999  -0.13010 127 GLU B C     
1952 O  O     . GLU B 127 ? 1.85293 0.84809 1.21472 0.26277  0.14147  -0.11293 127 GLU B O     
1953 C  CB    . GLU B 127 ? 1.97628 0.87058 1.23410 0.20713  0.15913  -0.17208 127 GLU B CB    
1954 N  N     . VAL B 128 ? 1.80068 0.85389 1.17949 0.33753  0.16415  -0.12935 128 VAL B N     
1955 C  CA    . VAL B 128 ? 1.90003 0.97277 1.30396 0.38820  0.16529  -0.10652 128 VAL B CA    
1956 C  C     . VAL B 128 ? 1.95069 0.93444 1.30577 0.41917  0.18695  -0.10381 128 VAL B C     
1957 O  O     . VAL B 128 ? 2.02126 0.98694 1.35672 0.43483  0.20520  -0.11910 128 VAL B O     
1958 C  CB    . VAL B 128 ? 1.78175 0.97187 1.25006 0.42763  0.16169  -0.10371 128 VAL B CB    
1959 C  CG1   . VAL B 128 ? 1.65202 0.86545 1.14317 0.47975  0.15905  -0.07994 128 VAL B CG1   
1960 C  CG2   . VAL B 128 ? 1.58211 0.87124 1.10437 0.38540  0.13877  -0.10314 128 VAL B CG2   
1961 N  N     . VAL B 129 ? 1.84404 0.78650 1.18608 0.42097  0.18374  -0.08174 129 VAL B N     
1962 C  CA    . VAL B 129 ? 2.11907 0.99156 1.42145 0.44447  0.20081  -0.07300 129 VAL B CA    
1963 C  C     . VAL B 129 ? 2.04705 0.95209 1.37375 0.47950  0.19212  -0.04277 129 VAL B C     
1964 O  O     . VAL B 129 ? 2.04414 0.97357 1.39061 0.46219  0.17581  -0.02797 129 VAL B O     
1965 C  CB    . VAL B 129 ? 2.06165 0.81871 1.29803 0.39618  0.21019  -0.08081 129 VAL B CB    
1966 N  N     . GLU B 130 ? 2.18368 1.08886 1.50690 0.52846  0.20291  -0.03349 130 GLU B N     
1967 C  CA    . GLU B 130 ? 2.18293 1.11681 1.52160 0.56406  0.19403  -0.00535 130 GLU B CA    
1968 C  C     . GLU B 130 ? 2.32717 1.15305 1.60398 0.55375  0.20545  0.00846  130 GLU B C     
1969 O  O     . GLU B 130 ? 2.43907 1.18003 1.66550 0.55509  0.22656  -0.00032 130 GLU B O     
1970 C  CB    . GLU B 130 ? 2.19595 1.19261 1.56562 0.62289  0.19741  -0.00131 130 GLU B CB    
1971 C  CG    . GLU B 130 ? 2.22550 1.26092 1.61124 0.66011  0.18441  0.02698  130 GLU B CG    
1972 C  CD    . GLU B 130 ? 2.22542 1.35787 1.66250 0.71124  0.17941  0.02948  130 GLU B CD    
1973 O  OE1   . GLU B 130 ? 2.17149 1.33830 1.63224 0.71874  0.18940  0.00945  130 GLU B OE1   
1974 O  OE2   . GLU B 130 ? 2.29761 1.47348 1.75107 0.74208  0.16560  0.05099  130 GLU B OE2   
1975 N  N     . VAL B 131 ? 2.24208 1.07056 1.52088 0.54257  0.19323  0.02963  131 VAL B N     
1976 C  CA    . VAL B 131 ? 2.24166 0.97366 1.46415 0.52880  0.20447  0.04425  131 VAL B CA    
1977 C  C     . VAL B 131 ? 2.32592 1.08583 1.55329 0.57314  0.19740  0.07234  131 VAL B C     
1978 O  O     . VAL B 131 ? 2.25033 1.10832 1.52763 0.60666  0.18057  0.07969  131 VAL B O     
1979 C  CB    . VAL B 131 ? 2.21056 0.90748 1.42252 0.46643  0.19991  0.04347  131 VAL B CB    
1980 C  CG1   . VAL B 131 ? 2.20948 0.87996 1.41371 0.42069  0.20388  0.01502  131 VAL B CG1   
1981 C  CG2   . VAL B 131 ? 2.16369 0.94815 1.42732 0.46291  0.17731  0.05786  131 VAL B CG2   
1982 N  N     . GLU B 132 ? 2.35129 1.02320 1.52356 0.57071  0.21037  0.08725  132 GLU B N     
1983 C  CA    . GLU B 132 ? 2.40531 1.08843 1.56934 0.60929  0.20477  0.11467  132 GLU B CA    
1984 C  C     . GLU B 132 ? 2.39679 1.02991 1.53048 0.57328  0.20592  0.13071  132 GLU B C     
1985 O  O     . GLU B 132 ? 2.36995 0.96532 1.49496 0.51830  0.21075  0.12053  132 GLU B O     
1986 C  CB    . GLU B 132 ? 2.50240 1.12508 1.62317 0.65598  0.22286  0.12097  132 GLU B CB    
1987 C  CG    . GLU B 132 ? 2.49984 1.21021 1.66264 0.71751  0.21194  0.12647  132 GLU B CG    
1988 C  CD    . GLU B 132 ? 2.59278 1.32475 1.77768 0.73063  0.22133  0.10275  132 GLU B CD    
1989 O  OE1   . GLU B 132 ? 2.61160 1.28945 1.77581 0.69143  0.23487  0.08130  132 GLU B OE1   
1990 O  OE2   . GLU B 132 ? 2.51642 1.32072 1.73904 0.77899  0.21542  0.10512  132 GLU B OE2   
1991 N  N     . VAL B 134 ? 2.61004 1.31085 1.81375 0.41601  0.17832  0.13651  134 VAL B N     
1992 C  CA    . VAL B 134 ? 2.47160 1.17548 1.69781 0.35872  0.17620  0.12234  134 VAL B CA    
1993 C  C     . VAL B 134 ? 2.55807 1.20785 1.76097 0.31114  0.18762  0.13381  134 VAL B C     
1994 O  O     . VAL B 134 ? 2.53473 1.14726 1.70346 0.32475  0.19703  0.15284  134 VAL B O     
1995 C  CB    . VAL B 134 ? 2.22694 1.03570 1.51640 0.36181  0.15414  0.11975  134 VAL B CB    
1996 N  N     . SER B 135 ? 2.61032 1.25886 1.83286 0.25451  0.18694  0.12215  135 SER B N     
1997 C  CA    . SER B 135 ? 2.65562 1.26076 1.86446 0.20229  0.19928  0.13026  135 SER B CA    
1998 C  C     . SER B 135 ? 2.50200 1.15304 1.73021 0.20949  0.19512  0.15458  135 SER B C     
1999 O  O     . SER B 135 ? 2.39408 1.12519 1.66273 0.23307  0.17799  0.15973  135 SER B O     
2000 C  CB    . SER B 135 ? 2.55626 1.16705 1.79194 0.13937  0.19580  0.11179  135 SER B CB    
2001 O  OG    . SER B 135 ? 2.54931 1.11422 1.76014 0.12826  0.19947  0.08737  135 SER B OG    
2002 N  N     . GLN B 136 ? 2.44929 1.04730 1.64506 0.18804  0.21231  0.16868  136 GLN B N     
2003 C  CA    . GLN B 136 ? 2.32205 0.95335 1.52834 0.18801  0.21280  0.19080  136 GLN B CA    
2004 C  C     . GLN B 136 ? 2.14795 0.82166 1.40262 0.13293  0.21192  0.18857  136 GLN B C     
2005 O  O     . GLN B 136 ? 2.14671 0.79086 1.40702 0.07999  0.22052  0.17607  136 GLN B O     
2006 C  CB    . GLN B 136 ? 2.35749 0.91199 1.50619 0.18740  0.23412  0.20662  136 GLN B CB    
2007 C  CG    . GLN B 136 ? 2.30422 0.86763 1.45988 0.15383  0.24506  0.22288  136 GLN B CG    
2008 C  CD    . GLN B 136 ? 2.28414 0.87581 1.42510 0.19657  0.23998  0.24501  136 GLN B CD    
2009 O  OE1   . GLN B 136 ? 2.13788 0.67772 1.22532 0.22803  0.24784  0.25746  136 GLN B OE1   
2010 N  NE2   . GLN B 136 ? 2.22216 0.89435 1.40749 0.19710  0.22694  0.24993  136 GLN B NE2   
2011 N  N     . THR B 137 ? 2.10107 0.84755 1.39158 0.14465  0.20136  0.20036  137 THR B N     
2012 C  CA    . THR B 137 ? 2.15421 0.95045 1.49554 0.09929  0.20113  0.20039  137 THR B CA    
2013 C  C     . THR B 137 ? 2.19843 1.02098 1.54200 0.10051  0.20961  0.22211  137 THR B C     
2014 O  O     . THR B 137 ? 2.16420 0.97168 1.46979 0.13851  0.21104  0.23609  137 THR B O     
2015 C  CB    . THR B 137 ? 2.17641 1.04324 1.56624 0.10952  0.17988  0.18886  137 THR B CB    
2016 O  OG1   . THR B 137 ? 2.18270 1.12349 1.63734 0.05958  0.17691  0.18301  137 THR B OG1   
2017 C  CG2   . THR B 137 ? 2.12923 1.05496 1.52596 0.16515  0.16464  0.19879  137 THR B CG2   
2018 N  N     . GLN B 138 ? 2.37483 1.23889 1.76332 0.05783  0.21587  0.22455  138 GLN B N     
2019 C  CA    . GLN B 138 ? 2.36858 1.26070 1.76174 0.05527  0.22748  0.24321  138 GLN B CA    
2020 C  C     . GLN B 138 ? 2.41587 1.37493 1.82460 0.09785  0.21040  0.24954  138 GLN B C     
2021 O  O     . GLN B 138 ? 2.34696 1.31498 1.73367 0.11666  0.21531  0.26454  138 GLN B O     
2022 C  CB    . GLN B 138 ? 2.26026 1.17980 1.70179 -0.00530 0.24373  0.24320  138 GLN B CB    
2023 N  N     . ARG B 139 ? 2.22349 1.25371 1.68024 0.10916  0.18597  0.23113  139 ARG B N     
2024 C  CA    . ARG B 139 ? 2.10611 1.21910 1.58819 0.14436  0.16616  0.22991  139 ARG B CA    
2025 C  C     . ARG B 139 ? 2.20847 1.28620 1.63260 0.20230  0.15800  0.24196  139 ARG B C     
2026 O  O     . ARG B 139 ? 2.13528 1.25747 1.55614 0.22875  0.14878  0.25006  139 ARG B O     
2027 C  CB    . ARG B 139 ? 1.95005 1.14575 1.49636 0.13922  0.14354  0.20596  139 ARG B CB    
2028 N  N     . GLY B 140 ? 2.37218 1.38435 1.75702 0.22025  0.15926  0.23963  140 GLY B N     
2029 C  CA    . GLY B 140 ? 2.31979 1.32698 1.66772 0.27165  0.14865  0.24554  140 GLY B CA    
2030 C  C     . GLY B 140 ? 2.18073 1.26312 1.55979 0.31086  0.12269  0.23566  140 GLY B C     
2031 O  O     . GLY B 140 ? 2.00395 1.10897 1.41654 0.30716  0.11469  0.21898  140 GLY B O     
2032 N  N     . GLU B 141 ? 2.11873 1.24219 1.48608 0.34698  0.10920  0.24506  141 GLU B N     
2033 C  CA    . GLU B 141 ? 2.04766 1.25261 1.44689 0.38266  0.08390  0.23550  141 GLU B CA    
2034 C  C     . GLU B 141 ? 1.91202 1.18874 1.34302 0.37287  0.07419  0.23622  141 GLU B C     
2035 O  O     . GLU B 141 ? 1.79816 1.15787 1.26895 0.38809  0.05387  0.22259  141 GLU B O     
2036 C  CB    . GLU B 141 ? 1.90974 1.12154 1.27852 0.42958  0.07214  0.24338  141 GLU B CB    
2037 N  N     . LYS C 3   ? 1.42426 1.49420 1.72931 -0.46851 -0.14750 0.07250  3   LYS C N     
2038 C  CA    . LYS C 3   ? 1.45918 1.57839 1.82791 -0.44461 -0.12226 0.09462  3   LYS C CA    
2039 C  C     . LYS C 3   ? 1.41661 1.62340 1.84097 -0.40519 -0.13793 0.11133  3   LYS C C     
2040 O  O     . LYS C 3   ? 1.34415 1.62669 1.81065 -0.41890 -0.17026 0.11449  3   LYS C O     
2041 C  CB    . LYS C 3   ? 1.35034 1.51371 1.77821 -0.49264 -0.11224 0.09991  3   LYS C CB    
2042 N  N     . VAL C 4   ? 1.35983 1.55278 1.78030 -0.35625 -0.11514 0.12213  4   VAL C N     
2043 C  CA    . VAL C 4   ? 1.26033 1.51839 1.72325 -0.31549 -0.12299 0.13763  4   VAL C CA    
2044 C  C     . VAL C 4   ? 1.18167 1.46747 1.69318 -0.29318 -0.08943 0.15514  4   VAL C C     
2045 O  O     . VAL C 4   ? 1.21638 1.44549 1.69963 -0.29153 -0.05845 0.15379  4   VAL C O     
2046 C  CB    . VAL C 4   ? 1.15651 1.36676 1.55834 -0.27703 -0.12864 0.13061  4   VAL C CB    
2047 C  CG1   . VAL C 4   ? 1.07232 1.34884 1.51122 -0.24850 -0.14706 0.14395  4   VAL C CG1   
2048 C  CG2   . VAL C 4   ? 1.28851 1.43663 1.61965 -0.29905 -0.14685 0.10880  4   VAL C CG2   
2049 N  N     . ILE C 5   ? 1.08253 1.45303 1.66370 -0.27415 -0.09484 0.17224  5   ILE C N     
2050 C  CA    . ILE C 5   ? 0.97692 1.38033 1.60866 -0.25290 -0.06198 0.18864  5   ILE C CA    
2051 C  C     . ILE C 5   ? 0.99985 1.40796 1.62807 -0.20089 -0.05661 0.19756  5   ILE C C     
2052 O  O     . ILE C 5   ? 1.01775 1.44105 1.63724 -0.18484 -0.08314 0.19783  5   ILE C O     
2053 C  CB    . ILE C 5   ? 0.91612 1.41872 1.64268 -0.27585 -0.06463 0.20208  5   ILE C CB    
2054 C  CG1   . ILE C 5   ? 0.86022 1.44572 1.63623 -0.26003 -0.09917 0.21289  5   ILE C CG1   
2055 C  CG2   . ILE C 5   ? 0.98366 1.48184 1.71252 -0.33475 -0.07099 0.19100  5   ILE C CG2   
2056 C  CD1   . ILE C 5   ? 0.95137 1.64762 1.83008 -0.27460 -0.10271 0.22852  5   ILE C CD1   
2057 N  N     . LEU C 6   ? 1.02109 1.41051 1.65024 -0.17656 -0.02063 0.20435  6   LEU C N     
2058 C  CA    . LEU C 6   ? 0.92755 1.31383 1.55039 -0.13082 -0.00876 0.21122  6   LEU C CA    
2059 C  C     . LEU C 6   ? 0.93437 1.37475 1.62380 -0.11579 0.01946  0.22811  6   LEU C C     
2060 O  O     . LEU C 6   ? 1.01261 1.43591 1.70428 -0.12401 0.05121  0.22959  6   LEU C O     
2061 C  CB    . LEU C 6   ? 0.94356 1.24552 1.48984 -0.11367 0.00867  0.19975  6   LEU C CB    
2062 C  CG    . LEU C 6   ? 0.92312 1.21299 1.45659 -0.07296 0.02774  0.20392  6   LEU C CG    
2063 C  CD1   . LEU C 6   ? 0.88808 1.20259 1.42754 -0.05170 0.00555  0.20684  6   LEU C CD1   
2064 C  CD2   . LEU C 6   ? 0.86809 1.08307 1.32926 -0.06286 0.04153  0.19163  6   LEU C CD2   
2065 N  N     . LYS C 7   ? 0.84284 1.34499 1.58318 -0.09218 0.00967  0.24153  7   LYS C N     
2066 C  CA    . LYS C 7   ? 0.91299 1.47103 1.72126 -0.07237 0.03706  0.25828  7   LYS C CA    
2067 C  C     . LYS C 7   ? 0.84136 1.35216 1.61349 -0.03252 0.06685  0.25881  7   LYS C C     
2068 O  O     . LYS C 7   ? 0.88712 1.37331 1.62521 -0.00762 0.05451  0.25684  7   LYS C O     
2069 C  CB    . LYS C 7   ? 0.86173 1.50995 1.74361 -0.06249 0.01193  0.27424  7   LYS C CB    
2070 N  N     . ILE C 8   ? 0.92442 1.42046 1.70034 -0.02921 0.10686  0.26074  8   ILE C N     
2071 C  CA    . ILE C 8   ? 0.86547 1.31348 1.60201 0.00307  0.13779  0.25890  8   ILE C CA    
2072 C  C     . ILE C 8   ? 0.94649 1.44129 1.74500 0.02205  0.17339  0.27344  8   ILE C C     
2073 O  O     . ILE C 8   ? 0.98097 1.51097 1.82375 0.00182  0.19211  0.27918  8   ILE C O     
2074 C  CB    . ILE C 8   ? 0.86027 1.23081 1.52264 -0.00852 0.15439  0.24528  8   ILE C CB    
2075 C  CG1   . ILE C 8   ? 0.94717 1.27484 1.55365 -0.02521 0.12140  0.23124  8   ILE C CG1   
2076 C  CG2   . ILE C 8   ? 0.92240 1.24719 1.54095 0.02206  0.18204  0.24164  8   ILE C CG2   
2077 C  CD1   . ILE C 8   ? 0.98114 1.23546 1.51587 -0.03154 0.13425  0.21986  8   ILE C CD1   
2078 N  N     . LYS C 9   ? 0.88989 1.38215 1.69001 0.06025  0.18537  0.27895  9   LYS C N     
2079 C  CA    . LYS C 9   ? 0.81251 1.33602 1.66088 0.08590  0.22459  0.29113  9   LYS C CA    
2080 C  C     . LYS C 9   ? 0.91829 1.36562 1.69805 0.10352  0.25986  0.28076  9   LYS C C     
2081 O  O     . LYS C 9   ? 0.94330 1.34035 1.66760 0.12036  0.25176  0.27224  9   LYS C O     
2082 C  CB    . LYS C 9   ? 0.72778 1.30533 1.63174 0.11903  0.21330  0.30701  9   LYS C CB    
2083 N  N     . ARG C 10  ? 0.93801 1.37719 1.71932 0.09710  0.29898  0.28097  10  ARG C N     
2084 C  CA    . ARG C 10  ? 0.91556 1.28199 1.62519 0.10833  0.33170  0.27006  10  ARG C CA    
2085 C  C     . ARG C 10  ? 0.95934 1.32951 1.68822 0.14568  0.36704  0.27611  10  ARG C C     
2086 O  O     . ARG C 10  ? 1.05850 1.46658 1.83347 0.15151  0.38448  0.28363  10  ARG C O     
2087 C  CB    . ARG C 10  ? 1.00885 1.35505 1.69821 0.08275  0.35738  0.26775  10  ARG C CB    
2088 C  CG    . ARG C 10  ? 1.02618 1.35446 1.68726 0.04763  0.32703  0.26163  10  ARG C CG    
2089 C  CD    . ARG C 10  ? 1.11377 1.40041 1.73362 0.02658  0.35473  0.25967  10  ARG C CD    
2090 N  NE    . ARG C 10  ? 1.12428 1.46216 1.80985 0.01078  0.38420  0.27201  10  ARG C NE    
2091 C  CZ    . ARG C 10  ? 1.19493 1.50538 1.85657 -0.01206 0.41175  0.27385  10  ARG C CZ    
2092 N  NH1   . ARG C 10  ? 1.20781 1.43911 1.77975 -0.01874 0.41196  0.26581  10  ARG C NH1   
2093 N  NH2   . ARG C 10  ? 1.09652 1.45913 1.82161 -0.02776 0.43739  0.28334  10  ARG C NH2   
2094 N  N     . LEU C 11  ? 1.00548 1.31891 1.67545 0.16634  0.36773  0.26611  11  LEU C N     
2095 C  CA    . LEU C 11  ? 0.97727 1.26707 1.63789 0.19818  0.39892  0.26617  11  LEU C CA    
2096 C  C     . LEU C 11  ? 1.04714 1.30265 1.67448 0.19432  0.44045  0.25924  11  LEU C C     
2097 O  O     . LEU C 11  ? 1.13880 1.37668 1.73687 0.17082  0.44846  0.25412  11  LEU C O     
2098 C  CB    . LEU C 11  ? 0.99090 1.22282 1.59235 0.21465  0.39452  0.25546  11  LEU C CB    
2099 C  CG    . LEU C 11  ? 0.88614 1.13896 1.51049 0.22724  0.35869  0.26311  11  LEU C CG    
2100 C  CD1   . LEU C 11  ? 0.85983 1.04348 1.41678 0.24208  0.36222  0.25082  11  LEU C CD1   
2101 C  CD2   . LEU C 11  ? 0.73874 1.04842 1.43138 0.24515  0.35456  0.28123  11  LEU C CD2   
2102 N  N     . PRO C 12  ? 1.10782 1.35042 1.73569 0.21739  0.46769  0.25997  12  PRO C N     
2103 C  CA    . PRO C 12  ? 1.14805 1.35851 1.74398 0.21423  0.50767  0.25338  12  PRO C CA    
2104 C  C     . PRO C 12  ? 1.23951 1.37908 1.74643 0.20050  0.52048  0.23709  12  PRO C C     
2105 O  O     . PRO C 12  ? 1.23644 1.36040 1.71910 0.18578  0.54262  0.23422  12  PRO C O     
2106 C  CB    . PRO C 12  ? 1.15345 1.34656 1.75067 0.24589  0.53094  0.25466  12  PRO C CB    
2107 C  CG    . PRO C 12  ? 1.12820 1.38120 1.79475 0.26160  0.50329  0.27002  12  PRO C CG    
2108 C  CD    . PRO C 12  ? 1.14968 1.41140 1.81235 0.24708  0.46333  0.26940  12  PRO C CD    
2109 N  N     . HIS C 13  ? 1.16101 1.25819 1.61608 0.20414  0.50684  0.22625  13  HIS C N     
2110 C  CA    . HIS C 13  ? 1.17130 1.20966 1.54192 0.18985  0.51399  0.21064  13  HIS C CA    
2111 C  C     . HIS C 13  ? 1.14772 1.20001 1.51266 0.16363  0.48517  0.21249  13  HIS C C     
2112 O  O     . HIS C 13  ? 1.17903 1.18325 1.46858 0.15135  0.47245  0.19889  13  HIS C O     
2113 C  CB    . HIS C 13  ? 1.05847 1.04359 1.36937 0.20128  0.51147  0.19476  13  HIS C CB    
2114 C  CG    . HIS C 13  ? 1.26325 1.27040 1.60374 0.20786  0.47683  0.19799  13  HIS C CG    
2115 N  ND1   . HIS C 13  ? 1.34947 1.31867 1.65986 0.22288  0.47784  0.18891  13  HIS C ND1   
2116 C  CD2   . HIS C 13  ? 1.15064 1.20618 1.53841 0.19795  0.43673  0.20786  13  HIS C CD2   
2117 C  CE1   . HIS C 13  ? 1.10910 1.10359 1.44758 0.22318  0.44064  0.19464  13  HIS C CE1   
2118 N  NE2   . HIS C 13  ? 1.09516 1.14282 1.48000 0.20857  0.41453  0.20564  13  HIS C NE2   
2119 N  N     . ALA C 14  ? 1.15282 1.26496 1.58849 0.15260  0.46626  0.22678  14  ALA C N     
2120 C  CA    . ALA C 14  ? 1.11557 1.23068 1.53985 0.12418  0.43600  0.22706  14  ALA C CA    
2121 C  C     . ALA C 14  ? 1.14785 1.30919 1.63135 0.10631  0.45079  0.24168  14  ALA C C     
2122 O  O     . ALA C 14  ? 1.19165 1.35562 1.67221 0.08068  0.42818  0.24329  14  ALA C O     
2123 C  CB    . ALA C 14  ? 0.99662 1.12952 1.43455 0.11992  0.38646  0.22483  14  ALA C CB    
2124 N  N     . GLN C 15  ? 1.11004 1.30346 1.64232 0.11785  0.48571  0.25008  15  GLN C N     
2125 C  CA    . GLN C 15  ? 1.16040 1.39952 1.74657 0.09722  0.49349  0.25981  15  GLN C CA    
2126 C  C     . GLN C 15  ? 1.23206 1.42425 1.76053 0.07506  0.51719  0.25729  15  GLN C C     
2127 O  O     . GLN C 15  ? 1.23420 1.44907 1.78932 0.04690  0.51604  0.26433  15  GLN C O     
2128 C  CB    . GLN C 15  ? 1.22932 1.51031 1.87107 0.11678  0.51195  0.26434  15  GLN C CB    
2129 C  CG    . GLN C 15  ? 1.15337 1.48788 1.85846 0.13745  0.48551  0.27157  15  GLN C CG    
2130 C  CD    . GLN C 15  ? 1.26821 1.64572 2.02819 0.15823  0.50427  0.27836  15  GLN C CD    
2131 O  OE1   . GLN C 15  ? 1.31765 1.67754 2.06286 0.16099  0.54085  0.27539  15  GLN C OE1   
2132 N  NE2   . GLN C 15  ? 1.22966 1.66387 2.05122 0.17381  0.47908  0.28808  15  GLN C NE2   
2133 N  N     . ASP C 16  ? 1.19964 1.32383 1.64480 0.08574  0.53769  0.24705  16  ASP C N     
2134 C  CA    . ASP C 16  ? 1.27904 1.35186 1.65726 0.06737  0.55673  0.24577  16  ASP C CA    
2135 C  C     . ASP C 16  ? 1.20824 1.24310 1.53319 0.05132  0.53344  0.24676  16  ASP C C     
2136 O  O     . ASP C 16  ? 1.19317 1.19741 1.48185 0.03017  0.54037  0.25204  16  ASP C O     
2137 C  CB    . ASP C 16  ? 1.35644 1.37267 1.66264 0.08435  0.58554  0.23421  16  ASP C CB    
2138 C  CG    . ASP C 16  ? 1.46130 1.43892 1.71320 0.10288  0.57315  0.22156  16  ASP C CG    
2139 O  OD1   . ASP C 16  ? 1.31764 1.32621 1.61229 0.11464  0.55208  0.22163  16  ASP C OD1   
2140 O  OD2   . ASP C 16  ? 1.43084 1.34782 1.59536 0.10424  0.58347  0.21110  16  ASP C OD2   
2141 N  N     . LEU C 17  ? 1.23144 1.25965 1.54032 0.06195  0.49296  0.23647  17  LEU C N     
2142 C  CA    . LEU C 17  ? 1.17355 1.16585 1.42879 0.05067  0.45410  0.23049  17  LEU C CA    
2143 C  C     . LEU C 17  ? 1.14587 1.16894 1.44949 0.02588  0.43252  0.23926  17  LEU C C     
2144 O  O     . LEU C 17  ? 1.20861 1.29381 1.59525 0.02043  0.43097  0.24643  17  LEU C O     
2145 C  CB    . LEU C 17  ? 1.20747 1.19324 1.44250 0.06697  0.41978  0.21685  17  LEU C CB    
2146 C  CG    . LEU C 17  ? 1.27752 1.23120 1.46348 0.08726  0.43745  0.20481  17  LEU C CG    
2147 C  CD1   . LEU C 17  ? 1.10377 1.05758 1.28079 0.09786  0.40389  0.19202  17  LEU C CD1   
2148 C  CD2   . LEU C 17  ? 1.18675 1.08188 1.28333 0.08382  0.45134  0.19994  17  LEU C CD2   
2149 N  N     . PRO C 18  ? 1.15014 1.12985 1.40157 0.01078  0.41540  0.23877  18  PRO C N     
2150 C  CA    . PRO C 18  ? 1.25747 1.25471 1.54522 -0.01616 0.39747  0.24491  18  PRO C CA    
2151 C  C     . PRO C 18  ? 1.24218 1.27582 1.56966 -0.01474 0.35461  0.23829  18  PRO C C     
2152 O  O     . PRO C 18  ? 1.22060 1.24695 1.52522 0.00574  0.33320  0.22814  18  PRO C O     
2153 C  CB    . PRO C 18  ? 1.27738 1.20233 1.48195 -0.02485 0.39270  0.24528  18  PRO C CB    
2154 C  CG    . PRO C 18  ? 1.19357 1.07939 1.32715 0.00187  0.38538  0.23554  18  PRO C CG    
2155 C  CD    . PRO C 18  ? 1.16022 1.07119 1.31482 0.01807  0.41305  0.23327  18  PRO C CD    
2156 N  N     . LEU C 19  ? 1.31036 1.38309 1.69551 -0.03957 0.34286  0.24365  19  LEU C N     
2157 C  CA    . LEU C 19  ? 1.29789 1.40301 1.71583 -0.04236 0.30169  0.23793  19  LEU C CA    
2158 C  C     . LEU C 19  ? 1.36902 1.41752 1.71676 -0.03889 0.27180  0.22671  19  LEU C C     
2159 O  O     . LEU C 19  ? 1.45866 1.44868 1.74536 -0.04411 0.27942  0.22670  19  LEU C O     
2160 C  CB    . LEU C 19  ? 1.26895 1.42134 1.75197 -0.07562 0.29408  0.24430  19  LEU C CB    
2161 C  CG    . LEU C 19  ? 1.31648 1.55854 1.89648 -0.07541 0.29721  0.25297  19  LEU C CG    
2162 C  CD1   . LEU C 19  ? 1.24827 1.53343 1.88317 -0.11567 0.28705  0.25714  19  LEU C CD1   
2163 C  CD2   . LEU C 19  ? 1.24695 1.51862 1.84524 -0.04935 0.26749  0.24907  19  LEU C CD2   
2164 N  N     . PRO C 20  ? 1.35434 1.41863 1.70832 -0.02817 0.23901  0.21807  20  PRO C N     
2165 C  CA    . PRO C 20  ? 1.31882 1.33855 1.61704 -0.02694 0.21088  0.20721  20  PRO C CA    
2166 C  C     . PRO C 20  ? 1.31182 1.31003 1.60480 -0.05640 0.20224  0.20835  20  PRO C C     
2167 O  O     . PRO C 20  ? 1.30765 1.34635 1.65484 -0.08028 0.19498  0.21165  20  PRO C O     
2168 C  CB    . PRO C 20  ? 1.22581 1.27929 1.54760 -0.01505 0.18216  0.19972  20  PRO C CB    
2169 C  CG    . PRO C 20  ? 1.20301 1.29785 1.56758 0.00116  0.19965  0.20585  20  PRO C CG    
2170 C  CD    . PRO C 20  ? 1.28705 1.40584 1.69348 -0.01294 0.22905  0.21851  20  PRO C CD    
2171 N  N     . SER C 21  ? 1.36965 1.30254 1.59501 -0.05464 0.20289  0.20563  21  SER C N     
2172 C  CA    . SER C 21  ? 1.38998 1.28370 1.59578 -0.08089 0.19929  0.20634  21  SER C CA    
2173 C  C     . SER C 21  ? 1.33541 1.17205 1.47502 -0.06556 0.17908  0.19689  21  SER C C     
2174 O  O     . SER C 21  ? 1.37862 1.19649 1.47700 -0.03640 0.17748  0.19393  21  SER C O     
2175 C  CB    . SER C 21  ? 1.39299 1.25398 1.58221 -0.09714 0.23416  0.21884  21  SER C CB    
2176 O  OG    . SER C 21  ? 1.44356 1.36251 1.69786 -0.10888 0.25693  0.22745  21  SER C OG    
2177 N  N     . TYR C 22  ? 1.28961 1.10104 1.42038 -0.08577 0.16382  0.19132  22  TYR C N     
2178 C  CA    . TYR C 22  ? 1.33637 1.08665 1.40320 -0.07068 0.14999  0.18356  22  TYR C CA    
2179 C  C     . TYR C 22  ? 1.33806 1.02069 1.34311 -0.06111 0.17204  0.19398  22  TYR C C     
2180 O  O     . TYR C 22  ? 1.36375 1.02109 1.36647 -0.08535 0.19498  0.20437  22  TYR C O     
2181 C  CB    . TYR C 22  ? 1.37254 1.10316 1.43940 -0.09680 0.13306  0.17440  22  TYR C CB    
2182 C  CG    . TYR C 22  ? 1.29912 1.08854 1.41252 -0.10345 0.10664  0.16386  22  TYR C CG    
2183 C  CD1   . TYR C 22  ? 1.29274 1.08419 1.38694 -0.07904 0.08544  0.15214  22  TYR C CD1   
2184 C  CD2   . TYR C 22  ? 1.22627 1.07111 1.40226 -0.13416 0.10290  0.16649  22  TYR C CD2   
2185 C  CE1   . TYR C 22  ? 1.23318 1.07211 1.36202 -0.08526 0.06265  0.14402  22  TYR C CE1   
2186 C  CE2   . TYR C 22  ? 1.21886 1.11563 1.43171 -0.13821 0.07665  0.15917  22  TYR C CE2   
2187 C  CZ    . TYR C 22  ? 1.24798 1.13727 1.43328 -0.11387 0.05727  0.14827  22  TYR C CZ    
2188 O  OH    . TYR C 22  ? 1.15776 1.09273 1.37217 -0.11794 0.03253  0.14240  22  TYR C OH    
2189 N  N     . ALA C 23  ? 1.35473 1.01018 1.30944 -0.02613 0.16508  0.19194  23  ALA C N     
2190 C  CA    . ALA C 23  ? 1.37174 0.96423 1.26183 -0.01124 0.18225  0.20384  23  ALA C CA    
2191 C  C     . ALA C 23  ? 1.52582 1.04265 1.37400 -0.02594 0.18776  0.20791  23  ALA C C     
2192 O  O     . ALA C 23  ? 1.49722 0.96989 1.32196 -0.04316 0.21307  0.22125  23  ALA C O     
2193 C  CB    . ALA C 23  ? 1.17721 0.76706 1.02714 0.02981  0.16769  0.19984  23  ALA C CB    
2194 N  N     . THR C 24  ? 1.54670 1.04278 1.38141 -0.02023 0.16705  0.19616  24  THR C N     
2195 C  CA    . THR C 24  ? 1.57494 0.99092 1.36438 -0.03211 0.17184  0.19691  24  THR C CA    
2196 C  C     . THR C 24  ? 1.51569 0.94683 1.34537 -0.07289 0.16343  0.18450  24  THR C C     
2197 O  O     . THR C 24  ? 1.49076 0.99554 1.37831 -0.08164 0.14690  0.17475  24  THR C O     
2198 C  CB    . THR C 24  ? 1.54630 0.91877 1.28175 0.00869  0.15683  0.19207  24  THR C CB    
2199 O  OG1   . THR C 24  ? 1.55654 0.97458 1.32369 0.01425  0.13209  0.17350  24  THR C OG1   
2200 C  CG2   . THR C 24  ? 1.55479 0.93360 1.25950 0.04977  0.15718  0.20223  24  THR C CG2   
2201 N  N     . PRO C 25  ? 1.61437 0.97459 1.41137 -0.09997 0.17422  0.18471  25  PRO C N     
2202 C  CA    . PRO C 25  ? 1.55540 0.92944 1.38603 -0.14349 0.16394  0.17082  25  PRO C CA    
2203 C  C     . PRO C 25  ? 1.56683 0.96411 1.40456 -0.13106 0.13457  0.15177  25  PRO C C     
2204 O  O     . PRO C 25  ? 1.62298 1.04378 1.49069 -0.16603 0.12151  0.13950  25  PRO C O     
2205 C  CB    . PRO C 25  ? 1.61642 0.88825 1.38938 -0.16896 0.18355  0.17368  25  PRO C CB    
2206 C  CG    . PRO C 25  ? 1.65542 0.88445 1.39002 -0.15256 0.21071  0.19491  25  PRO C CG    
2207 C  CD    . PRO C 25  ? 1.62187 0.88692 1.35089 -0.09843 0.19922  0.19924  25  PRO C CD    
2208 N  N     . HIS C 26  ? 1.58521 0.97953 1.39633 -0.08427 0.12381  0.14869  26  HIS C N     
2209 C  CA    . HIS C 26  ? 1.57099 0.98738 1.38737 -0.07230 0.09977  0.13063  26  HIS C CA    
2210 C  C     . HIS C 26  ? 1.49872 0.97750 1.33563 -0.03311 0.08740  0.12981  26  HIS C C     
2211 O  O     . HIS C 26  ? 1.49216 0.96868 1.31114 -0.00682 0.07449  0.11848  26  HIS C O     
2212 C  CB    . HIS C 26  ? 1.63904 0.96685 1.38939 -0.05937 0.10120  0.12165  26  HIS C CB    
2213 C  CG    . HIS C 26  ? 1.72624 0.98434 1.45004 -0.10239 0.11283  0.11810  26  HIS C CG    
2214 N  ND1   . HIS C 26  ? 1.66173 0.94649 1.41806 -0.14966 0.10153  0.10509  26  HIS C ND1   
2215 C  CD2   . HIS C 26  ? 1.69796 0.85851 1.36288 -0.10720 0.13471  0.12573  26  HIS C CD2   
2216 C  CE1   . HIS C 26  ? 1.72096 0.92993 1.44149 -0.18528 0.11593  0.10276  26  HIS C CE1   
2217 N  NE2   . HIS C 26  ? 1.78831 0.91680 1.45163 -0.16034 0.13786  0.11541  26  HIS C NE2   
2218 N  N     . SER C 27  ? 1.44655 0.97971 1.31981 -0.03024 0.09327  0.14062  27  SER C N     
2219 C  CA    . SER C 27  ? 1.37365 0.96688 1.26871 -0.00122 0.08239  0.13784  27  SER C CA    
2220 C  C     . SER C 27  ? 1.33408 0.98857 1.27720 -0.01546 0.06362  0.12607  27  SER C C     
2221 O  O     . SER C 27  ? 1.29608 0.96496 1.26870 -0.04938 0.05948  0.12423  27  SER C O     
2222 C  CB    . SER C 27  ? 1.39870 1.02063 1.30943 0.00508  0.09753  0.15182  27  SER C CB    
2223 O  OG    . SER C 27  ? 1.48816 1.05325 1.34628 0.02228  0.11291  0.16374  27  SER C OG    
2224 N  N     . SER C 28  ? 1.32492 1.01665 1.27441 0.01000  0.05173  0.11856  28  SER C N     
2225 C  CA    . SER C 28  ? 1.21808 0.95881 1.20171 0.00105  0.03436  0.10825  28  SER C CA    
2226 C  C     . SER C 28  ? 1.19880 1.00340 1.23296 -0.00297 0.03530  0.11530  28  SER C C     
2227 O  O     . SER C 28  ? 1.09051 0.93396 1.15743 -0.01616 0.02225  0.11179  28  SER C O     
2228 C  CB    . SER C 28  ? 1.06144 0.80378 1.02241 0.02796  0.02333  0.09495  28  SER C CB    
2229 O  OG    . SER C 28  ? 1.30574 0.98937 1.22199 0.03479  0.02343  0.08743  28  SER C OG    
2230 N  N     . GLY C 29  ? 1.15775 0.97064 1.19505 0.00922  0.05094  0.12548  29  GLY C N     
2231 C  CA    . GLY C 29  ? 1.17449 1.04005 1.25276 0.01089  0.05523  0.13056  29  GLY C CA    
2232 C  C     . GLY C 29  ? 1.18723 1.05442 1.28018 0.00372  0.07788  0.14475  29  GLY C C     
2233 O  O     . GLY C 29  ? 1.22449 1.04905 1.28619 0.00265  0.09157  0.15125  29  GLY C O     
2234 N  N     . LEU C 30  ? 1.15472 1.06952 1.29386 0.00029  0.08361  0.15026  30  LEU C N     
2235 C  CA    . LEU C 30  ? 1.13885 1.06410 1.29799 -0.00340 0.10880  0.16277  30  LEU C CA    
2236 C  C     . LEU C 30  ? 1.12273 1.04404 1.25639 0.02100  0.12147  0.16171  30  LEU C C     
2237 O  O     . LEU C 30  ? 1.12415 1.05681 1.24821 0.03662  0.10985  0.15199  30  LEU C O     
2238 C  CB    . LEU C 30  ? 1.13560 1.11699 1.36156 -0.01673 0.11021  0.16988  30  LEU C CB    
2239 C  CG    . LEU C 30  ? 1.10714 1.10868 1.37194 -0.04737 0.10095  0.17362  30  LEU C CG    
2240 C  CD1   . LEU C 30  ? 1.24031 1.20705 1.49122 -0.06833 0.11985  0.18004  30  LEU C CD1   
2241 C  CD2   . LEU C 30  ? 1.16385 1.15895 1.41581 -0.05539 0.07071  0.16205  30  LEU C CD2   
2242 N  N     . ASP C 31  ? 1.23558 1.13961 1.35558 0.02141  0.14642  0.17101  31  ASP C N     
2243 C  CA    . ASP C 31  ? 1.13023 1.02735 1.21976 0.04108  0.15932  0.16914  31  ASP C CA    
2244 C  C     . ASP C 31  ? 1.11139 1.04944 1.24086 0.04594  0.16848  0.16824  31  ASP C C     
2245 O  O     . ASP C 31  ? 1.15400 1.12026 1.33242 0.03596  0.18201  0.17735  31  ASP C O     
2246 C  CB    . ASP C 31  ? 1.20114 1.06248 1.25683 0.03935  0.18487  0.17995  31  ASP C CB    
2247 C  CG    . ASP C 31  ? 1.48661 1.29614 1.48924 0.04160  0.17726  0.18230  31  ASP C CG    
2248 O  OD1   . ASP C 31  ? 1.48661 1.28154 1.49946 0.02511  0.17108  0.18484  31  ASP C OD1   
2249 O  OD2   . ASP C 31  ? 1.59405 1.37611 1.54264 0.06024  0.17709  0.18163  31  ASP C OD2   
2250 N  N     . LEU C 32  ? 1.03860 0.98001 1.14778 0.06144  0.16193  0.15732  32  LEU C N     
2251 C  CA    . LEU C 32  ? 0.93405 0.89939 1.06702 0.06868  0.17366  0.15526  32  LEU C CA    
2252 C  C     . LEU C 32  ? 1.09920 1.04151 1.19111 0.07790  0.19654  0.15262  32  LEU C C     
2253 O  O     . LEU C 32  ? 1.08411 1.00541 1.12560 0.08473  0.18779  0.14344  32  LEU C O     
2254 C  CB    . LEU C 32  ? 0.94623 0.92643 1.08201 0.07447  0.15215  0.14352  32  LEU C CB    
2255 C  CG    . LEU C 32  ? 1.00226 1.01570 1.19043 0.06994  0.14201  0.14862  32  LEU C CG    
2256 C  CD1   . LEU C 32  ? 0.95831 0.98463 1.17939 0.05425  0.13546  0.15906  32  LEU C CD1   
2257 C  CD2   . LEU C 32  ? 0.83191 0.84955 1.00916 0.07243  0.11844  0.13714  32  LEU C CD2   
2258 N  N     . ARG C 33  ? 1.07078 1.01933 1.18391 0.07852  0.22562  0.16028  33  ARG C N     
2259 C  CA    . ARG C 33  ? 1.12517 1.04686 1.19543 0.08477  0.25204  0.15823  33  ARG C CA    
2260 C  C     . ARG C 33  ? 1.09651 1.02257 1.17070 0.09457  0.26731  0.15003  33  ARG C C     
2261 O  O     . ARG C 33  ? 0.86620 0.81880 0.99047 0.09824  0.26898  0.15363  33  ARG C O     
2262 C  CB    . ARG C 33  ? 1.06484 0.97972 1.14547 0.07748  0.28163  0.17284  33  ARG C CB    
2263 C  CG    . ARG C 33  ? 1.13609 1.02206 1.18205 0.06856  0.27512  0.17964  33  ARG C CG    
2264 C  CD    . ARG C 33  ? 1.10757 0.97911 1.15226 0.05946  0.31009  0.19328  33  ARG C CD    
2265 N  NE    . ARG C 33  ? 1.14678 0.97017 1.12649 0.05728  0.31033  0.19841  33  ARG C NE    
2266 C  CZ    . ARG C 33  ? 1.16908 0.97481 1.14750 0.04445  0.30363  0.20773  33  ARG C CZ    
2267 N  NH1   . ARG C 33  ? 1.27135 1.10660 1.31022 0.02859  0.29493  0.21109  33  ARG C NH1   
2268 N  NH2   . ARG C 33  ? 1.15909 0.91328 1.07008 0.04726  0.30550  0.21396  33  ARG C NH2   
2269 N  N     . ALA C 34  ? 1.13367 1.03014 1.15028 0.09887  0.27830  0.13918  34  ALA C N     
2270 C  CA    . ALA C 34  ? 1.05485 0.94139 1.06027 0.10559  0.29664  0.12847  34  ALA C CA    
2271 C  C     . ALA C 34  ? 1.20489 1.08800 1.23232 0.11130  0.33732  0.13839  34  ALA C C     
2272 O  O     . ALA C 34  ? 1.06593 0.92451 1.05670 0.10979  0.36084  0.14040  34  ALA C O     
2273 C  CB    . ALA C 34  ? 1.04756 0.90478 0.98014 0.10371  0.29237  0.11126  34  ALA C CB    
2274 N  N     . ALA C 35  ? 1.08973 0.99814 1.17611 0.11957  0.34651  0.14543  35  ALA C N     
2275 C  CA    . ALA C 35  ? 1.07059 0.98552 1.19055 0.12938  0.38620  0.15598  35  ALA C CA    
2276 C  C     . ALA C 35  ? 1.06092 0.93830 1.14193 0.14093  0.41485  0.14307  35  ALA C C     
2277 O  O     . ALA C 35  ? 1.11436 0.99679 1.22755 0.15592  0.42905  0.14524  35  ALA C O     
2278 C  CB    . ALA C 35  ? 1.03409 1.00019 1.23946 0.13563  0.38044  0.17173  35  ALA C CB    
2279 N  N     . ILE C 36  ? 1.15975 0.99534 1.16551 0.13385  0.42318  0.12952  36  ILE C N     
2280 C  CA    . ILE C 36  ? 1.26709 1.05782 1.21935 0.13860  0.44934  0.11290  36  ILE C CA    
2281 C  C     . ILE C 36  ? 1.37926 1.13947 1.28629 0.13747  0.48551  0.11284  36  ILE C C     
2282 O  O     . ILE C 36  ? 1.35245 1.11759 1.24757 0.12909  0.48118  0.12186  36  ILE C O     
2283 C  CB    . ILE C 36  ? 1.35212 1.12117 1.24637 0.12668  0.42060  0.09152  36  ILE C CB    
2284 C  CG1   . ILE C 36  ? 1.57668 1.30004 1.42641 0.12865  0.44664  0.07302  36  ILE C CG1   
2285 C  CG2   . ILE C 36  ? 1.28532 1.04541 1.12233 0.11387  0.40184  0.08637  36  ILE C CG2   
2286 C  CD1   . ILE C 36  ? 1.54492 1.26894 1.44507 0.14628  0.46658  0.07985  36  ILE C CD1   
2287 N  N     . GLU C 37  ? 1.39173 1.11443 1.26914 0.14623  0.52404  0.10284  37  GLU C N     
2288 C  CA    . GLU C 37  ? 1.39319 1.08180 1.22317 0.14514  0.56002  0.10087  37  GLU C CA    
2289 C  C     . GLU C 37  ? 1.57538 1.22281 1.30565 0.12938  0.55061  0.08375  37  GLU C C     
2290 O  O     . GLU C 37  ? 1.53832 1.18165 1.23598 0.12152  0.54736  0.09104  37  GLU C O     
2291 C  CB    . GLU C 37  ? 1.24434 0.90595 1.08203 0.15811  0.58895  0.09481  37  GLU C CB    
2292 N  N     . LYS C 38  ? 1.58121 1.19801 1.26141 0.12301  0.54177  0.06085  38  LYS C N     
2293 C  CA    . LYS C 38  ? 1.60998 1.19363 1.19701 0.10613  0.52781  0.04188  38  LYS C CA    
2294 C  C     . LYS C 38  ? 1.55926 1.17634 1.14684 0.09509  0.47202  0.03944  38  LYS C C     
2295 O  O     . LYS C 38  ? 1.53359 1.18540 1.18083 0.09769  0.44769  0.04358  38  LYS C O     
2296 C  CB    . LYS C 38  ? 1.60748 1.14398 1.14391 0.09897  0.54156  0.01600  38  LYS C CB    
2297 N  N     . PRO C 39  ? 1.60825 1.21616 1.12905 0.08464  0.45167  0.03361  39  PRO C N     
2298 C  CA    . PRO C 39  ? 1.48093 1.12272 1.00082 0.07749  0.40007  0.02999  39  PRO C CA    
2299 C  C     . PRO C 39  ? 1.55485 1.20154 1.07139 0.06571  0.38288  0.00674  39  PRO C C     
2300 O  O     . PRO C 39  ? 1.55104 1.16082 1.01767 0.05503  0.40215  -0.01400 39  PRO C O     
2301 C  CB    . PRO C 39  ? 1.52136 1.14562 0.96010 0.07214  0.38881  0.02832  39  PRO C CB    
2302 C  CG    . PRO C 39  ? 1.55452 1.12668 0.93370 0.06918  0.43351  0.02034  39  PRO C CG    
2303 C  CD    . PRO C 39  ? 1.50538 1.07340 0.94864 0.08134  0.47510  0.03226  39  PRO C CD    
2304 N  N     . LEU C 40  ? 1.50577 1.19481 1.07286 0.06579  0.34847  0.00956  40  LEU C N     
2305 C  CA    . LEU C 40  ? 1.48291 1.18156 1.05639 0.05322  0.33237  -0.00986 40  LEU C CA    
2306 C  C     . LEU C 40  ? 1.51982 1.24260 1.05181 0.03873  0.29392  -0.02550 40  LEU C C     
2307 O  O     . LEU C 40  ? 1.60022 1.35348 1.13644 0.04627  0.26580  -0.01405 40  LEU C O     
2308 C  CB    . LEU C 40  ? 1.40346 1.13528 1.05606 0.06150  0.31959  0.00224  40  LEU C CB    
2309 C  CG    . LEU C 40  ? 1.32410 1.03550 1.01382 0.06893  0.34975  0.00517  40  LEU C CG    
2310 C  CD1   . LEU C 40  ? 1.34798 1.09726 1.11383 0.07971  0.33335  0.02303  40  LEU C CD1   
2311 C  CD2   . LEU C 40  ? 1.42529 1.10618 1.07814 0.05281  0.35719  -0.01962 40  LEU C CD2   
2312 N  N     . LYS C 41  ? 1.45471 1.16429 0.94770 0.01801  0.29325  -0.05167 41  LYS C N     
2313 C  CA    . LYS C 41  ? 1.53385 1.27640 0.99442 0.00076  0.25629  -0.06958 41  LYS C CA    
2314 C  C     . LYS C 41  ? 1.44843 1.22219 0.95211 -0.01159 0.23880  -0.08105 41  LYS C C     
2315 O  O     . LYS C 41  ? 1.46304 1.20619 0.97088 -0.02268 0.26162  -0.09238 41  LYS C O     
2316 C  CB    . LYS C 41  ? 1.51524 1.22317 0.89168 -0.02061 0.26643  -0.09382 41  LYS C CB    
2317 C  CG    . LYS C 41  ? 1.63763 1.31612 0.95835 -0.01049 0.28013  -0.08371 41  LYS C CG    
2318 C  CD    . LYS C 41  ? 1.58092 1.26381 0.82168 -0.02936 0.25753  -0.10321 41  LYS C CD    
2319 C  CE    . LYS C 41  ? 1.57079 1.22499 0.75132 -0.01720 0.26754  -0.08947 41  LYS C CE    
2320 N  NZ    . LYS C 41  ? 1.72377 1.39234 0.82762 -0.03179 0.23627  -0.10414 41  LYS C NZ    
2321 N  N     . ILE C 42  ? 1.38605 1.21686 0.91911 -0.00835 0.20084  -0.07740 42  ILE C N     
2322 C  CA    . ILE C 42  ? 1.37396 1.24096 0.94903 -0.01960 0.18335  -0.08710 42  ILE C CA    
2323 C  C     . ILE C 42  ? 1.34384 1.25553 0.89097 -0.03936 0.15184  -0.10849 42  ILE C C     
2324 O  O     . ILE C 42  ? 1.30973 1.26327 0.85536 -0.02649 0.12236  -0.10083 42  ILE C O     
2325 C  CB    . ILE C 42  ? 1.23453 1.13477 0.87507 0.00184  0.16807  -0.06525 42  ILE C CB    
2326 C  CG1   . ILE C 42  ? 1.18621 1.05388 0.85126 0.02258  0.19293  -0.04122 42  ILE C CG1   
2327 C  CG2   . ILE C 42  ? 1.18420 1.10529 0.86498 -0.00995 0.16208  -0.07402 42  ILE C CG2   
2328 C  CD1   . ILE C 42  ? 1.04636 0.94322 0.76797 0.04027  0.17676  -0.02089 42  ILE C CD1   
2329 N  N     . LYS C 43  ? 1.38026 1.28363 0.90554 -0.07052 0.15818  -0.13492 43  LYS C N     
2330 C  CA    . LYS C 43  ? 1.43648 1.39143 0.94349 -0.09498 0.12831  -0.15787 43  LYS C CA    
2331 C  C     . LYS C 43  ? 1.36904 1.39341 0.93894 -0.08782 0.09972  -0.15279 43  LYS C C     
2332 O  O     . LYS C 43  ? 1.29617 1.31662 0.91555 -0.07087 0.10708  -0.13610 43  LYS C O     
2333 C  CB    . LYS C 43  ? 1.45697 1.37912 0.92669 -0.13507 0.14685  -0.18844 43  LYS C CB    
2334 C  CG    . LYS C 43  ? 1.61471 1.45093 1.03044 -0.13909 0.18736  -0.19277 43  LYS C CG    
2335 C  CD    . LYS C 43  ? 1.68202 1.48576 1.04242 -0.18291 0.20007  -0.22780 43  LYS C CD    
2336 C  CE    . LYS C 43  ? 1.66166 1.49401 1.05824 -0.20972 0.19280  -0.24300 43  LYS C CE    
2337 N  NZ    . LYS C 43  ? 1.49558 1.29663 0.94145 -0.19221 0.21650  -0.22514 43  LYS C NZ    
2338 N  N     . PRO C 44  ? 1.37958 1.47107 0.94902 -0.09972 0.06671  -0.16701 44  PRO C N     
2339 C  CA    . PRO C 44  ? 1.27998 1.43878 0.90995 -0.09460 0.04425  -0.16556 44  PRO C CA    
2340 C  C     . PRO C 44  ? 1.24385 1.38581 0.90484 -0.11553 0.06527  -0.17488 44  PRO C C     
2341 O  O     . PRO C 44  ? 1.18916 1.29100 0.82006 -0.14709 0.08688  -0.19407 44  PRO C O     
2342 C  CB    . PRO C 44  ? 1.26965 1.50167 0.88667 -0.11196 0.01080  -0.18542 44  PRO C CB    
2343 C  CG    . PRO C 44  ? 1.39138 1.60070 0.94533 -0.10565 0.00478  -0.18285 44  PRO C CG    
2344 C  CD    . PRO C 44  ? 1.40435 1.51965 0.91988 -0.11149 0.04549  -0.18080 44  PRO C CD    
2345 N  N     . PHE C 45  ? 1.20846 1.37431 0.92427 -0.09715 0.06035  -0.16048 45  PHE C N     
2346 C  CA    . PHE C 45  ? 1.17511 1.32895 0.92139 -0.11231 0.07714  -0.16495 45  PHE C CA    
2347 C  C     . PHE C 45  ? 1.13970 1.20968 0.86806 -0.11403 0.11275  -0.15789 45  PHE C C     
2348 O  O     . PHE C 45  ? 1.07846 1.12182 0.80986 -0.13457 0.13148  -0.16648 45  PHE C O     
2349 C  CB    . PHE C 45  ? 1.14668 1.34162 0.89259 -0.15277 0.07167  -0.19416 45  PHE C CB    
2350 C  CG    . PHE C 45  ? 1.20725 1.49672 0.98073 -0.14986 0.03683  -0.20137 45  PHE C CG    
2351 C  CD1   . PHE C 45  ? 1.15720 1.48687 0.97250 -0.11314 0.01886  -0.18178 45  PHE C CD1   
2352 C  CD2   . PHE C 45  ? 1.23906 1.57782 0.99647 -0.18332 0.02216  -0.22799 45  PHE C CD2   
2353 C  CE1   . PHE C 45  ? 1.14623 1.56261 0.98862 -0.10478 -0.01138 -0.18699 45  PHE C CE1   
2354 C  CE2   . PHE C 45  ? 1.25228 1.68732 1.04132 -0.17717 -0.01118 -0.23324 45  PHE C CE2   
2355 C  CZ    . PHE C 45  ? 1.19372 1.66721 1.02618 -0.13518 -0.02718 -0.21184 45  PHE C CZ    
2356 N  N     . GLU C 46  ? 1.09514 1.12305 0.80534 -0.09138 0.12384  -0.14118 46  GLU C N     
2357 C  CA    . GLU C 46  ? 1.11145 1.06724 0.81137 -0.08598 0.15777  -0.13159 46  GLU C CA    
2358 C  C     . GLU C 46  ? 1.02327 0.97558 0.76719 -0.05302 0.15866  -0.10235 46  GLU C C     
2359 O  O     . GLU C 46  ? 1.05506 1.04349 0.81981 -0.03282 0.13731  -0.08907 46  GLU C O     
2360 C  CB    . GLU C 46  ? 1.13813 1.04789 0.78363 -0.08795 0.17544  -0.13665 46  GLU C CB    
2361 C  CG    . GLU C 46  ? 1.22011 1.05399 0.84965 -0.08562 0.21544  -0.13263 46  GLU C CG    
2362 C  CD    . GLU C 46  ? 1.50251 1.29076 1.07731 -0.08480 0.23590  -0.13747 46  GLU C CD    
2363 O  OE1   . GLU C 46  ? 1.45357 1.26813 1.00473 -0.08178 0.21744  -0.13841 46  GLU C OE1   
2364 O  OE2   . GLU C 46  ? 1.61898 1.34241 1.17140 -0.08547 0.27166  -0.13971 46  GLU C OE2   
2365 N  N     . ARG C 47  ? 0.89670 0.80403 0.65290 -0.04798 0.18326  -0.09238 47  ARG C N     
2366 C  CA    . ARG C 47  ? 0.95339 0.85862 0.75222 -0.02091 0.18431  -0.06586 47  ARG C CA    
2367 C  C     . ARG C 47  ? 0.97653 0.82873 0.76807 -0.00722 0.21499  -0.05331 47  ARG C C     
2368 O  O     . ARG C 47  ? 1.02346 0.82914 0.78290 -0.01860 0.24051  -0.06459 47  ARG C O     
2369 C  CB    . ARG C 47  ? 0.90067 0.81652 0.73231 -0.02422 0.17946  -0.06229 47  ARG C CB    
2370 C  CG    . ARG C 47  ? 0.99668 0.86950 0.80676 -0.04433 0.20254  -0.07428 47  ARG C CG    
2371 C  CD    . ARG C 47  ? 0.96877 0.86921 0.78833 -0.06520 0.19110  -0.08662 47  ARG C CD    
2372 N  NE    . ARG C 47  ? 0.91028 0.76370 0.69917 -0.09029 0.21501  -0.10095 47  ARG C NE    
2373 C  CZ    . ARG C 47  ? 0.93834 0.74428 0.72836 -0.08439 0.23449  -0.08870 47  ARG C CZ    
2374 N  NH1   . ARG C 47  ? 1.12432 0.93090 0.94796 -0.05551 0.23041  -0.06257 47  ARG C NH1   
2375 N  NH2   . ARG C 47  ? 0.94370 0.69910 0.69798 -0.10864 0.25809  -0.10276 47  ARG C NH2   
2376 N  N     . VAL C 48  ? 0.82928 0.68842 0.65125 0.01693  0.21409  -0.03040 48  VAL C N     
2377 C  CA    . VAL C 48  ? 0.92512 0.74714 0.75106 0.03307  0.24297  -0.01620 48  VAL C CA    
2378 C  C     . VAL C 48  ? 0.92949 0.76822 0.81193 0.05290  0.23857  0.00872  48  VAL C C     
2379 O  O     . VAL C 48  ? 0.85957 0.73581 0.76965 0.05612  0.21271  0.01631  48  VAL C O     
2380 C  CB    . VAL C 48  ? 0.94549 0.75936 0.74274 0.03851  0.25134  -0.01509 48  VAL C CB    
2381 C  CG1   . VAL C 48  ? 0.89845 0.68998 0.63298 0.01778  0.25783  -0.04036 48  VAL C CG1   
2382 C  CG2   . VAL C 48  ? 0.88331 0.73808 0.69747 0.04693  0.22394  -0.00409 48  VAL C CG2   
2383 N  N     . LEU C 49  ? 0.94504 0.75578 0.84363 0.06667  0.26423  0.02104  49  LEU C N     
2384 C  CA    . LEU C 49  ? 0.93759 0.76752 0.89164 0.08553  0.26118  0.04541  49  LEU C CA    
2385 C  C     . LEU C 49  ? 1.00176 0.83301 0.97170 0.10022  0.27911  0.05927  49  LEU C C     
2386 O  O     . LEU C 49  ? 1.09251 0.89225 1.05342 0.10987  0.31124  0.06075  49  LEU C O     
2387 C  CB    . LEU C 49  ? 1.00083 0.80522 0.96637 0.09343  0.27536  0.05183  49  LEU C CB    
2388 C  CG    . LEU C 49  ? 1.00980 0.83988 1.03190 0.11214  0.26638  0.07697  49  LEU C CG    
2389 C  CD1   . LEU C 49  ? 0.88422 0.75388 0.92539 0.10313  0.23046  0.07892  49  LEU C CD1   
2390 C  CD2   . LEU C 49  ? 0.83985 0.63576 0.86339 0.12478  0.28440  0.08490  49  LEU C CD2   
2391 N  N     . ILE C 50  ? 0.90828 0.77259 0.89982 0.10144  0.26118  0.06898  50  ILE C N     
2392 C  CA    . ILE C 50  ? 1.09076 0.95744 1.09226 0.10973  0.27770  0.08082  50  ILE C CA    
2393 C  C     . ILE C 50  ? 0.92731 0.82373 0.99430 0.12211  0.27748  0.10356  50  ILE C C     
2394 O  O     . ILE C 50  ? 0.78818 0.71394 0.88413 0.11862  0.24959  0.11000  50  ILE C O     
2395 C  CB    . ILE C 50  ? 1.07042 0.94748 1.04632 0.10145  0.26026  0.07745  50  ILE C CB    
2396 C  CG1   . ILE C 50  ? 1.08851 0.94743 1.00321 0.08934  0.25486  0.05518  50  ILE C CG1   
2397 C  CG2   . ILE C 50  ? 0.93016 0.80264 0.91051 0.10756  0.28148  0.09047  50  ILE C CG2   
2398 C  CD1   . ILE C 50  ? 1.04970 0.92199 0.93791 0.08569  0.23270  0.05315  50  ILE C CD1   
2399 N  N     . PRO C 51  ? 0.95301 0.84583 1.04492 0.13596  0.30746  0.11529  51  PRO C N     
2400 C  CA    . PRO C 51  ? 0.88433 0.81718 1.04510 0.14634  0.30536  0.13716  51  PRO C CA    
2401 C  C     . PRO C 51  ? 0.94222 0.90036 1.12122 0.13730  0.29897  0.14601  51  PRO C C     
2402 O  O     . PRO C 51  ? 1.00373 0.94182 1.14570 0.13130  0.31217  0.14065  51  PRO C O     
2403 C  CB    . PRO C 51  ? 0.90417 0.82403 1.08265 0.16650  0.34435  0.14473  51  PRO C CB    
2404 C  CG    . PRO C 51  ? 0.78777 0.66124 0.90309 0.16180  0.37109  0.12827  51  PRO C CG    
2405 C  CD    . PRO C 51  ? 1.00069 0.85382 1.05934 0.14302  0.34592  0.10801  51  PRO C CD    
2406 N  N     . THR C 52  ? 0.88525 0.88459 1.11771 0.13485  0.27833  0.15980  52  THR C N     
2407 C  CA    . THR C 52  ? 0.90772 0.92904 1.16182 0.12296  0.27349  0.16900  52  THR C CA    
2408 C  C     . THR C 52  ? 0.93051 0.98576 1.24518 0.12922  0.29733  0.18640  52  THR C C     
2409 O  O     . THR C 52  ? 0.92697 0.99238 1.25309 0.11725  0.30529  0.19304  52  THR C O     
2410 C  CB    . THR C 52  ? 0.79711 0.84066 1.06702 0.11019  0.23492  0.17028  52  THR C CB    
2411 O  OG1   . THR C 52  ? 0.76592 0.84272 1.08490 0.11698  0.22195  0.17984  52  THR C OG1   
2412 C  CG2   . THR C 52  ? 0.84934 0.86590 1.06440 0.10491  0.21341  0.15328  52  THR C CG2   
2413 N  N     . GLY C 53  ? 0.88838 0.96121 1.24203 0.14823  0.31035  0.19454  53  GLY C N     
2414 C  CA    . GLY C 53  ? 0.91861 1.03807 1.34239 0.15664  0.32957  0.21244  53  GLY C CA    
2415 C  C     . GLY C 53  ? 0.90852 1.08492 1.39192 0.14280  0.30003  0.22473  53  GLY C C     
2416 O  O     . GLY C 53  ? 0.90708 1.12853 1.44804 0.13911  0.31326  0.23774  53  GLY C O     
2417 N  N     . LEU C 54  ? 0.91136 1.08767 1.38150 0.13290  0.26122  0.21978  54  LEU C N     
2418 C  CA    . LEU C 54  ? 0.88207 1.10274 1.39398 0.11468  0.22981  0.22728  54  LEU C CA    
2419 C  C     . LEU C 54  ? 0.84372 1.09198 1.38308 0.12633  0.20301  0.23427  54  LEU C C     
2420 O  O     . LEU C 54  ? 0.82211 1.03629 1.32050 0.13669  0.19475  0.22632  54  LEU C O     
2421 C  CB    . LEU C 54  ? 0.75332 0.94300 1.21625 0.09081  0.20742  0.21455  54  LEU C CB    
2422 C  CG    . LEU C 54  ? 0.88674 1.06618 1.34057 0.07020  0.21972  0.21469  54  LEU C CG    
2423 C  CD1   . LEU C 54  ? 0.95396 1.11431 1.39482 0.07939  0.26171  0.21656  54  LEU C CD1   
2424 C  CD2   . LEU C 54  ? 0.83303 0.96783 1.22462 0.05775  0.19934  0.20133  54  LEU C CD2   
2425 N  N     . ILE C 55  ? 0.84347 1.15461 1.45099 0.12315  0.18943  0.24950  55  ILE C N     
2426 C  CA    . ILE C 55  ? 0.81343 1.15744 1.44747 0.13124  0.15776  0.25876  55  ILE C CA    
2427 C  C     . ILE C 55  ? 0.87877 1.25858 1.53416 0.10028  0.12347  0.25878  55  ILE C C     
2428 O  O     . ILE C 55  ? 0.92694 1.35362 1.63436 0.08440  0.12751  0.26623  55  ILE C O     
2429 C  CB    . ILE C 55  ? 0.81314 1.20580 1.51192 0.16121  0.17123  0.27909  55  ILE C CB    
2430 C  CG1   . ILE C 55  ? 0.76306 1.10577 1.42920 0.19192  0.20659  0.27674  55  ILE C CG1   
2431 C  CG2   . ILE C 55  ? 0.80442 1.23773 1.53170 0.16789  0.13327  0.29178  55  ILE C CG2   
2432 C  CD1   . ILE C 55  ? 0.60432 0.98592 1.33109 0.22667  0.22904  0.29654  55  ILE C CD1   
2433 N  N     . LEU C 56  ? 0.84386 1.19997 1.45751 0.08965  0.09203  0.24931  56  LEU C N     
2434 C  CA    . LEU C 56  ? 0.88363 1.25249 1.49604 0.05746  0.06215  0.24343  56  LEU C CA    
2435 C  C     . LEU C 56  ? 0.91464 1.33568 1.56407 0.05523  0.02693  0.25451  56  LEU C C     
2436 O  O     . LEU C 56  ? 0.88302 1.30859 1.53191 0.07962  0.01871  0.26319  56  LEU C O     
2437 C  CB    . LEU C 56  ? 0.85737 1.16344 1.39459 0.04649  0.05181  0.22383  56  LEU C CB    
2438 C  CG    . LEU C 56  ? 0.92602 1.17790 1.41472 0.05447  0.08011  0.21245  56  LEU C CG    
2439 C  CD1   . LEU C 56  ? 0.86632 1.07085 1.29096 0.04724  0.06461  0.19492  56  LEU C CD1   
2440 C  CD2   . LEU C 56  ? 0.91843 1.17116 1.42114 0.04139  0.10320  0.21441  56  LEU C CD2   
2441 N  N     . GLU C 57  ? 0.94871 1.40601 1.62595 0.02425  0.00595  0.25420  57  GLU C N     
2442 C  CA    . GLU C 57  ? 0.92746 1.42752 1.62388 0.01262  -0.03470 0.25967  57  GLU C CA    
2443 C  C     . GLU C 57  ? 0.94501 1.40149 1.58432 -0.01949 -0.05604 0.24016  57  GLU C C     
2444 O  O     . GLU C 57  ? 0.94854 1.42063 1.60214 -0.05351 -0.06600 0.23480  57  GLU C O     
2445 C  CB    . GLU C 57  ? 0.92708 1.51624 1.71005 0.00149  -0.04372 0.27547  57  GLU C CB    
2446 C  CG    . GLU C 57  ? 1.01742 1.65597 1.81807 -0.01031 -0.09009 0.28174  57  GLU C CG    
2447 C  CD    . GLU C 57  ? 0.96674 1.70715 1.86169 -0.00506 -0.10032 0.30313  57  GLU C CD    
2448 O  OE1   . GLU C 57  ? 0.92223 1.69802 1.87385 -0.00095 -0.06984 0.31048  57  GLU C OE1   
2449 O  OE2   . GLU C 57  ? 0.90058 1.68822 1.81287 -0.00422 -0.13885 0.31309  57  GLU C OE2   
2450 N  N     . ILE C 58  ? 0.88939 1.28850 1.46273 -0.00900 -0.06026 0.22877  58  ILE C N     
2451 C  CA    . ILE C 58  ? 0.91065 1.26616 1.42674 -0.03287 -0.07891 0.21020  58  ILE C CA    
2452 C  C     . ILE C 58  ? 0.95168 1.34588 1.48021 -0.05140 -0.11772 0.21353  58  ILE C C     
2453 O  O     . ILE C 58  ? 0.95824 1.37837 1.49570 -0.03298 -0.13405 0.22567  58  ILE C O     
2454 C  CB    . ILE C 58  ? 0.97108 1.26649 1.42146 -0.01502 -0.07207 0.19807  58  ILE C CB    
2455 C  CG1   . ILE C 58  ? 0.81520 1.08007 1.25499 0.00281  -0.03668 0.19535  58  ILE C CG1   
2456 C  CG2   . ILE C 58  ? 0.91547 1.16751 1.31004 -0.03639 -0.08727 0.17871  58  ILE C CG2   
2457 C  CD1   . ILE C 58  ? 0.77306 0.98849 1.15524 0.01770  -0.02971 0.18270  58  ILE C CD1   
2458 N  N     . PRO C 59  ? 0.99685 1.39275 1.52197 -0.08812 -0.13345 0.20338  59  PRO C N     
2459 C  CA    . PRO C 59  ? 0.92230 1.35887 1.45827 -0.11028 -0.17250 0.20525  59  PRO C CA    
2460 C  C     . PRO C 59  ? 1.03541 1.43684 1.50912 -0.10192 -0.19348 0.19818  59  PRO C C     
2461 O  O     . PRO C 59  ? 1.08847 1.42801 1.50566 -0.08899 -0.17855 0.18602  59  PRO C O     
2462 C  CB    . PRO C 59  ? 0.90306 1.32514 1.43088 -0.15472 -0.17703 0.18998  59  PRO C CB    
2463 C  CG    . PRO C 59  ? 1.01447 1.36254 1.49625 -0.14930 -0.14494 0.17689  59  PRO C CG    
2464 C  CD    . PRO C 59  ? 0.93674 1.29239 1.44255 -0.11211 -0.11597 0.18971  59  PRO C CD    
2465 N  N     . GLU C 60  ? 1.27372 1.71960 1.75925 -0.10996 -0.22878 0.20655  60  GLU C N     
2466 C  CA    . GLU C 60  ? 1.22534 1.64169 1.65074 -0.10322 -0.24967 0.20250  60  GLU C CA    
2467 C  C     . GLU C 60  ? 1.19394 1.54143 1.54649 -0.12775 -0.25012 0.17557  60  GLU C C     
2468 O  O     . GLU C 60  ? 1.17411 1.51254 1.52482 -0.16084 -0.25313 0.16210  60  GLU C O     
2469 C  CB    . GLU C 60  ? 1.31445 1.79419 1.76399 -0.11119 -0.29096 0.21707  60  GLU C CB    
2470 C  CG    . GLU C 60  ? 1.43523 1.88479 1.81774 -0.10556 -0.31396 0.21525  60  GLU C CG    
2471 C  CD    . GLU C 60  ? 1.58327 2.04175 1.93570 -0.14536 -0.35202 0.20318  60  GLU C CD    
2472 O  OE1   . GLU C 60  ? 1.57240 2.05726 1.95572 -0.17984 -0.35977 0.19450  60  GLU C OE1   
2473 O  OE2   . GLU C 60  ? 1.65907 2.09503 1.95307 -0.14438 -0.37296 0.20166  60  GLU C OE2   
2474 N  N     . GLY C 61  ? 1.18521 1.48184 1.47704 -0.11111 -0.24448 0.16764  61  GLY C N     
2475 C  CA    . GLY C 61  ? 1.19989 1.43110 1.42318 -0.12643 -0.24024 0.14270  61  GLY C CA    
2476 C  C     . GLY C 61  ? 1.14194 1.32584 1.35114 -0.11584 -0.20562 0.13052  61  GLY C C     
2477 O  O     . GLY C 61  ? 1.13217 1.26164 1.28599 -0.12109 -0.19878 0.11087  61  GLY C O     
2478 N  N     . TYR C 62  ? 1.13668 1.34006 1.39245 -0.09962 -0.18352 0.14183  62  TYR C N     
2479 C  CA    . TYR C 62  ? 1.07439 1.23753 1.31657 -0.08800 -0.15276 0.13277  62  TYR C CA    
2480 C  C     . TYR C 62  ? 0.99640 1.16741 1.25409 -0.05532 -0.13226 0.14348  62  TYR C C     
2481 O  O     . TYR C 62  ? 1.00673 1.21684 1.29926 -0.04208 -0.13703 0.16086  62  TYR C O     
2482 C  CB    . TYR C 62  ? 0.99320 1.16089 1.26650 -0.10580 -0.14172 0.13339  62  TYR C CB    
2483 C  CG    . TYR C 62  ? 1.11105 1.26548 1.36815 -0.14312 -0.15932 0.12168  62  TYR C CG    
2484 C  CD1   . TYR C 62  ? 1.18350 1.27224 1.38448 -0.15283 -0.15155 0.10223  62  TYR C CD1   
2485 C  CD2   . TYR C 62  ? 1.14268 1.35017 1.44009 -0.16874 -0.18351 0.12966  62  TYR C CD2   
2486 C  CE1   . TYR C 62  ? 1.25203 1.31807 1.43116 -0.18862 -0.16485 0.08974  62  TYR C CE1   
2487 C  CE2   . TYR C 62  ? 1.20329 1.39622 1.48225 -0.20829 -0.19977 0.11647  62  TYR C CE2   
2488 C  CZ    . TYR C 62  ? 1.32089 1.43784 1.53748 -0.21890 -0.18905 0.09585  62  TYR C CZ    
2489 O  OH    . TYR C 62  ? 1.28512 1.37701 1.47635 -0.25972 -0.20243 0.08099  62  TYR C OH    
2490 N  N     . GLU C 63  ? 0.91255 1.04477 1.14218 -0.04201 -0.10944 0.13275  63  GLU C N     
2491 C  CA    . GLU C 63  ? 0.88586 1.01760 1.12122 -0.01589 -0.08840 0.13819  63  GLU C CA    
2492 C  C     . GLU C 63  ? 0.90024 1.01531 1.13990 -0.01028 -0.06400 0.13464  63  GLU C C     
2493 O  O     . GLU C 63  ? 0.96057 1.05651 1.19090 -0.02393 -0.06249 0.12768  63  GLU C O     
2494 C  CB    . GLU C 63  ? 0.90399 1.00830 1.09309 -0.00508 -0.08672 0.12738  63  GLU C CB    
2495 C  CG    . GLU C 63  ? 0.91714 0.98290 1.06375 -0.00798 -0.08014 0.10714  63  GLU C CG    
2496 C  CD    . GLU C 63  ? 0.96066 1.00994 1.07406 0.00489  -0.07092 0.09698  63  GLU C CD    
2497 O  OE1   . GLU C 63  ? 0.96213 1.02235 1.08142 0.01418  -0.06719 0.10545  63  GLU C OE1   
2498 O  OE2   . GLU C 63  ? 1.00995 1.03513 1.09196 0.00588  -0.06598 0.08071  63  GLU C OE2   
2499 N  N     . GLY C 64  ? 0.79410 0.91134 1.04228 0.00961  -0.04420 0.13960  64  GLY C N     
2500 C  CA    . GLY C 64  ? 0.81644 0.91642 1.06028 0.01720  -0.02110 0.13631  64  GLY C CA    
2501 C  C     . GLY C 64  ? 0.82585 0.90036 1.03059 0.03094  -0.01141 0.12331  64  GLY C C     
2502 O  O     . GLY C 64  ? 0.82516 0.90270 1.02301 0.03946  -0.01078 0.12302  64  GLY C O     
2503 N  N     . GLN C 65  ? 0.80454 0.85464 0.98359 0.03261  -0.00390 0.11322  65  GLN C N     
2504 C  CA    . GLN C 65  ? 0.73038 0.76552 0.87680 0.04453  0.00309  0.09999  65  GLN C CA    
2505 C  C     . GLN C 65  ? 0.81647 0.84373 0.95835 0.05377  0.02117  0.10100  65  GLN C C     
2506 O  O     . GLN C 65  ? 0.83187 0.84363 0.96666 0.05206  0.02424  0.10293  65  GLN C O     
2507 C  CB    . GLN C 65  ? 0.71490 0.73072 0.82948 0.04256  -0.00767 0.08612  65  GLN C CB    
2508 C  CG    . GLN C 65  ? 0.81472 0.83260 0.92245 0.03261  -0.02411 0.08233  65  GLN C CG    
2509 C  CD    . GLN C 65  ? 0.86945 0.86386 0.94296 0.03281  -0.02987 0.06710  65  GLN C CD    
2510 O  OE1   . GLN C 65  ? 0.85060 0.83579 0.90667 0.04604  -0.02170 0.05808  65  GLN C OE1   
2511 N  NE2   . GLN C 65  ? 0.74282 0.72821 0.80556 0.01917  -0.04408 0.06406  65  GLN C NE2   
2512 N  N     . VAL C 66  ? 0.76484 0.79755 0.90516 0.06229  0.03386  0.09960  66  VAL C N     
2513 C  CA    . VAL C 66  ? 0.76558 0.78886 0.89098 0.07017  0.04978  0.09733  66  VAL C CA    
2514 C  C     . VAL C 66  ? 0.77049 0.78658 0.86227 0.07606  0.04330  0.08258  66  VAL C C     
2515 O  O     . VAL C 66  ? 0.69640 0.72142 0.77833 0.07646  0.03873  0.07120  66  VAL C O     
2516 C  CB    . VAL C 66  ? 0.68199 0.70893 0.81268 0.07491  0.06658  0.09873  66  VAL C CB    
2517 C  CG1   . VAL C 66  ? 0.68195 0.69662 0.78803 0.08046  0.08162  0.09351  66  VAL C CG1   
2518 C  CG2   . VAL C 66  ? 0.69471 0.73331 0.86386 0.07489  0.07413  0.11524  66  VAL C CG2   
2519 N  N     . ARG C 67  ? 0.82088 0.82185 0.89564 0.08130  0.04364  0.08373  67  ARG C N     
2520 C  CA    . ARG C 67  ? 0.76428 0.76175 0.81060 0.09206  0.03582  0.07267  67  ARG C CA    
2521 C  C     . ARG C 67  ? 0.86191 0.85428 0.88526 0.10199  0.04422  0.07303  67  ARG C C     
2522 O  O     . ARG C 67  ? 0.86052 0.83994 0.88423 0.09988  0.05724  0.08366  67  ARG C O     
2523 C  CB    . ARG C 67  ? 0.85749 0.83377 0.89436 0.09379  0.02611  0.07414  67  ARG C CB    
2524 C  CG    . ARG C 67  ? 0.80105 0.78012 0.84984 0.08324  0.01526  0.07024  67  ARG C CG    
2525 C  CD    . ARG C 67  ? 0.79844 0.74736 0.83053 0.08309  0.00837  0.06941  67  ARG C CD    
2526 N  NE    . ARG C 67  ? 0.80273 0.75123 0.83766 0.07174  -0.00245 0.06315  67  ARG C NE    
2527 C  CZ    . ARG C 67  ? 0.83690 0.75540 0.85431 0.06699  -0.00839 0.05936  67  ARG C CZ    
2528 N  NH1   . ARG C 67  ? 0.97350 0.85630 0.97006 0.07355  -0.00362 0.06233  67  ARG C NH1   
2529 N  NH2   . ARG C 67  ? 0.92378 0.84251 0.93890 0.05499  -0.01840 0.05244  67  ARG C NH2   
2530 N  N     . PRO C 68  ? 0.76911 0.77458 0.77213 0.11251  0.03709  0.06157  68  PRO C N     
2531 C  CA    . PRO C 68  ? 0.81723 0.82141 0.79369 0.12151  0.04110  0.06158  68  PRO C CA    
2532 C  C     . PRO C 68  ? 0.95569 0.92991 0.90917 0.13367  0.04070  0.07385  68  PRO C C     
2533 O  O     . PRO C 68  ? 0.90990 0.86630 0.86309 0.13855  0.03431  0.07776  68  PRO C O     
2534 C  CB    . PRO C 68  ? 0.79941 0.83662 0.76773 0.12816  0.02924  0.04531  68  PRO C CB    
2535 C  CG    . PRO C 68  ? 0.84286 0.89650 0.83507 0.11845  0.02588  0.03641  68  PRO C CG    
2536 C  CD    . PRO C 68  ? 0.76500 0.79365 0.77035 0.11507  0.02585  0.04734  68  PRO C CD    
2537 N  N     . ARG C 69  ? 0.94255 0.90529 0.87062 0.13773  0.04929  0.07972  69  ARG C N     
2538 C  CA    . ARG C 69  ? 1.04603 0.97539 0.94196 0.15060  0.05047  0.09275  69  ARG C CA    
2539 C  C     . ARG C 69  ? 1.00047 0.94227 0.86908 0.17329  0.03303  0.08767  69  ARG C C     
2540 O  O     . ARG C 69  ? 1.03613 1.01228 0.89811 0.17592  0.02550  0.07638  69  ARG C O     
2541 C  CB    . ARG C 69  ? 1.01382 0.92328 0.88889 0.14553  0.06893  0.10239  69  ARG C CB    
2542 C  CG    . ARG C 69  ? 1.09873 0.99370 1.00214 0.12817  0.08858  0.11244  69  ARG C CG    
2543 C  CD    . ARG C 69  ? 1.12364 0.99120 0.99984 0.12664  0.10988  0.12439  69  ARG C CD    
2544 N  NE    . ARG C 69  ? 1.32881 1.16279 1.15795 0.14077  0.10575  0.13428  69  ARG C NE    
2545 C  CZ    . ARG C 69  ? 1.38120 1.17953 1.20436 0.13960  0.10975  0.14726  69  ARG C CZ    
2546 N  NH1   . ARG C 69  ? 1.33412 1.13139 1.19784 0.12192  0.11611  0.15054  69  ARG C NH1   
2547 N  NH2   . ARG C 69  ? 1.40747 1.16891 1.18033 0.15594  0.10678  0.15739  69  ARG C NH2   
2548 N  N     . SER C 70  ? 0.88849 0.80263 0.74137 0.18969  0.02690  0.09591  70  SER C N     
2549 C  CA    . SER C 70  ? 1.05269 0.98029 0.88304 0.21763  0.01022  0.09370  70  SER C CA    
2550 C  C     . SER C 70  ? 1.01618 0.94389 0.80647 0.22958  0.00757  0.10061  70  SER C C     
2551 O  O     . SER C 70  ? 0.92428 0.89136 0.70565 0.24588  -0.00931 0.09340  70  SER C O     
2552 C  CB    . SER C 70  ? 1.10841 0.99331 0.92442 0.23513  0.00837  0.10288  70  SER C CB    
2553 O  OG    . SER C 70  ? 1.25476 1.08102 1.04235 0.23119  0.02242  0.12081  70  SER C OG    
2554 N  N     . GLY C 71  ? 1.01949 0.90649 0.78492 0.22077  0.02400  0.11436  71  GLY C N     
2555 C  CA    . GLY C 71  ? 1.08434 0.96370 0.80284 0.23006  0.02363  0.12176  71  GLY C CA    
2556 C  C     . GLY C 71  ? 1.07683 1.00302 0.79820 0.21829  0.01901  0.10535  71  GLY C C     
2557 O  O     . GLY C 71  ? 1.05160 1.01029 0.75171 0.23238  -0.00000 0.09965  71  GLY C O     
2558 N  N     . LEU C 72  ? 1.03649 0.96656 0.78376 0.19238  0.03616  0.09748  72  LEU C N     
2559 C  CA    . LEU C 72  ? 1.10564 1.06827 0.85060 0.17801  0.03623  0.08055  72  LEU C CA    
2560 C  C     . LEU C 72  ? 1.05958 1.07834 0.82821 0.17962  0.01462  0.06201  72  LEU C C     
2561 O  O     . LEU C 72  ? 1.07896 1.12961 0.83296 0.17229  0.00642  0.04773  72  LEU C O     
2562 C  CB    . LEU C 72  ? 1.03970 0.99048 0.81107 0.15445  0.06083  0.07715  72  LEU C CB    
2563 C  CG    . LEU C 72  ? 1.23487 1.14061 0.99061 0.14924  0.08715  0.09303  72  LEU C CG    
2564 C  CD1   . LEU C 72  ? 1.10226 1.00800 0.88725 0.13064  0.11019  0.08745  72  LEU C CD1   
2565 C  CD2   . LEU C 72  ? 1.24637 1.13063 0.93966 0.15707  0.08955  0.09876  72  LEU C CD2   
2566 N  N     . ALA C 73  ? 0.96292 0.99446 0.76649 0.18680  0.00650  0.06081  73  ALA C N     
2567 C  CA    . ALA C 73  ? 0.96168 1.04863 0.79073 0.18807  -0.01037 0.04341  73  ALA C CA    
2568 C  C     . ALA C 73  ? 1.04358 1.16546 0.84948 0.21068  -0.03309 0.04229  73  ALA C C     
2569 O  O     . ALA C 73  ? 0.98562 1.15997 0.79651 0.20269  -0.04519 0.02568  73  ALA C O     
2570 C  CB    . ALA C 73  ? 0.91826 1.00487 0.78293 0.19275  -0.01138 0.04332  73  ALA C CB    
2571 N  N     . TRP C 74  ? 1.10305 1.19674 0.88266 0.23882  -0.03945 0.06035  74  TRP C N     
2572 C  CA    . TRP C 74  ? 1.11921 1.24868 0.87885 0.26704  -0.06352 0.06252  74  TRP C CA    
2573 C  C     . TRP C 74  ? 1.03927 1.16984 0.75076 0.26389  -0.06956 0.06500  74  TRP C C     
2574 O  O     . TRP C 74  ? 1.14850 1.33706 0.85549 0.26718  -0.09090 0.05404  74  TRP C O     
2575 C  CB    . TRP C 74  ? 1.12643 1.21886 0.87110 0.30258  -0.06750 0.08211  74  TRP C CB    
2576 C  CG    . TRP C 74  ? 1.16148 1.28525 0.88147 0.33865  -0.09222 0.08954  74  TRP C CG    
2577 C  CD1   . TRP C 74  ? 1.16006 1.23884 0.82963 0.36884  -0.09677 0.11280  74  TRP C CD1   
2578 C  CD2   . TRP C 74  ? 1.14996 1.35978 0.89490 0.34878  -0.11630 0.07484  74  TRP C CD2   
2579 N  NE1   . TRP C 74  ? 1.22464 1.35656 0.88570 0.40106  -0.12428 0.11498  74  TRP C NE1   
2580 C  CE2   . TRP C 74  ? 1.17289 1.39070 0.88348 0.38860  -0.13721 0.09115  74  TRP C CE2   
2581 C  CE3   . TRP C 74  ? 1.09586 1.37753 0.88903 0.32731  -0.12154 0.05005  74  TRP C CE3   
2582 C  CZ2   . TRP C 74  ? 1.23545 1.53961 0.96464 0.40859  -0.16540 0.08322  74  TRP C CZ2   
2583 C  CZ3   . TRP C 74  ? 1.08272 1.44782 0.89406 0.34288  -0.14681 0.04069  74  TRP C CZ3   
2584 C  CH2   . TRP C 74  ? 1.18629 1.56669 0.96891 0.38375  -0.16964 0.05706  74  TRP C CH2   
2585 N  N     . LYS C 75  ? 1.17779 1.24712 0.85238 0.25584  -0.05061 0.07851  75  LYS C N     
2586 C  CA    . LYS C 75  ? 1.24079 1.30147 0.85910 0.25415  -0.05392 0.08215  75  LYS C CA    
2587 C  C     . LYS C 75  ? 1.23558 1.33600 0.85734 0.22345  -0.05448 0.05782  75  LYS C C     
2588 O  O     . LYS C 75  ? 1.17790 1.31086 0.76626 0.22412  -0.07336 0.05081  75  LYS C O     
2589 C  CB    . LYS C 75  ? 1.33069 1.31536 0.91141 0.24942  -0.02730 0.10096  75  LYS C CB    
2590 C  CG    . LYS C 75  ? 1.33143 1.26469 0.89919 0.27428  -0.02311 0.12515  75  LYS C CG    
2591 C  CD    . LYS C 75  ? 1.41068 1.27433 0.94708 0.26185  0.00710  0.14145  75  LYS C CD    
2592 C  CE    . LYS C 75  ? 1.45504 1.31747 1.03468 0.22895  0.03233  0.13020  75  LYS C CE    
2593 N  NZ    . LYS C 75  ? 1.61449 1.42100 1.17019 0.21598  0.06374  0.14466  75  LYS C NZ    
2594 N  N     . LYS C 76  ? 1.23178 1.32799 0.89032 0.19598  -0.03448 0.04477  76  LYS C N     
2595 C  CA    . LYS C 76  ? 1.19689 1.30919 0.84978 0.16481  -0.02704 0.02317  76  LYS C CA    
2596 C  C     . LYS C 76  ? 1.09220 1.24999 0.79651 0.14575  -0.02969 0.00184  76  LYS C C     
2597 O  O     . LYS C 76  ? 1.13768 1.31235 0.83427 0.11911  -0.02655 -0.01845 76  LYS C O     
2598 C  CB    . LYS C 76  ? 1.09554 1.14737 0.73123 0.14782  0.00683  0.02812  76  LYS C CB    
2599 C  CG    . LYS C 76  ? 1.25685 1.26041 0.83541 0.16002  0.01576  0.04703  76  LYS C CG    
2600 C  CD    . LYS C 76  ? 1.25864 1.20960 0.83125 0.14428  0.05306  0.05171  76  LYS C CD    
2601 C  CE    . LYS C 76  ? 1.20711 1.11077 0.71663 0.15246  0.06559  0.06824  76  LYS C CE    
2602 N  NZ    . LYS C 76  ? 1.46973 1.35582 0.96845 0.17869  0.05436  0.09204  76  LYS C NZ    
2603 N  N     . GLY C 77  ? 1.02724 1.20028 0.77816 0.15667  -0.03347 0.00507  77  GLY C N     
2604 C  CA    . GLY C 77  ? 1.03711 1.24637 0.83229 0.13752  -0.03210 -0.01348 77  GLY C CA    
2605 C  C     . GLY C 77  ? 0.96212 1.13227 0.77569 0.11636  -0.00538 -0.01494 77  GLY C C     
2606 O  O     . GLY C 77  ? 0.97156 1.16288 0.81289 0.09758  -0.00128 -0.02990 77  GLY C O     
2607 N  N     . LEU C 78  ? 0.92125 1.03665 0.72062 0.11932  0.01347  0.00100  78  LEU C N     
2608 C  CA    . LEU C 78  ? 0.90268 0.98607 0.72423 0.10436  0.03748  0.00282  78  LEU C CA    
2609 C  C     . LEU C 78  ? 0.91334 0.99856 0.77708 0.11176  0.03500  0.01064  78  LEU C C     
2610 O  O     . LEU C 78  ? 0.94898 1.02781 0.81509 0.13085  0.02590  0.02346  78  LEU C O     
2611 C  CB    . LEU C 78  ? 0.92624 0.95969 0.72420 0.10576  0.05922  0.01739  78  LEU C CB    
2612 C  CG    . LEU C 78  ? 1.16201 1.17807 0.91615 0.09270  0.07255  0.00800  78  LEU C CG    
2613 C  CD1   . LEU C 78  ? 1.16280 1.13191 0.89485 0.09903  0.09506  0.02528  78  LEU C CD1   
2614 C  CD2   . LEU C 78  ? 0.98073 0.99479 0.74622 0.06997  0.08766  -0.00922 78  LEU C CD2   
2615 N  N     . THR C 79  ? 0.82223 0.91050 0.71366 0.09613  0.04398  0.00296  79  THR C N     
2616 C  CA    . THR C 79  ? 0.81302 0.90050 0.73884 0.09999  0.04186  0.00946  79  THR C CA    
2617 C  C     . THR C 79  ? 0.82585 0.89506 0.77009 0.08429  0.05911  0.00966  79  THR C C     
2618 O  O     . THR C 79  ? 0.82597 0.88640 0.75777 0.07065  0.07249  0.00120  79  THR C O     
2619 C  CB    . THR C 79  ? 0.74149 0.87087 0.68271 0.10409  0.02460  -0.00228 79  THR C CB    
2620 O  OG1   . THR C 79  ? 0.76147 0.88142 0.72404 0.11301  0.02125  0.00620  79  THR C OG1   
2621 C  CG2   . THR C 79  ? 0.79907 0.95196 0.74970 0.08192  0.02932  -0.02060 79  THR C CG2   
2622 N  N     . VAL C 80  ? 0.80652 0.86727 0.77722 0.08707  0.05850  0.01968  80  VAL C N     
2623 C  CA    . VAL C 80  ? 0.72024 0.76720 0.71028 0.07673  0.07093  0.02329  80  VAL C CA    
2624 C  C     . VAL C 80  ? 0.75377 0.81924 0.74806 0.06474  0.06785  0.00856  80  VAL C C     
2625 O  O     . VAL C 80  ? 0.78255 0.87077 0.78433 0.06727  0.05444  0.00264  80  VAL C O     
2626 C  CB    . VAL C 80  ? 0.76762 0.80314 0.78260 0.08229  0.06817  0.03985  80  VAL C CB    
2627 C  CG1   . VAL C 80  ? 0.75277 0.77992 0.78845 0.07514  0.07751  0.04587  80  VAL C CG1   
2628 C  CG2   . VAL C 80  ? 0.74697 0.76434 0.75798 0.08997  0.07434  0.05383  80  VAL C CG2   
2629 N  N     . LEU C 81  ? 0.77918 0.83095 0.76628 0.05152  0.08321  0.00249  81  LEU C N     
2630 C  CA    . LEU C 81  ? 0.72682 0.79119 0.71088 0.03548  0.08430  -0.01293 81  LEU C CA    
2631 C  C     . LEU C 81  ? 0.81764 0.88264 0.82060 0.03560  0.07953  -0.00671 81  LEU C C     
2632 O  O     . LEU C 81  ? 0.71587 0.80465 0.72091 0.02867  0.07272  -0.01801 81  LEU C O     
2633 C  CB    . LEU C 81  ? 0.80820 0.84422 0.77286 0.02054  0.10522  -0.02000 81  LEU C CB    
2634 C  CG    . LEU C 81  ? 0.87657 0.91745 0.83096 -0.00204 0.11111  -0.03755 81  LEU C CG    
2635 C  CD1   . LEU C 81  ? 0.90124 0.99214 0.85532 -0.01036 0.09536  -0.05569 81  LEU C CD1   
2636 C  CD2   . LEU C 81  ? 0.85634 0.85753 0.78301 -0.01701 0.13424  -0.04537 81  LEU C CD2   
2637 N  N     . ASN C 82  ? 0.83065 0.87286 0.84738 0.04306  0.08300  0.01104  82  ASN C N     
2638 C  CA    . ASN C 82  ? 0.72019 0.76048 0.74946 0.04281  0.07639  0.01860  82  ASN C CA    
2639 C  C     . ASN C 82  ? 0.72782 0.77894 0.77071 0.05321  0.05941  0.02633  82  ASN C C     
2640 O  O     . ASN C 82  ? 0.66102 0.70477 0.71555 0.05457  0.05325  0.03795  82  ASN C O     
2641 C  CB    . ASN C 82  ? 0.78936 0.80209 0.82544 0.04466  0.08780  0.03387  82  ASN C CB    
2642 C  CG    . ASN C 82  ? 0.70963 0.71603 0.76423 0.05740  0.09081  0.05012  82  ASN C CG    
2643 O  OD1   . ASN C 82  ? 0.78533 0.79302 0.83487 0.06082  0.09542  0.04737  82  ASN C OD1   
2644 N  ND2   . ASN C 82  ? 0.71676 0.71909 0.79286 0.06396  0.08810  0.06762  82  ASN C ND2   
2645 N  N     . ALA C 83  ? 0.74037 0.80639 0.77875 0.06042  0.05137  0.02016  83  ALA C N     
2646 C  CA    . ALA C 83  ? 0.71960 0.78418 0.76448 0.07029  0.03876  0.02737  83  ALA C CA    
2647 C  C     . ALA C 83  ? 0.73512 0.80702 0.77938 0.06798  0.02947  0.02094  83  ALA C C     
2648 O  O     . ALA C 83  ? 0.81886 0.90969 0.85665 0.06408  0.03074  0.00671  83  ALA C O     
2649 C  CB    . ALA C 83  ? 0.64796 0.71939 0.68166 0.08218  0.03421  0.02407  83  ALA C CB    
2650 N  N     . PRO C 84  ? 0.73591 0.79416 0.78580 0.06821  0.02105  0.03008  84  PRO C N     
2651 C  CA    . PRO C 84  ? 0.73925 0.78246 0.80310 0.06816  0.01921  0.04647  84  PRO C CA    
2652 C  C     . PRO C 84  ? 0.74832 0.78942 0.82716 0.06197  0.02488  0.05774  84  PRO C C     
2653 O  O     . PRO C 84  ? 0.74023 0.78091 0.81695 0.05618  0.02049  0.05858  84  PRO C O     
2654 C  CB    . PRO C 84  ? 0.69906 0.73208 0.75874 0.06673  0.00609  0.04670  84  PRO C CB    
2655 C  CG    . PRO C 84  ? 0.70399 0.74377 0.74997 0.06340  0.00319  0.03439  84  PRO C CG    
2656 C  CD    . PRO C 84  ? 0.68592 0.74501 0.72700 0.06728  0.01270  0.02239  84  PRO C CD    
2657 N  N     . GLY C 85  ? 0.72646 0.76431 0.81801 0.06525  0.03598  0.06732  85  GLY C N     
2658 C  CA    . GLY C 85  ? 0.67432 0.70974 0.78213 0.06511  0.04381  0.07936  85  GLY C CA    
2659 C  C     . GLY C 85  ? 0.74171 0.78437 0.87178 0.06255  0.02997  0.09344  85  GLY C C     
2660 O  O     . GLY C 85  ? 0.82002 0.86784 0.96591 0.06045  0.02376  0.09995  85  GLY C O     
2661 N  N     . THR C 86  ? 0.75265 0.79517 0.88191 0.06108  0.02473  0.09857  86  THR C N     
2662 C  CA    . THR C 86  ? 0.84159 0.89531 0.98697 0.05730  0.00655  0.11096  86  THR C CA    
2663 C  C     . THR C 86  ? 0.79696 0.86579 0.98024 0.06559  0.01109  0.13072  86  THR C C     
2664 O  O     . THR C 86  ? 0.83603 0.89780 1.02204 0.07637  0.02456  0.13807  86  THR C O     
2665 C  CB    . THR C 86  ? 0.91029 0.95617 1.03176 0.05342  -0.00231 0.10919  86  THR C CB    
2666 O  OG1   . THR C 86  ? 0.99834 1.03343 1.08838 0.04826  0.00232  0.08977  86  THR C OG1   
2667 C  CG2   . THR C 86  ? 0.89047 0.94678 1.01592 0.04533  -0.02628 0.11612  86  THR C CG2   
2668 N  N     . ILE C 87  ? 0.73953 0.82840 0.95228 0.06043  0.00169  0.13900  87  ILE C N     
2669 C  CA    . ILE C 87  ? 0.73371 0.84968 0.99223 0.06727  0.00389  0.15833  87  ILE C CA    
2670 C  C     . ILE C 87  ? 0.76930 0.91007 1.04328 0.05940  -0.02357 0.16837  87  ILE C C     
2671 O  O     . ILE C 87  ? 0.76987 0.92012 1.04748 0.04209  -0.03999 0.16434  87  ILE C O     
2672 C  CB    . ILE C 87  ? 0.81121 0.93759 1.09558 0.06362  0.01569  0.16061  87  ILE C CB    
2673 C  CG1   . ILE C 87  ? 0.83994 0.93815 1.09608 0.06892  0.03807  0.14842  87  ILE C CG1   
2674 C  CG2   . ILE C 87  ? 0.69368 0.85335 1.03050 0.07343  0.02419  0.18011  87  ILE C CG2   
2675 C  CD1   . ILE C 87  ? 0.74331 0.83029 0.99642 0.08459  0.06064  0.15081  87  ILE C CD1   
2676 N  N     . ASP C 88  ? 0.72686 0.87457 1.00544 0.07158  -0.02880 0.18150  88  ASP C N     
2677 C  CA    . ASP C 88  ? 0.82785 1.00026 1.11511 0.06570  -0.05791 0.19239  88  ASP C CA    
2678 C  C     . ASP C 88  ? 0.83953 1.06244 1.18540 0.06131  -0.06879 0.20671  88  ASP C C     
2679 O  O     . ASP C 88  ? 0.80617 1.04633 1.19117 0.07042  -0.04933 0.21393  88  ASP C O     
2680 C  CB    . ASP C 88  ? 0.89676 1.05996 1.17025 0.08370  -0.05935 0.20599  88  ASP C CB    
2681 C  CG    . ASP C 88  ? 0.97526 1.09135 1.19055 0.08164  -0.04931 0.19116  88  ASP C CG    
2682 O  OD1   . ASP C 88  ? 0.96594 1.07027 1.14772 0.06473  -0.06198 0.17654  88  ASP C OD1   
2683 O  OD2   . ASP C 88  ? 0.93655 1.02675 1.13946 0.09574  -0.02678 0.19307  88  ASP C OD2   
2684 N  N     . ALA C 89  ? 0.92894 1.17709 1.27960 0.04492  -0.09974 0.20977  89  ALA C N     
2685 C  CA    . ALA C 89  ? 0.85611 1.15855 1.26349 0.03295  -0.11356 0.22038  89  ALA C CA    
2686 C  C     . ALA C 89  ? 0.80077 1.15092 1.26501 0.05771  -0.11104 0.24553  89  ALA C C     
2687 O  O     . ALA C 89  ? 0.84177 1.23609 1.36465 0.05655  -0.10350 0.25433  89  ALA C O     
2688 C  CB    . ALA C 89  ? 0.94963 1.26611 1.34226 0.00641  -0.14944 0.21551  89  ALA C CB    
2689 N  N     . ASP C 90  ? 0.87112 1.21177 1.31874 0.08143  -0.11501 0.25806  90  ASP C N     
2690 C  CA    . ASP C 90  ? 0.91449 1.29480 1.41145 0.11148  -0.11252 0.28405  90  ASP C CA    
2691 C  C     . ASP C 90  ? 0.93729 1.28982 1.44099 0.13834  -0.07123 0.28669  90  ASP C C     
2692 O  O     . ASP C 90  ? 0.86882 1.22854 1.39174 0.17014  -0.06267 0.30645  90  ASP C O     
2693 C  CB    . ASP C 90  ? 0.91640 1.29368 1.38637 0.12614  -0.13728 0.29924  90  ASP C CB    
2694 C  CG    . ASP C 90  ? 0.94050 1.24361 1.33383 0.12908  -0.12515 0.28734  90  ASP C CG    
2695 O  OD1   . ASP C 90  ? 0.93301 1.19378 1.29901 0.12072  -0.09955 0.26700  90  ASP C OD1   
2696 O  OD2   . ASP C 90  ? 1.00776 1.29714 1.36786 0.13898  -0.14167 0.29887  90  ASP C OD2   
2697 N  N     . TYR C 91  ? 0.85568 1.17378 1.34012 0.12727  -0.04559 0.26750  91  TYR C N     
2698 C  CA    . TYR C 91  ? 0.86708 1.15383 1.34839 0.14802  -0.00658 0.26625  91  TYR C CA    
2699 C  C     . TYR C 91  ? 0.88820 1.22062 1.43540 0.15556  0.01141  0.27673  91  TYR C C     
2700 O  O     . TYR C 91  ? 0.91042 1.26464 1.47798 0.13249  0.01017  0.26912  91  TYR C O     
2701 C  CB    . TYR C 91  ? 0.82459 1.05630 1.25056 0.13283  0.00994  0.24103  91  TYR C CB    
2702 C  CG    . TYR C 91  ? 0.91221 1.10772 1.32484 0.14949  0.04790  0.23648  91  TYR C CG    
2703 C  CD1   . TYR C 91  ? 0.84927 1.01214 1.24124 0.17200  0.06293  0.24310  91  TYR C CD1   
2704 C  CD2   . TYR C 91  ? 0.86790 1.05600 1.28194 0.14146  0.06938  0.22526  91  TYR C CD2   
2705 C  CE1   . TYR C 91  ? 0.92103 1.04513 1.29481 0.18390  0.09842  0.23635  91  TYR C CE1   
2706 C  CE2   . TYR C 91  ? 0.83126 0.98431 1.22637 0.15440  0.10309  0.21947  91  TYR C CE2   
2707 C  CZ    . TYR C 91  ? 0.92473 1.04593 1.29995 0.17445  0.11751  0.22383  91  TYR C CZ    
2708 O  OH    . TYR C 91  ? 0.88230 0.96321 1.23310 0.18413  0.15186  0.21559  91  TYR C OH    
2709 N  N     . ARG C 92  ? 0.91175 1.25541 1.49044 0.18828  0.03067  0.29445  92  ARG C N     
2710 C  CA    . ARG C 92  ? 0.85370 1.24242 1.49781 0.20044  0.05343  0.30558  92  ARG C CA    
2711 C  C     . ARG C 92  ? 0.94001 1.28027 1.56322 0.21727  0.09934  0.29815  92  ARG C C     
2712 O  O     . ARG C 92  ? 0.93179 1.30085 1.60328 0.23233  0.12574  0.30734  92  ARG C O     
2713 C  CB    . ARG C 92  ? 0.88265 1.33403 1.59035 0.22852  0.04075  0.33365  92  ARG C CB    
2714 C  CG    . ARG C 92  ? 0.91739 1.42543 1.64868 0.21004  -0.00729 0.34160  92  ARG C CG    
2715 C  CD    . ARG C 92  ? 0.82197 1.35399 1.56474 0.16682  -0.01891 0.32566  92  ARG C CD    
2716 N  NE    . ARG C 92  ? 0.88611 1.44488 1.62144 0.14102  -0.06455 0.32435  92  ARG C NE    
2717 C  CZ    . ARG C 92  ? 0.91084 1.45768 1.62087 0.10140  -0.07898 0.30526  92  ARG C CZ    
2718 N  NH1   . ARG C 92  ? 0.92882 1.43860 1.61880 0.08473  -0.05350 0.28791  92  ARG C NH1   
2719 N  NH2   . ARG C 92  ? 0.99421 1.56229 1.69370 0.07903  -0.11955 0.30377  92  ARG C NH2   
2720 N  N     . GLY C 93  ? 0.90611 1.17560 1.45841 0.21362  0.11014  0.28084  93  GLY C N     
2721 C  CA    . GLY C 93  ? 0.89399 1.11384 1.41715 0.22447  0.15090  0.27053  93  GLY C CA    
2722 C  C     . GLY C 93  ? 0.89239 1.10484 1.40312 0.20097  0.16417  0.25352  93  GLY C C     
2723 O  O     . GLY C 93  ? 0.82475 1.06572 1.34891 0.17652  0.14406  0.24981  93  GLY C O     
2724 N  N     . GLU C 94  ? 0.83057 0.99841 1.30948 0.20866  0.19964  0.24314  94  GLU C N     
2725 C  CA    . GLU C 94  ? 0.83115 0.98285 1.28637 0.18987  0.21460  0.22791  94  GLU C CA    
2726 C  C     . GLU C 94  ? 0.80582 0.91849 1.19740 0.16855  0.19707  0.20713  94  GLU C C     
2727 O  O     . GLU C 94  ? 0.78704 0.85782 1.13350 0.17237  0.20084  0.19689  94  GLU C O     
2728 C  CB    . GLU C 94  ? 0.89642 1.01595 1.33780 0.20633  0.25897  0.22460  94  GLU C CB    
2729 C  CG    . GLU C 94  ? 0.88747 0.98241 1.29146 0.18841  0.27500  0.20917  94  GLU C CG    
2730 C  CD    . GLU C 94  ? 0.92293 0.97624 1.29806 0.20279  0.31832  0.20262  94  GLU C CD    
2731 O  OE1   . GLU C 94  ? 0.83749 0.87075 1.21360 0.22591  0.33626  0.20698  94  GLU C OE1   
2732 O  OE2   . GLU C 94  ? 0.95196 0.98782 1.29854 0.19142  0.33528  0.19333  94  GLU C OE2   
2733 N  N     . VAL C 95  ? 0.80794 0.93408 1.19658 0.14618  0.17954  0.20094  95  VAL C N     
2734 C  CA    . VAL C 95  ? 0.80478 0.90125 1.13968 0.12959  0.16257  0.18257  95  VAL C CA    
2735 C  C     . VAL C 95  ? 0.85696 0.91061 1.14153 0.13032  0.18637  0.16704  95  VAL C C     
2736 O  O     . VAL C 95  ? 0.86996 0.91844 1.15390 0.13119  0.20895  0.16766  95  VAL C O     
2737 C  CB    . VAL C 95  ? 0.77064 0.88589 1.11325 0.10922  0.14145  0.18117  95  VAL C CB    
2738 C  CG1   . VAL C 95  ? 0.72370 0.80747 1.01130 0.09802  0.12966  0.16266  95  VAL C CG1   
2739 C  CG2   . VAL C 95  ? 0.72063 0.87433 1.10203 0.10354  0.11325  0.19220  95  VAL C CG2   
2740 N  N     . LYS C 96  ? 0.79305 0.81691 1.03352 0.12791  0.18163  0.15265  96  LYS C N     
2741 C  CA    . LYS C 96  ? 0.83402 0.82123 1.02350 0.12447  0.19887  0.13524  96  LYS C CA    
2742 C  C     . LYS C 96  ? 0.83066 0.81408 0.98409 0.10914  0.17619  0.11889  96  LYS C C     
2743 O  O     . LYS C 96  ? 0.83278 0.83183 0.99441 0.10331  0.15150  0.11910  96  LYS C O     
2744 C  CB    . LYS C 96  ? 0.80581 0.75994 0.97484 0.13395  0.21919  0.13082  96  LYS C CB    
2745 C  CG    . LYS C 96  ? 0.85599 0.80908 1.05755 0.15508  0.24665  0.14660  96  LYS C CG    
2746 C  CD    . LYS C 96  ? 1.01355 0.91841 1.18211 0.16463  0.27194  0.13974  96  LYS C CD    
2747 C  CE    . LYS C 96  ? 1.00975 0.90076 1.19244 0.18508  0.30978  0.14792  96  LYS C CE    
2748 N  NZ    . LYS C 96  ? 0.91531 0.74628 1.05509 0.19309  0.33855  0.13822  96  LYS C NZ    
2749 N  N     . VAL C 97  ? 0.84147 0.80549 0.95393 0.10379  0.18499  0.10471  97  VAL C N     
2750 C  CA    . VAL C 97  ? 0.74043 0.70727 0.82172 0.09337  0.16486  0.09013  97  VAL C CA    
2751 C  C     . VAL C 97  ? 0.81661 0.76335 0.85554 0.08644  0.17262  0.07084  97  VAL C C     
2752 O  O     . VAL C 97  ? 0.90559 0.82793 0.92266 0.08769  0.19611  0.06631  97  VAL C O     
2753 C  CB    . VAL C 97  ? 0.77970 0.74868 0.85056 0.09295  0.16236  0.09287  97  VAL C CB    
2754 C  CG1   . VAL C 97  ? 0.77017 0.74390 0.81008 0.08822  0.14119  0.07956  97  VAL C CG1   
2755 C  CG2   . VAL C 97  ? 0.75378 0.73999 0.86574 0.09392  0.15660  0.11025  97  VAL C CG2   
2756 N  N     . ILE C 98  ? 0.82705 0.78426 0.85374 0.07723  0.15428  0.05832  98  ILE C N     
2757 C  CA    . ILE C 98  ? 0.82440 0.77129 0.81477 0.06479  0.15824  0.03782  98  ILE C CA    
2758 C  C     . ILE C 98  ? 0.81749 0.78568 0.78669 0.06062  0.14076  0.02630  98  ILE C C     
2759 O  O     . ILE C 98  ? 0.85823 0.85208 0.83620 0.05941  0.11987  0.02262  98  ILE C O     
2760 C  CB    . ILE C 98  ? 0.78479 0.73151 0.77847 0.05603  0.15343  0.03204  98  ILE C CB    
2761 C  CG1   . ILE C 98  ? 0.84469 0.77285 0.86143 0.06615  0.16565  0.04898  98  ILE C CG1   
2762 C  CG2   . ILE C 98  ? 0.63704 0.57021 0.59387 0.03809  0.16245  0.00997  98  ILE C CG2   
2763 C  CD1   . ILE C 98  ? 0.73583 0.65645 0.74941 0.05889  0.16192  0.04686  98  ILE C CD1   
2764 N  N     . LEU C 99  ? 0.80635 0.76342 0.74553 0.06043  0.14969  0.02118  99  LEU C N     
2765 C  CA    . LEU C 99  ? 0.83938 0.81661 0.75291 0.05899  0.13236  0.01125  99  LEU C CA    
2766 C  C     . LEU C 99  ? 0.81221 0.79674 0.69681 0.04116  0.13088  -0.01202 99  LEU C C     
2767 O  O     . LEU C 99  ? 0.86487 0.82090 0.72978 0.02968  0.15132  -0.02088 99  LEU C O     
2768 C  CB    . LEU C 99  ? 0.77780 0.73885 0.66753 0.06768  0.14057  0.01950  99  LEU C CB    
2769 C  CG    . LEU C 99  ? 0.91203 0.86950 0.82494 0.08125  0.14010  0.04089  99  LEU C CG    
2770 C  CD1   . LEU C 99  ? 1.02301 0.95904 0.90254 0.08639  0.15273  0.04730  99  LEU C CD1   
2771 C  CD2   . LEU C 99  ? 0.74834 0.72994 0.67597 0.08749  0.11376  0.04367  99  LEU C CD2   
2772 N  N     . VAL C 100 ? 0.82467 0.84777 0.70746 0.03853  0.10760  -0.02238 100 VAL C N     
2773 C  CA    . VAL C 100 ? 0.84302 0.88709 0.70315 0.01885  0.10187  -0.04563 100 VAL C CA    
2774 C  C     . VAL C 100 ? 0.93124 1.00699 0.77033 0.02633  0.08084  -0.04948 100 VAL C C     
2775 O  O     . VAL C 100 ? 0.81738 0.91362 0.67159 0.04630  0.06382  -0.03775 100 VAL C O     
2776 C  CB    . VAL C 100 ? 0.88951 0.96157 0.77461 0.00657  0.09430  -0.05602 100 VAL C CB    
2777 C  CG1   . VAL C 100 ? 0.81974 0.92478 0.73588 0.02434  0.07423  -0.04638 100 VAL C CG1   
2778 C  CG2   . VAL C 100 ? 0.90815 1.00935 0.77414 -0.01822 0.08871  -0.08139 100 VAL C CG2   
2779 N  N     . ASN C 101 ? 1.04439 1.12016 0.84446 0.01101  0.08214  -0.06539 101 ASN C N     
2780 C  CA    . ASN C 101 ? 0.96073 1.06911 0.73466 0.01765  0.05966  -0.06918 101 ASN C CA    
2781 C  C     . ASN C 101 ? 0.96941 1.14158 0.75992 0.00544  0.03712  -0.08767 101 ASN C C     
2782 O  O     . ASN C 101 ? 1.05086 1.23416 0.82713 -0.02366 0.04023  -0.10989 101 ASN C O     
2783 C  CB    . ASN C 101 ? 1.14795 1.22473 0.86645 0.00626  0.07130  -0.07707 101 ASN C CB    
2784 C  CG    . ASN C 101 ? 1.23191 1.34602 0.91676 0.01020  0.04460  -0.08262 101 ASN C CG    
2785 O  OD1   . ASN C 101 ? 1.16471 1.31687 0.86649 0.03247  0.02041  -0.07189 101 ASN C OD1   
2786 N  ND2   . ASN C 101 ? 1.36326 1.46454 0.99695 -0.01044 0.04875  -0.09931 101 ASN C ND2   
2787 N  N     . LEU C 102 ? 1.00621 1.22005 0.82709 0.02692  0.01619  -0.07922 102 LEU C N     
2788 C  CA    . LEU C 102 ? 1.07058 1.35500 0.91443 0.02114  -0.00518 -0.09468 102 LEU C CA    
2789 C  C     . LEU C 102 ? 1.01574 1.34568 0.84012 0.03628  -0.03275 -0.09502 102 LEU C C     
2790 O  O     . LEU C 102 ? 0.97581 1.37388 0.82698 0.04224  -0.05404 -0.10265 102 LEU C O     
2791 C  CB    . LEU C 102 ? 0.91574 1.21968 0.80631 0.03667  -0.00846 -0.08707 102 LEU C CB    
2792 C  CG    . LEU C 102 ? 0.94920 1.22199 0.85915 0.01862  0.01375  -0.08947 102 LEU C CG    
2793 C  CD1   . LEU C 102 ? 0.86885 1.16210 0.81730 0.03265  0.00907  -0.08374 102 LEU C CD1   
2794 C  CD2   . LEU C 102 ? 0.90585 1.18949 0.80783 -0.01894 0.02351  -0.11316 102 LEU C CD2   
2795 N  N     . GLY C 103 ? 1.23281 1.52793 1.01075 0.04426  -0.03231 -0.08590 103 GLY C N     
2796 C  CA    . GLY C 103 ? 1.31164 1.64465 1.05949 0.05622  -0.05898 -0.08608 103 GLY C CA    
2797 C  C     . GLY C 103 ? 1.37479 1.73299 1.09196 0.02113  -0.06477 -0.11192 103 GLY C C     
2798 O  O     . GLY C 103 ? 1.38359 1.72424 1.10108 -0.01327 -0.04551 -0.13047 103 GLY C O     
2799 N  N     . ASN C 104 ? 1.36281 1.75996 1.04887 0.02995  -0.09234 -0.11276 104 ASN C N     
2800 C  CA    . ASN C 104 ? 1.37160 1.80147 1.02415 -0.00423 -0.10454 -0.13837 104 ASN C CA    
2801 C  C     . ASN C 104 ? 1.42650 1.79294 1.00303 -0.01341 -0.09321 -0.13787 104 ASN C C     
2802 O  O     . ASN C 104 ? 1.33111 1.71677 0.86683 -0.04216 -0.10432 -0.15932 104 ASN C O     
2803 C  CB    . ASN C 104 ? 1.45565 1.98347 1.12409 0.00867  -0.14671 -0.14228 104 ASN C CB    
2804 C  CG    . ASN C 104 ? 1.54327 2.07301 1.20246 0.06073  -0.16620 -0.11209 104 ASN C CG    
2805 O  OD1   . ASN C 104 ? 1.48277 1.96887 1.16016 0.08937  -0.15152 -0.09008 104 ASN C OD1   
2806 N  ND2   . ASN C 104 ? 1.28080 1.85866 0.90807 0.07244  -0.19977 -0.11069 104 ASN C ND2   
2807 N  N     . GLU C 105 ? 1.50090 1.79337 1.05662 0.00798  -0.07030 -0.11523 105 GLU C N     
2808 C  CA    . GLU C 105 ? 1.53860 1.76867 1.02199 0.00335  -0.05539 -0.11220 105 GLU C CA    
2809 C  C     . GLU C 105 ? 1.47647 1.62593 0.96059 -0.00299 -0.01100 -0.10684 105 GLU C C     
2810 O  O     . GLU C 105 ? 1.42469 1.56576 0.96352 0.00474  0.00306  -0.09814 105 GLU C O     
2811 C  CB    . GLU C 105 ? 1.64758 1.87085 1.09630 0.04108  -0.07265 -0.08536 105 GLU C CB    
2812 C  CG    . GLU C 105 ? 1.74094 2.04662 1.19475 0.05845  -0.11852 -0.08439 105 GLU C CG    
2813 C  CD    . GLU C 105 ? 1.94105 2.23507 1.38144 0.10566  -0.13212 -0.05138 105 GLU C CD    
2814 O  OE1   . GLU C 105 ? 2.02413 2.24258 1.43301 0.11769  -0.10681 -0.03177 105 GLU C OE1   
2815 O  OE2   . GLU C 105 ? 1.99636 2.35606 1.45842 0.13105  -0.16641 -0.04476 105 GLU C OE2   
2816 N  N     . GLU C 106 ? 1.68243 1.77421 1.10405 -0.01621 0.01094  -0.11209 106 GLU C N     
2817 C  CA    . GLU C 106 ? 1.59111 1.60908 1.01240 -0.01703 0.05450  -0.10488 106 GLU C CA    
2818 C  C     . GLU C 106 ? 1.57151 1.56220 1.00535 0.01763  0.06328  -0.07220 106 GLU C C     
2819 O  O     . GLU C 106 ? 1.63789 1.63395 1.03939 0.03752  0.04582  -0.05705 106 GLU C O     
2820 C  CB    . GLU C 106 ? 1.69189 1.65509 1.03997 -0.04041 0.07872  -0.12182 106 GLU C CB    
2821 C  CG    . GLU C 106 ? 1.84129 1.82439 1.16539 -0.08037 0.07035  -0.15682 106 GLU C CG    
2822 C  CD    . GLU C 106 ? 1.93947 1.84738 1.21740 -0.10558 0.11175  -0.17516 106 GLU C CD    
2823 O  OE1   . GLU C 106 ? 1.95088 1.79782 1.22126 -0.08872 0.14707  -0.15956 106 GLU C OE1   
2824 O  OE2   . GLU C 106 ? 1.81597 1.72548 1.06588 -0.14262 0.11051  -0.20565 106 GLU C OE2   
2825 N  N     . VAL C 107 ? 1.31288 1.27389 0.79257 0.02395  0.09002  -0.06086 107 VAL C N     
2826 C  CA    . VAL C 107 ? 1.33163 1.26870 0.83129 0.05057  0.10051  -0.03189 107 VAL C CA    
2827 C  C     . VAL C 107 ? 1.34914 1.22677 0.84150 0.04697  0.14386  -0.02633 107 VAL C C     
2828 O  O     . VAL C 107 ? 1.43204 1.29123 0.93282 0.03036  0.16562  -0.04102 107 VAL C O     
2829 C  CB    . VAL C 107 ? 1.31793 1.28697 0.88918 0.06414  0.08744  -0.02095 107 VAL C CB    
2830 C  CG1   . VAL C 107 ? 1.26076 1.28627 0.83830 0.07627  0.04791  -0.02174 107 VAL C CG1   
2831 C  CG2   . VAL C 107 ? 1.17557 1.14924 0.79048 0.04643  0.10008  -0.03486 107 VAL C CG2   
2832 N  N     . VAL C 108 ? 1.22420 1.07092 0.70060 0.06346  0.15816  -0.00436 108 VAL C N     
2833 C  CA    . VAL C 108 ? 1.33916 1.13650 0.81249 0.06330  0.20098  0.00369  108 VAL C CA    
2834 C  C     . VAL C 108 ? 1.27553 1.07449 0.81010 0.07885  0.20913  0.02796  108 VAL C C     
2835 O  O     . VAL C 108 ? 1.23373 1.04054 0.77001 0.09275  0.19233  0.04511  108 VAL C O     
2836 C  CB    . VAL C 108 ? 1.37967 1.13659 0.77534 0.06374  0.21719  0.00692  108 VAL C CB    
2837 C  CG1   . VAL C 108 ? 1.39523 1.10443 0.78855 0.06138  0.26653  0.00978  108 VAL C CG1   
2838 C  CG2   . VAL C 108 ? 1.26521 1.02946 0.59461 0.04764  0.19776  -0.01674 108 VAL C CG2   
2839 N  N     . ILE C 109 ? 1.29367 1.08412 0.87641 0.07640  0.23428  0.02939  109 ILE C N     
2840 C  CA    . ILE C 109 ? 1.24035 1.03445 0.88217 0.08697  0.24457  0.05096  109 ILE C CA    
2841 C  C     . ILE C 109 ? 1.31880 1.07686 0.94966 0.08914  0.28636  0.06123  109 ILE C C     
2842 O  O     . ILE C 109 ? 1.35137 1.08964 0.97912 0.08497  0.31493  0.05164  109 ILE C O     
2843 C  CB    . ILE C 109 ? 1.30441 1.12291 1.01249 0.08503  0.24000  0.04806  109 ILE C CB    
2844 C  CG1   . ILE C 109 ? 1.14770 1.00415 0.87895 0.08691  0.20133  0.04619  109 ILE C CG1   
2845 C  CG2   . ILE C 109 ? 1.22834 1.04530 0.99222 0.09216  0.26159  0.06718  109 ILE C CG2   
2846 C  CD1   . ILE C 109 ? 1.21827 1.09351 0.91276 0.07878  0.17727  0.02587  109 ILE C CD1   
2847 N  N     . GLU C 110 ? 1.38163 1.12815 1.00415 0.09582  0.29254  0.08055  110 GLU C N     
2848 C  CA    . GLU C 110 ? 1.41716 1.13091 1.02245 0.09647  0.33380  0.09067  110 GLU C CA    
2849 C  C     . GLU C 110 ? 1.34166 1.07101 1.02549 0.09929  0.35651  0.10469  110 GLU C C     
2850 O  O     . GLU C 110 ? 1.25214 1.01357 0.99731 0.10037  0.33977  0.10530  110 GLU C O     
2851 C  CB    . GLU C 110 ? 1.39541 1.08512 0.94672 0.09984  0.33194  0.10522  110 GLU C CB    
2852 C  CG    . GLU C 110 ? 1.56424 1.21923 1.02430 0.09671  0.34039  0.09498  110 GLU C CG    
2853 C  CD    . GLU C 110 ? 1.68333 1.30406 1.12460 0.09264  0.39061  0.09260  110 GLU C CD    
2854 O  OE1   . GLU C 110 ? 1.60928 1.23617 1.11102 0.09497  0.41989  0.10403  110 GLU C OE1   
2855 O  OE2   . GLU C 110 ? 1.70242 1.29191 1.06821 0.08720  0.40096  0.07878  110 GLU C OE2   
2856 N  N     . ARG C 111 ? 1.46232 1.17177 1.14419 0.10009  0.39522  0.11630  111 ARG C N     
2857 C  CA    . ARG C 111 ? 1.42150 1.15456 1.18178 0.10236  0.41775  0.13059  111 ARG C CA    
2858 C  C     . ARG C 111 ? 1.42435 1.18340 1.22996 0.09859  0.39324  0.14643  111 ARG C C     
2859 O  O     . ARG C 111 ? 1.57930 1.32031 1.34555 0.09573  0.37985  0.15390  111 ARG C O     
2860 C  CB    . ARG C 111 ? 1.58931 1.29873 1.33588 0.10287  0.46720  0.13906  111 ARG C CB    
2861 N  N     . GLY C 112 ? 1.28716 1.08515 1.17164 0.09907  0.38730  0.15155  112 GLY C N     
2862 C  CA    . GLY C 112 ? 1.30310 1.12634 1.23539 0.09213  0.36658  0.16451  112 GLY C CA    
2863 C  C     . GLY C 112 ? 1.20630 1.01596 1.09932 0.09028  0.33063  0.16301  112 GLY C C     
2864 O  O     . GLY C 112 ? 1.20980 1.00957 1.10215 0.08346  0.32725  0.17571  112 GLY C O     
2865 N  N     . GLU C 113 ? 1.25307 1.06132 1.11311 0.09631  0.30537  0.14750  113 GLU C N     
2866 C  CA    . GLU C 113 ? 1.21726 1.01841 1.04194 0.09956  0.27160  0.14537  113 GLU C CA    
2867 C  C     . GLU C 113 ? 1.09299 0.92437 0.96801 0.09840  0.24261  0.14382  113 GLU C C     
2868 O  O     . GLU C 113 ? 1.12699 0.98499 1.04269 0.09744  0.23815  0.13599  113 GLU C O     
2869 C  CB    . GLU C 113 ? 1.22714 1.02036 0.99335 0.10515  0.25819  0.12867  113 GLU C CB    
2870 C  CG    . GLU C 113 ? 1.16539 0.96109 0.90059 0.11303  0.22235  0.12679  113 GLU C CG    
2871 C  CD    . GLU C 113 ? 1.31168 1.10759 0.98993 0.11654  0.20857  0.11121  113 GLU C CD    
2872 O  OE1   . GLU C 113 ? 1.24218 1.02157 0.88768 0.11100  0.23013  0.10350  113 GLU C OE1   
2873 O  OE2   . GLU C 113 ? 1.27776 1.09207 0.94436 0.12440  0.17655  0.10591  113 GLU C OE2   
2874 N  N     . ARG C 114 ? 1.16729 0.98863 1.03383 0.09910  0.22450  0.15163  114 ARG C N     
2875 C  CA    . ARG C 114 ? 1.06376 0.90645 0.96454 0.09865  0.19645  0.14799  114 ARG C CA    
2876 C  C     . ARG C 114 ? 1.08463 0.94745 0.97371 0.10652  0.17365  0.13035  114 ARG C C     
2877 O  O     . ARG C 114 ? 1.17450 1.02925 1.01724 0.11624  0.15986  0.12490  114 ARG C O     
2878 C  CB    . ARG C 114 ? 1.07773 0.89383 0.95761 0.10029  0.18461  0.15799  114 ARG C CB    
2879 N  N     . ILE C 115 ? 1.00654 0.89722 0.93722 0.10207  0.16983  0.12210  115 ILE C N     
2880 C  CA    . ILE C 115 ? 1.00939 0.91901 0.93221 0.10461  0.15308  0.10472  115 ILE C CA    
2881 C  C     . ILE C 115 ? 0.95648 0.88878 0.91235 0.10338  0.13033  0.10042  115 ILE C C     
2882 O  O     . ILE C 115 ? 0.86908 0.81863 0.81778 0.10462  0.11539  0.08615  115 ILE C O     
2883 C  CB    . ILE C 115 ? 0.93617 0.84784 0.86277 0.10022  0.17234  0.09612  115 ILE C CB    
2884 C  CG1   . ILE C 115 ? 1.01687 0.93328 0.99279 0.09754  0.19249  0.10794  115 ILE C CG1   
2885 C  CG2   . ILE C 115 ? 1.12856 1.01670 1.00190 0.10132  0.18848  0.09153  115 ILE C CG2   
2886 C  CD1   . ILE C 115 ? 1.03128 0.97228 1.05299 0.09544  0.17878  0.10722  115 ILE C CD1   
2887 N  N     . ALA C 116 ? 0.90567 0.83911 0.89547 0.09872  0.12790  0.11119  116 ALA C N     
2888 C  CA    . ALA C 116 ? 0.95342 0.90289 0.96740 0.09632  0.10700  0.10699  116 ALA C CA    
2889 C  C     . ALA C 116 ? 0.99149 0.93094 1.02627 0.08866  0.10566  0.11949  116 ALA C C     
2890 O  O     . ALA C 116 ? 1.03525 0.95936 1.07067 0.08396  0.12218  0.13141  116 ALA C O     
2891 C  CB    . ALA C 116 ? 0.94377 0.91574 0.98775 0.09148  0.10681  0.10103  116 ALA C CB    
2892 N  N     . GLN C 117 ? 0.95816 0.90493 1.00742 0.08486  0.08724  0.11561  117 GLN C N     
2893 C  CA    . GLN C 117 ? 0.96271 0.90035 1.03081 0.07238  0.08335  0.12397  117 GLN C CA    
2894 C  C     . GLN C 117 ? 0.97417 0.93789 1.07786 0.06276  0.06994  0.12113  117 GLN C C     
2895 O  O     . GLN C 117 ? 0.96617 0.94251 1.06551 0.06826  0.05864  0.11054  117 GLN C O     
2896 C  CB    . GLN C 117 ? 1.00265 0.90692 1.03545 0.07761  0.07367  0.12218  117 GLN C CB    
2897 C  CG    . GLN C 117 ? 0.98608 0.89472 0.99554 0.09349  0.05766  0.10849  117 GLN C CG    
2898 C  CD    . GLN C 117 ? 1.21692 1.08944 1.18908 0.10612  0.05204  0.10920  117 GLN C CD    
2899 O  OE1   . GLN C 117 ? 1.23230 1.08583 1.20249 0.10168  0.04420  0.10672  117 GLN C OE1   
2900 N  NE2   . GLN C 117 ? 1.23671 1.09621 1.17500 0.12296  0.05620  0.11286  117 GLN C NE2   
2901 N  N     . LEU C 118 ? 0.96765 0.94130 1.10576 0.04716  0.07122  0.13100  118 LEU C N     
2902 C  CA    . LEU C 118 ? 0.84072 0.84278 1.01343 0.03739  0.05675  0.13157  118 LEU C CA    
2903 C  C     . LEU C 118 ? 0.93019 0.91783 1.09814 0.02104  0.04090  0.12911  118 LEU C C     
2904 O  O     . LEU C 118 ? 1.03912 1.01710 1.21667 0.00560  0.04682  0.13641  118 LEU C O     
2905 C  CB    . LEU C 118 ? 0.80846 0.84336 1.02993 0.03285  0.06842  0.14493  118 LEU C CB    
2906 C  CG    . LEU C 118 ? 0.80356 0.87305 1.06602 0.02151  0.05116  0.15047  118 LEU C CG    
2907 C  CD1   . LEU C 118 ? 0.75631 0.83483 1.01163 0.03199  0.03803  0.14460  118 LEU C CD1   
2908 C  CD2   . LEU C 118 ? 0.72917 0.83558 1.04569 0.01838  0.06470  0.16603  118 LEU C CD2   
2909 N  N     . VAL C 119 ? 0.84351 0.82706 0.99425 0.02225  0.02300  0.11791  119 VAL C N     
2910 C  CA    . VAL C 119 ? 0.88086 0.84403 1.01822 0.00691  0.00837  0.11208  119 VAL C CA    
2911 C  C     . VAL C 119 ? 0.94759 0.94280 1.11470 -0.00846 -0.00872 0.11405  119 VAL C C     
2912 O  O     . VAL C 119 ? 0.91756 0.93457 1.09021 0.00045  -0.01544 0.11241  119 VAL C O     
2913 C  CB    . VAL C 119 ? 0.90083 0.83440 0.99361 0.02050  0.00211  0.09743  119 VAL C CB    
2914 C  CG1   . VAL C 119 ? 0.97262 0.87860 1.04657 0.00478  -0.01054 0.08953  119 VAL C CG1   
2915 C  CG2   . VAL C 119 ? 0.84341 0.74956 0.90702 0.03840  0.01532  0.09787  119 VAL C CG2   
2916 N  N     . ILE C 120 ? 0.94166 0.93921 1.12563 -0.03277 -0.01609 0.11796  120 ILE C N     
2917 C  CA    . ILE C 120 ? 0.94303 0.97198 1.15059 -0.04994 -0.03756 0.11936  120 ILE C CA    
2918 C  C     . ILE C 120 ? 0.99225 0.98637 1.15565 -0.05973 -0.05346 0.10348  120 ILE C C     
2919 O  O     . ILE C 120 ? 1.12717 1.07842 1.26207 -0.07114 -0.05006 0.09598  120 ILE C O     
2920 C  CB    . ILE C 120 ? 0.94179 1.00134 1.19557 -0.07472 -0.03884 0.13075  120 ILE C CB    
2921 C  CG1   . ILE C 120 ? 0.79577 0.88114 1.08796 -0.06302 -0.01550 0.14516  120 ILE C CG1   
2922 C  CG2   . ILE C 120 ? 0.76063 0.86592 1.04437 -0.08854 -0.06455 0.13474  120 ILE C CG2   
2923 C  CD1   . ILE C 120 ? 0.72765 0.84818 1.04374 -0.03899 -0.01310 0.15294  120 ILE C CD1   
2924 N  N     . ALA C 121 ? 0.90911 0.91592 1.06233 -0.05478 -0.06828 0.09847  121 ALA C N     
2925 C  CA    . ALA C 121 ? 1.07887 1.05219 1.18590 -0.06112 -0.08005 0.08214  121 ALA C CA    
2926 C  C     . ALA C 121 ? 1.07258 1.07378 1.18459 -0.07357 -0.10326 0.08352  121 ALA C C     
2927 O  O     . ALA C 121 ? 1.06684 1.10993 1.21166 -0.06549 -0.10764 0.09692  121 ALA C O     
2928 C  CB    . ALA C 121 ? 0.99255 0.94223 1.06452 -0.03526 -0.06858 0.07108  121 ALA C CB    
2929 N  N     . PRO C 122 ? 1.10180 1.07689 1.17740 -0.09223 -0.11803 0.07036  122 PRO C N     
2930 C  CA    . PRO C 122 ? 1.05722 1.05601 1.12802 -0.10451 -0.14244 0.07166  122 PRO C CA    
2931 C  C     . PRO C 122 ? 1.05254 1.04802 1.09666 -0.08304 -0.13938 0.06832  122 PRO C C     
2932 O  O     . PRO C 122 ? 1.10006 1.06070 1.10801 -0.07012 -0.12507 0.05419  122 PRO C O     
2933 C  CB    . PRO C 122 ? 1.06900 1.02940 1.09855 -0.13323 -0.15512 0.05500  122 PRO C CB    
2934 C  CG    . PRO C 122 ? 1.12126 1.02444 1.11657 -0.12264 -0.13255 0.04136  122 PRO C CG    
2935 C  CD    . PRO C 122 ? 1.23487 1.15348 1.26879 -0.10422 -0.11294 0.05447  122 PRO C CD    
2936 N  N     . VAL C 123 ? 1.07605 1.10894 1.13931 -0.07873 -0.15181 0.08231  123 VAL C N     
2937 C  CA    . VAL C 123 ? 1.12286 1.15049 1.15778 -0.06362 -0.14955 0.08112  123 VAL C CA    
2938 C  C     . VAL C 123 ? 1.10235 1.13415 1.10973 -0.08021 -0.17618 0.08194  123 VAL C C     
2939 O  O     . VAL C 123 ? 1.09689 1.15685 1.12660 -0.09797 -0.19908 0.09087  123 VAL C O     
2940 C  CB    . VAL C 123 ? 1.00351 1.05877 1.07273 -0.04118 -0.13759 0.09794  123 VAL C CB    
2941 C  CG1   . VAL C 123 ? 1.09927 1.19830 1.20872 -0.04309 -0.15591 0.11989  123 VAL C CG1   
2942 C  CG2   . VAL C 123 ? 1.08320 1.12084 1.11737 -0.02759 -0.12651 0.09244  123 VAL C CG2   
2943 N  N     . GLN C 124 ? 1.23034 1.23625 1.18801 -0.07578 -0.17326 0.07221  124 GLN C N     
2944 C  CA    . GLN C 124 ? 1.25056 1.24871 1.16520 -0.09226 -0.19634 0.06956  124 GLN C CA    
2945 C  C     . GLN C 124 ? 1.20296 1.21646 1.11051 -0.07852 -0.20092 0.08635  124 GLN C C     
2946 O  O     . GLN C 124 ? 1.20155 1.19827 1.09185 -0.06251 -0.17908 0.08341  124 GLN C O     
2947 C  CB    . GLN C 124 ? 1.23790 1.18548 1.09024 -0.10012 -0.18713 0.04399  124 GLN C CB    
2948 C  CG    . GLN C 124 ? 1.35790 1.28950 1.15777 -0.12352 -0.21147 0.03699  124 GLN C CG    
2949 C  CD    . GLN C 124 ? 1.46267 1.40324 1.27408 -0.15240 -0.23630 0.03513  124 GLN C CD    
2950 O  OE1   . GLN C 124 ? 1.48197 1.47109 1.34319 -0.15785 -0.25561 0.05393  124 GLN C OE1   
2951 N  NE2   . GLN C 124 ? 1.49646 1.39003 1.26234 -0.17160 -0.23422 0.01177  124 GLN C NE2   
2952 N  N     . ARG C 125 ? 1.11080 1.15651 1.03142 -0.08521 -0.22932 0.10442  125 ARG C N     
2953 C  CA    . ARG C 125 ? 1.21829 1.27125 1.12172 -0.07208 -0.23756 0.12280  125 ARG C CA    
2954 C  C     . ARG C 125 ? 1.20168 1.21717 1.02785 -0.08470 -0.24507 0.11054  125 ARG C C     
2955 O  O     . ARG C 125 ? 1.19349 1.20102 0.98967 -0.10859 -0.26578 0.09867  125 ARG C O     
2956 C  CB    . ARG C 125 ? 1.26269 1.36851 1.21010 -0.07072 -0.26732 0.14854  125 ARG C CB    
2957 C  CG    . ARG C 125 ? 1.14400 1.25385 1.05950 -0.06110 -0.28685 0.16862  125 ARG C CG    
2958 C  CD    . ARG C 125 ? 1.30029 1.38684 1.20704 -0.03338 -0.25944 0.17995  125 ARG C CD    
2959 N  NE    . ARG C 125 ? 1.30014 1.41430 1.27347 -0.01143 -0.24408 0.19508  125 ARG C NE    
2960 C  CZ    . ARG C 125 ? 1.29203 1.42914 1.29226 0.01205  -0.25011 0.22307  125 ARG C CZ    
2961 N  NH1   . ARG C 125 ? 1.21137 1.34872 1.17834 0.01850  -0.27329 0.24179  125 ARG C NH1   
2962 N  NH2   . ARG C 125 ? 1.10856 1.26569 1.16679 0.03140  -0.23138 0.23312  125 ARG C NH2   
2963 N  N     . VAL C 126 ? 1.14914 1.13871 0.93985 -0.07099 -0.22624 0.11227  126 VAL C N     
2964 C  CA    . VAL C 126 ? 1.27553 1.22603 0.98978 -0.08157 -0.22584 0.10021  126 VAL C CA    
2965 C  C     . VAL C 126 ? 1.29500 1.24569 0.97986 -0.07313 -0.23947 0.12442  126 VAL C C     
2966 O  O     . VAL C 126 ? 1.34426 1.31579 1.06592 -0.05343 -0.23862 0.14817  126 VAL C O     
2967 C  CB    . VAL C 126 ? 1.25129 1.16735 0.94092 -0.07608 -0.18795 0.07847  126 VAL C CB    
2968 C  CG1   . VAL C 126 ? 1.19703 1.11362 0.91878 -0.07731 -0.17460 0.05915  126 VAL C CG1   
2969 C  CG2   . VAL C 126 ? 1.11097 1.02799 0.81528 -0.05673 -0.16406 0.09102  126 VAL C CG2   
2970 N  N     . GLU C 127 ? 1.16747 1.08942 0.77989 -0.08723 -0.25091 0.11847  127 GLU C N     
2971 C  CA    . GLU C 127 ? 1.32731 1.23741 0.89333 -0.08019 -0.26252 0.14063  127 GLU C CA    
2972 C  C     . GLU C 127 ? 1.39302 1.25595 0.90743 -0.07653 -0.22527 0.13064  127 GLU C C     
2973 O  O     . GLU C 127 ? 1.37237 1.20383 0.83659 -0.09154 -0.21182 0.10595  127 GLU C O     
2974 C  CB    . GLU C 127 ? 1.19331 1.10333 0.70678 -0.10036 -0.30167 0.14201  127 GLU C CB    
2975 N  N     . VAL C 128 ? 1.34666 1.20389 0.87360 -0.05742 -0.20643 0.14902  128 VAL C N     
2976 C  CA    . VAL C 128 ? 1.38089 1.19806 0.86673 -0.05734 -0.16825 0.13967  128 VAL C CA    
2977 C  C     . VAL C 128 ? 1.45786 1.23597 0.85427 -0.06757 -0.17457 0.14475  128 VAL C C     
2978 O  O     . VAL C 128 ? 1.47107 1.24763 0.84178 -0.06102 -0.20176 0.17173  128 VAL C O     
2979 C  CB    . VAL C 128 ? 1.39999 1.21607 0.92024 -0.03813 -0.14606 0.15716  128 VAL C CB    
2980 C  CG1   . VAL C 128 ? 1.43884 1.21976 0.92540 -0.04423 -0.10409 0.14286  128 VAL C CG1   
2981 C  CG2   . VAL C 128 ? 1.27142 1.12666 0.87542 -0.02759 -0.14431 0.15503  128 VAL C CG2   
2982 N  N     . VAL C 129 ? 1.49934 1.24673 0.84685 -0.08214 -0.14907 0.11950  129 VAL C N     
2983 C  CA    . VAL C 129 ? 1.44801 1.15230 0.70296 -0.09413 -0.14744 0.12033  129 VAL C CA    
2984 C  C     . VAL C 129 ? 1.54376 1.21843 0.77286 -0.09846 -0.09852 0.10503  129 VAL C C     
2985 O  O     . VAL C 129 ? 1.46346 1.14946 0.72224 -0.10197 -0.07294 0.07780  129 VAL C O     
2986 C  CB    . VAL C 129 ? 1.51496 1.21115 0.72417 -0.11350 -0.16906 0.10051  129 VAL C CB    
2987 C  CG1   . VAL C 129 ? 1.52295 1.16855 0.63107 -0.12703 -0.15632 0.09498  129 VAL C CG1   
2988 C  CG2   . VAL C 129 ? 1.50713 1.23428 0.73271 -0.11494 -0.22070 0.11787  129 VAL C CG2   
2989 N  N     . GLU C 130 ? 1.55256 1.19069 0.72714 -0.09811 -0.08518 0.12325  130 GLU C N     
2990 C  CA    . GLU C 130 ? 1.54228 1.15303 0.69004 -0.10676 -0.03726 0.11032  130 GLU C CA    
2991 C  C     . GLU C 130 ? 1.62112 1.19700 0.68461 -0.12486 -0.02507 0.09317  130 GLU C C     
2992 O  O     . GLU C 130 ? 1.66025 1.20664 0.65188 -0.12961 -0.04859 0.10792  130 GLU C O     
2993 C  CB    . GLU C 130 ? 1.55665 1.13741 0.68604 -0.09958 -0.02287 0.13840  130 GLU C CB    
2994 C  CG    . GLU C 130 ? 1.63388 1.18614 0.73492 -0.11418 0.02833  0.12542  130 GLU C CG    
2995 C  CD    . GLU C 130 ? 1.75509 1.27034 0.83904 -0.10926 0.04519  0.15217  130 GLU C CD    
2996 O  OE1   . GLU C 130 ? 1.67784 1.19647 0.78886 -0.08919 0.02040  0.17865  130 GLU C OE1   
2997 O  OE2   . GLU C 130 ? 1.92901 1.41018 0.97222 -0.12561 0.08537  0.14654  130 GLU C OE2   
2998 N  N     . VAL C 131 ? 1.61737 1.19837 0.68915 -0.13371 0.01178  0.06221  131 VAL C N     
2999 C  CA    . VAL C 131 ? 1.63407 1.18291 0.63060 -0.14935 0.03240  0.04206  131 VAL C CA    
3000 C  C     . VAL C 131 ? 1.67617 1.21372 0.66200 -0.15829 0.08526  0.03258  131 VAL C C     
3001 O  O     . VAL C 131 ? 1.59833 1.16234 0.64713 -0.15414 0.10558  0.03237  131 VAL C O     
3002 C  CB    . VAL C 131 ? 1.64721 1.21272 0.65977 -0.15081 0.02920  0.01040  131 VAL C CB    
3003 C  CG1   . VAL C 131 ? 1.55728 1.13598 0.58574 -0.14732 -0.02168 0.01851  131 VAL C CG1   
3004 C  CG2   . VAL C 131 ? 1.61402 1.22081 0.70821 -0.14190 0.05855  -0.01107 131 VAL C CG2   
3005 N  N     . GLU C 132 ? 1.70165 1.19972 0.60441 -0.17320 0.10824  0.02380  132 GLU C N     
3006 C  CA    . GLU C 132 ? 1.78521 1.27257 0.67077 -0.18638 0.16155  0.01330  132 GLU C CA    
3007 C  C     . GLU C 132 ? 1.80328 1.32257 0.72090 -0.18843 0.19599  -0.02438 132 GLU C C     
3008 O  O     . GLU C 132 ? 1.88257 1.40858 0.80218 -0.19964 0.24221  -0.03671 132 GLU C O     
3009 C  CB    . GLU C 132 ? 1.82451 1.24807 0.59729 -0.20162 0.17301  0.02735  132 GLU C CB    
3010 N  N     . GLU C 133 ? 1.76699 1.30611 0.71028 -0.17764 0.17584  -0.04243 133 GLU C N     
3011 C  CA    . GLU C 133 ? 1.66666 1.23324 0.64030 -0.17299 0.20689  -0.07648 133 GLU C CA    
3012 C  C     . GLU C 133 ? 1.60451 1.19309 0.62600 -0.15660 0.17549  -0.08707 133 GLU C C     
3013 O  O     . GLU C 133 ? 1.71214 1.27764 0.70410 -0.15742 0.13469  -0.07651 133 GLU C O     
3014 C  CB    . GLU C 133 ? 1.83215 1.35738 0.71712 -0.18531 0.23643  -0.09404 133 GLU C CB    
3015 N  N     . VAL C 134 ? 1.63500 1.26907 0.72963 -0.14260 0.19445  -0.10721 134 VAL C N     
3016 C  CA    . VAL C 134 ? 1.65868 1.30935 0.79809 -0.12593 0.17135  -0.11801 134 VAL C CA    
3017 C  C     . VAL C 134 ? 1.57247 1.20781 0.68279 -0.11939 0.19695  -0.14867 134 VAL C C     
3018 O  O     . VAL C 134 ? 1.62870 1.25287 0.69873 -0.12569 0.23525  -0.16227 134 VAL C O     
3019 C  CB    . VAL C 134 ? 1.53499 1.24365 0.77533 -0.11030 0.16967  -0.11555 134 VAL C CB    
3020 C  CG1   . VAL C 134 ? 1.49475 1.21199 0.75827 -0.11635 0.15100  -0.08704 134 VAL C CG1   
3021 C  CG2   . VAL C 134 ? 1.45031 1.20109 0.73200 -0.10359 0.21376  -0.13584 134 VAL C CG2   
3022 N  N     . SER C 135 ? 1.63355 1.26516 0.76322 -0.10632 0.17806  -0.15956 135 SER C N     
3023 C  CA    . SER C 135 ? 1.79919 1.40638 0.89848 -0.09655 0.20122  -0.18844 135 SER C CA    
3024 C  C     . SER C 135 ? 1.68856 1.34707 0.85896 -0.07240 0.23738  -0.20501 135 SER C C     
3025 O  O     . SER C 135 ? 1.60775 1.31566 0.85902 -0.05880 0.22789  -0.19708 135 SER C O     
3026 C  CB    . SER C 135 ? 1.73547 1.30910 0.82059 -0.09428 0.16764  -0.19342 135 SER C CB    
3027 O  OG    . SER C 135 ? 1.64648 1.25870 0.81444 -0.07929 0.14714  -0.18411 135 SER C OG    
3028 N  N     . GLN C 136 ? 1.77840 1.42749 0.91778 -0.06639 0.27906  -0.22799 136 GLN C N     
3029 C  CA    . GLN C 136 ? 1.80875 1.50989 1.01519 -0.03905 0.31271  -0.24538 136 GLN C CA    
3030 C  C     . GLN C 136 ? 1.80564 1.49733 1.04049 -0.01256 0.29687  -0.25418 136 GLN C C     
3031 O  O     . GLN C 136 ? 1.92348 1.55130 1.09822 -0.01551 0.28322  -0.26211 136 GLN C O     
3032 C  CB    . GLN C 136 ? 1.62858 1.32080 0.79283 -0.03739 0.36335  -0.26792 136 GLN C CB    
3033 N  N     . THR C 137 ? 1.91052 1.66307 1.23326 0.01178  0.29848  -0.25269 137 THR C N     
3034 C  CA    . THR C 137 ? 1.97828 1.72084 1.33067 0.03617  0.27888  -0.25445 137 THR C CA    
3035 C  C     . THR C 137 ? 1.98757 1.79468 1.41779 0.07193  0.30181  -0.26312 137 THR C C     
3036 O  O     . THR C 137 ? 1.98315 1.86033 1.46798 0.07157  0.31683  -0.26017 137 THR C O     
3037 C  CB    . THR C 137 ? 1.97133 1.71364 1.34756 0.02309  0.23251  -0.23067 137 THR C CB    
3038 O  OG1   . THR C 137 ? 2.25017 1.93817 1.55590 -0.00717 0.20912  -0.22244 137 THR C OG1   
3039 C  CG2   . THR C 137 ? 1.90516 1.63400 1.30922 0.04554  0.21483  -0.23147 137 THR C CG2   
3040 N  N     . GLN C 138 ? 2.13981 1.92055 1.57166 0.10215  0.30375  -0.27369 138 GLN C N     
3041 C  CA    . GLN C 138 ? 2.13524 1.96559 1.63180 0.14452  0.32224  -0.28136 138 GLN C CA    
3042 C  C     . GLN C 138 ? 2.15559 2.08328 1.74129 0.14954  0.31902  -0.26998 138 GLN C C     
3043 O  O     . GLN C 138 ? 2.11391 2.10414 1.73459 0.15562  0.34951  -0.27937 138 GLN C O     
3044 C  CB    . GLN C 138 ? 2.18971 1.97260 1.68281 0.16788  0.30217  -0.27931 138 GLN C CB    
3045 N  N     . ARG C 139 ? 1.74353 1.68544 1.36548 0.14495  0.28348  -0.25097 139 ARG C N     
3046 C  CA    . ARG C 139 ? 1.62191 1.65082 1.32493 0.15198  0.27848  -0.24214 139 ARG C CA    
3047 C  C     . ARG C 139 ? 1.56087 1.63878 1.27819 0.12177  0.29355  -0.24172 139 ARG C C     
3048 O  O     . ARG C 139 ? 1.44225 1.60052 1.22459 0.12725  0.30253  -0.24313 139 ARG C O     
3049 C  CB    . ARG C 139 ? 1.39432 1.41744 1.12050 0.14799  0.23906  -0.22191 139 ARG C CB    
3050 C  CG    . ARG C 139 ? 1.34797 1.37028 1.06762 0.10920  0.21924  -0.20582 139 ARG C CG    
3051 C  CD    . ARG C 139 ? 1.27880 1.29659 1.02334 0.10824  0.18436  -0.18687 139 ARG C CD    
3052 N  NE    . ARG C 139 ? 1.25183 1.33661 1.06405 0.12701  0.18128  -0.18342 139 ARG C NE    
3053 C  CZ    . ARG C 139 ? 1.24429 1.33239 1.08060 0.15753  0.17140  -0.18101 139 ARG C CZ    
3054 N  NH1   . ARG C 139 ? 1.31054 1.33531 1.11062 0.17232  0.16608  -0.18223 139 ARG C NH1   
3055 N  NH2   . ARG C 139 ? 1.13578 1.28890 1.02955 0.17206  0.16663  -0.17718 139 ARG C NH2   
3056 N  N     . GLY C 140 ? 1.54829 1.57853 1.20373 0.08915  0.29652  -0.23978 140 GLY C N     
3057 C  CA    . GLY C 140 ? 1.43646 1.50085 1.09514 0.05983  0.31530  -0.23888 140 GLY C CA    
3058 C  C     . GLY C 140 ? 1.45320 1.55739 1.15869 0.04259  0.29364  -0.22175 140 GLY C C     
3059 O  O     . GLY C 140 ? 1.33273 1.40698 1.03302 0.03735  0.25985  -0.20493 140 GLY C O     
3060 N  N     . GLU C 141 ? 1.47444 1.64726 1.22621 0.03229  0.31512  -0.22720 141 GLU C N     
3061 C  CA    . GLU C 141 ? 1.32958 1.53923 1.12253 0.01299  0.30009  -0.21471 141 GLU C CA    
3062 C  C     . GLU C 141 ? 1.13661 1.42369 1.00901 0.03652  0.29300  -0.21939 141 GLU C C     
3063 O  O     . GLU C 141 ? 1.22667 1.52416 1.12653 0.03492  0.26655  -0.20717 141 GLU C O     
3064 C  CB    . GLU C 141 ? 1.23618 1.46233 1.01902 -0.02308 0.32753  -0.21700 141 GLU C CB    
3065 O  OP3   . DU  D .   ? 1.41149 1.14973 1.18692 0.19291  0.05945  0.14639  201 DU  A OP3   
3066 P  P     . DU  D .   ? 1.53261 1.19931 1.26252 0.20620  0.06491  0.16180  201 DU  A P     
3067 O  OP1   . DU  D .   ? 1.40746 1.04076 1.15543 0.17576  0.07996  0.16569  201 DU  A OP1   
3068 O  OP2   . DU  D .   ? 1.45454 1.09629 1.13202 0.22549  0.06879  0.17680  201 DU  A OP2   
3069 O  "O5'" . DU  D .   ? 1.56641 1.23709 1.29342 0.23268  0.04660  0.15231  201 DU  A "O5'" 
3070 C  "C5'" . DU  D .   ? 1.37932 1.04971 1.13572 0.21957  0.04377  0.14014  201 DU  A "C5'" 
3071 C  "C4'" . DU  D .   ? 1.44339 1.08672 1.17538 0.25016  0.03542  0.13747  201 DU  A "C4'" 
3072 O  "O4'" . DU  D .   ? 1.40031 1.09802 1.13700 0.28033  0.01934  0.13045  201 DU  A "O4'" 
3073 C  "C3'" . DU  D .   ? 1.38534 1.02172 1.13809 0.23761  0.03363  0.12288  201 DU  A "C3'" 
3074 O  "O3'" . DU  D .   ? 1.39802 0.96245 1.12834 0.21908  0.04662  0.12962  201 DU  A "O3'" 
3075 C  "C2'" . DU  D .   ? 1.30518 0.95012 1.04550 0.27689  0.02328  0.11588  201 DU  A "C2'" 
3076 C  "C1'" . DU  D .   ? 1.37238 1.07409 1.11565 0.29966  0.01215  0.11895  201 DU  A "C1'" 
3077 N  N1    . DU  D .   ? 1.23775 1.01922 1.02370 0.29656  0.00077  0.10098  201 DU  A N1    
3078 C  C2    . DU  D .   ? 1.22448 1.04229 1.01500 0.32944  -0.01025 0.09325  201 DU  A C2    
3079 O  O2    . DU  D .   ? 1.30023 1.08754 1.06191 0.36461  -0.01183 0.10160  201 DU  A O2    
3080 N  N3    . DU  D .   ? 0.99354 0.88486 0.82430 0.32033  -0.01787 0.07595  201 DU  A N3    
3081 C  C4    . DU  D .   ? 1.07725 0.99996 0.93757 0.28468  -0.01543 0.06707  201 DU  A C4    
3082 O  O4    . DU  D .   ? 0.89868 0.88050 0.78856 0.27922  -0.02084 0.05207  201 DU  A O4    
3083 C  C5    . DU  D .   ? 1.14141 1.02301 0.99516 0.25732  -0.00492 0.07721  201 DU  A C5    
3084 C  C6    . DU  D .   ? 1.10929 0.92726 0.92967 0.26279  0.00269  0.09287  201 DU  A C6    
3085 MG MG    . MG  E .   ? 0.94855 1.44672 1.05254 0.08055  0.18784  -0.19253 202 MG  A MG    
3086 O  OP3   . DU  F .   ? 1.03214 1.40092 1.10195 0.18533  0.11594  -0.15244 201 DU  B OP3   
3087 P  P     . DU  F .   ? 1.14790 1.49300 1.19103 0.18597  0.14085  -0.16560 201 DU  B P     
3088 O  OP1   . DU  F .   ? 0.92618 1.35015 1.01119 0.20273  0.16051  -0.18126 201 DU  B OP1   
3089 O  OP2   . DU  F .   ? 1.19891 1.46417 1.19773 0.20316  0.13591  -0.16054 201 DU  B OP2   
3090 O  "O5'" . DU  F .   ? 1.01614 1.33849 1.03356 0.14071  0.14780  -0.16500 201 DU  B "O5'" 
3091 C  "C5'" . DU  F .   ? 1.03144 1.29862 1.02077 0.11896  0.12943  -0.14916 201 DU  B "C5'" 
3092 C  "C4'" . DU  F .   ? 0.91670 1.15186 0.86982 0.08655  0.14045  -0.14932 201 DU  B "C4'" 
3093 O  "O4'" . DU  F .   ? 0.92187 1.17421 0.88758 0.05890  0.13776  -0.14250 201 DU  B "O4'" 
3094 C  "C3'" . DU  F .   ? 0.95494 1.11304 0.85731 0.07990  0.12786  -0.13908 201 DU  B "C3'" 
3095 O  "O3'" . DU  F .   ? 1.22146 1.35195 1.08211 0.07015  0.14525  -0.14839 201 DU  B "O3'" 
3096 C  "C2'" . DU  F .   ? 0.97858 1.12102 0.87857 0.05598  0.11257  -0.12227 201 DU  B "C2'" 
3097 C  "C1'" . DU  F .   ? 1.02261 1.21638 0.95112 0.03987  0.12684  -0.12757 201 DU  B "C1'" 
3098 N  N1    . DU  F .   ? 0.86232 1.06281 0.81091 0.03017  0.11349  -0.11553 201 DU  B N1    
3099 C  C2    . DU  F .   ? 0.77985 0.97462 0.71916 0.00264  0.12201  -0.11122 201 DU  B C2    
3100 O  O2    . DU  F .   ? 0.99202 1.17664 0.90654 -0.01452 0.13940  -0.11570 201 DU  B O2    
3101 N  N3    . DU  F .   ? 0.75469 0.95012 0.70983 -0.00367 0.11178  -0.10131 201 DU  B N3    
3102 C  C4    . DU  F .   ? 0.72992 0.93362 0.70806 0.01317  0.09441  -0.09528 201 DU  B C4    
3103 O  O4    . DU  F .   ? 0.81837 1.01886 0.80482 0.00464  0.08970  -0.08761 201 DU  B O4    
3104 C  C5    . DU  F .   ? 0.78784 0.99733 0.77323 0.04026  0.08581  -0.09870 201 DU  B C5    
3105 C  C6    . DU  F .   ? 0.81200 1.01830 0.78291 0.04822  0.09552  -0.10858 201 DU  B C6    
3106 O  OP3   . DU  G .   ? 1.17692 1.14078 1.26584 0.09020  0.05666  0.14684  201 DU  C OP3   
3107 P  P     . DU  G .   ? 1.43778 1.38445 1.54276 0.11253  0.07524  0.16556  201 DU  C P     
3108 O  OP1   . DU  G .   ? 1.25118 1.15354 1.32201 0.10805  0.10433  0.15245  201 DU  C OP1   
3109 O  OP2   . DU  G .   ? 1.11199 1.06446 1.22625 0.12768  0.05927  0.19053  201 DU  C OP2   
3110 O  "O5'" . DU  G .   ? 1.14479 1.12321 1.29512 0.12041  0.07821  0.16865  201 DU  C "O5'" 
3111 C  "C5'" . DU  G .   ? 1.07228 1.07340 1.26644 0.14166  0.07711  0.19210  201 DU  C "C5'" 
3112 C  "C4'" . DU  G .   ? 1.04285 1.08349 1.27906 0.13896  0.07361  0.19197  201 DU  C "C4'" 
3113 O  "O4'" . DU  G .   ? 0.93865 0.96114 1.15998 0.13279  0.09599  0.17468  201 DU  C "O4'" 
3114 C  "C3'" . DU  G .   ? 0.87858 0.94947 1.12179 0.11986  0.04499  0.18610  201 DU  C "C3'" 
3115 O  "O3'" . DU  G .   ? 0.90239 1.00938 1.17838 0.12417  0.02098  0.20502  201 DU  C "O3'" 
3116 C  "C2'" . DU  G .   ? 0.87417 0.95816 1.13639 0.11368  0.05506  0.17834  201 DU  C "C2'" 
3117 C  "C1'" . DU  G .   ? 0.83397 0.88683 1.07957 0.12332  0.08745  0.17160  201 DU  C "C1'" 
3118 N  N1    . DU  G .   ? 0.85253 0.88635 1.06350 0.10989  0.09453  0.14976  201 DU  C N1    
3119 C  C2    . DU  G .   ? 0.72788 0.75866 0.94302 0.11204  0.11369  0.14615  201 DU  C C2    
3120 O  O2    . DU  G .   ? 0.90263 0.94489 1.14979 0.12357  0.12796  0.15917  201 DU  C O2    
3121 N  N3    . DU  G .   ? 0.57101 0.58730 0.75131 0.10119  0.11585  0.12731  201 DU  C N3    
3122 C  C4    . DU  G .   ? 0.81929 0.82986 0.96884 0.08977  0.10217  0.11178  201 DU  C C4    
3123 O  O4    . DU  G .   ? 0.65934 0.66457 0.78419 0.08366  0.10428  0.09695  201 DU  C O4    
3124 C  C5    . DU  G .   ? 0.83269 0.84650 0.98198 0.08724  0.08650  0.11552  201 DU  C C5    
3125 C  C6    . DU  G .   ? 0.82925 0.85162 1.00503 0.09669  0.08264  0.13415  201 DU  C C6    
3126 MG MG    . MG  H .   ? 1.60405 1.32822 1.22579 0.32049  0.01015  0.17144  202 MG  C MG    
3127 O  O     . HOH I .   ? 0.70944 0.87299 0.71568 0.13012  0.03215  -0.07009 301 HOH A O     
3128 O  O     . HOH I .   ? 1.51975 1.14166 1.13786 0.30229  0.03600  0.18207  302 HOH A O     
3129 O  O     . HOH I .   ? 0.93377 0.98920 1.22716 0.21344  0.06814  0.26557  303 HOH A O     
3130 O  O     . HOH I .   ? 1.51665 0.95586 1.22009 0.12596  0.10350  0.17203  304 HOH A O     
3131 O  O     . HOH J .   ? 0.99189 1.78865 1.13697 -0.20258 0.01904  -0.26439 301 HOH B O     
3132 O  O     . HOH J .   ? 1.16492 0.72531 0.85608 -0.01022 0.20944  0.13174  302 HOH B O     
3133 O  O     . HOH J .   ? 1.04133 1.00073 1.03184 0.07820  -0.03897 0.19260  303 HOH B O     
3134 O  O     . HOH J .   ? 2.04115 0.94795 1.30216 0.61891  0.14081  0.16359  304 HOH B O     
3135 O  O     . HOH K .   ? 0.67519 0.66977 0.74788 0.07793  0.11539  0.07132  301 HOH C O     
# 
