data_5J0G
# 
_entry.id   5J0G 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5J0G         
WWPDB D_1000219766 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5J0G 
_pdbx_database_status.recvd_initial_deposition_date   2016-03-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Wang, H.'       1 
'Lang, L.'       2 
'Logan, D.'      3 
'Danielsson, J.' 4 
'Oliveberg, M.'  5 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'J. Am. Chem. Soc.' 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            138 
_citation.language                  ? 
_citation.page_first                15571 
_citation.page_last                 15579 
_citation.title                     'Tricking a Protein To Swap Strands.' 
_citation.year                      2016 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.6b05151 
_citation.pdbx_database_id_PubMed   27783493 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Wang, H.'       1 
primary 'Lang, L.'       2 
primary 'Logan, D.T.'    3 
primary 'Danielsson, J.' 4 
primary 'Oliveberg, M.'  5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5J0G 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.140 
_cell.length_a_esd                 ? 
_cell.length_b                     74.140 
_cell.length_b_esd                 ? 
_cell.length_c                     59.420 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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             ? 
# 
_symmetry.entry_id                         5J0G 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'OXIDOREDUCTASE,Superoxide dismutase [Cu-Zn]' 11189.499 2  1.15.1.1 ? ? ? 
2 water   nat water                                         18.015    24 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
_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       
;AGSRLASGVIGIAQAGAGATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHGAGGDLGNVTADKD
GVADVSIEDSVISLSGDHSIIGRTLVVHEKAGA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AGSRLASGVIGIAQAGAGATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHGAGGDLGNVTADKD
GVADVSIEDSVISLSGDHSIIGRTLVVHEKAGA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   GLY n 
1 3   SER n 
1 4   ARG n 
1 5   LEU n 
1 6   ALA n 
1 7   SER n 
1 8   GLY n 
1 9   VAL n 
1 10  ILE n 
1 11  GLY n 
1 12  ILE n 
1 13  ALA n 
1 14  GLN n 
1 15  ALA n 
1 16  GLY n 
1 17  ALA n 
1 18  GLY n 
1 19  ALA n 
1 20  THR n 
1 21  LYS n 
1 22  ALA n 
1 23  VAL n 
1 24  ALA n 
1 25  VAL n 
1 26  LEU n 
1 27  LYS n 
1 28  GLY n 
1 29  ASP n 
1 30  GLY n 
1 31  PRO n 
1 32  VAL n 
1 33  GLN n 
1 34  GLY n 
1 35  ILE n 
1 36  ILE n 
1 37  ASN n 
1 38  PHE n 
1 39  GLU n 
1 40  GLN n 
1 41  LYS n 
1 42  GLU n 
1 43  SER n 
1 44  ASN n 
1 45  GLY n 
1 46  PRO n 
1 47  VAL n 
1 48  LYS n 
1 49  VAL n 
1 50  TRP n 
1 51  GLY n 
1 52  SER n 
1 53  ILE n 
1 54  LYS n 
1 55  GLY n 
1 56  LEU n 
1 57  THR n 
1 58  GLU n 
1 59  GLY n 
1 60  LEU n 
1 61  HIS n 
1 62  GLY n 
1 63  PHE n 
1 64  HIS n 
1 65  VAL n 
1 66  HIS n 
1 67  GLY n 
1 68  ALA n 
1 69  GLY n 
1 70  GLY n 
1 71  ASP n 
1 72  LEU n 
1 73  GLY n 
1 74  ASN n 
1 75  VAL n 
1 76  THR n 
1 77  ALA n 
1 78  ASP n 
1 79  LYS n 
1 80  ASP n 
1 81  GLY n 
1 82  VAL n 
1 83  ALA n 
1 84  ASP n 
1 85  VAL n 
1 86  SER n 
1 87  ILE n 
1 88  GLU n 
1 89  ASP n 
1 90  SER n 
1 91  VAL n 
1 92  ILE n 
1 93  SER n 
1 94  LEU n 
1 95  SER n 
1 96  GLY n 
1 97  ASP n 
1 98  HIS n 
1 99  SER n 
1 100 ILE n 
1 101 ILE n 
1 102 GLY n 
1 103 ARG n 
1 104 THR n 
1 105 LEU n 
1 106 VAL n 
1 107 VAL n 
1 108 HIS n 
1 109 GLU n 
1 110 LYS n 
1 111 ALA n 
1 112 GLY n 
1 113 ALA n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1  14  HUMAN ? ?    ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli K-12' 83333 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 19 113 Human ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli K-12' 83333 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 5J0G       5J0G   ? 1 ? 1 
2 UNP SODC_HUMAN P00441 ? 1 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKA
;
2 
# 
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 5J0G A 1  ? 14  ? 5J0G   1 ? 14  ? 1  14  
2 2 5J0G A 19 ? 111 ? P00441 2 ? 124 ? 19 111 
3 1 5J0G B 1  ? 14  ? 5J0G   1 ? 14  ? 1  14  
4 2 5J0G B 19 ? 111 ? P00441 2 ? 124 ? 19 111 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 5J0G ALA A 15  ? PDB ?      ?   ?   linker           15  1  
1 5J0G GLY A 16  ? PDB ?      ?   ?   linker           16  2  
1 5J0G ALA A 17  ? PDB ?      ?   ?   linker           17  3  
1 5J0G GLY A 18  ? PDB ?      ?   ?   linker           18  4  
2 5J0G ALA A 24  ? UNP P00441 CYS 7   conflict         24  5  
2 5J0G GLY A 67  ? UNP P00441 GLU 50  conflict         67  6  
2 5J0G ALA A 68  ? UNP P00441 PHE 51  conflict         68  7  
2 5J0G ?   A ?   ? UNP P00441 ASP 53  deletion         ?   8  
2 5J0G ?   A ?   ? UNP P00441 ASN 54  deletion         ?   9  
2 5J0G ?   A ?   ? UNP P00441 THR 55  deletion         ?   10 
2 5J0G ?   A ?   ? UNP P00441 ALA 56  deletion         ?   11 
2 5J0G ?   A ?   ? UNP P00441 GLY 57  deletion         ?   12 
2 5J0G ?   A ?   ? UNP P00441 CYS 58  deletion         ?   13 
2 5J0G ?   A ?   ? UNP P00441 THR 59  deletion         ?   14 
2 5J0G ?   A ?   ? UNP P00441 SER 60  deletion         ?   15 
2 5J0G ?   A ?   ? UNP P00441 ALA 61  deletion         ?   16 
2 5J0G ?   A ?   ? UNP P00441 GLY 62  deletion         ?   17 
2 5J0G ?   A ?   ? UNP P00441 PRO 63  deletion         ?   18 
2 5J0G ?   A ?   ? UNP P00441 HIS 64  deletion         ?   19 
2 5J0G ?   A ?   ? UNP P00441 PHE 65  deletion         ?   20 
2 5J0G ?   A ?   ? UNP P00441 ASN 66  deletion         ?   21 
2 5J0G ?   A ?   ? UNP P00441 PRO 67  deletion         ?   22 
2 5J0G ?   A ?   ? UNP P00441 LEU 68  deletion         ?   23 
2 5J0G ?   A ?   ? UNP P00441 SER 69  deletion         ?   24 
2 5J0G ?   A ?   ? UNP P00441 ARG 70  deletion         ?   25 
2 5J0G ?   A ?   ? UNP P00441 LYS 71  deletion         ?   26 
2 5J0G ?   A ?   ? UNP P00441 HIS 72  deletion         ?   27 
2 5J0G ?   A ?   ? UNP P00441 GLY 73  deletion         ?   28 
2 5J0G ?   A ?   ? UNP P00441 GLY 74  deletion         ?   29 
2 5J0G ?   A ?   ? UNP P00441 PRO 75  deletion         ?   30 
2 5J0G ?   A ?   ? UNP P00441 LYS 76  deletion         ?   31 
2 5J0G ?   A ?   ? UNP P00441 ASP 77  deletion         ?   32 
2 5J0G ?   A ?   ? UNP P00441 GLU 78  deletion         ?   33 
2 5J0G ?   A ?   ? UNP P00441 GLU 79  deletion         ?   34 
2 5J0G ?   A ?   ? UNP P00441 ARG 80  deletion         ?   35 
2 5J0G ?   A ?   ? UNP P00441 HIS 81  deletion         ?   36 
2 5J0G ?   A ?   ? UNP P00441 VAL 82  deletion         ?   37 
2 5J0G SER A 99  ? UNP P00441 CYS 112 conflict         99  38 
2 5J0G GLY A 112 ? UNP P00441 ?   ?   'expression tag' 112 39 
2 5J0G ALA A 113 ? UNP P00441 ?   ?   'expression tag' 113 40 
3 5J0G ALA B 15  ? PDB ?      ?   ?   linker           15  41 
3 5J0G GLY B 16  ? PDB ?      ?   ?   linker           16  42 
3 5J0G ALA B 17  ? PDB ?      ?   ?   linker           17  43 
3 5J0G GLY B 18  ? PDB ?      ?   ?   linker           18  44 
4 5J0G ALA B 24  ? UNP P00441 CYS 7   conflict         24  45 
4 5J0G GLY B 67  ? UNP P00441 GLU 50  conflict         67  46 
4 5J0G ALA B 68  ? UNP P00441 PHE 51  conflict         68  47 
4 5J0G ?   B ?   ? UNP P00441 ASP 53  deletion         ?   48 
4 5J0G ?   B ?   ? UNP P00441 ASN 54  deletion         ?   49 
4 5J0G ?   B ?   ? UNP P00441 THR 55  deletion         ?   50 
4 5J0G ?   B ?   ? UNP P00441 ALA 56  deletion         ?   51 
4 5J0G ?   B ?   ? UNP P00441 GLY 57  deletion         ?   52 
4 5J0G ?   B ?   ? UNP P00441 CYS 58  deletion         ?   53 
4 5J0G ?   B ?   ? UNP P00441 THR 59  deletion         ?   54 
4 5J0G ?   B ?   ? UNP P00441 SER 60  deletion         ?   55 
4 5J0G ?   B ?   ? UNP P00441 ALA 61  deletion         ?   56 
4 5J0G ?   B ?   ? UNP P00441 GLY 62  deletion         ?   57 
4 5J0G ?   B ?   ? UNP P00441 PRO 63  deletion         ?   58 
4 5J0G ?   B ?   ? UNP P00441 HIS 64  deletion         ?   59 
4 5J0G ?   B ?   ? UNP P00441 PHE 65  deletion         ?   60 
4 5J0G ?   B ?   ? UNP P00441 ASN 66  deletion         ?   61 
4 5J0G ?   B ?   ? UNP P00441 PRO 67  deletion         ?   62 
4 5J0G ?   B ?   ? UNP P00441 LEU 68  deletion         ?   63 
4 5J0G ?   B ?   ? UNP P00441 SER 69  deletion         ?   64 
4 5J0G ?   B ?   ? UNP P00441 ARG 70  deletion         ?   65 
4 5J0G ?   B ?   ? UNP P00441 LYS 71  deletion         ?   66 
4 5J0G ?   B ?   ? UNP P00441 HIS 72  deletion         ?   67 
4 5J0G ?   B ?   ? UNP P00441 GLY 73  deletion         ?   68 
4 5J0G ?   B ?   ? UNP P00441 GLY 74  deletion         ?   69 
4 5J0G ?   B ?   ? UNP P00441 PRO 75  deletion         ?   70 
4 5J0G ?   B ?   ? UNP P00441 LYS 76  deletion         ?   71 
4 5J0G ?   B ?   ? UNP P00441 ASP 77  deletion         ?   72 
4 5J0G ?   B ?   ? UNP P00441 GLU 78  deletion         ?   73 
4 5J0G ?   B ?   ? UNP P00441 GLU 79  deletion         ?   74 
4 5J0G ?   B ?   ? UNP P00441 ARG 80  deletion         ?   75 
4 5J0G ?   B ?   ? UNP P00441 HIS 81  deletion         ?   76 
4 5J0G ?   B ?   ? UNP P00441 VAL 82  deletion         ?   77 
4 5J0G SER B 99  ? UNP P00441 CYS 112 conflict         99  78 
4 5J0G GLY B 112 ? UNP P00441 ?   ?   'expression tag' 112 79 
4 5J0G ALA B 113 ? UNP P00441 ?   ?   'expression tag' 113 80 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
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 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_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                   5J0G 
_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            2.11 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         41.61 
_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_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              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 M di-ammonium hydrogen citrate,
20 % w/v PEG 3350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_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_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         MARRESEARCH 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-09-11 
# 
_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 
_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                        'MAX II BEAMLINE I911-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I911-3 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5J0G 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.50 
_reflns.d_resolution_low                 37.1 
_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                       6519 
_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             100 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  7.5 
_reflns.pdbx_Rmerge_I_obs                0.097 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            14.1 
_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                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.50 
_reflns_shell.d_res_low                   2.61 
_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           ? 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.661 
_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             ? 
_reflns_shell.pdbx_Rsym_value             ? 
_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                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            -0.6700 
_refine.aniso_B[1][2]                            -0.6700 
_refine.aniso_B[1][3]                            -0.0000 
_refine.aniso_B[2][2]                            -0.6700 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            2.1900 
_refine.B_iso_max                                122.190 
_refine.B_iso_mean                               48.9590 
_refine.B_iso_min                                16.820 
_refine.correlation_coeff_Fo_to_Fc               0.9520 
_refine.correlation_coeff_Fo_to_Fc_free          0.9360 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      : WITH TLS ADDED' 
_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                                 5J0G 
_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                            2.5000 
_refine.ls_d_res_low                             37.1000 
_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                     6195 
_refine.ls_number_reflns_R_free                  304 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9500 
_refine.ls_percent_reflns_R_free                 4.7000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1843 
_refine.ls_R_factor_R_free                       0.2354 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1818 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.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                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4bcz 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.3040 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             25.3820 
_refine.overall_SU_ML                            0.2440 
_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.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       2.5000 
_refine_hist.d_res_low                        37.1000 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             24 
_refine_hist.number_atoms_total               1600 
_refine_hist.pdbx_number_residues_total       226 
_refine_hist.pdbx_B_iso_mean_solvent          35.26 
_refine_hist.pdbx_number_atoms_protein        1576 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
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' ? 0.004  0.019  1596 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1564 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 0.881  1.945  2156 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 0.598  3.000  3598 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 5.026  5.000  224  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.035 25.714 56   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.184 15.000 252  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 4.581  15.000 4    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.057  0.200  250  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  1876 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  332  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 2.899  3.791  902  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.897  3.785  901  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 3.800  5.656  1124 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 1.271  3.000  3160 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 28.881 5.000  16   ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 19.775 5.000  3148 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.5010 
_refine_ls_shell.d_res_low                        2.5660 
_refine_ls_shell.number_reflns_all                477 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             28 
_refine_ls_shell.number_reflns_R_work             449 
_refine_ls_shell.percent_reflns_obs               100.0000 
_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                  0.4610 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2790 
_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_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5J0G 
_struct.title                        
'Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P7/8' 
_struct.pdbx_descriptor              'OXIDOREDUCTASE,Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5J0G 
_struct_keywords.text            'SOD1, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
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 GLY 112 A . ? GLY 112 A ALA 113 A ? ALA 113 A 1 -0.02 
2 GLY 45  B . ? GLY 45  B PRO 46  B ? PRO 46  B 1 0.70  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 71  ? ALA A 77  ? ASP A 71  ALA A 77  
AA1 2 GLY A 59  ? VAL A 65  ? GLY A 59  VAL A 65  
AA1 3 THR A 104 ? HIS A 108 ? THR A 104 HIS A 108 
AA1 4 LEU A 5   ? ALA A 15  ? LEU A 5   ALA A 15  
AA1 5 THR A 20  ? LYS A 27  ? THR A 20  LYS A 27  
AA1 6 GLN A 33  ? GLN A 40  ? GLN A 33  GLN A 40  
AA1 7 VAL A 47  ? LYS A 54  ? VAL A 47  LYS A 54  
AA1 8 ALA A 83  ? ASP A 89  ? ALA A 83  ASP A 89  
AA2 1 ASP B 71  ? ALA B 77  ? ASP B 71  ALA B 77  
AA2 2 GLY B 59  ? VAL B 65  ? GLY B 59  VAL B 65  
AA2 3 THR B 104 ? HIS B 108 ? THR B 104 HIS B 108 
AA2 4 LEU B 5   ? GLN B 14  ? LEU B 5   GLN B 14  
AA2 5 THR B 20  ? LYS B 27  ? THR B 20  LYS B 27  
AA2 6 GLN B 33  ? GLN B 40  ? GLN B 33  GLN B 40  
AA2 7 VAL B 47  ? LYS B 54  ? VAL B 47  LYS B 54  
AA2 8 ALA B 83  ? ASP B 89  ? ALA B 83  ASP B 89  
# 
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 ALA A 77  ? O ALA A 77  N GLY A 59  ? N GLY A 59  
AA1 2 3 N GLY A 62  ? N GLY A 62  O HIS A 108 ? O HIS A 108 
AA1 3 4 O LEU A 105 ? O LEU A 105 N GLY A 8   ? N GLY A 8   
AA1 4 5 N GLY A 11  ? N GLY A 11  O VAL A 23  ? O VAL A 23  
AA1 5 6 N THR A 20  ? N THR A 20  O GLN A 40  ? O GLN A 40  
AA1 6 7 N ASN A 37  ? N ASN A 37  O TRP A 50  ? O TRP A 50  
AA1 7 8 N VAL A 49  ? N VAL A 49  O ILE A 87  ? O ILE A 87  
AA2 1 2 O ALA B 77  ? O ALA B 77  N GLY B 59  ? N GLY B 59  
AA2 2 3 N HIS B 64  ? N HIS B 64  O VAL B 106 ? O VAL B 106 
AA2 3 4 O LEU B 105 ? O LEU B 105 N GLY B 8   ? N GLY B 8   
AA2 4 5 N ALA B 13  ? N ALA B 13  O LYS B 21  ? O LYS B 21  
AA2 5 6 N ALA B 22  ? N ALA B 22  O PHE B 38  ? O PHE B 38  
AA2 6 7 N GLU B 39  ? N GLU B 39  O LYS B 48  ? O LYS B 48  
AA2 7 8 N VAL B 49  ? N VAL B 49  O ILE B 87  ? O ILE B 87  
# 
_atom_sites.entry_id                    5J0G 
_atom_sites.fract_transf_matrix[1][1]   0.013488 
_atom_sites.fract_transf_matrix[1][2]   0.007787 
_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]   0.015575 
_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]   0.016829 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
# 
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   . ALA A 1 1   ? -6.648  9.142  -17.852 1.00 70.64  ? 1   ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? -6.013  9.651  -16.601 1.00 69.09  ? 1   ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? -6.539  11.039 -16.226 1.00 61.66  ? 1   ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? -6.053  12.054 -16.727 1.00 64.40  ? 1   ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? -4.494  9.677  -16.749 1.00 68.43  ? 1   ALA A CB  1 
ATOM   6    N N   . GLY A 1 2   ? -7.546  11.074 -15.355 1.00 56.51  ? 2   GLY A N   1 
ATOM   7    C CA  . GLY A 1 2   ? -8.027  12.328 -14.778 1.00 53.51  ? 2   GLY A CA  1 
ATOM   8    C C   . GLY A 1 2   ? -7.067  12.819 -13.710 1.00 51.06  ? 2   GLY A C   1 
ATOM   9    O O   . GLY A 1 2   ? -6.237  12.054 -13.215 1.00 50.55  ? 2   GLY A O   1 
ATOM   10   N N   . SER A 1 3   ? -7.179  14.091 -13.342 1.00 48.49  ? 3   SER A N   1 
ATOM   11   C CA  . SER A 1 3   ? -6.199  14.710 -12.448 1.00 49.09  ? 3   SER A CA  1 
ATOM   12   C C   . SER A 1 3   ? -6.387  14.271 -10.995 1.00 47.92  ? 3   SER A C   1 
ATOM   13   O O   . SER A 1 3   ? -7.508  14.266 -10.482 1.00 47.57  ? 3   SER A O   1 
ATOM   14   C CB  . SER A 1 3   ? -6.265  16.236 -12.554 1.00 52.01  ? 3   SER A CB  1 
ATOM   15   O OG  . SER A 1 3   ? -7.534  16.721 -12.160 1.00 57.76  ? 3   SER A OG  1 
ATOM   16   N N   . ARG A 1 4   ? -5.283  13.894 -10.349 1.00 45.77  ? 4   ARG A N   1 
ATOM   17   C CA  . ARG A 1 4   ? -5.292  13.513 -8.937  1.00 44.94  ? 4   ARG A CA  1 
ATOM   18   C C   . ARG A 1 4   ? -5.133  14.766 -8.078  1.00 41.45  ? 4   ARG A C   1 
ATOM   19   O O   . ARG A 1 4   ? -4.245  15.583 -8.323  1.00 40.38  ? 4   ARG A O   1 
ATOM   20   C CB  . ARG A 1 4   ? -4.164  12.524 -8.620  1.00 50.04  ? 4   ARG A CB  1 
ATOM   21   C CG  . ARG A 1 4   ? -4.101  11.308 -9.535  1.00 53.73  ? 4   ARG A CG  1 
ATOM   22   C CD  . ARG A 1 4   ? -3.143  10.250 -8.998  1.00 58.18  ? 4   ARG A CD  1 
ATOM   23   N NE  . ARG A 1 4   ? -3.834  9.167  -8.290  1.00 60.88  ? 4   ARG A NE  1 
ATOM   24   C CZ  . ARG A 1 4   ? -4.182  7.993  -8.824  1.00 62.81  ? 4   ARG A CZ  1 
ATOM   25   N NH1 . ARG A 1 4   ? -3.917  7.702  -10.097 1.00 65.35  ? 4   ARG A NH1 1 
ATOM   26   N NH2 . ARG A 1 4   ? -4.806  7.092  -8.073  1.00 64.54  ? 4   ARG A NH2 1 
ATOM   27   N N   . LEU A 1 5   ? -5.994  14.904 -7.073  1.00 39.22  ? 5   LEU A N   1 
ATOM   28   C CA  . LEU A 1 5   ? -5.994  16.065 -6.192  1.00 36.79  ? 5   LEU A CA  1 
ATOM   29   C C   . LEU A 1 5   ? -5.681  15.683 -4.756  1.00 35.25  ? 5   LEU A C   1 
ATOM   30   O O   . LEU A 1 5   ? -6.051  14.601 -4.292  1.00 36.06  ? 5   LEU A O   1 
ATOM   31   C CB  . LEU A 1 5   ? -7.366  16.735 -6.197  1.00 36.90  ? 5   LEU A CB  1 
ATOM   32   C CG  . LEU A 1 5   ? -7.938  17.220 -7.522  1.00 37.34  ? 5   LEU A CG  1 
ATOM   33   C CD1 . LEU A 1 5   ? -9.351  17.725 -7.277  1.00 38.74  ? 5   LEU A CD1 1 
ATOM   34   C CD2 . LEU A 1 5   ? -7.067  18.306 -8.131  1.00 37.80  ? 5   LEU A CD2 1 
ATOM   35   N N   . ALA A 1 6   ? -4.995  16.589 -4.065  1.00 33.52  ? 6   ALA A N   1 
ATOM   36   C CA  . ALA A 1 6   ? -4.955  16.602 -2.612  1.00 32.16  ? 6   ALA A CA  1 
ATOM   37   C C   . ALA A 1 6   ? -5.879  17.731 -2.189  1.00 30.71  ? 6   ALA A C   1 
ATOM   38   O O   . ALA A 1 6   ? -5.833  18.817 -2.775  1.00 31.09  ? 6   ALA A O   1 
ATOM   39   C CB  . ALA A 1 6   ? -3.546  16.859 -2.115  1.00 32.79  ? 6   ALA A CB  1 
ATOM   40   N N   . SER A 1 7   ? -6.722  17.478 -1.188  1.00 27.83  ? 7   SER A N   1 
ATOM   41   C CA  . SER A 1 7   ? -7.754  18.440 -0.800  1.00 24.50  ? 7   SER A CA  1 
ATOM   42   C C   . SER A 1 7   ? -8.113  18.388 0.678   1.00 22.69  ? 7   SER A C   1 
ATOM   43   O O   . SER A 1 7   ? -7.808  17.422 1.374   1.00 23.34  ? 7   SER A O   1 
ATOM   44   C CB  . SER A 1 7   ? -9.022  18.190 -1.613  1.00 24.34  ? 7   SER A CB  1 
ATOM   45   O OG  . SER A 1 7   ? -9.619  16.961 -1.232  1.00 27.18  ? 7   SER A OG  1 
ATOM   46   N N   . GLY A 1 8   ? -8.782  19.444 1.130   1.00 21.61  ? 8   GLY A N   1 
ATOM   47   C CA  . GLY A 1 8   ? -9.289  19.536 2.489   1.00 20.16  ? 8   GLY A CA  1 
ATOM   48   C C   . GLY A 1 8   ? -10.322 20.640 2.599   1.00 21.73  ? 8   GLY A C   1 
ATOM   49   O O   . GLY A 1 8   ? -10.247 21.644 1.887   1.00 23.83  ? 8   GLY A O   1 
ATOM   50   N N   . VAL A 1 9   ? -11.285 20.462 3.497   1.00 22.76  ? 9   VAL A N   1 
ATOM   51   C CA  . VAL A 1 9   ? -12.351 21.441 3.681   1.00 23.37  ? 9   VAL A CA  1 
ATOM   52   C C   . VAL A 1 9   ? -11.829 22.596 4.533   1.00 24.38  ? 9   VAL A C   1 
ATOM   53   O O   . VAL A 1 9   ? -11.068 22.388 5.477   1.00 27.16  ? 9   VAL A O   1 
ATOM   54   C CB  . VAL A 1 9   ? -13.590 20.810 4.352   1.00 23.48  ? 9   VAL A CB  1 
ATOM   55   C CG1 . VAL A 1 9   ? -14.734 21.811 4.432   1.00 24.17  ? 9   VAL A CG1 1 
ATOM   56   C CG2 . VAL A 1 9   ? -14.035 19.566 3.593   1.00 23.74  ? 9   VAL A CG2 1 
ATOM   57   N N   . ILE A 1 10  ? -12.239 23.812 4.195   1.00 25.39  ? 10  ILE A N   1 
ATOM   58   C CA  . ILE A 1 10  ? -11.795 25.004 4.914   1.00 25.79  ? 10  ILE A CA  1 
ATOM   59   C C   . ILE A 1 10  ? -12.684 25.231 6.137   1.00 26.87  ? 10  ILE A C   1 
ATOM   60   O O   . ILE A 1 10  ? -13.830 25.667 6.004   1.00 27.39  ? 10  ILE A O   1 
ATOM   61   C CB  . ILE A 1 10  ? -11.807 26.244 3.997   1.00 25.40  ? 10  ILE A CB  1 
ATOM   62   C CG1 . ILE A 1 10  ? -10.859 26.016 2.811   1.00 25.51  ? 10  ILE A CG1 1 
ATOM   63   C CG2 . ILE A 1 10  ? -11.407 27.492 4.780   1.00 24.97  ? 10  ILE A CG2 1 
ATOM   64   C CD1 . ILE A 1 10  ? -11.002 27.021 1.685   1.00 26.22  ? 10  ILE A CD1 1 
ATOM   65   N N   . GLY A 1 11  ? -12.144 24.933 7.319   1.00 27.98  ? 11  GLY A N   1 
ATOM   66   C CA  . GLY A 1 11  ? -12.896 25.014 8.570   1.00 30.29  ? 11  GLY A CA  1 
ATOM   67   C C   . GLY A 1 11  ? -12.572 26.235 9.416   1.00 32.61  ? 11  GLY A C   1 
ATOM   68   O O   . GLY A 1 11  ? -11.431 26.696 9.443   1.00 34.48  ? 11  GLY A O   1 
ATOM   69   N N   . ILE A 1 12  ? -13.588 26.748 10.111  1.00 35.93  ? 12  ILE A N   1 
ATOM   70   C CA  . ILE A 1 12  ? -13.451 27.904 11.005  1.00 40.08  ? 12  ILE A CA  1 
ATOM   71   C C   . ILE A 1 12  ? -12.534 27.570 12.171  1.00 39.62  ? 12  ILE A C   1 
ATOM   72   O O   . ILE A 1 12  ? -12.694 26.536 12.808  1.00 37.51  ? 12  ILE A O   1 
ATOM   73   C CB  . ILE A 1 12  ? -14.829 28.341 11.572  1.00 43.92  ? 12  ILE A CB  1 
ATOM   74   C CG1 . ILE A 1 12  ? -15.684 28.984 10.477  1.00 47.13  ? 12  ILE A CG1 1 
ATOM   75   C CG2 . ILE A 1 12  ? -14.679 29.309 12.745  1.00 44.69  ? 12  ILE A CG2 1 
ATOM   76   C CD1 . ILE A 1 12  ? -15.273 30.397 10.097  1.00 50.33  ? 12  ILE A CD1 1 
ATOM   77   N N   . ALA A 1 13  ? -11.584 28.457 12.451  1.00 46.33  ? 13  ALA A N   1 
ATOM   78   C CA  . ALA A 1 13  ? -10.702 28.312 13.610  1.00 49.78  ? 13  ALA A CA  1 
ATOM   79   C C   . ALA A 1 13  ? -11.141 29.261 14.717  1.00 53.73  ? 13  ALA A C   1 
ATOM   80   O O   . ALA A 1 13  ? -11.407 28.829 15.840  1.00 53.70  ? 13  ALA A O   1 
ATOM   81   C CB  . ALA A 1 13  ? -9.260  28.584 13.218  1.00 48.74  ? 13  ALA A CB  1 
ATOM   82   N N   . GLN A 1 14  ? -11.223 30.549 14.387  1.00 58.20  ? 14  GLN A N   1 
ATOM   83   C CA  . GLN A 1 14  ? -11.582 31.588 15.355  1.00 64.14  ? 14  GLN A CA  1 
ATOM   84   C C   . GLN A 1 14  ? -12.543 32.626 14.781  1.00 68.54  ? 14  GLN A C   1 
ATOM   85   O O   . GLN A 1 14  ? -12.678 32.774 13.564  1.00 63.10  ? 14  GLN A O   1 
ATOM   86   C CB  . GLN A 1 14  ? -10.323 32.301 15.875  1.00 68.74  ? 14  GLN A CB  1 
ATOM   87   C CG  . GLN A 1 14  ? -10.031 32.084 17.355  1.00 72.43  ? 14  GLN A CG  1 
ATOM   88   C CD  . GLN A 1 14  ? -9.527  30.686 17.679  1.00 74.58  ? 14  GLN A CD  1 
ATOM   89   O OE1 . GLN A 1 14  ? -8.866  30.043 16.863  1.00 75.29  ? 14  GLN A OE1 1 
ATOM   90   N NE2 . GLN A 1 14  ? -9.829  30.213 18.885  1.00 82.50  ? 14  GLN A NE2 1 
ATOM   91   N N   . ALA A 1 15  ? -13.209 33.331 15.692  1.00 75.26  ? 15  ALA A N   1 
ATOM   92   C CA  . ALA A 1 15  ? -14.015 34.503 15.370  1.00 77.38  ? 15  ALA A CA  1 
ATOM   93   C C   . ALA A 1 15  ? -13.648 35.616 16.347  1.00 85.05  ? 15  ALA A C   1 
ATOM   94   O O   . ALA A 1 15  ? -13.137 35.356 17.438  1.00 92.74  ? 15  ALA A O   1 
ATOM   95   C CB  . ALA A 1 15  ? -15.497 34.177 15.468  1.00 75.96  ? 15  ALA A CB  1 
ATOM   96   N N   . GLY A 1 16  ? -13.900 36.855 15.944  1.00 86.17  ? 16  GLY A N   1 
ATOM   97   C CA  . GLY A 1 16  ? -13.656 38.012 16.799  1.00 85.27  ? 16  GLY A CA  1 
ATOM   98   C C   . GLY A 1 16  ? -14.661 39.092 16.474  1.00 87.84  ? 16  GLY A C   1 
ATOM   99   O O   . GLY A 1 16  ? -15.681 38.825 15.831  1.00 91.29  ? 16  GLY A O   1 
ATOM   100  N N   . ALA A 1 17  ? -14.384 40.314 16.917  1.00 86.56  ? 17  ALA A N   1 
ATOM   101  C CA  . ALA A 1 17  ? -15.191 41.460 16.520  1.00 82.97  ? 17  ALA A CA  1 
ATOM   102  C C   . ALA A 1 17  ? -14.828 41.828 15.079  1.00 80.43  ? 17  ALA A C   1 
ATOM   103  O O   . ALA A 1 17  ? -14.140 42.821 14.834  1.00 71.31  ? 17  ALA A O   1 
ATOM   104  C CB  . ALA A 1 17  ? -14.956 42.632 17.463  1.00 78.86  ? 17  ALA A CB  1 
ATOM   105  N N   . GLY A 1 18  ? -15.287 41.005 14.134  1.00 82.97  ? 18  GLY A N   1 
ATOM   106  C CA  . GLY A 1 18  ? -14.958 41.167 12.716  1.00 82.32  ? 18  GLY A CA  1 
ATOM   107  C C   . GLY A 1 18  ? -13.881 40.214 12.219  1.00 79.99  ? 18  GLY A C   1 
ATOM   108  O O   . GLY A 1 18  ? -13.958 39.730 11.087  1.00 80.22  ? 18  GLY A O   1 
ATOM   109  N N   . ALA A 1 19  ? -12.880 39.947 13.061  1.00 75.25  ? 19  ALA A N   1 
ATOM   110  C CA  . ALA A 1 19  ? -11.733 39.112 12.684  1.00 72.34  ? 19  ALA A CA  1 
ATOM   111  C C   . ALA A 1 19  ? -12.103 37.630 12.567  1.00 72.05  ? 19  ALA A C   1 
ATOM   112  O O   . ALA A 1 19  ? -12.773 37.080 13.442  1.00 77.88  ? 19  ALA A O   1 
ATOM   113  C CB  . ALA A 1 19  ? -10.598 39.293 13.684  1.00 72.70  ? 19  ALA A CB  1 
ATOM   114  N N   . THR A 1 20  ? -11.655 36.997 11.482  1.00 64.82  ? 20  THR A N   1 
ATOM   115  C CA  . THR A 1 20  ? -11.931 35.583 11.215  1.00 56.48  ? 20  THR A CA  1 
ATOM   116  C C   . THR A 1 20  ? -10.636 34.834 10.907  1.00 51.14  ? 20  THR A C   1 
ATOM   117  O O   . THR A 1 20  ? -9.710  35.393 10.315  1.00 51.25  ? 20  THR A O   1 
ATOM   118  C CB  . THR A 1 20  ? -12.884 35.416 10.011  1.00 56.27  ? 20  THR A CB  1 
ATOM   119  O OG1 . THR A 1 20  ? -13.968 36.346 10.115  1.00 59.73  ? 20  THR A OG1 1 
ATOM   120  C CG2 . THR A 1 20  ? -13.442 34.001 9.945   1.00 55.36  ? 20  THR A CG2 1 
ATOM   121  N N   . LYS A 1 21  ? -10.581 33.568 11.315  1.00 45.26  ? 21  LYS A N   1 
ATOM   122  C CA  . LYS A 1 21  ? -9.480  32.674 10.955  1.00 42.51  ? 21  LYS A CA  1 
ATOM   123  C C   . LYS A 1 21  ? -10.039 31.323 10.511  1.00 40.03  ? 21  LYS A C   1 
ATOM   124  O O   . LYS A 1 21  ? -11.081 30.892 11.007  1.00 42.45  ? 21  LYS A O   1 
ATOM   125  C CB  . LYS A 1 21  ? -8.528  32.474 12.137  1.00 43.23  ? 21  LYS A CB  1 
ATOM   126  C CG  . LYS A 1 21  ? -8.075  33.758 12.812  1.00 44.97  ? 21  LYS A CG  1 
ATOM   127  C CD  . LYS A 1 21  ? -6.843  33.522 13.672  1.00 45.51  ? 21  LYS A CD  1 
ATOM   128  C CE  . LYS A 1 21  ? -6.531  34.707 14.573  1.00 46.79  ? 21  LYS A CE  1 
ATOM   129  N NZ  . LYS A 1 21  ? -5.986  35.865 13.816  1.00 48.55  ? 21  LYS A NZ  1 
ATOM   130  N N   . ALA A 1 22  ? -9.351  30.664 9.580   1.00 36.43  ? 22  ALA A N   1 
ATOM   131  C CA  . ALA A 1 22  ? -9.772  29.343 9.094   1.00 33.58  ? 22  ALA A CA  1 
ATOM   132  C C   . ALA A 1 22  ? -8.580  28.479 8.697   1.00 32.02  ? 22  ALA A C   1 
ATOM   133  O O   . ALA A 1 22  ? -7.510  28.997 8.387   1.00 34.26  ? 22  ALA A O   1 
ATOM   134  C CB  . ALA A 1 22  ? -10.725 29.488 7.921   1.00 33.74  ? 22  ALA A CB  1 
ATOM   135  N N   . VAL A 1 23  ? -8.783  27.162 8.707   1.00 30.12  ? 23  VAL A N   1 
ATOM   136  C CA  . VAL A 1 23  ? -7.721  26.198 8.415   1.00 29.03  ? 23  VAL A CA  1 
ATOM   137  C C   . VAL A 1 23  ? -8.207  25.136 7.436   1.00 27.35  ? 23  VAL A C   1 
ATOM   138  O O   . VAL A 1 23  ? -9.347  24.693 7.518   1.00 28.00  ? 23  VAL A O   1 
ATOM   139  C CB  . VAL A 1 23  ? -7.244  25.479 9.697   1.00 29.77  ? 23  VAL A CB  1 
ATOM   140  C CG1 . VAL A 1 23  ? -6.040  24.591 9.405   1.00 29.62  ? 23  VAL A CG1 1 
ATOM   141  C CG2 . VAL A 1 23  ? -6.895  26.486 10.778  1.00 31.22  ? 23  VAL A CG2 1 
ATOM   142  N N   . ALA A 1 24  ? -7.330  24.729 6.522   1.00 26.67  ? 24  ALA A N   1 
ATOM   143  C CA  . ALA A 1 24  ? -7.588  23.589 5.637   1.00 25.76  ? 24  ALA A CA  1 
ATOM   144  C C   . ALA A 1 24  ? -6.465  22.554 5.759   1.00 25.36  ? 24  ALA A C   1 
ATOM   145  O O   . ALA A 1 24  ? -5.319  22.825 5.393   1.00 27.17  ? 24  ALA A O   1 
ATOM   146  C CB  . ALA A 1 24  ? -7.727  24.049 4.193   1.00 24.79  ? 24  ALA A CB  1 
ATOM   147  N N   . VAL A 1 25  ? -6.798  21.379 6.290   1.00 24.60  ? 25  VAL A N   1 
ATOM   148  C CA  . VAL A 1 25  ? -5.858  20.265 6.349   1.00 23.65  ? 25  VAL A CA  1 
ATOM   149  C C   . VAL A 1 25  ? -5.945  19.519 5.019   1.00 24.89  ? 25  VAL A C   1 
ATOM   150  O O   . VAL A 1 25  ? -6.923  18.812 4.757   1.00 26.04  ? 25  VAL A O   1 
ATOM   151  C CB  . VAL A 1 25  ? -6.174  19.301 7.518   1.00 22.76  ? 25  VAL A CB  1 
ATOM   152  C CG1 . VAL A 1 25  ? -5.139  18.184 7.589   1.00 22.50  ? 25  VAL A CG1 1 
ATOM   153  C CG2 . VAL A 1 25  ? -6.231  20.059 8.838   1.00 22.74  ? 25  VAL A CG2 1 
ATOM   154  N N   . LEU A 1 26  ? -4.923  19.691 4.183   1.00 25.59  ? 26  LEU A N   1 
ATOM   155  C CA  . LEU A 1 26  ? -4.894  19.090 2.854   1.00 27.11  ? 26  LEU A CA  1 
ATOM   156  C C   . LEU A 1 26  ? -4.362  17.671 2.916   1.00 28.94  ? 26  LEU A C   1 
ATOM   157  O O   . LEU A 1 26  ? -3.308  17.423 3.492   1.00 32.63  ? 26  LEU A O   1 
ATOM   158  C CB  . LEU A 1 26  ? -4.014  19.909 1.912   1.00 28.12  ? 26  LEU A CB  1 
ATOM   159  C CG  . LEU A 1 26  ? -4.494  21.320 1.578   1.00 29.89  ? 26  LEU A CG  1 
ATOM   160  C CD1 . LEU A 1 26  ? -3.399  22.082 0.846   1.00 32.28  ? 26  LEU A CD1 1 
ATOM   161  C CD2 . LEU A 1 26  ? -5.765  21.273 0.745   1.00 30.44  ? 26  LEU A CD2 1 
ATOM   162  N N   . LYS A 1 27  ? -5.092  16.747 2.306   1.00 30.58  ? 27  LYS A N   1 
ATOM   163  C CA  . LYS A 1 27  ? -4.720  15.343 2.309   1.00 32.11  ? 27  LYS A CA  1 
ATOM   164  C C   . LYS A 1 27  ? -4.874  14.795 0.893   1.00 32.11  ? 27  LYS A C   1 
ATOM   165  O O   . LYS A 1 27  ? -5.896  15.022 0.243   1.00 31.23  ? 27  LYS A O   1 
ATOM   166  C CB  . LYS A 1 27  ? -5.608  14.568 3.288   1.00 35.16  ? 27  LYS A CB  1 
ATOM   167  C CG  . LYS A 1 27  ? -4.869  13.562 4.161   1.00 38.29  ? 27  LYS A CG  1 
ATOM   168  C CD  . LYS A 1 27  ? -4.096  12.555 3.326   1.00 40.21  ? 27  LYS A CD  1 
ATOM   169  C CE  . LYS A 1 27  ? -3.496  11.456 4.179   1.00 42.48  ? 27  LYS A CE  1 
ATOM   170  N NZ  . LYS A 1 27  ? -2.834  10.442 3.314   1.00 44.58  ? 27  LYS A NZ  1 
ATOM   171  N N   . GLY A 1 28  ? -3.850  14.093 0.417   1.00 32.92  ? 28  GLY A N   1 
ATOM   172  C CA  . GLY A 1 28  ? -3.879  13.493 -0.907  1.00 33.20  ? 28  GLY A CA  1 
ATOM   173  C C   . GLY A 1 28  ? -3.175  12.155 -0.960  1.00 34.13  ? 28  GLY A C   1 
ATOM   174  O O   . GLY A 1 28  ? -2.917  11.527 0.070   1.00 33.82  ? 28  GLY A O   1 
ATOM   175  N N   . ASP A 1 29  ? -2.857  11.732 -2.179  1.00 36.18  ? 29  ASP A N   1 
ATOM   176  C CA  . ASP A 1 29  ? -2.259  10.425 -2.425  1.00 38.06  ? 29  ASP A CA  1 
ATOM   177  C C   . ASP A 1 29  ? -0.806  10.419 -1.984  1.00 37.37  ? 29  ASP A C   1 
ATOM   178  O O   . ASP A 1 29  ? -0.129  11.450 -2.032  1.00 38.35  ? 29  ASP A O   1 
ATOM   179  C CB  . ASP A 1 29  ? -2.352  10.070 -3.911  1.00 40.73  ? 29  ASP A CB  1 
ATOM   180  C CG  . ASP A 1 29  ? -3.782  10.064 -4.416  1.00 44.42  ? 29  ASP A CG  1 
ATOM   181  O OD1 . ASP A 1 29  ? -4.609  9.327  -3.839  1.00 48.79  ? 29  ASP A OD1 1 
ATOM   182  O OD2 . ASP A 1 29  ? -4.081  10.800 -5.381  1.00 51.21  ? 29  ASP A OD2 1 
ATOM   183  N N   . GLY A 1 30  ? -0.335  9.255  -1.549  1.00 37.25  ? 30  GLY A N   1 
ATOM   184  C CA  . GLY A 1 30  ? 1.050   9.097  -1.131  1.00 37.29  ? 30  GLY A CA  1 
ATOM   185  C C   . GLY A 1 30  ? 1.419   10.055 -0.011  1.00 37.70  ? 30  GLY A C   1 
ATOM   186  O O   . GLY A 1 30  ? 0.670   10.189 0.958   1.00 43.07  ? 30  GLY A O   1 
ATOM   187  N N   . PRO A 1 31  ? 2.565   10.749 -0.144  1.00 36.06  ? 31  PRO A N   1 
ATOM   188  C CA  . PRO A 1 31  ? 3.058   11.605 0.935   1.00 34.64  ? 31  PRO A CA  1 
ATOM   189  C C   . PRO A 1 31  ? 2.504   13.034 0.924   1.00 32.95  ? 31  PRO A C   1 
ATOM   190  O O   . PRO A 1 31  ? 2.928   13.850 1.745   1.00 34.51  ? 31  PRO A O   1 
ATOM   191  C CB  . PRO A 1 31  ? 4.565   11.626 0.674   1.00 34.59  ? 31  PRO A CB  1 
ATOM   192  C CG  . PRO A 1 31  ? 4.670   11.547 -0.817  1.00 35.39  ? 31  PRO A CG  1 
ATOM   193  C CD  . PRO A 1 31  ? 3.482   10.758 -1.302  1.00 35.61  ? 31  PRO A CD  1 
ATOM   194  N N   . VAL A 1 32  ? 1.570   13.332 0.018   1.00 31.39  ? 32  VAL A N   1 
ATOM   195  C CA  . VAL A 1 32  ? 1.065   14.696 -0.144  1.00 29.84  ? 32  VAL A CA  1 
ATOM   196  C C   . VAL A 1 32  ? 0.209   15.098 1.057   1.00 32.70  ? 32  VAL A C   1 
ATOM   197  O O   . VAL A 1 32  ? -0.869  14.535 1.283   1.00 38.10  ? 32  VAL A O   1 
ATOM   198  C CB  . VAL A 1 32  ? 0.246   14.877 -1.442  1.00 28.74  ? 32  VAL A CB  1 
ATOM   199  C CG1 . VAL A 1 32  ? -0.269  16.309 -1.552  1.00 28.07  ? 32  VAL A CG1 1 
ATOM   200  C CG2 . VAL A 1 32  ? 1.086   14.535 -2.665  1.00 29.24  ? 32  VAL A CG2 1 
ATOM   201  N N   . GLN A 1 33  ? 0.705   16.071 1.821   1.00 32.09  ? 33  GLN A N   1 
ATOM   202  C CA  . GLN A 1 33  ? 0.005   16.576 2.998   1.00 29.67  ? 33  GLN A CA  1 
ATOM   203  C C   . GLN A 1 33  ? 0.406   18.019 3.266   1.00 27.71  ? 33  GLN A C   1 
ATOM   204  O O   . GLN A 1 33  ? 1.538   18.418 2.988   1.00 28.98  ? 33  GLN A O   1 
ATOM   205  C CB  . GLN A 1 33  ? 0.322   15.715 4.224   1.00 31.78  ? 33  GLN A CB  1 
ATOM   206  C CG  . GLN A 1 33  ? 1.810   15.574 4.527   1.00 33.44  ? 33  GLN A CG  1 
ATOM   207  C CD  . GLN A 1 33  ? 2.088   15.258 5.981   0.30 33.02  ? 33  GLN A CD  1 
ATOM   208  O OE1 . GLN A 1 33  ? 2.850   15.961 6.640   0.48 33.28  ? 33  GLN A OE1 1 
ATOM   209  N NE2 . GLN A 1 33  ? 1.466   14.204 6.489   0.77 32.51  ? 33  GLN A NE2 1 
ATOM   210  N N   . GLY A 1 34  ? -0.517  18.798 3.815   1.00 24.86  ? 34  GLY A N   1 
ATOM   211  C CA  . GLY A 1 34  ? -0.236  20.195 4.116   1.00 24.38  ? 34  GLY A CA  1 
ATOM   212  C C   . GLY A 1 34  ? -1.279  20.837 5.000   1.00 24.33  ? 34  GLY A C   1 
ATOM   213  O O   . GLY A 1 34  ? -2.344  20.267 5.238   1.00 24.88  ? 34  GLY A O   1 
ATOM   214  N N   . ILE A 1 35  ? -0.954  22.030 5.491   1.00 24.79  ? 35  ILE A N   1 
ATOM   215  C CA  . ILE A 1 35  ? -1.853  22.813 6.329   1.00 24.74  ? 35  ILE A CA  1 
ATOM   216  C C   . ILE A 1 35  ? -1.835  24.235 5.818   1.00 24.46  ? 35  ILE A C   1 
ATOM   217  O O   . ILE A 1 35  ? -0.777  24.853 5.743   1.00 26.42  ? 35  ILE A O   1 
ATOM   218  C CB  . ILE A 1 35  ? -1.415  22.809 7.806   1.00 26.22  ? 35  ILE A CB  1 
ATOM   219  C CG1 . ILE A 1 35  ? -1.133  21.373 8.257   1.00 27.49  ? 35  ILE A CG1 1 
ATOM   220  C CG2 . ILE A 1 35  ? -2.479  23.471 8.678   1.00 27.34  ? 35  ILE A CG2 1 
ATOM   221  C CD1 . ILE A 1 35  ? -0.945  21.210 9.746   1.00 28.86  ? 35  ILE A CD1 1 
ATOM   222  N N   . ILE A 1 36  ? -3.009  24.742 5.465   1.00 23.93  ? 36  ILE A N   1 
ATOM   223  C CA  . ILE A 1 36  ? -3.141  26.081 4.914   1.00 23.51  ? 36  ILE A CA  1 
ATOM   224  C C   . ILE A 1 36  ? -4.063  26.892 5.803   1.00 23.77  ? 36  ILE A C   1 
ATOM   225  O O   . ILE A 1 36  ? -5.201  26.492 6.051   1.00 24.10  ? 36  ILE A O   1 
ATOM   226  C CB  . ILE A 1 36  ? -3.714  26.043 3.487   1.00 23.07  ? 36  ILE A CB  1 
ATOM   227  C CG1 . ILE A 1 36  ? -2.840  25.163 2.585   1.00 23.19  ? 36  ILE A CG1 1 
ATOM   228  C CG2 . ILE A 1 36  ? -3.824  27.451 2.919   1.00 23.16  ? 36  ILE A CG2 1 
ATOM   229  C CD1 . ILE A 1 36  ? -1.435  25.688 2.351   1.00 23.33  ? 36  ILE A CD1 1 
ATOM   230  N N   . ASN A 1 37  ? -3.555  28.027 6.278   1.00 25.65  ? 37  ASN A N   1 
ATOM   231  C CA  . ASN A 1 37  ? -4.305  28.936 7.142   1.00 26.23  ? 37  ASN A CA  1 
ATOM   232  C C   . ASN A 1 37  ? -4.841  30.121 6.350   1.00 27.65  ? 37  ASN A C   1 
ATOM   233  O O   . ASN A 1 37  ? -4.235  30.547 5.368   1.00 28.46  ? 37  ASN A O   1 
ATOM   234  C CB  . ASN A 1 37  ? -3.410  29.450 8.273   1.00 26.10  ? 37  ASN A CB  1 
ATOM   235  C CG  . ASN A 1 37  ? -2.896  28.334 9.163   1.00 26.36  ? 37  ASN A CG  1 
ATOM   236  O OD1 . ASN A 1 37  ? -3.679  27.626 9.795   1.00 28.22  ? 37  ASN A OD1 1 
ATOM   237  N ND2 . ASN A 1 37  ? -1.576  28.174 9.224   1.00 24.15  ? 37  ASN A ND2 1 
ATOM   238  N N   . PHE A 1 38  ? -5.981  30.645 6.788   1.00 28.72  ? 38  PHE A N   1 
ATOM   239  C CA  . PHE A 1 38  ? -6.601  31.810 6.166   1.00 30.42  ? 38  PHE A CA  1 
ATOM   240  C C   . PHE A 1 38  ? -6.942  32.820 7.254   1.00 33.87  ? 38  PHE A C   1 
ATOM   241  O O   . PHE A 1 38  ? -7.425  32.436 8.321   1.00 36.80  ? 38  PHE A O   1 
ATOM   242  C CB  . PHE A 1 38  ? -7.883  31.407 5.435   1.00 29.45  ? 38  PHE A CB  1 
ATOM   243  C CG  . PHE A 1 38  ? -7.676  30.403 4.333   1.00 29.31  ? 38  PHE A CG  1 
ATOM   244  C CD1 . PHE A 1 38  ? -7.561  29.050 4.620   1.00 28.47  ? 38  PHE A CD1 1 
ATOM   245  C CD2 . PHE A 1 38  ? -7.627  30.809 3.007   1.00 30.63  ? 38  PHE A CD2 1 
ATOM   246  C CE1 . PHE A 1 38  ? -7.385  28.123 3.605   1.00 29.46  ? 38  PHE A CE1 1 
ATOM   247  C CE2 . PHE A 1 38  ? -7.451  29.889 1.988   1.00 29.35  ? 38  PHE A CE2 1 
ATOM   248  C CZ  . PHE A 1 38  ? -7.331  28.544 2.288   1.00 28.48  ? 38  PHE A CZ  1 
ATOM   249  N N   . GLU A 1 39  ? -6.704  34.103 6.985   1.00 37.27  ? 39  GLU A N   1 
ATOM   250  C CA  . GLU A 1 39  ? -6.973  35.152 7.971   1.00 43.40  ? 39  GLU A CA  1 
ATOM   251  C C   . GLU A 1 39  ? -7.531  36.434 7.358   1.00 46.40  ? 39  GLU A C   1 
ATOM   252  O O   . GLU A 1 39  ? -7.077  36.882 6.305   1.00 47.46  ? 39  GLU A O   1 
ATOM   253  C CB  . GLU A 1 39  ? -5.708  35.458 8.775   1.00 48.57  ? 39  GLU A CB  1 
ATOM   254  C CG  . GLU A 1 39  ? -5.544  34.551 9.982   1.00 52.49  ? 39  GLU A CG  1 
ATOM   255  C CD  . GLU A 1 39  ? -4.240  34.772 10.711  1.00 58.17  ? 39  GLU A CD  1 
ATOM   256  O OE1 . GLU A 1 39  ? -4.228  35.578 11.665  1.00 57.49  ? 39  GLU A OE1 1 
ATOM   257  O OE2 . GLU A 1 39  ? -3.233  34.141 10.323  1.00 61.28  ? 39  GLU A OE2 1 
ATOM   258  N N   . GLN A 1 40  ? -8.517  37.012 8.042   1.00 48.00  ? 40  GLN A N   1 
ATOM   259  C CA  . GLN A 1 40  ? -9.162  38.249 7.610   1.00 50.75  ? 40  GLN A CA  1 
ATOM   260  C C   . GLN A 1 40  ? -9.530  39.068 8.848   1.00 53.16  ? 40  GLN A C   1 
ATOM   261  O O   . GLN A 1 40  ? -10.223 38.574 9.735   1.00 52.77  ? 40  GLN A O   1 
ATOM   262  C CB  . GLN A 1 40  ? -10.414 37.927 6.790   1.00 51.30  ? 40  GLN A CB  1 
ATOM   263  C CG  . GLN A 1 40  ? -10.788 38.999 5.782   1.00 53.11  ? 40  GLN A CG  1 
ATOM   264  C CD  . GLN A 1 40  ? -12.129 38.745 5.110   1.00 55.94  ? 40  GLN A CD  1 
ATOM   265  O OE1 . GLN A 1 40  ? -13.051 38.203 5.721   1.00 56.44  ? 40  GLN A OE1 1 
ATOM   266  N NE2 . GLN A 1 40  ? -12.246 39.146 3.847   1.00 57.28  ? 40  GLN A NE2 1 
ATOM   267  N N   . LYS A 1 41  ? -9.053  40.307 8.913   1.00 56.82  ? 41  LYS A N   1 
ATOM   268  C CA  . LYS A 1 41  ? -9.296  41.173 10.068  1.00 67.48  ? 41  LYS A CA  1 
ATOM   269  C C   . LYS A 1 41  ? -10.695 41.787 10.026  1.00 72.92  ? 41  LYS A C   1 
ATOM   270  O O   . LYS A 1 41  ? -11.371 41.874 11.053  1.00 76.55  ? 41  LYS A O   1 
ATOM   271  C CB  . LYS A 1 41  ? -8.243  42.281 10.133  1.00 75.82  ? 41  LYS A CB  1 
ATOM   272  C CG  . LYS A 1 41  ? -8.231  43.064 11.440  1.00 83.72  ? 41  LYS A CG  1 
ATOM   273  C CD  . LYS A 1 41  ? -7.158  44.145 11.443  1.00 87.91  ? 41  LYS A CD  1 
ATOM   274  C CE  . LYS A 1 41  ? -5.760  43.556 11.569  1.00 90.40  ? 41  LYS A CE  1 
ATOM   275  N NZ  . LYS A 1 41  ? -4.709  44.608 11.598  1.00 91.90  ? 41  LYS A NZ  1 
ATOM   276  N N   . GLU A 1 42  ? -11.113 42.221 8.839   1.00 73.57  ? 42  GLU A N   1 
ATOM   277  C CA  . GLU A 1 42  ? -12.418 42.850 8.643   1.00 72.68  ? 42  GLU A CA  1 
ATOM   278  C C   . GLU A 1 42  ? -13.124 42.219 7.450   1.00 71.32  ? 42  GLU A C   1 
ATOM   279  O O   . GLU A 1 42  ? -12.470 41.801 6.493   1.00 68.56  ? 42  GLU A O   1 
ATOM   280  C CB  . GLU A 1 42  ? -12.242 44.350 8.398   1.00 74.07  ? 42  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 42  ? -11.643 45.112 9.573   1.00 77.56  ? 42  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 42  ? -11.069 46.463 9.179   1.00 79.68  ? 42  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 42  ? -11.512 47.031 8.156   1.00 76.84  ? 42  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 42  ? -10.171 46.959 9.897   1.00 77.70  ? 42  GLU A OE2 1 
ATOM   285  N N   . SER A 1 43  ? -14.454 42.152 7.507   1.00 69.34  ? 43  SER A N   1 
ATOM   286  C CA  . SER A 1 43  ? -15.250 41.660 6.379   1.00 74.43  ? 43  SER A CA  1 
ATOM   287  C C   . SER A 1 43  ? -15.005 42.553 5.168   1.00 78.35  ? 43  SER A C   1 
ATOM   288  O O   . SER A 1 43  ? -14.879 43.769 5.308   1.00 77.81  ? 43  SER A O   1 
ATOM   289  C CB  . SER A 1 43  ? -16.740 41.642 6.720   1.00 71.74  ? 43  SER A CB  1 
ATOM   290  O OG  . SER A 1 43  ? -17.243 42.956 6.866   1.00 68.04  ? 43  SER A OG  1 
ATOM   291  N N   . ASN A 1 44  ? -14.933 41.941 3.988   1.00 82.45  ? 44  ASN A N   1 
ATOM   292  C CA  . ASN A 1 44  ? -14.500 42.626 2.762   1.00 87.11  ? 44  ASN A CA  1 
ATOM   293  C C   . ASN A 1 44  ? -13.032 43.085 2.804   1.00 85.76  ? 44  ASN A C   1 
ATOM   294  O O   . ASN A 1 44  ? -12.606 43.892 1.973   1.00 91.59  ? 44  ASN A O   1 
ATOM   295  C CB  . ASN A 1 44  ? -15.437 43.803 2.414   1.00 90.96  ? 44  ASN A CB  1 
ATOM   296  C CG  . ASN A 1 44  ? -16.406 43.470 1.297   1.00 95.66  ? 44  ASN A CG  1 
ATOM   297  O OD1 . ASN A 1 44  ? -17.621 43.517 1.482   1.00 103.84 ? 44  ASN A OD1 1 
ATOM   298  N ND2 . ASN A 1 44  ? -15.872 43.136 0.127   1.00 102.39 ? 44  ASN A ND2 1 
ATOM   299  N N   . GLY A 1 45  ? -12.260 42.559 3.754   1.00 78.51  ? 45  GLY A N   1 
ATOM   300  C CA  . GLY A 1 45  ? -10.836 42.867 3.856   1.00 72.16  ? 45  GLY A CA  1 
ATOM   301  C C   . GLY A 1 45  ? -10.028 41.835 3.092   1.00 63.96  ? 45  GLY A C   1 
ATOM   302  O O   . GLY A 1 45  ? -10.557 40.782 2.733   1.00 61.26  ? 45  GLY A O   1 
ATOM   303  N N   . PRO A 1 46  ? -8.740  42.122 2.837   1.00 63.39  ? 46  PRO A N   1 
ATOM   304  C CA  . PRO A 1 46  ? -7.906  41.135 2.153   1.00 59.79  ? 46  PRO A CA  1 
ATOM   305  C C   . PRO A 1 46  ? -7.735  39.875 2.999   1.00 54.92  ? 46  PRO A C   1 
ATOM   306  O O   . PRO A 1 46  ? -7.768  39.955 4.231   1.00 55.32  ? 46  PRO A O   1 
ATOM   307  C CB  . PRO A 1 46  ? -6.568  41.861 1.980   1.00 64.10  ? 46  PRO A CB  1 
ATOM   308  C CG  . PRO A 1 46  ? -6.552  42.897 3.051   1.00 65.98  ? 46  PRO A CG  1 
ATOM   309  C CD  . PRO A 1 46  ? -7.979  43.328 3.207   1.00 64.07  ? 46  PRO A CD  1 
ATOM   310  N N   . VAL A 1 47  ? -7.572  38.730 2.338   1.00 47.61  ? 47  VAL A N   1 
ATOM   311  C CA  . VAL A 1 47  ? -7.380  37.451 3.027   1.00 45.52  ? 47  VAL A CA  1 
ATOM   312  C C   . VAL A 1 47  ? -5.943  36.961 2.865   1.00 46.57  ? 47  VAL A C   1 
ATOM   313  O O   . VAL A 1 47  ? -5.480  36.743 1.746   1.00 46.31  ? 47  VAL A O   1 
ATOM   314  C CB  . VAL A 1 47  ? -8.338  36.362 2.499   1.00 43.50  ? 47  VAL A CB  1 
ATOM   315  C CG1 . VAL A 1 47  ? -8.121  35.051 3.249   1.00 42.36  ? 47  VAL A CG1 1 
ATOM   316  C CG2 . VAL A 1 47  ? -9.787  36.818 2.625   1.00 43.93  ? 47  VAL A CG2 1 
ATOM   317  N N   . LYS A 1 48  ? -5.255  36.778 3.991   1.00 47.03  ? 48  LYS A N   1 
ATOM   318  C CA  . LYS A 1 48  ? -3.886  36.261 4.004   1.00 49.10  ? 48  LYS A CA  1 
ATOM   319  C C   . LYS A 1 48  ? -3.907  34.729 4.057   1.00 44.27  ? 48  LYS A C   1 
ATOM   320  O O   . LYS A 1 48  ? -4.345  34.143 5.049   1.00 42.84  ? 48  LYS A O   1 
ATOM   321  C CB  . LYS A 1 48  ? -3.113  36.830 5.206   1.00 55.49  ? 48  LYS A CB  1 
ATOM   322  C CG  . LYS A 1 48  ? -1.617  36.527 5.227   1.00 61.68  ? 48  LYS A CG  1 
ATOM   323  C CD  . LYS A 1 48  ? -0.868  37.256 4.119   1.00 68.38  ? 48  LYS A CD  1 
ATOM   324  C CE  . LYS A 1 48  ? 0.642   37.202 4.312   1.00 71.62  ? 48  LYS A CE  1 
ATOM   325  N NZ  . LYS A 1 48  ? 1.198   35.831 4.137   1.00 73.28  ? 48  LYS A NZ  1 
ATOM   326  N N   . VAL A 1 49  ? -3.441  34.095 2.981   1.00 40.82  ? 49  VAL A N   1 
ATOM   327  C CA  . VAL A 1 49  ? -3.341  32.640 2.898   1.00 37.55  ? 49  VAL A CA  1 
ATOM   328  C C   . VAL A 1 49  ? -1.891  32.230 3.129   1.00 37.24  ? 49  VAL A C   1 
ATOM   329  O O   . VAL A 1 49  ? -0.997  32.680 2.409   1.00 37.17  ? 49  VAL A O   1 
ATOM   330  C CB  . VAL A 1 49  ? -3.787  32.107 1.516   1.00 36.71  ? 49  VAL A CB  1 
ATOM   331  C CG1 . VAL A 1 49  ? -3.874  30.583 1.534   1.00 34.89  ? 49  VAL A CG1 1 
ATOM   332  C CG2 . VAL A 1 49  ? -5.124  32.714 1.103   1.00 36.01  ? 49  VAL A CG2 1 
ATOM   333  N N   . TRP A 1 50  ? -1.655  31.379 4.124   1.00 35.38  ? 50  TRP A N   1 
ATOM   334  C CA  . TRP A 1 50  ? -0.297  30.924 4.414   1.00 34.37  ? 50  TRP A CA  1 
ATOM   335  C C   . TRP A 1 50  ? -0.238  29.516 4.984   1.00 32.87  ? 50  TRP A C   1 
ATOM   336  O O   . TRP A 1 50  ? -1.210  29.018 5.551   1.00 31.97  ? 50  TRP A O   1 
ATOM   337  C CB  . TRP A 1 50  ? 0.409   31.896 5.362   1.00 36.43  ? 50  TRP A CB  1 
ATOM   338  C CG  . TRP A 1 50  ? -0.159  31.936 6.750   1.00 32.42  ? 50  TRP A CG  1 
ATOM   339  C CD1 . TRP A 1 50  ? -1.222  32.679 7.184   1.00 27.31  ? 50  TRP A CD1 1 
ATOM   340  C CD2 . TRP A 1 50  ? 0.318   31.214 7.891   1.00 34.78  ? 50  TRP A CD2 1 
ATOM   341  N NE1 . TRP A 1 50  ? -1.436  32.460 8.525   1.00 32.36  ? 50  TRP A NE1 1 
ATOM   342  C CE2 . TRP A 1 50  ? -0.505  31.566 8.983   1.00 34.40  ? 50  TRP A CE2 1 
ATOM   343  C CE3 . TRP A 1 50  ? 1.364   30.303 8.096   1.00 36.00  ? 50  TRP A CE3 1 
ATOM   344  C CZ2 . TRP A 1 50  ? -0.319  31.038 10.263  1.00 36.71  ? 50  TRP A CZ2 1 
ATOM   345  C CZ3 . TRP A 1 50  ? 1.550   29.775 9.376   1.00 37.82  ? 50  TRP A CZ3 1 
ATOM   346  C CH2 . TRP A 1 50  ? 0.711   30.145 10.441  1.00 38.00  ? 50  TRP A CH2 1 
ATOM   347  N N   . GLY A 1 51  ? 0.932   28.898 4.837   1.00 31.72  ? 51  GLY A N   1 
ATOM   348  C CA  . GLY A 1 51  ? 1.155   27.514 5.241   1.00 30.30  ? 51  GLY A CA  1 
ATOM   349  C C   . GLY A 1 51  ? 2.158   26.837 4.327   1.00 29.76  ? 51  GLY A C   1 
ATOM   350  O O   . GLY A 1 51  ? 2.989   27.499 3.700   1.00 29.23  ? 51  GLY A O   1 
ATOM   351  N N   . SER A 1 52  ? 2.079   25.513 4.243   1.00 30.14  ? 52  SER A N   1 
ATOM   352  C CA  . SER A 1 52  ? 3.000   24.749 3.411   1.00 30.79  ? 52  SER A CA  1 
ATOM   353  C C   . SER A 1 52  ? 2.453   23.372 3.089   1.00 30.29  ? 52  SER A C   1 
ATOM   354  O O   . SER A 1 52  ? 1.641   22.828 3.835   1.00 30.02  ? 52  SER A O   1 
ATOM   355  C CB  . SER A 1 52  ? 4.354   24.608 4.100   1.00 32.25  ? 52  SER A CB  1 
ATOM   356  O OG  . SER A 1 52  ? 4.220   23.916 5.324   1.00 35.83  ? 52  SER A OG  1 
ATOM   357  N N   . ILE A 1 53  ? 2.904   22.823 1.966   1.00 30.38  ? 53  ILE A N   1 
ATOM   358  C CA  . ILE A 1 53  ? 2.461   21.518 1.492   1.00 29.94  ? 53  ILE A CA  1 
ATOM   359  C C   . ILE A 1 53  ? 3.689   20.657 1.217   1.00 31.42  ? 53  ILE A C   1 
ATOM   360  O O   . ILE A 1 53  ? 4.652   21.124 0.612   1.00 32.39  ? 53  ILE A O   1 
ATOM   361  C CB  . ILE A 1 53  ? 1.611   21.644 0.210   1.00 29.45  ? 53  ILE A CB  1 
ATOM   362  C CG1 . ILE A 1 53  ? 0.473   22.655 0.419   1.00 29.34  ? 53  ILE A CG1 1 
ATOM   363  C CG2 . ILE A 1 53  ? 1.051   20.281 -0.198  1.00 29.41  ? 53  ILE A CG2 1 
ATOM   364  C CD1 . ILE A 1 53  ? -0.199  23.123 -0.856  1.00 29.16  ? 53  ILE A CD1 1 
ATOM   365  N N   . LYS A 1 54  ? 3.646   19.405 1.668   1.00 33.04  ? 54  LYS A N   1 
ATOM   366  C CA  . LYS A 1 54  ? 4.751   18.461 1.502   1.00 34.90  ? 54  LYS A CA  1 
ATOM   367  C C   . LYS A 1 54  ? 4.379   17.373 0.499   1.00 31.91  ? 54  LYS A C   1 
ATOM   368  O O   . LYS A 1 54  ? 3.208   17.211 0.154   1.00 30.63  ? 54  LYS A O   1 
ATOM   369  C CB  . LYS A 1 54  ? 5.100   17.816 2.850   1.00 40.21  ? 54  LYS A CB  1 
ATOM   370  C CG  . LYS A 1 54  ? 6.033   18.643 3.726   1.00 47.59  ? 54  LYS A CG  1 
ATOM   371  C CD  . LYS A 1 54  ? 5.853   18.351 5.215   1.00 55.23  ? 54  LYS A CD  1 
ATOM   372  C CE  . LYS A 1 54  ? 6.104   16.890 5.570   1.00 61.70  ? 54  LYS A CE  1 
ATOM   373  N NZ  . LYS A 1 54  ? 5.858   16.623 7.018   1.00 62.71  ? 54  LYS A NZ  1 
ATOM   374  N N   . GLY A 1 55  ? 5.386   16.642 0.030   1.00 31.20  ? 55  GLY A N   1 
ATOM   375  C CA  . GLY A 1 55  ? 5.175   15.440 -0.773  1.00 31.77  ? 55  GLY A CA  1 
ATOM   376  C C   . GLY A 1 55  ? 4.770   15.671 -2.217  1.00 32.82  ? 55  GLY A C   1 
ATOM   377  O O   . GLY A 1 55  ? 4.338   14.737 -2.895  1.00 35.79  ? 55  GLY A O   1 
ATOM   378  N N   . LEU A 1 56  ? 4.908   16.908 -2.688  1.00 32.40  ? 56  LEU A N   1 
ATOM   379  C CA  . LEU A 1 56  ? 4.573   17.263 -4.065  1.00 32.76  ? 56  LEU A CA  1 
ATOM   380  C C   . LEU A 1 56  ? 5.780   17.084 -4.968  1.00 34.48  ? 56  LEU A C   1 
ATOM   381  O O   . LEU A 1 56  ? 6.919   17.267 -4.537  1.00 36.06  ? 56  LEU A O   1 
ATOM   382  C CB  . LEU A 1 56  ? 4.128   18.723 -4.141  1.00 33.36  ? 56  LEU A CB  1 
ATOM   383  C CG  . LEU A 1 56  ? 2.803   19.092 -3.473  1.00 32.28  ? 56  LEU A CG  1 
ATOM   384  C CD1 . LEU A 1 56  ? 2.685   20.603 -3.316  1.00 31.81  ? 56  LEU A CD1 1 
ATOM   385  C CD2 . LEU A 1 56  ? 1.636   18.534 -4.274  1.00 31.60  ? 56  LEU A CD2 1 
ATOM   386  N N   . THR A 1 57  ? 5.533   16.734 -6.224  1.00 35.51  ? 57  THR A N   1 
ATOM   387  C CA  . THR A 1 57  ? 6.599   16.709 -7.220  1.00 36.10  ? 57  THR A CA  1 
ATOM   388  C C   . THR A 1 57  ? 7.106   18.134 -7.424  1.00 38.26  ? 57  THR A C   1 
ATOM   389  O O   . THR A 1 57  ? 6.340   19.093 -7.298  1.00 37.87  ? 57  THR A O   1 
ATOM   390  C CB  . THR A 1 57  ? 6.120   16.134 -8.567  1.00 34.95  ? 57  THR A CB  1 
ATOM   391  O OG1 . THR A 1 57  ? 4.927   16.810 -8.983  1.00 34.05  ? 57  THR A OG1 1 
ATOM   392  C CG2 . THR A 1 57  ? 5.836   14.645 -8.444  1.00 33.70  ? 57  THR A CG2 1 
ATOM   393  N N   . GLU A 1 58  ? 8.394   18.267 -7.724  1.00 41.19  ? 58  GLU A N   1 
ATOM   394  C CA  . GLU A 1 58  ? 9.004   19.577 -7.932  1.00 43.44  ? 58  GLU A CA  1 
ATOM   395  C C   . GLU A 1 58  ? 8.364   20.279 -9.123  1.00 43.35  ? 58  GLU A C   1 
ATOM   396  O O   . GLU A 1 58  ? 8.222   19.683 -10.189 1.00 44.38  ? 58  GLU A O   1 
ATOM   397  C CB  . GLU A 1 58  ? 10.500  19.424 -8.182  1.00 47.32  ? 58  GLU A CB  1 
ATOM   398  C CG  . GLU A 1 58  ? 11.255  20.740 -8.270  1.00 50.68  ? 58  GLU A CG  1 
ATOM   399  C CD  . GLU A 1 58  ? 12.641  20.583 -8.863  1.00 56.76  ? 58  GLU A CD  1 
ATOM   400  O OE1 . GLU A 1 58  ? 13.024  19.444 -9.210  1.00 55.62  ? 58  GLU A OE1 1 
ATOM   401  O OE2 . GLU A 1 58  ? 13.351  21.604 -8.978  1.00 62.38  ? 58  GLU A OE2 1 
ATOM   402  N N   . GLY A 1 59  ? 7.980   21.541 -8.934  1.00 42.27  ? 59  GLY A N   1 
ATOM   403  C CA  . GLY A 1 59  ? 7.386   22.347 -10.002 1.00 40.89  ? 59  GLY A CA  1 
ATOM   404  C C   . GLY A 1 59  ? 6.152   23.112 -9.562  1.00 39.59  ? 59  GLY A C   1 
ATOM   405  O O   . GLY A 1 59  ? 5.897   23.257 -8.370  1.00 38.97  ? 59  GLY A O   1 
ATOM   406  N N   . LEU A 1 60  ? 5.394   23.607 -10.540 1.00 41.04  ? 60  LEU A N   1 
ATOM   407  C CA  . LEU A 1 60  ? 4.158   24.352 -10.289 1.00 40.55  ? 60  LEU A CA  1 
ATOM   408  C C   . LEU A 1 60  ? 3.012   23.387 -10.024 1.00 38.36  ? 60  LEU A C   1 
ATOM   409  O O   . LEU A 1 60  ? 3.013   22.272 -10.535 1.00 38.43  ? 60  LEU A O   1 
ATOM   410  C CB  . LEU A 1 60  ? 3.803   25.231 -11.490 1.00 43.50  ? 60  LEU A CB  1 
ATOM   411  C CG  . LEU A 1 60  ? 4.771   26.364 -11.842 1.00 46.59  ? 60  LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 60  ? 4.462   26.929 -13.222 1.00 46.41  ? 60  LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 60  ? 4.716   27.458 -10.788 1.00 48.22  ? 60  LEU A CD2 1 
ATOM   414  N N   . HIS A 1 61  ? 2.038   23.813 -9.226  1.00 34.20  ? 61  HIS A N   1 
ATOM   415  C CA  . HIS A 1 61  ? 0.857   22.994 -8.941  1.00 30.71  ? 61  HIS A CA  1 
ATOM   416  C C   . HIS A 1 61  ? -0.377  23.873 -8.816  1.00 30.58  ? 61  HIS A C   1 
ATOM   417  O O   . HIS A 1 61  ? -0.399  24.799 -8.002  1.00 28.70  ? 61  HIS A O   1 
ATOM   418  C CB  . HIS A 1 61  ? 1.046   22.193 -7.647  1.00 30.56  ? 61  HIS A CB  1 
ATOM   419  C CG  . HIS A 1 61  ? 2.083   21.119 -7.749  1.00 31.56  ? 61  HIS A CG  1 
ATOM   420  N ND1 . HIS A 1 61  ? 1.775   19.816 -8.071  1.00 32.18  ? 61  HIS A ND1 1 
ATOM   421  C CD2 . HIS A 1 61  ? 3.425   21.158 -7.584  1.00 32.18  ? 61  HIS A CD2 1 
ATOM   422  C CE1 . HIS A 1 61  ? 2.882   19.097 -8.095  1.00 32.77  ? 61  HIS A CE1 1 
ATOM   423  N NE2 . HIS A 1 61  ? 3.898   19.888 -7.803  1.00 33.00  ? 61  HIS A NE2 1 
ATOM   424  N N   . GLY A 1 62  ? -1.391  23.584 -9.631  1.00 28.91  ? 62  GLY A N   1 
ATOM   425  C CA  . GLY A 1 62  ? -2.681  24.257 -9.536  1.00 30.46  ? 62  GLY A CA  1 
ATOM   426  C C   . GLY A 1 62  ? -3.158  24.275 -8.098  1.00 31.22  ? 62  GLY A C   1 
ATOM   427  O O   . GLY A 1 62  ? -3.138  23.250 -7.421  1.00 31.70  ? 62  GLY A O   1 
ATOM   428  N N   . PHE A 1 63  ? -3.565  25.451 -7.631  1.00 33.56  ? 63  PHE A N   1 
ATOM   429  C CA  . PHE A 1 63  ? -3.921  25.665 -6.231  1.00 33.81  ? 63  PHE A CA  1 
ATOM   430  C C   . PHE A 1 63  ? -5.101  26.617 -6.185  1.00 35.35  ? 63  PHE A C   1 
ATOM   431  O O   . PHE A 1 63  ? -4.955  27.797 -6.482  1.00 37.99  ? 63  PHE A O   1 
ATOM   432  C CB  . PHE A 1 63  ? -2.724  26.261 -5.487  1.00 31.96  ? 63  PHE A CB  1 
ATOM   433  C CG  . PHE A 1 63  ? -2.972  26.528 -4.028  1.00 31.13  ? 63  PHE A CG  1 
ATOM   434  C CD1 . PHE A 1 63  ? -3.024  25.483 -3.115  1.00 30.13  ? 63  PHE A CD1 1 
ATOM   435  C CD2 . PHE A 1 63  ? -3.115  27.826 -3.559  1.00 30.91  ? 63  PHE A CD2 1 
ATOM   436  C CE1 . PHE A 1 63  ? -3.234  25.725 -1.766  1.00 28.66  ? 63  PHE A CE1 1 
ATOM   437  C CE2 . PHE A 1 63  ? -3.326  28.074 -2.211  1.00 30.10  ? 63  PHE A CE2 1 
ATOM   438  C CZ  . PHE A 1 63  ? -3.388  27.022 -1.313  1.00 28.92  ? 63  PHE A CZ  1 
ATOM   439  N N   . HIS A 1 64  ? -6.277  26.098 -5.846  1.00 37.62  ? 64  HIS A N   1 
ATOM   440  C CA  . HIS A 1 64  ? -7.474  26.935 -5.783  1.00 40.99  ? 64  HIS A CA  1 
ATOM   441  C C   . HIS A 1 64  ? -8.610  26.330 -4.969  1.00 39.35  ? 64  HIS A C   1 
ATOM   442  O O   . HIS A 1 64  ? -8.647  25.131 -4.717  1.00 36.99  ? 64  HIS A O   1 
ATOM   443  C CB  . HIS A 1 64  ? -7.974  27.295 -7.196  1.00 45.72  ? 64  HIS A CB  1 
ATOM   444  C CG  . HIS A 1 64  ? -7.679  26.262 -8.239  1.00 46.57  ? 64  HIS A CG  1 
ATOM   445  N ND1 . HIS A 1 64  ? -6.794  26.485 -9.273  1.00 47.33  ? 64  HIS A ND1 1 
ATOM   446  C CD2 . HIS A 1 64  ? -8.158  25.010 -8.417  1.00 48.14  ? 64  HIS A CD2 1 
ATOM   447  C CE1 . HIS A 1 64  ? -6.736  25.412 -10.040 1.00 46.79  ? 64  HIS A CE1 1 
ATOM   448  N NE2 . HIS A 1 64  ? -7.554  24.502 -9.542  1.00 50.40  ? 64  HIS A NE2 1 
ATOM   449  N N   . VAL A 1 65  ? -9.527  27.200 -4.557  1.00 41.44  ? 65  VAL A N   1 
ATOM   450  C CA  . VAL A 1 65  ? -10.739 26.800 -3.858  1.00 41.12  ? 65  VAL A CA  1 
ATOM   451  C C   . VAL A 1 65  ? -11.761 26.365 -4.900  1.00 42.45  ? 65  VAL A C   1 
ATOM   452  O O   . VAL A 1 65  ? -11.995 27.078 -5.877  1.00 46.28  ? 65  VAL A O   1 
ATOM   453  C CB  . VAL A 1 65  ? -11.320 27.967 -3.028  1.00 41.24  ? 65  VAL A CB  1 
ATOM   454  C CG1 . VAL A 1 65  ? -12.591 27.538 -2.304  1.00 40.58  ? 65  VAL A CG1 1 
ATOM   455  C CG2 . VAL A 1 65  ? -10.282 28.485 -2.035  1.00 40.45  ? 65  VAL A CG2 1 
ATOM   456  N N   . HIS A 1 66  ? -12.367 25.201 -4.692  1.00 43.02  ? 66  HIS A N   1 
ATOM   457  C CA  . HIS A 1 66  ? -13.372 24.684 -5.618  1.00 43.03  ? 66  HIS A CA  1 
ATOM   458  C C   . HIS A 1 66  ? -14.645 25.529 -5.546  1.00 45.54  ? 66  HIS A C   1 
ATOM   459  O O   . HIS A 1 66  ? -15.387 25.470 -4.567  1.00 42.21  ? 66  HIS A O   1 
ATOM   460  C CB  . HIS A 1 66  ? -13.677 23.216 -5.309  1.00 41.28  ? 66  HIS A CB  1 
ATOM   461  C CG  . HIS A 1 66  ? -14.727 22.618 -6.192  1.00 40.33  ? 66  HIS A CG  1 
ATOM   462  N ND1 . HIS A 1 66  ? -14.538 22.413 -7.542  1.00 40.43  ? 66  HIS A ND1 1 
ATOM   463  C CD2 . HIS A 1 66  ? -15.975 22.175 -5.914  1.00 40.81  ? 66  HIS A CD2 1 
ATOM   464  C CE1 . HIS A 1 66  ? -15.628 21.873 -8.058  1.00 40.89  ? 66  HIS A CE1 1 
ATOM   465  N NE2 . HIS A 1 66  ? -16.513 21.716 -7.091  1.00 41.31  ? 66  HIS A NE2 1 
ATOM   466  N N   . GLY A 1 67  ? -14.877 26.317 -6.592  1.00 51.05  ? 67  GLY A N   1 
ATOM   467  C CA  . GLY A 1 67  ? -16.022 27.223 -6.658  1.00 59.22  ? 67  GLY A CA  1 
ATOM   468  C C   . GLY A 1 67  ? -15.675 28.517 -7.374  1.00 69.59  ? 67  GLY A C   1 
ATOM   469  O O   . GLY A 1 67  ? -14.522 28.737 -7.753  1.00 71.40  ? 67  GLY A O   1 
ATOM   470  N N   . ALA A 1 68  ? -16.677 29.376 -7.552  1.00 77.61  ? 68  ALA A N   1 
ATOM   471  C CA  . ALA A 1 68  ? -16.507 30.639 -8.271  1.00 78.93  ? 68  ALA A CA  1 
ATOM   472  C C   . ALA A 1 68  ? -15.696 31.644 -7.454  1.00 80.45  ? 68  ALA A C   1 
ATOM   473  O O   . ALA A 1 68  ? -15.914 31.799 -6.250  1.00 79.65  ? 68  ALA A O   1 
ATOM   474  C CB  . ALA A 1 68  ? -17.862 31.228 -8.636  1.00 81.46  ? 68  ALA A CB  1 
ATOM   475  N N   . GLY A 1 69  ? -14.763 32.322 -8.120  1.00 80.25  ? 69  GLY A N   1 
ATOM   476  C CA  . GLY A 1 69  ? -13.907 33.316 -7.477  1.00 80.04  ? 69  GLY A CA  1 
ATOM   477  C C   . GLY A 1 69  ? -12.895 32.704 -6.530  1.00 80.70  ? 69  GLY A C   1 
ATOM   478  O O   . GLY A 1 69  ? -12.549 33.308 -5.513  1.00 82.58  ? 69  GLY A O   1 
ATOM   479  N N   . GLY A 1 70  ? -12.411 31.512 -6.876  1.00 76.28  ? 70  GLY A N   1 
ATOM   480  C CA  . GLY A 1 70  ? -11.538 30.737 -5.998  1.00 72.11  ? 70  GLY A CA  1 
ATOM   481  C C   . GLY A 1 70  ? -10.151 30.447 -6.544  1.00 67.88  ? 70  GLY A C   1 
ATOM   482  O O   . GLY A 1 70  ? -9.441  29.611 -5.990  1.00 61.50  ? 70  GLY A O   1 
ATOM   483  N N   . ASP A 1 71  ? -9.752  31.130 -7.617  1.00 68.95  ? 71  ASP A N   1 
ATOM   484  C CA  . ASP A 1 71  ? -8.415  30.938 -8.183  1.00 68.33  ? 71  ASP A CA  1 
ATOM   485  C C   . ASP A 1 71  ? -7.373  31.678 -7.345  1.00 67.09  ? 71  ASP A C   1 
ATOM   486  O O   . ASP A 1 71  ? -7.473  32.891 -7.153  1.00 70.91  ? 71  ASP A O   1 
ATOM   487  C CB  . ASP A 1 71  ? -8.353  31.412 -9.639  1.00 70.32  ? 71  ASP A CB  1 
ATOM   488  C CG  . ASP A 1 71  ? -7.143  30.860 -10.387 1.00 69.80  ? 71  ASP A CG  1 
ATOM   489  O OD1 . ASP A 1 71  ? -6.115  30.558 -9.749  1.00 67.30  ? 71  ASP A OD1 1 
ATOM   490  O OD2 . ASP A 1 71  ? -7.218  30.729 -11.625 1.00 76.26  ? 71  ASP A OD2 1 
ATOM   491  N N   . LEU A 1 72  ? -6.386  30.931 -6.846  1.00 60.43  ? 72  LEU A N   1 
ATOM   492  C CA  . LEU A 1 72  ? -5.258  31.492 -6.099  1.00 55.92  ? 72  LEU A CA  1 
ATOM   493  C C   . LEU A 1 72  ? -3.941  31.277 -6.850  1.00 52.38  ? 72  LEU A C   1 
ATOM   494  O O   . LEU A 1 72  ? -2.859  31.408 -6.277  1.00 48.77  ? 72  LEU A O   1 
ATOM   495  C CB  . LEU A 1 72  ? -5.176  30.853 -4.709  1.00 52.31  ? 72  LEU A CB  1 
ATOM   496  C CG  . LEU A 1 72  ? -6.457  30.907 -3.873  1.00 53.12  ? 72  LEU A CG  1 
ATOM   497  C CD1 . LEU A 1 72  ? -6.301  30.083 -2.605  1.00 51.19  ? 72  LEU A CD1 1 
ATOM   498  C CD2 . LEU A 1 72  ? -6.836  32.342 -3.539  1.00 54.38  ? 72  LEU A CD2 1 
ATOM   499  N N   . GLY A 1 73  ? -4.042  30.951 -8.136  1.00 52.63  ? 73  GLY A N   1 
ATOM   500  C CA  . GLY A 1 73  ? -2.873  30.748 -8.979  1.00 55.05  ? 73  GLY A CA  1 
ATOM   501  C C   . GLY A 1 73  ? -2.230  29.396 -8.750  1.00 53.31  ? 73  GLY A C   1 
ATOM   502  O O   . GLY A 1 73  ? -2.920  28.379 -8.666  1.00 54.32  ? 73  GLY A O   1 
ATOM   503  N N   . ASN A 1 74  ? -0.903  29.389 -8.660  1.00 52.19  ? 74  ASN A N   1 
ATOM   504  C CA  . ASN A 1 74  ? -0.143  28.167 -8.432  1.00 49.54  ? 74  ASN A CA  1 
ATOM   505  C C   . ASN A 1 74  ? 0.809   28.320 -7.259  1.00 46.81  ? 74  ASN A C   1 
ATOM   506  O O   . ASN A 1 74  ? 1.164   29.433 -6.873  1.00 47.49  ? 74  ASN A O   1 
ATOM   507  C CB  . ASN A 1 74  ? 0.667   27.798 -9.676  1.00 52.00  ? 74  ASN A CB  1 
ATOM   508  C CG  . ASN A 1 74  ? -0.200  27.590 -10.903 1.00 53.71  ? 74  ASN A CG  1 
ATOM   509  O OD1 . ASN A 1 74  ? -1.316  27.079 -10.813 1.00 54.41  ? 74  ASN A OD1 1 
ATOM   510  N ND2 . ASN A 1 74  ? 0.315   27.978 -12.061 1.00 54.18  ? 74  ASN A ND2 1 
ATOM   511  N N   . VAL A 1 75  ? 1.215   27.186 -6.701  1.00 43.14  ? 75  VAL A N   1 
ATOM   512  C CA  . VAL A 1 75  ? 2.282   27.144 -5.708  1.00 39.82  ? 75  VAL A CA  1 
ATOM   513  C C   . VAL A 1 75  ? 3.468   26.405 -6.317  1.00 39.38  ? 75  VAL A C   1 
ATOM   514  O O   . VAL A 1 75  ? 3.295   25.599 -7.236  1.00 37.85  ? 75  VAL A O   1 
ATOM   515  C CB  . VAL A 1 75  ? 1.827   26.480 -4.390  1.00 39.24  ? 75  VAL A CB  1 
ATOM   516  C CG1 . VAL A 1 75  ? 0.756   27.332 -3.722  1.00 41.00  ? 75  VAL A CG1 1 
ATOM   517  C CG2 . VAL A 1 75  ? 1.320   25.057 -4.616  1.00 37.54  ? 75  VAL A CG2 1 
ATOM   518  N N   . THR A 1 76  ? 4.668   26.698 -5.818  1.00 39.47  ? 76  THR A N   1 
ATOM   519  C CA  . THR A 1 76  ? 5.896   26.101 -6.339  1.00 40.16  ? 76  THR A CA  1 
ATOM   520  C C   . THR A 1 76  ? 6.537   25.189 -5.293  1.00 40.49  ? 76  THR A C   1 
ATOM   521  O O   . THR A 1 76  ? 6.901   25.634 -4.200  1.00 39.35  ? 76  THR A O   1 
ATOM   522  C CB  . THR A 1 76  ? 6.915   27.178 -6.765  1.00 42.15  ? 76  THR A CB  1 
ATOM   523  O OG1 . THR A 1 76  ? 6.280   28.124 -7.637  1.00 44.53  ? 76  THR A OG1 1 
ATOM   524  C CG2 . THR A 1 76  ? 8.118   26.543 -7.484  1.00 42.71  ? 76  THR A CG2 1 
ATOM   525  N N   . ALA A 1 77  ? 6.669   23.912 -5.646  1.00 39.27  ? 77  ALA A N   1 
ATOM   526  C CA  . ALA A 1 77  ? 7.323   22.931 -4.797  1.00 37.69  ? 77  ALA A CA  1 
ATOM   527  C C   . ALA A 1 77  ? 8.800   22.865 -5.159  1.00 38.51  ? 77  ALA A C   1 
ATOM   528  O O   . ALA A 1 77  ? 9.145   22.755 -6.337  1.00 37.71  ? 77  ALA A O   1 
ATOM   529  C CB  . ALA A 1 77  ? 6.676   21.570 -4.978  1.00 37.62  ? 77  ALA A CB  1 
ATOM   530  N N   . ASP A 1 78  ? 9.664   22.927 -4.145  1.00 40.05  ? 78  ASP A N   1 
ATOM   531  C CA  . ASP A 1 78  ? 11.120  22.854 -4.343  1.00 41.83  ? 78  ASP A CA  1 
ATOM   532  C C   . ASP A 1 78  ? 11.586  21.402 -4.546  1.00 42.99  ? 78  ASP A C   1 
ATOM   533  O O   . ASP A 1 78  ? 10.759  20.498 -4.690  1.00 42.88  ? 78  ASP A O   1 
ATOM   534  C CB  . ASP A 1 78  ? 11.863  23.542 -3.179  1.00 41.63  ? 78  ASP A CB  1 
ATOM   535  C CG  . ASP A 1 78  ? 11.650  22.853 -1.830  1.00 41.46  ? 78  ASP A CG  1 
ATOM   536  O OD1 . ASP A 1 78  ? 10.891  21.868 -1.739  1.00 40.60  ? 78  ASP A OD1 1 
ATOM   537  O OD2 . ASP A 1 78  ? 12.257  23.312 -0.843  1.00 44.40  ? 78  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 79  ? 12.901  21.181 -4.571  1.00 45.71  ? 79  LYS A N   1 
ATOM   539  C CA  . LYS A 1 79  ? 13.449  19.831 -4.762  1.00 49.33  ? 79  LYS A CA  1 
ATOM   540  C C   . LYS A 1 79  ? 13.193  18.883 -3.585  1.00 45.66  ? 79  LYS A C   1 
ATOM   541  O O   . LYS A 1 79  ? 13.283  17.669 -3.750  1.00 54.15  ? 79  LYS A O   1 
ATOM   542  C CB  . LYS A 1 79  ? 14.951  19.882 -5.080  1.00 55.41  ? 79  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 79  ? 15.256  20.404 -6.476  1.00 61.63  ? 79  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 79  ? 16.538  19.824 -7.057  1.00 67.31  ? 79  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 79  ? 16.684  20.163 -8.537  1.00 68.75  ? 79  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 79  ? 16.967  21.607 -8.769  1.00 68.59  ? 79  LYS A NZ  1 
ATOM   547  N N   . ASP A 1 80  ? 12.879  19.430 -2.411  1.00 40.82  ? 80  ASP A N   1 
ATOM   548  C CA  . ASP A 1 80  ? 12.445  18.622 -1.264  1.00 40.65  ? 80  ASP A CA  1 
ATOM   549  C C   . ASP A 1 80  ? 10.978  18.193 -1.380  1.00 36.76  ? 80  ASP A C   1 
ATOM   550  O O   . ASP A 1 80  ? 10.519  17.338 -0.626  1.00 37.33  ? 80  ASP A O   1 
ATOM   551  C CB  . ASP A 1 80  ? 12.627  19.400 0.046   1.00 43.16  ? 80  ASP A CB  1 
ATOM   552  C CG  . ASP A 1 80  ? 14.066  19.784 0.307   1.00 44.57  ? 80  ASP A CG  1 
ATOM   553  O OD1 . ASP A 1 80  ? 14.964  19.045 -0.141  1.00 47.29  ? 80  ASP A OD1 1 
ATOM   554  O OD2 . ASP A 1 80  ? 14.295  20.824 0.964   1.00 48.31  ? 80  ASP A OD2 1 
ATOM   555  N N   . GLY A 1 81  ? 10.245  18.796 -2.312  1.00 33.58  ? 81  GLY A N   1 
ATOM   556  C CA  . GLY A 1 81  ? 8.820   18.528 -2.481  1.00 31.65  ? 81  GLY A CA  1 
ATOM   557  C C   . GLY A 1 81  ? 7.954   19.419 -1.608  1.00 30.46  ? 81  GLY A C   1 
ATOM   558  O O   . GLY A 1 81  ? 6.753   19.177 -1.457  1.00 30.40  ? 81  GLY A O   1 
ATOM   559  N N   . VAL A 1 82  ? 8.567   20.460 -1.047  1.00 30.66  ? 82  VAL A N   1 
ATOM   560  C CA  . VAL A 1 82  ? 7.893   21.360 -0.127  1.00 30.07  ? 82  VAL A CA  1 
ATOM   561  C C   . VAL A 1 82  ? 7.534   22.655 -0.844  1.00 31.14  ? 82  VAL A C   1 
ATOM   562  O O   . VAL A 1 82  ? 8.387   23.286 -1.473  1.00 32.82  ? 82  VAL A O   1 
ATOM   563  C CB  . VAL A 1 82  ? 8.777   21.678 1.093   1.00 29.02  ? 82  VAL A CB  1 
ATOM   564  C CG1 . VAL A 1 82  ? 8.080   22.663 2.021   1.00 29.01  ? 82  VAL A CG1 1 
ATOM   565  C CG2 . VAL A 1 82  ? 9.123   20.398 1.839   1.00 28.17  ? 82  VAL A CG2 1 
ATOM   566  N N   . ALA A 1 83  ? 6.262   23.034 -0.747  1.00 31.88  ? 83  ALA A N   1 
ATOM   567  C CA  . ALA A 1 83  ? 5.776   24.294 -1.284  1.00 33.81  ? 83  ALA A CA  1 
ATOM   568  C C   . ALA A 1 83  ? 5.318   25.163 -0.131  1.00 34.91  ? 83  ALA A C   1 
ATOM   569  O O   . ALA A 1 83  ? 4.348   24.828 0.550   1.00 35.40  ? 83  ALA A O   1 
ATOM   570  C CB  . ALA A 1 83  ? 4.620   24.054 -2.243  1.00 33.20  ? 83  ALA A CB  1 
ATOM   571  N N   . ASP A 1 84  ? 6.027   26.265 0.098   1.00 37.50  ? 84  ASP A N   1 
ATOM   572  C CA  . ASP A 1 84  ? 5.591   27.264 1.064   1.00 39.62  ? 84  ASP A CA  1 
ATOM   573  C C   . ASP A 1 84  ? 4.592   28.175 0.381   1.00 41.16  ? 84  ASP A C   1 
ATOM   574  O O   . ASP A 1 84  ? 4.809   28.592 -0.761  1.00 42.75  ? 84  ASP A O   1 
ATOM   575  C CB  . ASP A 1 84  ? 6.771   28.079 1.577   1.00 40.60  ? 84  ASP A CB  1 
ATOM   576  C CG  . ASP A 1 84  ? 7.749   27.242 2.367   1.00 44.42  ? 84  ASP A CG  1 
ATOM   577  O OD1 . ASP A 1 84  ? 7.313   26.567 3.325   1.00 46.98  ? 84  ASP A OD1 1 
ATOM   578  O OD2 . ASP A 1 84  ? 8.953   27.256 2.029   1.00 48.00  ? 84  ASP A OD2 1 
ATOM   579  N N   . VAL A 1 85  ? 3.495   28.467 1.078   1.00 42.23  ? 85  VAL A N   1 
ATOM   580  C CA  . VAL A 1 85  ? 2.441   29.325 0.553   1.00 40.88  ? 85  VAL A CA  1 
ATOM   581  C C   . VAL A 1 85  ? 2.372   30.600 1.374   1.00 42.45  ? 85  VAL A C   1 
ATOM   582  O O   . VAL A 1 85  ? 2.416   30.561 2.604   1.00 40.87  ? 85  VAL A O   1 
ATOM   583  C CB  . VAL A 1 85  ? 1.068   28.630 0.600   1.00 38.45  ? 85  VAL A CB  1 
ATOM   584  C CG1 . VAL A 1 85  ? -0.009  29.535 0.018   1.00 37.25  ? 85  VAL A CG1 1 
ATOM   585  C CG2 . VAL A 1 85  ? 1.124   27.303 -0.147  1.00 40.07  ? 85  VAL A CG2 1 
ATOM   586  N N   . SER A 1 86  ? 2.274   31.727 0.680   1.00 45.45  ? 86  SER A N   1 
ATOM   587  C CA  . SER A 1 86  ? 2.100   33.020 1.323   1.00 50.61  ? 86  SER A CA  1 
ATOM   588  C C   . SER A 1 86  ? 1.497   33.995 0.314   1.00 54.68  ? 86  SER A C   1 
ATOM   589  O O   . SER A 1 86  ? 2.213   34.637 -0.457  1.00 58.72  ? 86  SER A O   1 
ATOM   590  C CB  . SER A 1 86  ? 3.428   33.544 1.871   1.00 52.70  ? 86  SER A CB  1 
ATOM   591  O OG  . SER A 1 86  ? 3.201   34.608 2.775   1.00 56.79  ? 86  SER A OG  1 
ATOM   592  N N   . ILE A 1 87  ? 0.169   34.067 0.319   1.00 55.89  ? 87  ILE A N   1 
ATOM   593  C CA  . ILE A 1 87  ? -0.593  34.886 -0.617  1.00 57.38  ? 87  ILE A CA  1 
ATOM   594  C C   . ILE A 1 87  ? -1.499  35.816 0.174   1.00 56.17  ? 87  ILE A C   1 
ATOM   595  O O   . ILE A 1 87  ? -2.012  35.445 1.224   1.00 51.35  ? 87  ILE A O   1 
ATOM   596  C CB  . ILE A 1 87  ? -1.480  34.007 -1.532  1.00 58.79  ? 87  ILE A CB  1 
ATOM   597  C CG1 . ILE A 1 87  ? -0.622  33.022 -2.337  1.00 59.66  ? 87  ILE A CG1 1 
ATOM   598  C CG2 . ILE A 1 87  ? -2.312  34.868 -2.478  1.00 61.44  ? 87  ILE A CG2 1 
ATOM   599  C CD1 . ILE A 1 87  ? -1.392  31.836 -2.882  1.00 59.25  ? 87  ILE A CD1 1 
ATOM   600  N N   . GLU A 1 88  ? -1.685  37.031 -0.326  1.00 59.81  ? 88  GLU A N   1 
ATOM   601  C CA  . GLU A 1 88  ? -2.759  37.885 0.155   1.00 62.86  ? 88  GLU A CA  1 
ATOM   602  C C   . GLU A 1 88  ? -3.700  38.142 -1.011  1.00 63.01  ? 88  GLU A C   1 
ATOM   603  O O   . GLU A 1 88  ? -3.272  38.625 -2.057  1.00 65.48  ? 88  GLU A O   1 
ATOM   604  C CB  . GLU A 1 88  ? -2.224  39.194 0.730   1.00 66.77  ? 88  GLU A CB  1 
ATOM   605  C CG  . GLU A 1 88  ? -3.294  39.998 1.460   1.00 69.95  ? 88  GLU A CG  1 
ATOM   606  C CD  . GLU A 1 88  ? -2.756  40.831 2.609   1.00 72.95  ? 88  GLU A CD  1 
ATOM   607  O OE1 . GLU A 1 88  ? -1.743  40.439 3.224   1.00 77.43  ? 88  GLU A OE1 1 
ATOM   608  O OE2 . GLU A 1 88  ? -3.359  41.884 2.904   1.00 74.05  ? 88  GLU A OE2 1 
ATOM   609  N N   . ASP A 1 89  ? -4.972  37.794 -0.831  1.00 61.34  ? 89  ASP A N   1 
ATOM   610  C CA  . ASP A 1 89  ? -5.966  37.899 -1.895  1.00 64.27  ? 89  ASP A CA  1 
ATOM   611  C C   . ASP A 1 89  ? -7.219  38.608 -1.390  1.00 63.83  ? 89  ASP A C   1 
ATOM   612  O O   . ASP A 1 89  ? -7.713  38.310 -0.305  1.00 57.87  ? 89  ASP A O   1 
ATOM   613  C CB  . ASP A 1 89  ? -6.320  36.501 -2.414  1.00 65.92  ? 89  ASP A CB  1 
ATOM   614  C CG  . ASP A 1 89  ? -7.150  36.534 -3.688  1.00 68.61  ? 89  ASP A CG  1 
ATOM   615  O OD1 . ASP A 1 89  ? -6.965  37.458 -4.509  1.00 73.56  ? 89  ASP A OD1 1 
ATOM   616  O OD2 . ASP A 1 89  ? -7.983  35.624 -3.875  1.00 64.23  ? 89  ASP A OD2 1 
ATOM   617  N N   . SER A 1 90  ? -7.719  39.554 -2.181  1.00 68.14  ? 90  SER A N   1 
ATOM   618  C CA  . SER A 1 90  ? -8.926  40.306 -1.841  1.00 72.45  ? 90  SER A CA  1 
ATOM   619  C C   . SER A 1 90  ? -10.165 39.802 -2.588  1.00 75.85  ? 90  SER A C   1 
ATOM   620  O O   . SER A 1 90  ? -11.273 40.275 -2.334  1.00 76.00  ? 90  SER A O   1 
ATOM   621  C CB  . SER A 1 90  ? -8.715  41.792 -2.133  1.00 77.66  ? 90  SER A CB  1 
ATOM   622  O OG  . SER A 1 90  ? -7.626  42.304 -1.383  1.00 85.17  ? 90  SER A OG  1 
ATOM   623  N N   . VAL A 1 91  ? -9.974  38.847 -3.501  1.00 72.68  ? 91  VAL A N   1 
ATOM   624  C CA  . VAL A 1 91  ? -11.080 38.236 -4.245  1.00 66.32  ? 91  VAL A CA  1 
ATOM   625  C C   . VAL A 1 91  ? -11.877 37.313 -3.329  1.00 63.56  ? 91  VAL A C   1 
ATOM   626  O O   . VAL A 1 91  ? -13.099 37.430 -3.223  1.00 61.87  ? 91  VAL A O   1 
ATOM   627  C CB  . VAL A 1 91  ? -10.570 37.416 -5.450  1.00 69.97  ? 91  VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 91  ? -11.730 36.750 -6.185  1.00 69.67  ? 91  VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 91  ? -9.766  38.302 -6.390  1.00 69.93  ? 91  VAL A CG2 1 
ATOM   630  N N   . ILE A 1 92  ? -11.171 36.389 -2.684  1.00 57.74  ? 92  ILE A N   1 
ATOM   631  C CA  . ILE A 1 92  ? -11.778 35.485 -1.707  1.00 51.75  ? 92  ILE A CA  1 
ATOM   632  C C   . ILE A 1 92  ? -12.118 36.227 -0.418  1.00 48.67  ? 92  ILE A C   1 
ATOM   633  O O   . ILE A 1 92  ? -11.543 37.275 -0.121  1.00 51.64  ? 92  ILE A O   1 
ATOM   634  C CB  . ILE A 1 92  ? -10.856 34.288 -1.378  1.00 48.38  ? 92  ILE A CB  1 
ATOM   635  C CG1 . ILE A 1 92  ? -9.534  34.764 -0.756  1.00 47.25  ? 92  ILE A CG1 1 
ATOM   636  C CG2 . ILE A 1 92  ? -10.603 33.463 -2.632  1.00 49.49  ? 92  ILE A CG2 1 
ATOM   637  C CD1 . ILE A 1 92  ? -8.639  33.646 -0.267  1.00 46.84  ? 92  ILE A CD1 1 
ATOM   638  N N   . SER A 1 93  ? -13.058 35.672 0.340   1.00 46.78  ? 93  SER A N   1 
ATOM   639  C CA  . SER A 1 93  ? -13.459 36.240 1.626   1.00 45.99  ? 93  SER A CA  1 
ATOM   640  C C   . SER A 1 93  ? -13.839 35.125 2.591   1.00 44.39  ? 93  SER A C   1 
ATOM   641  O O   . SER A 1 93  ? -14.134 34.007 2.171   1.00 45.58  ? 93  SER A O   1 
ATOM   642  C CB  . SER A 1 93  ? -14.641 37.191 1.441   1.00 46.03  ? 93  SER A CB  1 
ATOM   643  O OG  . SER A 1 93  ? -15.052 37.741 2.681   1.00 48.12  ? 93  SER A OG  1 
ATOM   644  N N   . LEU A 1 94  ? -13.829 35.439 3.883   1.00 46.01  ? 94  LEU A N   1 
ATOM   645  C CA  . LEU A 1 94  ? -14.235 34.493 4.919   1.00 46.50  ? 94  LEU A CA  1 
ATOM   646  C C   . LEU A 1 94  ? -15.620 34.836 5.470   1.00 52.27  ? 94  LEU A C   1 
ATOM   647  O O   . LEU A 1 94  ? -16.047 34.271 6.483   1.00 52.75  ? 94  LEU A O   1 
ATOM   648  C CB  . LEU A 1 94  ? -13.206 34.475 6.051   1.00 44.21  ? 94  LEU A CB  1 
ATOM   649  C CG  . LEU A 1 94  ? -11.741 34.290 5.643   1.00 41.95  ? 94  LEU A CG  1 
ATOM   650  C CD1 . LEU A 1 94  ? -10.862 34.257 6.880   1.00 41.25  ? 94  LEU A CD1 1 
ATOM   651  C CD2 . LEU A 1 94  ? -11.545 33.028 4.822   1.00 41.73  ? 94  LEU A CD2 1 
ATOM   652  N N   . SER A 1 95  ? -16.313 35.758 4.799   1.00 57.76  ? 95  SER A N   1 
ATOM   653  C CA  . SER A 1 95  ? -17.672 36.159 5.170   1.00 61.32  ? 95  SER A CA  1 
ATOM   654  C C   . SER A 1 95  ? -18.436 36.649 3.941   1.00 67.26  ? 95  SER A C   1 
ATOM   655  O O   . SER A 1 95  ? -17.832 37.096 2.961   1.00 65.40  ? 95  SER A O   1 
ATOM   656  C CB  . SER A 1 95  ? -17.637 37.260 6.235   1.00 59.17  ? 95  SER A CB  1 
ATOM   657  O OG  . SER A 1 95  ? -16.971 38.417 5.758   1.00 56.35  ? 95  SER A OG  1 
ATOM   658  N N   . GLY A 1 96  ? -19.762 36.558 4.001   1.00 73.08  ? 96  GLY A N   1 
ATOM   659  C CA  . GLY A 1 96  ? -20.630 36.993 2.906   1.00 78.33  ? 96  GLY A CA  1 
ATOM   660  C C   . GLY A 1 96  ? -21.203 35.830 2.121   1.00 82.60  ? 96  GLY A C   1 
ATOM   661  O O   . GLY A 1 96  ? -21.153 34.683 2.569   1.00 78.09  ? 96  GLY A O   1 
ATOM   662  N N   . ASP A 1 97  ? -21.750 36.132 0.946   1.00 89.59  ? 97  ASP A N   1 
ATOM   663  C CA  . ASP A 1 97  ? -22.380 35.116 0.095   1.00 92.85  ? 97  ASP A CA  1 
ATOM   664  C C   . ASP A 1 97  ? -21.359 34.183 -0.570  1.00 87.48  ? 97  ASP A C   1 
ATOM   665  O O   . ASP A 1 97  ? -21.651 33.006 -0.792  1.00 81.50  ? 97  ASP A O   1 
ATOM   666  C CB  . ASP A 1 97  ? -23.289 35.766 -0.962  1.00 99.62  ? 97  ASP A CB  1 
ATOM   667  C CG  . ASP A 1 97  ? -22.532 36.670 -1.930  1.00 106.28 ? 97  ASP A CG  1 
ATOM   668  O OD1 . ASP A 1 97  ? -21.442 37.166 -1.571  1.00 109.14 ? 97  ASP A OD1 1 
ATOM   669  O OD2 . ASP A 1 97  ? -23.040 36.891 -3.050  1.00 119.08 ? 97  ASP A OD2 1 
ATOM   670  N N   . HIS A 1 98  ? -20.175 34.710 -0.886  1.00 87.97  ? 98  HIS A N   1 
ATOM   671  C CA  . HIS A 1 98  ? -19.082 33.907 -1.450  1.00 87.59  ? 98  HIS A CA  1 
ATOM   672  C C   . HIS A 1 98  ? -17.957 33.693 -0.428  1.00 77.83  ? 98  HIS A C   1 
ATOM   673  O O   . HIS A 1 98  ? -16.769 33.810 -0.747  1.00 73.34  ? 98  HIS A O   1 
ATOM   674  C CB  . HIS A 1 98  ? -18.540 34.555 -2.732  1.00 91.99  ? 98  HIS A CB  1 
ATOM   675  C CG  . HIS A 1 98  ? -19.481 34.474 -3.893  1.00 95.42  ? 98  HIS A CG  1 
ATOM   676  N ND1 . HIS A 1 98  ? -20.139 35.575 -4.397  0.48 94.78  ? 98  HIS A ND1 1 
ATOM   677  C CD2 . HIS A 1 98  ? -19.876 33.421 -4.648  1.00 96.98  ? 98  HIS A CD2 1 
ATOM   678  C CE1 . HIS A 1 98  ? -20.897 35.204 -5.414  1.00 96.01  ? 98  HIS A CE1 1 
ATOM   679  N NE2 . HIS A 1 98  ? -20.757 33.902 -5.586  1.00 99.79  ? 98  HIS A NE2 1 
ATOM   680  N N   . SER A 1 99  ? -18.344 33.375 0.804   1.00 65.88  ? 99  SER A N   1 
ATOM   681  C CA  . SER A 1 99  ? -17.392 33.002 1.842   1.00 56.62  ? 99  SER A CA  1 
ATOM   682  C C   . SER A 1 99  ? -16.803 31.644 1.484   1.00 49.27  ? 99  SER A C   1 
ATOM   683  O O   . SER A 1 99  ? -17.545 30.708 1.185   1.00 50.16  ? 99  SER A O   1 
ATOM   684  C CB  . SER A 1 99  ? -18.088 32.925 3.204   1.00 57.82  ? 99  SER A CB  1 
ATOM   685  O OG  . SER A 1 99  ? -17.206 32.467 4.215   1.00 55.08  ? 99  SER A OG  1 
ATOM   686  N N   . ILE A 1 100 ? -15.477 31.534 1.508   1.00 42.13  ? 100 ILE A N   1 
ATOM   687  C CA  . ILE A 1 100 ? -14.821 30.260 1.204   1.00 39.02  ? 100 ILE A CA  1 
ATOM   688  C C   . ILE A 1 100 ? -14.898 29.265 2.360   1.00 37.95  ? 100 ILE A C   1 
ATOM   689  O O   . ILE A 1 100 ? -14.457 28.125 2.221   1.00 38.22  ? 100 ILE A O   1 
ATOM   690  C CB  . ILE A 1 100 ? -13.347 30.436 0.770   1.00 38.66  ? 100 ILE A CB  1 
ATOM   691  C CG1 . ILE A 1 100 ? -12.482 30.994 1.911   1.00 36.73  ? 100 ILE A CG1 1 
ATOM   692  C CG2 . ILE A 1 100 ? -13.272 31.315 -0.469  1.00 40.38  ? 100 ILE A CG2 1 
ATOM   693  C CD1 . ILE A 1 100 ? -11.002 30.990 1.602   1.00 36.24  ? 100 ILE A CD1 1 
ATOM   694  N N   . ILE A 1 101 ? -15.454 29.695 3.492   1.00 38.62  ? 101 ILE A N   1 
ATOM   695  C CA  . ILE A 1 101 ? -15.653 28.814 4.640   1.00 39.45  ? 101 ILE A CA  1 
ATOM   696  C C   . ILE A 1 101 ? -16.596 27.683 4.257   1.00 38.85  ? 101 ILE A C   1 
ATOM   697  O O   . ILE A 1 101 ? -17.661 27.921 3.686   1.00 44.13  ? 101 ILE A O   1 
ATOM   698  C CB  . ILE A 1 101 ? -16.256 29.565 5.845   1.00 41.75  ? 101 ILE A CB  1 
ATOM   699  C CG1 . ILE A 1 101 ? -15.311 30.672 6.336   1.00 41.62  ? 101 ILE A CG1 1 
ATOM   700  C CG2 . ILE A 1 101 ? -16.582 28.596 6.978   1.00 41.28  ? 101 ILE A CG2 1 
ATOM   701  C CD1 . ILE A 1 101 ? -13.987 30.183 6.886   1.00 41.62  ? 101 ILE A CD1 1 
ATOM   702  N N   . GLY A 1 102 ? -16.195 26.455 4.572   1.00 37.91  ? 102 GLY A N   1 
ATOM   703  C CA  . GLY A 1 102 ? -16.984 25.276 4.236   1.00 37.74  ? 102 GLY A CA  1 
ATOM   704  C C   . GLY A 1 102 ? -16.724 24.740 2.838   1.00 36.80  ? 102 GLY A C   1 
ATOM   705  O O   . GLY A 1 102 ? -17.177 23.647 2.502   1.00 36.02  ? 102 GLY A O   1 
ATOM   706  N N   . ARG A 1 103 ? -16.003 25.499 2.017   1.00 36.10  ? 103 ARG A N   1 
ATOM   707  C CA  . ARG A 1 103 ? -15.653 25.046 0.676   1.00 35.92  ? 103 ARG A CA  1 
ATOM   708  C C   . ARG A 1 103 ? -14.317 24.303 0.699   1.00 32.91  ? 103 ARG A C   1 
ATOM   709  O O   . ARG A 1 103 ? -13.553 24.400 1.663   1.00 32.66  ? 103 ARG A O   1 
ATOM   710  C CB  . ARG A 1 103 ? -15.654 26.220 -0.316  1.00 39.75  ? 103 ARG A CB  1 
ATOM   711  C CG  . ARG A 1 103 ? -17.062 26.589 -0.774  1.00 43.03  ? 103 ARG A CG  1 
ATOM   712  C CD  . ARG A 1 103 ? -17.158 27.989 -1.352  1.00 49.39  ? 103 ARG A CD  1 
ATOM   713  N NE  . ARG A 1 103 ? -16.274 28.192 -2.499  1.00 57.36  ? 103 ARG A NE  1 
ATOM   714  C CZ  . ARG A 1 103 ? -16.174 29.331 -3.185  1.00 64.82  ? 103 ARG A CZ  1 
ATOM   715  N NH1 . ARG A 1 103 ? -16.908 30.391 -2.851  1.00 65.21  ? 103 ARG A NH1 1 
ATOM   716  N NH2 . ARG A 1 103 ? -15.334 29.412 -4.214  1.00 64.72  ? 103 ARG A NH2 1 
ATOM   717  N N   . THR A 1 104 ? -14.059 23.549 -0.363  1.00 30.54  ? 104 THR A N   1 
ATOM   718  C CA  . THR A 1 104 ? -12.910 22.656 -0.427  1.00 29.01  ? 104 THR A CA  1 
ATOM   719  C C   . THR A 1 104 ? -11.720 23.300 -1.133  1.00 30.43  ? 104 THR A C   1 
ATOM   720  O O   . THR A 1 104 ? -11.839 23.787 -2.260  1.00 31.15  ? 104 THR A O   1 
ATOM   721  C CB  . THR A 1 104 ? -13.288 21.348 -1.147  1.00 28.00  ? 104 THR A CB  1 
ATOM   722  O OG1 . THR A 1 104 ? -14.314 20.684 -0.401  1.00 27.75  ? 104 THR A OG1 1 
ATOM   723  C CG2 . THR A 1 104 ? -12.088 20.420 -1.277  1.00 27.26  ? 104 THR A CG2 1 
ATOM   724  N N   . LEU A 1 105 ? -10.576 23.295 -0.451  1.00 30.26  ? 105 LEU A N   1 
ATOM   725  C CA  . LEU A 1 105 ? -9.308  23.713 -1.037  1.00 29.99  ? 105 LEU A CA  1 
ATOM   726  C C   . LEU A 1 105 ? -8.688  22.514 -1.729  1.00 29.44  ? 105 LEU A C   1 
ATOM   727  O O   . LEU A 1 105 ? -8.647  21.423 -1.152  1.00 28.83  ? 105 LEU A O   1 
ATOM   728  C CB  . LEU A 1 105 ? -8.359  24.218 0.055   1.00 30.55  ? 105 LEU A CB  1 
ATOM   729  C CG  . LEU A 1 105 ? -7.007  24.794 -0.386  1.00 31.11  ? 105 LEU A CG  1 
ATOM   730  C CD1 . LEU A 1 105 ? -7.169  26.054 -1.222  1.00 32.11  ? 105 LEU A CD1 1 
ATOM   731  C CD2 . LEU A 1 105 ? -6.150  25.086 0.834   1.00 32.69  ? 105 LEU A CD2 1 
ATOM   732  N N   . VAL A 1 106 ? -8.207  22.711 -2.956  1.00 29.22  ? 106 VAL A N   1 
ATOM   733  C CA  . VAL A 1 106 ? -7.569  21.635 -3.717  1.00 29.15  ? 106 VAL A CA  1 
ATOM   734  C C   . VAL A 1 106 ? -6.206  22.064 -4.251  1.00 29.18  ? 106 VAL A C   1 
ATOM   735  O O   . VAL A 1 106 ? -5.973  23.249 -4.487  1.00 29.77  ? 106 VAL A O   1 
ATOM   736  C CB  . VAL A 1 106 ? -8.460  21.141 -4.888  1.00 29.20  ? 106 VAL A CB  1 
ATOM   737  C CG1 . VAL A 1 106 ? -9.795  20.629 -4.364  1.00 29.77  ? 106 VAL A CG1 1 
ATOM   738  C CG2 . VAL A 1 106 ? -8.699  22.233 -5.923  1.00 30.54  ? 106 VAL A CG2 1 
ATOM   739  N N   . VAL A 1 107 ? -5.311  21.089 -4.415  1.00 30.29  ? 107 VAL A N   1 
ATOM   740  C CA  . VAL A 1 107 ? -4.037  21.295 -5.109  1.00 30.87  ? 107 VAL A CA  1 
ATOM   741  C C   . VAL A 1 107 ? -3.777  20.132 -6.068  1.00 31.93  ? 107 VAL A C   1 
ATOM   742  O O   . VAL A 1 107 ? -3.927  18.964 -5.700  1.00 33.02  ? 107 VAL A O   1 
ATOM   743  C CB  . VAL A 1 107 ? -2.845  21.484 -4.132  1.00 30.07  ? 107 VAL A CB  1 
ATOM   744  C CG1 . VAL A 1 107 ? -2.693  20.303 -3.188  1.00 30.76  ? 107 VAL A CG1 1 
ATOM   745  C CG2 . VAL A 1 107 ? -1.544  21.711 -4.890  1.00 30.45  ? 107 VAL A CG2 1 
ATOM   746  N N   . HIS A 1 108 ? -3.406  20.462 -7.303  1.00 32.89  ? 108 HIS A N   1 
ATOM   747  C CA  . HIS A 1 108 ? -3.112  19.452 -8.314  1.00 33.89  ? 108 HIS A CA  1 
ATOM   748  C C   . HIS A 1 108 ? -1.803  18.756 -8.003  1.00 34.57  ? 108 HIS A C   1 
ATOM   749  O O   . HIS A 1 108 ? -0.763  19.404 -7.904  1.00 35.09  ? 108 HIS A O   1 
ATOM   750  C CB  . HIS A 1 108 ? -3.027  20.078 -9.706  1.00 34.77  ? 108 HIS A CB  1 
ATOM   751  C CG  . HIS A 1 108 ? -4.360  20.366 -10.317 1.00 37.23  ? 108 HIS A CG  1 
ATOM   752  N ND1 . HIS A 1 108 ? -4.827  19.697 -11.427 1.00 38.17  ? 108 HIS A ND1 1 
ATOM   753  C CD2 . HIS A 1 108 ? -5.332  21.241 -9.966  1.00 36.81  ? 108 HIS A CD2 1 
ATOM   754  C CE1 . HIS A 1 108 ? -6.027  20.152 -11.739 1.00 38.89  ? 108 HIS A CE1 1 
ATOM   755  N NE2 . HIS A 1 108 ? -6.356  21.090 -10.869 1.00 37.80  ? 108 HIS A NE2 1 
ATOM   756  N N   . GLU A 1 109 ? -1.863  17.435 -7.861  1.00 34.66  ? 109 GLU A N   1 
ATOM   757  C CA  . GLU A 1 109 ? -0.677  16.632 -7.580  1.00 34.92  ? 109 GLU A CA  1 
ATOM   758  C C   . GLU A 1 109 ? 0.226   16.476 -8.805  1.00 36.69  ? 109 GLU A C   1 
ATOM   759  O O   . GLU A 1 109 ? 1.415   16.222 -8.660  1.00 36.62  ? 109 GLU A O   1 
ATOM   760  C CB  . GLU A 1 109 ? -1.083  15.259 -7.042  1.00 34.67  ? 109 GLU A CB  1 
ATOM   761  C CG  . GLU A 1 109 ? -1.847  15.334 -5.729  1.00 35.17  ? 109 GLU A CG  1 
ATOM   762  C CD  . GLU A 1 109 ? -2.111  13.975 -5.118  1.00 36.27  ? 109 GLU A CD  1 
ATOM   763  O OE1 . GLU A 1 109 ? -2.212  12.983 -5.871  1.00 38.67  ? 109 GLU A OE1 1 
ATOM   764  O OE2 . GLU A 1 109 ? -2.224  13.904 -3.878  1.00 36.48  ? 109 GLU A OE2 1 
ATOM   765  N N   . LYS A 1 110 ? -0.332  16.623 -10.006 1.00 39.80  ? 110 LYS A N   1 
ATOM   766  C CA  . LYS A 1 110 ? 0.478   16.590 -11.226 1.00 42.78  ? 110 LYS A CA  1 
ATOM   767  C C   . LYS A 1 110 ? 1.153   17.944 -11.426 1.00 42.43  ? 110 LYS A C   1 
ATOM   768  O O   . LYS A 1 110 ? 0.496   18.984 -11.360 1.00 39.72  ? 110 LYS A O   1 
ATOM   769  C CB  . LYS A 1 110 ? -0.373  16.227 -12.444 1.00 45.73  ? 110 LYS A CB  1 
ATOM   770  C CG  . LYS A 1 110 ? 0.438   16.002 -13.713 1.00 49.86  ? 110 LYS A CG  1 
ATOM   771  C CD  . LYS A 1 110 ? -0.144  14.880 -14.557 1.00 53.84  ? 110 LYS A CD  1 
ATOM   772  C CE  . LYS A 1 110 ? 0.651   14.659 -15.834 1.00 56.84  ? 110 LYS A CE  1 
ATOM   773  N NZ  . LYS A 1 110 ? 0.307   15.653 -16.887 1.00 58.36  ? 110 LYS A NZ  1 
ATOM   774  N N   . ALA A 1 111 ? 2.461   17.922 -11.672 1.00 44.39  ? 111 ALA A N   1 
ATOM   775  C CA  . ALA A 1 111 ? 3.256   19.149 -11.738 1.00 46.64  ? 111 ALA A CA  1 
ATOM   776  C C   . ALA A 1 111 ? 2.841   20.063 -12.888 1.00 51.01  ? 111 ALA A C   1 
ATOM   777  O O   . ALA A 1 111 ? 2.725   19.629 -14.035 1.00 50.72  ? 111 ALA A O   1 
ATOM   778  C CB  . ALA A 1 111 ? 4.739   18.822 -11.844 1.00 47.22  ? 111 ALA A CB  1 
ATOM   779  N N   . GLY A 1 112 ? 2.591   21.324 -12.541 1.00 59.71  ? 112 GLY A N   1 
ATOM   780  C CA  . GLY A 1 112 ? 2.420   22.423 -13.489 1.00 67.79  ? 112 GLY A CA  1 
ATOM   781  C C   . GLY A 1 112 ? 1.620   22.074 -14.729 1.00 80.82  ? 112 GLY A C   1 
ATOM   782  O O   . GLY A 1 112 ? 0.486   21.613 -14.605 1.00 80.37  ? 112 GLY A O   1 
ATOM   783  N N   . ALA A 1 113 ? 2.181   22.279 -15.925 1.00 95.05  ? 113 ALA A N   1 
ATOM   784  C CA  . ALA A 1 113 ? 3.533   22.825 -16.127 1.00 99.51  ? 113 ALA A CA  1 
ATOM   785  C C   . ALA A 1 113 ? 3.674   23.448 -17.512 1.00 98.49  ? 113 ALA A C   1 
ATOM   786  O O   . ALA A 1 113 ? 2.968   23.083 -18.450 1.00 100.10 ? 113 ALA A O   1 
ATOM   787  C CB  . ALA A 1 113 ? 4.583   21.736 -15.938 1.00 104.33 ? 113 ALA A CB  1 
ATOM   788  O OXT . ALA A 1 113 ? 4.504   24.332 -17.724 1.00 88.84  ? 113 ALA A OXT 1 
ATOM   789  N N   . ALA B 1 1   ? 5.774   9.965  39.533  1.00 86.49  ? 1   ALA B N   1 
ATOM   790  C CA  . ALA B 1 1   ? 4.527   10.652 39.075  1.00 86.90  ? 1   ALA B CA  1 
ATOM   791  C C   . ALA B 1 1   ? 4.825   12.032 38.482  1.00 78.94  ? 1   ALA B C   1 
ATOM   792  O O   . ALA B 1 1   ? 4.182   13.023 38.834  1.00 87.61  ? 1   ALA B O   1 
ATOM   793  C CB  . ALA B 1 1   ? 3.533   10.768 40.227  1.00 89.70  ? 1   ALA B CB  1 
ATOM   794  N N   . GLY B 1 2   ? 5.801   12.087 37.577  1.00 70.67  ? 2   GLY B N   1 
ATOM   795  C CA  . GLY B 1 2   ? 6.170   13.334 36.908  1.00 64.98  ? 2   GLY B CA  1 
ATOM   796  C C   . GLY B 1 2   ? 5.188   13.687 35.808  1.00 57.78  ? 2   GLY B C   1 
ATOM   797  O O   . GLY B 1 2   ? 4.475   12.819 35.300  1.00 53.43  ? 2   GLY B O   1 
ATOM   798  N N   . SER B 1 3   ? 5.156   14.963 35.431  1.00 53.17  ? 3   SER B N   1 
ATOM   799  C CA  . SER B 1 3   ? 4.184   15.456 34.452  1.00 53.52  ? 3   SER B CA  1 
ATOM   800  C C   . SER B 1 3   ? 4.353   14.806 33.076  1.00 48.92  ? 3   SER B C   1 
ATOM   801  O O   . SER B 1 3   ? 5.463   14.729 32.546  1.00 40.20  ? 3   SER B O   1 
ATOM   802  C CB  . SER B 1 3   ? 4.284   16.981 34.309  1.00 56.40  ? 3   SER B CB  1 
ATOM   803  O OG  . SER B 1 3   ? 3.854   17.646 35.484  1.00 59.83  ? 3   SER B OG  1 
ATOM   804  N N   . ARG B 1 4   ? 3.242   14.334 32.514  1.00 50.36  ? 4   ARG B N   1 
ATOM   805  C CA  . ARG B 1 4   ? 3.208   13.859 31.136  1.00 50.92  ? 4   ARG B CA  1 
ATOM   806  C C   . ARG B 1 4   ? 2.845   15.036 30.230  1.00 49.08  ? 4   ARG B C   1 
ATOM   807  O O   . ARG B 1 4   ? 1.753   15.596 30.340  1.00 52.31  ? 4   ARG B O   1 
ATOM   808  C CB  . ARG B 1 4   ? 2.191   12.724 30.974  1.00 56.72  ? 4   ARG B CB  1 
ATOM   809  C CG  . ARG B 1 4   ? 2.387   11.565 31.943  1.00 61.34  ? 4   ARG B CG  1 
ATOM   810  C CD  . ARG B 1 4   ? 1.595   10.335 31.520  1.00 66.47  ? 4   ARG B CD  1 
ATOM   811  N NE  . ARG B 1 4   ? 2.223   9.625  30.401  1.00 70.83  ? 4   ARG B NE  1 
ATOM   812  C CZ  . ARG B 1 4   ? 3.048   8.579  30.509  1.00 71.66  ? 4   ARG B CZ  1 
ATOM   813  N NH1 . ARG B 1 4   ? 3.377   8.073  31.697  1.00 70.76  ? 4   ARG B NH1 1 
ATOM   814  N NH2 . ARG B 1 4   ? 3.550   8.026  29.407  1.00 72.39  ? 4   ARG B NH2 1 
ATOM   815  N N   . LEU B 1 5   ? 3.771   15.415 29.350  1.00 44.61  ? 5   LEU B N   1 
ATOM   816  C CA  . LEU B 1 5   ? 3.597   16.575 28.478  1.00 40.52  ? 5   LEU B CA  1 
ATOM   817  C C   . LEU B 1 5   ? 3.391   16.158 27.028  1.00 35.03  ? 5   LEU B C   1 
ATOM   818  O O   . LEU B 1 5   ? 3.952   15.162 26.571  1.00 38.49  ? 5   LEU B O   1 
ATOM   819  C CB  . LEU B 1 5   ? 4.835   17.476 28.528  1.00 42.30  ? 5   LEU B CB  1 
ATOM   820  C CG  . LEU B 1 5   ? 5.358   17.993 29.870  1.00 44.22  ? 5   LEU B CG  1 
ATOM   821  C CD1 . LEU B 1 5   ? 6.753   18.570 29.674  1.00 45.15  ? 5   LEU B CD1 1 
ATOM   822  C CD2 . LEU B 1 5   ? 4.422   19.031 30.468  1.00 46.16  ? 5   LEU B CD2 1 
ATOM   823  N N   . ALA B 1 6   ? 2.581   16.931 26.312  1.00 30.17  ? 6   ALA B N   1 
ATOM   824  C CA  . ALA B 1 6   ? 2.597   16.930 24.857  1.00 29.80  ? 6   ALA B CA  1 
ATOM   825  C C   . ALA B 1 6   ? 3.387   18.167 24.455  1.00 30.14  ? 6   ALA B C   1 
ATOM   826  O O   . ALA B 1 6   ? 3.253   19.216 25.088  1.00 30.16  ? 6   ALA B O   1 
ATOM   827  C CB  . ALA B 1 6   ? 1.186   16.990 24.295  1.00 30.05  ? 6   ALA B CB  1 
ATOM   828  N N   . SER B 1 7   ? 4.217   18.047 23.421  1.00 28.96  ? 7   SER B N   1 
ATOM   829  C CA  . SER B 1 7   ? 5.075   19.157 23.017  1.00 26.22  ? 7   SER B CA  1 
ATOM   830  C C   . SER B 1 7   ? 5.429   19.175 21.537  1.00 24.51  ? 7   SER B C   1 
ATOM   831  O O   . SER B 1 7   ? 5.227   18.204 20.805  1.00 22.97  ? 7   SER B O   1 
ATOM   832  C CB  . SER B 1 7   ? 6.364   19.143 23.840  1.00 26.36  ? 7   SER B CB  1 
ATOM   833  O OG  . SER B 1 7   ? 7.079   17.940 23.631  1.00 27.47  ? 7   SER B OG  1 
ATOM   834  N N   . GLY B 1 8   ? 5.968   20.315 21.121  1.00 24.11  ? 8   GLY B N   1 
ATOM   835  C CA  . GLY B 1 8   ? 6.468   20.506 19.773  1.00 21.66  ? 8   GLY B CA  1 
ATOM   836  C C   . GLY B 1 8   ? 7.329   21.747 19.740  1.00 21.00  ? 8   GLY B C   1 
ATOM   837  O O   . GLY B 1 8   ? 7.099   22.692 20.500  1.00 22.56  ? 8   GLY B O   1 
ATOM   838  N N   . VAL B 1 9   ? 8.322   21.744 18.859  1.00 20.83  ? 9   VAL B N   1 
ATOM   839  C CA  . VAL B 1 9   ? 9.226   22.881 18.714  1.00 21.31  ? 9   VAL B CA  1 
ATOM   840  C C   . VAL B 1 9   ? 8.537   23.970 17.892  1.00 22.16  ? 9   VAL B C   1 
ATOM   841  O O   . VAL B 1 9   ? 7.828   23.679 16.927  1.00 23.14  ? 9   VAL B O   1 
ATOM   842  C CB  . VAL B 1 9   ? 10.553  22.464 18.040  1.00 21.60  ? 9   VAL B CB  1 
ATOM   843  C CG1 . VAL B 1 9   ? 11.486  23.657 17.889  1.00 22.45  ? 9   VAL B CG1 1 
ATOM   844  C CG2 . VAL B 1 9   ? 11.237  21.362 18.844  1.00 21.61  ? 9   VAL B CG2 1 
ATOM   845  N N   . ILE B 1 10  ? 8.746   25.222 18.281  1.00 22.51  ? 10  ILE B N   1 
ATOM   846  C CA  . ILE B 1 10  ? 8.143   26.350 17.585  1.00 23.01  ? 10  ILE B CA  1 
ATOM   847  C C   . ILE B 1 10  ? 9.034   26.706 16.401  1.00 25.43  ? 10  ILE B C   1 
ATOM   848  O O   . ILE B 1 10  ? 10.139  27.219 16.583  1.00 27.11  ? 10  ILE B O   1 
ATOM   849  C CB  . ILE B 1 10  ? 7.979   27.565 18.519  1.00 22.76  ? 10  ILE B CB  1 
ATOM   850  C CG1 . ILE B 1 10  ? 7.143   27.177 19.744  1.00 21.63  ? 10  ILE B CG1 1 
ATOM   851  C CG2 . ILE B 1 10  ? 7.317   28.722 17.778  1.00 23.50  ? 10  ILE B CG2 1 
ATOM   852  C CD1 . ILE B 1 10  ? 7.282   28.127 20.909  1.00 21.65  ? 10  ILE B CD1 1 
ATOM   853  N N   . GLY B 1 11  ? 8.551   26.416 15.193  1.00 27.14  ? 11  GLY B N   1 
ATOM   854  C CA  . GLY B 1 11  ? 9.314   26.641 13.971  1.00 29.53  ? 11  GLY B CA  1 
ATOM   855  C C   . GLY B 1 11  ? 8.783   27.791 13.133  1.00 32.70  ? 11  GLY B C   1 
ATOM   856  O O   . GLY B 1 11  ? 7.612   28.148 13.237  1.00 33.33  ? 11  GLY B O   1 
ATOM   857  N N   . ILE B 1 12  ? 9.653   28.364 12.303  1.00 37.72  ? 12  ILE B N   1 
ATOM   858  C CA  . ILE B 1 12  ? 9.286   29.461 11.402  1.00 43.20  ? 12  ILE B CA  1 
ATOM   859  C C   . ILE B 1 12  ? 8.369   28.968 10.289  1.00 44.55  ? 12  ILE B C   1 
ATOM   860  O O   . ILE B 1 12  ? 8.631   27.932 9.677   1.00 41.48  ? 12  ILE B O   1 
ATOM   861  C CB  . ILE B 1 12  ? 10.543  30.136 10.777  1.00 49.10  ? 12  ILE B CB  1 
ATOM   862  C CG1 . ILE B 1 12  ? 11.009  31.316 11.635  1.00 53.00  ? 12  ILE B CG1 1 
ATOM   863  C CG2 . ILE B 1 12  ? 10.296  30.630 9.353   1.00 53.24  ? 12  ILE B CG2 1 
ATOM   864  C CD1 . ILE B 1 12  ? 12.260  31.021 12.422  1.00 56.70  ? 12  ILE B CD1 1 
ATOM   865  N N   . ALA B 1 13  ? 7.300   29.722 10.036  1.00 48.38  ? 13  ALA B N   1 
ATOM   866  C CA  . ALA B 1 13  ? 6.414   29.478 8.901   1.00 55.22  ? 13  ALA B CA  1 
ATOM   867  C C   . ALA B 1 13  ? 6.806   30.413 7.763   1.00 62.96  ? 13  ALA B C   1 
ATOM   868  O O   . ALA B 1 13  ? 7.167   29.964 6.672   1.00 63.48  ? 13  ALA B O   1 
ATOM   869  C CB  . ALA B 1 13  ? 4.966   29.702 9.300   1.00 55.08  ? 13  ALA B CB  1 
ATOM   870  N N   . GLN B 1 14  ? 6.736   31.714 8.028   1.00 67.63  ? 14  GLN B N   1 
ATOM   871  C CA  . GLN B 1 14  ? 7.194   32.718 7.081   1.00 76.27  ? 14  GLN B CA  1 
ATOM   872  C C   . GLN B 1 14  ? 8.233   33.599 7.782   1.00 75.73  ? 14  GLN B C   1 
ATOM   873  O O   . GLN B 1 14  ? 7.945   34.209 8.819   1.00 68.81  ? 14  GLN B O   1 
ATOM   874  C CB  . GLN B 1 14  ? 6.019   33.552 6.562   1.00 85.21  ? 14  GLN B CB  1 
ATOM   875  C CG  . GLN B 1 14  ? 6.070   33.804 5.062   1.00 95.31  ? 14  GLN B CG  1 
ATOM   876  C CD  . GLN B 1 14  ? 5.766   35.246 4.695   1.00 99.36  ? 14  GLN B CD  1 
ATOM   877  O OE1 . GLN B 1 14  ? 4.756   35.806 5.123   1.00 105.19 ? 14  GLN B OE1 1 
ATOM   878  N NE2 . GLN B 1 14  ? 6.641   35.854 3.895   1.00 102.13 ? 14  GLN B NE2 1 
ATOM   879  N N   . ALA B 1 15  ? 9.438   33.646 7.211   1.00 65.52  ? 15  ALA B N   1 
ATOM   880  C CA  . ALA B 1 15  ? 10.593  34.290 7.848   1.00 55.74  ? 15  ALA B CA  1 
ATOM   881  C C   . ALA B 1 15  ? 10.510  35.815 7.798   1.00 63.30  ? 15  ALA B C   1 
ATOM   882  O O   . ALA B 1 15  ? 10.443  36.405 6.714   1.00 68.43  ? 15  ALA B O   1 
ATOM   883  C CB  . ALA B 1 15  ? 11.887  33.816 7.195   1.00 53.20  ? 15  ALA B CB  1 
ATOM   884  N N   . GLY B 1 16  ? 10.523  36.440 8.977   1.00 64.33  ? 16  GLY B N   1 
ATOM   885  C CA  . GLY B 1 16  ? 10.530  37.903 9.108   1.00 60.85  ? 16  GLY B CA  1 
ATOM   886  C C   . GLY B 1 16  ? 9.616   38.645 8.144   1.00 64.15  ? 16  GLY B C   1 
ATOM   887  O O   . GLY B 1 16  ? 8.446   38.283 7.973   1.00 74.38  ? 16  GLY B O   1 
ATOM   888  N N   . ALA B 1 17  ? 10.167  39.692 7.526   1.00 67.46  ? 17  ALA B N   1 
ATOM   889  C CA  . ALA B 1 17  ? 9.474   40.513 6.522   1.00 67.31  ? 17  ALA B CA  1 
ATOM   890  C C   . ALA B 1 17  ? 8.249   41.271 7.056   1.00 74.88  ? 17  ALA B C   1 
ATOM   891  O O   . ALA B 1 17  ? 7.377   41.670 6.275   1.00 83.00  ? 17  ALA B O   1 
ATOM   892  C CB  . ALA B 1 17  ? 9.088   39.660 5.315   1.00 65.27  ? 17  ALA B CB  1 
ATOM   893  N N   . GLY B 1 18  ? 8.191   41.483 8.373   1.00 76.53  ? 18  GLY B N   1 
ATOM   894  C CA  . GLY B 1 18  ? 7.010   42.078 9.010   1.00 71.54  ? 18  GLY B CA  1 
ATOM   895  C C   . GLY B 1 18  ? 5.735   41.270 8.791   1.00 79.15  ? 18  GLY B C   1 
ATOM   896  O O   . GLY B 1 18  ? 4.625   41.792 8.918   1.00 84.96  ? 18  GLY B O   1 
ATOM   897  N N   . ALA B 1 19  ? 5.909   39.997 8.446   1.00 90.95  ? 19  ALA B N   1 
ATOM   898  C CA  . ALA B 1 19  ? 4.817   39.048 8.278   1.00 98.98  ? 19  ALA B CA  1 
ATOM   899  C C   . ALA B 1 19  ? 5.300   37.758 8.934   1.00 104.58 ? 19  ALA B C   1 
ATOM   900  O O   . ALA B 1 19  ? 5.365   36.699 8.301   1.00 106.81 ? 19  ALA B O   1 
ATOM   901  C CB  . ALA B 1 19  ? 4.509   38.840 6.802   1.00 107.03 ? 19  ALA B CB  1 
ATOM   902  N N   . THR B 1 20  ? 5.645   37.877 10.217  1.00 101.01 ? 20  THR B N   1 
ATOM   903  C CA  . THR B 1 20  ? 6.389   36.847 10.940  1.00 86.19  ? 20  THR B CA  1 
ATOM   904  C C   . THR B 1 20  ? 5.449   35.858 11.615  1.00 70.74  ? 20  THR B C   1 
ATOM   905  O O   . THR B 1 20  ? 4.655   36.229 12.483  1.00 60.65  ? 20  THR B O   1 
ATOM   906  C CB  . THR B 1 20  ? 7.308   37.465 12.018  1.00 91.80  ? 20  THR B CB  1 
ATOM   907  O OG1 . THR B 1 20  ? 7.438   38.879 11.805  1.00 89.59  ? 20  THR B OG1 1 
ATOM   908  C CG2 . THR B 1 20  ? 8.674   36.814 11.988  1.00 88.99  ? 20  THR B CG2 1 
ATOM   909  N N   . LYS B 1 21  ? 5.559   34.596 11.215  1.00 60.07  ? 21  LYS B N   1 
ATOM   910  C CA  . LYS B 1 21  ? 4.661   33.549 11.685  1.00 53.72  ? 21  LYS B CA  1 
ATOM   911  C C   . LYS B 1 21  ? 5.444   32.312 12.097  1.00 45.39  ? 21  LYS B C   1 
ATOM   912  O O   . LYS B 1 21  ? 6.451   31.968 11.477  1.00 43.28  ? 21  LYS B O   1 
ATOM   913  C CB  . LYS B 1 21  ? 3.667   33.189 10.579  1.00 57.55  ? 21  LYS B CB  1 
ATOM   914  C CG  . LYS B 1 21  ? 2.711   34.317 10.226  1.00 60.51  ? 21  LYS B CG  1 
ATOM   915  C CD  . LYS B 1 21  ? 2.271   34.273 8.772   1.00 62.27  ? 21  LYS B CD  1 
ATOM   916  C CE  . LYS B 1 21  ? 1.552   35.554 8.376   1.00 63.34  ? 21  LYS B CE  1 
ATOM   917  N NZ  . LYS B 1 21  ? 0.417   35.874 9.287   1.00 64.24  ? 21  LYS B NZ  1 
ATOM   918  N N   . ALA B 1 22  ? 4.975   31.649 13.148  1.00 38.48  ? 22  ALA B N   1 
ATOM   919  C CA  . ALA B 1 22  ? 5.579   30.408 13.606  1.00 33.60  ? 22  ALA B CA  1 
ATOM   920  C C   . ALA B 1 22  ? 4.502   29.377 13.917  1.00 29.23  ? 22  ALA B C   1 
ATOM   921  O O   . ALA B 1 22  ? 3.365   29.729 14.227  1.00 28.31  ? 22  ALA B O   1 
ATOM   922  C CB  . ALA B 1 22  ? 6.444   30.664 14.829  1.00 34.85  ? 22  ALA B CB  1 
ATOM   923  N N   . VAL B 1 23  ? 4.867   28.102 13.822  1.00 26.20  ? 23  VAL B N   1 
ATOM   924  C CA  . VAL B 1 23  ? 3.933   27.004 14.068  1.00 24.35  ? 23  VAL B CA  1 
ATOM   925  C C   . VAL B 1 23  ? 4.564   25.944 14.967  1.00 21.98  ? 23  VAL B C   1 
ATOM   926  O O   . VAL B 1 23  ? 5.727   25.576 14.777  1.00 20.97  ? 23  VAL B O   1 
ATOM   927  C CB  . VAL B 1 23  ? 3.495   26.319 12.756  1.00 25.55  ? 23  VAL B CB  1 
ATOM   928  C CG1 . VAL B 1 23  ? 2.361   25.336 13.024  1.00 25.50  ? 23  VAL B CG1 1 
ATOM   929  C CG2 . VAL B 1 23  ? 3.061   27.348 11.723  1.00 26.38  ? 23  VAL B CG2 1 
ATOM   930  N N   . ALA B 1 24  ? 3.786   25.458 15.937  1.00 20.62  ? 24  ALA B N   1 
ATOM   931  C CA  . ALA B 1 24  ? 4.194   24.337 16.795  1.00 19.17  ? 24  ALA B CA  1 
ATOM   932  C C   . ALA B 1 24  ? 3.235   23.170 16.609  1.00 19.25  ? 24  ALA B C   1 
ATOM   933  O O   . ALA B 1 24  ? 2.048   23.285 16.912  1.00 20.15  ? 24  ALA B O   1 
ATOM   934  C CB  . ALA B 1 24  ? 4.226   24.760 18.259  1.00 18.28  ? 24  ALA B CB  1 
ATOM   935  N N   . VAL B 1 25  ? 3.751   22.055 16.099  1.00 19.18  ? 25  VAL B N   1 
ATOM   936  C CA  . VAL B 1 25  ? 2.972   20.832 15.975  1.00 19.10  ? 25  VAL B CA  1 
ATOM   937  C C   . VAL B 1 25  ? 3.127   20.047 17.274  1.00 20.33  ? 25  VAL B C   1 
ATOM   938  O O   . VAL B 1 25  ? 4.189   19.476 17.537  1.00 22.06  ? 25  VAL B O   1 
ATOM   939  C CB  . VAL B 1 25  ? 3.434   19.970 14.776  1.00 18.77  ? 25  VAL B CB  1 
ATOM   940  C CG1 . VAL B 1 25  ? 2.587   18.710 14.661  1.00 18.81  ? 25  VAL B CG1 1 
ATOM   941  C CG2 . VAL B 1 25  ? 3.361   20.768 13.481  1.00 19.20  ? 25  VAL B CG2 1 
ATOM   942  N N   . LEU B 1 26  ? 2.066   20.028 18.083  1.00 20.58  ? 26  LEU B N   1 
ATOM   943  C CA  . LEU B 1 26  ? 2.082   19.353 19.381  1.00 21.01  ? 26  LEU B CA  1 
ATOM   944  C C   . LEU B 1 26  ? 1.791   17.862 19.264  1.00 24.67  ? 26  LEU B C   1 
ATOM   945  O O   . LEU B 1 26  ? 0.834   17.454 18.603  1.00 27.73  ? 26  LEU B O   1 
ATOM   946  C CB  . LEU B 1 26  ? 1.060   19.983 20.321  1.00 20.16  ? 26  LEU B CB  1 
ATOM   947  C CG  . LEU B 1 26  ? 1.332   21.432 20.706  1.00 20.36  ? 26  LEU B CG  1 
ATOM   948  C CD1 . LEU B 1 26  ? 0.138   21.991 21.457  1.00 21.01  ? 26  LEU B CD1 1 
ATOM   949  C CD2 . LEU B 1 26  ? 2.591   21.537 21.548  1.00 20.59  ? 26  LEU B CD2 1 
ATOM   950  N N   . LYS B 1 27  ? 2.623   17.064 19.928  1.00 27.68  ? 27  LYS B N   1 
ATOM   951  C CA  . LYS B 1 27  ? 2.504   15.615 19.933  1.00 32.12  ? 27  LYS B CA  1 
ATOM   952  C C   . LYS B 1 27  ? 2.724   15.124 21.360  1.00 33.56  ? 27  LYS B C   1 
ATOM   953  O O   . LYS B 1 27  ? 3.703   15.498 22.004  1.00 32.79  ? 27  LYS B O   1 
ATOM   954  C CB  . LYS B 1 27  ? 3.548   15.008 18.993  1.00 37.90  ? 27  LYS B CB  1 
ATOM   955  C CG  . LYS B 1 27  ? 3.491   13.492 18.852  1.00 44.75  ? 27  LYS B CG  1 
ATOM   956  C CD  . LYS B 1 27  ? 2.311   13.048 18.002  1.00 50.11  ? 27  LYS B CD  1 
ATOM   957  C CE  . LYS B 1 27  ? 2.247   11.533 17.884  1.00 54.50  ? 27  LYS B CE  1 
ATOM   958  N NZ  . LYS B 1 27  ? 1.766   10.891 19.139  1.00 58.10  ? 27  LYS B NZ  1 
ATOM   959  N N   . GLY B 1 28  ? 1.807   14.295 21.851  1.00 35.52  ? 28  GLY B N   1 
ATOM   960  C CA  . GLY B 1 28  ? 1.907   13.740 23.198  1.00 38.01  ? 28  GLY B CA  1 
ATOM   961  C C   . GLY B 1 28  ? 1.501   12.283 23.249  1.00 42.84  ? 28  GLY B C   1 
ATOM   962  O O   . GLY B 1 28  ? 1.561   11.574 22.245  1.00 43.52  ? 28  GLY B O   1 
ATOM   963  N N   . ASP B 1 29  ? 1.083   11.840 24.429  1.00 49.29  ? 29  ASP B N   1 
ATOM   964  C CA  . ASP B 1 29  ? 0.699   10.448 24.638  1.00 51.71  ? 29  ASP B CA  1 
ATOM   965  C C   . ASP B 1 29  ? -0.711  10.201 24.127  1.00 50.38  ? 29  ASP B C   1 
ATOM   966  O O   . ASP B 1 29  ? -1.588  11.050 24.268  1.00 52.48  ? 29  ASP B O   1 
ATOM   967  C CB  . ASP B 1 29  ? 0.797   10.087 26.121  1.00 55.75  ? 29  ASP B CB  1 
ATOM   968  C CG  . ASP B 1 29  ? 2.218   10.170 26.645  1.00 57.24  ? 29  ASP B CG  1 
ATOM   969  O OD1 . ASP B 1 29  ? 3.082   9.424  26.138  1.00 56.97  ? 29  ASP B OD1 1 
ATOM   970  O OD2 . ASP B 1 29  ? 2.474   10.980 27.561  1.00 62.08  ? 29  ASP B OD2 1 
ATOM   971  N N   . GLY B 1 30  ? -0.915  9.038  23.520  1.00 49.93  ? 30  GLY B N   1 
ATOM   972  C CA  . GLY B 1 30  ? -2.234  8.619  23.070  1.00 52.66  ? 30  GLY B CA  1 
ATOM   973  C C   . GLY B 1 30  ? -2.836  9.536  22.018  1.00 52.36  ? 30  GLY B C   1 
ATOM   974  O O   . GLY B 1 30  ? -2.237  9.741  20.960  1.00 60.39  ? 30  GLY B O   1 
ATOM   975  N N   . PRO B 1 31  ? -4.023  10.103 22.302  1.00 49.09  ? 31  PRO B N   1 
ATOM   976  C CA  . PRO B 1 31  ? -4.724  10.924 21.314  1.00 45.16  ? 31  PRO B CA  1 
ATOM   977  C C   . PRO B 1 31  ? -4.328  12.404 21.297  1.00 39.44  ? 31  PRO B C   1 
ATOM   978  O O   . PRO B 1 31  ? -4.876  13.163 20.497  1.00 41.19  ? 31  PRO B O   1 
ATOM   979  C CB  . PRO B 1 31  ? -6.182  10.791 21.751  1.00 46.60  ? 31  PRO B CB  1 
ATOM   980  C CG  . PRO B 1 31  ? -6.099  10.682 23.238  1.00 48.43  ? 31  PRO B CG  1 
ATOM   981  C CD  . PRO B 1 31  ? -4.802  9.980  23.550  1.00 48.38  ? 31  PRO B CD  1 
ATOM   982  N N   . VAL B 1 32  ? -3.393  12.811 22.157  1.00 35.71  ? 32  VAL B N   1 
ATOM   983  C CA  . VAL B 1 32  ? -3.071  14.232 22.312  1.00 30.70  ? 32  VAL B CA  1 
ATOM   984  C C   . VAL B 1 32  ? -2.280  14.749 21.111  1.00 31.98  ? 32  VAL B C   1 
ATOM   985  O O   . VAL B 1 32  ? -1.137  14.340 20.879  1.00 36.38  ? 32  VAL B O   1 
ATOM   986  C CB  . VAL B 1 32  ? -2.284  14.527 23.607  1.00 29.68  ? 32  VAL B CB  1 
ATOM   987  C CG1 . VAL B 1 32  ? -2.031  16.026 23.741  1.00 29.47  ? 32  VAL B CG1 1 
ATOM   988  C CG2 . VAL B 1 32  ? -3.039  14.018 24.829  1.00 29.85  ? 32  VAL B CG2 1 
ATOM   989  N N   . GLN B 1 33  ? -2.903  15.643 20.348  1.00 30.86  ? 33  GLN B N   1 
ATOM   990  C CA  . GLN B 1 33  ? -2.242  16.287 19.222  1.00 28.97  ? 33  GLN B CA  1 
ATOM   991  C C   . GLN B 1 33  ? -2.849  17.658 18.952  1.00 26.78  ? 33  GLN B C   1 
ATOM   992  O O   . GLN B 1 33  ? -4.010  17.905 19.277  1.00 30.08  ? 33  GLN B O   1 
ATOM   993  C CB  . GLN B 1 33  ? -2.319  15.410 17.967  1.00 32.19  ? 33  GLN B CB  1 
ATOM   994  C CG  . GLN B 1 33  ? -3.727  15.104 17.470  1.00 33.75  ? 33  GLN B CG  1 
ATOM   995  C CD  . GLN B 1 33  ? -3.733  14.615 16.032  0.30 35.39  ? 33  GLN B CD  1 
ATOM   996  O OE1 . GLN B 1 33  ? -3.232  15.294 15.137  0.48 36.06  ? 33  GLN B OE1 1 
ATOM   997  N NE2 . GLN B 1 33  ? -4.300  13.437 15.801  0.77 38.38  ? 33  GLN B NE2 1 
ATOM   998  N N   . GLY B 1 34  ? -2.057  18.545 18.360  1.00 22.82  ? 34  GLY B N   1 
ATOM   999  C CA  . GLY B 1 34  ? -2.521  19.897 18.066  1.00 20.86  ? 34  GLY B CA  1 
ATOM   1000 C C   . GLY B 1 34  ? -1.569  20.685 17.187  1.00 20.65  ? 34  GLY B C   1 
ATOM   1001 O O   . GLY B 1 34  ? -0.426  20.276 16.959  1.00 20.70  ? 34  GLY B O   1 
ATOM   1002 N N   . ILE B 1 35  ? -2.067  21.814 16.689  1.00 21.09  ? 35  ILE B N   1 
ATOM   1003 C CA  . ILE B 1 35  ? -1.288  22.749 15.884  1.00 21.25  ? 35  ILE B CA  1 
ATOM   1004 C C   . ILE B 1 35  ? -1.558  24.147 16.416  1.00 21.89  ? 35  ILE B C   1 
ATOM   1005 O O   . ILE B 1 35  ? -2.704  24.593 16.427  1.00 22.20  ? 35  ILE B O   1 
ATOM   1006 C CB  . ILE B 1 35  ? -1.695  22.708 14.395  1.00 22.58  ? 35  ILE B CB  1 
ATOM   1007 C CG1 . ILE B 1 35  ? -1.565  21.291 13.828  1.00 24.14  ? 35  ILE B CG1 1 
ATOM   1008 C CG2 . ILE B 1 35  ? -0.833  23.668 13.581  1.00 23.47  ? 35  ILE B CG2 1 
ATOM   1009 C CD1 . ILE B 1 35  ? -2.523  21.020 12.695  1.00 25.96  ? 35  ILE B CD1 1 
ATOM   1010 N N   . ILE B 1 36  ? -0.502  24.826 16.855  1.00 23.02  ? 36  ILE B N   1 
ATOM   1011 C CA  . ILE B 1 36  ? -0.611  26.153 17.459  1.00 23.31  ? 36  ILE B CA  1 
ATOM   1012 C C   . ILE B 1 36  ? 0.160   27.141 16.604  1.00 25.08  ? 36  ILE B C   1 
ATOM   1013 O O   . ILE B 1 36  ? 1.341   26.931 16.320  1.00 27.03  ? 36  ILE B O   1 
ATOM   1014 C CB  . ILE B 1 36  ? -0.026  26.169 18.887  1.00 22.70  ? 36  ILE B CB  1 
ATOM   1015 C CG1 . ILE B 1 36  ? -0.711  25.118 19.773  1.00 21.80  ? 36  ILE B CG1 1 
ATOM   1016 C CG2 . ILE B 1 36  ? -0.142  27.558 19.507  1.00 23.61  ? 36  ILE B CG2 1 
ATOM   1017 C CD1 . ILE B 1 36  ? -2.213  25.282 19.908  1.00 21.84  ? 36  ILE B CD1 1 
ATOM   1018 N N   . ASN B 1 37  ? -0.512  28.212 16.194  1.00 27.35  ? 37  ASN B N   1 
ATOM   1019 C CA  . ASN B 1 37  ? 0.094   29.228 15.346  1.00 29.03  ? 37  ASN B CA  1 
ATOM   1020 C C   . ASN B 1 37  ? 0.405   30.466 16.171  1.00 31.11  ? 37  ASN B C   1 
ATOM   1021 O O   . ASN B 1 37  ? -0.375  30.841 17.043  1.00 32.50  ? 37  ASN B O   1 
ATOM   1022 C CB  . ASN B 1 37  ? -0.845  29.589 14.198  1.00 29.74  ? 37  ASN B CB  1 
ATOM   1023 C CG  . ASN B 1 37  ? -1.211  28.388 13.342  1.00 30.02  ? 37  ASN B CG  1 
ATOM   1024 O OD1 . ASN B 1 37  ? -0.355  27.796 12.686  1.00 33.28  ? 37  ASN B OD1 1 
ATOM   1025 N ND2 . ASN B 1 37  ? -2.489  28.030 13.335  1.00 30.41  ? 37  ASN B ND2 1 
ATOM   1026 N N   . PHE B 1 38  ? 1.554   31.082 15.897  1.00 33.57  ? 38  PHE B N   1 
ATOM   1027 C CA  . PHE B 1 38  ? 1.995   32.295 16.588  1.00 35.54  ? 38  PHE B CA  1 
ATOM   1028 C C   . PHE B 1 38  ? 2.144   33.413 15.568  1.00 40.82  ? 38  PHE B C   1 
ATOM   1029 O O   . PHE B 1 38  ? 2.670   33.190 14.475  1.00 40.48  ? 38  PHE B O   1 
ATOM   1030 C CB  . PHE B 1 38  ? 3.344   32.073 17.283  1.00 34.38  ? 38  PHE B CB  1 
ATOM   1031 C CG  . PHE B 1 38  ? 3.307   31.038 18.370  1.00 31.68  ? 38  PHE B CG  1 
ATOM   1032 C CD1 . PHE B 1 38  ? 3.321   29.688 18.060  1.00 30.13  ? 38  PHE B CD1 1 
ATOM   1033 C CD2 . PHE B 1 38  ? 3.264   31.413 19.702  1.00 31.88  ? 38  PHE B CD2 1 
ATOM   1034 C CE1 . PHE B 1 38  ? 3.286   28.731 19.057  1.00 29.61  ? 38  PHE B CE1 1 
ATOM   1035 C CE2 . PHE B 1 38  ? 3.226   30.460 20.706  1.00 29.59  ? 38  PHE B CE2 1 
ATOM   1036 C CZ  . PHE B 1 38  ? 3.239   29.116 20.383  1.00 28.59  ? 38  PHE B CZ  1 
ATOM   1037 N N   . GLU B 1 39  ? 1.697   34.613 15.929  1.00 43.29  ? 39  GLU B N   1 
ATOM   1038 C CA  . GLU B 1 39  ? 1.756   35.760 15.029  1.00 48.15  ? 39  GLU B CA  1 
ATOM   1039 C C   . GLU B 1 39  ? 2.093   37.042 15.769  1.00 50.36  ? 39  GLU B C   1 
ATOM   1040 O O   . GLU B 1 39  ? 1.548   37.307 16.836  1.00 46.60  ? 39  GLU B O   1 
ATOM   1041 C CB  . GLU B 1 39  ? 0.426   35.914 14.300  1.00 52.79  ? 39  GLU B CB  1 
ATOM   1042 C CG  . GLU B 1 39  ? 0.355   35.103 13.024  1.00 55.09  ? 39  GLU B CG  1 
ATOM   1043 C CD  . GLU B 1 39  ? -1.019  35.119 12.406  1.00 59.45  ? 39  GLU B CD  1 
ATOM   1044 O OE1 . GLU B 1 39  ? -1.259  35.983 11.540  1.00 57.30  ? 39  GLU B OE1 1 
ATOM   1045 O OE2 . GLU B 1 39  ? -1.854  34.277 12.797  1.00 60.54  ? 39  GLU B OE2 1 
ATOM   1046 N N   . GLN B 1 40  ? 2.990   37.834 15.187  1.00 54.27  ? 40  GLN B N   1 
ATOM   1047 C CA  . GLN B 1 40  ? 3.411   39.101 15.772  1.00 59.52  ? 40  GLN B CA  1 
ATOM   1048 C C   . GLN B 1 40  ? 3.502   40.168 14.683  1.00 66.92  ? 40  GLN B C   1 
ATOM   1049 O O   . GLN B 1 40  ? 4.194   39.983 13.680  1.00 64.39  ? 40  GLN B O   1 
ATOM   1050 C CB  . GLN B 1 40  ? 4.760   38.936 16.467  1.00 60.23  ? 40  GLN B CB  1 
ATOM   1051 C CG  . GLN B 1 40  ? 5.027   39.993 17.523  1.00 61.00  ? 40  GLN B CG  1 
ATOM   1052 C CD  . GLN B 1 40  ? 6.454   39.976 18.033  1.00 64.35  ? 40  GLN B CD  1 
ATOM   1053 O OE1 . GLN B 1 40  ? 7.371   39.545 17.334  1.00 59.07  ? 40  GLN B OE1 1 
ATOM   1054 N NE2 . GLN B 1 40  ? 6.650   40.454 19.258  1.00 66.98  ? 40  GLN B NE2 1 
ATOM   1055 N N   . LYS B 1 41  ? 2.805   41.283 14.888  1.00 71.42  ? 41  LYS B N   1 
ATOM   1056 C CA  . LYS B 1 41  ? 2.699   42.317 13.862  1.00 82.46  ? 41  LYS B CA  1 
ATOM   1057 C C   . LYS B 1 41  ? 3.948   43.199 13.818  1.00 88.74  ? 41  LYS B C   1 
ATOM   1058 O O   . LYS B 1 41  ? 4.537   43.395 12.753  1.00 87.10  ? 41  LYS B O   1 
ATOM   1059 C CB  . LYS B 1 41  ? 1.446   43.171 14.087  1.00 92.94  ? 41  LYS B CB  1 
ATOM   1060 C CG  . LYS B 1 41  ? 0.918   43.818 12.817  1.00 101.22 ? 41  LYS B CG  1 
ATOM   1061 C CD  . LYS B 1 41  ? -0.323  44.651 13.080  1.00 108.27 ? 41  LYS B CD  1 
ATOM   1062 C CE  . LYS B 1 41  ? -0.929  45.152 11.780  1.00 110.77 ? 41  LYS B CE  1 
ATOM   1063 N NZ  . LYS B 1 41  ? -1.981  46.178 12.016  1.00 108.77 ? 41  LYS B NZ  1 
ATOM   1064 N N   . GLU B 1 42  ? 4.343   43.723 14.976  1.00 91.73  ? 42  GLU B N   1 
ATOM   1065 C CA  . GLU B 1 42  ? 5.503   44.609 15.087  1.00 94.79  ? 42  GLU B CA  1 
ATOM   1066 C C   . GLU B 1 42  ? 6.568   43.968 15.977  1.00 90.84  ? 42  GLU B C   1 
ATOM   1067 O O   . GLU B 1 42  ? 6.395   42.842 16.441  1.00 82.88  ? 42  GLU B O   1 
ATOM   1068 C CB  . GLU B 1 42  ? 5.083   45.968 15.665  1.00 102.29 ? 42  GLU B CB  1 
ATOM   1069 C CG  . GLU B 1 42  ? 3.799   46.561 15.086  1.00 113.24 ? 42  GLU B CG  1 
ATOM   1070 C CD  . GLU B 1 42  ? 3.900   46.948 13.617  1.00 113.48 ? 42  GLU B CD  1 
ATOM   1071 O OE1 . GLU B 1 42  ? 2.865   47.351 13.043  1.00 110.98 ? 42  GLU B OE1 1 
ATOM   1072 O OE2 . GLU B 1 42  ? 4.999   46.859 13.033  1.00 122.19 ? 42  GLU B OE2 1 
ATOM   1073 N N   . SER B 1 43  ? 7.667   44.685 16.209  1.00 94.48  ? 43  SER B N   1 
ATOM   1074 C CA  . SER B 1 43  ? 8.739   44.205 17.089  1.00 97.16  ? 43  SER B CA  1 
ATOM   1075 C C   . SER B 1 43  ? 8.277   44.088 18.542  1.00 93.59  ? 43  SER B C   1 
ATOM   1076 O O   . SER B 1 43  ? 8.674   43.160 19.248  1.00 87.73  ? 43  SER B O   1 
ATOM   1077 C CB  . SER B 1 43  ? 9.959   45.125 17.008  1.00 99.31  ? 43  SER B CB  1 
ATOM   1078 O OG  . SER B 1 43  ? 10.534  45.099 15.714  1.00 99.89  ? 43  SER B OG  1 
ATOM   1079 N N   . ASN B 1 44  ? 7.453   45.037 18.983  1.00 98.47  ? 44  ASN B N   1 
ATOM   1080 C CA  . ASN B 1 44  ? 6.824   44.972 20.306  1.00 106.42 ? 44  ASN B CA  1 
ATOM   1081 C C   . ASN B 1 44  ? 5.582   44.081 20.311  1.00 112.22 ? 44  ASN B C   1 
ATOM   1082 O O   . ASN B 1 44  ? 5.154   43.612 21.366  1.00 121.13 ? 44  ASN B O   1 
ATOM   1083 C CB  . ASN B 1 44  ? 6.464   46.372 20.803  1.00 105.55 ? 44  ASN B CB  1 
ATOM   1084 C CG  . ASN B 1 44  ? 7.688   47.215 21.098  1.00 116.49 ? 44  ASN B CG  1 
ATOM   1085 O OD1 . ASN B 1 44  ? 8.730   47.060 20.460  1.00 121.81 ? 44  ASN B OD1 1 
ATOM   1086 N ND2 . ASN B 1 44  ? 7.573   48.112 22.071  1.00 117.72 ? 44  ASN B ND2 1 
ATOM   1087 N N   . GLY B 1 45  ? 5.000   43.867 19.134  1.00 111.12 ? 45  GLY B N   1 
ATOM   1088 C CA  . GLY B 1 45  ? 3.905   42.918 18.971  1.00 104.70 ? 45  GLY B CA  1 
ATOM   1089 C C   . GLY B 1 45  ? 2.579   43.475 19.458  1.00 105.94 ? 45  GLY B C   1 
ATOM   1090 O O   . GLY B 1 45  ? 2.149   44.527 18.984  1.00 115.44 ? 45  GLY B O   1 
ATOM   1091 N N   . PRO B 1 46  ? 1.914   42.778 20.403  1.00 102.02 ? 46  PRO B N   1 
ATOM   1092 C CA  . PRO B 1 46  ? 2.302   41.527 21.061  1.00 90.51  ? 46  PRO B CA  1 
ATOM   1093 C C   . PRO B 1 46  ? 2.164   40.312 20.139  1.00 77.29  ? 46  PRO B C   1 
ATOM   1094 O O   . PRO B 1 46  ? 1.892   40.472 18.945  1.00 69.09  ? 46  PRO B O   1 
ATOM   1095 C CB  . PRO B 1 46  ? 1.319   41.423 22.243  1.00 91.94  ? 46  PRO B CB  1 
ATOM   1096 C CG  . PRO B 1 46  ? 0.585   42.722 22.293  1.00 98.63  ? 46  PRO B CG  1 
ATOM   1097 C CD  . PRO B 1 46  ? 0.608   43.242 20.894  1.00 105.31 ? 46  PRO B CD  1 
ATOM   1098 N N   . VAL B 1 47  ? 2.358   39.116 20.697  1.00 65.53  ? 47  VAL B N   1 
ATOM   1099 C CA  . VAL B 1 47  ? 2.257   37.869 19.932  1.00 62.24  ? 47  VAL B CA  1 
ATOM   1100 C C   . VAL B 1 47  ? 0.860   37.260 20.058  1.00 58.82  ? 47  VAL B C   1 
ATOM   1101 O O   . VAL B 1 47  ? 0.419   36.928 21.158  1.00 59.53  ? 47  VAL B O   1 
ATOM   1102 C CB  . VAL B 1 47  ? 3.298   36.824 20.393  1.00 58.93  ? 47  VAL B CB  1 
ATOM   1103 C CG1 . VAL B 1 47  ? 3.170   35.540 19.582  1.00 55.83  ? 47  VAL B CG1 1 
ATOM   1104 C CG2 . VAL B 1 47  ? 4.706   37.389 20.269  1.00 62.66  ? 47  VAL B CG2 1 
ATOM   1105 N N   . LYS B 1 48  ? 0.177   37.116 18.926  1.00 53.92  ? 48  LYS B N   1 
ATOM   1106 C CA  . LYS B 1 48  ? -1.110  36.434 18.873  1.00 53.82  ? 48  LYS B CA  1 
ATOM   1107 C C   . LYS B 1 48  ? -0.864  34.931 18.734  1.00 44.25  ? 48  LYS B C   1 
ATOM   1108 O O   . LYS B 1 48  ? -0.197  34.491 17.798  1.00 37.64  ? 48  LYS B O   1 
ATOM   1109 C CB  . LYS B 1 48  ? -1.939  36.957 17.691  1.00 63.10  ? 48  LYS B CB  1 
ATOM   1110 C CG  . LYS B 1 48  ? -3.355  36.401 17.594  1.00 71.46  ? 48  LYS B CG  1 
ATOM   1111 C CD  . LYS B 1 48  ? -4.233  36.859 18.751  1.00 77.93  ? 48  LYS B CD  1 
ATOM   1112 C CE  . LYS B 1 48  ? -5.694  36.487 18.535  1.00 79.54  ? 48  LYS B CE  1 
ATOM   1113 N NZ  . LYS B 1 48  ? -5.930  35.015 18.582  1.00 81.36  ? 48  LYS B NZ  1 
ATOM   1114 N N   . VAL B 1 49  ? -1.396  34.156 19.676  1.00 38.57  ? 49  VAL B N   1 
ATOM   1115 C CA  . VAL B 1 49  ? -1.277  32.700 19.662  1.00 35.83  ? 49  VAL B CA  1 
ATOM   1116 C C   . VAL B 1 49  ? -2.661  32.086 19.470  1.00 35.33  ? 49  VAL B C   1 
ATOM   1117 O O   . VAL B 1 49  ? -3.613  32.454 20.166  1.00 35.18  ? 49  VAL B O   1 
ATOM   1118 C CB  . VAL B 1 49  ? -0.671  32.174 20.979  1.00 36.59  ? 49  VAL B CB  1 
ATOM   1119 C CG1 . VAL B 1 49  ? -0.345  30.689 20.868  1.00 35.48  ? 49  VAL B CG1 1 
ATOM   1120 C CG2 . VAL B 1 49  ? 0.572   32.972 21.355  1.00 37.09  ? 49  VAL B CG2 1 
ATOM   1121 N N   . TRP B 1 50  ? -2.778  31.152 18.531  1.00 33.58  ? 50  TRP B N   1 
ATOM   1122 C CA  . TRP B 1 50  ? -4.060  30.508 18.259  1.00 32.82  ? 50  TRP B CA  1 
ATOM   1123 C C   . TRP B 1 50  ? -3.906  29.152 17.574  1.00 31.04  ? 50  TRP B C   1 
ATOM   1124 O O   . TRP B 1 50  ? -2.914  28.888 16.894  1.00 31.41  ? 50  TRP B O   1 
ATOM   1125 C CB  . TRP B 1 50  ? -4.938  31.420 17.398  1.00 35.99  ? 50  TRP B CB  1 
ATOM   1126 C CG  . TRP B 1 50  ? -4.385  31.648 16.025  1.00 36.13  ? 50  TRP B CG  1 
ATOM   1127 C CD1 . TRP B 1 50  ? -3.419  32.541 15.668  1.00 37.58  ? 50  TRP B CD1 1 
ATOM   1128 C CD2 . TRP B 1 50  ? -4.757  30.959 14.829  1.00 35.44  ? 50  TRP B CD2 1 
ATOM   1129 N NE1 . TRP B 1 50  ? -3.169  32.457 14.320  1.00 37.81  ? 50  TRP B NE1 1 
ATOM   1130 C CE2 . TRP B 1 50  ? -3.976  31.491 13.781  1.00 36.74  ? 50  TRP B CE2 1 
ATOM   1131 C CE3 . TRP B 1 50  ? -5.672  29.941 14.542  1.00 36.08  ? 50  TRP B CE3 1 
ATOM   1132 C CZ2 . TRP B 1 50  ? -4.086  31.044 12.466  1.00 38.22  ? 50  TRP B CZ2 1 
ATOM   1133 C CZ3 . TRP B 1 50  ? -5.782  29.496 13.230  1.00 38.00  ? 50  TRP B CZ3 1 
ATOM   1134 C CH2 . TRP B 1 50  ? -4.994  30.048 12.209  1.00 38.37  ? 50  TRP B CH2 1 
ATOM   1135 N N   . GLY B 1 51  ? -4.917  28.309 17.746  1.00 29.20  ? 51  GLY B N   1 
ATOM   1136 C CA  . GLY B 1 51  ? -4.906  26.954 17.210  1.00 27.79  ? 51  GLY B CA  1 
ATOM   1137 C C   . GLY B 1 51  ? -5.867  26.086 17.993  1.00 26.90  ? 51  GLY B C   1 
ATOM   1138 O O   . GLY B 1 51  ? -6.825  26.591 18.585  1.00 29.33  ? 51  GLY B O   1 
ATOM   1139 N N   . SER B 1 52  ? -5.617  24.780 18.001  1.00 24.81  ? 52  SER B N   1 
ATOM   1140 C CA  . SER B 1 52  ? -6.443  23.862 18.775  1.00 25.25  ? 52  SER B CA  1 
ATOM   1141 C C   . SER B 1 52  ? -5.677  22.608 19.164  1.00 24.28  ? 52  SER B C   1 
ATOM   1142 O O   . SER B 1 52  ? -4.734  22.196 18.485  1.00 24.67  ? 52  SER B O   1 
ATOM   1143 C CB  . SER B 1 52  ? -7.720  23.490 18.014  1.00 25.37  ? 52  SER B CB  1 
ATOM   1144 O OG  . SER B 1 52  ? -7.432  22.751 16.840  1.00 28.62  ? 52  SER B OG  1 
ATOM   1145 N N   . ILE B 1 53  ? -6.080  22.023 20.284  1.00 24.36  ? 53  ILE B N   1 
ATOM   1146 C CA  . ILE B 1 53  ? -5.490  20.791 20.777  1.00 24.63  ? 53  ILE B CA  1 
ATOM   1147 C C   . ILE B 1 53  ? -6.618  19.798 21.029  1.00 25.71  ? 53  ILE B C   1 
ATOM   1148 O O   . ILE B 1 53  ? -7.669  20.157 21.556  1.00 26.01  ? 53  ILE B O   1 
ATOM   1149 C CB  . ILE B 1 53  ? -4.702  21.019 22.077  1.00 25.70  ? 53  ILE B CB  1 
ATOM   1150 C CG1 . ILE B 1 53  ? -3.780  22.239 21.947  1.00 26.41  ? 53  ILE B CG1 1 
ATOM   1151 C CG2 . ILE B 1 53  ? -3.892  19.775 22.427  1.00 26.66  ? 53  ILE B CG2 1 
ATOM   1152 C CD1 . ILE B 1 53  ? -3.261  22.754 23.274  1.00 27.22  ? 53  ILE B CD1 1 
ATOM   1153 N N   . LYS B 1 54  ? -6.390  18.551 20.639  1.00 27.75  ? 54  LYS B N   1 
ATOM   1154 C CA  . LYS B 1 54  ? -7.395  17.503 20.734  1.00 30.16  ? 54  LYS B CA  1 
ATOM   1155 C C   . LYS B 1 54  ? -6.825  16.351 21.561  1.00 30.40  ? 54  LYS B C   1 
ATOM   1156 O O   . LYS B 1 54  ? -5.611  16.194 21.646  1.00 30.14  ? 54  LYS B O   1 
ATOM   1157 C CB  . LYS B 1 54  ? -7.776  17.039 19.326  1.00 34.36  ? 54  LYS B CB  1 
ATOM   1158 C CG  . LYS B 1 54  ? -8.250  18.182 18.421  1.00 40.72  ? 54  LYS B CG  1 
ATOM   1159 C CD  . LYS B 1 54  ? -8.075  17.891 16.933  1.00 46.22  ? 54  LYS B CD  1 
ATOM   1160 C CE  . LYS B 1 54  ? -8.153  19.166 16.098  1.00 52.47  ? 54  LYS B CE  1 
ATOM   1161 N NZ  . LYS B 1 54  ? -6.931  20.017 16.221  1.00 54.77  ? 54  LYS B NZ  1 
ATOM   1162 N N   . GLY B 1 55  ? -7.703  15.568 22.184  1.00 30.38  ? 55  GLY B N   1 
ATOM   1163 C CA  . GLY B 1 55  ? -7.291  14.402 22.972  1.00 30.69  ? 55  GLY B CA  1 
ATOM   1164 C C   . GLY B 1 55  ? -6.943  14.691 24.427  1.00 31.30  ? 55  GLY B C   1 
ATOM   1165 O O   . GLY B 1 55  ? -6.328  13.861 25.098  1.00 32.48  ? 55  GLY B O   1 
ATOM   1166 N N   . LEU B 1 56  ? -7.340  15.859 24.923  1.00 31.57  ? 56  LEU B N   1 
ATOM   1167 C CA  . LEU B 1 56  ? -7.049  16.249 26.301  1.00 31.88  ? 56  LEU B CA  1 
ATOM   1168 C C   . LEU B 1 56  ? -8.184  15.832 27.226  1.00 35.70  ? 56  LEU B C   1 
ATOM   1169 O O   . LEU B 1 56  ? -9.333  15.716 26.805  1.00 38.40  ? 56  LEU B O   1 
ATOM   1170 C CB  . LEU B 1 56  ? -6.826  17.762 26.394  1.00 31.66  ? 56  LEU B CB  1 
ATOM   1171 C CG  . LEU B 1 56  ? -5.570  18.297 25.692  1.00 29.98  ? 56  LEU B CG  1 
ATOM   1172 C CD1 . LEU B 1 56  ? -5.644  19.804 25.494  1.00 29.70  ? 56  LEU B CD1 1 
ATOM   1173 C CD2 . LEU B 1 56  ? -4.310  17.928 26.462  1.00 29.96  ? 56  LEU B CD2 1 
ATOM   1174 N N   . THR B 1 57  ? -7.857  15.599 28.489  1.00 38.44  ? 57  THR B N   1 
ATOM   1175 C CA  . THR B 1 57  ? -8.884  15.362 29.494  1.00 42.09  ? 57  THR B CA  1 
ATOM   1176 C C   . THR B 1 57  ? -9.625  16.672 29.723  1.00 45.38  ? 57  THR B C   1 
ATOM   1177 O O   . THR B 1 57  ? -9.025  17.743 29.653  1.00 43.49  ? 57  THR B O   1 
ATOM   1178 C CB  . THR B 1 57  ? -8.287  14.858 30.821  1.00 43.07  ? 57  THR B CB  1 
ATOM   1179 O OG1 . THR B 1 57  ? -7.264  15.757 31.266  1.00 40.55  ? 57  THR B OG1 1 
ATOM   1180 C CG2 . THR B 1 57  ? -7.700  13.461 30.648  1.00 43.97  ? 57  THR B CG2 1 
ATOM   1181 N N   . GLU B 1 58  ? -10.928 16.585 29.974  1.00 49.81  ? 58  GLU B N   1 
ATOM   1182 C CA  . GLU B 1 58  ? -11.753 17.771 30.193  1.00 52.66  ? 58  GLU B CA  1 
ATOM   1183 C C   . GLU B 1 58  ? -11.210 18.601 31.352  1.00 51.41  ? 58  GLU B C   1 
ATOM   1184 O O   . GLU B 1 58  ? -10.979 18.071 32.439  1.00 53.08  ? 58  GLU B O   1 
ATOM   1185 C CB  . GLU B 1 58  ? -13.199 17.363 30.482  1.00 58.88  ? 58  GLU B CB  1 
ATOM   1186 C CG  . GLU B 1 58  ? -14.140 18.525 30.771  1.00 64.08  ? 58  GLU B CG  1 
ATOM   1187 C CD  . GLU B 1 58  ? -15.589 18.093 30.888  1.00 69.67  ? 58  GLU B CD  1 
ATOM   1188 O OE1 . GLU B 1 58  ? -15.846 16.884 31.086  1.00 72.47  ? 58  GLU B OE1 1 
ATOM   1189 O OE2 . GLU B 1 58  ? -16.473 18.969 30.786  1.00 72.10  ? 58  GLU B OE2 1 
ATOM   1190 N N   . GLY B 1 59  ? -11.000 19.895 31.112  1.00 47.88  ? 59  GLY B N   1 
ATOM   1191 C CA  . GLY B 1 59  ? -10.556 20.817 32.157  1.00 49.64  ? 59  GLY B CA  1 
ATOM   1192 C C   . GLY B 1 59  ? -9.438  21.749 31.730  1.00 49.85  ? 59  GLY B C   1 
ATOM   1193 O O   . GLY B 1 59  ? -9.192  21.939 30.538  1.00 51.31  ? 59  GLY B O   1 
ATOM   1194 N N   . LEU B 1 60  ? -8.767  22.331 32.721  1.00 50.55  ? 60  LEU B N   1 
ATOM   1195 C CA  . LEU B 1 60  ? -7.660  23.260 32.495  1.00 48.30  ? 60  LEU B CA  1 
ATOM   1196 C C   . LEU B 1 60  ? -6.338  22.515 32.378  1.00 44.82  ? 60  LEU B C   1 
ATOM   1197 O O   . LEU B 1 60  ? -6.096  21.554 33.106  1.00 48.04  ? 60  LEU B O   1 
ATOM   1198 C CB  . LEU B 1 60  ? -7.567  24.267 33.642  1.00 50.74  ? 60  LEU B CB  1 
ATOM   1199 C CG  . LEU B 1 60  ? -8.702  25.287 33.731  1.00 53.98  ? 60  LEU B CG  1 
ATOM   1200 C CD1 . LEU B 1 60  ? -8.769  25.896 35.123  1.00 56.53  ? 60  LEU B CD1 1 
ATOM   1201 C CD2 . LEU B 1 60  ? -8.532  26.370 32.677  1.00 52.55  ? 60  LEU B CD2 1 
ATOM   1202 N N   . HIS B 1 61  ? -5.482  22.974 31.469  1.00 40.49  ? 61  HIS B N   1 
ATOM   1203 C CA  . HIS B 1 61  ? -4.170  22.366 31.250  1.00 38.71  ? 61  HIS B CA  1 
ATOM   1204 C C   . HIS B 1 61  ? -3.098  23.434 31.142  1.00 37.11  ? 61  HIS B C   1 
ATOM   1205 O O   . HIS B 1 61  ? -3.247  24.382 30.375  1.00 39.48  ? 61  HIS B O   1 
ATOM   1206 C CB  . HIS B 1 61  ? -4.181  21.542 29.963  1.00 37.38  ? 61  HIS B CB  1 
ATOM   1207 C CG  . HIS B 1 61  ? -5.106  20.370 30.011  1.00 39.13  ? 61  HIS B CG  1 
ATOM   1208 N ND1 . HIS B 1 61  ? -4.692  19.111 30.381  1.00 39.56  ? 61  HIS B ND1 1 
ATOM   1209 C CD2 . HIS B 1 61  ? -6.432  20.271 29.754  1.00 40.08  ? 61  HIS B CD2 1 
ATOM   1210 C CE1 . HIS B 1 61  ? -5.720  18.282 30.340  1.00 40.42  ? 61  HIS B CE1 1 
ATOM   1211 N NE2 . HIS B 1 61  ? -6.787  18.962 29.962  1.00 41.28  ? 61  HIS B NE2 1 
ATOM   1212 N N   . GLY B 1 62  ? -2.018  23.274 31.902  1.00 34.75  ? 62  GLY B N   1 
ATOM   1213 C CA  . GLY B 1 62  ? -0.861  24.160 31.796  1.00 34.89  ? 62  GLY B CA  1 
ATOM   1214 C C   . GLY B 1 62  ? -0.371  24.282 30.362  1.00 35.60  ? 62  GLY B C   1 
ATOM   1215 O O   . GLY B 1 62  ? -0.285  23.286 29.639  1.00 35.24  ? 62  GLY B O   1 
ATOM   1216 N N   . PHE B 1 63  ? -0.052  25.509 29.957  1.00 36.01  ? 63  PHE B N   1 
ATOM   1217 C CA  . PHE B 1 63  ? 0.310   25.813 28.574  1.00 36.86  ? 63  PHE B CA  1 
ATOM   1218 C C   . PHE B 1 63  ? 1.456   26.821 28.575  1.00 38.25  ? 63  PHE B C   1 
ATOM   1219 O O   . PHE B 1 63  ? 1.241   28.009 28.833  1.00 41.62  ? 63  PHE B O   1 
ATOM   1220 C CB  . PHE B 1 63  ? -0.918  26.376 27.847  1.00 35.99  ? 63  PHE B CB  1 
ATOM   1221 C CG  . PHE B 1 63  ? -0.749  26.516 26.357  1.00 37.06  ? 63  PHE B CG  1 
ATOM   1222 C CD1 . PHE B 1 63  ? -0.564  25.397 25.554  1.00 36.49  ? 63  PHE B CD1 1 
ATOM   1223 C CD2 . PHE B 1 63  ? -0.811  27.763 25.750  1.00 38.44  ? 63  PHE B CD2 1 
ATOM   1224 C CE1 . PHE B 1 63  ? -0.421  25.523 24.179  1.00 35.82  ? 63  PHE B CE1 1 
ATOM   1225 C CE2 . PHE B 1 63  ? -0.669  27.894 24.378  1.00 38.03  ? 63  PHE B CE2 1 
ATOM   1226 C CZ  . PHE B 1 63  ? -0.476  26.773 23.591  1.00 36.18  ? 63  PHE B CZ  1 
ATOM   1227 N N   . HIS B 1 64  ? 2.674   26.345 28.316  1.00 38.13  ? 64  HIS B N   1 
ATOM   1228 C CA  . HIS B 1 64  ? 3.860   27.203 28.409  1.00 41.92  ? 64  HIS B CA  1 
ATOM   1229 C C   . HIS B 1 64  ? 4.880   26.937 27.313  1.00 37.74  ? 64  HIS B C   1 
ATOM   1230 O O   . HIS B 1 64  ? 5.023   25.811 26.842  1.00 35.40  ? 64  HIS B O   1 
ATOM   1231 C CB  . HIS B 1 64  ? 4.580   27.033 29.761  1.00 47.20  ? 64  HIS B CB  1 
ATOM   1232 C CG  . HIS B 1 64  ? 3.742   26.416 30.837  1.00 53.91  ? 64  HIS B CG  1 
ATOM   1233 N ND1 . HIS B 1 64  ? 2.955   27.158 31.692  1.00 59.02  ? 64  HIS B ND1 1 
ATOM   1234 C CD2 . HIS B 1 64  ? 3.580   25.124 31.204  1.00 60.83  ? 64  HIS B CD2 1 
ATOM   1235 C CE1 . HIS B 1 64  ? 2.340   26.349 32.536  1.00 62.44  ? 64  HIS B CE1 1 
ATOM   1236 N NE2 . HIS B 1 64  ? 2.702   25.109 32.261  1.00 64.87  ? 64  HIS B NE2 1 
ATOM   1237 N N   . VAL B 1 65  ? 5.596   27.991 26.933  1.00 37.82  ? 65  VAL B N   1 
ATOM   1238 C CA  . VAL B 1 65  ? 6.830   27.862 26.172  1.00 37.09  ? 65  VAL B CA  1 
ATOM   1239 C C   . VAL B 1 65  ? 7.932   27.621 27.194  1.00 38.47  ? 65  VAL B C   1 
ATOM   1240 O O   . VAL B 1 65  ? 8.120   28.428 28.102  1.00 40.38  ? 65  VAL B O   1 
ATOM   1241 C CB  . VAL B 1 65  ? 7.156   29.142 25.380  1.00 35.90  ? 65  VAL B CB  1 
ATOM   1242 C CG1 . VAL B 1 65  ? 8.451   28.971 24.594  1.00 35.15  ? 65  VAL B CG1 1 
ATOM   1243 C CG2 . VAL B 1 65  ? 6.003   29.500 24.451  1.00 35.34  ? 65  VAL B CG2 1 
ATOM   1244 N N   . HIS B 1 66  ? 8.649   26.510 27.054  1.00 39.67  ? 66  HIS B N   1 
ATOM   1245 C CA  . HIS B 1 66  ? 9.674   26.147 28.021  1.00 41.26  ? 66  HIS B CA  1 
ATOM   1246 C C   . HIS B 1 66  ? 10.808  27.176 28.043  1.00 47.32  ? 66  HIS B C   1 
ATOM   1247 O O   . HIS B 1 66  ? 11.423  27.459 27.013  1.00 47.11  ? 66  HIS B O   1 
ATOM   1248 C CB  . HIS B 1 66  ? 10.235  24.753 27.729  1.00 40.29  ? 66  HIS B CB  1 
ATOM   1249 C CG  . HIS B 1 66  ? 11.338  24.348 28.655  1.00 40.58  ? 66  HIS B CG  1 
ATOM   1250 N ND1 . HIS B 1 66  ? 11.116  24.015 29.973  1.00 42.49  ? 66  HIS B ND1 1 
ATOM   1251 C CD2 . HIS B 1 66  ? 12.672  24.241 28.458  1.00 41.23  ? 66  HIS B CD2 1 
ATOM   1252 C CE1 . HIS B 1 66  ? 12.267  23.712 30.547  1.00 43.26  ? 66  HIS B CE1 1 
ATOM   1253 N NE2 . HIS B 1 66  ? 13.226  23.841 29.649  1.00 43.18  ? 66  HIS B NE2 1 
ATOM   1254 N N   . GLY B 1 67  ? 11.070  27.723 29.228  1.00 53.62  ? 67  GLY B N   1 
ATOM   1255 C CA  . GLY B 1 67  ? 12.105  28.735 29.413  1.00 60.62  ? 67  GLY B CA  1 
ATOM   1256 C C   . GLY B 1 67  ? 11.611  29.888 30.264  1.00 70.17  ? 67  GLY B C   1 
ATOM   1257 O O   . GLY B 1 67  ? 10.638  29.751 31.010  1.00 73.78  ? 67  GLY B O   1 
ATOM   1258 N N   . ALA B 1 68  ? 12.282  31.029 30.144  1.00 76.62  ? 68  ALA B N   1 
ATOM   1259 C CA  . ALA B 1 68  ? 11.943  32.212 30.927  1.00 75.92  ? 68  ALA B CA  1 
ATOM   1260 C C   . ALA B 1 68  ? 10.778  32.975 30.295  1.00 79.38  ? 68  ALA B C   1 
ATOM   1261 O O   . ALA B 1 68  ? 10.755  33.197 29.081  1.00 73.93  ? 68  ALA B O   1 
ATOM   1262 C CB  . ALA B 1 68  ? 13.157  33.117 31.063  1.00 78.39  ? 68  ALA B CB  1 
ATOM   1263 N N   . GLY B 1 69  ? 9.813   33.361 31.129  1.00 76.16  ? 69  GLY B N   1 
ATOM   1264 C CA  . GLY B 1 69  ? 8.692   34.205 30.712  1.00 75.69  ? 69  GLY B CA  1 
ATOM   1265 C C   . GLY B 1 69  ? 7.849   33.619 29.600  1.00 75.25  ? 69  GLY B C   1 
ATOM   1266 O O   . GLY B 1 69  ? 7.471   34.326 28.664  1.00 69.63  ? 69  GLY B O   1 
ATOM   1267 N N   . GLY B 1 70  ? 7.553   32.327 29.710  1.00 76.75  ? 70  GLY B N   1 
ATOM   1268 C CA  . GLY B 1 70  ? 6.788   31.611 28.693  1.00 72.25  ? 70  GLY B CA  1 
ATOM   1269 C C   . GLY B 1 70  ? 5.476   31.024 29.182  1.00 74.38  ? 70  GLY B C   1 
ATOM   1270 O O   . GLY B 1 70  ? 4.835   30.274 28.450  1.00 72.62  ? 70  GLY B O   1 
ATOM   1271 N N   . ASP B 1 71  ? 5.067   31.362 30.405  1.00 76.26  ? 71  ASP B N   1 
ATOM   1272 C CA  . ASP B 1 71  ? 3.801   30.874 30.959  1.00 74.98  ? 71  ASP B CA  1 
ATOM   1273 C C   . ASP B 1 71  ? 2.620   31.648 30.369  1.00 73.25  ? 71  ASP B C   1 
ATOM   1274 O O   . ASP B 1 71  ? 2.377   32.798 30.737  1.00 66.50  ? 71  ASP B O   1 
ATOM   1275 C CB  . ASP B 1 71  ? 3.797   30.982 32.492  1.00 79.02  ? 71  ASP B CB  1 
ATOM   1276 C CG  . ASP B 1 71  ? 2.489   30.501 33.117  1.00 77.13  ? 71  ASP B CG  1 
ATOM   1277 O OD1 . ASP B 1 71  ? 1.910   29.507 32.629  1.00 69.80  ? 71  ASP B OD1 1 
ATOM   1278 O OD2 . ASP B 1 71  ? 2.041   31.117 34.105  1.00 79.68  ? 71  ASP B OD2 1 
ATOM   1279 N N   . LEU B 1 72  ? 1.891   31.004 29.459  1.00 69.31  ? 72  LEU B N   1 
ATOM   1280 C CA  . LEU B 1 72  ? 0.712   31.600 28.826  1.00 67.86  ? 72  LEU B CA  1 
ATOM   1281 C C   . LEU B 1 72  ? -0.590  31.129 29.488  1.00 62.39  ? 72  LEU B C   1 
ATOM   1282 O O   . LEU B 1 72  ? -1.655  31.170 28.872  1.00 60.68  ? 72  LEU B O   1 
ATOM   1283 C CB  . LEU B 1 72  ? 0.686   31.261 27.333  1.00 70.19  ? 72  LEU B CB  1 
ATOM   1284 C CG  . LEU B 1 72  ? 1.980   31.497 26.549  1.00 71.97  ? 72  LEU B CG  1 
ATOM   1285 C CD1 . LEU B 1 72  ? 1.819   31.008 25.119  1.00 71.36  ? 72  LEU B CD1 1 
ATOM   1286 C CD2 . LEU B 1 72  ? 2.381   32.963 26.574  1.00 73.85  ? 72  LEU B CD2 1 
ATOM   1287 N N   . GLY B 1 73  ? -0.496  30.678 30.738  1.00 62.87  ? 73  GLY B N   1 
ATOM   1288 C CA  . GLY B 1 73  ? -1.666  30.287 31.519  1.00 60.57  ? 73  GLY B CA  1 
ATOM   1289 C C   . GLY B 1 73  ? -2.114  28.862 31.258  1.00 55.46  ? 73  GLY B C   1 
ATOM   1290 O O   . GLY B 1 73  ? -1.293  27.963 31.067  1.00 52.83  ? 73  GLY B O   1 
ATOM   1291 N N   . ASN B 1 74  ? -3.428  28.661 31.273  1.00 54.94  ? 74  ASN B N   1 
ATOM   1292 C CA  . ASN B 1 74  ? -4.025  27.365 30.989  1.00 53.49  ? 74  ASN B CA  1 
ATOM   1293 C C   . ASN B 1 74  ? -4.961  27.453 29.791  1.00 49.27  ? 74  ASN B C   1 
ATOM   1294 O O   . ASN B 1 74  ? -5.622  28.471 29.584  1.00 50.68  ? 74  ASN B O   1 
ATOM   1295 C CB  . ASN B 1 74  ? -4.821  26.863 32.198  1.00 57.23  ? 74  ASN B CB  1 
ATOM   1296 C CG  . ASN B 1 74  ? -3.964  26.671 33.436  1.00 59.81  ? 74  ASN B CG  1 
ATOM   1297 O OD1 . ASN B 1 74  ? -2.750  26.502 33.353  1.00 60.53  ? 74  ASN B OD1 1 
ATOM   1298 N ND2 . ASN B 1 74  ? -4.602  26.687 34.597  1.00 65.15  ? 74  ASN B ND2 1 
ATOM   1299 N N   . VAL B 1 75  ? -5.008  26.384 29.003  1.00 44.75  ? 75  VAL B N   1 
ATOM   1300 C CA  . VAL B 1 75  ? -6.031  26.235 27.969  1.00 41.81  ? 75  VAL B CA  1 
ATOM   1301 C C   . VAL B 1 75  ? -7.154  25.396 28.563  1.00 42.67  ? 75  VAL B C   1 
ATOM   1302 O O   . VAL B 1 75  ? -6.935  24.670 29.536  1.00 42.93  ? 75  VAL B O   1 
ATOM   1303 C CB  . VAL B 1 75  ? -5.488  25.595 26.663  1.00 38.74  ? 75  VAL B CB  1 
ATOM   1304 C CG1 . VAL B 1 75  ? -4.421  26.484 26.043  1.00 38.84  ? 75  VAL B CG1 1 
ATOM   1305 C CG2 . VAL B 1 75  ? -4.945  24.187 26.895  1.00 36.65  ? 75  VAL B CG2 1 
ATOM   1306 N N   . THR B 1 76  ? -8.349  25.509 27.991  1.00 45.35  ? 76  THR B N   1 
ATOM   1307 C CA  . THR B 1 76  ? -9.515  24.789 28.497  1.00 47.47  ? 76  THR B CA  1 
ATOM   1308 C C   . THR B 1 76  ? -10.015 23.776 27.471  1.00 47.79  ? 76  THR B C   1 
ATOM   1309 O O   . THR B 1 76  ? -10.467 24.150 26.384  1.00 44.58  ? 76  THR B O   1 
ATOM   1310 C CB  . THR B 1 76  ? -10.660 25.755 28.856  1.00 51.62  ? 76  THR B CB  1 
ATOM   1311 O OG1 . THR B 1 76  ? -10.157 26.802 29.699  1.00 58.58  ? 76  THR B OG1 1 
ATOM   1312 C CG2 . THR B 1 76  ? -11.787 25.015 29.579  1.00 53.51  ? 76  THR B CG2 1 
ATOM   1313 N N   . ALA B 1 77  ? -9.927  22.496 27.828  1.00 46.04  ? 77  ALA B N   1 
ATOM   1314 C CA  . ALA B 1 77  ? -10.452 21.419 26.998  1.00 42.52  ? 77  ALA B CA  1 
ATOM   1315 C C   . ALA B 1 77  ? -11.872 21.091 27.444  1.00 45.50  ? 77  ALA B C   1 
ATOM   1316 O O   . ALA B 1 77  ? -12.118 20.877 28.633  1.00 44.71  ? 77  ALA B O   1 
ATOM   1317 C CB  . ALA B 1 77  ? -9.564  20.189 27.100  1.00 40.88  ? 77  ALA B CB  1 
ATOM   1318 N N   . ASP B 1 78  ? -12.801 21.058 26.489  1.00 46.52  ? 78  ASP B N   1 
ATOM   1319 C CA  . ASP B 1 78  ? -14.211 20.769 26.781  1.00 47.75  ? 78  ASP B CA  1 
ATOM   1320 C C   . ASP B 1 78  ? -14.444 19.257 26.934  1.00 49.06  ? 78  ASP B C   1 
ATOM   1321 O O   . ASP B 1 78  ? -13.486 18.482 26.950  1.00 45.24  ? 78  ASP B O   1 
ATOM   1322 C CB  . ASP B 1 78  ? -15.117 21.380 25.699  1.00 47.11  ? 78  ASP B CB  1 
ATOM   1323 C CG  . ASP B 1 78  ? -14.903 20.768 24.320  1.00 46.58  ? 78  ASP B CG  1 
ATOM   1324 O OD1 . ASP B 1 78  ? -14.127 19.799 24.188  1.00 46.24  ? 78  ASP B OD1 1 
ATOM   1325 O OD2 . ASP B 1 78  ? -15.520 21.266 23.359  1.00 51.74  ? 78  ASP B OD2 1 
ATOM   1326 N N   . LYS B 1 79  ? -15.705 18.839 27.047  1.00 52.39  ? 79  LYS B N   1 
ATOM   1327 C CA  . LYS B 1 79  ? -16.028 17.406 27.208  1.00 60.04  ? 79  LYS B CA  1 
ATOM   1328 C C   . LYS B 1 79  ? -15.635 16.530 25.998  1.00 55.60  ? 79  LYS B C   1 
ATOM   1329 O O   . LYS B 1 79  ? -15.455 15.320 26.146  1.00 54.15  ? 79  LYS B O   1 
ATOM   1330 C CB  . LYS B 1 79  ? -17.500 17.166 27.633  1.00 67.32  ? 79  LYS B CB  1 
ATOM   1331 C CG  . LYS B 1 79  ? -18.577 18.077 27.042  1.00 75.31  ? 79  LYS B CG  1 
ATOM   1332 C CD  . LYS B 1 79  ? -18.844 17.800 25.571  1.00 79.65  ? 79  LYS B CD  1 
ATOM   1333 C CE  . LYS B 1 79  ? -19.870 18.766 24.998  1.00 84.23  ? 79  LYS B CE  1 
ATOM   1334 N NZ  . LYS B 1 79  ? -19.317 20.139 24.818  1.00 87.94  ? 79  LYS B NZ  1 
ATOM   1335 N N   . ASP B 1 80  ? -15.478 17.140 24.823  1.00 51.69  ? 80  ASP B N   1 
ATOM   1336 C CA  . ASP B 1 80  ? -14.954 16.437 23.643  1.00 48.57  ? 80  ASP B CA  1 
ATOM   1337 C C   . ASP B 1 80  ? -13.435 16.224 23.716  1.00 43.32  ? 80  ASP B C   1 
ATOM   1338 O O   . ASP B 1 80  ? -12.876 15.456 22.933  1.00 42.55  ? 80  ASP B O   1 
ATOM   1339 C CB  . ASP B 1 80  ? -15.289 17.207 22.357  1.00 50.54  ? 80  ASP B CB  1 
ATOM   1340 C CG  . ASP B 1 80  ? -16.784 17.360 22.131  1.00 49.35  ? 80  ASP B CG  1 
ATOM   1341 O OD1 . ASP B 1 80  ? -17.567 16.649 22.789  1.00 52.62  ? 80  ASP B OD1 1 
ATOM   1342 O OD2 . ASP B 1 80  ? -17.176 18.195 21.288  1.00 48.81  ? 80  ASP B OD2 1 
ATOM   1343 N N   . GLY B 1 81  ? -12.775 16.904 24.649  1.00 38.94  ? 81  GLY B N   1 
ATOM   1344 C CA  . GLY B 1 81  ? -11.322 16.867 24.762  1.00 38.25  ? 81  GLY B CA  1 
ATOM   1345 C C   . GLY B 1 81  ? -10.632 17.847 23.826  1.00 37.72  ? 81  GLY B C   1 
ATOM   1346 O O   . GLY B 1 81  ? -9.417  17.773 23.627  1.00 39.83  ? 81  GLY B O   1 
ATOM   1347 N N   . VAL B 1 82  ? -11.408 18.770 23.258  1.00 36.35  ? 82  VAL B N   1 
ATOM   1348 C CA  . VAL B 1 82  ? -10.887 19.775 22.335  1.00 32.49  ? 82  VAL B CA  1 
ATOM   1349 C C   . VAL B 1 82  ? -10.673 21.088 23.073  1.00 32.78  ? 82  VAL B C   1 
ATOM   1350 O O   . VAL B 1 82  ? -11.579 21.581 23.743  1.00 35.50  ? 82  VAL B O   1 
ATOM   1351 C CB  . VAL B 1 82  ? -11.856 20.026 21.163  1.00 31.16  ? 82  VAL B CB  1 
ATOM   1352 C CG1 . VAL B 1 82  ? -11.327 21.130 20.254  1.00 30.24  ? 82  VAL B CG1 1 
ATOM   1353 C CG2 . VAL B 1 82  ? -12.082 18.741 20.380  1.00 30.86  ? 82  VAL B CG2 1 
ATOM   1354 N N   . ALA B 1 83  ? -9.474  21.645 22.938  1.00 31.58  ? 83  ALA B N   1 
ATOM   1355 C CA  . ALA B 1 83  ? -9.151  22.959 23.484  1.00 32.32  ? 83  ALA B CA  1 
ATOM   1356 C C   . ALA B 1 83  ? -8.822  23.922 22.349  1.00 33.63  ? 83  ALA B C   1 
ATOM   1357 O O   . ALA B 1 83  ? -7.840  23.730 21.634  1.00 33.35  ? 83  ALA B O   1 
ATOM   1358 C CB  . ALA B 1 83  ? -7.977  22.858 24.445  1.00 30.85  ? 83  ALA B CB  1 
ATOM   1359 N N   . ASP B 1 84  ? -9.662  24.937 22.169  1.00 36.80  ? 84  ASP B N   1 
ATOM   1360 C CA  . ASP B 1 84  ? -9.369  26.021 21.242  1.00 39.69  ? 84  ASP B CA  1 
ATOM   1361 C C   . ASP B 1 84  ? -8.485  27.031 21.954  1.00 42.05  ? 84  ASP B C   1 
ATOM   1362 O O   . ASP B 1 84  ? -8.778  27.426 23.082  1.00 43.54  ? 84  ASP B O   1 
ATOM   1363 C CB  . ASP B 1 84  ? -10.653 26.700 20.771  1.00 41.73  ? 84  ASP B CB  1 
ATOM   1364 C CG  . ASP B 1 84  ? -11.492 25.805 19.889  1.00 45.87  ? 84  ASP B CG  1 
ATOM   1365 O OD1 . ASP B 1 84  ? -10.948 25.238 18.917  1.00 50.22  ? 84  ASP B OD1 1 
ATOM   1366 O OD2 . ASP B 1 84  ? -12.701 25.673 20.163  1.00 48.96  ? 84  ASP B OD2 1 
ATOM   1367 N N   . VAL B 1 85  ? -7.403  27.438 21.295  1.00 43.79  ? 85  VAL B N   1 
ATOM   1368 C CA  . VAL B 1 85  ? -6.447  28.371 21.875  1.00 44.12  ? 85  VAL B CA  1 
ATOM   1369 C C   . VAL B 1 85  ? -6.658  29.759 21.285  1.00 48.80  ? 85  VAL B C   1 
ATOM   1370 O O   . VAL B 1 85  ? -6.735  29.920 20.067  1.00 47.11  ? 85  VAL B O   1 
ATOM   1371 C CB  . VAL B 1 85  ? -4.995  27.922 21.622  1.00 43.25  ? 85  VAL B CB  1 
ATOM   1372 C CG1 . VAL B 1 85  ? -4.012  28.912 22.233  1.00 44.56  ? 85  VAL B CG1 1 
ATOM   1373 C CG2 . VAL B 1 85  ? -4.768  26.530 22.192  1.00 43.40  ? 85  VAL B CG2 1 
ATOM   1374 N N   . SER B 1 86  ? -6.767  30.750 22.166  1.00 52.76  ? 86  SER B N   1 
ATOM   1375 C CA  . SER B 1 86  ? -6.836  32.151 21.766  1.00 56.71  ? 86  SER B CA  1 
ATOM   1376 C C   . SER B 1 86  ? -6.158  33.004 22.834  1.00 60.92  ? 86  SER B C   1 
ATOM   1377 O O   . SER B 1 86  ? -6.756  33.320 23.864  1.00 69.16  ? 86  SER B O   1 
ATOM   1378 C CB  . SER B 1 86  ? -8.286  32.590 21.568  1.00 54.73  ? 86  SER B CB  1 
ATOM   1379 O OG  . SER B 1 86  ? -8.336  33.892 21.018  1.00 56.74  ? 86  SER B OG  1 
ATOM   1380 N N   . ILE B 1 87  ? -4.897  33.348 22.589  1.00 60.91  ? 87  ILE B N   1 
ATOM   1381 C CA  . ILE B 1 87  ? -4.095  34.096 23.550  1.00 63.68  ? 87  ILE B CA  1 
ATOM   1382 C C   . ILE B 1 87  ? -3.337  35.208 22.833  1.00 64.38  ? 87  ILE B C   1 
ATOM   1383 O O   . ILE B 1 87  ? -2.977  35.070 21.665  1.00 64.11  ? 87  ILE B O   1 
ATOM   1384 C CB  . ILE B 1 87  ? -3.092  33.177 24.289  1.00 66.43  ? 87  ILE B CB  1 
ATOM   1385 C CG1 . ILE B 1 87  ? -3.790  31.888 24.756  1.00 66.17  ? 87  ILE B CG1 1 
ATOM   1386 C CG2 . ILE B 1 87  ? -2.458  33.911 25.468  1.00 69.61  ? 87  ILE B CG2 1 
ATOM   1387 C CD1 . ILE B 1 87  ? -2.924  30.953 25.574  1.00 64.83  ? 87  ILE B CD1 1 
ATOM   1388 N N   . GLU B 1 88  ? -3.121  36.314 23.537  1.00 66.42  ? 88  GLU B N   1 
ATOM   1389 C CA  . GLU B 1 88  ? -2.260  37.388 23.053  1.00 72.67  ? 88  GLU B CA  1 
ATOM   1390 C C   . GLU B 1 88  ? -1.365  37.836 24.209  1.00 71.49  ? 88  GLU B C   1 
ATOM   1391 O O   . GLU B 1 88  ? -1.821  38.522 25.124  1.00 75.08  ? 88  GLU B O   1 
ATOM   1392 C CB  . GLU B 1 88  ? -3.098  38.547 22.498  1.00 81.05  ? 88  GLU B CB  1 
ATOM   1393 C CG  . GLU B 1 88  ? -2.357  39.432 21.503  1.00 89.13  ? 88  GLU B CG  1 
ATOM   1394 C CD  . GLU B 1 88  ? -3.281  40.369 20.741  1.00 97.32  ? 88  GLU B CD  1 
ATOM   1395 O OE1 . GLU B 1 88  ? -3.160  40.445 19.499  1.00 100.64 ? 88  GLU B OE1 1 
ATOM   1396 O OE2 . GLU B 1 88  ? -4.130  41.027 21.379  1.00 102.63 ? 88  GLU B OE2 1 
ATOM   1397 N N   . ASP B 1 89  ? -0.100  37.418 24.170  1.00 72.27  ? 89  ASP B N   1 
ATOM   1398 C CA  . ASP B 1 89  ? 0.835   37.646 25.272  1.00 72.51  ? 89  ASP B CA  1 
ATOM   1399 C C   . ASP B 1 89  ? 1.821   38.761 24.937  1.00 74.83  ? 89  ASP B C   1 
ATOM   1400 O O   . ASP B 1 89  ? 2.290   38.861 23.804  1.00 68.12  ? 89  ASP B O   1 
ATOM   1401 C CB  . ASP B 1 89  ? 1.597   36.357 25.593  1.00 72.89  ? 89  ASP B CB  1 
ATOM   1402 C CG  . ASP B 1 89  ? 2.326   36.418 26.929  1.00 73.69  ? 89  ASP B CG  1 
ATOM   1403 O OD1 . ASP B 1 89  ? 1.734   36.903 27.916  1.00 82.58  ? 89  ASP B OD1 1 
ATOM   1404 O OD2 . ASP B 1 89  ? 3.489   35.968 26.997  1.00 70.47  ? 89  ASP B OD2 1 
ATOM   1405 N N   . SER B 1 90  ? 2.133   39.583 25.938  1.00 78.02  ? 90  SER B N   1 
ATOM   1406 C CA  . SER B 1 90  ? 3.042   40.721 25.780  1.00 79.99  ? 90  SER B CA  1 
ATOM   1407 C C   . SER B 1 90  ? 4.491   40.377 26.120  1.00 80.37  ? 90  SER B C   1 
ATOM   1408 O O   . SER B 1 90  ? 5.412   41.047 25.654  1.00 84.49  ? 90  SER B O   1 
ATOM   1409 C CB  . SER B 1 90  ? 2.584   41.881 26.667  1.00 82.60  ? 90  SER B CB  1 
ATOM   1410 O OG  . SER B 1 90  ? 1.235   42.224 26.403  1.00 87.21  ? 90  SER B OG  1 
ATOM   1411 N N   . VAL B 1 91  ? 4.686   39.335 26.927  1.00 78.27  ? 91  VAL B N   1 
ATOM   1412 C CA  . VAL B 1 91  ? 6.015   38.972 27.423  1.00 77.55  ? 91  VAL B CA  1 
ATOM   1413 C C   . VAL B 1 91  ? 6.864   38.372 26.299  1.00 71.21  ? 91  VAL B C   1 
ATOM   1414 O O   . VAL B 1 91  ? 7.961   38.854 26.014  1.00 65.89  ? 91  VAL B O   1 
ATOM   1415 C CB  . VAL B 1 91  ? 5.930   37.977 28.609  1.00 83.40  ? 91  VAL B CB  1 
ATOM   1416 C CG1 . VAL B 1 91  ? 7.319   37.665 29.156  1.00 84.06  ? 91  VAL B CG1 1 
ATOM   1417 C CG2 . VAL B 1 91  ? 5.043   38.530 29.719  1.00 83.79  ? 91  VAL B CG2 1 
ATOM   1418 N N   . ILE B 1 92  ? 6.345   37.326 25.661  1.00 66.29  ? 92  ILE B N   1 
ATOM   1419 C CA  . ILE B 1 92  ? 7.062   36.635 24.581  1.00 60.47  ? 92  ILE B CA  1 
ATOM   1420 C C   . ILE B 1 92  ? 7.141   37.458 23.291  1.00 54.73  ? 92  ILE B C   1 
ATOM   1421 O O   . ILE B 1 92  ? 6.386   38.411 23.100  1.00 52.37  ? 92  ILE B O   1 
ATOM   1422 C CB  . ILE B 1 92  ? 6.433   35.259 24.258  1.00 56.76  ? 92  ILE B CB  1 
ATOM   1423 C CG1 . ILE B 1 92  ? 4.957   35.398 23.859  1.00 54.36  ? 92  ILE B CG1 1 
ATOM   1424 C CG2 . ILE B 1 92  ? 6.578   34.323 25.450  1.00 60.49  ? 92  ILE B CG2 1 
ATOM   1425 C CD1 . ILE B 1 92  ? 4.437   34.251 23.025  1.00 51.74  ? 92  ILE B CD1 1 
ATOM   1426 N N   . SER B 1 93  ? 8.064   37.067 22.415  1.00 49.77  ? 93  SER B N   1 
ATOM   1427 C CA  . SER B 1 93  ? 8.242   37.702 21.107  1.00 49.23  ? 93  SER B CA  1 
ATOM   1428 C C   . SER B 1 93  ? 8.673   36.670 20.070  1.00 48.41  ? 93  SER B C   1 
ATOM   1429 O O   . SER B 1 93  ? 9.092   35.569 20.424  1.00 47.47  ? 93  SER B O   1 
ATOM   1430 C CB  . SER B 1 93  ? 9.293   38.808 21.194  1.00 43.58  ? 93  SER B CB  1 
ATOM   1431 O OG  . SER B 1 93  ? 9.581   39.341 19.914  1.00 47.25  ? 93  SER B OG  1 
ATOM   1432 N N   . LEU B 1 94  ? 8.570   37.037 18.794  1.00 49.64  ? 94  LEU B N   1 
ATOM   1433 C CA  . LEU B 1 94  ? 9.006   36.175 17.691  1.00 52.70  ? 94  LEU B CA  1 
ATOM   1434 C C   . LEU B 1 94  ? 10.349  36.611 17.100  1.00 55.61  ? 94  LEU B C   1 
ATOM   1435 O O   . LEU B 1 94  ? 10.862  35.973 16.179  1.00 51.23  ? 94  LEU B O   1 
ATOM   1436 C CB  . LEU B 1 94  ? 7.943   36.138 16.588  1.00 50.17  ? 94  LEU B CB  1 
ATOM   1437 C CG  . LEU B 1 94  ? 6.572   35.574 16.968  1.00 46.79  ? 94  LEU B CG  1 
ATOM   1438 C CD1 . LEU B 1 94  ? 5.680   35.526 15.740  1.00 48.19  ? 94  LEU B CD1 1 
ATOM   1439 C CD2 . LEU B 1 94  ? 6.684   34.193 17.596  1.00 44.98  ? 94  LEU B CD2 1 
ATOM   1440 N N   . SER B 1 95  ? 10.911  37.693 17.631  1.00 63.39  ? 95  SER B N   1 
ATOM   1441 C CA  . SER B 1 95  ? 12.222  38.180 17.209  1.00 69.46  ? 95  SER B CA  1 
ATOM   1442 C C   . SER B 1 95  ? 12.951  38.823 18.387  1.00 72.13  ? 95  SER B C   1 
ATOM   1443 O O   . SER B 1 95  ? 12.375  39.000 19.463  1.00 68.48  ? 95  SER B O   1 
ATOM   1444 C CB  . SER B 1 95  ? 12.073  39.178 16.057  1.00 70.32  ? 95  SER B CB  1 
ATOM   1445 O OG  . SER B 1 95  ? 11.123  40.182 16.371  1.00 67.86  ? 95  SER B OG  1 
ATOM   1446 N N   . GLY B 1 96  ? 14.220  39.160 18.180  1.00 75.02  ? 96  GLY B N   1 
ATOM   1447 C CA  . GLY B 1 96  ? 15.037  39.775 19.222  1.00 78.76  ? 96  GLY B CA  1 
ATOM   1448 C C   . GLY B 1 96  ? 15.506  38.764 20.248  1.00 78.27  ? 96  GLY B C   1 
ATOM   1449 O O   . GLY B 1 96  ? 15.542  37.562 19.976  1.00 72.65  ? 96  GLY B O   1 
ATOM   1450 N N   . ASP B 1 97  ? 15.863  39.256 21.432  1.00 83.22  ? 97  ASP B N   1 
ATOM   1451 C CA  . ASP B 1 97  ? 16.361  38.400 22.512  1.00 83.19  ? 97  ASP B CA  1 
ATOM   1452 C C   . ASP B 1 97  ? 15.252  37.571 23.163  1.00 73.06  ? 97  ASP B C   1 
ATOM   1453 O O   . ASP B 1 97  ? 15.508  36.476 23.661  1.00 63.87  ? 97  ASP B O   1 
ATOM   1454 C CB  . ASP B 1 97  ? 17.074  39.236 23.578  1.00 87.79  ? 97  ASP B CB  1 
ATOM   1455 C CG  . ASP B 1 97  ? 18.336  39.891 23.055  1.00 92.57  ? 97  ASP B CG  1 
ATOM   1456 O OD1 . ASP B 1 97  ? 18.258  40.593 22.025  1.00 88.55  ? 97  ASP B OD1 1 
ATOM   1457 O OD2 . ASP B 1 97  ? 19.404  39.708 23.677  1.00 89.10  ? 97  ASP B OD2 1 
ATOM   1458 N N   . HIS B 1 98  ? 14.025  38.088 23.147  1.00 73.09  ? 98  HIS B N   1 
ATOM   1459 C CA  . HIS B 1 98  ? 12.877  37.396 23.751  1.00 75.45  ? 98  HIS B CA  1 
ATOM   1460 C C   . HIS B 1 98  ? 12.292  36.281 22.868  1.00 68.62  ? 98  HIS B C   1 
ATOM   1461 O O   . HIS B 1 98  ? 11.266  35.689 23.216  1.00 68.34  ? 98  HIS B O   1 
ATOM   1462 C CB  . HIS B 1 98  ? 11.770  38.407 24.105  1.00 84.92  ? 98  HIS B CB  1 
ATOM   1463 C CG  . HIS B 1 98  ? 11.748  38.803 25.549  1.00 94.05  ? 98  HIS B CG  1 
ATOM   1464 N ND1 . HIS B 1 98  ? 12.080  40.069 25.981  0.48 95.86  ? 98  HIS B ND1 1 
ATOM   1465 C CD2 . HIS B 1 98  ? 11.428  38.098 26.660  1.00 95.69  ? 98  HIS B CD2 1 
ATOM   1466 C CE1 . HIS B 1 98  ? 11.966  40.126 27.296  1.00 99.77  ? 98  HIS B CE1 1 
ATOM   1467 N NE2 . HIS B 1 98  ? 11.573  38.943 27.733  1.00 95.31  ? 98  HIS B NE2 1 
ATOM   1468 N N   . SER B 1 99  ? 12.952  35.981 21.748  1.00 60.22  ? 99  SER B N   1 
ATOM   1469 C CA  . SER B 1 99  ? 12.377  35.119 20.719  1.00 50.57  ? 99  SER B CA  1 
ATOM   1470 C C   . SER B 1 99  ? 12.053  33.721 21.237  1.00 46.07  ? 99  SER B C   1 
ATOM   1471 O O   . SER B 1 99  ? 12.901  33.059 21.834  1.00 47.56  ? 99  SER B O   1 
ATOM   1472 C CB  . SER B 1 99  ? 13.316  35.020 19.517  1.00 47.22  ? 99  SER B CB  1 
ATOM   1473 O OG  . SER B 1 99  ? 12.674  34.369 18.437  1.00 42.21  ? 99  SER B OG  1 
ATOM   1474 N N   . ILE B 1 100 ? 10.814  33.289 21.007  1.00 41.70  ? 100 ILE B N   1 
ATOM   1475 C CA  . ILE B 1 100 ? 10.379  31.921 21.321  1.00 38.17  ? 100 ILE B CA  1 
ATOM   1476 C C   . ILE B 1 100 ? 10.634  30.957 20.158  1.00 37.25  ? 100 ILE B C   1 
ATOM   1477 O O   . ILE B 1 100 ? 10.338  29.767 20.254  1.00 33.50  ? 100 ILE B O   1 
ATOM   1478 C CB  . ILE B 1 100 ? 8.887   31.866 21.708  1.00 37.26  ? 100 ILE B CB  1 
ATOM   1479 C CG1 . ILE B 1 100 ? 7.993   32.249 20.521  1.00 36.09  ? 100 ILE B CG1 1 
ATOM   1480 C CG2 . ILE B 1 100 ? 8.628   32.761 22.911  1.00 39.22  ? 100 ILE B CG2 1 
ATOM   1481 C CD1 . ILE B 1 100 ? 6.516   32.054 20.784  1.00 35.59  ? 100 ILE B CD1 1 
ATOM   1482 N N   . ILE B 1 101 ? 11.174  31.486 19.062  1.00 37.97  ? 101 ILE B N   1 
ATOM   1483 C CA  . ILE B 1 101 ? 11.556  30.686 17.905  1.00 36.79  ? 101 ILE B CA  1 
ATOM   1484 C C   . ILE B 1 101 ? 12.618  29.671 18.316  1.00 34.21  ? 101 ILE B C   1 
ATOM   1485 O O   . ILE B 1 101 ? 13.675  30.043 18.824  1.00 32.85  ? 101 ILE B O   1 
ATOM   1486 C CB  . ILE B 1 101 ? 12.136  31.574 16.782  1.00 40.45  ? 101 ILE B CB  1 
ATOM   1487 C CG1 . ILE B 1 101 ? 11.081  32.559 16.237  1.00 41.49  ? 101 ILE B CG1 1 
ATOM   1488 C CG2 . ILE B 1 101 ? 12.722  30.726 15.664  1.00 41.54  ? 101 ILE B CG2 1 
ATOM   1489 C CD1 . ILE B 1 101 ? 9.874   31.923 15.573  1.00 41.52  ? 101 ILE B CD1 1 
ATOM   1490 N N   . GLY B 1 102 ? 12.332  28.392 18.093  1.00 32.93  ? 102 GLY B N   1 
ATOM   1491 C CA  . GLY B 1 102 ? 13.264  27.320 18.438  1.00 33.13  ? 102 GLY B CA  1 
ATOM   1492 C C   . GLY B 1 102 ? 13.045  26.750 19.827  1.00 32.83  ? 102 GLY B C   1 
ATOM   1493 O O   . GLY B 1 102 ? 13.524  25.659 20.130  1.00 31.51  ? 102 GLY B O   1 
ATOM   1494 N N   . ARG B 1 103 ? 12.334  27.488 20.678  1.00 34.60  ? 103 ARG B N   1 
ATOM   1495 C CA  . ARG B 1 103 ? 11.960  26.986 21.994  1.00 36.20  ? 103 ARG B CA  1 
ATOM   1496 C C   . ARG B 1 103 ? 10.770  26.027 21.858  1.00 33.52  ? 103 ARG B C   1 
ATOM   1497 O O   . ARG B 1 103 ? 10.069  26.021 20.840  1.00 36.39  ? 103 ARG B O   1 
ATOM   1498 C CB  . ARG B 1 103 ? 11.679  28.146 22.967  1.00 42.12  ? 103 ARG B CB  1 
ATOM   1499 C CG  . ARG B 1 103 ? 12.952  28.739 23.570  1.00 48.54  ? 103 ARG B CG  1 
ATOM   1500 C CD  . ARG B 1 103 ? 12.766  30.139 24.148  1.00 59.01  ? 103 ARG B CD  1 
ATOM   1501 N NE  . ARG B 1 103 ? 11.905  30.175 25.334  1.00 69.39  ? 103 ARG B NE  1 
ATOM   1502 C CZ  . ARG B 1 103 ? 11.657  31.265 26.066  1.00 76.13  ? 103 ARG B CZ  1 
ATOM   1503 N NH1 . ARG B 1 103 ? 12.201  32.438 25.749  1.00 78.43  ? 103 ARG B NH1 1 
ATOM   1504 N NH2 . ARG B 1 103 ? 10.857  31.185 27.126  1.00 77.57  ? 103 ARG B NH2 1 
ATOM   1505 N N   . THR B 1 104 ? 10.569  25.201 22.880  1.00 30.65  ? 104 THR B N   1 
ATOM   1506 C CA  . THR B 1 104 ? 9.574   24.137 22.843  1.00 28.27  ? 104 THR B CA  1 
ATOM   1507 C C   . THR B 1 104 ? 8.305   24.547 23.575  1.00 29.15  ? 104 THR B C   1 
ATOM   1508 O O   . THR B 1 104 ? 8.352   25.019 24.715  1.00 31.73  ? 104 THR B O   1 
ATOM   1509 C CB  . THR B 1 104 ? 10.124  22.846 23.475  1.00 27.62  ? 104 THR B CB  1 
ATOM   1510 O OG1 . THR B 1 104 ? 11.250  22.386 22.715  1.00 29.48  ? 104 THR B OG1 1 
ATOM   1511 C CG2 . THR B 1 104 ? 9.061   21.757 23.501  1.00 27.94  ? 104 THR B CG2 1 
ATOM   1512 N N   . LEU B 1 105 ? 7.172   24.363 22.906  1.00 28.84  ? 105 LEU B N   1 
ATOM   1513 C CA  . LEU B 1 105 ? 5.873   24.594 23.515  1.00 27.43  ? 105 LEU B CA  1 
ATOM   1514 C C   . LEU B 1 105 ? 5.463   23.310 24.211  1.00 27.74  ? 105 LEU B C   1 
ATOM   1515 O O   . LEU B 1 105 ? 5.651   22.224 23.665  1.00 26.84  ? 105 LEU B O   1 
ATOM   1516 C CB  . LEU B 1 105 ? 4.842   24.963 22.449  1.00 26.42  ? 105 LEU B CB  1 
ATOM   1517 C CG  . LEU B 1 105 ? 3.427   25.270 22.939  1.00 25.78  ? 105 LEU B CG  1 
ATOM   1518 C CD1 . LEU B 1 105 ? 3.421   26.543 23.764  1.00 26.92  ? 105 LEU B CD1 1 
ATOM   1519 C CD2 . LEU B 1 105 ? 2.469   25.400 21.765  1.00 26.02  ? 105 LEU B CD2 1 
ATOM   1520 N N   . VAL B 1 106 ? 4.918   23.431 25.415  1.00 29.37  ? 106 VAL B N   1 
ATOM   1521 C CA  . VAL B 1 106 ? 4.467   22.265 26.162  1.00 31.04  ? 106 VAL B CA  1 
ATOM   1522 C C   . VAL B 1 106 ? 3.060   22.479 26.708  1.00 32.40  ? 106 VAL B C   1 
ATOM   1523 O O   . VAL B 1 106 ? 2.686   23.601 27.052  1.00 33.46  ? 106 VAL B O   1 
ATOM   1524 C CB  . VAL B 1 106 ? 5.441   21.906 27.307  1.00 34.08  ? 106 VAL B CB  1 
ATOM   1525 C CG1 . VAL B 1 106 ? 6.823   21.595 26.750  1.00 35.13  ? 106 VAL B CG1 1 
ATOM   1526 C CG2 . VAL B 1 106 ? 5.532   23.022 28.341  1.00 36.49  ? 106 VAL B CG2 1 
ATOM   1527 N N   . VAL B 1 107 ? 2.283   21.398 26.759  1.00 32.67  ? 107 VAL B N   1 
ATOM   1528 C CA  . VAL B 1 107 ? 0.962   21.405 27.393  1.00 34.26  ? 107 VAL B CA  1 
ATOM   1529 C C   . VAL B 1 107 ? 0.846   20.212 28.346  1.00 35.12  ? 107 VAL B C   1 
ATOM   1530 O O   . VAL B 1 107 ? 1.272   19.104 28.015  1.00 37.74  ? 107 VAL B O   1 
ATOM   1531 C CB  . VAL B 1 107 ? -0.187  21.403 26.350  1.00 33.41  ? 107 VAL B CB  1 
ATOM   1532 C CG1 . VAL B 1 107 ? -0.172  20.142 25.498  1.00 32.78  ? 107 VAL B CG1 1 
ATOM   1533 C CG2 . VAL B 1 107 ? -1.543  21.572 27.026  1.00 33.36  ? 107 VAL B CG2 1 
ATOM   1534 N N   . HIS B 1 108 ? 0.287   20.450 29.531  1.00 37.05  ? 108 HIS B N   1 
ATOM   1535 C CA  . HIS B 1 108 ? 0.144   19.404 30.546  1.00 38.88  ? 108 HIS B CA  1 
ATOM   1536 C C   . HIS B 1 108 ? -1.028  18.494 30.223  1.00 39.37  ? 108 HIS B C   1 
ATOM   1537 O O   . HIS B 1 108 ? -2.163  18.955 30.157  1.00 39.32  ? 108 HIS B O   1 
ATOM   1538 C CB  . HIS B 1 108 ? -0.065  20.018 31.932  1.00 40.42  ? 108 HIS B CB  1 
ATOM   1539 C CG  . HIS B 1 108 ? 1.199   20.485 32.581  1.00 45.67  ? 108 HIS B CG  1 
ATOM   1540 N ND1 . HIS B 1 108 ? 1.799   19.802 33.617  1.00 48.94  ? 108 HIS B ND1 1 
ATOM   1541 C CD2 . HIS B 1 108 ? 1.981   21.563 32.337  1.00 46.53  ? 108 HIS B CD2 1 
ATOM   1542 C CE1 . HIS B 1 108 ? 2.895   20.441 33.986  1.00 51.43  ? 108 HIS B CE1 1 
ATOM   1543 N NE2 . HIS B 1 108 ? 3.029   21.512 33.224  1.00 50.05  ? 108 HIS B NE2 1 
ATOM   1544 N N   . GLU B 1 109 ? -0.754  17.204 30.044  1.00 39.79  ? 109 GLU B N   1 
ATOM   1545 C CA  . GLU B 1 109 ? -1.801  16.227 29.733  1.00 44.23  ? 109 GLU B CA  1 
ATOM   1546 C C   . GLU B 1 109 ? -2.708  15.930 30.930  1.00 48.52  ? 109 GLU B C   1 
ATOM   1547 O O   . GLU B 1 109 ? -3.869  15.556 30.755  1.00 46.64  ? 109 GLU B O   1 
ATOM   1548 C CB  . GLU B 1 109 ? -1.187  14.934 29.203  1.00 45.99  ? 109 GLU B CB  1 
ATOM   1549 C CG  . GLU B 1 109 ? -0.433  15.120 27.894  1.00 47.38  ? 109 GLU B CG  1 
ATOM   1550 C CD  . GLU B 1 109 ? 0.068   13.815 27.313  1.00 51.35  ? 109 GLU B CD  1 
ATOM   1551 O OE1 . GLU B 1 109 ? 0.424   12.905 28.094  1.00 58.57  ? 109 GLU B OE1 1 
ATOM   1552 O OE2 . GLU B 1 109 ? 0.111   13.702 26.069  1.00 45.44  ? 109 GLU B OE2 1 
ATOM   1553 N N   . LYS B 1 110 ? -2.175  16.088 32.140  1.00 51.46  ? 110 LYS B N   1 
ATOM   1554 C CA  . LYS B 1 110 ? -2.983  15.982 33.351  1.00 56.00  ? 110 LYS B CA  1 
ATOM   1555 C C   . LYS B 1 110 ? -3.732  17.297 33.568  1.00 55.34  ? 110 LYS B C   1 
ATOM   1556 O O   . LYS B 1 110 ? -3.131  18.374 33.531  1.00 49.97  ? 110 LYS B O   1 
ATOM   1557 C CB  . LYS B 1 110 ? -2.108  15.659 34.564  1.00 61.20  ? 110 LYS B CB  1 
ATOM   1558 C CG  . LYS B 1 110 ? -2.898  15.381 35.835  1.00 66.49  ? 110 LYS B CG  1 
ATOM   1559 C CD  . LYS B 1 110 ? -2.034  14.755 36.918  1.00 73.40  ? 110 LYS B CD  1 
ATOM   1560 C CE  . LYS B 1 110 ? -2.856  14.421 38.153  1.00 80.00  ? 110 LYS B CE  1 
ATOM   1561 N NZ  . LYS B 1 110 ? -2.070  13.656 39.159  1.00 86.50  ? 110 LYS B NZ  1 
ATOM   1562 N N   . ALA B 1 111 ? -5.041  17.202 33.793  1.00 54.76  ? 111 ALA B N   1 
ATOM   1563 C CA  . ALA B 1 111 ? -5.882  18.384 33.992  1.00 62.98  ? 111 ALA B CA  1 
ATOM   1564 C C   . ALA B 1 111 ? -5.652  19.035 35.360  1.00 70.31  ? 111 ALA B C   1 
ATOM   1565 O O   . ALA B 1 111 ? -4.998  18.462 36.235  1.00 66.52  ? 111 ALA B O   1 
ATOM   1566 C CB  . ALA B 1 111 ? -7.352  18.022 33.823  1.00 64.26  ? 111 ALA B CB  1 
ATOM   1567 N N   . GLY B 1 112 ? -6.198  20.238 35.529  1.00 82.16  ? 112 GLY B N   1 
ATOM   1568 C CA  . GLY B 1 112 ? -6.104  20.974 36.787  1.00 86.62  ? 112 GLY B CA  1 
ATOM   1569 C C   . GLY B 1 112 ? -4.774  21.685 36.932  1.00 98.58  ? 112 GLY B C   1 
ATOM   1570 O O   . GLY B 1 112 ? -4.686  22.897 36.736  1.00 93.99  ? 112 GLY B O   1 
ATOM   1571 N N   . ALA B 1 113 ? -3.740  20.921 37.279  1.00 109.44 ? 113 ALA B N   1 
ATOM   1572 C CA  . ALA B 1 113 ? -2.393  21.461 37.457  1.00 110.03 ? 113 ALA B CA  1 
ATOM   1573 C C   . ALA B 1 113 ? -1.345  20.357 37.336  1.00 109.99 ? 113 ALA B C   1 
ATOM   1574 O O   . ALA B 1 113 ? -1.246  19.482 38.196  1.00 105.59 ? 113 ALA B O   1 
ATOM   1575 C CB  . ALA B 1 113 ? -2.278  22.155 38.807  1.00 113.78 ? 113 ALA B CB  1 
ATOM   1576 O OXT . ALA B 1 113 ? -0.577  20.310 36.374  1.00 97.21  ? 113 ALA B OXT 1 
HETATM 1577 O O   . HOH C 2 .   ? -16.516 21.658 0.476   1.00 27.17  ? 201 HOH A O   1 
HETATM 1578 O O   . HOH C 2 .   ? -11.451 16.619 0.552   1.00 29.85  ? 202 HOH A O   1 
HETATM 1579 O O   . HOH C 2 .   ? -8.360  16.614 5.311   1.00 43.48  ? 203 HOH A O   1 
HETATM 1580 O O   . HOH C 2 .   ? -9.537  20.521 6.654   1.00 27.28  ? 204 HOH A O   1 
HETATM 1581 O O   . HOH C 2 .   ? -0.728  12.055 2.685   1.00 40.88  ? 205 HOH A O   1 
HETATM 1582 O O   . HOH C 2 .   ? 4.591   30.230 -7.029  1.00 38.06  ? 206 HOH A O   1 
HETATM 1583 O O   . HOH C 2 .   ? -3.206  25.626 11.671  1.00 27.36  ? 207 HOH A O   1 
HETATM 1584 O O   . HOH C 2 .   ? -13.526 46.039 4.250   1.00 41.35  ? 208 HOH A O   1 
HETATM 1585 O O   . HOH C 2 .   ? -10.861 18.238 5.251   1.00 27.32  ? 209 HOH A O   1 
HETATM 1586 O O   . HOH C 2 .   ? -3.230  16.635 -10.820 1.00 30.86  ? 210 HOH A O   1 
HETATM 1587 O O   . HOH C 2 .   ? -9.991  9.465  -14.945 1.00 33.27  ? 211 HOH A O   1 
HETATM 1588 O O   . HOH C 2 .   ? 9.716   16.320 -5.009  1.00 38.19  ? 212 HOH A O   1 
HETATM 1589 O O   . HOH C 2 .   ? 1.905   25.073 8.595   1.00 33.15  ? 213 HOH A O   1 
HETATM 1590 O O   . HOH D 2 .   ? 6.709   21.754 15.524  1.00 16.82  ? 201 HOH B O   1 
HETATM 1591 O O   . HOH D 2 .   ? 10.701  41.891 24.370  1.00 43.43  ? 202 HOH B O   1 
HETATM 1592 O O   . HOH D 2 .   ? 6.288   15.514 24.802  1.00 48.08  ? 203 HOH B O   1 
HETATM 1593 O O   . HOH D 2 .   ? -3.883  18.068 14.986  1.00 46.02  ? 204 HOH B O   1 
HETATM 1594 O O   . HOH D 2 .   ? 6.483   23.556 12.870  1.00 29.82  ? 205 HOH B O   1 
HETATM 1595 O O   . HOH D 2 .   ? -0.227  25.858 10.550  1.00 32.73  ? 206 HOH B O   1 
HETATM 1596 O O   . HOH D 2 .   ? -11.434 23.406 16.671  1.00 40.61  ? 207 HOH B O   1 
HETATM 1597 O O   . HOH D 2 .   ? -13.224 24.068 23.959  1.00 43.42  ? 208 HOH B O   1 
HETATM 1598 O O   . HOH D 2 .   ? 0.758   16.697 33.114  1.00 35.76  ? 209 HOH B O   1 
HETATM 1599 O O   . HOH D 2 .   ? -0.729  17.508 15.448  1.00 40.90  ? 210 HOH B O   1 
HETATM 1600 O O   . HOH D 2 .   ? -4.942  24.721 13.770  1.00 30.44  ? 211 HOH B O   1 
# 
# 
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   ALA 1   1   1   ALA ALA A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  GLN 33  33  33  GLN GLN A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  GLN 40  40  40  GLN GLN A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  TRP 50  50  50  TRP TRP A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  HIS 61  61  61  HIS HIS A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  PHE 63  63  63  PHE PHE A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 THR 104 104 104 THR THR A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 HIS 108 108 108 HIS HIS A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   SER 3   3   3   SER SER B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  ILE 10  10  10  ILE ILE B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  ILE 12  12  12  ILE ILE B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  GLY 18  18  18  GLY GLY B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  THR 20  20  20  THR THR B . n 
B 1 21  LYS 21  21  21  LYS LYS B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  VAL 23  23  23  VAL VAL B . n 
B 1 24  ALA 24  24  24  ALA ALA B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  ASP 29  29  29  ASP ASP B . n 
B 1 30  GLY 30  30  30  GLY GLY B . n 
B 1 31  PRO 31  31  31  PRO PRO B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  GLN 33  33  33  GLN GLN B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  PHE 38  38  38  PHE PHE B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  GLN 40  40  40  GLN GLN B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  TRP 50  50  50  TRP TRP B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  LYS 54  54  54  LYS LYS B . n 
B 1 55  GLY 55  55  55  GLY GLY B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  GLU 58  58  58  GLU GLU B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  HIS 61  61  61  HIS HIS B . n 
B 1 62  GLY 62  62  62  GLY GLY B . n 
B 1 63  PHE 63  63  63  PHE PHE B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  THR 76  76  76  THR THR B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  ASP 78  78  78  ASP ASP B . n 
B 1 79  LYS 79  79  79  LYS LYS B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  ALA 83  83  83  ALA ALA B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ILE 87  87  87  ILE ILE B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  ASP 89  89  89  ASP ASP B . n 
B 1 90  SER 90  90  90  SER SER B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ILE 92  92  92  ILE ILE B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  SER 95  95  95  SER SER B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  HIS 98  98  98  HIS HIS B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 ILE 101 101 101 ILE ILE B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 ARG 103 103 103 ARG ARG B . n 
B 1 104 THR 104 104 104 THR THR B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 HIS 108 108 108 HIS HIS B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1  201 38 HOH HOH A . 
C 2 HOH 2  202 20 HOH HOH A . 
C 2 HOH 3  203 19 HOH HOH A . 
C 2 HOH 4  204 2  HOH HOH A . 
C 2 HOH 5  205 4  HOH HOH A . 
C 2 HOH 6  206 22 HOH HOH A . 
C 2 HOH 7  207 31 HOH HOH A . 
C 2 HOH 8  208 30 HOH HOH A . 
C 2 HOH 9  209 11 HOH HOH A . 
C 2 HOH 10 210 17 HOH HOH A . 
C 2 HOH 11 211 29 HOH HOH A . 
C 2 HOH 12 212 5  HOH HOH A . 
C 2 HOH 13 213 26 HOH HOH A . 
D 2 HOH 1  201 1  HOH HOH B . 
D 2 HOH 2  202 10 HOH HOH B . 
D 2 HOH 3  203 21 HOH HOH B . 
D 2 HOH 4  204 35 HOH HOH B . 
D 2 HOH 5  205 9  HOH HOH B . 
D 2 HOH 6  206 23 HOH HOH B . 
D 2 HOH 7  207 28 HOH HOH B . 
D 2 HOH 8  208 3  HOH HOH B . 
D 2 HOH 9  209 25 HOH HOH B . 
D 2 HOH 10 210 34 HOH HOH B . 
D 2 HOH 11 211 7  HOH HOH B . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_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_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2017-02-01 
2 'Structure model' 1 1 2018-01-17 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Data collection' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            diffrn_source 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_diffrn_source.pdbx_synchrotron_site' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -5.0764 26.6978 0.0766  0.1269 0.1258 0.1404 -0.0085 -0.0200 0.0158  0.0865 0.0091 0.0869 0.0223  
-0.0660 -0.0087 -0.0290 0.0037 0.0254 0.0141  0.0349 0.0294  -0.0108 -0.0107 0.0249  
'X-RAY DIFFRACTION' 2 ? refined 1.2257  26.9943 22.4106 0.1243 0.1224 0.1334 0.0081  -0.0034 -0.0128 0.3850 0.0220 0.0592 -0.0890 
0.1495  -0.0347 -0.0441 0.0132 0.0309 -0.0426 0.0909 -0.0324 0.0051  -0.0064 -0.0183 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 1 A 113 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 1 B 113 ? ? ? ? ? ? 
# 
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 scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.7.0032 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? iMOSFLM     ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    HIS 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     98 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -107.92 
_pdbx_validate_torsion.psi             44.08 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
